path: root/plip/test/pdb/1het.pdb

HEADER    OXIDOREDUCTASE                          25-NOV-00   1HET              
TITLE     ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE                 
TITLE    2 CONTAINING A HYDROXIDE ADDUCT TO NADH                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALCOHOL DEHYDROGENASE E CHAIN;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ALCOHOL DEHYDROGENASE I;                                    
COMPND   5 EC: 1.1.1.1;                                                         
COMPND   6 OTHER_DETAILS: ADDUCT BETWEEN NC6 OF NADH AND ZINC BOUND             
COMPND   7  HYDROXIDE                                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   3 ORGANISM_COMMON: DOMESTIC HORSE;                                     
SOURCE   4 ORGANISM_TAXID: 9796;                                                
SOURCE   5 ORGAN: LIVER                                                         
KEYWDS    OXIDOREDUCTASE, OXIDOREDUCTASE(NAD(A)-CHOH(D))                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.MEIJERS,R.J.MORRIS,H.W.ADOLPH,A.MERLI,V.S.LAMZIN,                   
AUTHOR   2 E.S.CEDERGEN-ZEPPEZAUER                                              
REVDAT   3   24-FEB-09 1HET    1       VERSN                                    
REVDAT   2   16-AUG-01 1HET    1       REMARK LINK   ATOM   ANISOU              
REVDAT   2 2                           HETATM CONECT MASTER                     
REVDAT   1   31-MAY-01 1HET    0                                                
JRNL        AUTH   R.MEIJERS,R.J.MORRIS,H.W.ADOLPH,A.MERLI,V.S.LAMZIN,          
JRNL        AUTH 2 E.S.CEDERGEN-ZEPPEZAUER                                      
JRNL        TITL   ON THE ENZYMATIC ACTIVATION OF NADH                          
JRNL        REF    J.BIOL.CHEM.                  V. 276  9316 2001              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   11134046                                                     
JRNL        DOI    10.1074/JBC.M010870200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.RAMASWAMY,D.H.PARK,B.V.PLAPP                               
REMARK   1  TITL   SUBSTITUTIONS IN A FLEXIBLE LOOP OF HORSE LIVER              
REMARK   1  TITL 2 ALCOHOL DEHYDROGENASE HINDER THE CONFORMATIONAL              
REMARK   1  TITL 3 CHANGE AND UNMASK HYDROGEN TRANSFER                          
REMARK   1  REF    BIOCHEMISTRY                  V.  38 13951 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   10529241                                                     
REMARK   1  DOI    10.1021/BI991731I                                            
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   H.W.ADOLPH,M.KIEFER,E.S.CEDERGREN-ZEPPEZAUER                 
REMARK   1  TITL   ELECTROSTATIC EFFECTS IN THE KINETICS OF COENZYME            
REMARK   1  TITL 2 BINDING TO ISOZYMES OF ALCOHOL DEHYDROGENASE FROM            
REMARK   1  TITL 3 HORSE LIVER                                                  
REMARK   1  REF    BIOCHEMISTRY                  V.  36  8743 1997              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   9220961                                                      
REMARK   1  DOI    10.1021/BI970398K                                            
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   S.AL-KARADAGHI,E.S.CEDERGREN-ZEPPEZAUER,Z.DAUTER,            
REMARK   1  AUTH 2 K.S.WILSON                                                   
REMARK   1  TITL   REFINED STRUCTURE OF CU-SUBSTITUTED ALCOHOL                  
REMARK   1  TITL 2 DEHYDROGENASE AT 2.1 A RESOLUTION                            
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  51   805 1995              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   15299812                                                     
REMARK   1  DOI    10.1107/S090744499500045X                                    
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   S.AL-KARADAGHI,E.S.CEDERGREN-ZEPPEZAUER,K.PETRATOS,          
REMARK   1  AUTH 2 S.HOVMOELLER,H.TERRY,Z.DAUTER,K.S.WILSON                     
REMARK   1  TITL   REFINED CRYSTAL STRUCTURE OF LIVER ALCOHOL                   
REMARK   1  TITL 2 DEHYDROGENASE-NADH COMPLEX AT 1.8 ANGSTROM                   
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  50   793 1994              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   15299346                                                     
REMARK   1  DOI    10.1107/S0907444994005263                                    
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   F.COLONNA-CESARI,D.PERAHIA,M.KARPLUS,H.EKLUND,               
REMARK   1  AUTH 2 C.I.BRANDEN,O.TAPIA                                          
REMARK   1  TITL   INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE.           
REMARK   1  TITL 2 {S}TRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE             
REMARK   1  TITL 3 BENDING MODE                                                 
REMARK   1  REF    J.BIOL.CHEM.                  V. 261 15273 1986              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   3771574                                                      
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   H.EKLUND,J.-P.SAMAMA,T.A.JONES                               
REMARK   1  TITL   CRYSTALLOGRAPHIC INVESTIGATIONS OF NICOTINAMIDE              
REMARK   1  TITL 2 ADENINE DINUCLEOTIDE                                         
REMARK   1  REF    BIOCHEMISTRY                  V.  23  5982 1984              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   6098306                                                      
REMARK   1  DOI    10.1021/BI00320A014                                          
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   G.SCHNEIDER,H.EKLUND,E.CEDERGREN-ZEPPEZAUER,                 
REMARK   1  AUTH 2 M.ZEPPEZAUER                                                 
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE ACTIVE SITE IN                     
REMARK   1  TITL 2 SPECIFICALLY METAL-DEPLETED AND COBALT-SUBSTITUTED           
REMARK   1  TITL 3 HORSE LIVER ALCOHOL DEHYDROGENASE DERIVATIVES                
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  80  5289 1983              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   6351056                                                      
REMARK   1  DOI    10.1073/PNAS.80.17.5289                                      
REMARK   1 REFERENCE 8                                                          
REMARK   1  AUTH   E.CEDERGREN-ZEPPEZAUER                                       
REMARK   1  TITL   CRYSTAL-STRUCTURE DETERMINATION OF REDUCED                   
REMARK   1  TITL 2 NICOTINAMIDE ADENINE DINUCLEOTIDE COMPLEX WITH               
REMARK   1  TITL 3 HORSE LIVER ALCOHOL DEHYDROGENASE MAINTAINED IN              
REMARK   1  TITL 4 ITS APO CONFORMATION BY ZINC-BOUND IMIDAZOLE                 
REMARK   1  REF    BIOCHEMISTRY                  V.  22  5761 1983              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   6362718                                                      
REMARK   1  DOI    10.1021/BI00294A013                                          
REMARK   1 REFERENCE 9                                                          
REMARK   1  AUTH   E.CEDERGREN-ZEPPEZAUER,J.-P.SAMAMA,H.EKLUND                  
REMARK   1  TITL   CRYSTAL STRUCTURE DETERMINATIONS OF COENZYME                 
REMARK   1  TITL 2 ANALOGUE AND SUBSTRATE COMPLEXES OF LIVER ALCOHOL            
REMARK   1  TITL 3 DEHYDROGENASE: BINDING OF                                    
REMARK   1  TITL 4 1,4,5,6-TETRAHYDRONICOTINAMIDE ADENINE                       
REMARK   1  TITL 5 DINUCLEOTIDE AND                                             
REMARK   1  TITL 6 TRANS-4-({N},{N}-DIMETHYLAMINO)CINNAMALDEHYDE TO             
REMARK   1  TITL 7 THE ENZYME                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  21  4895 1982              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   6753930                                                      
REMARK   1  DOI    10.1021/BI00263A011                                          
REMARK   1 REFERENCE 10                                                         
REMARK   1  AUTH   H.EKLUND,B.NORDSTROM,E.ZEPPEZAUER,G.SODERLUND,               
REMARK   1  AUTH 2 I.OHLSSON,T.BOIWE,B.-O.SODERBERG,O.TAPIA,                    
REMARK   1  AUTH 3 C.-I.BRANDEN,A.AKESON                                        
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF HORSE LIVER ALCOHOL           
REMARK   1  TITL 2 DEHYDROGENASE AT 2.4 ANGSTROM RESOLUTION                     
REMARK   1  REF    J.MOL.BIOL.                   V. 102    27 1976              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   178875                                                       
REMARK   1  DOI    10.1016/0022-2836(76)90072-3                                 
REMARK   1 REFERENCE 11                                                         
REMARK   1  AUTH   C.-I.BRANDEN,H.EKLUND,B.NORDSTROM,T.BOIWE,                   
REMARK   1  AUTH 2 G.SODERLUND,E.ZEPPEZAUER,I.OHLSSON,A.AKESON                  
REMARK   1  TITL   STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE AT 2.9              
REMARK   1  TITL 2 ANGSTROM RESOLUTION                                          
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  70  2439 1973              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1  PMID   4365379                                                      
REMARK   1  DOI    10.1073/PNAS.70.8.2439                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 252601                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT UNTIL FINAL          
REMARK   3                                      REFINEMENT ROUND                
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.123                           
REMARK   3   R VALUE            (WORKING SET) : 0.118                           
REMARK   3   FREE R VALUE                     : 0.135                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.05                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6106                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 152                                     
REMARK   3   SOLVENT ATOMS            : 1436                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 9.4                            
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.8                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.03          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.015 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.034 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SHELX WAS USED IN PARALLEL TO REFINE      
REMARK   3  OCCUPANCIES OF DISORDERED RESIDUES                                  
REMARK   4                                                                      
REMARK   4 1HET COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-NOV-00.                  
REMARK 100 THE PDBE ID CODE IS EBI-5150.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 120.0                              
REMARK 200  PH                             : 8.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.927                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH X-RAY RESEARCH         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 267243                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 2OHX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300                                                                      
REMARK 300 DETAILS:BIOLOGICAL_UNIT: DIMERIC                                     
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ALCOHOL + NAD(+) = ALDEHYDE OR KETONE + NADH.                       
REMARK 400  REQUIRES ZINC FOR ITS ACTIVITY.                                     
REMARK 400  DIMER OF IDENTICAL OR NONIDENTICAL CHAINS OF TWO TYPES              
REMARK 400  (E AND S) CODED BY 2 SEPARATE GENES AT DIFFERENT LOCI.              
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  2356  -  O    HOH A  2659              2.18            
REMARK 500   O    HOH A  2357  -  O    HOH A  2659              1.74            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  84   CB  -  CG  -  CD  ANGL. DEV. = -18.2 DEGREES          
REMARK 500    ARG A  84   CD  -  NE  -  CZ  ANGL. DEV. =  29.6 DEGREES          
REMARK 500    ARG A  84   CG  -  CD  -  NE  ANGL. DEV. = -19.7 DEGREES          
REMARK 500    ARG A 101   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    CYS A 174   CA  -  CB  -  SG  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ARG A 271   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 369   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    LYS B  10   CB  -  CG  -  CD  ANGL. DEV. =  32.1 DEGREES          
REMARK 500    LYS B  10   CD  -  CE  -  NZ  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ARG B 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    CYS B 174   CA  -  CB  -  SG  ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    GLU B 239   CG  -  CD  -  OE2 ANGL. DEV. =  13.1 DEGREES          
REMARK 500    GLU B 239   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    GLN B 251   CG  -  CD  -  OE1 ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ARG B 312   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  67       -3.78   -145.25                                   
REMARK 500    ILE A 368      -88.07   -101.11                                   
REMARK 500    HIS B  67       -4.78   -143.87                                   
REMARK 500    THR B 143      -56.26   -121.87                                   
REMARK 500    ILE B 368      -92.07    -99.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  67   NE2                                                    
REMARK 620 2 HOH A2741B  O    85.6                                              
REMARK 620 3 CYS A  46   SG  107.9 107.2                                        
REMARK 620 4 CYS A 174   SG  111.1 101.1 133.0                                  
REMARK 620 5 HOH A2740A  O   120.1  37.8  81.7 100.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 100   SG                                                     
REMARK 620 2 CYS A  97   SG  109.7                                              
REMARK 620 3 CYS A 111   SG  119.5 104.3                                        
REMARK 620 4 CYS A 103   SG  105.0 116.0 102.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 400  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  46   SG                                                     
REMARK 620 2 HIS B  67   NE2 106.8                                              
REMARK 620 3 CYS B 174   SG  132.8 112.5                                        
REMARK 620 4 HOH B2672B  O   109.0  83.6 100.3                                  
REMARK 620 5 HOH B2673A  O    81.7 115.2 103.2  36.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  97   SG                                                     
REMARK 620 2 CYS B 100   SG  109.9                                              
REMARK 620 3 CYS B 111   SG  104.8 119.5                                        
REMARK 620 4 CYS B 103   SG  114.6 105.0 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HEU   RELATED DB: PDB                                   
REMARK 900  ATOMIC X-RAY STRUCTURE OF LIVER ALCOHOL DEHYDROGENASE               
REMARK 900  CONTAINING CADMIUM AND A HYDROXIDE ADDUCT TO NADH                   
REMARK 900 RELATED ID: 1A71   RELATED DB: PDB                                   
REMARK 900  TERNARY COMPLEX OF AN ACTIVE SITE DOUBLE MUTANT OF HORSE            
REMARK 900  LIVER ALCOHOL DEHYDROGENASE, PHE93=>TRP, VAL203=>ALA                
REMARK 900  WITH NAD AND TRIFLUOROETHANOL                                       
REMARK 900 RELATED ID: 1A72   RELATED DB: PDB                                   
REMARK 900  AN ACTIVE-SITE DOUBLE MUTANT (PHE93->TRP, VAL203->ALA)              
REMARK 900  OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH THE            
REMARK 900  ISOSTERIC NAD ANALOG CPAD                                           
REMARK 900 RELATED ID: 1AXE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE ACTIVE-SITE MUTANT PHE93->TRP              
REMARK 900  OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH NAD            
REMARK 900  AND INHIBITOR TRIFLUOROETHANOL                                      
REMARK 900 RELATED ID: 1AXG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE VAL203->ALA MUTANT OF LIVER                
REMARK 900  ALCOHOL DEHYDROGENASE COMPLEXED WITH COFACTOR NAD AND               
REMARK 900  INHIBITOR TRIFLUOROETHANOL SOLVED TO 2.5 ANGSTROM                   
REMARK 900  RESOLUTION                                                          
REMARK 900 RELATED ID: 1BTO   RELATED DB: PDB                                   
REMARK 900  HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND             
REMARK 900  (1S,3R)3-BUTYLTHIOLANE 1-OXIDE                                      
REMARK 900 RELATED ID: 1LDE   RELATED DB: PDB                                   
REMARK 900  HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND             
REMARK 900  N-FORMYL PIPERDINE                                                  
REMARK 900 RELATED ID: 1LDY   RELATED DB: PDB                                   
REMARK 900  HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND             
REMARK 900  CYCLOHEXYL FORMAMIDE (CXF)                                          
REMARK 900 RELATED ID: 1QLH   RELATED DB: PDB                                   
REMARK 900  HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD                  
REMARK 900  DOUBLE MUTANT OF GLY 293 ALA AND  PRO 295 THR                       
REMARK 900 RELATED ID: 1QLJ   RELATED DB: PDB                                   
REMARK 900  HORSE LIVER ALCOHOL DEHYDROGENASE APO ENZYME DOUBLE                 
REMARK 900  MUTANT OF GLY 293 ALA AND  PRO 295 THR                              
REMARK 900 RELATED ID: 3BTO   RELATED DB: PDB                                   
REMARK 900  HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND             
REMARK 900  (1S,3S)3-BUTYLTHIOLANE 1-OXIDE                                      
DBREF  1HET A    1   374  UNP    P00327   ADHE_HORSE       1    374             
DBREF  1HET B    1   374  UNP    P00327   ADHE_HORSE       1    374             
SEQRES   1 A  374  SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL          
SEQRES   2 A  374  LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL          
SEQRES   3 A  374  GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS          
SEQRES   4 A  374  MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL          
SEQRES   5 A  374  VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA          
SEQRES   6 A  374  GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU          
SEQRES   7 A  374  GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO          
SEQRES   8 A  374  LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS          
SEQRES   9 A  374  HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER          
SEQRES  10 A  374  MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE          
SEQRES  11 A  374  THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR          
SEQRES  12 A  374  SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER          
SEQRES  13 A  374  VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL          
SEQRES  14 A  374  CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER          
SEQRES  15 A  374  ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS          
SEQRES  16 A  374  ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE          
SEQRES  17 A  374  MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY          
SEQRES  18 A  374  VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU          
SEQRES  19 A  374  VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS          
SEQRES  20 A  374  LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY          
SEQRES  21 A  374  GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP          
SEQRES  22 A  374  THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR          
SEQRES  23 A  374  GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN          
SEQRES  24 A  374  ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG          
SEQRES  25 A  374  THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS          
SEQRES  26 A  374  ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS          
SEQRES  27 A  374  LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO          
SEQRES  28 A  374  PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER          
SEQRES  29 A  374  GLY GLU SER ILE ARG THR ILE LEU THR PHE                      
SEQRES   1 B  374  SER THR ALA GLY LYS VAL ILE LYS CYS LYS ALA ALA VAL          
SEQRES   2 B  374  LEU TRP GLU GLU LYS LYS PRO PHE SER ILE GLU GLU VAL          
SEQRES   3 B  374  GLU VAL ALA PRO PRO LYS ALA HIS GLU VAL ARG ILE LYS          
SEQRES   4 B  374  MET VAL ALA THR GLY ILE CYS ARG SER ASP ASP HIS VAL          
SEQRES   5 B  374  VAL SER GLY THR LEU VAL THR PRO LEU PRO VAL ILE ALA          
SEQRES   6 B  374  GLY HIS GLU ALA ALA GLY ILE VAL GLU SER ILE GLY GLU          
SEQRES   7 B  374  GLY VAL THR THR VAL ARG PRO GLY ASP LYS VAL ILE PRO          
SEQRES   8 B  374  LEU PHE THR PRO GLN CYS GLY LYS CYS ARG VAL CYS LYS          
SEQRES   9 B  374  HIS PRO GLU GLY ASN PHE CYS LEU LYS ASN ASP LEU SER          
SEQRES  10 B  374  MET PRO ARG GLY THR MET GLN ASP GLY THR SER ARG PHE          
SEQRES  11 B  374  THR CYS ARG GLY LYS PRO ILE HIS HIS PHE LEU GLY THR          
SEQRES  12 B  374  SER THR PHE SER GLN TYR THR VAL VAL ASP GLU ILE SER          
SEQRES  13 B  374  VAL ALA LYS ILE ASP ALA ALA SER PRO LEU GLU LYS VAL          
SEQRES  14 B  374  CYS LEU ILE GLY CYS GLY PHE SER THR GLY TYR GLY SER          
SEQRES  15 B  374  ALA VAL LYS VAL ALA LYS VAL THR GLN GLY SER THR CYS          
SEQRES  16 B  374  ALA VAL PHE GLY LEU GLY GLY VAL GLY LEU SER VAL ILE          
SEQRES  17 B  374  MET GLY CYS LYS ALA ALA GLY ALA ALA ARG ILE ILE GLY          
SEQRES  18 B  374  VAL ASP ILE ASN LYS ASP LYS PHE ALA LYS ALA LYS GLU          
SEQRES  19 B  374  VAL GLY ALA THR GLU CYS VAL ASN PRO GLN ASP TYR LYS          
SEQRES  20 B  374  LYS PRO ILE GLN GLU VAL LEU THR GLU MET SER ASN GLY          
SEQRES  21 B  374  GLY VAL ASP PHE SER PHE GLU VAL ILE GLY ARG LEU ASP          
SEQRES  22 B  374  THR MET VAL THR ALA LEU SER CYS CYS GLN GLU ALA TYR          
SEQRES  23 B  374  GLY VAL SER VAL ILE VAL GLY VAL PRO PRO ASP SER GLN          
SEQRES  24 B  374  ASN LEU SER MET ASN PRO MET LEU LEU LEU SER GLY ARG          
SEQRES  25 B  374  THR TRP LYS GLY ALA ILE PHE GLY GLY PHE LYS SER LYS          
SEQRES  26 B  374  ASP SER VAL PRO LYS LEU VAL ALA ASP PHE MET ALA LYS          
SEQRES  27 B  374  LYS PHE ALA LEU ASP PRO LEU ILE THR HIS VAL LEU PRO          
SEQRES  28 B  374  PHE GLU LYS ILE ASN GLU GLY PHE ASP LEU LEU ARG SER          
SEQRES  29 B  374  GLY GLU SER ILE ARG THR ILE LEU THR PHE                      
HET     ZN  A 400       1                                                       
HET     ZN  A 401       1                                                       
HET     ZN  B 400       1                                                       
HET     ZN  B 401       1                                                       
HET    NAD  A 402      54                                                       
HET    NAD  B 402      54                                                       
HET    MRD  A 403      16                                                       
HET    MRD  B 403      16                                                       
HET    MRD  B 404       8                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   7  NAD    2(C21 H27 N7 O14 P2)                                         
FORMUL   9  MRD    3(C6 H14 O2)                                                 
FORMUL  12  HOH   *1436(H2 O1)                                                  
HELIX    1 H1A CYS A   46  THR A   56  1                                  11    
HELIX    2 H2A PRO A  165  PHE A  176  1                                  12    
HELIX    3 HAA SER A  177  VAL A  189  1                                  13    
HELIX    4 HBA GLY A  201  ALA A  216  1                                  16    
HELIX    5 HCA ASN A  225  ALA A  237  1                                  13    
HELIX    6 HDA PRO A  249  GLY A  260  1                                  12    
HELIX    7 HEA ARG A  271  CYS A  282  1                                  12    
HELIX    8 S5A ASN A  304  GLY A  311  5                                   8    
HELIX    9 H3A LYS A  323  LYS A  338  1                                  16    
HELIX   10 H4A LYS A  354  GLY A  365  1                                  12    
HELIX   11 H1B CYS B   46  THR B   56  1                                  11    
HELIX   12 H2B PRO B  165  PHE B  176  1                                  12    
HELIX   13 HAB SER B  177  VAL B  189  1                                  13    
HELIX   14 HBB GLY B  201  ALA B  216  1                                  16    
HELIX   15 HCB ASN B  225  ALA B  237  1                                  13    
HELIX   16 HDB PRO B  249  GLY B  260  1                                  12    
HELIX   17 HEB ARG B  271  CYS B  282  1                                  12    
HELIX   18 S5B ASN B  304  GLY B  311  5                                   8    
HELIX   19 H3B LYS B  323  LYS B  338  1                                  16    
HELIX   20 H4B LYS B  354  GLY B  365  1                                  12    
SHEET    1 S1A 4 GLU A  68  ALA A  70  0                                        
SHEET    2 S1A 4 VAL A  41  ILE A  45 -1  N  ALA A  42   O  ALA A  70           
SHEET    3 S1A 4 ARG A 369  PHE A 374 -1  N  LEU A 372   O  THR A  43           
SHEET    4 S1A 4 LEU A 345  PHE A 352  1  N  LEU A 350   O  ILE A 371           
SHEET    1 S2A 5 GLN A 148  VAL A 152  0                                        
SHEET    2 S2A 5 GLU A  35  MET A  40 -1  N  ILE A  38   O  THR A 150           
SHEET    3 S2A 5 GLY A  71  GLY A  77 -1  N  GLU A  74   O  ARG A  37           
SHEET    4 S2A 5 GLY A  86  LEU A  92 -1  O  ASP A  87   N  VAL A  73           
SHEET    5 S2A 5 SER A 156  ILE A 160 -1  N  ALA A 158   O  ILE A  90           
SHEET    1 S3A 6 ILE A   7  VAL A  13  0                                        
SHEET    2 S3A 6 SER A  22  ALA A  29 -1  O  GLU A  24   N  ALA A  11           
SHEET    3 S3A 6 ARG A 129  CYS A 132 -1  O  THR A 131   N  GLU A  27           
SHEET    4 S3A 6 LYS A 135  HIS A 138 -1  O  LYS A 135   N  CYS A 132           
SHEET    5 S3A 6 PRO A  62  GLY A  66  1  O  PRO A  62   N  HIS A 138           
SHEET    6 S3A 6 THR A 145  PHE A 146  1  N  THR A 145   O  GLY A  66           
SHEET    1 S4A 6 THR A 238  VAL A 241  0                                        
SHEET    2 S4A 6 GLY A 215  ASP A 223  1  O  ILE A 219   N  THR A 238           
SHEET    3 S4A 6 GLY A 192  GLY A 199  1  O  CYS A 195   N  ILE A 220           
SHEET    4 S4A 6 VAL A 262  VAL A 268  1  O  PHE A 264   N  ALA A 196           
SHEET    5 S4A 6 GLY A 287  GLY A 293  1  O  VAL A 290   N  GLU A 267           
SHEET    6 S4A 6 THR A 313  ALA A 317  1  O  THR A 313   N  SER A 289           
SHEET    1 S1B 4 GLU B  68  ALA B  70  0                                        
SHEET    2 S1B 4 VAL B  41  ILE B  45 -1  N  ALA B  42   O  ALA B  70           
SHEET    3 S1B 4 ARG B 369  PHE B 374 -1  N  LEU B 372   O  THR B  43           
SHEET    4 S1B 4 LEU B 345  PHE B 352  1  N  LEU B 350   O  ILE B 371           
SHEET    1 S2B 5 GLN B 148  VAL B 152  0                                        
SHEET    2 S2B 5 GLU B  35  MET B  40 -1  N  ILE B  38   O  THR B 150           
SHEET    3 S2B 5 GLY B  71  GLY B  77 -1  N  GLU B  74   O  ARG B  37           
SHEET    4 S2B 5 GLY B  86  LEU B  92 -1  O  ASP B  87   N  VAL B  73           
SHEET    5 S2B 5 SER B 156  ILE B 160 -1  N  ALA B 158   O  ILE B  90           
SHEET    1 S3B 6 ILE B   7  VAL B  13  0                                        
SHEET    2 S3B 6 SER B  22  ALA B  29 -1  O  GLU B  24   N  ALA B  11           
SHEET    3 S3B 6 ARG B 129  CYS B 132 -1  O  THR B 131   N  GLU B  27           
SHEET    4 S3B 6 LYS B 135  HIS B 138 -1  O  LYS B 135   N  CYS B 132           
SHEET    5 S3B 6 PRO B  62  GLY B  66  1  O  PRO B  62   N  HIS B 138           
SHEET    6 S3B 6 THR B 145  PHE B 146  1  N  THR B 145   O  GLY B  66           
SHEET    1 S4B 6 THR B 238  VAL B 241  0                                        
SHEET    2 S4B 6 GLY B 215  ASP B 223  1  O  ILE B 219   N  THR B 238           
SHEET    3 S4B 6 GLY B 192  GLY B 199  1  O  CYS B 195   N  ILE B 220           
SHEET    4 S4B 6 VAL B 262  VAL B 268  1  O  PHE B 264   N  ALA B 196           
SHEET    5 S4B 6 GLY B 287  GLY B 293  1  O  VAL B 290   N  GLU B 267           
SHEET    6 S4B 6 THR B 313  ALA B 317  1  O  THR B 313   N  SER B 289           
LINK        ZN    ZN A 400                 NE2 HIS A  67     1555   1555  2.09  
LINK        ZN    ZN A 400                 O  BHOH A2741     1555   1555  2.13  
LINK        ZN    ZN A 400                 SG  CYS A  46     1555   1555  2.30  
LINK        ZN    ZN A 400                 SG  CYS A 174     1555   1555  2.28  
LINK        ZN    ZN A 400                 O  AHOH A2740     1555   1555  2.28  
LINK        ZN    ZN A 401                 SG  CYS A 100     1555   1555  2.44  
LINK        ZN    ZN A 401                 SG  CYS A  97     1555   1555  2.43  
LINK        ZN    ZN A 401                 SG  CYS A 111     1555   1555  2.44  
LINK        ZN    ZN A 401                 SG  CYS A 103     1555   1555  2.45  
LINK        ZN    ZN B 400                 NE2 HIS B  67     1555   1555  2.11  
LINK        ZN    ZN B 400                 SG  CYS B 174     1555   1555  2.26  
LINK        ZN    ZN B 400                 O  BHOH B2672     1555   1555  2.12  
LINK        ZN    ZN B 400                 O  AHOH B2673     1555   1555  2.32  
LINK        ZN    ZN B 400                 SG  CYS B  46     1555   1555  2.31  
LINK        ZN    ZN B 401                 SG  CYS B 100     1555   1555  2.43  
LINK        ZN    ZN B 401                 SG  CYS B 111     1555   1555  2.44  
LINK        ZN    ZN B 401                 SG  CYS B 103     1555   1555  2.43  
LINK        ZN    ZN B 401                 SG  CYS B  97     1555   1555  2.48  
CISPEP   1 LEU A   61    PRO A   62          0        -6.43                     
CISPEP   2 LEU B   61    PRO B   62          0        -1.29                     
SITE     1 AC1  6 CYS A  46  HIS A  67  CYS A 174  NAD A 402                    
SITE     2 AC1  6 HOH A2740  HOH A2741                                          
SITE     1 AC2  4 CYS A  97  CYS A 100  CYS A 103  CYS A 111                    
SITE     1 AC3  6 CYS B  46  HIS B  67  CYS B 174  NAD B 402                    
SITE     2 AC3  6 HOH B2672  HOH B2673                                          
SITE     1 AC4  4 CYS B  97  CYS B 100  CYS B 103  CYS B 111                    
SITE     1 AC5 36 ARG A  47  SER A  48  HIS A  51  CYS A 174                    
SITE     2 AC5 36 THR A 178  GLY A 201  GLY A 202  VAL A 203                    
SITE     3 AC5 36 ASP A 223  ILE A 224  LYS A 228  VAL A 268                    
SITE     4 AC5 36 ILE A 269  ARG A 271  VAL A 292  VAL A 294                    
SITE     5 AC5 36 ALA A 317  ILE A 318  PHE A 319  ARG A 369                    
SITE     6 AC5 36  ZN A 400  MRD A 403  HOH A2538  HOH A2609                    
SITE     7 AC5 36 HOH A2740  HOH A2742  HOH A2743  HOH A2744                    
SITE     8 AC5 36 HOH A2745  HOH A2746  HOH A2747  HOH A2748                    
SITE     9 AC5 36 HOH A2749  HOH A2750  HOH A2751  LEU B 309                    
SITE     1 AC6 35 ARG B  47  SER B  48  HIS B  51  CYS B 174                    
SITE     2 AC6 35 THR B 178  GLY B 199  GLY B 201  GLY B 202                    
SITE     3 AC6 35 VAL B 203  ASP B 223  ILE B 224  LYS B 228                    
SITE     4 AC6 35 VAL B 268  ILE B 269  ARG B 271  VAL B 292                    
SITE     5 AC6 35 VAL B 294  ALA B 317  ILE B 318  PHE B 319                    
SITE     6 AC6 35 LEU B 362  ARG B 369   ZN B 400  MRD B 403                    
SITE     7 AC6 35 HOH B2549  HOH B2673  HOH B2674  HOH B2675                    
SITE     8 AC6 35 HOH B2676  HOH B2678  HOH B2679  HOH B2680                    
SITE     9 AC6 35 HOH B2681  HOH B2682  HOH B2683                               
SITE     1 AC7  8 SER A  48  LEU A  57  LEU A 116  VAL A 294                    
SITE     2 AC7  8 NAD A 402  HOH A2377  HOH A2741  HOH A2752                    
SITE     1 AC8  9 SER B  48  LEU B  57  LEU B 116  LEU B 141                    
SITE     2 AC8  9 VAL B 294  NAD B 402  HOH B2345  HOH B2672                    
SITE     3 AC8  9 HOH B2684                                                     
SITE     1 AC9  4 GLU A 239  ARG B 218  THR B 238  GLU B 239                    
CRYST1   51.100   44.400   94.000 104.60 101.50  70.50 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019569 -0.006930  0.002643        0.00000                         
SCALE2      0.000000  0.023893  0.004898        0.00000                         
SCALE3      0.000000  0.000000  0.011082        0.00000                         
MTRIX1   1  0.129250  0.985840 -0.106810        0.39900    1                    
MTRIX2   1  0.986150 -0.139080 -0.090370       -0.21490    1                    
MTRIX3   1 -0.103940 -0.093660 -0.990160        0.44230    1                    
ATOM      1  N   SER A   1      23.200  14.450  51.603  1.00 66.50           N  
ANISOU    1  N   SER A   1     8718   8578   7971    125    150    251       N  
ATOM      2  CA  SER A   1      23.635  13.993  50.255  1.00 63.44           C  
ANISOU    2  CA  SER A   1     8475   7833   7795   -141    -53    225       C  
ATOM      3  C   SER A   1      22.916  12.710  49.847  1.00 53.30           C  
ANISOU    3  C   SER A   1     6985   7550   5714    425    -16     72       C  
ATOM      4  O   SER A   1      22.774  11.779  50.627  1.00 52.03           O  
ANISOU    4  O   SER A   1     6922   7179   5669    115      8   -235       O  
ATOM      5  CB  SER A   1      25.143  13.750  50.168  1.00 68.54           C  
ANISOU    5  CB  SER A   1     8661   8728   8651    131     16    459       C  
ATOM      6  OG  SER A   1      25.503  13.325  48.860  1.00 70.06           O  
ANISOU    6  OG  SER A   1     8843   8966   8809    171    143    404       O  
ATOM      7  N   THR A   2      22.505  12.677  48.584  1.00 37.41           N  
ANISOU    7  N   THR A   2     4746   4300   5166   -219    472   -329       N  
ATOM      8  CA  THR A   2      21.834  11.482  48.053  1.00 25.69           C  
ANISOU    8  CA  THR A   2     3316   3757   2687    394    329     23       C  
ATOM      9  C   THR A   2      22.743  10.683  47.122  1.00 19.88           C  
ANISOU    9  C   THR A   2     2783   2773   1998   -177    -25     37       C  
ATOM     10  O   THR A   2      22.339   9.618  46.641  1.00 17.33           O  
ANISOU   10  O   THR A   2     2466   2535   1584     49   -242    280       O  
ATOM     11  CB  THR A   2      20.554  11.936  47.323  1.00 22.63           C  
ANISOU   11  CB  THR A   2     3147   2951   2500    144    284   -312       C  
ATOM     12  OG1 THR A   2      20.890  12.987  46.400  1.00 21.48           O  
ANISOU   12  OG1 THR A   2     3157   2673   2332    285     53   -441       O  
ATOM     13  CG2 THR A   2      19.496  12.443  48.295  1.00 24.19           C  
ANISOU   13  CG2 THR A   2     3005   3440   2745    121    355   -309       C  
ATOM     14  N   ALA A   3      23.954  11.163  46.833  1.00 19.73           N  
ANISOU   14  N   ALA A   3     2728   2894   1875   -124     51   -377       N  
ATOM     15  CA  ALA A   3      24.848  10.451  45.928  1.00 19.81           C  
ANISOU   15  CA  ALA A   3     2552   2854   2122    -74    134   -135       C  
ATOM     16  C   ALA A   3      25.138   9.032  46.416  1.00 19.79           C  
ANISOU   16  C   ALA A   3     2591   2983   1944      5    -13    -35       C  
ATOM     17  O   ALA A   3      25.359   8.775  47.622  1.00 21.76           O  
ANISOU   17  O   ALA A   3     2747   3636   1884   -190    -65    -37       O  
ATOM     18  CB  ALA A   3      26.156  11.218  45.747  1.00 23.22           C  
ANISOU   18  CB  ALA A   3     2703   3399   2720   -262    250     -5       C  
ATOM     19  N   GLY A   4      25.032   8.065  45.504  1.00 17.88           N  
ANISOU   19  N   GLY A   4     2279   2762   1752     82   -151    156       N  
ATOM     20  CA  GLY A   4      25.242   6.664  45.814  1.00 18.25           C  
ANISOU   20  CA  GLY A   4     2333   2830   1770    269   -199    258       C  
ATOM     21  C   GLY A   4      24.108   5.958  46.520  1.00 17.59           C  
ANISOU   21  C   GLY A   4     2336   2633   1714    323   -192    260       C  
ATOM     22  O   GLY A   4      24.193   4.746  46.805  1.00 20.73           O  
ANISOU   22  O   GLY A   4     2804   2801   2270    525   -195    578       O  
ATOM     23  N   LYS A   5      23.012   6.649  46.804  1.00 17.09           N  
ANISOU   23  N   LYS A   5     2221   2695   1577    289   -212    364       N  
ATOM     24  CA  LYS A   5      21.879   6.094  47.515  1.00 17.10           C  
ANISOU   24  CA  LYS A   5     2157   2601   1739    162   -215    388       C  
ATOM     25  C   LYS A   5      20.626   5.988  46.635  1.00 14.87           C  
ANISOU   25  C   LYS A   5     2102   2097   1452    158   -134    376       C  
ATOM     26  O   LYS A   5      20.447   6.764  45.671  1.00 14.56           O  
ANISOU   26  O   LYS A   5     2153   2075   1304    254   -200    357       O  
ATOM     27  CB  LYS A   5      21.513   7.001  48.713  1.00 20.92           C  
ANISOU   27  CB  LYS A   5     2963   3099   1888     53    -87    134       C  
ATOM     28  CG ALYS A   5      22.671   7.302  49.675  0.68 24.38           C  
ANISOU   28  CG ALYS A   5     2987   4017   2259      9   -197    154       C  
ATOM     29  CD ALYS A   5      22.298   8.434  50.627  0.68 30.32           C  
ANISOU   29  CD ALYS A   5     4081   4047   3392    221    273    -34       C  
ATOM     30  CE ALYS A   5      23.356   8.596  51.712  0.68 34.11           C  
ANISOU   30  CE ALYS A   5     4217   4854   3890    187     30    169       C  
ATOM     31  NZ ALYS A   5      23.183   9.840  52.509  0.68 35.87           N  
ANISOU   31  NZ ALYS A   5     4618   4890   4120    280     86    141       N  
ATOM     32  CG BLYS A   5      22.591   6.996  49.800  0.32 24.31           C  
ANISOU   32  CG BLYS A   5     3066   3621   2550     62   -323    231       C  
ATOM     33  CD BLYS A   5      22.107   7.688  51.064  0.32 28.34           C  
ANISOU   33  CD BLYS A   5     3882   3828   3059    144    167     84       C  
ATOM     34  CE BLYS A   5      23.201   7.759  52.122  0.32 30.69           C  
ANISOU   34  CE BLYS A   5     4123   4140   3399    187    -52    114       C  
ATOM     35  NZ BLYS A   5      24.425   8.429  51.601  0.32 32.08           N  
ANISOU   35  NZ BLYS A   5     4162   4389   3640    139     19     87       N  
ATOM     36  N   VAL A   6      19.732   5.075  46.929  1.00 14.72           N  
ANISOU   36  N   VAL A   6     2167   2037   1388    187   -133    319       N  
ATOM     37  CA  VAL A   6      18.418   5.003  46.324  1.00 13.94           C  
ANISOU   37  CA  VAL A   6     2046   1813   1437     79     10    185       C  
ATOM     38  C   VAL A   6      17.637   6.251  46.718  1.00 13.88           C  
ANISOU   38  C   VAL A   6     2080   1952   1241    186    -52    132       C  
ATOM     39  O   VAL A   6      17.677   6.694  47.886  1.00 15.86           O  
ANISOU   39  O   VAL A   6     2480   2306   1241    437    -54    145       O  
ATOM     40  CB  VAL A   6      17.666   3.748  46.803  1.00 15.64           C  
ANISOU   40  CB  VAL A   6     2200   1987   1757    -31     58    425       C  
ATOM     41  CG1 VAL A   6      16.227   3.758  46.317  1.00 17.43           C  
ANISOU   41  CG1 VAL A   6     2332   2280   2010     77   -115    548       C  
ATOM     42  CG2 VAL A   6      18.396   2.487  46.354  1.00 18.08           C  
ANISOU   42  CG2 VAL A   6     2595   2194   2080    238    -87    308       C  
ATOM     43  N   ILE A   7      16.943   6.883  45.752  1.00 12.90           N  
ANISOU   43  N   ILE A   7     1761   1786   1353    167      2    174       N  
ATOM     44  CA  ILE A   7      16.032   7.981  46.022  1.00 12.71           C  
ANISOU   44  CA  ILE A   7     1830   1669   1329    105      6    177       C  
ATOM     45  C   ILE A   7      14.572   7.497  45.918  1.00 11.73           C  
ANISOU   45  C   ILE A   7     1847   1407   1203     97     18     89       C  
ATOM     46  O   ILE A   7      14.219   6.896  44.893  1.00 14.17           O  
ANISOU   46  O   ILE A   7     1957   2067   1358    -22     77   -210       O  
ATOM     47  CB  ILE A   7      16.271   9.182  45.065  1.00 13.13           C  
ANISOU   47  CB  ILE A   7     1770   1654   1566    125   -110    346       C  
ATOM     48  CG1 ILE A   7      17.584   9.898  45.374  1.00 13.19           C  
ANISOU   48  CG1 ILE A   7     1869   1692   1451    114   -130    145       C  
ATOM     49  CG2 ILE A   7      15.081  10.149  45.102  1.00 14.96           C  
ANISOU   49  CG2 ILE A   7     2039   1636   2009    189    100    409       C  
ATOM     50  CD1 ILE A   7      17.960  10.992  44.372  1.00 14.51           C  
ANISOU   50  CD1 ILE A   7     2105   1774   1633    228    164    161       C  
ATOM     51  N   LYS A   8      13.760   7.764  46.939  1.00 11.56           N  
ANISOU   51  N   LYS A   8     1768   1469   1157     56     19    136       N  
ATOM     52  CA  LYS A   8      12.318   7.581  46.855  1.00 11.95           C  
ANISOU   52  CA  LYS A   8     1758   1528   1256     37    118    255       C  
ATOM     53  C   LYS A   8      11.704   8.895  46.393  1.00 11.51           C  
ANISOU   53  C   LYS A   8     1827   1423   1123    -53      3    148       C  
ATOM     54  O   LYS A   8      12.025   9.938  47.009  1.00 11.95           O  
ANISOU   54  O   LYS A   8     1750   1524   1268     68    -26     36       O  
ATOM     55  CB ALYS A   8      11.720   7.158  48.220  0.64 13.04           C  
ANISOU   55  CB ALYS A   8     2037   1577   1339    -38    144    418       C  
ATOM     56  CG ALYS A   8      12.194   5.765  48.630  0.64 14.57           C  
ANISOU   56  CG ALYS A   8     2217   1566   1752   -193     57    445       C  
ATOM     57  CD ALYS A   8      11.590   5.406  49.983  0.64 18.45           C  
ANISOU   57  CD ALYS A   8     2594   2511   1905   -211     58    714       C  
ATOM     58  CE ALYS A   8      11.848   4.005  50.469  0.64 21.55           C  
ANISOU   58  CE ALYS A   8     3217   2538   2432    -49    -84    600       C  
ATOM     59  NZ ALYS A   8      11.071   3.612  51.681  0.64 23.86           N  
ANISOU   59  NZ ALYS A   8     3251   3116   2698   -141     84    598       N  
ATOM     60  CB BLYS A   8      11.719   7.220  48.228  0.35 14.19           C  
ANISOU   60  CB BLYS A   8     2066   1969   1355     43    159    347       C  
ATOM     61  CG BLYS A   8      11.603   5.722  48.436  0.35 16.80           C  
ANISOU   61  CG BLYS A   8     2375   2024   1984    -94    -30    254       C  
ATOM     62  CD BLYS A   8      10.986   5.412  49.793  0.35 19.81           C  
ANISOU   62  CD BLYS A   8     2618   2669   2241   -188    149    398       C  
ATOM     63  CE BLYS A   8      10.790   3.915  49.973  0.35 21.52           C  
ANISOU   63  CE BLYS A   8     2877   2691   2608   -182    124    382       C  
ATOM     64  NZ BLYS A   8      12.072   3.172  49.857  0.35 22.65           N  
ANISOU   64  NZ BLYS A   8     3001   2796   2808   -101    171    259       N  
ATOM     65  N   CYS A   9      10.872   8.916  45.359  1.00 10.98           N  
ANISOU   65  N   CYS A   9     1729   1364   1081      0    -22    166       N  
ATOM     66  CA  CYS A   9      10.271  10.153  44.863  1.00 10.90           C  
ANISOU   66  CA  CYS A   9     1555   1233   1353    -26     78    133       C  
ATOM     67  C   CYS A   9       8.936   9.815  44.209  1.00 10.95           C  
ANISOU   67  C   CYS A   9     1521   1436   1203    -44    130     33       C  
ATOM     68  O   CYS A   9       8.565   8.651  44.064  1.00 13.84           O  
ANISOU   68  O   CYS A   9     1922   1529   1808    -39   -144    -21       O  
ATOM     69  CB  CYS A   9      11.205  10.876  43.887  1.00 11.11           C  
ANISOU   69  CB  CYS A   9     1699   1430   1092     14    111    132       C  
ATOM     70  SG  CYS A   9      11.458  10.006  42.299  1.00 10.84           S  
ANISOU   70  SG  CYS A   9     1764   1248   1106    -12    219    152       S  
ATOM     71  N   LYS A  10       8.193  10.826  43.777  1.00 10.74           N  
ANISOU   71  N   LYS A  10     1527   1452   1101    -33    157     99       N  
ATOM     72  CA  LYS A  10       6.941  10.609  43.052  1.00 11.72           C  
ANISOU   72  CA  LYS A  10     1610   1547   1295     53     45     60       C  
ATOM     73  C   LYS A  10       7.220  10.543  41.529  1.00 11.17           C  
ANISOU   73  C   LYS A  10     1423   1489   1331   -107     -6    177       C  
ATOM     74  O   LYS A  10       8.072  11.306  40.990  1.00 11.75           O  
ANISOU   74  O   LYS A  10     1633   1455   1378   -187    -28    226       O  
ATOM     75  CB  LYS A  10       5.926  11.706  43.395  1.00 14.39           C  
ANISOU   75  CB  LYS A  10     1834   1810   1823    204     70    -74       C  
ATOM     76  CG  LYS A  10       5.561  11.819  44.892  1.00 17.46           C  
ANISOU   76  CG  LYS A  10     2313   2255   2065    157    395   -106       C  
ATOM     77  CD  LYS A  10       5.100  10.530  45.552  1.00 18.55           C  
ANISOU   77  CD  LYS A  10     2389   2353   2304    -26    442   -109       C  
ATOM     78  CE  LYS A  10       4.542  10.659  46.971  1.00 21.03           C  
ANISOU   78  CE  LYS A  10     2817   2892   2282     44    431   -251       C  
ATOM     79  NZ  LYS A  10       5.556  11.079  47.994  1.00 21.63           N  
ANISOU   79  NZ  LYS A  10     3143   2978   2098   -256    410     51       N  
ATOM     80  N   ALA A  11       6.462   9.687  40.852  1.00 11.34           N  
ANISOU   80  N   ALA A  11     1629   1486   1195   -146    -81    222       N  
ATOM     81  CA  ALA A  11       6.480   9.586  39.393  1.00 10.70           C  
ANISOU   81  CA  ALA A  11     1523   1349   1191   -180     94    234       C  
ATOM     82  C   ALA A  11       5.065   9.275  38.900  1.00 10.56           C  
ANISOU   82  C   ALA A  11     1420   1374   1217   -135    132    226       C  
ATOM     83  O   ALA A  11       4.204   8.811  39.663  1.00 13.79           O  
ANISOU   83  O   ALA A  11     1621   2464   1157   -257    109    395       O  
ATOM     84  CB  ALA A  11       7.451   8.528  38.913  1.00 11.43           C  
ANISOU   84  CB  ALA A  11     1690   1381   1273     20     14    379       C  
ATOM     85  N   ALA A  12       4.840   9.490  37.587  1.00 10.61           N  
ANISOU   85  N   ALA A  12     1564   1294   1174   -178      8    155       N  
ATOM     86  CA  ALA A  12       3.567   9.145  36.960  1.00 10.60           C  
ANISOU   86  CA  ALA A  12     1426   1381   1222   -180    178    223       C  
ATOM     87  C   ALA A  12       3.771   7.794  36.260  1.00 10.64           C  
ANISOU   87  C   ALA A  12     1566   1361   1116   -373    215    183       C  
ATOM     88  O   ALA A  12       4.399   7.711  35.206  1.00 12.48           O  
ANISOU   88  O   ALA A  12     2171   1362   1207   -360    412    144       O  
ATOM     89  CB  ALA A  12       3.173  10.212  35.944  1.00 12.21           C  
ANISOU   89  CB  ALA A  12     1547   1702   1389   -177     50    464       C  
ATOM     90  N   VAL A  13       3.234   6.743  36.880  1.00 11.05           N  
ANISOU   90  N   VAL A  13     1654   1367   1176   -281    296    203       N  
ATOM     91  CA  VAL A  13       3.352   5.377  36.370  1.00 10.70           C  
ANISOU   91  CA  VAL A  13     1533   1292   1241   -167    137    357       C  
ATOM     92  C   VAL A  13       2.113   5.046  35.537  1.00  9.93           C  
ANISOU   92  C   VAL A  13     1376   1078   1318   -169    260    214       C  
ATOM     93  O   VAL A  13       0.963   5.334  35.906  1.00 12.23           O  
ANISOU   93  O   VAL A  13     1483   1753   1411   -108    258    214       O  
ATOM     94  CB  VAL A  13       3.505   4.387  37.546  1.00 11.42           C  
ANISOU   94  CB  VAL A  13     1635   1365   1339   -342    188    410       C  
ATOM     95  CG1 VAL A  13       3.608   2.944  37.044  1.00 12.68           C  
ANISOU   95  CG1 VAL A  13     2080   1319   1420   -167    136    410       C  
ATOM     96  CG2 VAL A  13       4.722   4.726  38.381  1.00 13.54           C  
ANISOU   96  CG2 VAL A  13     1815   1758   1570   -169     35    419       C  
ATOM     97  N   LEU A  14       2.352   4.446  34.351  1.00 10.28           N  
ANISOU   97  N   LEU A  14     1496   1202   1209   -224    266    292       N  
ATOM     98  CA  LEU A  14       1.287   3.938  33.496  1.00 10.62           C  
ANISOU   98  CA  LEU A  14     1544   1212   1281   -159    204    268       C  
ATOM     99  C   LEU A  14       1.316   2.408  33.605  1.00 10.90           C  
ANISOU   99  C   LEU A  14     1635   1293   1213   -202    216    251       C  
ATOM    100  O   LEU A  14       2.228   1.738  33.124  1.00 11.10           O  
ANISOU  100  O   LEU A  14     1636   1259   1321   -240    243    278       O  
ATOM    101  CB  LEU A  14       1.469   4.394  32.031  1.00 11.06           C  
ANISOU  101  CB  LEU A  14     1585   1370   1249   -199    121    351       C  
ATOM    102  CG  LEU A  14       0.270   4.014  31.133  1.00 12.31           C  
ANISOU  102  CG  LEU A  14     1719   1592   1368   -386    104    374       C  
ATOM    103  CD1 LEU A  14      -0.963   4.856  31.416  1.00 14.15           C  
ANISOU  103  CD1 LEU A  14     1785   2002   1589   -233     97    388       C  
ATOM    104  CD2 LEU A  14       0.657   4.081  29.657  1.00 14.02           C  
ANISOU  104  CD2 LEU A  14     2144   1861   1322   -193     83    430       C  
ATOM    105  N   TRP A  15       0.306   1.876  34.321  1.00 11.71           N  
ANISOU  105  N   TRP A  15     1745   1419   1286   -332    309    383       N  
ATOM    106  CA  TRP A  15       0.208   0.446  34.571  1.00 12.92           C  
ANISOU  106  CA  TRP A  15     2103   1407   1397   -419    231    413       C  
ATOM    107  C   TRP A  15      -0.476  -0.291  33.419  1.00 14.40           C  
ANISOU  107  C   TRP A  15     2227   1579   1666   -491    140    348       C  
ATOM    108  O   TRP A  15      -0.214  -1.485  33.242  1.00 17.41           O  
ANISOU  108  O   TRP A  15     3023   1691   1901   -357     76    276       O  
ATOM    109  CB  TRP A  15      -0.578   0.215  35.903  1.00 13.41           C  
ANISOU  109  CB  TRP A  15     1947   1628   1521   -347    245    359       C  
ATOM    110  CG  TRP A  15       0.134   0.635  37.141  1.00 13.28           C  
ANISOU  110  CG  TRP A  15     1970   1631   1446   -437    314    444       C  
ATOM    111  CD1 TRP A  15      -0.138   1.754  37.872  1.00 14.63           C  
ANISOU  111  CD1 TRP A  15     2134   1823   1601   -220    344    375       C  
ATOM    112  CD2 TRP A  15       1.209  -0.055  37.812  1.00 13.07           C  
ANISOU  112  CD2 TRP A  15     2057   1666   1243   -275    309    351       C  
ATOM    113  NE1 TRP A  15       0.694   1.799  38.954  1.00 14.55           N  
ANISOU  113  NE1 TRP A  15     2289   1753   1487   -283    385    276       N  
ATOM    114  CE2 TRP A  15       1.513   0.716  38.965  1.00 13.03           C  
ANISOU  114  CE2 TRP A  15     1993   1674   1283   -381    354    330       C  
ATOM    115  CE3 TRP A  15       1.932  -1.231  37.616  1.00 12.88           C  
ANISOU  115  CE3 TRP A  15     2049   1699   1147   -277    265    420       C  
ATOM    116  CZ2 TRP A  15       2.503   0.339  39.873  1.00 13.98           C  
ANISOU  116  CZ2 TRP A  15     2165   1719   1428   -513    164    304       C  
ATOM    117  CZ3 TRP A  15       2.906  -1.609  38.529  1.00 14.46           C  
ANISOU  117  CZ3 TRP A  15     2194   1841   1459   -208    125    475       C  
ATOM    118  CH2 TRP A  15       3.214  -0.790  39.647  1.00 14.31           C  
ANISOU  118  CH2 TRP A  15     2027   2076   1333   -257    154    501       C  
ATOM    119  N   GLU A  16      -1.355   0.366  32.674  1.00 15.77           N  
ANISOU  119  N   GLU A  16     2356   1895   1739   -646     -4    553       N  
ATOM    120  CA  GLU A  16      -2.250  -0.230  31.702  1.00 19.35           C  
ANISOU  120  CA  GLU A  16     2792   2502   2057   -691   -218    569       C  
ATOM    121  C   GLU A  16      -2.541   0.780  30.605  1.00 16.16           C  
ANISOU  121  C   GLU A  16     2297   2156   1689   -576     76    259       C  
ATOM    122  O   GLU A  16      -2.684   1.946  30.899  1.00 16.66           O  
ANISOU  122  O   GLU A  16     2401   2147   1782   -595    116    448       O  
ATOM    123  CB AGLU A  16      -3.527  -0.764  32.396  0.52 23.94           C  
ANISOU  123  CB AGLU A  16     2911   3217   2969   -766      5    621       C  
ATOM    124  CG AGLU A  16      -4.033  -0.018  33.615  0.52 30.80           C  
ANISOU  124  CG AGLU A  16     3883   4059   3760   -121    142     93       C  
ATOM    125  CD AGLU A  16      -4.837  -0.844  34.610  0.52 33.69           C  
ANISOU  125  CD AGLU A  16     4264   4513   4022   -153    280    338       C  
ATOM    126  OE1AGLU A  16      -5.408  -1.860  34.150  0.52 33.77           O  
ANISOU  126  OE1AGLU A  16     4197   4569   4065   -313    400    470       O  
ATOM    127  OE2AGLU A  16      -4.911  -0.519  35.827  0.52 31.45           O  
ANISOU  127  OE2AGLU A  16     3992   4096   3861   -550    690    707       O  
ATOM    128  CB BGLU A  16      -3.558  -0.603  32.462  0.48 21.19           C  
ANISOU  128  CB BGLU A  16     2991   2792   2269   -664     55    626       C  
ATOM    129  CG BGLU A  16      -4.640  -1.266  31.662  0.48 22.20           C  
ANISOU  129  CG BGLU A  16     3081   3057   2297   -616     37    566       C  
ATOM    130  CD BGLU A  16      -5.882  -1.668  32.455  0.48 24.07           C  
ANISOU  130  CD BGLU A  16     3324   3301   2519   -682    257    606       C  
ATOM    131  OE1BGLU A  16      -6.060  -1.315  33.636  0.48 21.77           O  
ANISOU  131  OE1BGLU A  16     2771   2863   2638   -763    392    601       O  
ATOM    132  OE2BGLU A  16      -6.695  -2.352  31.796  0.48 25.14           O  
ANISOU  132  OE2BGLU A  16     3356   3574   2622   -816    298    643       O  
ATOM    133  N   GLU A  17      -2.772   0.314  29.374  1.00 15.58           N  
ANISOU  133  N   GLU A  17     2217   2008   1694   -573     29    435       N  
ATOM    134  CA  GLU A  17      -3.223   1.170  28.291  1.00 15.90           C  
ANISOU  134  CA  GLU A  17     2210   2239   1593   -269     34    271       C  
ATOM    135  C   GLU A  17      -4.589   1.765  28.598  1.00 14.49           C  
ANISOU  135  C   GLU A  17     1841   2141   1523   -605     -6    283       C  
ATOM    136  O   GLU A  17      -5.420   1.118  29.315  1.00 16.82           O  
ANISOU  136  O   GLU A  17     2084   2538   1770   -811    188    429       O  
ATOM    137  CB AGLU A  17      -3.441   0.513  26.925  0.62 14.69           C  
ANISOU  137  CB AGLU A  17     2036   1965   1580   -228    181    318       C  
ATOM    138  CG AGLU A  17      -2.164   0.046  26.263  0.62 15.55           C  
ANISOU  138  CG AGLU A  17     2177   1884   1846   -126    326    228       C  
ATOM    139  CD AGLU A  17      -2.446  -0.681  24.952  0.62 18.47           C  
ANISOU  139  CD AGLU A  17     2407   2547   2063   -244    294    -68       C  
ATOM    140  OE1AGLU A  17      -3.486  -0.472  24.290  0.62 20.66           O  
ANISOU  140  OE1AGLU A  17     2794   2718   2339     96     71   -371       O  
ATOM    141  OE2AGLU A  17      -1.558  -1.510  24.645  0.62 20.36           O  
ANISOU  141  OE2AGLU A  17     2701   2560   2474   -208    258   -396       O  
ATOM    142  CB BGLU A  17      -3.178   0.207  27.079  0.38 19.10           C  
ANISOU  142  CB BGLU A  17     2759   2589   1908   -203     95     55       C  
ATOM    143  CG BGLU A  17      -1.998  -0.739  27.070  0.38 22.78           C  
ANISOU  143  CG BGLU A  17     2837   3187   2631     12     70    -30       C  
ATOM    144  CD BGLU A  17      -1.897  -2.092  27.699  0.38 23.87           C  
ANISOU  144  CD BGLU A  17     3063   3259   2748    -90      6     70       C  
ATOM    145  OE1BGLU A  17      -2.286  -2.541  28.810  0.38 19.61           O  
ANISOU  145  OE1BGLU A  17     2456   2303   2693   -161    -23   -148       O  
ATOM    146  OE2BGLU A  17      -1.232  -2.929  26.988  0.38 27.49           O  
ANISOU  146  OE2BGLU A  17     3519   3552   3374    203     63   -107       O  
ATOM    147  N   LYS A  18      -4.922   2.943  28.096  1.00 14.99           N  
ANISOU  147  N   LYS A  18     1899   2162   1635   -587    196    374       N  
ATOM    148  CA  LYS A  18      -6.206   3.584  28.125  1.00 17.13           C  
ANISOU  148  CA  LYS A  18     2119   2381   2007   -371    185    186       C  
ATOM    149  C   LYS A  18      -6.708   3.888  29.526  1.00 17.85           C  
ANISOU  149  C   LYS A  18     2085   2800   1898   -531    210    258       C  
ATOM    150  O   LYS A  18      -7.921   3.854  29.795  1.00 21.30           O  
ANISOU  150  O   LYS A  18     2140   3438   2516   -377    183      7       O  
ATOM    151  CB  LYS A  18      -7.234   2.721  27.324  1.00 22.08           C  
ANISOU  151  CB  LYS A  18     2556   3123   2709   -731    -69    221       C  
ATOM    152  CG  LYS A  18      -6.835   2.662  25.827  1.00 29.96           C  
ANISOU  152  CG  LYS A  18     3922   4382   3078   -180    415    415       C  
ATOM    153  CD  LYS A  18      -7.831   1.834  25.018  1.00 37.90           C  
ANISOU  153  CD  LYS A  18     4734   5043   4624   -452   -255    226       C  
ATOM    154  CE  LYS A  18      -7.265   1.517  23.640  1.00 44.23           C  
ANISOU  154  CE  LYS A  18     5785   6039   4981   -263    208    210       C  
ATOM    155  NZ  LYS A  18      -6.071   0.624  23.747  1.00 47.76           N  
ANISOU  155  NZ  LYS A  18     6179   6366   5603     23     58    200       N  
ATOM    156  N   LYS A  19      -5.779   4.127  30.463  1.00 15.57           N  
ANISOU  156  N   LYS A  19     1968   2255   1694   -670    382    178       N  
ATOM    157  CA  LYS A  19      -6.091   4.497  31.837  1.00 16.02           C  
ANISOU  157  CA  LYS A  19     2150   2212   1726   -547    229    188       C  
ATOM    158  C   LYS A  19      -5.313   5.753  32.242  1.00 14.20           C  
ANISOU  158  C   LYS A  19     1590   2113   1694   -393    182    196       C  
ATOM    159  O   LYS A  19      -4.266   6.049  31.612  1.00 13.81           O  
ANISOU  159  O   LYS A  19     1672   1938   1638   -309    318    301       O  
ATOM    160  CB  LYS A  19      -5.731   3.364  32.807  1.00 19.29           C  
ANISOU  160  CB  LYS A  19     2988   2406   1935   -327    232    286       C  
ATOM    161  CG  LYS A  19      -6.499   2.050  32.653  1.00 23.13           C  
ANISOU  161  CG  LYS A  19     3282   2892   2614   -626    402     74       C  
ATOM    162  CD  LYS A  19      -7.989   2.230  32.934  1.00 28.56           C  
ANISOU  162  CD  LYS A  19     3414   3943   3495   -260    403    220       C  
ATOM    163  CE  LYS A  19      -8.768   0.931  32.730  1.00 31.78           C  
ANISOU  163  CE  LYS A  19     3899   4164   4011   -387    302     36       C  
ATOM    164  NZ  LYS A  19      -8.746   0.115  33.966  1.00 34.13           N  
ANISOU  164  NZ  LYS A  19     4158   4604   4205   -271    245    244       N  
ATOM    165  N   PRO A  20      -5.805   6.481  33.210  1.00 14.32           N  
ANISOU  165  N   PRO A  20     1639   2196   1607   -358    244    253       N  
ATOM    166  CA  PRO A  20      -5.060   7.618  33.740  1.00 13.71           C  
ANISOU  166  CA  PRO A  20     1529   2031   1649   -194    229    285       C  
ATOM    167  C   PRO A  20      -3.700   7.175  34.273  1.00 12.20           C  
ANISOU  167  C   PRO A  20     1605   1680   1351   -224    198    329       C  
ATOM    168  O   PRO A  20      -3.458   6.040  34.725  1.00 13.22           O  
ANISOU  168  O   PRO A  20     1629   1800   1592   -365    185    402       O  
ATOM    169  CB  PRO A  20      -5.918   8.155  34.915  1.00 15.22           C  
ANISOU  169  CB  PRO A  20     1559   2314   1910   -186    351    129       C  
ATOM    170  CG  PRO A  20      -7.299   7.648  34.553  1.00 18.48           C  
ANISOU  170  CG  PRO A  20     1696   2906   2418   -322    364   -124       C  
ATOM    171  CD  PRO A  20      -7.092   6.282  33.922  1.00 17.19           C  
ANISOU  171  CD  PRO A  20     1636   2606   2287   -367    384    123       C  
ATOM    172  N   PHE A  21      -2.751   8.127  34.254  1.00 11.75           N  
ANISOU  172  N   PHE A  21     1496   1674   1295   -256    280    340       N  
ATOM    173  CA  PHE A  21      -1.486   7.930  34.958  1.00 11.54           C  
ANISOU  173  CA  PHE A  21     1541   1562   1281   -245    213    304       C  
ATOM    174  C   PHE A  21      -1.742   7.852  36.473  1.00 11.51           C  
ANISOU  174  C   PHE A  21     1560   1479   1332    -21    183    189       C  
ATOM    175  O   PHE A  21      -2.621   8.553  36.991  1.00 13.10           O  
ANISOU  175  O   PHE A  21     1863   1771   1345    173    353    334       O  
ATOM    176  CB  PHE A  21      -0.530   9.099  34.657  1.00 11.58           C  
ANISOU  176  CB  PHE A  21     1443   1583   1374   -178    154    290       C  
ATOM    177  CG  PHE A  21      -0.061   9.169  33.228  1.00 10.40           C  
ANISOU  177  CG  PHE A  21     1322   1264   1367   -236    172    123       C  
ATOM    178  CD1 PHE A  21       1.021   8.415  32.803  1.00 11.06           C  
ANISOU  178  CD1 PHE A  21     1382   1410   1412   -116    157    230       C  
ATOM    179  CD2 PHE A  21      -0.710   9.977  32.294  1.00 11.32           C  
ANISOU  179  CD2 PHE A  21     1357   1558   1386    -59    211    257       C  
ATOM    180  CE1 PHE A  21       1.425   8.466  31.459  1.00 10.82           C  
ANISOU  180  CE1 PHE A  21     1332   1379   1399   -256    213    298       C  
ATOM    181  CE2 PHE A  21      -0.342  10.029  30.962  1.00 10.84           C  
ANISOU  181  CE2 PHE A  21     1213   1570   1335   -173     65    433       C  
ATOM    182  CZ  PHE A  21       0.729   9.268  30.560  1.00 11.33           C  
ANISOU  182  CZ  PHE A  21     1454   1520   1330   -219    181    239       C  
ATOM    183  N   SER A  22      -0.901   7.096  37.183  1.00 12.05           N  
ANISOU  183  N   SER A  22     1597   1741   1240    -14    183    352       N  
ATOM    184  CA  SER A  22      -0.961   6.993  38.652  1.00 12.29           C  
ANISOU  184  CA  SER A  22     1716   1695   1258   -114    338    423       C  
ATOM    185  C   SER A  22       0.242   7.697  39.246  1.00 12.47           C  
ANISOU  185  C   SER A  22     1656   1808   1276    -10    223    349       C  
ATOM    186  O   SER A  22       1.391   7.254  39.071  1.00 13.61           O  
ANISOU  186  O   SER A  22     1734   2008   1428     29    153    310       O  
ATOM    187  CB  SER A  22      -0.916   5.506  39.037  1.00 14.71           C  
ANISOU  187  CB  SER A  22     2310   1833   1445   -172    500    431       C  
ATOM    188  OG  SER A  22      -0.966   5.397  40.465  1.00 17.38           O  
ANISOU  188  OG  SER A  22     2746   2310   1546    -32    606    605       O  
ATOM    189  N   ILE A  23       0.027   8.789  39.990  1.00 12.61           N  
ANISOU  189  N   ILE A  23     1618   1862   1312    -38    266    309       N  
ATOM    190  CA  ILE A  23       1.105   9.537  40.634  1.00 13.91           C  
ANISOU  190  CA  ILE A  23     1851   2020   1415    -53     39    311       C  
ATOM    191  C   ILE A  23       1.367   8.870  41.978  1.00 13.83           C  
ANISOU  191  C   ILE A  23     1870   2172   1215     -9    240    311       C  
ATOM    192  O   ILE A  23       0.507   8.918  42.898  1.00 16.20           O  
ANISOU  192  O   ILE A  23     2198   2498   1458    218    459    304       O  
ATOM    193  CB AILE A  23       0.744  11.025  40.754  0.55 15.58           C  
ANISOU  193  CB AILE A  23     2152   2012   1756    -66     41    310       C  
ATOM    194  CG1AILE A  23       0.445  11.648  39.386  0.55 17.69           C  
ANISOU  194  CG1AILE A  23     2574   2267   1880   -164    -12    413       C  
ATOM    195  CG2AILE A  23       1.890  11.827  41.385  0.55 18.70           C  
ANISOU  195  CG2AILE A  23     2315   2373   2416   -319     94    118       C  
ATOM    196  CD1AILE A  23      -0.860  11.342  38.713  0.55 18.09           C  
ANISOU  196  CD1AILE A  23     2653   2403   1817   -137    -41    306       C  
ATOM    197  CB BILE A  23       0.753  11.022  40.863  0.45 16.16           C  
ANISOU  197  CB BILE A  23     2241   2131   1768    -37    -13    190       C  
ATOM    198  CG1BILE A  23       0.687  11.797  39.550  0.45 18.89           C  
ANISOU  198  CG1BILE A  23     2663   2725   1788   -206   -151    298       C  
ATOM    199  CG2BILE A  23       1.714  11.678  41.869  0.45 18.90           C  
ANISOU  199  CG2BILE A  23     2576   2624   1979   -309    -61     69       C  
ATOM    200  CD1BILE A  23       1.986  12.248  38.953  0.45 18.90           C  
ANISOU  200  CD1BILE A  23     2394   2394   2394      0      0      0       C  
ATOM    201  N   GLU A  24       2.503   8.201  42.119  1.00 13.57           N  
ANISOU  201  N   GLU A  24     1912   2065   1180     47    227    311       N  
ATOM    202  CA  GLU A  24       2.824   7.462  43.331  1.00 13.76           C  
ANISOU  202  CA  GLU A  24     1962   1902   1365    -97    117    349       C  
ATOM    203  C   GLU A  24       4.320   7.315  43.507  1.00 12.62           C  
ANISOU  203  C   GLU A  24     1898   1706   1193      3    158     16       C  
ATOM    204  O   GLU A  24       5.127   7.659  42.648  1.00 13.19           O  
ANISOU  204  O   GLU A  24     2124   1570   1319    -76    216    243       O  
ATOM    205  CB  GLU A  24       2.146   6.125  43.294  1.00 14.32           C  
ANISOU  205  CB  GLU A  24     2080   1920   1440    -96    261    396       C  
ATOM    206  CG  GLU A  24       2.576   5.208  42.184  1.00 14.39           C  
ANISOU  206  CG  GLU A  24     2184   1611   1673    -67    214    356       C  
ATOM    207  CD  GLU A  24       1.799   3.909  42.209  1.00 15.59           C  
ANISOU  207  CD  GLU A  24     2557   1869   1498   -283    231    438       C  
ATOM    208  OE1 GLU A  24       2.062   3.083  43.148  1.00 16.63           O  
ANISOU  208  OE1 GLU A  24     2836   1808   1674    -51    312    584       O  
ATOM    209  OE2 GLU A  24       0.895   3.642  41.399  1.00 15.84           O  
ANISOU  209  OE2 GLU A  24     2852   1602   1562   -106    118    428       O  
ATOM    210  N   GLU A  25       4.709   6.814  44.703  1.00 12.86           N  
ANISOU  210  N   GLU A  25     1811   1834   1240     53     24     49       N  
ATOM    211  CA  GLU A  25       6.113   6.708  45.051  1.00 12.59           C  
ANISOU  211  CA  GLU A  25     1844   1767   1172    -42     62    -16       C  
ATOM    212  C   GLU A  25       6.817   5.612  44.235  1.00 11.77           C  
ANISOU  212  C   GLU A  25     1804   1482   1187   -162     16     87       C  
ATOM    213  O   GLU A  25       6.323   4.470  44.169  1.00 13.22           O  
ANISOU  213  O   GLU A  25     2093   1521   1409   -187    200     91       O  
ATOM    214  CB  GLU A  25       6.281   6.450  46.564  1.00 14.03           C  
ANISOU  214  CB  GLU A  25     2082   2018   1229     44     44     65       C  
ATOM    215  CG  GLU A  25       7.761   6.373  46.972  1.00 14.24           C  
ANISOU  215  CG  GLU A  25     2142   2007   1263    -37     59    101       C  
ATOM    216  CD  GLU A  25       7.921   6.368  48.474  1.00 15.86           C  
ANISOU  216  CD  GLU A  25     2508   2128   1391     82     61     55       C  
ATOM    217  OE1 GLU A  25       7.990   7.458  49.069  1.00 18.81           O  
ANISOU  217  OE1 GLU A  25     3192   2445   1509      2   -102   -149       O  
ATOM    218  OE2 GLU A  25       8.004   5.283  49.095  1.00 18.80           O  
ANISOU  218  OE2 GLU A  25     3198   2302   1642    115   -224    180       O  
ATOM    219  N   VAL A  26       8.008   5.915  43.742  1.00 12.06           N  
ANISOU  219  N   VAL A  26     1744   1569   1268      0     18    126       N  
ATOM    220  CA  VAL A  26       8.900   4.984  43.074  1.00 11.03           C  
ANISOU  220  CA  VAL A  26     1648   1357   1186   -199    127    204       C  
ATOM    221  C   VAL A  26      10.263   5.041  43.752  1.00 11.17           C  
ANISOU  221  C   VAL A  26     1670   1375   1198    -66    137    198       C  
ATOM    222  O   VAL A  26      10.587   6.029  44.458  1.00 12.94           O  
ANISOU  222  O   VAL A  26     2024   1522   1373    218    -98    -25       O  
ATOM    223  CB  VAL A  26       9.054   5.247  41.555  1.00 11.51           C  
ANISOU  223  CB  VAL A  26     1841   1351   1181   -142     17    223       C  
ATOM    224  CG1 VAL A  26       7.694   5.192  40.880  1.00 12.50           C  
ANISOU  224  CG1 VAL A  26     1901   1616   1234   -317     38    258       C  
ATOM    225  CG2 VAL A  26       9.750   6.590  41.291  1.00 12.55           C  
ANISOU  225  CG2 VAL A  26     1950   1564   1256   -263     50    383       C  
ATOM    226  N   GLU A  27      11.079   4.009  43.580  1.00 11.84           N  
ANISOU  226  N   GLU A  27     1817   1423   1257     95    152    318       N  
ATOM    227  CA  GLU A  27      12.471   3.976  44.004  1.00 11.90           C  
ANISOU  227  CA  GLU A  27     1981   1414   1127    -56     81    237       C  
ATOM    228  C   GLU A  27      13.361   4.102  42.770  1.00 11.40           C  
ANISOU  228  C   GLU A  27     1729   1368   1234     13     62    183       C  
ATOM    229  O   GLU A  27      13.209   3.344  41.796  1.00 13.24           O  
ANISOU  229  O   GLU A  27     2196   1457   1376    -21    185    118       O  
ATOM    230  CB AGLU A  27      12.799   2.667  44.738  0.52 14.60           C  
ANISOU  230  CB AGLU A  27     2412   1672   1463     52    -10    418       C  
ATOM    231  CG AGLU A  27      12.079   2.539  46.081  0.52 18.43           C  
ANISOU  231  CG AGLU A  27     2726   2595   1682    -78    183    388       C  
ATOM    232  CD AGLU A  27      12.377   1.198  46.737  0.52 22.22           C  
ANISOU  232  CD AGLU A  27     3138   2739   2565     28     15    479       C  
ATOM    233  OE1AGLU A  27      11.924   0.176  46.186  0.52 22.35           O  
ANISOU  233  OE1AGLU A  27     3109   2758   2626    137    -96    404       O  
ATOM    234  OE2AGLU A  27      13.097   1.198  47.769  0.52 24.89           O  
ANISOU  234  OE2AGLU A  27     3238   3390   2830    243   -202    366       O  
ATOM    235  CB BGLU A  27      12.758   2.671  44.768  0.48 14.05           C  
ANISOU  235  CB BGLU A  27     2404   1675   1260     37     36    384       C  
ATOM    236  CG BGLU A  27      11.797   2.517  45.941  0.48 17.81           C  
ANISOU  236  CG BGLU A  27     2637   2423   1708   -108    337    317       C  
ATOM    237  CD BGLU A  27      12.232   1.610  47.061  0.48 21.50           C  
ANISOU  237  CD BGLU A  27     3006   2866   2297    113    -40    488       C  
ATOM    238  OE1BGLU A  27      13.238   0.853  46.911  0.48 21.97           O  
ANISOU  238  OE1BGLU A  27     3085   2791   2471    149     12    514       O  
ATOM    239  OE2BGLU A  27      11.507   1.666  48.086  0.48 24.49           O  
ANISOU  239  OE2BGLU A  27     3267   3326   2713     15    235    304       O  
ATOM    240  N   VAL A  28      14.282   5.052  42.804  1.00 11.14           N  
ANISOU  240  N   VAL A  28     1724   1324   1184    -36    121     93       N  
ATOM    241  CA  VAL A  28      15.205   5.361  41.699  1.00 10.92           C  
ANISOU  241  CA  VAL A  28     1612   1280   1255    -42      6    212       C  
ATOM    242  C   VAL A  28      16.620   4.998  42.137  1.00 11.12           C  
ANISOU  242  C   VAL A  28     1733   1429   1063     93     -1    232       C  
ATOM    243  O   VAL A  28      17.183   5.607  43.067  1.00 12.06           O  
ANISOU  243  O   VAL A  28     1702   1591   1288     36   -108    151       O  
ATOM    244  CB  VAL A  28      15.109   6.850  41.294  1.00 11.22           C  
ANISOU  244  CB  VAL A  28     1624   1338   1301     55    -15    232       C  
ATOM    245  CG1 VAL A  28      15.986   7.075  40.058  1.00 12.60           C  
ANISOU  245  CG1 VAL A  28     1958   1469   1359    143    159    150       C  
ATOM    246  CG2 VAL A  28      13.680   7.260  41.028  1.00 11.90           C  
ANISOU  246  CG2 VAL A  28     1675   1358   1489    138    -41    146       C  
ATOM    247  N   ALA A  29      17.201   3.982  41.498  1.00 11.41           N  
ANISOU  247  N   ALA A  29     1736   1384   1214    168   -105    235       N  
ATOM    248  CA  ALA A  29      18.561   3.543  41.868  1.00 11.69           C  
ANISOU  248  CA  ALA A  29     1608   1611   1222    101     19    166       C  
ATOM    249  C   ALA A  29      19.612   4.568  41.531  1.00 11.29           C  
ANISOU  249  C   ALA A  29     1655   1459   1177    132    -39    195       C  
ATOM    250  O   ALA A  29      19.398   5.424  40.627  1.00 12.15           O  
ANISOU  250  O   ALA A  29     1765   1617   1233    121   -160    232       O  
ATOM    251  CB  ALA A  29      18.856   2.259  41.076  1.00 13.38           C  
ANISOU  251  CB  ALA A  29     1922   1680   1483    267   -156    177       C  
ATOM    252  N   PRO A  30      20.775   4.542  42.181  1.00 12.68           N  
ANISOU  252  N   PRO A  30     1708   1732   1377    161   -103    275       N  
ATOM    253  CA  PRO A  30      21.857   5.460  41.811  1.00 12.50           C  
ANISOU  253  CA  PRO A  30     1629   1716   1405    157   -218    213       C  
ATOM    254  C   PRO A  30      22.459   5.102  40.448  1.00 12.54           C  
ANISOU  254  C   PRO A  30     1680   1576   1508    145    -54    286       C  
ATOM    255  O   PRO A  30      22.327   3.959  39.973  1.00 13.42           O  
ANISOU  255  O   PRO A  30     1964   1603   1530    191     80    233       O  
ATOM    256  CB  PRO A  30      22.893   5.331  42.936  1.00 15.12           C  
ANISOU  256  CB  PRO A  30     2012   2181   1551     69   -343    421       C  
ATOM    257  CG  PRO A  30      22.597   3.966  43.507  1.00 15.10           C  
ANISOU  257  CG  PRO A  30     2117   2058   1561    159   -294    338       C  
ATOM    258  CD  PRO A  30      21.137   3.646  43.310  1.00 13.75           C  
ANISOU  258  CD  PRO A  30     2000   1850   1373    131   -196    403       C  
ATOM    259  N   PRO A  31      23.117   6.047  39.775  1.00 12.62           N  
ANISOU  259  N   PRO A  31     1843   1604   1349    134    -67    178       N  
ATOM    260  CA  PRO A  31      23.668   5.791  38.441  1.00 11.98           C  
ANISOU  260  CA  PRO A  31     1609   1529   1412    155    -95     77       C  
ATOM    261  C   PRO A  31      24.846   4.830  38.483  1.00 12.82           C  
ANISOU  261  C   PRO A  31     1708   1738   1427    280    -76    129       C  
ATOM    262  O   PRO A  31      25.753   4.969  39.337  1.00 15.31           O  
ANISOU  262  O   PRO A  31     2037   2069   1712    420   -328     86       O  
ATOM    263  CB  PRO A  31      24.093   7.182  37.933  1.00 13.42           C  
ANISOU  263  CB  PRO A  31     1902   1705   1493    105   -128    178       C  
ATOM    264  CG  PRO A  31      24.336   7.952  39.224  1.00 12.58           C  
ANISOU  264  CG  PRO A  31     1530   1855   1396    147   -101    169       C  
ATOM    265  CD  PRO A  31      23.317   7.419  40.218  1.00 12.86           C  
ANISOU  265  CD  PRO A  31     1765   1691   1429    121    -32    147       C  
ATOM    266  N   LYS A  32      24.891   3.908  37.546  1.00 12.63           N  
ANISOU  266  N   LYS A  32     1664   1646   1490    296    -41    106       N  
ATOM    267  CA  LYS A  32      26.049   3.030  37.303  1.00 14.12           C  
ANISOU  267  CA  LYS A  32     1812   1747   1807    370    -40    144       C  
ATOM    268  C   LYS A  32      27.046   3.752  36.427  1.00 13.96           C  
ANISOU  268  C   LYS A  32     1787   1913   1604    461    -30    165       C  
ATOM    269  O   LYS A  32      26.902   4.962  36.103  1.00 14.28           O  
ANISOU  269  O   LYS A  32     1845   1977   1602    385   -147    365       O  
ATOM    270  CB ALYS A  32      25.654   1.714  36.605  0.67 14.84           C  
ANISOU  270  CB ALYS A  32     1999   1885   1754    213      0    126       C  
ATOM    271  CG ALYS A  32      24.604   0.869  37.309  0.67 15.98           C  
ANISOU  271  CG ALYS A  32     1939   2006   2125    118    -74    188       C  
ATOM    272  CD ALYS A  32      24.314  -0.429  36.574  0.67 17.13           C  
ANISOU  272  CD ALYS A  32     2283   1994   2231    308   -152    125       C  
ATOM    273  CE ALYS A  32      23.147  -1.230  37.101  0.67 19.54           C  
ANISOU  273  CE ALYS A  32     2564   2412   2449    114   -101    311       C  
ATOM    274  NZ ALYS A  32      22.895  -2.466  36.274  0.67 20.63           N  
ANISOU  274  NZ ALYS A  32     2949   2633   2254    189   -337    337       N  
ATOM    275  CB BLYS A  32      25.564   1.653  36.852  0.33 14.71           C  
ANISOU  275  CB BLYS A  32     1934   1862   1792    170    -92    149       C  
ATOM    276  CG BLYS A  32      24.700   0.995  37.945  0.33 15.50           C  
ANISOU  276  CG BLYS A  32     2079   1954   1854     61    -31    130       C  
ATOM    277  CD BLYS A  32      24.476  -0.473  37.638  0.33 16.19           C  
ANISOU  277  CD BLYS A  32     2265   1981   1905      6    -77    119       C  
ATOM    278  CE BLYS A  32      23.390  -1.136  38.467  0.33 17.30           C  
ANISOU  278  CE BLYS A  32     2340   2071   2164    -53     42     49       C  
ATOM    279  NZ BLYS A  32      23.530  -2.625  38.434  0.33 18.00           N  
ANISOU  279  NZ BLYS A  32     2677   2062   2101    -12      6     49       N  
ATOM    280  N   ALA A  33      28.107   3.073  36.002  1.00 15.07           N  
ANISOU  280  N   ALA A  33     1869   1973   1885    587     80    400       N  
ATOM    281  CA  ALA A  33      29.136   3.687  35.168  1.00 15.54           C  
ANISOU  281  CA  ALA A  33     1536   2209   2160    546    -39    498       C  
ATOM    282  C   ALA A  33      28.496   4.331  33.922  1.00 14.30           C  
ANISOU  282  C   ALA A  33     1567   1938   1927    459     -8    294       C  
ATOM    283  O   ALA A  33      27.614   3.757  33.291  1.00 15.68           O  
ANISOU  283  O   ALA A  33     1874   2057   2027    382     42    204       O  
ATOM    284  CB  ALA A  33      30.194   2.677  34.733  1.00 18.51           C  
ANISOU  284  CB  ALA A  33     2110   2490   2434    782     37    366       C  
ATOM    285  N   HIS A  34      28.945   5.513  33.567  1.00 14.83           N  
ANISOU  285  N   HIS A  34     1693   2152   1788    315     31    343       N  
ATOM    286  CA  HIS A  34      28.468   6.194  32.350  1.00 13.74           C  
ANISOU  286  CA  HIS A  34     1633   1933   1655    295     57    308       C  
ATOM    287  C   HIS A  34      26.970   6.474  32.388  1.00 12.39           C  
ANISOU  287  C   HIS A  34     1504   1772   1430    174    -29    206       C  
ATOM    288  O   HIS A  34      26.367   6.618  31.319  1.00 13.30           O  
ANISOU  288  O   HIS A  34     1805   1840   1407    396      5    211       O  
ATOM    289  CB  HIS A  34      28.911   5.484  31.062  1.00 15.29           C  
ANISOU  289  CB  HIS A  34     1878   2230   1703    519     -4    203       C  
ATOM    290  CG  HIS A  34      30.424   5.406  30.986  1.00 19.59           C  
ANISOU  290  CG  HIS A  34     2133   3037   2273    297    100     23       C  
ATOM    291  ND1 HIS A  34      31.077   4.217  31.238  1.00 23.27           N  
ANISOU  291  ND1 HIS A  34     2619   3477   2745    655    140     15       N  
ATOM    292  CD2 HIS A  34      31.348   6.358  30.757  1.00 22.70           C  
ANISOU  292  CD2 HIS A  34     2417   3484   2726     40    234   -138       C  
ATOM    293  CE1 HIS A  34      32.372   4.441  31.120  1.00 24.34           C  
ANISOU  293  CE1 HIS A  34     2642   3517   3091    408     64   -149       C  
ATOM    294  NE2 HIS A  34      32.590   5.705  30.822  1.00 24.15           N  
ANISOU  294  NE2 HIS A  34     2499   3618   3057    117    144   -113       N  
ATOM    295  N   GLU A  35      26.394   6.669  33.567  1.00 11.65           N  
ANISOU  295  N   GLU A  35     1381   1732   1313    246    -83    237       N  
ATOM    296  CA  GLU A  35      24.981   7.064  33.744  1.00 11.02           C  
ANISOU  296  CA  GLU A  35     1344   1584   1259    176    -92    164       C  
ATOM    297  C   GLU A  35      24.919   8.351  34.554  1.00 10.65           C  
ANISOU  297  C   GLU A  35     1259   1477   1311     99   -168    186       C  
ATOM    298  O   GLU A  35      25.858   8.705  35.283  1.00 11.60           O  
ANISOU  298  O   GLU A  35     1458   1562   1386     65   -242    172       O  
ATOM    299  CB  GLU A  35      24.146   5.952  34.392  1.00 11.65           C  
ANISOU  299  CB  GLU A  35     1563   1437   1427    131    -47     87       C  
ATOM    300  CG  GLU A  35      24.158   4.644  33.616  1.00 12.35           C  
ANISOU  300  CG  GLU A  35     1831   1546   1314    163     -3     95       C  
ATOM    301  CD  GLU A  35      23.451   3.493  34.302  1.00 11.74           C  
ANISOU  301  CD  GLU A  35     1631   1584   1248    130   -127     31       C  
ATOM    302  OE1 GLU A  35      22.917   3.653  35.414  1.00 11.97           O  
ANISOU  302  OE1 GLU A  35     1744   1500   1303     87      1    207       O  
ATOM    303  OE2 GLU A  35      23.457   2.375  33.713  1.00 14.44           O  
ANISOU  303  OE2 GLU A  35     2246   1673   1568    147     66     80       O  
ATOM    304  N   VAL A  36      23.765   9.036  34.449  1.00 10.55           N  
ANISOU  304  N   VAL A  36     1321   1406   1282     63   -108     92       N  
ATOM    305  CA  VAL A  36      23.537  10.361  35.039  1.00 10.61           C  
ANISOU  305  CA  VAL A  36     1416   1349   1264     29    -54    136       C  
ATOM    306  C   VAL A  36      22.151  10.390  35.676  1.00 10.20           C  
ANISOU  306  C   VAL A  36     1289   1386   1201    -78   -129    227       C  
ATOM    307  O   VAL A  36      21.155  10.055  35.001  1.00 11.03           O  
ANISOU  307  O   VAL A  36     1346   1537   1307    -62   -103     36       O  
ATOM    308  CB  VAL A  36      23.616  11.428  33.915  1.00 11.30           C  
ANISOU  308  CB  VAL A  36     1475   1545   1273     26    -55    171       C  
ATOM    309  CG1 VAL A  36      23.339  12.820  34.476  1.00 12.44           C  
ANISOU  309  CG1 VAL A  36     1442   1496   1790    100   -109    209       C  
ATOM    310  CG2 VAL A  36      24.951  11.429  33.184  1.00 12.18           C  
ANISOU  310  CG2 VAL A  36     1519   1568   1541    -24    -12    166       C  
ATOM    311  N   ARG A  37      22.060  10.777  36.965  1.00 10.39           N  
ANISOU  311  N   ARG A  37     1333   1411   1205     51   -188    141       N  
ATOM    312  CA  ARG A  37      20.765  10.920  37.636  1.00 10.01           C  
ANISOU  312  CA  ARG A  37     1230   1323   1250    -54   -250    207       C  
ATOM    313  C   ARG A  37      20.392  12.399  37.693  1.00 10.29           C  
ANISOU  313  C   ARG A  37     1356   1380   1174    -56   -123    179       C  
ATOM    314  O   ARG A  37      21.222  13.223  38.091  1.00 11.26           O  
ANISOU  314  O   ARG A  37     1498   1416   1366     51   -303     62       O  
ATOM    315  CB  ARG A  37      20.745  10.242  39.011  1.00 10.92           C  
ANISOU  315  CB  ARG A  37     1622   1407   1120     31    -64    154       C  
ATOM    316  CG  ARG A  37      19.374  10.251  39.692  1.00 10.54           C  
ANISOU  316  CG  ARG A  37     1506   1348   1152      5   -108    165       C  
ATOM    317  CD  ARG A  37      19.263   9.178  40.769  1.00 11.78           C  
ANISOU  317  CD  ARG A  37     1800   1500   1175    -21   -187    146       C  
ATOM    318  NE  ARG A  37      20.174   9.453  41.893  1.00 11.44           N  
ANISOU  318  NE  ARG A  37     1612   1483   1253    -24   -162    198       N  
ATOM    319  CZ  ARG A  37      20.259   8.739  43.013  1.00 11.44           C  
ANISOU  319  CZ  ARG A  37     1627   1534   1187    -22    -60    164       C  
ATOM    320  NH1 ARG A  37      19.509   7.657  43.167  1.00 11.93           N  
ANISOU  320  NH1 ARG A  37     1714   1517   1304    -23   -302    169       N  
ATOM    321  NH2 ARG A  37      21.067   9.109  43.998  1.00 12.90           N  
ANISOU  321  NH2 ARG A  37     1873   1724   1303      3   -197    179       N  
ATOM    322  N   ILE A  38      19.155  12.717  37.261  1.00 10.06           N  
ANISOU  322  N   ILE A  38     1367   1159   1296    -74   -169    204       N  
ATOM    323  CA  ILE A  38      18.704  14.071  37.020  1.00 10.93           C  
ANISOU  323  CA  ILE A  38     1589   1265   1298    173   -123    120       C  
ATOM    324  C   ILE A  38      17.484  14.390  37.890  1.00  9.95           C  
ANISOU  324  C   ILE A  38     1336   1207   1239    -21   -164    132       C  
ATOM    325  O   ILE A  38      16.506  13.613  37.889  1.00 10.92           O  
ANISOU  325  O   ILE A  38     1466   1297   1386    -84    -84     34       O  
ATOM    326  CB  ILE A  38      18.309  14.266  35.520  1.00 10.05           C  
ANISOU  326  CB  ILE A  38     1321   1181   1317     35   -137    149       C  
ATOM    327  CG1 ILE A  38      19.439  13.832  34.562  1.00 11.71           C  
ANISOU  327  CG1 ILE A  38     1628   1360   1463    -62     33    119       C  
ATOM    328  CG2 ILE A  38      17.918  15.712  35.250  1.00 13.26           C  
ANISOU  328  CG2 ILE A  38     2190   1260   1588    158    114    203       C  
ATOM    329  CD1 ILE A  38      19.026  13.761  33.106  1.00 12.47           C  
ANISOU  329  CD1 ILE A  38     1857   1389   1490    -66    -47    249       C  
ATOM    330  N   LYS A  39      17.519  15.518  38.576  1.00 10.32           N  
ANISOU  330  N   LYS A  39     1365   1184   1372     89   -239     54       N  
ATOM    331  CA  LYS A  39      16.351  16.091  39.248  1.00 11.22           C  
ANISOU  331  CA  LYS A  39     1603   1370   1292    140   -169     83       C  
ATOM    332  C   LYS A  39      15.549  16.868  38.175  1.00 10.67           C  
ANISOU  332  C   LYS A  39     1455   1213   1384    -44    -70    230       C  
ATOM    333  O   LYS A  39      16.059  17.871  37.611  1.00 12.15           O  
ANISOU  333  O   LYS A  39     1598   1320   1699   -122    -76    337       O  
ATOM    334  CB  LYS A  39      16.740  17.049  40.391  1.00 13.25           C  
ANISOU  334  CB  LYS A  39     1890   1658   1486    117   -136   -172       C  
ATOM    335  CG ALYS A  39      15.499  17.459  41.191  0.61 15.39           C  
ANISOU  335  CG ALYS A  39     2057   2247   1543    145    -38   -136       C  
ATOM    336  CD ALYS A  39      15.766  18.221  42.489  0.61 19.00           C  
ANISOU  336  CD ALYS A  39     2523   2748   1950     98   -305   -363       C  
ATOM    337  CE ALYS A  39      14.508  18.856  43.034  0.61 22.59           C  
ANISOU  337  CE ALYS A  39     2756   3365   2462    207     19   -235       C  
ATOM    338  NZ ALYS A  39      14.513  19.380  44.418  0.61 24.61           N  
ANISOU  338  NZ ALYS A  39     3192   3546   2612    329    -41   -424       N  
ATOM    339  CG BLYS A  39      15.539  17.777  40.987  0.39 14.44           C  
ANISOU  339  CG BLYS A  39     2127   1880   1480    147     59   -206       C  
ATOM    340  CD BLYS A  39      15.972  18.815  42.014  0.39 15.98           C  
ANISOU  340  CD BLYS A  39     2404   1856   1810     87    -50   -238       C  
ATOM    341  CE BLYS A  39      14.794  19.655  42.494  0.39 19.31           C  
ANISOU  341  CE BLYS A  39     2527   2378   2434    187    217   -174       C  
ATOM    342  NZ BLYS A  39      13.552  18.899  42.767  0.39 21.01           N  
ANISOU  342  NZ BLYS A  39     2572   2703   2707    148    249    -99       N  
ATOM    343  N   MET A  40      14.336  16.403  37.838  1.00 10.48           N  
ANISOU  343  N   MET A  40     1350   1219   1414      5   -108    286       N  
ATOM    344  CA  MET A  40      13.576  17.051  36.770  1.00 10.62           C  
ANISOU  344  CA  MET A  40     1483   1157   1393      4   -197    133       C  
ATOM    345  C   MET A  40      12.985  18.373  37.243  1.00  9.39           C  
ANISOU  345  C   MET A  40     1341   1196   1029    -13   -103    159       C  
ATOM    346  O   MET A  40      12.560  18.512  38.391  1.00 10.87           O  
ANISOU  346  O   MET A  40     1713   1310   1108     95    -40    228       O  
ATOM    347  CB AMET A  40      12.470  16.166  36.190  0.55 11.55           C  
ANISOU  347  CB AMET A  40     1616   1254   1517    -48   -157     79       C  
ATOM    348  CG AMET A  40      12.243  16.346  34.693  0.55 13.02           C  
ANISOU  348  CG AMET A  40     1915   1435   1599    -50   -229    188       C  
ATOM    349  SD AMET A  40      13.696  16.095  33.582  0.55 13.24           S  
ANISOU  349  SD AMET A  40     1865   1594   1572    181   -306    352       S  
ATOM    350  CE AMET A  40      14.531  14.967  34.649  0.55  1.16           C  
ANISOU  350  CE AMET A  40      143    141    158      1     12      2       C  
ATOM    351  CB BMET A  40      12.460  16.103  36.316  0.45 10.72           C  
ANISOU  351  CB BMET A  40     1577   1166   1331    -92   -139    238       C  
ATOM    352  CG BMET A  40      12.843  14.872  35.534  0.45 12.43           C  
ANISOU  352  CG BMET A  40     1644   1263   1814   -273    156     71       C  
ATOM    353  SD BMET A  40      13.274  15.172  33.760  0.45 17.44           S  
ANISOU  353  SD BMET A  40     2429   2187   2010   -583    258    260       S  
ATOM    354  CE BMET A  40      15.020  15.275  34.098  0.45 17.82           C  
ANISOU  354  CE BMET A  40     2430   2352   1990   -164    -14    245       C  
ATOM    355  N   VAL A  41      12.956  19.357  36.330  1.00  9.55           N  
ANISOU  355  N   VAL A  41     1419   1066   1143     47    -34    152       N  
ATOM    356  CA  VAL A  41      12.398  20.690  36.603  1.00  9.29           C  
ANISOU  356  CA  VAL A  41     1291   1140   1097     23    -86     89       C  
ATOM    357  C   VAL A  41      11.114  20.962  35.850  1.00  9.18           C  
ANISOU  357  C   VAL A  41     1285   1057   1146     47    -38    146       C  
ATOM    358  O   VAL A  41      10.115  21.455  36.421  1.00  9.97           O  
ANISOU  358  O   VAL A  41     1443   1165   1180     46    -22     54       O  
ATOM    359  CB  VAL A  41      13.471  21.783  36.418  1.00  9.94           C  
ANISOU  359  CB  VAL A  41     1398   1151   1227   -131    -93     89       C  
ATOM    360  CG1 VAL A  41      12.864  23.179  36.562  1.00 11.85           C  
ANISOU  360  CG1 VAL A  41     1802   1268   1434   -100     20   -105       C  
ATOM    361  CG2 VAL A  41      14.596  21.585  37.442  1.00 11.88           C  
ANISOU  361  CG2 VAL A  41     1605   1483   1427    -35   -269    -87       C  
ATOM    362  N   ALA A  42      11.097  20.642  34.538  1.00  8.67           N  
ANISOU  362  N   ALA A  42     1302    956   1036    -77    -88    135       N  
ATOM    363  CA  ALA A  42       9.911  20.860  33.711  1.00  8.73           C  
ANISOU  363  CA  ALA A  42     1209    959   1151    106    -54     51       C  
ATOM    364  C   ALA A  42       9.817  19.776  32.618  1.00  8.63           C  
ANISOU  364  C   ALA A  42     1198   1053   1028     13     44     41       C  
ATOM    365  O   ALA A  42      10.885  19.374  32.100  1.00  9.95           O  
ANISOU  365  O   ALA A  42     1238   1325   1218    -94      0    -88       O  
ATOM    366  CB  ALA A  42       9.910  22.253  33.070  1.00 11.02           C  
ANISOU  366  CB  ALA A  42     1819   1124   1245    -11   -117    185       C  
ATOM    367  N   THR A  43       8.609  19.388  32.248  1.00  8.73           N  
ANISOU  367  N   THR A  43     1251   1036   1030    -65     48    -16       N  
ATOM    368  CA  THR A  43       8.413  18.443  31.131  1.00  8.14           C  
ANISOU  368  CA  THR A  43     1212    816   1063    -20     36     26       C  
ATOM    369  C   THR A  43       7.152  18.839  30.382  1.00  7.88           C  
ANISOU  369  C   THR A  43     1041    914   1039    -38    132     13       C  
ATOM    370  O   THR A  43       6.149  19.216  30.983  1.00  9.36           O  
ANISOU  370  O   THR A  43     1274   1203   1080     80    105     52       O  
ATOM    371  CB  THR A  43       8.411  16.989  31.681  1.00  9.21           C  
ANISOU  371  CB  THR A  43     1363    990   1146    -62    109     95       C  
ATOM    372  OG1 THR A  43       8.411  16.055  30.596  1.00  9.12           O  
ANISOU  372  OG1 THR A  43     1385    910   1169   -102     47    102       O  
ATOM    373  CG2 THR A  43       7.220  16.682  32.596  1.00 10.22           C  
ANISOU  373  CG2 THR A  43     1450   1209   1225    -59     97    169       C  
ATOM    374  N   GLY A  44       7.217  18.741  29.046  1.00  8.36           N  
ANISOU  374  N   GLY A  44     1060   1067   1051    -44     -9    163       N  
ATOM    375  CA  GLY A  44       6.062  18.986  28.198  1.00  9.14           C  
ANISOU  375  CA  GLY A  44     1272   1122   1078    -97    -32    120       C  
ATOM    376  C   GLY A  44       5.224  17.724  27.973  1.00  8.57           C  
ANISOU  376  C   GLY A  44     1203    989   1063    -30   -104    127       C  
ATOM    377  O   GLY A  44       5.711  16.601  28.026  1.00 10.97           O  
ANISOU  377  O   GLY A  44     1349   1140   1682    120   -119     45       O  
ATOM    378  N   ILE A  45       3.953  17.945  27.656  1.00  8.19           N  
ANISOU  378  N   ILE A  45     1165    981    966    -39     74     53       N  
ATOM    379  CA  ILE A  45       3.024  16.874  27.259  1.00  9.00           C  
ANISOU  379  CA  ILE A  45     1206   1203   1012    -65     35     50       C  
ATOM    380  C   ILE A  45       3.002  16.838  25.712  1.00  8.26           C  
ANISOU  380  C   ILE A  45     1179   1003    956      3     67    166       C  
ATOM    381  O   ILE A  45       2.415  17.722  25.070  1.00  9.77           O  
ANISOU  381  O   ILE A  45     1378   1254   1081     65    137    219       O  
ATOM    382  CB  ILE A  45       1.635  17.047  27.866  1.00  9.34           C  
ANISOU  382  CB  ILE A  45     1130   1373   1044   -108     75    164       C  
ATOM    383  CG1 ILE A  45       1.709  16.897  29.387  1.00 10.16           C  
ANISOU  383  CG1 ILE A  45     1400   1405   1056     24    205    220       C  
ATOM    384  CG2 ILE A  45       0.638  16.059  27.280  1.00 10.29           C  
ANISOU  384  CG2 ILE A  45     1130   1662   1116   -174     28    183       C  
ATOM    385  CD1 ILE A  45       0.430  17.199  30.157  1.00 10.90           C  
ANISOU  385  CD1 ILE A  45     1405   1565   1170    -22     88    269       C  
ATOM    386  N   CYS A  46       3.634  15.830  25.126  1.00  8.34           N  
ANISOU  386  N   CYS A  46     1197   1004    969     -5     70    225       N  
ATOM    387  CA  CYS A  46       3.713  15.675  23.670  1.00  8.62           C  
ANISOU  387  CA  CYS A  46     1282   1013    979    -98    -19    177       C  
ATOM    388  C   CYS A  46       2.717  14.596  23.242  1.00  8.08           C  
ANISOU  388  C   CYS A  46     1135    954    982    -53     66    254       C  
ATOM    389  O   CYS A  46       2.464  13.615  23.994  1.00  8.77           O  
ANISOU  389  O   CYS A  46     1297   1005   1029   -117     50    239       O  
ATOM    390  CB  CYS A  46       5.169  15.275  23.294  1.00  8.91           C  
ANISOU  390  CB  CYS A  46     1170   1178   1038    -42    101    179       C  
ATOM    391  SG  CYS A  46       5.400  14.769  21.540  1.00  7.67           S  
ANISOU  391  SG  CYS A  46     1026    896    993   -128    120    208       S  
ATOM    392  N   ARG A  47       2.163  14.672  22.015  1.00  8.13           N  
ANISOU  392  N   ARG A  47     1124    959   1006    -65     11    241       N  
ATOM    393  CA  ARG A  47       1.254  13.616  21.534  1.00  8.68           C  
ANISOU  393  CA  ARG A  47     1135   1049   1113   -151     83    350       C  
ATOM    394  C   ARG A  47       1.925  12.241  21.556  1.00  8.16           C  
ANISOU  394  C   ARG A  47     1168   1016    916   -199     98    288       C  
ATOM    395  O   ARG A  47       1.189  11.254  21.766  1.00  8.66           O  
ANISOU  395  O   ARG A  47     1182   1020   1089   -182     88    291       O  
ATOM    396  CB  ARG A  47       0.736  13.997  20.130  1.00  8.43           C  
ANISOU  396  CB  ARG A  47     1174   1037    992    -98    138    265       C  
ATOM    397  CG  ARG A  47      -0.220  12.985  19.544  1.00  9.39           C  
ANISOU  397  CG  ARG A  47     1151   1266   1151   -222     15    341       C  
ATOM    398  CD  ARG A  47      -1.539  12.753  20.302  1.00  9.80           C  
ANISOU  398  CD  ARG A  47     1083   1310   1331   -184      5    323       C  
ATOM    399  NE  ARG A  47      -2.367  13.935  20.256  1.00 10.75           N  
ANISOU  399  NE  ARG A  47     1181   1460   1444   -122     -1    261       N  
ATOM    400  CZ  ARG A  47      -3.640  13.944  20.664  1.00 11.85           C  
ANISOU  400  CZ  ARG A  47     1301   1746   1455    -62     95    258       C  
ATOM    401  NH1 ARG A  47      -4.193  12.877  21.290  1.00 13.42           N  
ANISOU  401  NH1 ARG A  47     1364   2061   1674   -175    133    431       N  
ATOM    402  NH2 ARG A  47      -4.376  15.017  20.471  1.00 14.06           N  
ANISOU  402  NH2 ARG A  47     1500   2109   1732    225     85    206       N  
ATOM    403  N   SER A  48       3.233  12.093  21.388  1.00  7.83           N  
ANISOU  403  N   SER A  48     1073    876   1026   -106    124    241       N  
ATOM    404  CA  SER A  48       3.810  10.746  21.479  1.00  8.21           C  
ANISOU  404  CA  SER A  48     1143    908   1067   -139    147    256       C  
ATOM    405  C   SER A  48       3.628  10.119  22.878  1.00  8.06           C  
ANISOU  405  C   SER A  48     1127    850   1086     14    115    208       C  
ATOM    406  O   SER A  48       3.584   8.883  22.974  1.00  9.08           O  
ANISOU  406  O   SER A  48     1450    968   1031    -72    128    223       O  
ATOM    407  CB  SER A  48       5.305  10.719  21.123  1.00  8.20           C  
ANISOU  407  CB  SER A  48     1120   1069    928    -87    120    248       C  
ATOM    408  OG  SER A  48       5.481  11.021  19.735  1.00  8.97           O  
ANISOU  408  OG  SER A  48     1169   1235   1004   -171     -7    359       O  
ATOM    409  N   ASP A  49       3.632  10.925  23.973  1.00  7.88           N  
ANISOU  409  N   ASP A  49     1135    923    935   -154    118    236       N  
ATOM    410  CA  ASP A  49       3.372  10.351  25.294  1.00  7.88           C  
ANISOU  410  CA  ASP A  49     1059    964    972    -39    129    282       C  
ATOM    411  C   ASP A  49       1.943   9.808  25.331  1.00  8.18           C  
ANISOU  411  C   ASP A  49     1187    990    931   -190      3    195       C  
ATOM    412  O   ASP A  49       1.674   8.730  25.912  1.00 10.06           O  
ANISOU  412  O   ASP A  49     1451   1180   1191   -278    161    231       O  
ATOM    413  CB  ASP A  49       3.614  11.384  26.406  1.00  8.70           C  
ANISOU  413  CB  ASP A  49     1154   1128   1024   -123     78    217       C  
ATOM    414  CG  ASP A  49       5.019  11.935  26.378  1.00  8.19           C  
ANISOU  414  CG  ASP A  49     1144   1098    871    -95     72    240       C  
ATOM    415  OD1 ASP A  49       5.981  11.123  26.563  1.00  9.13           O  
ANISOU  415  OD1 ASP A  49     1259   1126   1084   -102     25    222       O  
ATOM    416  OD2 ASP A  49       5.159  13.165  26.166  1.00  9.09           O  
ANISOU  416  OD2 ASP A  49     1240   1102   1113   -100     83    175       O  
ATOM    417  N   ASP A  50       0.961  10.518  24.751  1.00  8.80           N  
ANISOU  417  N   ASP A  50     1026   1164   1154   -171     88    257       N  
ATOM    418  CA  ASP A  50      -0.405  10.040  24.634  1.00  8.93           C  
ANISOU  418  CA  ASP A  50     1057   1188   1147   -149    121    179       C  
ATOM    419  C   ASP A  50      -0.489   8.793  23.797  1.00  8.84           C  
ANISOU  419  C   ASP A  50     1185   1134   1041   -286     15    211       C  
ATOM    420  O   ASP A  50      -1.325   7.894  24.102  1.00 10.72           O  
ANISOU  420  O   ASP A  50     1462   1328   1283   -407     50    249       O  
ATOM    421  CB  ASP A  50      -1.337  11.131  24.086  1.00  9.74           C  
ANISOU  421  CB  ASP A  50     1257   1339   1103    -85     70    274       C  
ATOM    422  CG  ASP A  50      -2.778  10.701  24.053  1.00 11.24           C  
ANISOU  422  CG  ASP A  50     1354   1627   1291    -95    170    282       C  
ATOM    423  OD1 ASP A  50      -3.357  10.465  25.151  1.00 13.01           O  
ANISOU  423  OD1 ASP A  50     1414   2090   1439    -52    265    333       O  
ATOM    424  OD2 ASP A  50      -3.305  10.567  22.916  1.00 12.80           O  
ANISOU  424  OD2 ASP A  50     1396   1979   1490   -256     46    151       O  
ATOM    425  N   HIS A  51       0.338   8.648  22.741  1.00  8.79           N  
ANISOU  425  N   HIS A  51     1257   1093    990   -262     70    194       N  
ATOM    426  CA  HIS A  51       0.350   7.447  21.920  1.00  9.64           C  
ANISOU  426  CA  HIS A  51     1510   1108   1044   -291    115    168       C  
ATOM    427  C   HIS A  51       0.697   6.206  22.753  1.00 10.05           C  
ANISOU  427  C   HIS A  51     1628   1141   1050   -375    110    194       C  
ATOM    428  O   HIS A  51       0.253   5.093  22.387  1.00 10.72           O  
ANISOU  428  O   HIS A  51     1775   1110   1188   -448    168    110       O  
ATOM    429  CB  HIS A  51       1.316   7.565  20.732  1.00 10.00           C  
ANISOU  429  CB  HIS A  51     1629   1058   1113   -179    172    239       C  
ATOM    430  CG  HIS A  51       0.934   8.518  19.630  1.00  9.26           C  
ANISOU  430  CG  HIS A  51     1450   1045   1023   -308     99    173       C  
ATOM    431  ND1 HIS A  51      -0.368   8.911  19.378  1.00 10.11           N  
ANISOU  431  ND1 HIS A  51     1494   1169   1177   -180     77    245       N  
ATOM    432  CD2 HIS A  51       1.766   9.090  18.696  1.00  9.36           C  
ANISOU  432  CD2 HIS A  51     1304   1147   1104   -223    135    208       C  
ATOM    433  CE1 HIS A  51      -0.331   9.700  18.299  1.00 10.07           C  
ANISOU  433  CE1 HIS A  51     1440   1273   1113   -168    102    246       C  
ATOM    434  NE2 HIS A  51       0.940   9.802  17.873  1.00  9.93           N  
ANISOU  434  NE2 HIS A  51     1417   1119   1239   -279      6    220       N  
ATOM    435  N   VAL A  52       1.518   6.346  23.795  1.00  8.98           N  
ANISOU  435  N   VAL A  52     1431    862   1120   -343     74    305       N  
ATOM    436  CA  VAL A  52       1.786   5.209  24.686  1.00  9.88           C  
ANISOU  436  CA  VAL A  52     1569   1035   1151   -165    114    364       C  
ATOM    437  C   VAL A  52       0.477   4.788  25.370  1.00 10.77           C  
ANISOU  437  C   VAL A  52     1701   1117   1274   -250    207    346       C  
ATOM    438  O   VAL A  52       0.166   3.568  25.465  1.00 12.02           O  
ANISOU  438  O   VAL A  52     1885   1198   1483   -374    255    333       O  
ATOM    439  CB  VAL A  52       2.875   5.555  25.721  1.00 10.55           C  
ANISOU  439  CB  VAL A  52     1421   1428   1162   -139    105    363       C  
ATOM    440  CG1 VAL A  52       3.094   4.394  26.698  1.00 11.92           C  
ANISOU  440  CG1 VAL A  52     1745   1455   1328   -146     94    425       C  
ATOM    441  CG2 VAL A  52       4.205   5.924  25.050  1.00 11.98           C  
ANISOU  441  CG2 VAL A  52     1572   1593   1386   -167    106    458       C  
ATOM    442  N   VAL A  53      -0.289   5.740  25.883  1.00 10.91           N  
ANISOU  442  N   VAL A  53     1683   1246   1217   -275    323    255       N  
ATOM    443  CA  VAL A  53      -1.559   5.436  26.544  1.00 11.95           C  
ANISOU  443  CA  VAL A  53     1724   1597   1219   -406    255    383       C  
ATOM    444  C   VAL A  53      -2.559   4.789  25.599  1.00 12.70           C  
ANISOU  444  C   VAL A  53     1941   1546   1337   -610    247    297       C  
ATOM    445  O   VAL A  53      -3.270   3.827  25.980  1.00 13.73           O  
ANISOU  445  O   VAL A  53     1933   1708   1576   -693    248    323       O  
ATOM    446  CB  VAL A  53      -2.170   6.713  27.152  1.00 11.94           C  
ANISOU  446  CB  VAL A  53     1561   1717   1258   -331    263    250       C  
ATOM    447  CG1 VAL A  53      -3.468   6.351  27.896  1.00 12.90           C  
ANISOU  447  CG1 VAL A  53     1645   1775   1482   -391    249    173       C  
ATOM    448  CG2 VAL A  53      -1.218   7.433  28.106  1.00 12.50           C  
ANISOU  448  CG2 VAL A  53     1669   1805   1277   -249    149    350       C  
ATOM    449  N   SER A  54      -2.662   5.280  24.357  1.00 11.88           N  
ANISOU  449  N   SER A  54     1614   1632   1269   -542    105    242       N  
ATOM    450  CA  SER A  54      -3.676   4.772  23.438  1.00 12.37           C  
ANISOU  450  CA  SER A  54     1587   1733   1379   -559     96    245       C  
ATOM    451  C   SER A  54      -3.266   3.474  22.778  1.00 13.38           C  
ANISOU  451  C   SER A  54     1831   1580   1671   -635     83    260       C  
ATOM    452  O   SER A  54      -4.131   2.854  22.100  1.00 16.89           O  
ANISOU  452  O   SER A  54     2091   2250   2078   -666   -142     -4       O  
ATOM    453  CB  SER A  54      -3.984   5.831  22.374  1.00 13.83           C  
ANISOU  453  CB  SER A  54     1576   2239   1440   -518     10    439       C  
ATOM    454  OG  SER A  54      -2.900   6.024  21.504  1.00 13.64           O  
ANISOU  454  OG  SER A  54     1772   1941   1470   -360    114    359       O  
ATOM    455  N   GLY A  55      -2.032   3.048  22.895  1.00 13.33           N  
ANISOU  455  N   GLY A  55     1942   1620   1505   -539    199    263       N  
ATOM    456  CA  GLY A  55      -1.538   1.878  22.174  1.00 13.92           C  
ANISOU  456  CA  GLY A  55     2070   1563   1656   -588    136    187       C  
ATOM    457  C   GLY A  55      -1.134   2.187  20.729  1.00 13.42           C  
ANISOU  457  C   GLY A  55     2063   1608   1429   -524     12     62       C  
ATOM    458  O   GLY A  55      -0.762   1.255  19.976  1.00 16.77           O  
ANISOU  458  O   GLY A  55     3013   1645   1712   -374     24     42       O  
ATOM    459  N   THR A  56      -1.107   3.426  20.291  1.00 13.09           N  
ANISOU  459  N   THR A  56     1943   1658   1370   -513     99    158       N  
ATOM    460  CA  THR A  56      -0.590   3.822  18.964  1.00 12.61           C  
ANISOU  460  CA  THR A  56     1877   1556   1357   -458    100    139       C  
ATOM    461  C   THR A  56       0.907   3.537  18.858  1.00 11.49           C  
ANISOU  461  C   THR A  56     1925   1180   1262   -251     61    179       C  
ATOM    462  O   THR A  56       1.424   3.062  17.820  1.00 13.21           O  
ANISOU  462  O   THR A  56     2147   1467   1406   -287    117     43       O  
ATOM    463  CB  THR A  56      -0.918   5.299  18.728  1.00 13.57           C  
ANISOU  463  CB  THR A  56     2064   1615   1475   -263    -51    221       C  
ATOM    464  OG1 THR A  56      -2.324   5.429  18.520  1.00 18.54           O  
ANISOU  464  OG1 THR A  56     2247   2020   2776   -412   -137    402       O  
ATOM    465  CG2 THR A  56      -0.170   5.899  17.524  1.00 14.39           C  
ANISOU  465  CG2 THR A  56     2551   1504   1412   -366    121      5       C  
ATOM    466  N   LEU A  57       1.651   3.888  19.922  1.00 11.70           N  
ANISOU  466  N   LEU A  57     1897   1326   1222   -297    -23    218       N  
ATOM    467  CA  LEU A  57       3.093   3.707  20.017  1.00 11.45           C  
ANISOU  467  CA  LEU A  57     1840   1178   1332   -289     33    168       C  
ATOM    468  C   LEU A  57       3.320   2.579  21.029  1.00 11.27           C  
ANISOU  468  C   LEU A  57     1834   1258   1189   -268    204     59       C  
ATOM    469  O   LEU A  57       3.003   2.758  22.233  1.00 13.30           O  
ANISOU  469  O   LEU A  57     2263   1472   1319   -259    214     82       O  
ATOM    470  CB ALEU A  57       3.737   5.036  20.472  0.66 12.48           C  
ANISOU  470  CB ALEU A  57     1799   1128   1816   -219    104    -26       C  
ATOM    471  CG ALEU A  57       5.273   5.124  20.438  0.66 12.76           C  
ANISOU  471  CG ALEU A  57     1795   1318   1736   -198    152    -56       C  
ATOM    472  CD1ALEU A  57       5.613   6.596  20.729  0.66 14.39           C  
ANISOU  472  CD1ALEU A  57     1976   1402   2089   -268    170   -168       C  
ATOM    473  CD2ALEU A  57       5.960   4.167  21.405  0.66 13.03           C  
ANISOU  473  CD2ALEU A  57     1739   1398   1815   -274   -116   -161       C  
ATOM    474  CB BLEU A  57       3.832   4.986  20.451  0.34 12.01           C  
ANISOU  474  CB BLEU A  57     1727   1224   1613   -249      0     56       C  
ATOM    475  CG BLEU A  57       5.331   4.906  20.777  0.34 11.77           C  
ANISOU  475  CG BLEU A  57     1741   1177   1556   -167    -23    -36       C  
ATOM    476  CD1BLEU A  57       6.117   4.385  19.587  0.34 13.83           C  
ANISOU  476  CD1BLEU A  57     1890   1573   1792   -128    174   -112       C  
ATOM    477  CD2BLEU A  57       5.881   6.251  21.251  0.34 12.32           C  
ANISOU  477  CD2BLEU A  57     1915   1251   1513   -277    -81     -1       C  
ATOM    478  N   VAL A  58       3.806   1.431  20.571  1.00 11.48           N  
ANISOU  478  N   VAL A  58     2073   1094   1195   -281     67    240       N  
ATOM    479  CA  VAL A  58       3.999   0.264  21.425  1.00 12.47           C  
ANISOU  479  CA  VAL A  58     2286   1166   1288   -292     72    243       C  
ATOM    480  C   VAL A  58       5.359   0.293  22.112  1.00 12.69           C  
ANISOU  480  C   VAL A  58     2154   1309   1359   -149    153    158       C  
ATOM    481  O   VAL A  58       6.411   0.387  21.452  1.00 15.19           O  
ANISOU  481  O   VAL A  58     2225   2104   1441   -119    183    397       O  
ATOM    482  CB  VAL A  58       3.818  -1.054  20.611  1.00 14.17           C  
ANISOU  482  CB  VAL A  58     2565   1290   1528   -356   -102    157       C  
ATOM    483  CG1 VAL A  58       4.213  -2.272  21.436  1.00 16.57           C  
ANISOU  483  CG1 VAL A  58     3216   1307   1772   -237   -169    262       C  
ATOM    484  CG2 VAL A  58       2.366  -1.145  20.172  1.00 14.49           C  
ANISOU  484  CG2 VAL A  58     2589   1397   1521   -422    -68    211       C  
ATOM    485  N   THR A  59       5.352   0.207  23.436  1.00 11.46           N  
ANISOU  485  N   THR A  59     2010   1072   1271   -192     27    230       N  
ATOM    486  CA  THR A  59       6.580   0.078  24.245  1.00 11.68           C  
ANISOU  486  CA  THR A  59     1934   1032   1474   -251     42    392       C  
ATOM    487  C   THR A  59       6.191  -0.750  25.474  1.00 10.21           C  
ANISOU  487  C   THR A  59     1679    880   1321   -131    123    184       C  
ATOM    488  O   THR A  59       5.021  -0.669  25.885  1.00 11.82           O  
ANISOU  488  O   THR A  59     1744   1282   1465   -139     50    184       O  
ATOM    489  CB  THR A  59       7.113   1.499  24.617  1.00 11.32           C  
ANISOU  489  CB  THR A  59     1965    932   1406   -356     53    329       C  
ATOM    490  OG1 THR A  59       8.441   1.417  25.106  1.00 12.18           O  
ANISOU  490  OG1 THR A  59     1898   1174   1556   -413    160    208       O  
ATOM    491  CG2 THR A  59       6.194   2.191  25.596  1.00 13.09           C  
ANISOU  491  CG2 THR A  59     1983   1176   1815   -106    -45     46       C  
ATOM    492  N   PRO A  60       7.089  -1.493  26.086  1.00  9.95           N  
ANISOU  492  N   PRO A  60     1515    936   1331   -227    202    222       N  
ATOM    493  CA  PRO A  60       6.672  -2.359  27.213  1.00 10.72           C  
ANISOU  493  CA  PRO A  60     1623   1021   1430   -362    123    304       C  
ATOM    494  C   PRO A  60       6.091  -1.587  28.389  1.00 10.94           C  
ANISOU  494  C   PRO A  60     1726    985   1447   -268     60    242       C  
ATOM    495  O   PRO A  60       6.595  -0.538  28.826  1.00 10.87           O  
ANISOU  495  O   PRO A  60     1748   1049   1331   -343    116    173       O  
ATOM    496  CB  PRO A  60       7.963  -3.089  27.612  1.00 12.24           C  
ANISOU  496  CB  PRO A  60     1926   1295   1431    -56     44    225       C  
ATOM    497  CG  PRO A  60       8.714  -3.197  26.289  1.00 12.05           C  
ANISOU  497  CG  PRO A  60     1928   1048   1601   -170    171    267       C  
ATOM    498  CD  PRO A  60       8.446  -1.838  25.638  1.00 10.94           C  
ANISOU  498  CD  PRO A  60     1567   1002   1587   -193     14    223       C  
ATOM    499  N   LEU A  61       5.005  -2.122  28.962  1.00 11.66           N  
ANISOU  499  N   LEU A  61     1750   1247   1433   -388    131     81       N  
ATOM    500  CA  LEU A  61       4.339  -1.637  30.168  1.00 11.11           C  
ANISOU  500  CA  LEU A  61     1830   1056   1335   -303    207    278       C  
ATOM    501  C   LEU A  61       4.602  -2.608  31.327  1.00 11.87           C  
ANISOU  501  C   LEU A  61     1973   1008   1530   -277    290    299       C  
ATOM    502  O   LEU A  61       4.887  -3.786  31.093  1.00 14.31           O  
ANISOU  502  O   LEU A  61     2571   1090   1777   -233    348    297       O  
ATOM    503  CB  LEU A  61       2.829  -1.497  29.999  1.00 14.44           C  
ANISOU  503  CB  LEU A  61     1847   1807   1833   -495    195    426       C  
ATOM    504  CG  LEU A  61       2.220  -0.567  28.995  1.00 23.19           C  
ANISOU  504  CG  LEU A  61     2724   2947   3142     13     -1   1081       C  
ATOM    505  CD1 LEU A  61       0.831  -0.066  29.490  1.00 24.13           C  
ANISOU  505  CD1 LEU A  61     2873   2907   3389     -7    158    756       C  
ATOM    506  CD2 LEU A  61       2.982   0.585  28.460  1.00 20.90           C  
ANISOU  506  CD2 LEU A  61     2697   2498   2747    162    167    739       C  
ATOM    507  N   PRO A  62       4.493  -2.172  32.590  1.00 11.60           N  
ANISOU  507  N   PRO A  62     2070    971   1368   -333    271    454       N  
ATOM    508  CA  PRO A  62       4.267  -0.802  33.033  1.00 10.89           C  
ANISOU  508  CA  PRO A  62     1707   1128   1302   -307    432    293       C  
ATOM    509  C   PRO A  62       5.463   0.092  32.741  1.00  9.78           C  
ANISOU  509  C   PRO A  62     1495   1041   1181   -167    259    311       C  
ATOM    510  O   PRO A  62       6.595  -0.375  32.618  1.00 10.60           O  
ANISOU  510  O   PRO A  62     1599   1125   1304   -201    193    404       O  
ATOM    511  CB  PRO A  62       4.026  -0.933  34.565  1.00 11.88           C  
ANISOU  511  CB  PRO A  62     1937   1265   1312   -347    238    434       C  
ATOM    512  CG  PRO A  62       4.907  -2.119  34.907  1.00 13.26           C  
ANISOU  512  CG  PRO A  62     2085   1449   1504   -211    229    482       C  
ATOM    513  CD  PRO A  62       4.761  -3.083  33.751  1.00 12.78           C  
ANISOU  513  CD  PRO A  62     2143   1179   1534   -352    194    572       C  
ATOM    514  N   VAL A  63       5.206   1.415  32.608  1.00  9.94           N  
ANISOU  514  N   VAL A  63     1560   1032   1186   -257    221    346       N  
ATOM    515  CA  VAL A  63       6.246   2.359  32.148  1.00  9.24           C  
ANISOU  515  CA  VAL A  63     1436    949   1127   -272    212    237       C  
ATOM    516  C   VAL A  63       6.133   3.719  32.821  1.00  8.74           C  
ANISOU  516  C   VAL A  63     1225    984   1113   -169    164    299       C  
ATOM    517  O   VAL A  63       5.032   4.164  33.156  1.00  9.77           O  
ANISOU  517  O   VAL A  63     1324   1063   1327   -144    186    305       O  
ATOM    518  CB  VAL A  63       6.151   2.495  30.582  1.00  9.15           C  
ANISOU  518  CB  VAL A  63     1368    995   1115   -282    164    221       C  
ATOM    519  CG1 VAL A  63       4.849   3.171  30.134  1.00 11.08           C  
ANISOU  519  CG1 VAL A  63     1580   1450   1177   -171     91    296       C  
ATOM    520  CG2 VAL A  63       7.374   3.193  29.976  1.00 10.01           C  
ANISOU  520  CG2 VAL A  63     1444   1286   1073   -329    274     95       C  
ATOM    521  N   ILE A  64       7.286   4.393  32.918  1.00  8.62           N  
ANISOU  521  N   ILE A  64     1230    946   1100   -182    159    230       N  
ATOM    522  CA  ILE A  64       7.343   5.844  33.190  1.00  9.39           C  
ANISOU  522  CA  ILE A  64     1490    932   1144   -123     78    305       C  
ATOM    523  C   ILE A  64       7.613   6.537  31.835  1.00  8.34           C  
ANISOU  523  C   ILE A  64     1113    896   1159   -242     76    224       C  
ATOM    524  O   ILE A  64       8.732   6.398  31.299  1.00  8.94           O  
ANISOU  524  O   ILE A  64     1315    987   1096   -168     77    239       O  
ATOM    525  CB  ILE A  64       8.402   6.198  34.253  1.00  9.60           C  
ANISOU  525  CB  ILE A  64     1625   1054    969   -127    119    220       C  
ATOM    526  CG1 ILE A  64       8.008   5.549  35.600  1.00 12.19           C  
ANISOU  526  CG1 ILE A  64     1966   1447   1219   -253     28    356       C  
ATOM    527  CG2 ILE A  64       8.512   7.712  34.398  1.00 10.14           C  
ANISOU  527  CG2 ILE A  64     1737   1079   1038   -103    183    214       C  
ATOM    528  CD1 ILE A  64       9.050   5.683  36.691  1.00 14.55           C  
ANISOU  528  CD1 ILE A  64     2095   1973   1462    -83    -22    242       C  
ATOM    529  N   ALA A  65       6.608   7.192  31.278  1.00  8.52           N  
ANISOU  529  N   ALA A  65     1206    917   1115   -175    159    263       N  
ATOM    530  CA  ALA A  65       6.736   7.903  29.988  1.00  8.96           C  
ANISOU  530  CA  ALA A  65     1400    934   1071   -183     80    301       C  
ATOM    531  C   ALA A  65       7.383   9.275  30.227  1.00  8.71           C  
ANISOU  531  C   ALA A  65     1376    894   1037   -157     -8    196       C  
ATOM    532  O   ALA A  65       7.986   9.521  31.253  1.00  9.38           O  
ANISOU  532  O   ALA A  65     1502    920   1142   -139    -46    211       O  
ATOM    533  CB  ALA A  65       5.392   7.933  29.294  1.00 10.06           C  
ANISOU  533  CB  ALA A  65     1436   1115   1271   -226     68    162       C  
ATOM    534  N   GLY A  66       7.273  10.149  29.197  1.00  8.82           N  
ANISOU  534  N   GLY A  66     1397    891   1063   -158     17    261       N  
ATOM    535  CA  GLY A  66       7.905  11.457  29.204  1.00  9.09           C  
ANISOU  535  CA  GLY A  66     1411    879   1162   -170    -48    189       C  
ATOM    536  C   GLY A  66       9.222  11.450  28.461  1.00  8.59           C  
ANISOU  536  C   GLY A  66     1200    851   1213    -72   -144    212       C  
ATOM    537  O   GLY A  66      10.097  10.611  28.742  1.00  9.51           O  
ANISOU  537  O   GLY A  66     1342    970   1301    -10    -43    239       O  
ATOM    538  N   HIS A  67       9.371  12.381  27.506  1.00  8.42           N  
ANISOU  538  N   HIS A  67     1212    875   1113    -67     22    232       N  
ATOM    539  CA  HIS A  67      10.600  12.479  26.715  1.00  9.09           C  
ANISOU  539  CA  HIS A  67     1235    970   1248    -71     42    140       C  
ATOM    540  C   HIS A  67      10.976  13.912  26.344  1.00  9.22           C  
ANISOU  540  C   HIS A  67     1201    971   1331   -177    146     90       C  
ATOM    541  O   HIS A  67      12.047  14.056  25.690  1.00 11.52           O  
ANISOU  541  O   HIS A  67     1362   1068   1947    -24    312     76       O  
ATOM    542  CB  HIS A  67      10.462  11.589  25.466  1.00  8.43           C  
ANISOU  542  CB  HIS A  67      955    949   1298   -125     46    238       C  
ATOM    543  CG  HIS A  67       9.387  12.072  24.582  1.00  8.19           C  
ANISOU  543  CG  HIS A  67     1107    772   1235   -203    146    133       C  
ATOM    544  ND1 HIS A  67       8.020  11.920  24.821  1.00  8.45           N  
ANISOU  544  ND1 HIS A  67     1111    866   1232   -115      5    151       N  
ATOM    545  CD2 HIS A  67       9.454  12.768  23.407  1.00  9.48           C  
ANISOU  545  CD2 HIS A  67      872    979   1751   -111    188    394       C  
ATOM    546  CE1 HIS A  67       7.349  12.512  23.844  1.00  7.81           C  
ANISOU  546  CE1 HIS A  67      819    735   1415   -167    316    105       C  
ATOM    547  NE2 HIS A  67       8.167  13.051  22.946  1.00  8.87           N  
ANISOU  547  NE2 HIS A  67     1192    771   1409    -77    204    454       N  
ATOM    548  N   GLU A  68      10.182  14.922  26.667  1.00  7.77           N  
ANISOU  548  N   GLU A  68     1051    839   1064   -152     85    198       N  
ATOM    549  CA  GLU A  68      10.406  16.336  26.321  1.00  7.59           C  
ANISOU  549  CA  GLU A  68     1049    839    995    -34     32    156       C  
ATOM    550  C   GLU A  68      10.613  17.061  27.643  1.00  7.52           C  
ANISOU  550  C   GLU A  68     1148    756    952     14     82    177       C  
ATOM    551  O   GLU A  68       9.614  17.305  28.351  1.00  8.78           O  
ANISOU  551  O   GLU A  68     1131   1187   1019    -21     79     68       O  
ATOM    552  CB  GLU A  68       9.192  16.837  25.566  1.00  7.18           C  
ANISOU  552  CB  GLU A  68      955    801    973    -92    124    163       C  
ATOM    553  CG  GLU A  68       9.212  18.297  25.106  1.00  8.74           C  
ANISOU  553  CG  GLU A  68     1245    958   1118    -13    137    220       C  
ATOM    554  CD  GLU A  68       7.942  18.634  24.325  1.00  8.44           C  
ANISOU  554  CD  GLU A  68     1231   1002    975     71    175    111       C  
ATOM    555  OE1 GLU A  68       6.912  18.977  24.925  1.00 10.86           O  
ANISOU  555  OE1 GLU A  68     1270   1662   1195    133     92     42       O  
ATOM    556  OE2 GLU A  68       7.975  18.520  23.053  1.00  9.89           O  
ANISOU  556  OE2 GLU A  68     1324   1415   1019    161    123    247       O  
ATOM    557  N   ALA A  69      11.865  17.358  28.051  1.00  7.29           N  
ANISOU  557  N   ALA A  69     1030    789    950    -41     86    199       N  
ATOM    558  CA  ALA A  69      12.044  17.815  29.452  1.00  7.51           C  
ANISOU  558  CA  ALA A  69      994    850   1011    -23      2    153       C  
ATOM    559  C   ALA A  69      13.397  18.498  29.620  1.00  7.54           C  
ANISOU  559  C   ALA A  69     1112    814    937    -61     53    204       C  
ATOM    560  O   ALA A  69      14.267  18.491  28.751  1.00  8.69           O  
ANISOU  560  O   ALA A  69     1210   1024   1068   -166     97     83       O  
ATOM    561  CB  ALA A  69      11.986  16.612  30.401  1.00  8.81           C  
ANISOU  561  CB  ALA A  69     1225    982   1141   -144   -109    144       C  
ATOM    562  N   ALA A  70      13.540  19.100  30.806  1.00  8.48           N  
ANISOU  562  N   ALA A  70     1194    984   1045    -37     29     39       N  
ATOM    563  CA  ALA A  70      14.818  19.667  31.229  1.00  9.27           C  
ANISOU  563  CA  ALA A  70     1297   1051   1174    -43    -35    -25       C  
ATOM    564  C   ALA A  70      14.944  19.552  32.766  1.00  8.90           C  
ANISOU  564  C   ALA A  70     1150   1020   1210     40     18    -60       C  
ATOM    565  O   ALA A  70      13.939  19.585  33.493  1.00  9.48           O  
ANISOU  565  O   ALA A  70     1201   1210   1190     55    -57     13       O  
ATOM    566  CB  ALA A  70      14.953  21.118  30.766  1.00 10.37           C  
ANISOU  566  CB  ALA A  70     1562   1104   1274   -183    -79     40       C  
ATOM    567  N   GLY A  71      16.193  19.450  33.247  1.00  9.79           N  
ANISOU  567  N   GLY A  71     1206   1262   1251   -118   -119     29       N  
ATOM    568  CA  GLY A  71      16.426  19.322  34.674  1.00  9.92           C  
ANISOU  568  CA  GLY A  71     1217   1270   1282    -65    -99    -65       C  
ATOM    569  C   GLY A  71      17.864  19.648  35.064  1.00  9.21           C  
ANISOU  569  C   GLY A  71     1208   1109   1180    -47   -121    -61       C  
ATOM    570  O   GLY A  71      18.594  20.281  34.289  1.00 10.53           O  
ANISOU  570  O   GLY A  71     1447   1307   1246   -148   -105     14       O  
ATOM    571  N   ILE A  72      18.214  19.273  36.287  1.00 10.38           N  
ANISOU  571  N   ILE A  72     1286   1394   1262    -80   -171     35       N  
ATOM    572  CA  ILE A  72      19.526  19.580  36.883  1.00 10.94           C  
ANISOU  572  CA  ILE A  72     1365   1375   1415    -78   -178     10       C  
ATOM    573  C   ILE A  72      20.180  18.286  37.333  1.00 10.31           C  
ANISOU  573  C   ILE A  72     1312   1407   1201   -133   -167     19       C  
ATOM    574  O   ILE A  72      19.535  17.474  38.023  1.00 12.01           O  
ANISOU  574  O   ILE A  72     1470   1584   1511   -102   -124    168       O  
ATOM    575  CB  ILE A  72      19.382  20.591  38.070  1.00 12.32           C  
ANISOU  575  CB  ILE A  72     1502   1639   1539    -15   -287    -41       C  
ATOM    576  CG1 ILE A  72      18.838  21.939  37.521  1.00 14.62           C  
ANISOU  576  CG1 ILE A  72     2047   1669   1840     90   -424   -172       C  
ATOM    577  CG2 ILE A  72      20.711  20.803  38.798  1.00 13.90           C  
ANISOU  577  CG2 ILE A  72     1757   1849   1677     43   -422   -156       C  
ATOM    578  CD1 ILE A  72      18.314  22.888  38.566  1.00 17.58           C  
ANISOU  578  CD1 ILE A  72     2417   2261   2002    145   -256   -294       C  
ATOM    579  N   VAL A  73      21.443  18.047  37.023  1.00 10.56           N  
ANISOU  579  N   VAL A  73     1316   1281   1415   -230   -204    174       N  
ATOM    580  CA  VAL A  73      22.133  16.807  37.412  1.00 11.06           C  
ANISOU  580  CA  VAL A  73     1572   1289   1341   -104   -241     39       C  
ATOM    581  C   VAL A  73      22.254  16.723  38.938  1.00 11.87           C  
ANISOU  581  C   VAL A  73     1629   1429   1454    -89   -251      8       C  
ATOM    582  O   VAL A  73      22.808  17.635  39.576  1.00 11.97           O  
ANISOU  582  O   VAL A  73     1598   1498   1452   -103   -383      8       O  
ATOM    583  CB  VAL A  73      23.526  16.704  36.744  1.00 11.55           C  
ANISOU  583  CB  VAL A  73     1516   1475   1399   -110   -282    100       C  
ATOM    584  CG1 VAL A  73      24.281  15.484  37.224  1.00 11.93           C  
ANISOU  584  CG1 VAL A  73     1408   1586   1541    -60   -263    146       C  
ATOM    585  CG2 VAL A  73      23.424  16.748  35.219  1.00 11.90           C  
ANISOU  585  CG2 VAL A  73     1383   1690   1450    -68   -240    108       C  
ATOM    586  N   GLU A  74      21.782  15.635  39.539  1.00 11.47           N  
ANISOU  586  N   GLU A  74     1400   1477   1481    -38   -242    101       N  
ATOM    587  CA  GLU A  74      21.939  15.310  40.958  1.00 11.93           C  
ANISOU  587  CA  GLU A  74     1668   1481   1383    -46   -272     53       C  
ATOM    588  C   GLU A  74      23.250  14.560  41.207  1.00 12.77           C  
ANISOU  588  C   GLU A  74     1711   1734   1407     64   -304     63       C  
ATOM    589  O   GLU A  74      23.961  14.875  42.172  1.00 14.43           O  
ANISOU  589  O   GLU A  74     1945   1996   1541      3   -421      5       O  
ATOM    590  CB AGLU A  74      20.701  14.565  41.490  0.87 12.48           C  
ANISOU  590  CB AGLU A  74     1716   1711   1316    -23   -186    157       C  
ATOM    591  CG AGLU A  74      20.864  13.930  42.879  0.87 11.50           C  
ANISOU  591  CG AGLU A  74     1543   1535   1291    120    -71    179       C  
ATOM    592  CD AGLU A  74      21.459  12.530  42.914  0.87 10.47           C  
ANISOU  592  CD AGLU A  74     1417   1354   1206    -95    -30    171       C  
ATOM    593  OE1AGLU A  74      21.498  11.910  41.833  0.87 11.12           O  
ANISOU  593  OE1AGLU A  74     1547   1400   1276     64    -67     72       O  
ATOM    594  OE2AGLU A  74      21.824  12.078  44.038  0.87 12.36           O  
ANISOU  594  OE2AGLU A  74     1676   1701   1318     -4   -221    235       O  
ATOM    595  CB BGLU A  74      20.793  14.432  41.472  0.13 14.85           C  
ANISOU  595  CB BGLU A  74     1805   1910   1929   -130    -56     98       C  
ATOM    596  CG BGLU A  74      20.733  14.199  42.962  0.13 17.52           C  
ANISOU  596  CG BGLU A  74     2298   2397   1963    -57     18     35       C  
ATOM    597  CD BGLU A  74      21.523  13.089  43.596  0.13 19.12           C  
ANISOU  597  CD BGLU A  74     2493   2556   2217    101    -10     43       C  
ATOM    598  OE1BGLU A  74      22.756  13.196  43.770  0.13 20.15           O  
ANISOU  598  OE1BGLU A  74     2507   2748   2400     37     66     11       O  
ATOM    599  OE2BGLU A  74      20.940  12.047  43.983  0.13 19.48           O  
ANISOU  599  OE2BGLU A  74     2457   2712   2232     34     28     76       O  
ATOM    600  N   SER A  75      23.626  13.598  40.371  1.00 12.29           N  
ANISOU  600  N   SER A  75     1557   1557   1557      0      0      0       N  
ATOM    601  CA  SER A  75      24.862  12.832  40.558  1.00 12.72           C  
ANISOU  601  CA  SER A  75     1586   1769   1478    137   -365    187       C  
ATOM    602  C   SER A  75      25.228  12.148  39.245  1.00 12.86           C  
ANISOU  602  C   SER A  75     1587   1792   1508     89   -287    157       C  
ATOM    603  O   SER A  75      24.399  11.969  38.334  1.00 12.63           O  
ANISOU  603  O   SER A  75     1529   1708   1561    -21   -257    125       O  
ATOM    604  CB  SER A  75      24.766  11.770  41.666  1.00 13.27           C  
ANISOU  604  CB  SER A  75     1661   1894   1485     89   -295    214       C  
ATOM    605  OG  SER A  75      23.848  10.714  41.385  1.00 12.93           O  
ANISOU  605  OG  SER A  75     1736   1682   1493     99   -215    263       O  
ATOM    606  N   ILE A  76      26.522  11.794  39.142  1.00 13.06           N  
ANISOU  606  N   ILE A  76     1611   1809   1542    174   -241    129       N  
ATOM    607  CA  ILE A  76      27.061  11.125  37.965  1.00 12.94           C  
ANISOU  607  CA  ILE A  76     1536   1886   1494    133   -302    190       C  
ATOM    608  C   ILE A  76      27.729   9.816  38.368  1.00 13.55           C  
ANISOU  608  C   ILE A  76     1645   1938   1564    255   -316    126       C  
ATOM    609  O   ILE A  76      28.339   9.703  39.445  1.00 15.20           O  
ANISOU  609  O   ILE A  76     1983   2273   1520    279   -392    132       O  
ATOM    610  CB  ILE A  76      28.054  11.995  37.155  1.00 13.43           C  
ANISOU  610  CB  ILE A  76     1540   1998   1566     13   -355    227       C  
ATOM    611  CG1 ILE A  76      29.309  12.386  37.956  1.00 15.13           C  
ANISOU  611  CG1 ILE A  76     1639   2208   1900    -42   -318    104       C  
ATOM    612  CG2 ILE A  76      27.332  13.189  36.561  1.00 13.35           C  
ANISOU  612  CG2 ILE A  76     1535   1896   1641   -136   -344    285       C  
ATOM    613  CD1 ILE A  76      30.379  13.112  37.168  1.00 16.27           C  
ANISOU  613  CD1 ILE A  76     1788   2391   2003   -161   -298     88       C  
ATOM    614  N   GLY A  77      27.616   8.817  37.507  1.00 13.93           N  
ANISOU  614  N   GLY A  77     1784   1963   1545    216   -275    170       N  
ATOM    615  CA  GLY A  77      28.279   7.536  37.699  1.00 14.56           C  
ANISOU  615  CA  GLY A  77     2037   1774   1722     69   -154    185       C  
ATOM    616  C   GLY A  77      29.742   7.655  37.285  1.00 15.66           C  
ANISOU  616  C   GLY A  77     2099   2121   1728     97   -255    285       C  
ATOM    617  O   GLY A  77      30.247   8.620  36.707  1.00 15.96           O  
ANISOU  617  O   GLY A  77     1784   2225   2056    188   -266    421       O  
ATOM    618  N   GLU A  78      30.463   6.554  37.594  1.00 19.83           N  
ANISOU  618  N   GLU A  78     2726   2587   2223    504   -271    405       N  
ATOM    619  CA  GLU A  78      31.873   6.462  37.260  1.00 25.55           C  
ANISOU  619  CA  GLU A  78     2867   4105   2736    274   -181    239       C  
ATOM    620  C   GLU A  78      32.131   6.670  35.773  1.00 19.53           C  
ANISOU  620  C   GLU A  78     2091   2675   2654    383   -255    116       C  
ATOM    621  O   GLU A  78      31.425   6.140  34.913  1.00 18.59           O  
ANISOU  621  O   GLU A  78     2053   2783   2229    455    -74    175       O  
ATOM    622  CB AGLU A  78      32.356   5.029  37.621  0.63 34.99           C  
ANISOU  622  CB AGLU A  78     4414   4434   4446    805   -424    151       C  
ATOM    623  CG AGLU A  78      31.654   4.390  38.795  0.63 47.11           C  
ANISOU  623  CG AGLU A  78     6049   6748   5103    345    200    538       C  
ATOM    624  CD AGLU A  78      31.543   2.884  38.825  0.63 54.49           C  
ANISOU  624  CD AGLU A  78     7568   6944   6191    220     71    471       C  
ATOM    625  OE1AGLU A  78      32.573   2.200  38.639  0.63 56.60           O  
ANISOU  625  OE1AGLU A  78     7586   7362   6558    296    187    552       O  
ATOM    626  OE2AGLU A  78      30.430   2.347  39.051  0.63 56.28           O  
ANISOU  626  OE2AGLU A  78     7527   7337   6518    281    160    506       O  
ATOM    627  CB BGLU A  78      32.392   5.083  37.694  0.37 32.40           C  
ANISOU  627  CB BGLU A  78     4423   4132   3755    258   -315    422       C  
ATOM    628  CG BGLU A  78      33.802   4.742  37.252  0.37 40.86           C  
ANISOU  628  CG BGLU A  78     4712   5871   4942    212     83    189       C  
ATOM    629  CD BGLU A  78      34.167   3.303  37.569  0.37 46.15           C  
ANISOU  629  CD BGLU A  78     5617   5973   5945    243    -65    288       C  
ATOM    630  OE1BGLU A  78      33.849   2.834  38.681  0.37 47.36           O  
ANISOU  630  OE1BGLU A  78     5807   6165   6021    294     44    312       O  
ATOM    631  OE2BGLU A  78      34.767   2.638  36.701  0.37 47.37           O  
ANISOU  631  OE2BGLU A  78     5775   6225   6000    251     87    305       O  
ATOM    632  N   GLY A  79      33.140   7.416  35.409  1.00 18.48           N  
ANISOU  632  N   GLY A  79     1976   2730   2316    538   -331    382       N  
ATOM    633  CA  GLY A  79      33.580   7.641  34.059  1.00 18.48           C  
ANISOU  633  CA  GLY A  79     1830   2766   2426    528   -138    334       C  
ATOM    634  C   GLY A  79      32.828   8.678  33.253  1.00 17.40           C  
ANISOU  634  C   GLY A  79     1738   2623   2249    414   -151    257       C  
ATOM    635  O   GLY A  79      33.224   8.952  32.104  1.00 19.20           O  
ANISOU  635  O   GLY A  79     1924   2949   2422    423     23    348       O  
ATOM    636  N   VAL A  80      31.788   9.304  33.776  1.00 15.60           N  
ANISOU  636  N   VAL A  80     1570   2344   2012    259   -218    221       N  
ATOM    637  CA  VAL A  80      31.090  10.407  33.071  1.00 14.40           C  
ANISOU  637  CA  VAL A  80     1391   2205   1875    125   -102    260       C  
ATOM    638  C   VAL A  80      32.005  11.625  32.932  1.00 14.45           C  
ANISOU  638  C   VAL A  80     1347   2254   1888    171   -134    152       C  
ATOM    639  O   VAL A  80      32.619  12.053  33.939  1.00 17.01           O  
ANISOU  639  O   VAL A  80     1663   2737   2062     -8   -414    219       O  
ATOM    640  CB  VAL A  80      29.803  10.760  33.824  1.00 13.18           C  
ANISOU  640  CB  VAL A  80     1448   1955   1606     46   -102    261       C  
ATOM    641  CG1 VAL A  80      29.178  12.053  33.336  1.00 13.07           C  
ANISOU  641  CG1 VAL A  80     1383   1903   1681    109   -125     60       C  
ATOM    642  CG2 VAL A  80      28.789   9.624  33.720  1.00 13.63           C  
ANISOU  642  CG2 VAL A  80     1432   2027   1722     14   -191    284       C  
ATOM    643  N   THR A  81      32.089  12.189  31.737  1.00 15.09           N  
ANISOU  643  N   THR A  81     1407   2423   1901     35   -156    276       N  
ATOM    644  CA  THR A  81      32.984  13.305  31.457  1.00 16.09           C  
ANISOU  644  CA  THR A  81     1438   2559   2115    -30   -135    274       C  
ATOM    645  C   THR A  81      32.281  14.523  30.896  1.00 16.53           C  
ANISOU  645  C   THR A  81     1613   2499   2169    -26   -312    237       C  
ATOM    646  O   THR A  81      32.889  15.606  30.778  1.00 20.03           O  
ANISOU  646  O   THR A  81     1983   2786   2840   -320   -372    319       O  
ATOM    647  CB  THR A  81      34.090  12.908  30.438  1.00 17.66           C  
ANISOU  647  CB  THR A  81     1648   2848   2213     28      5    305       C  
ATOM    648  OG1 THR A  81      33.478  12.521  29.199  1.00 18.78           O  
ANISOU  648  OG1 THR A  81     1842   2989   2303    -66    117     96       O  
ATOM    649  CG2 THR A  81      34.979  11.788  30.962  1.00 19.60           C  
ANISOU  649  CG2 THR A  81     1534   2934   2980      1     53    463       C  
ATOM    650  N   THR A  82      31.012  14.431  30.454  1.00 14.33           N  
ANISOU  650  N   THR A  82     1420   2402   1623    -33   -187    264       N  
ATOM    651  CA  THR A  82      30.345  15.481  29.675  1.00 13.79           C  
ANISOU  651  CA  THR A  82     1486   1844   1909   -303   -159    182       C  
ATOM    652  C   THR A  82      29.389  16.333  30.487  1.00 13.17           C  
ANISOU  652  C   THR A  82     1322   1825   1855   -311   -200    256       C  
ATOM    653  O   THR A  82      28.895  17.364  29.981  1.00 14.71           O  
ANISOU  653  O   THR A  82     1598   1970   2021   -177    -94    409       O  
ATOM    654  CB  THR A  82      29.655  14.896  28.423  1.00 14.11           C  
ANISOU  654  CB  THR A  82     1502   2028   1832   -228   -131    109       C  
ATOM    655  OG1 THR A  82      28.631  13.961  28.828  1.00 13.84           O  
ANISOU  655  OG1 THR A  82     1418   2051   1791   -212   -263     55       O  
ATOM    656  CG2 THR A  82      30.660  14.212  27.492  1.00 16.04           C  
ANISOU  656  CG2 THR A  82     1885   2324   1884   -158    -64     85       C  
ATOM    657  N   VAL A  83      29.027  15.937  31.704  1.00 13.49           N  
ANISOU  657  N   VAL A  83     1462   1911   1754   -191   -170    160       N  
ATOM    658  CA  VAL A  83      28.171  16.693  32.607  1.00 14.05           C  
ANISOU  658  CA  VAL A  83     1534   1884   1920   -125   -165     98       C  
ATOM    659  C   VAL A  83      28.727  16.524  34.034  1.00 14.26           C  
ANISOU  659  C   VAL A  83     1634   1821   1964    -90   -175    139       C  
ATOM    660  O   VAL A  83      29.447  15.544  34.315  1.00 14.67           O  
ANISOU  660  O   VAL A  83     1576   2071   1928    -24   -281    124       O  
ATOM    661  CB  VAL A  83      26.682  16.302  32.529  1.00 13.41           C  
ANISOU  661  CB  VAL A  83     1412   1813   1869    -10   -203    200       C  
ATOM    662  CG1 VAL A  83      26.076  16.461  31.135  1.00 14.21           C  
ANISOU  662  CG1 VAL A  83     1564   2051   1783     86    -96    237       C  
ATOM    663  CG2 VAL A  83      26.445  14.898  33.056  1.00 14.52           C  
ANISOU  663  CG2 VAL A  83     1486   1918   2112    -84   -221    276       C  
ATOM    664  N   ARG A  84      28.330  17.411  34.924  1.00 14.65           N  
ANISOU  664  N   ARG A  84     1758   1915   1891    -87   -253     74       N  
ATOM    665  CA  ARG A  84      28.660  17.360  36.344  1.00 17.04           C  
ANISOU  665  CA  ARG A  84     2236   2327   1909     62   -216     11       C  
ATOM    666  C   ARG A  84      27.460  17.716  37.213  1.00 14.58           C  
ANISOU  666  C   ARG A  84     1990   1792   1759    -44   -301    157       C  
ATOM    667  O   ARG A  84      26.548  18.400  36.751  1.00 14.22           O  
ANISOU  667  O   ARG A  84     1749   1865   1789   -224   -329    220       O  
ATOM    668  CB  ARG A  84      29.774  18.241  36.824  1.00 22.71           C  
ANISOU  668  CB  ARG A  84     2445   3655   2530   -162   -289   -338       C  
ATOM    669  CG  ARG A  84      30.132  19.481  36.147  1.00 35.03           C  
ANISOU  669  CG  ARG A  84     4792   4452   4067   -307     63    330       C  
ATOM    670  CD  ARG A  84      31.693  19.153  36.170  1.00 45.34           C  
ANISOU  670  CD  ARG A  84     5185   6847   5196    485    167    -37       C  
ATOM    671  NE  ARG A  84      32.027  20.464  35.794  1.00 54.39           N  
ANISOU  671  NE  ARG A  84     6982   7195   6488    315    352    251       N  
ATOM    672  CZ  ARG A  84      32.789  21.481  35.779  1.00 60.17           C  
ANISOU  672  CZ  ARG A  84     7645   7822   7394   -126    519     46       C  
ATOM    673  NH1 ARG A  84      32.416  22.586  35.147  1.00 62.23           N  
ANISOU  673  NH1 ARG A  84     7856   8163   7626     93    402    197       N  
ATOM    674  NH2 ARG A  84      33.961  21.433  36.397  1.00 61.85           N  
ANISOU  674  NH2 ARG A  84     7833   8056   7610    109    374    185       N  
ATOM    675  N   PRO A  85      27.454  17.286  38.478  1.00 13.88           N  
ANISOU  675  N   PRO A  85     1786   1826   1662   -110   -392    129       N  
ATOM    676  CA  PRO A  85      26.402  17.686  39.414  1.00 14.05           C  
ANISOU  676  CA  PRO A  85     1915   1830   1595   -137   -417     43       C  
ATOM    677  C   PRO A  85      26.178  19.198  39.377  1.00 13.72           C  
ANISOU  677  C   PRO A  85     1780   1865   1568   -187   -319    150       C  
ATOM    678  O   PRO A  85      27.137  19.994  39.378  1.00 15.33           O  
ANISOU  678  O   PRO A  85     1966   1998   1860   -351   -381    -16       O  
ATOM    679  CB  PRO A  85      26.828  17.151  40.802  1.00 15.63           C  
ANISOU  679  CB  PRO A  85     2037   2255   1649     54   -457    117       C  
ATOM    680  CG  PRO A  85      27.747  16.015  40.406  1.00 16.92           C  
ANISOU  680  CG  PRO A  85     2141   2173   2112     91   -460    241       C  
ATOM    681  CD  PRO A  85      28.488  16.469  39.143  1.00 15.97           C  
ANISOU  681  CD  PRO A  85     1871   2005   2191    -61   -482    301       C  
ATOM    682  N   GLY A  86      24.904  19.606  39.306  1.00 13.12           N  
ANISOU  682  N   GLY A  86     1847   1661   1476   -127   -400    -65       N  
ATOM    683  CA  GLY A  86      24.540  21.003  39.250  1.00 12.86           C  
ANISOU  683  CA  GLY A  86     1720   1728   1440   -177   -308   -132       C  
ATOM    684  C   GLY A  86      24.332  21.553  37.845  1.00 12.52           C  
ANISOU  684  C   GLY A  86     1622   1597   1539   -181   -362    -13       C  
ATOM    685  O   GLY A  86      23.761  22.659  37.710  1.00 13.93           O  
ANISOU  685  O   GLY A  86     1997   1585   1710   -104   -401   -103       O  
ATOM    686  N   ASP A  87      24.764  20.861  36.807  1.00 11.83           N  
ANISOU  686  N   ASP A  87     1490   1572   1434   -276   -232     88       N  
ATOM    687  CA  ASP A  87      24.577  21.362  35.429  1.00 12.00           C  
ANISOU  687  CA  ASP A  87     1543   1607   1411   -104   -314     50       C  
ATOM    688  C   ASP A  87      23.102  21.225  35.024  1.00 11.16           C  
ANISOU  688  C   ASP A  87     1575   1251   1414   -283   -274     -5       C  
ATOM    689  O   ASP A  87      22.416  20.272  35.397  1.00 11.89           O  
ANISOU  689  O   ASP A  87     1556   1416   1548   -322   -259    172       O  
ATOM    690  CB  ASP A  87      25.417  20.528  34.434  1.00 13.35           C  
ANISOU  690  CB  ASP A  87     1624   1854   1595   -137   -299    -16       C  
ATOM    691  CG  ASP A  87      26.917  20.796  34.448  1.00 14.90           C  
ANISOU  691  CG  ASP A  87     1711   1958   1994   -114   -268     79       C  
ATOM    692  OD1 ASP A  87      27.332  21.850  35.003  1.00 15.87           O  
ANISOU  692  OD1 ASP A  87     1738   2011   2282   -233   -302    105       O  
ATOM    693  OD2 ASP A  87      27.653  19.964  33.855  1.00 15.69           O  
ANISOU  693  OD2 ASP A  87     1819   2127   2015   -124   -102    120       O  
ATOM    694  N   LYS A  88      22.646  22.192  34.221  1.00 11.05           N  
ANISOU  694  N   LYS A  88     1421   1274   1503   -243   -349     70       N  
ATOM    695  CA  LYS A  88      21.355  22.092  33.527  1.00 10.63           C  
ANISOU  695  CA  LYS A  88     1343   1270   1425   -243   -259     20       C  
ATOM    696  C   LYS A  88      21.550  21.206  32.285  1.00  9.96           C  
ANISOU  696  C   LYS A  88     1091   1378   1314   -171   -197     58       C  
ATOM    697  O   LYS A  88      22.566  21.251  31.603  1.00 11.01           O  
ANISOU  697  O   LYS A  88     1366   1327   1492   -299   -125    -42       O  
ATOM    698  CB  LYS A  88      20.870  23.488  33.105  1.00 10.88           C  
ANISOU  698  CB  LYS A  88     1576   1219   1338   -200   -243     43       C  
ATOM    699  CG  LYS A  88      20.365  24.315  34.294  1.00 11.86           C  
ANISOU  699  CG  LYS A  88     1811   1273   1422   -153   -225     56       C  
ATOM    700  CD  LYS A  88      19.895  25.717  33.919  1.00 11.92           C  
ANISOU  700  CD  LYS A  88     1944   1183   1401   -269   -277     70       C  
ATOM    701  CE  LYS A  88      19.259  26.427  35.086  1.00 12.84           C  
ANISOU  701  CE  LYS A  88     2193   1116   1568   -216   -183     21       C  
ATOM    702  NZ  LYS A  88      18.974  27.868  34.742  1.00 13.92           N  
ANISOU  702  NZ  LYS A  88     2408   1264   1618    -59   -170    -61       N  
ATOM    703  N   VAL A  89      20.549  20.314  32.102  1.00  9.56           N  
ANISOU  703  N   VAL A  89     1309   1068   1257   -112   -111     69       N  
ATOM    704  CA  VAL A  89      20.599  19.299  31.054  1.00  9.13           C  
ANISOU  704  CA  VAL A  89     1145   1146   1179   -150    -68     -1       C  
ATOM    705  C   VAL A  89      19.223  19.085  30.417  1.00  8.86           C  
ANISOU  705  C   VAL A  89     1141   1057   1168    -64     32    110       C  
ATOM    706  O   VAL A  89      18.177  19.292  31.021  1.00 10.03           O  
ANISOU  706  O   VAL A  89     1209   1340   1263   -134    -49    -74       O  
ATOM    707  CB  VAL A  89      21.099  17.942  31.623  1.00 10.18           C  
ANISOU  707  CB  VAL A  89     1294   1193   1380   -161   -103     58       C  
ATOM    708  CG1 VAL A  89      22.599  17.990  31.972  1.00 10.55           C  
ANISOU  708  CG1 VAL A  89     1340   1361   1309     18   -109    120       C  
ATOM    709  CG2 VAL A  89      20.275  17.486  32.797  1.00 11.22           C  
ANISOU  709  CG2 VAL A  89     1229   1345   1688   -206    -85    305       C  
ATOM    710  N   ILE A  90      19.283  18.582  29.159  1.00  8.59           N  
ANISOU  710  N   ILE A  90     1131   1017   1117   -171    -60     55       N  
ATOM    711  CA  ILE A  90      18.098  18.093  28.449  1.00  8.82           C  
ANISOU  711  CA  ILE A  90     1120   1093   1139   -140    -33    140       C  
ATOM    712  C   ILE A  90      18.331  16.623  28.104  1.00  8.89           C  
ANISOU  712  C   ILE A  90     1226   1150   1002   -159     11     41       C  
ATOM    713  O   ILE A  90      19.325  16.299  27.420  1.00  8.96           O  
ANISOU  713  O   ILE A  90     1066   1114   1224   -162     24    147       O  
ATOM    714  CB  ILE A  90      17.789  18.934  27.171  1.00  8.61           C  
ANISOU  714  CB  ILE A  90     1146    963   1163   -183    -79     93       C  
ATOM    715  CG1 ILE A  90      17.314  20.320  27.581  1.00  9.60           C  
ANISOU  715  CG1 ILE A  90     1295   1113   1239    -19    -20     63       C  
ATOM    716  CG2 ILE A  90      16.780  18.291  26.240  1.00  9.30           C  
ANISOU  716  CG2 ILE A  90     1276   1075   1184   -135   -119    119       C  
ATOM    717  CD1 ILE A  90      17.173  21.331  26.466  1.00 10.34           C  
ANISOU  717  CD1 ILE A  90     1554   1050   1325     21    -97     41       C  
ATOM    718  N   PRO A  91      17.460  15.695  28.543  1.00  8.26           N  
ANISOU  718  N   PRO A  91     1126    989   1022   -101    -20     80       N  
ATOM    719  CA  PRO A  91      17.527  14.294  28.114  1.00  8.42           C  
ANISOU  719  CA  PRO A  91     1123    941   1134    -89     30    144       C  
ATOM    720  C   PRO A  91      17.282  14.185  26.601  1.00  8.34           C  
ANISOU  720  C   PRO A  91     1079    893   1195   -133    -43    173       C  
ATOM    721  O   PRO A  91      16.452  14.931  26.053  1.00  8.71           O  
ANISOU  721  O   PRO A  91     1178   1006   1127    -39    -42     40       O  
ATOM    722  CB  PRO A  91      16.431  13.603  28.929  1.00 10.40           C  
ANISOU  722  CB  PRO A  91     1385   1168   1398   -178    193    191       C  
ATOM    723  CG  PRO A  91      16.111  14.524  30.057  1.00 12.37           C  
ANISOU  723  CG  PRO A  91     1756   1200   1745   -155    381     66       C  
ATOM    724  CD  PRO A  91      16.335  15.932  29.475  1.00  9.47           C  
ANISOU  724  CD  PRO A  91     1240   1151   1209   -155     51     75       C  
ATOM    725  N   LEU A  92      17.979  13.255  25.956  1.00  8.17           N  
ANISOU  725  N   LEU A  92     1057   1000   1048    -72    -30    127       N  
ATOM    726  CA  LEU A  92      17.950  13.077  24.497  1.00  8.12           C  
ANISOU  726  CA  LEU A  92     1202    883    998   -109    -26    173       C  
ATOM    727  C   LEU A  92      17.246  11.751  24.178  1.00  7.40           C  
ANISOU  727  C   LEU A  92      999    880    933    -19     44    179       C  
ATOM    728  O   LEU A  92      17.855  10.679  24.391  1.00  8.99           O  
ANISOU  728  O   LEU A  92     1206    900   1308     -9    -85    134       O  
ATOM    729  CB  LEU A  92      19.387  13.068  23.930  1.00  8.84           C  
ANISOU  729  CB  LEU A  92     1316    916   1128   -103     50    179       C  
ATOM    730  CG  LEU A  92      20.250  14.271  24.342  1.00  8.84           C  
ANISOU  730  CG  LEU A  92     1132    976   1250   -181     56    133       C  
ATOM    731  CD1 LEU A  92      21.676  14.058  23.816  1.00  9.69           C  
ANISOU  731  CD1 LEU A  92     1239   1228   1214   -191    -89    105       C  
ATOM    732  CD2 LEU A  92      19.665  15.590  23.855  1.00  9.93           C  
ANISOU  732  CD2 LEU A  92     1418   1067   1289   -114     36     78       C  
ATOM    733  N   PHE A  93      16.008  11.796  23.686  1.00  7.48           N  
ANISOU  733  N   PHE A  93     1014    901    927    -58     11    230       N  
ATOM    734  CA  PHE A  93      15.282  10.539  23.354  1.00  7.68           C  
ANISOU  734  CA  PHE A  93     1138    849    931   -134     23    280       C  
ATOM    735  C   PHE A  93      15.904   9.847  22.160  1.00  7.54           C  
ANISOU  735  C   PHE A  93     1120    744    999   -129    -17    201       C  
ATOM    736  O   PHE A  93      15.705   8.626  22.023  1.00  8.85           O  
ANISOU  736  O   PHE A  93     1274    898   1191    -94    -12    153       O  
ATOM    737  CB  PHE A  93      13.777  10.768  23.217  1.00  7.96           C  
ANISOU  737  CB  PHE A  93     1006    979   1040   -164    122    251       C  
ATOM    738  CG  PHE A  93      13.283  11.435  21.948  1.00  7.17           C  
ANISOU  738  CG  PHE A  93      925    771   1029   -127    145    181       C  
ATOM    739  CD1 PHE A  93      13.167  10.693  20.773  1.00  7.36           C  
ANISOU  739  CD1 PHE A  93      864    800   1131    -46     16    130       C  
ATOM    740  CD2 PHE A  93      12.939  12.775  21.926  1.00  8.07           C  
ANISOU  740  CD2 PHE A  93      966    923   1177    -11     92    168       C  
ATOM    741  CE1 PHE A  93      12.733  11.299  19.585  1.00  8.71           C  
ANISOU  741  CE1 PHE A  93     1076   1080   1152    -43     -8    148       C  
ATOM    742  CE2 PHE A  93      12.506  13.378  20.759  1.00  9.13           C  
ANISOU  742  CE2 PHE A  93     1147    900   1421     40     46    292       C  
ATOM    743  CZ  PHE A  93      12.388  12.653  19.577  1.00  9.45           C  
ANISOU  743  CZ  PHE A  93     1144   1174   1273    -28    -42    413       C  
ATOM    744  N   THR A  94      16.592  10.560  21.276  1.00  7.52           N  
ANISOU  744  N   THR A  94     1029    940    888    -81      2    149       N  
ATOM    745  CA  THR A  94      17.459   9.995  20.256  1.00  8.60           C  
ANISOU  745  CA  THR A  94     1134   1087   1049    -64     22    -46       C  
ATOM    746  C   THR A  94      18.895  10.127  20.770  1.00  8.66           C  
ANISOU  746  C   THR A  94     1125   1062   1104    -65     23     63       C  
ATOM    747  O   THR A  94      19.341  11.277  20.951  1.00  9.48           O  
ANISOU  747  O   THR A  94     1206   1117   1279    -99    115     10       O  
ATOM    748  CB  THR A  94      17.278  10.739  18.916  1.00 10.05           C  
ANISOU  748  CB  THR A  94     1096   1635   1089     54     66     54       C  
ATOM    749  OG1 THR A  94      15.902  10.693  18.525  1.00 12.14           O  
ANISOU  749  OG1 THR A  94     1173   2217   1223     88    -74    177       O  
ATOM    750  CG2 THR A  94      18.098  10.090  17.793  1.00 12.87           C  
ANISOU  750  CG2 THR A  94     1476   2272   1142    -48    182   -163       C  
ATOM    751  N   PRO A  95      19.622   9.056  21.096  1.00  8.76           N  
ANISOU  751  N   PRO A  95     1071   1054   1204   -128    -18    108       N  
ATOM    752  CA  PRO A  95      20.980   9.212  21.612  1.00  8.90           C  
ANISOU  752  CA  PRO A  95     1077   1230   1072    -60    -87    185       C  
ATOM    753  C   PRO A  95      21.957   9.706  20.562  1.00  8.67           C  
ANISOU  753  C   PRO A  95     1052   1137   1107    -58    -26    121       C  
ATOM    754  O   PRO A  95      21.664   9.753  19.358  1.00  8.84           O  
ANISOU  754  O   PRO A  95     1066   1100   1194    -30    -15    115       O  
ATOM    755  CB  PRO A  95      21.392   7.781  22.070  1.00 10.61           C  
ANISOU  755  CB  PRO A  95     1304   1238   1491    -58     -1    357       C  
ATOM    756  CG  PRO A  95      20.207   6.927  21.860  1.00 13.55           C  
ANISOU  756  CG  PRO A  95     1591   1341   2216    -50   -490    155       C  
ATOM    757  CD  PRO A  95      19.213   7.639  20.984  1.00  9.56           C  
ANISOU  757  CD  PRO A  95     1097   1107   1428    -62    -89     51       C  
ATOM    758  N   GLN A  96      23.187  10.037  21.002  1.00  8.69           N  
ANISOU  758  N   GLN A  96      991   1147   1164    -21     51     80       N  
ATOM    759  CA  GLN A  96      24.283  10.306  20.060  1.00  9.33           C  
ANISOU  759  CA  GLN A  96     1184   1183   1178    -17    115     67       C  
ATOM    760  C   GLN A  96      25.538   9.646  20.655  1.00  9.61           C  
ANISOU  760  C   GLN A  96     1143   1353   1155    -75     76     81       C  
ATOM    761  O   GLN A  96      26.302  10.273  21.401  1.00 11.35           O  
ANISOU  761  O   GLN A  96     1349   1570   1395   -121    -56     -9       O  
ATOM    762  CB  GLN A  96      24.504  11.769  19.762  1.00  9.36           C  
ANISOU  762  CB  GLN A  96     1181   1166   1209    -40    148     98       C  
ATOM    763  CG  GLN A  96      25.555  11.965  18.655  1.00  9.85           C  
ANISOU  763  CG  GLN A  96     1148   1252   1343   -122     55    114       C  
ATOM    764  CD  GLN A  96      25.779  13.402  18.237  1.00 10.24           C  
ANISOU  764  CD  GLN A  96     1062   1354   1475   -190    137     49       C  
ATOM    765  OE1 GLN A  96      25.098  14.340  18.667  1.00 10.58           O  
ANISOU  765  OE1 GLN A  96     1184   1316   1520   -170    175     65       O  
ATOM    766  NE2 GLN A  96      26.754  13.622  17.322  1.00 12.25           N  
ANISOU  766  NE2 GLN A  96     1297   1612   1748   -122    328    142       N  
ATOM    767  N   CYS A  97      25.798   8.374  20.305  1.00  9.48           N  
ANISOU  767  N   CYS A  97     1053   1372   1178    153    -74      7       N  
ATOM    768  CA  CYS A  97      26.967   7.651  20.832  1.00 11.12           C  
ANISOU  768  CA  CYS A  97     1214   1593   1418    195    -55    213       C  
ATOM    769  C   CYS A  97      28.276   8.203  20.268  1.00 11.41           C  
ANISOU  769  C   CYS A  97     1178   1795   1363    168   -149     61       C  
ATOM    770  O   CYS A  97      29.350   8.034  20.902  1.00 13.86           O  
ANISOU  770  O   CYS A  97     1238   2375   1653    215   -210     23       O  
ATOM    771  CB  CYS A  97      26.846   6.139  20.657  1.00 12.10           C  
ANISOU  771  CB  CYS A  97     1563   1696   1338    200    -97    234       C  
ATOM    772  SG  CYS A  97      27.280   5.467  19.015  1.00 11.13           S  
ANISOU  772  SG  CYS A  97     1245   1556   1428    289     57    147       S  
ATOM    773  N   GLY A  98      28.258   8.790  19.078  1.00 11.34           N  
ANISOU  773  N   GLY A  98     1263   1705   1342    -38    -57     33       N  
ATOM    774  CA  GLY A  98      29.447   9.310  18.429  1.00 13.90           C  
ANISOU  774  CA  GLY A  98     1380   2209   1692   -131     77    -65       C  
ATOM    775  C   GLY A  98      30.359   8.301  17.761  1.00 14.73           C  
ANISOU  775  C   GLY A  98     1406   2454   1737     -4      0   -132       C  
ATOM    776  O   GLY A  98      31.366   8.714  17.146  1.00 18.16           O  
ANISOU  776  O   GLY A  98     1630   2906   2364    -60    345    -61       O  
ATOM    777  N   LYS A  99      30.034   7.002  17.837  1.00 14.72           N  
ANISOU  777  N   LYS A  99     1309   2345   1940    216    -86   -227       N  
ATOM    778  CA  LYS A  99      30.948   5.959  17.385  1.00 17.22           C  
ANISOU  778  CA  LYS A  99     1690   2528   2325    485    -68   -311       C  
ATOM    779  C   LYS A  99      30.365   5.047  16.316  1.00 17.33           C  
ANISOU  779  C   LYS A  99     1705   2595   2283    407    -93   -334       C  
ATOM    780  O   LYS A  99      31.155   4.373  15.610  1.00 20.62           O  
ANISOU  780  O   LYS A  99     1890   3255   2690    592    -57   -653       O  
ATOM    781  CB ALYS A  99      31.365   5.069  18.560  0.58 23.31           C  
ANISOU  781  CB ALYS A  99     2654   3145   3057    642      2    224       C  
ATOM    782  CG ALYS A  99      31.982   5.638  19.820  0.58 30.98           C  
ANISOU  782  CG ALYS A  99     3576   4484   3711    326   -124   -411       C  
ATOM    783  CD ALYS A  99      32.172   4.494  20.814  0.58 38.65           C  
ANISOU  783  CD ALYS A  99     4701   5075   4908    437    148    337       C  
ATOM    784  CE ALYS A  99      32.529   4.928  22.220  0.58 43.93           C  
ANISOU  784  CE ALYS A  99     5354   6119   5220    323    165   -152       C  
ATOM    785  NZ ALYS A  99      32.681   3.755  23.132  0.58 46.93           N  
ANISOU  785  NZ ALYS A  99     5836   6363   5631    373    229    109       N  
ATOM    786  CB BLYS A  99      31.419   5.158  18.610  0.42 16.93           C  
ANISOU  786  CB BLYS A  99     1751   2383   2298    461    -86   -328       C  
ATOM    787  CG BLYS A  99      32.212   5.951  19.643  0.42 18.11           C  
ANISOU  787  CG BLYS A  99     1982   2557   2340    392   -229   -235       C  
ATOM    788  CD BLYS A  99      32.444   5.134  20.902  0.42 22.57           C  
ANISOU  788  CD BLYS A  99     2858   3109   2609    340   -105    158       C  
ATOM    789  CE BLYS A  99      33.444   5.806  21.830  0.42 25.42           C  
ANISOU  789  CE BLYS A  99     3062   3617   2978     70   -208    121       C  
ATOM    790  NZ BLYS A  99      32.970   7.129  22.309  0.42 27.02           N  
ANISOU  790  NZ BLYS A  99     3232   3686   3349    169   -185    142       N  
ATOM    791  N   CYS A 100      29.050   4.965  16.137  1.00 13.76           N  
ANISOU  791  N   CYS A 100     1614   1979   1636    343   -112    -40       N  
ATOM    792  CA  CYS A 100      28.439   4.067  15.160  1.00 13.05           C  
ANISOU  792  CA  CYS A 100     1479   1700   1781    244    -10      2       C  
ATOM    793  C   CYS A 100      28.498   4.692  13.773  1.00 12.61           C  
ANISOU  793  C   CYS A 100     1243   1814   1733    241     33    -64       C  
ATOM    794  O   CYS A 100      28.771   5.869  13.585  1.00 12.94           O  
ANISOU  794  O   CYS A 100     1410   1921   1584    217    110    -87       O  
ATOM    795  CB  CYS A 100      27.027   3.689  15.590  1.00 12.37           C  
ANISOU  795  CB  CYS A 100     1599   1407   1695    298     76     59       C  
ATOM    796  SG  CYS A 100      25.773   5.006  15.358  1.00 10.45           S  
ANISOU  796  SG  CYS A 100     1214   1407   1350    106     57     73       S  
ATOM    797  N   ARG A 101      28.135   3.904  12.751  1.00 14.03           N  
ANISOU  797  N   ARG A 101     1714   1913   1705    268    149   -134       N  
ATOM    798  CA  ARG A 101      28.219   4.351  11.356  1.00 15.23           C  
ANISOU  798  CA  ARG A 101     2067   2078   1641    289    280   -162       C  
ATOM    799  C   ARG A 101      27.278   5.521  11.094  1.00 13.07           C  
ANISOU  799  C   ARG A 101     1640   1879   1447     59    225   -168       C  
ATOM    800  O   ARG A 101      27.540   6.376  10.254  1.00 14.29           O  
ANISOU  800  O   ARG A 101     1800   2035   1595      6    377   -166       O  
ATOM    801  CB AARG A 101      27.974   3.169  10.387  0.67 16.33           C  
ANISOU  801  CB AARG A 101     2257   2078   1869    328    175   -264       C  
ATOM    802  CG AARG A 101      28.561   3.401   9.015  0.67 18.53           C  
ANISOU  802  CG AARG A 101     2557   2454   2029    122    219   -170       C  
ATOM    803  CD AARG A 101      28.509   2.172   8.128  0.67 19.05           C  
ANISOU  803  CD AARG A 101     2451   2472   2313     43    -13   -308       C  
ATOM    804  NE AARG A 101      27.170   1.665   7.827  0.67 19.59           N  
ANISOU  804  NE AARG A 101     2455   2358   2630      9   -162   -199       N  
ATOM    805  CZ AARG A 101      26.836   0.689   6.978  0.67 17.72           C  
ANISOU  805  CZ AARG A 101     2011   2499   2223    148    -94   -205       C  
ATOM    806  NH1AARG A 101      27.806   0.107   6.260  0.67 18.69           N  
ANISOU  806  NH1AARG A 101     2538   2555   2010    182    145   -107       N  
ATOM    807  NH2AARG A 101      25.567   0.273   6.745  0.67 13.61           N  
ANISOU  807  NH2AARG A 101     1757   1914   1501    354   -156    347       N  
ATOM    808  CB BARG A 101      27.944   3.195  10.369  0.33 19.23           C  
ANISOU  808  CB BARG A 101     2609   2369   2330    149    224   -432       C  
ATOM    809  CG BARG A 101      27.597   3.665   8.976  0.33 25.02           C  
ANISOU  809  CG BARG A 101     3226   3423   2857    203     42    191       C  
ATOM    810  CD BARG A 101      27.612   2.683   7.850  0.33 28.85           C  
ANISOU  810  CD BARG A 101     3875   3760   3328    223     37   -121       C  
ATOM    811  NE BARG A 101      26.577   1.659   7.852  0.33 32.02           N  
ANISOU  811  NE BARG A 101     4124   4078   3965      4     25     46       N  
ATOM    812  CZ BARG A 101      26.130   1.088   6.727  0.33 33.20           C  
ANISOU  812  CZ BARG A 101     4309   4293   4012     85    -35     -2       C  
ATOM    813  NH1BARG A 101      26.614   1.458   5.552  0.33 34.14           N  
ANISOU  813  NH1BARG A 101     4496   4393   4082     78     34     47       N  
ATOM    814  NH2BARG A 101      25.195   0.151   6.778  0.33 32.73           N  
ANISOU  814  NH2BARG A 101     4194   4261   3980    138    -72    105       N  
ATOM    815  N   VAL A 102      26.127   5.565  11.800  1.00 11.91           N  
ANISOU  815  N   VAL A 102     1464   1656   1404     45    131    -88       N  
ATOM    816  CA  VAL A 102      25.164   6.672  11.655  1.00 10.28           C  
ANISOU  816  CA  VAL A 102     1353   1366   1187    -95     61     45       C  
ATOM    817  C   VAL A 102      25.705   7.969  12.257  1.00 10.61           C  
ANISOU  817  C   VAL A 102     1303   1487   1241    -55     88      0       C  
ATOM    818  O   VAL A 102      25.687   9.034  11.635  1.00 10.73           O  
ANISOU  818  O   VAL A 102     1267   1589   1220    -94      9     79       O  
ATOM    819  CB  VAL A 102      23.785   6.279  12.212  1.00 10.85           C  
ANISOU  819  CB  VAL A 102     1350   1599   1175   -173     79     99       C  
ATOM    820  CG1 VAL A 102      22.838   7.483  12.136  1.00 11.41           C  
ANISOU  820  CG1 VAL A 102     1432   1600   1303   -143     66   -103       C  
ATOM    821  CG2 VAL A 102      23.186   5.089  11.496  1.00 12.13           C  
ANISOU  821  CG2 VAL A 102     1576   1474   1558   -148    145     27       C  
ATOM    822  N   CYS A 103      26.221   7.870  13.494  1.00 10.19           N  
ANISOU  822  N   CYS A 103     1188   1444   1239    -60     60     23       N  
ATOM    823  CA  CYS A 103      26.803   9.051  14.135  1.00 11.01           C  
ANISOU  823  CA  CYS A 103     1299   1554   1329      4      0      9       C  
ATOM    824  C   CYS A 103      27.975   9.634  13.321  1.00 11.29           C  
ANISOU  824  C   CYS A 103     1219   1671   1399    -10    -33    -42       C  
ATOM    825  O   CYS A 103      28.164  10.863  13.327  1.00 12.17           O  
ANISOU  825  O   CYS A 103     1334   1852   1440   -243     44    -22       O  
ATOM    826  CB  CYS A 103      27.256   8.722  15.564  1.00 11.39           C  
ANISOU  826  CB  CYS A 103     1383   1709   1236      6     14     85       C  
ATOM    827  SG  CYS A 103      25.843   8.623  16.753  1.00  9.56           S  
ANISOU  827  SG  CYS A 103     1171   1372   1088     87     37     92       S  
ATOM    828  N   LYS A 104      28.751   8.785  12.643  1.00 11.53           N  
ANISOU  828  N   LYS A 104     1115   1751   1514    -18     -9      3       N  
ATOM    829  CA  LYS A 104      29.870   9.254  11.814  1.00 14.00           C  
ANISOU  829  CA  LYS A 104     1342   2256   1722    -85    157     96       C  
ATOM    830  C   LYS A 104      29.459   9.747  10.436  1.00 13.77           C  
ANISOU  830  C   LYS A 104     1344   2311   1578   -126    223     45       C  
ATOM    831  O   LYS A 104      30.266  10.392   9.729  1.00 17.18           O  
ANISOU  831  O   LYS A 104     1600   3136   1790   -455    165    246       O  
ATOM    832  CB  LYS A 104      30.914   8.125  11.694  1.00 17.55           C  
ANISOU  832  CB  LYS A 104     1928   2589   2150    155    339     -6       C  
ATOM    833  CG  LYS A 104      31.593   7.729  13.002  1.00 23.58           C  
ANISOU  833  CG  LYS A 104     2820   3606   2534    161     -8    323       C  
ATOM    834  CD ALYS A 104      32.793   6.825  12.774  0.58 28.31           C  
ANISOU  834  CD ALYS A 104     3357   4070   3329    483    153    226       C  
ATOM    835  CE ALYS A 104      32.381   5.390  12.513  0.58 33.22           C  
ANISOU  835  CE ALYS A 104     4392   4380   3851      8     38    217       C  
ATOM    836  NZ ALYS A 104      33.562   4.509  12.249  0.58 36.21           N  
ANISOU  836  NZ ALYS A 104     4702   4714   4340    258    149    206       N  
ATOM    837  CD BLYS A 104      32.560   8.769  13.518  0.42 27.74           C  
ANISOU  837  CD BLYS A 104     3529   3748   3265   -115    168    -14       C  
ATOM    838  CE BLYS A 104      33.536   8.158  14.522  0.42 31.12           C  
ANISOU  838  CE BLYS A 104     4022   4259   3543    230     81    180       C  
ATOM    839  NZ BLYS A 104      34.814   8.931  14.562  0.42 33.20           N  
ANISOU  839  NZ BLYS A 104     4188   4508   3919     79     84    233       N  
ATOM    840  N   HIS A 105      28.226   9.498   9.987  1.00 12.75           N  
ANISOU  840  N   HIS A 105     1380   2005   1458   -136    184     64       N  
ATOM    841  CA  HIS A 105      27.762   9.945   8.661  1.00 12.32           C  
ANISOU  841  CA  HIS A 105     1400   1994   1287   -202    299    -18       C  
ATOM    842  C   HIS A 105      27.412  11.403   8.698  1.00 13.64           C  
ANISOU  842  C   HIS A 105     1643   1957   1583   -260    298    -29       C  
ATOM    843  O   HIS A 105      26.799  11.872   9.675  1.00 17.12           O  
ANISOU  843  O   HIS A 105     2719   2106   1680    -88    481   -203       O  
ATOM    844  CB  HIS A 105      26.522   9.100   8.303  1.00 12.22           C  
ANISOU  844  CB  HIS A 105     1554   1733   1356   -222    228    -97       C  
ATOM    845  CG  HIS A 105      26.108   9.272   6.869  1.00 12.99           C  
ANISOU  845  CG  HIS A 105     1703   1650   1581   -224    -33     58       C  
ATOM    846  ND1 HIS A 105      25.326  10.345   6.443  1.00 15.49           N  
ANISOU  846  ND1 HIS A 105     2437   1741   1706    -18   -261      8       N  
ATOM    847  CD2 HIS A 105      26.296   8.435   5.821  1.00 13.24           C  
ANISOU  847  CD2 HIS A 105     1659   1875   1498   -250    -39     11       C  
ATOM    848  CE1 HIS A 105      25.114  10.138   5.141  1.00 16.04           C  
ANISOU  848  CE1 HIS A 105     2688   1707   1702   -188   -261    116       C  
ATOM    849  NE2 HIS A 105      25.693   9.025   4.730  1.00 14.99           N  
ANISOU  849  NE2 HIS A 105     2147   2098   1450   -162    -65     36       N  
ATOM    850  N   PRO A 106      27.667  12.187   7.635  1.00 14.82           N  
ANISOU  850  N   PRO A 106     1694   2060   1877   -311    344    121       N  
ATOM    851  CA  PRO A 106      27.380  13.612   7.667  1.00 17.99           C  
ANISOU  851  CA  PRO A 106     2383   2081   2372   -280    236    219       C  
ATOM    852  C   PRO A 106      25.923  13.973   7.855  1.00 18.67           C  
ANISOU  852  C   PRO A 106     2494   2237   2364    -77    169    100       C  
ATOM    853  O   PRO A 106      25.627  15.040   8.410  1.00 22.91           O  
ANISOU  853  O   PRO A 106     3513   2214   2977    -23    338     41       O  
ATOM    854  CB  PRO A 106      27.909  14.220   6.347  1.00 20.44           C  
ANISOU  854  CB  PRO A 106     2414   2616   2735   -292    484    491       C  
ATOM    855  CG  PRO A 106      28.310  13.025   5.561  1.00 21.77           C  
ANISOU  855  CG  PRO A 106     3066   2748   2456   -390    504    437       C  
ATOM    856  CD  PRO A 106      28.362  11.773   6.404  1.00 17.86           C  
ANISOU  856  CD  PRO A 106     1985   2758   2045   -148    537    375       C  
ATOM    857  N   GLU A 107      24.996  13.150   7.355  1.00 16.27           N  
ANISOU  857  N   GLU A 107     2143   2166   1873    -61    440    294       N  
ATOM    858  CA  GLU A 107      23.585  13.528   7.438  1.00 20.29           C  
ANISOU  858  CA  GLU A 107     2285   2702   2721    114    364    593       C  
ATOM    859  C   GLU A 107      22.818  12.755   8.507  1.00 19.09           C  
ANISOU  859  C   GLU A 107     2405   2365   2485    260    444    459       C  
ATOM    860  O   GLU A 107      21.966  13.378   9.210  1.00 22.24           O  
ANISOU  860  O   GLU A 107     2840   2783   2828    230    541     53       O  
ATOM    861  CB AGLU A 107      22.966  13.308   6.048  0.63 29.54           C  
ANISOU  861  CB AGLU A 107     3615   4213   3397    240   -288     13       C  
ATOM    862  CG AGLU A 107      23.642  14.057   4.906  0.63 39.99           C  
ANISOU  862  CG AGLU A 107     5045   5828   4322    -41    309    533       C  
ATOM    863  CD AGLU A 107      23.322  15.534   4.884  0.63 46.85           C  
ANISOU  863  CD AGLU A 107     6463   6067   5271    283    158    396       C  
ATOM    864  OE1AGLU A 107      22.134  15.887   5.024  0.63 48.24           O  
ANISOU  864  OE1AGLU A 107     6431   6352   5546    156    258    487       O  
ATOM    865  OE2AGLU A 107      24.262  16.348   4.720  0.63 49.11           O  
ANISOU  865  OE2AGLU A 107     6490   6511   5660    182    283    453       O  
ATOM    866  CB BGLU A 107      22.951  13.296   6.057  0.37 24.72           C  
ANISOU  866  CB BGLU A 107     2933   3339   3120    178    -43    201       C  
ATOM    867  CG BGLU A 107      23.635  14.004   4.895  0.37 30.38           C  
ANISOU  867  CG BGLU A 107     3729   4277   3536    134    212    521       C  
ATOM    868  CD BGLU A 107      23.839  15.481   5.149  0.37 34.52           C  
ANISOU  868  CD BGLU A 107     4567   4410   4141    157      6    329       C  
ATOM    869  OE1BGLU A 107      22.970  16.106   5.797  0.37 34.83           O  
ANISOU  869  OE1BGLU A 107     4502   4566   4164     96    163    459       O  
ATOM    870  OE2BGLU A 107      24.878  16.018   4.702  0.37 35.73           O  
ANISOU  870  OE2BGLU A 107     4611   4688   4277    190    129    396       O  
ATOM    871  N   GLY A 108      23.180  11.549   8.815  1.00 14.50           N  
ANISOU  871  N   GLY A 108     1992   1838   1678    -99    743    135       N  
ATOM    872  CA  GLY A 108      22.364  10.700   9.682  1.00 14.44           C  
ANISOU  872  CA  GLY A 108     2188   1589   1708   -117    845     60       C  
ATOM    873  C   GLY A 108      22.311  11.146  11.117  1.00 11.52           C  
ANISOU  873  C   GLY A 108     1453   1302   1621     48    334     73       C  
ATOM    874  O   GLY A 108      23.278  11.653  11.644  1.00 14.00           O  
ANISOU  874  O   GLY A 108     1446   2074   1800   -118    266    269       O  
ATOM    875  N   ASN A 109      21.179  10.870  11.797  1.00  9.94           N  
ANISOU  875  N   ASN A 109     1399   1120   1258     39    294    121       N  
ATOM    876  CA  ASN A 109      21.042  11.158  13.220  1.00  9.14           C  
ANISOU  876  CA  ASN A 109     1281    999   1191    -10     78    114       C  
ATOM    877  C   ASN A 109      20.407  10.011  14.007  1.00  8.21           C  
ANISOU  877  C   ASN A 109      966   1122   1030    -53    -12    105       C  
ATOM    878  O   ASN A 109      20.383  10.105  15.266  1.00  8.92           O  
ANISOU  878  O   ASN A 109     1170   1130   1091    -42     16     99       O  
ATOM    879  CB  ASN A 109      20.245  12.431  13.518  1.00  8.84           C  
ANISOU  879  CB  ASN A 109     1083    964   1310    -57     10     92       C  
ATOM    880  CG  ASN A 109      18.748  12.276  13.340  1.00  8.82           C  
ANISOU  880  CG  ASN A 109     1082   1014   1254    -12    -14     60       C  
ATOM    881  OD1 ASN A 109      18.286  11.468  12.529  1.00 11.14           O  
ANISOU  881  OD1 ASN A 109     1194   1374   1665      4    -57   -255       O  
ATOM    882  ND2 ASN A 109      17.983  12.981  14.169  1.00  8.55           N  
ANISOU  882  ND2 ASN A 109     1104   1012   1133    -76     62    129       N  
ATOM    883  N   PHE A 110      19.920   8.956  13.368  1.00  8.58           N  
ANISOU  883  N   PHE A 110     1107   1131   1021   -177     23    175       N  
ATOM    884  CA  PHE A 110      19.199   7.875  14.074  1.00  8.95           C  
ANISOU  884  CA  PHE A 110     1254   1156    992    -93    114    191       C  
ATOM    885  C   PHE A 110      20.212   6.846  14.602  1.00  8.53           C  
ANISOU  885  C   PHE A 110     1128   1060   1054    -68    164     99       C  
ATOM    886  O   PHE A 110      20.409   5.775  14.069  1.00  9.86           O  
ANISOU  886  O   PHE A 110     1308   1183   1255    -88     75     65       O  
ATOM    887  CB  PHE A 110      18.128   7.280  13.146  1.00 10.07           C  
ANISOU  887  CB  PHE A 110     1337   1269   1219   -123     34    117       C  
ATOM    888  CG  PHE A 110      17.128   6.352  13.818  1.00  9.58           C  
ANISOU  888  CG  PHE A 110     1343   1135   1163    -14    -30    242       C  
ATOM    889  CD1 PHE A 110      16.334   6.769  14.877  1.00 13.18           C  
ANISOU  889  CD1 PHE A 110     1435   1525   2047   -138    384    -74       C  
ATOM    890  CD2 PHE A 110      16.931   5.068  13.345  1.00 10.75           C  
ANISOU  890  CD2 PHE A 110     1475   1333   1277   -204     64     71       C  
ATOM    891  CE1 PHE A 110      15.396   5.917  15.440  1.00 14.32           C  
ANISOU  891  CE1 PHE A 110     1648   1537   2257   -162    529    -60       C  
ATOM    892  CE2 PHE A 110      15.999   4.222  13.907  1.00 10.84           C  
ANISOU  892  CE2 PHE A 110     1569   1286   1265   -254    -15    165       C  
ATOM    893  CZ  PHE A 110      15.218   4.644  14.951  1.00 12.63           C  
ANISOU  893  CZ  PHE A 110     1610   1369   1819   -254    236    155       C  
ATOM    894  N   CYS A 111      20.911   7.287  15.675  1.00  8.95           N  
ANISOU  894  N   CYS A 111     1250   1063   1088    -74     -6    105       N  
ATOM    895  CA  CYS A 111      21.995   6.502  16.305  1.00  8.94           C  
ANISOU  895  CA  CYS A 111     1169   1196   1033    -22    166    122       C  
ATOM    896  C   CYS A 111      21.540   5.069  16.548  1.00  9.30           C  
ANISOU  896  C   CYS A 111     1254   1193   1085    -45      2     76       C  
ATOM    897  O   CYS A 111      20.448   4.817  17.068  1.00  9.86           O  
ANISOU  897  O   CYS A 111     1282   1223   1240    -74     30    193       O  
ATOM    898  CB  CYS A 111      22.337   7.167  17.642  1.00  9.29           C  
ANISOU  898  CB  CYS A 111     1021   1242   1269     49     -8    107       C  
ATOM    899  SG  CYS A 111      23.532   6.281  18.691  1.00  8.93           S  
ANISOU  899  SG  CYS A 111     1165   1139   1091     85      2    109       S  
ATOM    900  N   LEU A 112      22.448   4.115  16.258  1.00  9.78           N  
ANISOU  900  N   LEU A 112     1438   1113   1163    -68     21     35       N  
ATOM    901  CA  LEU A 112      22.131   2.687  16.412  1.00 10.46           C  
ANISOU  901  CA  LEU A 112     1485   1209   1279    -43     33     59       C  
ATOM    902  C   LEU A 112      21.924   2.260  17.858  1.00 10.33           C  
ANISOU  902  C   LEU A 112     1540   1091   1295     36     71    112       C  
ATOM    903  O   LEU A 112      21.433   1.127  18.048  1.00 12.52           O  
ANISOU  903  O   LEU A 112     2007   1291   1457    -35    -57    238       O  
ATOM    904  CB  LEU A 112      23.201   1.875  15.672  1.00 13.18           C  
ANISOU  904  CB  LEU A 112     2056   1458   1496    181    258    -46       C  
ATOM    905  CG  LEU A 112      23.094   2.025  14.123  1.00 15.07           C  
ANISOU  905  CG  LEU A 112     2681   1459   1587      6    359    -95       C  
ATOM    906  CD1 LEU A 112      24.359   1.593  13.421  1.00 19.47           C  
ANISOU  906  CD1 LEU A 112     2574   2642   2182   -140    450   -239       C  
ATOM    907  CD2 LEU A 112      21.884   1.311  13.558  1.00 17.13           C  
ANISOU  907  CD2 LEU A 112     2459   2271   1780    390    -28   -153       C  
ATOM    908  N   LYS A 113      22.253   3.073  18.858  1.00  9.88           N  
ANISOU  908  N   LYS A 113     1311   1301   1141     13     27    208       N  
ATOM    909  CA  LYS A 113      21.944   2.738  20.264  1.00 10.55           C  
ANISOU  909  CA  LYS A 113     1356   1442   1209    -21     45    268       C  
ATOM    910  C   LYS A 113      20.527   3.135  20.677  1.00  9.37           C  
ANISOU  910  C   LYS A 113     1346   1106   1109    -87     31    177       C  
ATOM    911  O   LYS A 113      20.166   2.960  21.842  1.00 10.83           O  
ANISOU  911  O   LYS A 113     1463   1467   1183     84    116    323       O  
ATOM    912  CB ALYS A 113      22.940   3.484  21.192  0.56 10.01           C  
ANISOU  912  CB ALYS A 113     1127   1610   1066    132     -6    305       C  
ATOM    913  CG ALYS A 113      24.413   3.277  20.899  0.56 10.93           C  
ANISOU  913  CG ALYS A 113     1065   1794   1294     78   -174    413       C  
ATOM    914  CD ALYS A 113      24.798   1.807  20.945  0.56 14.43           C  
ANISOU  914  CD ALYS A 113     1691   1857   1937    194     73    186       C  
ATOM    915  CE ALYS A 113      26.320   1.711  20.816  0.56 17.74           C  
ANISOU  915  CE ALYS A 113     1786   2350   2604    406     59    306       C  
ATOM    916  NZ ALYS A 113      26.772   0.296  20.778  0.56 20.61           N  
ANISOU  916  NZ ALYS A 113     2313   2379   3138    488     16    287       N  
ATOM    917  CB BLYS A 113      23.056   3.308  21.167  0.44 15.66           C  
ANISOU  917  CB BLYS A 113     1829   2386   1735   -247   -194    109       C  
ATOM    918  CG BLYS A 113      24.389   2.563  20.924  0.44 21.15           C  
ANISOU  918  CG BLYS A 113     2256   3265   2515    150     32     -3       C  
ATOM    919  CD BLYS A 113      24.371   1.287  21.745  0.44 26.52           C  
ANISOU  919  CD BLYS A 113     3332   3665   3080    -22     65    365       C  
ATOM    920  CE BLYS A 113      25.287   0.183  21.263  0.44 30.80           C  
ANISOU  920  CE BLYS A 113     3838   4232   3635    282    245    129       C  
ATOM    921  NZ BLYS A 113      24.623  -1.154  21.437  0.44 31.81           N  
ANISOU  921  NZ BLYS A 113     4065   4248   3773    288    332    193       N  
ATOM    922  N   ASN A 114      19.701   3.627  19.763  1.00  9.26           N  
ANISOU  922  N   ASN A 114     1274   1081   1162    -80     54    154       N  
ATOM    923  CA  ASN A 114      18.336   4.055  20.099  1.00  9.40           C  
ANISOU  923  CA  ASN A 114     1248   1091   1233    -25     74    216       C  
ATOM    924  C   ASN A 114      17.476   2.915  20.660  1.00  8.95           C  
ANISOU  924  C   ASN A 114     1322    899   1178     -3     68    124       C  
ATOM    925  O   ASN A 114      17.683   1.738  20.350  1.00 10.41           O  
ANISOU  925  O   ASN A 114     1491   1021   1445    -29    173    128       O  
ATOM    926  CB  ASN A 114      17.664   4.632  18.826  1.00  9.81           C  
ANISOU  926  CB  ASN A 114     1405   1076   1245     -4     95    186       C  
ATOM    927  CG  ASN A 114      17.198   3.578  17.845  1.00  9.49           C  
ANISOU  927  CG  ASN A 114     1290   1107   1207   -157     80    300       C  
ATOM    928  OD1 ASN A 114      16.146   2.955  18.041  1.00 11.27           O  
ANISOU  928  OD1 ASN A 114     1433   1405   1443   -270     91    149       O  
ATOM    929  ND2 ASN A 114      17.970   3.388  16.768  1.00 11.02           N  
ANISOU  929  ND2 ASN A 114     1369   1577   1243   -155      5    177       N  
ATOM    930  N   ASP A 115      16.479   3.300  21.460  1.00  9.39           N  
ANISOU  930  N   ASP A 115     1290    986   1290    -29    138    173       N  
ATOM    931  CA  ASP A 115      15.443   2.396  21.958  1.00  9.89           C  
ANISOU  931  CA  ASP A 115     1312   1181   1264   -152    128    204       C  
ATOM    932  C   ASP A 115      14.093   2.645  21.258  1.00 11.26           C  
ANISOU  932  C   ASP A 115     1322   1666   1288   -171    124    160       C  
ATOM    933  O   ASP A 115      13.019   2.411  21.846  1.00 15.47           O  
ANISOU  933  O   ASP A 115     1491   2726   1660   -283    152    260       O  
ATOM    934  CB  ASP A 115      15.264   2.474  23.481  1.00  9.98           C  
ANISOU  934  CB  ASP A 115     1445   1006   1339   -161    198     90       C  
ATOM    935  CG  ASP A 115      14.467   1.314  24.067  1.00 10.34           C  
ANISOU  935  CG  ASP A 115     1475   1104   1351   -149    219    -25       C  
ATOM    936  OD1 ASP A 115      14.741   0.179  23.627  1.00 11.82           O  
ANISOU  936  OD1 ASP A 115     1845   1124   1522   -252    373     32       O  
ATOM    937  OD2 ASP A 115      13.629   1.534  24.985  1.00 12.24           O  
ANISOU  937  OD2 ASP A 115     1891   1378   1381   -228    336    -36       O  
ATOM    938  N   LEU A 116      14.153   3.131  20.011  1.00 10.28           N  
ANISOU  938  N   LEU A 116     1242   1318   1345   -134     29    108       N  
ATOM    939  CA  LEU A 116      12.960   3.479  19.251  1.00 13.25           C  
ANISOU  939  CA  LEU A 116     1503   1941   1592      2    -75     -2       C  
ATOM    940  C   LEU A 116      12.506   2.389  18.288  1.00 16.38           C  
ANISOU  940  C   LEU A 116     1825   2405   1994   -187     15   -333       C  
ATOM    941  O   LEU A 116      11.283   2.135  18.182  1.00 20.67           O  
ANISOU  941  O   LEU A 116     1889   3353   2612   -388    -18   -639       O  
ATOM    942  CB  LEU A 116      13.212   4.782  18.465  1.00 14.01           C  
ANISOU  942  CB  LEU A 116     2086   1988   1248    122   -198    -73       C  
ATOM    943  CG  LEU A 116      13.003   6.082  19.258  1.00 15.83           C  
ANISOU  943  CG  LEU A 116     2764   1753   1498     76    -68    142       C  
ATOM    944  CD1 LEU A 116      13.961   6.225  20.403  1.00 17.10           C  
ANISOU  944  CD1 LEU A 116     2530   1747   2219   -305   -274   -121       C  
ATOM    945  CD2 LEU A 116      13.060   7.295  18.338  1.00 17.32           C  
ANISOU  945  CD2 LEU A 116     2877   1873   1830    195    172    319       C  
ATOM    946  N   SER A 117      13.415   1.840  17.501  1.00 16.10           N  
ANISOU  946  N   SER A 117     2075   2082   1960   -241     42   -403       N  
ATOM    947  CA  SER A 117      13.041   0.858  16.491  1.00 20.10           C  
ANISOU  947  CA  SER A 117     2779   2773   2084   -312    137   -634       C  
ATOM    948  C   SER A 117      12.479  -0.418  17.057  1.00 25.57           C  
ANISOU  948  C   SER A 117     3640   3435   2638   -420    284    -25       C  
ATOM    949  O   SER A 117      11.552  -0.963  16.410  1.00 30.73           O  
ANISOU  949  O   SER A 117     4390   4426   2860   -853    -50   -261       O  
ATOM    950  CB ASER A 117      14.293   0.410  15.719  0.41 17.32           C  
ANISOU  950  CB ASER A 117     2575   2177   1831   -247    -35   -348       C  
ATOM    951  OG ASER A 117      14.708   1.418  14.845  0.41 16.73           O  
ANISOU  951  OG ASER A 117     2656   2103   1598   -230    -60   -394       O  
ATOM    952  CB BSER A 117      14.194   0.637  15.511  0.41 16.42           C  
ANISOU  952  CB BSER A 117     2310   2114   1816   -168   -180   -424       C  
ATOM    953  OG BSER A 117      15.379   0.160  16.109  0.41 14.57           O  
ANISOU  953  OG BSER A 117     2364   1707   1466   -240     14    -53       O  
ATOM    954  N   MET A 118      13.074  -0.972  18.094  1.00 25.49           N  
ANISOU  954  N   MET A 118     4134   3710   1839   -111    453   -348       N  
ATOM    955  CA  MET A 118      12.551  -2.243  18.668  1.00 30.56           C  
ANISOU  955  CA  MET A 118     4332   4472   2807   -660    284     95       C  
ATOM    956  C   MET A 118      12.710  -2.156  20.213  1.00 24.43           C  
ANISOU  956  C   MET A 118     3293   3389   2602   -416    359    126       C  
ATOM    957  O   MET A 118      13.669  -2.568  20.847  1.00 23.71           O  
ANISOU  957  O   MET A 118     3573   3461   1975   -385    449    -80       O  
ATOM    958  CB  MET A 118      13.317  -3.445  18.163  1.00 41.72           C  
ANISOU  958  CB  MET A 118     5463   5243   5146    197    656    162       C  
ATOM    959  CG  MET A 118      12.995  -3.876  16.730  1.00 52.54           C  
ANISOU  959  CG  MET A 118     6987   7510   5464    -37    205    117       C  
ATOM    960  SD  MET A 118      13.856  -5.401  16.301  1.00 59.64           S  
ANISOU  960  SD  MET A 118     7963   8122   6574    492    157   -362       S  
ATOM    961  CE  MET A 118      13.085  -6.545  17.442  1.00 62.97           C  
ANISOU  961  CE  MET A 118     8252   8539   7135    469    253      3       C  
ATOM    962  N   PRO A 119      11.729  -1.537  20.787  1.00 20.95           N  
ANISOU  962  N   PRO A 119     2804   3117   2038   -686   -143    -94       N  
ATOM    963  CA  PRO A 119      11.879  -1.056  22.174  1.00 20.08           C  
ANISOU  963  CA  PRO A 119     2668   3177   1784   -528    -82     72       C  
ATOM    964  C   PRO A 119      11.979  -2.109  23.220  1.00 20.42           C  
ANISOU  964  C   PRO A 119     2972   2986   1800   -725    205     30       C  
ATOM    965  O   PRO A 119      11.174  -3.060  23.262  1.00 24.83           O  
ANISOU  965  O   PRO A 119     3639   3498   2295  -1357    161    -85       O  
ATOM    966  CB  PRO A 119      10.708  -0.083  22.397  1.00 22.34           C  
ANISOU  966  CB  PRO A 119     2925   3430   2134   -260     29    186       C  
ATOM    967  CG  PRO A 119       9.690  -0.717  21.474  1.00 23.76           C  
ANISOU  967  CG  PRO A 119     2803   3322   2904   -365    111    -24       C  
ATOM    968  CD  PRO A 119      10.506  -1.008  20.217  1.00 23.72           C  
ANISOU  968  CD  PRO A 119     2967   3668   2377   -316     28    333       C  
ATOM    969  N   ARG A 120      12.964  -1.924  24.096  1.00 16.53           N  
ANISOU  969  N   ARG A 120     2744   1895   1641   -719    315     -3       N  
ATOM    970  CA  ARG A 120      13.155  -2.778  25.254  1.00 15.61           C  
ANISOU  970  CA  ARG A 120     2573   1653   1704   -502    300    -55       C  
ATOM    971  C   ARG A 120      12.602  -2.075  26.506  1.00 13.31           C  
ANISOU  971  C   ARG A 120     2119   1471   1469   -326    176     52       C  
ATOM    972  O   ARG A 120      12.309  -2.745  27.510  1.00 13.06           O  
ANISOU  972  O   ARG A 120     2104   1273   1584   -336    305     47       O  
ATOM    973  CB  ARG A 120      14.640  -3.091  25.458  1.00 18.95           C  
ANISOU  973  CB  ARG A 120     2801   2056   2342     11    308    -30       C  
ATOM    974  CG  ARG A 120      15.469  -3.893  24.472  1.00 20.73           C  
ANISOU  974  CG  ARG A 120     2895   2502   2482    198    218    -98       C  
ATOM    975  CD  ARG A 120      16.898  -4.129  24.945  1.00 22.78           C  
ANISOU  975  CD  ARG A 120     2964   2850   2843    143     58     85       C  
ATOM    976  NE  ARG A 120      17.805  -2.977  24.840  1.00 22.33           N  
ANISOU  976  NE  ARG A 120     2872   2975   2638    117    247     78       N  
ATOM    977  CZ  ARG A 120      19.028  -2.914  25.367  1.00 24.29           C  
ANISOU  977  CZ  ARG A 120     2960   3404   2865    326    225    -94       C  
ATOM    978  NH1 ARG A 120      19.507  -3.970  26.031  1.00 26.76           N  
ANISOU  978  NH1 ARG A 120     3501   3964   2701    565    273    149       N  
ATOM    979  NH2 ARG A 120      19.798  -1.849  25.242  1.00 25.41           N  
ANISOU  979  NH2 ARG A 120     3174   3373   3109    259    -33   -245       N  
ATOM    980  N   GLY A 121      12.567  -0.717  26.584  1.00 11.55           N  
ANISOU  980  N   GLY A 121     1753   1390   1246   -267    165     64       N  
ATOM    981  CA  GLY A 121      12.166  -0.046  27.821  1.00 11.23           C  
ANISOU  981  CA  GLY A 121     1619   1324   1323    -92    112    157       C  
ATOM    982  C   GLY A 121      13.177  -0.219  28.946  1.00 10.40           C  
ANISOU  982  C   GLY A 121     1512   1099   1340    -14    219    183       C  
ATOM    983  O   GLY A 121      12.787  -0.360  30.120  1.00 11.14           O  
ANISOU  983  O   GLY A 121     1847   1102   1285     81    287    210       O  
ATOM    984  N   THR A 122      14.456  -0.183  28.628  1.00  9.97           N  
ANISOU  984  N   THR A 122     1513   1000   1275     -2    135    194       N  
ATOM    985  CA  THR A 122      15.519  -0.329  29.586  1.00 10.64           C  
ANISOU  985  CA  THR A 122     1593   1092   1359    -30     -6    151       C  
ATOM    986  C   THR A 122      16.583   0.749  29.369  1.00 10.23           C  
ANISOU  986  C   THR A 122     1569   1022   1298     19    -38    191       C  
ATOM    987  O   THR A 122      16.534   1.530  28.398  1.00 11.14           O  
ANISOU  987  O   THR A 122     1687   1222   1323    -40     49    260       O  
ATOM    988  CB  THR A 122      16.214  -1.702  29.437  1.00 12.18           C  
ANISOU  988  CB  THR A 122     1826   1134   1669     11     -6    110       C  
ATOM    989  OG1 THR A 122      16.879  -1.808  28.168  1.00 14.23           O  
ANISOU  989  OG1 THR A 122     2132   1227   2048    129    305   -122       O  
ATOM    990  CG2 THR A 122      15.245  -2.860  29.600  1.00 14.06           C  
ANISOU  990  CG2 THR A 122     2179   1133   2028    -63     10    316       C  
ATOM    991  N   MET A 123      17.587   0.791  30.248  1.00 10.79           N  
ANISOU  991  N   MET A 123     1541   1155   1402    -76     -9    153       N  
ATOM    992  CA  MET A 123      18.849   1.474  30.087  1.00 11.22           C  
ANISOU  992  CA  MET A 123     1578   1261   1423    -54      6    168       C  
ATOM    993  C   MET A 123      19.650   0.778  28.985  1.00 11.69           C  
ANISOU  993  C   MET A 123     1691   1345   1405     24    -82    108       C  
ATOM    994  O   MET A 123      19.321  -0.360  28.566  1.00 12.48           O  
ANISOU  994  O   MET A 123     1818   1357   1565     57     67     50       O  
ATOM    995  CB  MET A 123      19.659   1.470  31.393  1.00 11.25           C  
ANISOU  995  CB  MET A 123     1521   1386   1369    -63     73    183       C  
ATOM    996  CG  MET A 123      18.944   2.208  32.519  1.00 13.48           C  
ANISOU  996  CG  MET A 123     1917   1677   1528   -106    127    -66       C  
ATOM    997  SD  MET A 123      18.864   4.018  32.327  1.00 13.34           S  
ANISOU  997  SD  MET A 123     1716   1526   1826    146    -85   -275       S  
ATOM    998  CE  MET A 123      20.570   4.430  32.569  1.00 13.35           C  
ANISOU  998  CE  MET A 123     1981   1659   1432   -105     59    140       C  
ATOM    999  N   GLN A 124      20.792   1.351  28.573  1.00 11.39           N  
ANISOU  999  N   GLN A 124     1529   1421   1376    149    -13     57       N  
ATOM   1000  CA  GLN A 124      21.658   0.681  27.579  1.00 12.03           C  
ANISOU 1000  CA  GLN A 124     1636   1532   1404     78     59     94       C  
ATOM   1001  C   GLN A 124      22.091  -0.697  28.035  1.00 13.06           C  
ANISOU 1001  C   GLN A 124     1911   1536   1515    167    103     53       C  
ATOM   1002  O   GLN A 124      22.223  -1.615  27.179  1.00 15.41           O  
ANISOU 1002  O   GLN A 124     2291   1779   1785    315    146   -120       O  
ATOM   1003  CB  GLN A 124      22.916   1.497  27.261  1.00 12.74           C  
ANISOU 1003  CB  GLN A 124     1804   1642   1397    -27    -27     79       C  
ATOM   1004  CG  GLN A 124      22.638   2.754  26.431  1.00 13.11           C  
ANISOU 1004  CG  GLN A 124     1750   1756   1473     13     -1    177       C  
ATOM   1005  CD  GLN A 124      22.160   2.434  25.031  1.00 13.28           C  
ANISOU 1005  CD  GLN A 124     1871   1767   1407     69     69    114       C  
ATOM   1006  OE1 GLN A 124      22.614   1.495  24.372  1.00 16.67           O  
ANISOU 1006  OE1 GLN A 124     2508   2368   1457    542    -87   -152       O  
ATOM   1007  NE2 GLN A 124      21.203   3.224  24.576  1.00 12.64           N  
ANISOU 1007  NE2 GLN A 124     1624   1894   1285     18     79    152       N  
ATOM   1008  N   ASP A 125      22.282  -0.957  29.329  1.00 12.99           N  
ANISOU 1008  N   ASP A 125     1797   1599   1538    311     10    109       N  
ATOM   1009  CA  ASP A 125      22.708  -2.273  29.810  1.00 13.81           C  
ANISOU 1009  CA  ASP A 125     1840   1551   1856    430      1    -37       C  
ATOM   1010  C   ASP A 125      21.590  -3.303  29.924  1.00 14.45           C  
ANISOU 1010  C   ASP A 125     2134   1596   1761    310    166     38       C  
ATOM   1011  O   ASP A 125      21.875  -4.433  30.417  1.00 17.75           O  
ANISOU 1011  O   ASP A 125     2813   1620   2310    576    111     95       O  
ATOM   1012  CB  ASP A 125      23.487  -2.142  31.121  1.00 15.22           C  
ANISOU 1012  CB  ASP A 125     2042   1828   1913    333    -25     65       C  
ATOM   1013  CG  ASP A 125      22.649  -1.883  32.367  1.00 14.75           C  
ANISOU 1013  CG  ASP A 125     2038   1734   1833    343    -71    -86       C  
ATOM   1014  OD1 ASP A 125      21.415  -1.718  32.257  1.00 14.18           O  
ANISOU 1014  OD1 ASP A 125     2057   1549   1783    324    128     32       O  
ATOM   1015  OD2 ASP A 125      23.228  -1.857  33.498  1.00 17.08           O  
ANISOU 1015  OD2 ASP A 125     2566   2019   1907    430   -150    -37       O  
ATOM   1016  N   GLY A 126      20.374  -3.010  29.508  1.00 14.35           N  
ANISOU 1016  N   GLY A 126     2127   1689   1634    217     87     61       N  
ATOM   1017  CA  GLY A 126      19.279  -3.971  29.518  1.00 14.45           C  
ANISOU 1017  CA  GLY A 126     2235   1436   1819    238    107    -53       C  
ATOM   1018  C   GLY A 126      18.570  -4.121  30.840  1.00 13.35           C  
ANISOU 1018  C   GLY A 126     2046   1315   1712    139    -27     34       C  
ATOM   1019  O   GLY A 126      17.727  -5.015  30.950  1.00 15.40           O  
ANISOU 1019  O   GLY A 126     2677   1497   1676   -191     69    145       O  
ATOM   1020  N   THR A 127      18.802  -3.255  31.800  1.00 13.33           N  
ANISOU 1020  N   THR A 127     2096   1427   1542    248    -31     43       N  
ATOM   1021  CA  THR A 127      18.171  -3.287  33.111  1.00 13.09           C  
ANISOU 1021  CA  THR A 127     2069   1232   1672    181     33    182       C  
ATOM   1022  C   THR A 127      17.411  -1.976  33.363  1.00 11.91           C  
ANISOU 1022  C   THR A 127     2005   1192   1329    120    -64    168       C  
ATOM   1023  O   THR A 127      17.570  -0.988  32.605  1.00 13.21           O  
ANISOU 1023  O   THR A 127     2316   1210   1492    187    183    305       O  
ATOM   1024  CB  THR A 127      19.169  -3.572  34.264  1.00 14.58           C  
ANISOU 1024  CB  THR A 127     2223   1520   1796    290    -87    209       C  
ATOM   1025  OG1 THR A 127      20.028  -2.443  34.452  1.00 15.30           O  
ANISOU 1025  OG1 THR A 127     2305   1735   1773    263   -261     67       O  
ATOM   1026  CG2 THR A 127      19.988  -4.841  34.009  1.00 16.85           C  
ANISOU 1026  CG2 THR A 127     2534   1573   2297    404   -241    179       C  
ATOM   1027  N   SER A 128      16.638  -1.916  34.428  1.00 11.71           N  
ANISOU 1027  N   SER A 128     2009   1058   1382    194     18    233       N  
ATOM   1028  CA  SER A 128      15.864  -0.758  34.825  1.00 11.11           C  
ANISOU 1028  CA  SER A 128     1783   1107   1332     92    107    160       C  
ATOM   1029  C   SER A 128      16.346  -0.164  36.148  1.00 11.38           C  
ANISOU 1029  C   SER A 128     1770   1368   1184    198     20    223       C  
ATOM   1030  O   SER A 128      16.777  -0.924  37.070  1.00 13.51           O  
ANISOU 1030  O   SER A 128     2479   1372   1283    158    -49    332       O  
ATOM   1031  CB  SER A 128      14.390  -1.120  34.986  1.00 13.12           C  
ANISOU 1031  CB  SER A 128     1862   1498   1625    -20     75     70       C  
ATOM   1032  OG  SER A 128      13.698  -0.021  35.587  1.00 15.01           O  
ANISOU 1032  OG  SER A 128     2048   1861   1796     61     20   -176       O  
ATOM   1033  N   ARG A 129      16.284   1.151  36.274  1.00 10.87           N  
ANISOU 1033  N   ARG A 129     1749   1276   1106    182     -9    213       N  
ATOM   1034  CA  ARG A 129      16.615   1.862  37.492  1.00 10.76           C  
ANISOU 1034  CA  ARG A 129     1648   1261   1179      7     -3    209       C  
ATOM   1035  C   ARG A 129      15.393   2.150  38.370  1.00 10.60           C  
ANISOU 1035  C   ARG A 129     1644   1215   1168    112    -76    240       C  
ATOM   1036  O   ARG A 129      15.537   2.791  39.445  1.00 12.32           O  
ANISOU 1036  O   ARG A 129     1931   1575   1174      1    -53    200       O  
ATOM   1037  CB  ARG A 129      17.351   3.176  37.155  1.00 11.32           C  
ANISOU 1037  CB  ARG A 129     1647   1348   1306     18     57    342       C  
ATOM   1038  CG  ARG A 129      18.661   2.968  36.404  1.00 11.87           C  
ANISOU 1038  CG  ARG A 129     1736   1404   1371    -89     37    137       C  
ATOM   1039  CD  ARG A 129      19.828   2.437  37.268  1.00 12.67           C  
ANISOU 1039  CD  ARG A 129     1597   1655   1563     30     17     -8       C  
ATOM   1040  NE  ARG A 129      20.874   1.944  36.353  1.00 13.63           N  
ANISOU 1040  NE  ARG A 129     1860   1562   1758     12    168    -76       N  
ATOM   1041  CZ  ARG A 129      20.780   0.761  35.747  1.00 14.47           C  
ANISOU 1041  CZ  ARG A 129     1967   1575   1956    -52    292   -211       C  
ATOM   1042  NH1 ARG A 129      19.848  -0.139  36.084  1.00 15.88           N  
ANISOU 1042  NH1 ARG A 129     2235   1663   2138   -135    436    -89       N  
ATOM   1043  NH2 ARG A 129      21.668   0.475  34.803  1.00 15.96           N  
ANISOU 1043  NH2 ARG A 129     2313   1629   2122     30    427   -282       N  
ATOM   1044  N   PHE A 130      14.187   1.727  37.967  1.00 10.73           N  
ANISOU 1044  N   PHE A 130     1662   1228   1187     14     -2    339       N  
ATOM   1045  CA  PHE A 130      12.955   2.063  38.663  1.00 10.97           C  
ANISOU 1045  CA  PHE A 130     1744   1237   1185    -52     55    274       C  
ATOM   1046  C   PHE A 130      12.238   0.858  39.269  1.00 11.29           C  
ANISOU 1046  C   PHE A 130     1903   1202   1186      6    123    327       C  
ATOM   1047  O   PHE A 130      12.089  -0.175  38.587  1.00 12.37           O  
ANISOU 1047  O   PHE A 130     2199   1210   1291    -74    185    309       O  
ATOM   1048  CB  PHE A 130      11.954   2.698  37.647  1.00 11.74           C  
ANISOU 1048  CB  PHE A 130     1871   1347   1242   -138     14    470       C  
ATOM   1049  CG  PHE A 130      12.351   3.998  37.003  1.00 11.62           C  
ANISOU 1049  CG  PHE A 130     1903   1280   1231   -188     11    335       C  
ATOM   1050  CD1 PHE A 130      12.597   5.109  37.767  1.00 13.52           C  
ANISOU 1050  CD1 PHE A 130     2443   1450   1244   -256   -253    390       C  
ATOM   1051  CD2 PHE A 130      12.493   4.096  35.625  1.00 11.55           C  
ANISOU 1051  CD2 PHE A 130     1830   1320   1239    -13    -11    364       C  
ATOM   1052  CE1 PHE A 130      12.916   6.328  37.166  1.00 14.08           C  
ANISOU 1052  CE1 PHE A 130     2531   1372   1447   -217   -338    351       C  
ATOM   1053  CE2 PHE A 130      12.782   5.309  35.027  1.00 12.35           C  
ANISOU 1053  CE2 PHE A 130     1932   1398   1364     29     65    491       C  
ATOM   1054  CZ  PHE A 130      13.003   6.404  35.787  1.00 13.61           C  
ANISOU 1054  CZ  PHE A 130     2156   1574   1440   -300   -223    471       C  
ATOM   1055  N   THR A 131      11.707   1.018  40.482  1.00 11.74           N  
ANISOU 1055  N   THR A 131     2057   1118   1285     -5    208    335       N  
ATOM   1056  CA  THR A 131      10.807   0.038  41.092  1.00 12.62           C  
ANISOU 1056  CA  THR A 131     2069   1211   1513    -42    256    456       C  
ATOM   1057  C   THR A 131       9.601   0.770  41.673  1.00 12.62           C  
ANISOU 1057  C   THR A 131     2043   1429   1324   -106    241    175       C  
ATOM   1058  O   THR A 131       9.715   1.924  42.113  1.00 14.18           O  
ANISOU 1058  O   THR A 131     2357   1365   1667    -77    312     73       O  
ATOM   1059  CB ATHR A 131      11.620  -0.571  42.283  0.58 13.89           C  
ANISOU 1059  CB ATHR A 131     2109   1471   1697    -25     55    382       C  
ATOM   1060  OG1ATHR A 131      12.925  -1.027  41.888  0.58 14.45           O  
ANISOU 1060  OG1ATHR A 131     2180   1562   1749     50     24    437       O  
ATOM   1061  CG2ATHR A 131      10.922  -1.774  42.916  0.58 15.78           C  
ANISOU 1061  CG2ATHR A 131     2357   1719   1921    -76    253    559       C  
ATOM   1062  CB BTHR A 131      11.309  -0.987  42.085  0.42 12.85           C  
ANISOU 1062  CB BTHR A 131     2167   1307   1408    103     95    306       C  
ATOM   1063  OG1BTHR A 131      11.739  -0.194  43.188  0.42 14.40           O  
ANISOU 1063  OG1BTHR A 131     2762   1378   1332    283   -309    345       O  
ATOM   1064  CG2BTHR A 131      12.376  -1.874  41.510  0.42 11.92           C  
ANISOU 1064  CG2BTHR A 131     2035   1040   1453     19    -34    222       C  
ATOM   1065  N   CYS A 132       8.426   0.134  41.659  1.00 12.41           N  
ANISOU 1065  N   CYS A 132     2109   1325   1283    -87    243    229       N  
ATOM   1066  CA  CYS A 132       7.198   0.737  42.192  1.00 12.55           C  
ANISOU 1066  CA  CYS A 132     2208   1303   1257   -113    329    405       C  
ATOM   1067  C   CYS A 132       6.371  -0.405  42.779  1.00 12.71           C  
ANISOU 1067  C   CYS A 132     2140   1479   1211   -110    386    340       C  
ATOM   1068  O   CYS A 132       6.152  -1.406  42.092  1.00 13.32           O  
ANISOU 1068  O   CYS A 132     2442   1436   1184   -247    391    402       O  
ATOM   1069  CB  CYS A 132       6.415   1.479  41.119  1.00 13.08           C  
ANISOU 1069  CB  CYS A 132     2141   1514   1315   -240    138    370       C  
ATOM   1070  SG  CYS A 132       4.930   2.315  41.742  1.00 12.41           S  
ANISOU 1070  SG  CYS A 132     2084   1458   1175   -236    229    400       S  
ATOM   1071  N   ARG A 133       5.965  -0.298  44.049  1.00 13.43           N  
ANISOU 1071  N   ARG A 133     2414   1512   1176   -194    338    418       N  
ATOM   1072  CA  ARG A 133       5.232  -1.388  44.723  1.00 13.14           C  
ANISOU 1072  CA  ARG A 133     2068   1589   1337   -140    410    440       C  
ATOM   1073  C   ARG A 133       6.067  -2.646  44.734  1.00 14.27           C  
ANISOU 1073  C   ARG A 133     2281   1691   1452    -93    185    481       C  
ATOM   1074  O   ARG A 133       5.517  -3.767  44.823  1.00 17.17           O  
ANISOU 1074  O   ARG A 133     2899   1700   1927   -119    464    551       O  
ATOM   1075  CB  ARG A 133       3.864  -1.616  44.114  1.00 13.01           C  
ANISOU 1075  CB  ARG A 133     1996   1437   1510   -235    587    355       C  
ATOM   1076  CG  ARG A 133       2.984  -0.401  43.963  1.00 13.85           C  
ANISOU 1076  CG  ARG A 133     2125   1767   1371    -74    419    450       C  
ATOM   1077  CD  ARG A 133       1.631  -0.710  43.397  1.00 13.67           C  
ANISOU 1077  CD  ARG A 133     2133   1829   1233    -94    387    428       C  
ATOM   1078  NE  ARG A 133       0.813   0.430  43.075  1.00 13.90           N  
ANISOU 1078  NE  ARG A 133     2258   1704   1320    -88    388    385       N  
ATOM   1079  CZ  ARG A 133      -0.455   0.405  42.724  1.00 15.48           C  
ANISOU 1079  CZ  ARG A 133     2233   2138   1509    -82    404    209       C  
ATOM   1080  NH1 ARG A 133      -1.184  -0.710  42.792  1.00 16.85           N  
ANISOU 1080  NH1 ARG A 133     2277   2233   1894   -153    175     41       N  
ATOM   1081  NH2 ARG A 133      -1.051   1.528  42.327  1.00 17.09           N  
ANISOU 1081  NH2 ARG A 133     2391   2243   1859    -51    303    422       N  
ATOM   1082  N   GLY A 134       7.383  -2.563  44.725  1.00 14.46           N  
ANISOU 1082  N   GLY A 134     2329   1801   1364      4    217    492       N  
ATOM   1083  CA  GLY A 134       8.295  -3.687  44.697  1.00 16.12           C  
ANISOU 1083  CA  GLY A 134     2548   1996   1580    190    212    396       C  
ATOM   1084  C   GLY A 134       8.476  -4.288  43.299  1.00 16.78           C  
ANISOU 1084  C   GLY A 134     2756   1899   1721    147    200    318       C  
ATOM   1085  O   GLY A 134       9.224  -5.270  43.222  1.00 21.07           O  
ANISOU 1085  O   GLY A 134     3359   2311   2335    532    442    251       O  
ATOM   1086  N   LYS A 135       7.858  -3.770  42.260  1.00 16.16           N  
ANISOU 1086  N   LYS A 135     2961   1778   1402   -135    464    563       N  
ATOM   1087  CA  LYS A 135       7.953  -4.307  40.913  1.00 18.21           C  
ANISOU 1087  CA  LYS A 135     3390   1930   1599   -124    768    403       C  
ATOM   1088  C   LYS A 135       8.788  -3.368  40.025  1.00 14.82           C  
ANISOU 1088  C   LYS A 135     2644   1515   1473   -156    372    287       C  
ATOM   1089  O   LYS A 135       8.760  -2.204  40.074  1.00 14.58           O  
ANISOU 1089  O   LYS A 135     2722   1329   1490   -231    423    239       O  
ATOM   1090  CB  LYS A 135       6.543  -4.315  40.288  1.00 31.70           C  
ANISOU 1090  CB  LYS A 135     4336   4292   3417    366   -382     10       C  
ATOM   1091  CG  LYS A 135       5.490  -5.120  41.038  1.00 50.30           C  
ANISOU 1091  CG  LYS A 135     6071   7584   5458   -645    678    632       C  
ATOM   1092  CD  LYS A 135       5.913  -6.569  41.188  1.00 64.70           C  
ANISOU 1092  CD  LYS A 135     8086   8281   8215     24    378   1125       C  
ATOM   1093  CE  LYS A 135       6.107  -7.280  39.859  1.00 75.10           C  
ANISOU 1093  CE  LYS A 135     9743  10267   8523   -398    718    599       C  
ATOM   1094  NZ  LYS A 135       7.073  -8.410  39.974  1.00 80.28           N  
ANISOU 1094  NZ  LYS A 135    10349  10712   9441     -8    732    803       N  
ATOM   1095  N  APRO A 136       9.798  -4.001  39.268  0.54 12.81           N  
ANISOU 1095  N  APRO A 136     2443    916   1508   -146    152    508       N  
ATOM   1096  CA APRO A 136      10.593  -3.187  38.308  0.54 12.16           C  
ANISOU 1096  CA APRO A 136     2003   1142   1476   -166    103    323       C  
ATOM   1097  C  APRO A 136       9.693  -2.528  37.270  0.54 12.59           C  
ANISOU 1097  C  APRO A 136     2149   1289   1347   -261     66    324       C  
ATOM   1098  O  APRO A 136       8.735  -3.142  36.797  0.54 14.51           O  
ANISOU 1098  O  APRO A 136     2214   1544   1755   -315    -55    412       O  
ATOM   1099  CB APRO A 136      11.601  -4.149  37.658  0.54 13.83           C  
ANISOU 1099  CB APRO A 136     2079   1504   1671      2     21    194       C  
ATOM   1100  CG APRO A 136      11.478  -5.428  38.425  0.54 15.88           C  
ANISOU 1100  CG APRO A 136     2225   1678   2131    -41     84    368       C  
ATOM   1101  CD APRO A 136      10.159  -5.507  39.108  0.54 13.63           C  
ANISOU 1101  CD APRO A 136     2275   1109   1794   -153     58    250       C  
ATOM   1102  N  BPRO A 136       9.384  -4.131  39.007  0.46 13.62           N  
ANISOU 1102  N  BPRO A 136     2496   1289   1392   -185    162    304       N  
ATOM   1103  CA BPRO A 136      10.216  -3.371  38.050  0.46 11.99           C  
ANISOU 1103  CA BPRO A 136     2113   1169   1272    -40     51    181       C  
ATOM   1104  C  BPRO A 136       9.348  -2.574  37.106  0.46 10.82           C  
ANISOU 1104  C  BPRO A 136     1920   1169   1023   -345     13    189       C  
ATOM   1105  O  BPRO A 136       8.301  -3.054  36.651  0.46 11.21           O  
ANISOU 1105  O  BPRO A 136     1833   1139   1287   -257     45    386       O  
ATOM   1106  CB BPRO A 136      11.108  -4.365  37.306  0.46 12.86           C  
ANISOU 1106  CB BPRO A 136     2258   1260   1367     73    -37     93       C  
ATOM   1107  CG BPRO A 136      10.415  -5.663  37.499  0.46 14.90           C  
ANISOU 1107  CG BPRO A 136     2565   1510   1587   -168     83     94       C  
ATOM   1108  CD BPRO A 136       9.488  -5.635  38.667  0.46 13.97           C  
ANISOU 1108  CD BPRO A 136     2403   1369   1536   -135     -4    239       C  
ATOM   1109  CA  ILE A 137       9.061  -0.487  35.916  1.00 11.28           C  
ANISOU 1109  CA  ILE A 137     1901   1318   1067    -74    143    337       C  
ATOM   1110  C   ILE A 137       9.920  -0.146  34.690  1.00 10.30           C  
ANISOU 1110  C   ILE A 137     1642   1153   1120   -255     87    351       C  
ATOM   1111  O   ILE A 137      11.124   0.157  34.860  1.00 11.72           O  
ANISOU 1111  O   ILE A 137     1679   1591   1182   -151    128    365       O  
ATOM   1112  CB  ILE A 137       8.549   0.822  36.583  1.00 11.56           C  
ANISOU 1112  CB  ILE A 137     1856   1313   1225   -112    237    369       C  
ATOM   1113  CG1 ILE A 137       7.816   0.528  37.925  1.00 12.97           C  
ANISOU 1113  CG1 ILE A 137     2130   1613   1185   -229    195    436       C  
ATOM   1114  CG2 ILE A 137       7.658   1.634  35.626  1.00 12.06           C  
ANISOU 1114  CG2 ILE A 137     1837   1516   1231   -119    103    298       C  
ATOM   1115  CD1 ILE A 137       6.556  -0.335  37.739  1.00 14.66           C  
ANISOU 1115  CD1 ILE A 137     2181   1908   1482   -361    414    348       C  
ATOM   1116  N  AILE A 137       9.887  -1.264  36.873  0.54 12.57           N  
ANISOU 1116  N  AILE A 137     2210   1267   1300   -137    151    523       N  
ATOM   1117  N  BILE A 137       9.806  -1.356  36.803  0.46 11.49           N  
ANISOU 1117  N  BILE A 137     2052   1098   1214   -156    161    418       N  
ATOM   1118  N   HIS A 138       9.392  -0.206  33.463  1.00 10.19           N  
ANISOU 1118  N   HIS A 138     1699   1084   1088   -220    122    343       N  
ATOM   1119  CA  HIS A 138      10.183   0.113  32.281  1.00  9.65           C  
ANISOU 1119  CA  HIS A 138     1611    987   1068   -154    188    318       C  
ATOM   1120  C   HIS A 138      10.471   1.626  32.152  1.00  9.20           C  
ANISOU 1120  C   HIS A 138     1418    975   1104    -70     88    299       C  
ATOM   1121  O   HIS A 138       9.683   2.468  32.559  1.00  9.99           O  
ANISOU 1121  O   HIS A 138     1651   1071   1072    -88    155    288       O  
ATOM   1122  CB AHIS A 138       9.336  -0.300  31.027  0.63  9.74           C  
ANISOU 1122  CB AHIS A 138     1700    977   1022   -242    155    309       C  
ATOM   1123  CG AHIS A 138       9.239  -1.792  30.872  0.63 10.34           C  
ANISOU 1123  CG AHIS A 138     1659    995   1275   -115    149    207       C  
ATOM   1124  ND1AHIS A 138       8.116  -2.487  31.313  0.63 13.55           N  
ANISOU 1124  ND1AHIS A 138     1907   1340   1903   -317    196    401       N  
ATOM   1125  CD2AHIS A 138      10.078  -2.697  30.325  0.63 11.30           C  
ANISOU 1125  CD2AHIS A 138     1795   1021   1476     67     22    224       C  
ATOM   1126  CE1AHIS A 138       8.282  -3.769  31.055  0.63 13.42           C  
ANISOU 1126  CE1AHIS A 138     1742   1508   1850     49     75    125       C  
ATOM   1127  NE2AHIS A 138       9.471  -3.977  30.496  0.63 12.37           N  
ANISOU 1127  NE2AHIS A 138     1666   1205   1831     -2     30    224       N  
ATOM   1128  CB BHIS A 138       9.577  -0.366  30.963  0.37  9.35           C  
ANISOU 1128  CB BHIS A 138     1559    803   1191    -49     93    191       C  
ATOM   1129  CG BHIS A 138       9.501  -1.859  30.862  0.37  8.81           C  
ANISOU 1129  CG BHIS A 138     1366    790   1191   -113    244    286       C  
ATOM   1130  ND1BHIS A 138      10.532  -2.608  30.328  0.37  9.71           N  
ANISOU 1130  ND1BHIS A 138     1477    860   1352     -5    229    258       N  
ATOM   1131  CD2BHIS A 138       8.505  -2.709  31.213  0.37 10.09           C  
ANISOU 1131  CD2BHIS A 138     1396    905   1533   -197    207    314       C  
ATOM   1132  CE1BHIS A 138      10.155  -3.892  30.382  0.37  8.99           C  
ANISOU 1132  CE1BHIS A 138     1140    769   1505    168    114    154       C  
ATOM   1133  NE2BHIS A 138       8.932  -3.976  30.900  0.37 10.07           N  
ANISOU 1133  NE2BHIS A 138     1361   1026   1439    -91    408    474       N  
ATOM   1134  N   HIS A 139      11.617   1.884  31.494  1.00  9.39           N  
ANISOU 1134  N   HIS A 139     1431    896   1241   -115    112    382       N  
ATOM   1135  CA  HIS A 139      11.953   3.193  30.971  1.00  8.68           C  
ANISOU 1135  CA  HIS A 139     1462    773   1065   -158    -42    310       C  
ATOM   1136  C   HIS A 139      11.255   3.422  29.620  1.00  8.82           C  
ANISOU 1136  C   HIS A 139     1361    953   1039   -203     39    191       C  
ATOM   1137  O   HIS A 139      10.698   2.492  29.026  1.00  9.55           O  
ANISOU 1137  O   HIS A 139     1519   1027   1084   -260     -5    283       O  
ATOM   1138  CB  HIS A 139      13.480   3.301  30.790  1.00  9.74           C  
ANISOU 1138  CB  HIS A 139     1441   1042   1216   -176    -79    442       C  
ATOM   1139  CG  HIS A 139      14.282   3.222  32.052  1.00  9.65           C  
ANISOU 1139  CG  HIS A 139     1562   1082   1021    -39     -5    247       C  
ATOM   1140  ND1 HIS A 139      15.079   4.252  32.494  1.00 10.22           N  
ANISOU 1140  ND1 HIS A 139     1458   1370   1056   -127   -116    201       N  
ATOM   1141  CD2 HIS A 139      14.479   2.214  32.969  1.00 10.67           C  
ANISOU 1141  CD2 HIS A 139     1454   1341   1259   -114   -111    404       C  
ATOM   1142  CE1 HIS A 139      15.675   3.872  33.637  1.00 10.57           C  
ANISOU 1142  CE1 HIS A 139     1503   1272   1242   -151   -127    174       C  
ATOM   1143  NE2 HIS A 139      15.352   2.616  33.940  1.00 10.90           N  
ANISOU 1143  NE2 HIS A 139     1659   1220   1264     34   -153    353       N  
ATOM   1144  N   PHE A 140      11.274   4.674  29.136  1.00  8.93           N  
ANISOU 1144  N   PHE A 140     1546    888    958   -100    -36    269       N  
ATOM   1145  CA  PHE A 140      10.684   5.046  27.845  1.00  8.41           C  
ANISOU 1145  CA  PHE A 140     1373    801   1021   -206     39    332       C  
ATOM   1146  C   PHE A 140      11.701   5.874  27.065  1.00  7.92           C  
ANISOU 1146  C   PHE A 140     1220    727   1062    -71     36    205       C  
ATOM   1147  O   PHE A 140      12.104   6.977  27.530  1.00  8.60           O  
ANISOU 1147  O   PHE A 140     1344    867   1059   -178     25    169       O  
ATOM   1148  CB  PHE A 140       9.407   5.884  28.068  1.00  9.40           C  
ANISOU 1148  CB  PHE A 140     1497    966   1108    -84    118    232       C  
ATOM   1149  CG  PHE A 140       8.731   6.372  26.801  1.00  8.56           C  
ANISOU 1149  CG  PHE A 140     1253    877   1123   -136     79    301       C  
ATOM   1150  CD1 PHE A 140       8.358   5.460  25.821  1.00  9.36           C  
ANISOU 1150  CD1 PHE A 140     1274   1036   1248   -233    -76    313       C  
ATOM   1151  CD2 PHE A 140       8.446   7.725  26.598  1.00  9.77           C  
ANISOU 1151  CD2 PHE A 140     1516    963   1234   -145     63    319       C  
ATOM   1152  CE1 PHE A 140       7.720   5.900  24.666  1.00 10.59           C  
ANISOU 1152  CE1 PHE A 140     1476   1290   1257   -304   -124    295       C  
ATOM   1153  CE2 PHE A 140       7.782   8.134  25.460  1.00 11.11           C  
ANISOU 1153  CE2 PHE A 140     1592   1198   1432     16     16    368       C  
ATOM   1154  CZ  PHE A 140       7.438   7.241  24.465  1.00 11.34           C  
ANISOU 1154  CZ  PHE A 140     1432   1358   1519   -250   -213    421       C  
ATOM   1155  N   LEU A 141      12.149   5.366  25.917  1.00  7.93           N  
ANISOU 1155  N   LEU A 141     1201    830    982   -199    109    225       N  
ATOM   1156  CA  LEU A 141      13.078   6.041  25.003  1.00  8.72           C  
ANISOU 1156  CA  LEU A 141     1261    993   1060   -245    178    254       C  
ATOM   1157  C   LEU A 141      14.380   6.422  25.680  1.00  8.41           C  
ANISOU 1157  C   LEU A 141     1243    799   1153   -114    119    129       C  
ATOM   1158  O   LEU A 141      15.066   7.396  25.313  1.00  9.07           O  
ANISOU 1158  O   LEU A 141     1187   1055   1203   -241    186    128       O  
ATOM   1159  CB  LEU A 141      12.434   7.257  24.303  1.00  9.53           C  
ANISOU 1159  CB  LEU A 141     1391   1132   1098   -264    115    378       C  
ATOM   1160  CG  LEU A 141      11.026   7.083  23.712  1.00 10.75           C  
ANISOU 1160  CG  LEU A 141     1504   1353   1228   -216    -36    394       C  
ATOM   1161  CD1 LEU A 141      10.578   8.372  23.015  1.00 11.94           C  
ANISOU 1161  CD1 LEU A 141     1625   1394   1517    -71     -3    373       C  
ATOM   1162  CD2 LEU A 141      10.932   5.904  22.739  1.00 14.14           C  
ANISOU 1162  CD2 LEU A 141     2278   1583   1513   -264      0    173       C  
ATOM   1163  N   GLY A 142      14.762   5.698  26.760  1.00  9.17           N  
ANISOU 1163  N   GLY A 142     1287    990   1208    -33     -6    218       N  
ATOM   1164  CA  GLY A 142      15.952   6.026  27.516  1.00  9.63           C  
ANISOU 1164  CA  GLY A 142     1327    999   1335     56    -23     76       C  
ATOM   1165  C   GLY A 142      15.815   7.271  28.357  1.00 11.13           C  
ANISOU 1165  C   GLY A 142     1414   1308   1507    -81    -55   -134       C  
ATOM   1166  O   GLY A 142      16.811   7.619  29.019  1.00 16.62           O  
ANISOU 1166  O   GLY A 142     1458   2218   2640    161   -307   -859       O  
ATOM   1167  N   THR A 143      14.666   7.924  28.467  1.00  8.64           N  
ANISOU 1167  N   THR A 143     1284    912   1085    -94     -5    109       N  
ATOM   1168  CA  THR A 143      14.534   9.217  29.123  1.00  8.30           C  
ANISOU 1168  CA  THR A 143     1237    878   1038    -49    -14     77       C  
ATOM   1169  C   THR A 143      13.595   9.188  30.343  1.00  8.62           C  
ANISOU 1169  C   THR A 143     1224   1097    954    -42    -57    146       C  
ATOM   1170  O   THR A 143      13.987   9.734  31.396  1.00 13.46           O  
ANISOU 1170  O   THR A 143     1722   2247   1144   -459      3    127       O  
ATOM   1171  CB  THR A 143      14.091  10.314  28.104  1.00  8.51           C  
ANISOU 1171  CB  THR A 143     1372    827   1033   -117    176    172       C  
ATOM   1172  OG1 THR A 143      12.848   9.985  27.499  1.00  9.57           O  
ANISOU 1172  OG1 THR A 143     1515   1019   1101     26    -59    262       O  
ATOM   1173  CG2 THR A 143      15.143  10.516  27.031  1.00 10.41           C  
ANISOU 1173  CG2 THR A 143     1604   1254   1099   -141    304    128       C  
ATOM   1174  N   SER A 144      12.371   8.745  30.252  1.00  8.45           N  
ANISOU 1174  N   SER A 144     1235   1066    909   -165      4    245       N  
ATOM   1175  CA  SER A 144      11.436   8.635  31.401  1.00  8.44           C  
ANISOU 1175  CA  SER A 144     1252    941   1012   -133     16    236       C  
ATOM   1176  C   SER A 144      11.391   9.912  32.235  1.00  8.49           C  
ANISOU 1176  C   SER A 144     1210   1017   1001   -154    -33    217       C  
ATOM   1177  O   SER A 144      11.748   9.934  33.416  1.00  9.63           O  
ANISOU 1177  O   SER A 144     1586   1020   1052    -46   -163    153       O  
ATOM   1178  CB  SER A 144      11.798   7.421  32.281  1.00  9.01           C  
ANISOU 1178  CB  SER A 144     1423    891   1110    -51      7    167       C  
ATOM   1179  OG  SER A 144      11.450   6.207  31.574  1.00  9.12           O  
ANISOU 1179  OG  SER A 144     1497    791   1175    -68     38    205       O  
ATOM   1180  N   THR A 145      10.842  10.970  31.629  1.00  9.03           N  
ANISOU 1180  N   THR A 145     1388    863   1182    -45   -142    194       N  
ATOM   1181  CA  THR A 145      10.867  12.289  32.250  1.00  9.05           C  
ANISOU 1181  CA  THR A 145     1359    925   1157   -101    -37    150       C  
ATOM   1182  C   THR A 145       9.669  12.622  33.107  1.00  8.72           C  
ANISOU 1182  C   THR A 145     1353    865   1096    -51    -44    173       C  
ATOM   1183  O   THR A 145       9.680  13.677  33.773  1.00  9.73           O  
ANISOU 1183  O   THR A 145     1603    991   1104   -127    106     89       O  
ATOM   1184  CB  THR A 145      11.094  13.403  31.198  1.00  9.48           C  
ANISOU 1184  CB  THR A 145     1412    993   1196    -64     14    187       C  
ATOM   1185  OG1 THR A 145       9.919  13.562  30.402  1.00  9.45           O  
ANISOU 1185  OG1 THR A 145     1545    939   1107    -72    -15    263       O  
ATOM   1186  CG2 THR A 145      12.280  13.097  30.296  1.00 10.20           C  
ANISOU 1186  CG2 THR A 145     1427    946   1505   -184    172    105       C  
ATOM   1187  N   PHE A 146       8.648  11.730  33.177  1.00  9.28           N  
ANISOU 1187  N   PHE A 146     1424   1122    979   -147    -28    213       N  
ATOM   1188  CA  PHE A 146       7.501  11.934  34.066  1.00  9.37           C  
ANISOU 1188  CA  PHE A 146     1538   1030    991   -199    -33    187       C  
ATOM   1189  C   PHE A 146       7.792  11.414  35.485  1.00  9.51           C  
ANISOU 1189  C   PHE A 146     1386   1201   1025   -152     64    251       C  
ATOM   1190  O   PHE A 146       7.046  10.600  36.055  1.00 10.39           O  
ANISOU 1190  O   PHE A 146     1565   1212   1173   -188     30    246       O  
ATOM   1191  CB  PHE A 146       6.238  11.301  33.492  1.00  9.58           C  
ANISOU 1191  CB  PHE A 146     1490   1047   1104    -89      1    136       C  
ATOM   1192  CG  PHE A 146       5.667  11.898  32.214  1.00  9.04           C  
ANISOU 1192  CG  PHE A 146     1278   1118   1040   -116     68    211       C  
ATOM   1193  CD1 PHE A 146       6.022  13.141  31.718  1.00  9.51           C  
ANISOU 1193  CD1 PHE A 146     1424   1045   1146    -87    -24    225       C  
ATOM   1194  CD2 PHE A 146       4.684  11.204  31.529  1.00  9.74           C  
ANISOU 1194  CD2 PHE A 146     1318   1207   1176   -137     94    185       C  
ATOM   1195  CE1 PHE A 146       5.426  13.693  30.590  1.00 10.33           C  
ANISOU 1195  CE1 PHE A 146     1331   1350   1242    -28     46    285       C  
ATOM   1196  CE2 PHE A 146       4.091  11.720  30.375  1.00 10.21           C  
ANISOU 1196  CE2 PHE A 146     1431   1342   1108    -35     10     31       C  
ATOM   1197  CZ  PHE A 146       4.464  12.975  29.899  1.00 10.77           C  
ANISOU 1197  CZ  PHE A 146     1444   1345   1301     -1     36    165       C  
ATOM   1198  N   SER A 147       8.882  11.920  36.077  1.00 10.47           N  
ANISOU 1198  N   SER A 147     1684   1270   1025   -191    -95    308       N  
ATOM   1199  CA  SER A 147       9.322  11.494  37.402  1.00 10.44           C  
ANISOU 1199  CA  SER A 147     1578   1310   1081    -44    -67    291       C  
ATOM   1200  C   SER A 147      10.135  12.627  38.000  1.00  9.59           C  
ANISOU 1200  C   SER A 147     1391   1303    948    -48    -31    264       C  
ATOM   1201  O   SER A 147      10.894  13.317  37.290  1.00 10.42           O  
ANISOU 1201  O   SER A 147     1585   1220   1155   -160     32    215       O  
ATOM   1202  CB  SER A 147      10.220  10.251  37.307  1.00 10.03           C  
ANISOU 1202  CB  SER A 147     1577   1124   1109   -185    -43    329       C  
ATOM   1203  OG  SER A 147      10.616   9.824  38.611  1.00 10.61           O  
ANISOU 1203  OG  SER A 147     1640   1288   1104    -13    -33    246       O  
ATOM   1204  N   GLN A 148      10.070  12.802  39.338  1.00  9.69           N  
ANISOU 1204  N   GLN A 148     1378   1221   1081    -48     19    172       N  
ATOM   1205  CA  GLN A 148      10.876  13.840  40.004  1.00  9.94           C  
ANISOU 1205  CA  GLN A 148     1511   1099   1166    -28     21    120       C  
ATOM   1206  C   GLN A 148      12.372  13.611  39.765  1.00  9.51           C  
ANISOU 1206  C   GLN A 148     1490   1099   1023    -27   -113    214       C  
ATOM   1207  O   GLN A 148      13.174  14.560  39.730  1.00 10.16           O  
ANISOU 1207  O   GLN A 148     1471   1232   1158    -82    -75    102       O  
ATOM   1208  CB  GLN A 148      10.533  13.908  41.491  1.00 10.35           C  
ANISOU 1208  CB  GLN A 148     1583   1242   1106     11     30    119       C  
ATOM   1209  CG  GLN A 148       9.158  14.535  41.749  1.00 10.80           C  
ANISOU 1209  CG  GLN A 148     1677   1344   1081     34    -31    158       C  
ATOM   1210  CD  GLN A 148       8.701  14.439  43.202  1.00 11.29           C  
ANISOU 1210  CD  GLN A 148     1717   1417   1156    177    -62     93       C  
ATOM   1211  OE1 GLN A 148       9.138  13.563  43.972  1.00 11.01           O  
ANISOU 1211  OE1 GLN A 148     1652   1367   1166    150     46    114       O  
ATOM   1212  NE2 GLN A 148       7.774  15.310  43.590  1.00 12.84           N  
ANISOU 1212  NE2 GLN A 148     1893   1665   1320    226     59     29       N  
ATOM   1213  N   TYR A 149      12.784  12.320  39.674  1.00  9.98           N  
ANISOU 1213  N   TYR A 149     1520   1136   1135     61     53    218       N  
ATOM   1214  CA  TYR A 149      14.159  11.952  39.340  1.00  9.99           C  
ANISOU 1214  CA  TYR A 149     1436   1222   1137     51   -100    104       C  
ATOM   1215  C   TYR A 149      14.152  10.865  38.268  1.00  9.48           C  
ANISOU 1215  C   TYR A 149     1361   1219   1021    -36    -66    233       C  
ATOM   1216  O   TYR A 149      13.347   9.924  38.339  1.00 10.45           O  
ANISOU 1216  O   TYR A 149     1597   1250   1126    -77      8    139       O  
ATOM   1217  CB  TYR A 149      14.958  11.402  40.548  1.00 11.32           C  
ANISOU 1217  CB  TYR A 149     1766   1449   1084     63   -102    238       C  
ATOM   1218  CG  TYR A 149      15.296  12.461  41.597  1.00 10.84           C  
ANISOU 1218  CG  TYR A 149     1623   1335   1161    142    -76    157       C  
ATOM   1219  CD1 TYR A 149      14.354  12.856  42.539  1.00 12.38           C  
ANISOU 1219  CD1 TYR A 149     1758   1654   1293     95     29     83       C  
ATOM   1220  CD2 TYR A 149      16.501  13.122  41.584  1.00 11.35           C  
ANISOU 1220  CD2 TYR A 149     1522   1527   1265    211   -129    149       C  
ATOM   1221  CE1 TYR A 149      14.610  13.845  43.489  1.00 14.45           C  
ANISOU 1221  CE1 TYR A 149     1931   2069   1492     99    152   -208       C  
ATOM   1222  CE2 TYR A 149      16.810  14.096  42.526  1.00 13.97           C  
ANISOU 1222  CE2 TYR A 149     1893   1835   1580     38   -120    -58       C  
ATOM   1223  CZ  TYR A 149      15.840  14.447  43.436  1.00 14.57           C  
ANISOU 1223  CZ  TYR A 149     1993   1941   1602     47    -87   -250       C  
ATOM   1224  OH  TYR A 149      16.179  15.423  44.375  1.00 21.33           O  
ANISOU 1224  OH  TYR A 149     2833   2840   2430   -172   -188   -963       O  
ATOM   1225  N   THR A 150      15.084  10.950  37.312  1.00  9.82           N  
ANISOU 1225  N   THR A 150     1484   1133   1114     -7     20     93       N  
ATOM   1226  CA  THR A 150      15.289   9.872  36.328  1.00  9.39           C  
ANISOU 1226  CA  THR A 150     1292   1166   1111    -76    -82     48       C  
ATOM   1227  C   THR A 150      16.785   9.568  36.233  1.00  9.18           C  
ANISOU 1227  C   THR A 150     1367   1060   1062   -147    -80    184       C  
ATOM   1228  O   THR A 150      17.633  10.342  36.715  1.00 10.10           O  
ANISOU 1228  O   THR A 150     1336   1188   1314    -63   -117    127       O  
ATOM   1229  CB  THR A 150      14.655  10.214  34.955  1.00  9.53           C  
ANISOU 1229  CB  THR A 150     1345   1133   1143    -47    -94    121       C  
ATOM   1230  OG1 THR A 150      14.728   9.007  34.169  1.00 10.29           O  
ANISOU 1230  OG1 THR A 150     1496   1315   1097     53   -129     74       O  
ATOM   1231  CG2 THR A 150      15.393  11.339  34.246  1.00 10.51           C  
ANISOU 1231  CG2 THR A 150     1488   1311   1193   -153    -87    168       C  
ATOM   1232  N   VAL A 151      17.109   8.435  35.614  1.00  9.71           N  
ANISOU 1232  N   VAL A 151     1279   1189   1219    -43     94    158       N  
ATOM   1233  CA  VAL A 151      18.504   8.055  35.359  1.00  9.33           C  
ANISOU 1233  CA  VAL A 151     1319   1094   1132    -37    -29    106       C  
ATOM   1234  C   VAL A 151      18.606   7.804  33.839  1.00  9.03           C  
ANISOU 1234  C   VAL A 151     1140   1130   1160     28     -6    155       C  
ATOM   1235  O   VAL A 151      17.758   7.087  33.313  1.00 10.53           O  
ANISOU 1235  O   VAL A 151     1422   1240   1339    -10      3     48       O  
ATOM   1236  CB  VAL A 151      18.933   6.799  36.142  1.00 10.52           C  
ANISOU 1236  CB  VAL A 151     1439   1205   1351    134    -95    163       C  
ATOM   1237  CG1 VAL A 151      20.378   6.452  35.869  1.00 12.80           C  
ANISOU 1237  CG1 VAL A 151     1629   1815   1421    227   -228    150       C  
ATOM   1238  CG2 VAL A 151      18.767   6.996  37.645  1.00 12.58           C  
ANISOU 1238  CG2 VAL A 151     1944   1525   1313    180     -2    300       C  
ATOM   1239  N   VAL A 152      19.617   8.398  33.198  1.00  9.76           N  
ANISOU 1239  N   VAL A 152     1301   1276   1132     64     96    144       N  
ATOM   1240  CA  VAL A 152      19.789   8.262  31.748  1.00 10.13           C  
ANISOU 1240  CA  VAL A 152     1255   1460   1135     24    -75    143       C  
ATOM   1241  C   VAL A 152      21.228   7.870  31.458  1.00 10.17           C  
ANISOU 1241  C   VAL A 152     1178   1489   1195    -57    -97    113       C  
ATOM   1242  O   VAL A 152      22.162   8.200  32.207  1.00 11.79           O  
ANISOU 1242  O   VAL A 152     1249   1873   1357     54   -117    -43       O  
ATOM   1243  CB  VAL A 152      19.421   9.573  31.003  1.00 10.57           C  
ANISOU 1243  CB  VAL A 152     1357   1531   1129    -53     11    234       C  
ATOM   1244  CG1 VAL A 152      17.979   9.978  31.280  1.00 11.88           C  
ANISOU 1244  CG1 VAL A 152     1445   1495   1573     51    -36    357       C  
ATOM   1245  CG2 VAL A 152      20.402  10.663  31.239  1.00 12.76           C  
ANISOU 1245  CG2 VAL A 152     1535   1592   1724     -7    -38    107       C  
ATOM   1246  N   ASP A 153      21.487   7.199  30.343  1.00 10.04           N  
ANISOU 1246  N   ASP A 153     1255   1348   1213     86   -142     82       N  
ATOM   1247  CA  ASP A 153      22.854   6.942  29.871  1.00 10.51           C  
ANISOU 1247  CA  ASP A 153     1359   1447   1188    106    -81     61       C  
ATOM   1248  C   ASP A 153      23.496   8.266  29.441  1.00  9.92           C  
ANISOU 1248  C   ASP A 153     1196   1452   1123     97    -91     78       C  
ATOM   1249  O   ASP A 153      22.806   9.171  28.932  1.00 10.44           O  
ANISOU 1249  O   ASP A 153     1311   1472   1182     51   -114    189       O  
ATOM   1250  CB  ASP A 153      22.788   5.919  28.712  1.00 10.85           C  
ANISOU 1250  CB  ASP A 153     1480   1444   1200    198    -85     72       C  
ATOM   1251  CG  ASP A 153      22.405   4.539  29.252  1.00 11.58           C  
ANISOU 1251  CG  ASP A 153     1532   1502   1366     47    -19    198       C  
ATOM   1252  OD1 ASP A 153      23.309   3.881  29.844  1.00 13.64           O  
ANISOU 1252  OD1 ASP A 153     2006   1650   1527    149    -42    269       O  
ATOM   1253  OD2 ASP A 153      21.241   4.125  29.086  1.00 12.71           O  
ANISOU 1253  OD2 ASP A 153     1693   1526   1609     24    -59    124       O  
ATOM   1254  N   GLU A 154      24.817   8.385  29.552  1.00 10.22           N  
ANISOU 1254  N   GLU A 154     1213   1408   1261     48    -94    230       N  
ATOM   1255  CA  GLU A 154      25.539   9.603  29.170  1.00 10.59           C  
ANISOU 1255  CA  GLU A 154     1266   1497   1260     31   -162    168       C  
ATOM   1256  C   GLU A 154      25.291   9.992  27.719  1.00  9.77           C  
ANISOU 1256  C   GLU A 154     1174   1295   1243     74   -158    159       C  
ATOM   1257  O   GLU A 154      25.186  11.199  27.408  1.00 10.94           O  
ANISOU 1257  O   GLU A 154     1314   1438   1405     26   -128    140       O  
ATOM   1258  CB  GLU A 154      27.028   9.442  29.496  1.00 11.87           C  
ANISOU 1258  CB  GLU A 154     1312   1801   1396    -13   -314    191       C  
ATOM   1259  CG  GLU A 154      27.813  10.728  29.259  1.00 12.62           C  
ANISOU 1259  CG  GLU A 154     1338   1841   1616    -35   -261    102       C  
ATOM   1260  CD  GLU A 154      29.280  10.645  29.637  1.00 13.11           C  
ANISOU 1260  CD  GLU A 154     1386   1908   1686   -106   -216    266       C  
ATOM   1261  OE1 GLU A 154      29.848   9.520  29.746  1.00 15.17           O  
ANISOU 1261  OE1 GLU A 154     1412   2215   2138     83   -298    210       O  
ATOM   1262  OE2 GLU A 154      29.904  11.746  29.785  1.00 13.90           O  
ANISOU 1262  OE2 GLU A 154     1382   2044   1856    -16   -169     97       O  
ATOM   1263  N   ILE A 155      25.178   9.033  26.797  1.00  9.33           N  
ANISOU 1263  N   ILE A 155     1136   1248   1159    -29   -136    171       N  
ATOM   1264  CA  ILE A 155      24.920   9.323  25.380  1.00  9.90           C  
ANISOU 1264  CA  ILE A 155     1188   1371   1203    124   -115    210       C  
ATOM   1265  C   ILE A 155      23.501   9.863  25.132  1.00  9.40           C  
ANISOU 1265  C   ILE A 155     1193   1191   1185     91   -100    125       C  
ATOM   1266  O   ILE A 155      23.212  10.302  24.004  1.00 10.70           O  
ANISOU 1266  O   ILE A 155     1405   1406   1256     77    -76    190       O  
ATOM   1267  CB  ILE A 155      25.184   8.090  24.492  1.00 10.59           C  
ANISOU 1267  CB  ILE A 155     1311   1509   1204     99    -71     94       C  
ATOM   1268  CG1 ILE A 155      24.252   6.934  24.809  1.00 11.50           C  
ANISOU 1268  CG1 ILE A 155     1708   1359   1303    103    -83     99       C  
ATOM   1269  CG2 ILE A 155      26.659   7.668  24.539  1.00 12.15           C  
ANISOU 1269  CG2 ILE A 155     1402   1829   1387    281    -68     66       C  
ATOM   1270  CD1 ILE A 155      24.243   5.819  23.768  1.00 13.12           C  
ANISOU 1270  CD1 ILE A 155     2021   1549   1413    321   -145     -9       C  
ATOM   1271  N   SER A 156      22.657   9.883  26.152  1.00  9.09           N  
ANISOU 1271  N   SER A 156     1126   1232   1097     93    -90    107       N  
ATOM   1272  CA  SER A 156      21.294  10.379  26.111  1.00  9.80           C  
ANISOU 1272  CA  SER A 156     1224   1247   1254    135   -244     62       C  
ATOM   1273  C   SER A 156      21.078  11.637  26.988  1.00  8.93           C  
ANISOU 1273  C   SER A 156     1118   1122   1153     76   -106    196       C  
ATOM   1274  O   SER A 156      19.949  11.908  27.422  1.00  9.59           O  
ANISOU 1274  O   SER A 156     1178   1228   1240     98   -141     41       O  
ATOM   1275  CB  SER A 156      20.331   9.264  26.546  1.00 10.60           C  
ANISOU 1275  CB  SER A 156     1190   1464   1374     53   -208   -164       C  
ATOM   1276  OG  SER A 156      20.320   8.156  25.641  1.00 13.08           O  
ANISOU 1276  OG  SER A 156     1485   1448   2036    127   -225   -288       O  
ATOM   1277  N   VAL A 157      22.156  12.414  27.175  1.00  9.27           N  
ANISOU 1277  N   VAL A 157     1172   1218   1133      9     25    143       N  
ATOM   1278  CA  VAL A 157      22.002  13.696  27.890  1.00 10.23           C  
ANISOU 1278  CA  VAL A 157     1361   1291   1234   -100     33     52       C  
ATOM   1279  C   VAL A 157      22.917  14.751  27.316  1.00  9.78           C  
ANISOU 1279  C   VAL A 157     1348   1239   1131     -4    102     30       C  
ATOM   1280  O   VAL A 157      24.073  14.441  26.939  1.00 11.36           O  
ANISOU 1280  O   VAL A 157     1347   1368   1603      6     24    222       O  
ATOM   1281  CB  VAL A 157      22.168  13.543  29.421  1.00 11.64           C  
ANISOU 1281  CB  VAL A 157     1865   1324   1233   -154    -73     36       C  
ATOM   1282  CG1 VAL A 157      23.582  13.196  29.765  1.00 15.16           C  
ANISOU 1282  CG1 VAL A 157     2181   2017   1560    311   -157     25       C  
ATOM   1283  CG2 VAL A 157      21.679  14.789  30.167  1.00 13.47           C  
ANISOU 1283  CG2 VAL A 157     2204   1496   1416    -10   -149    -61       C  
ATOM   1284  N   ALA A 158      22.454  16.010  27.240  1.00  9.59           N  
ANISOU 1284  N   ALA A 158     1122   1109   1413   -176    106    188       N  
ATOM   1285  CA  ALA A 158      23.282  17.135  26.801  1.00 10.16           C  
ANISOU 1285  CA  ALA A 158     1140   1202   1518   -219    149    110       C  
ATOM   1286  C   ALA A 158      23.266  18.231  27.882  1.00  9.66           C  
ANISOU 1286  C   ALA A 158     1206   1181   1284   -237     57    198       C  
ATOM   1287  O   ALA A 158      22.220  18.610  28.402  1.00 11.16           O  
ANISOU 1287  O   ALA A 158     1348   1618   1275   -191     54    -10       O  
ATOM   1288  CB  ALA A 158      22.760  17.734  25.504  1.00 12.09           C  
ANISOU 1288  CB  ALA A 158     1845   1272   1479   -407     92    134       C  
ATOM   1289  N   LYS A 159      24.481  18.751  28.142  1.00 11.31           N  
ANISOU 1289  N   LYS A 159     1213   1406   1679   -126    -33      6       N  
ATOM   1290  CA  LYS A 159      24.662  19.939  28.992  1.00 11.81           C  
ANISOU 1290  CA  LYS A 159     1333   1531   1623   -302   -144     54       C  
ATOM   1291  C   LYS A 159      24.240  21.208  28.237  1.00 11.63           C  
ANISOU 1291  C   LYS A 159     1482   1452   1484   -318   -135     49       C  
ATOM   1292  O   LYS A 159      24.594  21.383  27.049  1.00 12.62           O  
ANISOU 1292  O   LYS A 159     1665   1579   1550   -403    -64    -29       O  
ATOM   1293  CB  LYS A 159      26.132  20.077  29.382  1.00 13.56           C  
ANISOU 1293  CB  LYS A 159     1338   1859   1957   -369   -145    201       C  
ATOM   1294  CG  LYS A 159      26.473  21.257  30.273  1.00 16.19           C  
ANISOU 1294  CG  LYS A 159     1879   2211   2060   -369   -242      4       C  
ATOM   1295  CD  LYS A 159      27.967  21.328  30.598  1.00 19.10           C  
ANISOU 1295  CD  LYS A 159     2004   2829   2424   -300   -223     96       C  
ATOM   1296  CE  LYS A 159      28.321  22.567  31.387  1.00 22.17           C  
ANISOU 1296  CE  LYS A 159     2776   3020   2627   -619   -329     62       C  
ATOM   1297  NZ  LYS A 159      29.802  22.658  31.713  1.00 26.74           N  
ANISOU 1297  NZ  LYS A 159     2849   3942   3370   -560   -381    143       N  
ATOM   1298  N   ILE A 160      23.485  22.084  28.891  1.00 11.06           N  
ANISOU 1298  N   ILE A 160     1456   1336   1412   -277   -215    168       N  
ATOM   1299  CA  ILE A 160      23.007  23.323  28.266  1.00 11.09           C  
ANISOU 1299  CA  ILE A 160     1479   1434   1302   -245   -115    180       C  
ATOM   1300  C   ILE A 160      23.427  24.537  29.116  1.00 12.61           C  
ANISOU 1300  C   ILE A 160     1725   1543   1525   -286   -179    144       C  
ATOM   1301  O   ILE A 160      23.883  24.409  30.260  1.00 13.60           O  
ANISOU 1301  O   ILE A 160     1908   1507   1753   -439   -405     32       O  
ATOM   1302  CB  ILE A 160      21.491  23.263  27.990  1.00 11.06           C  
ANISOU 1302  CB  ILE A 160     1461   1246   1494   -138    -39     23       C  
ATOM   1303  CG1 ILE A 160      20.674  23.185  29.285  1.00 11.75           C  
ANISOU 1303  CG1 ILE A 160     1468   1572   1423   -191   -123     47       C  
ATOM   1304  CG2 ILE A 160      21.162  22.096  27.041  1.00 11.41           C  
ANISOU 1304  CG2 ILE A 160     1498   1278   1558   -176    -78     10       C  
ATOM   1305  CD1 ILE A 160      19.214  23.471  29.078  1.00 11.53           C  
ANISOU 1305  CD1 ILE A 160     1497   1354   1530   -163    -19    154       C  
ATOM   1306  N   ASP A 161      23.173  25.732  28.573  1.00 12.96           N  
ANISOU 1306  N   ASP A 161     1893   1399   1634   -365   -191     69       N  
ATOM   1307  CA  ASP A 161      23.552  26.999  29.225  1.00 13.84           C  
ANISOU 1307  CA  ASP A 161     2057   1533   1670   -370    -78     22       C  
ATOM   1308  C   ASP A 161      23.027  27.026  30.647  1.00 13.25           C  
ANISOU 1308  C   ASP A 161     1927   1475   1632   -348    -80     -8       C  
ATOM   1309  O   ASP A 161      21.813  26.851  30.909  1.00 12.58           O  
ANISOU 1309  O   ASP A 161     1893   1318   1568   -364    -78    -34       O  
ATOM   1310  CB AASP A 161      22.912  28.143  28.400  0.61 15.32           C  
ANISOU 1310  CB AASP A 161     2530   1648   1643   -336   -182     84       C  
ATOM   1311  CG AASP A 161      23.285  29.552  28.762  0.61 15.66           C  
ANISOU 1311  CG AASP A 161     2279   1761   1908   -411     -1     80       C  
ATOM   1312  OD1AASP A 161      23.665  29.824  29.925  0.61 16.49           O  
ANISOU 1312  OD1AASP A 161     2772   1498   1993   -639   -166    157       O  
ATOM   1313  OD2AASP A 161      23.225  30.463  27.895  0.61 18.31           O  
ANISOU 1313  OD2AASP A 161     2748   2000   2208   -577   -246    211       O  
ATOM   1314  CB BASP A 161      23.100  28.184  28.375  0.39 17.00           C  
ANISOU 1314  CB BASP A 161     2720   1852   1889   -196     -6    224       C  
ATOM   1315  CG BASP A 161      23.790  29.465  28.818  0.39 18.90           C  
ANISOU 1315  CG BASP A 161     2988   2015   2177   -336    110    148       C  
ATOM   1316  OD1BASP A 161      23.380  30.006  29.865  0.39 18.16           O  
ANISOU 1316  OD1BASP A 161     2913   1795   2193   -466     84    132       O  
ATOM   1317  OD2BASP A 161      24.717  29.865  28.071  0.39 21.88           O  
ANISOU 1317  OD2BASP A 161     3183   2575   2554   -487    289    187       O  
ATOM   1318  N   ALA A 162      23.888  27.398  31.620  1.00 14.24           N  
ANISOU 1318  N   ALA A 162     2081   1498   1830   -471   -177    -32       N  
ATOM   1319  CA  ALA A 162      23.508  27.512  33.024  1.00 14.97           C  
ANISOU 1319  CA  ALA A 162     2068   1803   1816   -270   -319    -56       C  
ATOM   1320  C   ALA A 162      22.435  28.552  33.322  1.00 14.06           C  
ANISOU 1320  C   ALA A 162     2048   1587   1708   -385   -286    -83       C  
ATOM   1321  O   ALA A 162      21.749  28.429  34.359  1.00 14.39           O  
ANISOU 1321  O   ALA A 162     2205   1546   1715   -447   -237    -96       O  
ATOM   1322  CB  ALA A 162      24.775  27.861  33.844  1.00 16.12           C  
ANISOU 1322  CB  ALA A 162     2075   1975   2076   -216   -399   -272       C  
ATOM   1323  N   ALA A 163      22.262  29.530  32.423  1.00 14.07           N  
ANISOU 1323  N   ALA A 163     2034   1380   1931   -399   -318    -24       N  
ATOM   1324  CA  ALA A 163      21.231  30.551  32.625  1.00 13.90           C  
ANISOU 1324  CA  ALA A 163     2002   1321   1960   -438   -208    -19       C  
ATOM   1325  C   ALA A 163      19.911  30.262  31.926  1.00 13.14           C  
ANISOU 1325  C   ALA A 163     1774   1399   1821   -388    -15   -143       C  
ATOM   1326  O   ALA A 163      18.963  31.058  31.971  1.00 15.56           O  
ANISOU 1326  O   ALA A 163     2164   1422   2327   -293   -112     16       O  
ATOM   1327  CB  ALA A 163      21.784  31.918  32.115  1.00 16.28           C  
ANISOU 1327  CB  ALA A 163     2508   1277   2402   -520   -186    -76       C  
ATOM   1328  N   SER A 164      19.766  29.061  31.303  1.00 13.03           N  
ANISOU 1328  N   SER A 164     1812   1476   1663   -470   -163   -115       N  
ATOM   1329  C   SER A 164      17.295  28.641  31.377  1.00 11.36           C  
ANISOU 1329  C   SER A 164     1709   1154   1454   -365    -76     82       C  
ATOM   1330  O   SER A 164      17.355  28.032  32.470  1.00 12.58           O  
ANISOU 1330  O   SER A 164     1936   1348   1496   -360   -129    119       O  
ATOM   1331  CA ASER A 164      18.568  28.690  30.563  0.54 12.02           C  
ANISOU 1331  CA ASER A 164     1547   1392   1630   -247   -142     31       C  
ATOM   1332  CB ASER A 164      18.718  27.219  30.060  0.54 11.91           C  
ANISOU 1332  CB ASER A 164     1580   1324   1622   -258    -78    126       C  
ATOM   1333  OG ASER A 164      19.812  27.051  29.177  0.54 12.44           O  
ANISOU 1333  OG ASER A 164     1645   1460   1622   -447    -80    -73       O  
ATOM   1334  CA BSER A 164      18.521  28.896  30.512  0.46 12.98           C  
ANISOU 1334  CA BSER A 164     1570   1648   1713   -323    -58    -27       C  
ATOM   1335  CB BSER A 164      18.711  27.854  29.401  0.46 13.77           C  
ANISOU 1335  CB BSER A 164     1732   1628   1873    -92    -34    -50       C  
ATOM   1336  OG BSER A 164      19.048  26.616  30.044  0.46 12.14           O  
ANISOU 1336  OG BSER A 164     1592   1264   1757   -140     94   -312       O  
ATOM   1337  N   PRO A 165      16.140  29.085  30.899  1.00 11.17           N  
ANISOU 1337  N   PRO A 165     1838    938   1467   -242   -104     47       N  
ATOM   1338  CA  PRO A 165      14.875  28.961  31.628  1.00 11.37           C  
ANISOU 1338  CA  PRO A 165     1855   1008   1455    -87    -53    -64       C  
ATOM   1339  C   PRO A 165      14.288  27.575  31.324  1.00 11.43           C  
ANISOU 1339  C   PRO A 165     1903   1110   1331   -181   -132     82       C  
ATOM   1340  O   PRO A 165      13.806  27.332  30.212  1.00 11.12           O  
ANISOU 1340  O   PRO A 165     1777   1137   1312   -176   -101    203       O  
ATOM   1341  CB  PRO A 165      14.001  30.090  31.095  1.00 13.14           C  
ANISOU 1341  CB  PRO A 165     2106   1183   1703     48   -230     44       C  
ATOM   1342  CG  PRO A 165      14.534  30.297  29.697  1.00 14.12           C  
ANISOU 1342  CG  PRO A 165     2226   1224   1916   -199    -93    274       C  
ATOM   1343  CD  PRO A 165      16.029  29.997  29.721  1.00 13.21           C  
ANISOU 1343  CD  PRO A 165     2090   1333   1596   -304   -348    215       C  
ATOM   1344  N   LEU A 166      14.403  26.628  32.272  1.00 10.79           N  
ANISOU 1344  N   LEU A 166     1790   1060   1250   -125   -106    -37       N  
ATOM   1345  CA  LEU A 166      14.050  25.235  32.009  1.00 10.25           C  
ANISOU 1345  CA  LEU A 166     1632    957   1305   -113      6    132       C  
ATOM   1346  C   LEU A 166      12.585  25.017  31.663  1.00 10.21           C  
ANISOU 1346  C   LEU A 166     1635    977   1266    -42     39    194       C  
ATOM   1347  O   LEU A 166      12.298  24.041  30.930  1.00 10.57           O  
ANISOU 1347  O   LEU A 166     1573   1088   1356   -113    -33     55       O  
ATOM   1348  CB  LEU A 166      14.513  24.371  33.193  1.00 11.14           C  
ANISOU 1348  CB  LEU A 166     1530   1226   1478    -57    -71    246       C  
ATOM   1349  CG ALEU A 166      16.046  24.358  33.360  0.65 11.32           C  
ANISOU 1349  CG ALEU A 166     1553   1289   1458     -4     28    224       C  
ATOM   1350  CD1ALEU A 166      16.442  23.257  34.342  0.65 12.12           C  
ANISOU 1350  CD1ALEU A 166     1518   1286   1803    150    -88    273       C  
ATOM   1351  CD2ALEU A 166      16.826  24.216  32.047  0.65 11.18           C  
ANISOU 1351  CD2ALEU A 166     1491   1432   1326   -220   -123    150       C  
ATOM   1352  CG BLEU A 166      15.939  24.432  33.711  0.35 10.65           C  
ANISOU 1352  CG BLEU A 166     1532   1311   1203    -56     -5     80       C  
ATOM   1353  CD1BLEU A 166      16.085  23.721  35.058  0.35 10.64           C  
ANISOU 1353  CD1BLEU A 166     1403   1352   1289    -83    -54    154       C  
ATOM   1354  CD2BLEU A 166      16.905  23.780  32.725  0.35 11.71           C  
ANISOU 1354  CD2BLEU A 166     1598   1472   1377     70    -49     41       C  
ATOM   1355  N   GLU A 167      11.702  25.878  32.142  1.00 10.66           N  
ANISOU 1355  N   GLU A 167     1649   1175   1226    -27     97    -17       N  
ATOM   1356  CA  GLU A 167      10.286  25.771  31.843  1.00 11.31           C  
ANISOU 1356  CA  GLU A 167     1678   1418   1199    -14     50     66       C  
ATOM   1357  C   GLU A 167       9.941  26.124  30.384  1.00 10.50           C  
ANISOU 1357  C   GLU A 167     1529   1153   1308    -68     87    101       C  
ATOM   1358  O   GLU A 167       8.778  25.925  29.978  1.00 11.64           O  
ANISOU 1358  O   GLU A 167     1676   1428   1319    -96     21    127       O  
ATOM   1359  CB  GLU A 167       9.434  26.585  32.835  1.00 12.89           C  
ANISOU 1359  CB  GLU A 167     1843   1667   1387    155     53    -22       C  
ATOM   1360  CG  GLU A 167       9.317  28.060  32.593  1.00 15.40           C  
ANISOU 1360  CG  GLU A 167     2263   1809   1779    136    184   -102       C  
ATOM   1361  CD  GLU A 167      10.497  28.940  32.843  1.00 16.94           C  
ANISOU 1361  CD  GLU A 167     2465   1819   2153    137    -86   -241       C  
ATOM   1362  OE1 GLU A 167      11.585  28.461  33.208  1.00 17.20           O  
ANISOU 1362  OE1 GLU A 167     2534   1751   2251    219    -61   -424       O  
ATOM   1363  OE2 GLU A 167      10.336  30.198  32.641  1.00 20.71           O  
ANISOU 1363  OE2 GLU A 167     3173   1885   2811    334   -219   -366       O  
ATOM   1364  N   LYS A 168      10.899  26.701  29.659  1.00 10.21           N  
ANISOU 1364  N   LYS A 168     1555   1185   1140    -78     19    115       N  
ATOM   1365  CA  LYS A 168      10.741  26.982  28.222  1.00 10.17           C  
ANISOU 1365  CA  LYS A 168     1672   1062   1130    -35     12    125       C  
ATOM   1366  C   LYS A 168      11.580  25.992  27.402  1.00  9.46           C  
ANISOU 1366  C   LYS A 168     1524    981   1090    -70    -50    187       C  
ATOM   1367  O   LYS A 168      11.074  25.382  26.435  1.00  9.74           O  
ANISOU 1367  O   LYS A 168     1600    938   1162   -118   -101    145       O  
ATOM   1368  CB ALYS A 168      11.261  28.418  27.915  0.64 11.89           C  
ANISOU 1368  CB ALYS A 168     2146    948   1425     99    -15     71       C  
ATOM   1369  CG ALYS A 168      10.733  29.547  28.794  0.64 12.24           C  
ANISOU 1369  CG ALYS A 168     1924   1270   1457    266    -41     61       C  
ATOM   1370  CD ALYS A 168       9.228  29.745  28.696  0.64 14.48           C  
ANISOU 1370  CD ALYS A 168     1978   1819   1705    228   -132   -203       C  
ATOM   1371  CE ALYS A 168       8.854  31.097  29.341  0.64 16.74           C  
ANISOU 1371  CE ALYS A 168     2468   2271   1622    592   -231   -487       C  
ATOM   1372  NZ ALYS A 168       7.386  31.338  29.225  0.64 16.77           N  
ANISOU 1372  NZ ALYS A 168     2521   1869   1984    541   -206   -153       N  
ATOM   1373  CB BLYS A 168      11.025  28.424  27.852  0.36 10.63           C  
ANISOU 1373  CB BLYS A 168     1796    997   1248    -10    -19     -1       C  
ATOM   1374  CG BLYS A 168      10.052  29.385  28.543  0.36 10.41           C  
ANISOU 1374  CG BLYS A 168     1503   1344   1109    134   -177     69       C  
ATOM   1375  CD BLYS A 168      10.430  30.785  28.104  0.36 13.43           C  
ANISOU 1375  CD BLYS A 168     1904   1399   1799    -44    -37     23       C  
ATOM   1376  CE BLYS A 168      10.292  30.965  26.598  0.36 17.79           C  
ANISOU 1376  CE BLYS A 168     2373   2504   1882   -100    -41    -59       C  
ATOM   1377  NZ BLYS A 168      10.382  32.404  26.299  0.36 16.80           N  
ANISOU 1377  NZ BLYS A 168     2259   2473   1653    291     65     -8       N  
ATOM   1378  N   VAL A 169      12.876  25.827  27.732  1.00  9.21           N  
ANISOU 1378  N   VAL A 169     1434    931   1133    -72    -66     94       N  
ATOM   1379  CA  VAL A 169      13.789  25.090  26.860  1.00  9.22           C  
ANISOU 1379  CA  VAL A 169     1388   1059   1055    -34   -142     50       C  
ATOM   1380  C   VAL A 169      13.565  23.580  26.904  1.00  8.64           C  
ANISOU 1380  C   VAL A 169     1267   1055    961   -149     28     85       C  
ATOM   1381  O   VAL A 169      14.067  22.894  26.005  1.00  8.89           O  
ANISOU 1381  O   VAL A 169     1307   1022   1047   -208     21    138       O  
ATOM   1382  CB  VAL A 169      15.264  25.437  27.067  1.00 10.02           C  
ANISOU 1382  CB  VAL A 169     1384   1110   1313   -134    -87     17       C  
ATOM   1383  CG1 VAL A 169      15.564  26.910  26.784  1.00 11.99           C  
ANISOU 1383  CG1 VAL A 169     1751   1186   1617   -245    144     50       C  
ATOM   1384  CG2 VAL A 169      15.766  24.998  28.443  1.00 11.37           C  
ANISOU 1384  CG2 VAL A 169     1542   1409   1369   -176    -39     -3       C  
ATOM   1385  N   CYS A 170      12.734  23.063  27.809  1.00  8.17           N  
ANISOU 1385  N   CYS A 170     1141    938   1024    -90     22    101       N  
ATOM   1386  CA  CYS A 170      12.301  21.671  27.702  1.00  8.49           C  
ANISOU 1386  CA  CYS A 170     1320    887   1019   -158     23    141       C  
ATOM   1387  C   CYS A 170      11.738  21.360  26.313  1.00  7.70           C  
ANISOU 1387  C   CYS A 170     1138    812    975   -107    133    139       C  
ATOM   1388  O   CYS A 170      11.868  20.219  25.864  1.00  8.52           O  
ANISOU 1388  O   CYS A 170     1256    832   1148   -185     46    191       O  
ATOM   1389  CB  CYS A 170      11.276  21.340  28.815  1.00  9.30           C  
ANISOU 1389  CB  CYS A 170     1479    979   1074   -151     49    190       C  
ATOM   1390  SG  CYS A 170       9.817  22.407  28.898  1.00  9.42           S  
ANISOU 1390  SG  CYS A 170     1303   1212   1064    -58    100    199       S  
ATOM   1391  N   LEU A 171      11.092  22.335  25.611  1.00  8.24           N  
ANISOU 1391  N   LEU A 171     1220    904   1009   -148    -33    194       N  
ATOM   1392  CA  LEU A 171      10.539  22.073  24.291  1.00  7.78           C  
ANISOU 1392  CA  LEU A 171     1275    806    876    -93     19    118       C  
ATOM   1393  C   LEU A 171      11.597  21.778  23.227  1.00  7.57           C  
ANISOU 1393  C   LEU A 171     1099    771   1006   -131      6    157       C  
ATOM   1394  O   LEU A 171      11.296  21.147  22.190  1.00  8.21           O  
ANISOU 1394  O   LEU A 171     1183    916   1019   -132    -47    113       O  
ATOM   1395  CB  LEU A 171       9.650  23.264  23.853  1.00  9.16           C  
ANISOU 1395  CB  LEU A 171     1359   1063   1058     78     47     80       C  
ATOM   1396  CG  LEU A 171       8.395  23.484  24.697  1.00 10.64           C  
ANISOU 1396  CG  LEU A 171     1432   1407   1203    170    150     87       C  
ATOM   1397  CD1 LEU A 171       7.567  24.654  24.225  1.00 17.53           C  
ANISOU 1397  CD1 LEU A 171     2487   2206   1968    868    298    658       C  
ATOM   1398  CD2 LEU A 171       7.546  22.208  24.715  1.00 17.26           C  
ANISOU 1398  CD2 LEU A 171     1650   2246   2663   -274    389   -672       C  
ATOM   1399  N   ILE A 172      12.854  22.165  23.442  1.00  7.81           N  
ANISOU 1399  N   ILE A 172     1092    842   1035   -121     66     79       N  
ATOM   1400  CA  ILE A 172      13.973  21.783  22.562  1.00  8.02           C  
ANISOU 1400  CA  ILE A 172     1151    892   1004   -115     40    126       C  
ATOM   1401  C   ILE A 172      14.282  20.276  22.665  1.00  7.33           C  
ANISOU 1401  C   ILE A 172     1055    784    945   -144     -5     52       C  
ATOM   1402  O   ILE A 172      14.859  19.693  21.745  1.00  8.17           O  
ANISOU 1402  O   ILE A 172     1264    827   1011   -133     79    159       O  
ATOM   1403  CB  ILE A 172      15.180  22.712  22.851  1.00  8.30           C  
ANISOU 1403  CB  ILE A 172     1232    821   1101   -132      7    143       C  
ATOM   1404  CG1 ILE A 172      14.859  24.142  22.378  1.00  9.28           C  
ANISOU 1404  CG1 ILE A 172     1274    869   1385   -239     37    184       C  
ATOM   1405  CG2 ILE A 172      16.478  22.229  22.198  1.00  9.93           C  
ANISOU 1405  CG2 ILE A 172     1306   1122   1344   -259    111     48       C  
ATOM   1406  CD1 ILE A 172      15.809  25.206  22.906  1.00 10.23           C  
ANISOU 1406  CD1 ILE A 172     1559   1029   1299   -319    107    114       C  
ATOM   1407  N   GLY A 173      13.823  19.619  23.738  1.00  8.00           N  
ANISOU 1407  N   GLY A 173     1166    804   1070   -100     23    157       N  
ATOM   1408  CA  GLY A 173      13.960  18.180  23.843  1.00  8.17           C  
ANISOU 1408  CA  GLY A 173     1279    757   1069    -78    -62    223       C  
ATOM   1409  C   GLY A 173      13.012  17.387  22.942  1.00  7.26           C  
ANISOU 1409  C   GLY A 173     1005    868    885     -2     96    172       C  
ATOM   1410  O   GLY A 173      13.214  16.160  22.798  1.00  7.86           O  
ANISOU 1410  O   GLY A 173     1119    827   1039    -14    -92    186       O  
ATOM   1411  N   CYS A 174      11.992  17.988  22.333  1.00  7.05           N  
ANISOU 1411  N   CYS A 174      979    766    935   -129      1    203       N  
ATOM   1412  CA  CYS A 174      11.220  17.235  21.345  1.00  7.20           C  
ANISOU 1412  CA  CYS A 174     1099    748    887   -184      5    207       C  
ATOM   1413  C   CYS A 174      10.554  18.178  20.329  1.00  6.90           C  
ANISOU 1413  C   CYS A 174      998    762    861   -170     14     95       C  
ATOM   1414  O   CYS A 174      10.969  18.257  19.156  1.00  7.54           O  
ANISOU 1414  O   CYS A 174     1111    897    857    -85     22    213       O  
ATOM   1415  CB  CYS A 174      10.211  16.262  21.964  1.00  7.50           C  
ANISOU 1415  CB  CYS A 174     1158    800    890   -280   -100    141       C  
ATOM   1416  SG  CYS A 174       9.416  15.398  20.516  1.00  7.50           S  
ANISOU 1416  SG  CYS A 174     1104    837    908   -243     -1    213       S  
ATOM   1417  N   GLY A 175       9.443  18.806  20.721  1.00  7.42           N  
ANISOU 1417  N   GLY A 175     1073    780    967    -57    -31    207       N  
ATOM   1418  CA  GLY A 175       8.544  19.337  19.690  1.00  8.02           C  
ANISOU 1418  CA  GLY A 175     1162    954    932    -26     16    239       C  
ATOM   1419  C   GLY A 175       9.117  20.452  18.841  1.00  7.32           C  
ANISOU 1419  C   GLY A 175     1016    845    919    -19     56    199       C  
ATOM   1420  O   GLY A 175       8.912  20.463  17.602  1.00  8.43           O  
ANISOU 1420  O   GLY A 175     1310    909    983    -79     -8    246       O  
ATOM   1421  N   PHE A 176       9.766  21.434  19.463  1.00  7.84           N  
ANISOU 1421  N   PHE A 176     1177    826    975    -68     14    216       N  
ATOM   1422  CA  PHE A 176      10.341  22.531  18.673  1.00  8.28           C  
ANISOU 1422  CA  PHE A 176     1386    819    940   -114      1    238       C  
ATOM   1423  C   PHE A 176      11.401  21.999  17.700  1.00  7.97           C  
ANISOU 1423  C   PHE A 176     1218    915    895   -158     41    254       C  
ATOM   1424  O   PHE A 176      11.379  22.268  16.480  1.00  8.17           O  
ANISOU 1424  O   PHE A 176     1328    829    946   -104     29    228       O  
ATOM   1425  CB  PHE A 176      10.943  23.668  19.556  1.00  8.56           C  
ANISOU 1425  CB  PHE A 176     1334    868   1051   -129    -17    155       C  
ATOM   1426  CG  PHE A 176      11.686  24.649  18.675  1.00  8.65           C  
ANISOU 1426  CG  PHE A 176     1437    845   1005   -198    -51    117       C  
ATOM   1427  CD1 PHE A 176      10.987  25.609  17.943  1.00  9.47           C  
ANISOU 1427  CD1 PHE A 176     1520    941   1136   -121     36    165       C  
ATOM   1428  CD2 PHE A 176      13.055  24.555  18.522  1.00  9.13           C  
ANISOU 1428  CD2 PHE A 176     1389    871   1210   -219   -156    109       C  
ATOM   1429  CE1 PHE A 176      11.647  26.464  17.044  1.00 10.08           C  
ANISOU 1429  CE1 PHE A 176     1777    918   1134   -219     -7    216       C  
ATOM   1430  CE2 PHE A 176      13.729  25.392  17.606  1.00 10.76           C  
ANISOU 1430  CE2 PHE A 176     1520   1263   1306   -296   -109    168       C  
ATOM   1431  CZ  PHE A 176      12.995  26.345  16.892  1.00 10.18           C  
ANISOU 1431  CZ  PHE A 176     1734   1003   1132   -375    -53    203       C  
ATOM   1432  N   SER A 177      12.392  21.261  18.226  1.00  7.62           N  
ANISOU 1432  N   SER A 177     1184    838    872   -158      7    201       N  
ATOM   1433  CA  SER A 177      13.524  20.835  17.393  1.00  7.88           C  
ANISOU 1433  CA  SER A 177     1185    820    988   -168     70    217       C  
ATOM   1434  C   SER A 177      13.075  19.957  16.254  1.00  7.30           C  
ANISOU 1434  C   SER A 177      959    861    956     24    -13    239       C  
ATOM   1435  O   SER A 177      13.542  20.042  15.107  1.00  8.48           O  
ANISOU 1435  O   SER A 177     1247   1026    951    -31     71    316       O  
ATOM   1436  CB  SER A 177      14.553  20.125  18.270  1.00  8.64           C  
ANISOU 1436  CB  SER A 177     1119   1107   1056    -78    -23    105       C  
ATOM   1437  OG  SER A 177      14.921  21.007  19.338  1.00  9.40           O  
ANISOU 1437  OG  SER A 177     1346   1109   1115   -203    -48    176       O  
ATOM   1438  N   THR A 178      12.106  19.063  16.556  1.00  7.31           N  
ANISOU 1438  N   THR A 178     1089    742    946    -90     78    197       N  
ATOM   1439  CA  THR A 178      11.593  18.173  15.523  1.00  6.85           C  
ANISOU 1439  CA  THR A 178     1013    807    784    -31    110    175       C  
ATOM   1440  C   THR A 178      10.948  18.977  14.398  1.00  6.52           C  
ANISOU 1440  C   THR A 178      936    689    852   -134     66    138       C  
ATOM   1441  O   THR A 178      11.262  18.753  13.209  1.00  7.34           O  
ANISOU 1441  O   THR A 178     1051    853    887    -16    114    196       O  
ATOM   1442  CB  THR A 178      10.562  17.206  16.124  1.00  6.90           C  
ANISOU 1442  CB  THR A 178     1012    663    949    -77     71    190       C  
ATOM   1443  OG1 THR A 178      11.202  16.344  17.089  1.00  7.58           O  
ANISOU 1443  OG1 THR A 178     1090    811    978   -107     50    332       O  
ATOM   1444  CG2 THR A 178       9.939  16.350  15.035  1.00  8.35           C  
ANISOU 1444  CG2 THR A 178     1258    903   1011    -60     20     98       C  
ATOM   1445  N   GLY A 179      10.019  19.888  14.726  1.00  7.11           N  
ANISOU 1445  N   GLY A 179     1061    809    831    -31    113    211       N  
ATOM   1446  CA  GLY A 179       9.352  20.563  13.616  1.00  7.81           C  
ANISOU 1446  CA  GLY A 179     1184    837    947    -26     79    286       C  
ATOM   1447  C   GLY A 179      10.255  21.497  12.856  1.00  7.53           C  
ANISOU 1447  C   GLY A 179     1019    914    929      0     54    246       C  
ATOM   1448  O   GLY A 179      10.288  21.550  11.612  1.00  8.37           O  
ANISOU 1448  O   GLY A 179     1226    984    971     49     70    276       O  
ATOM   1449  N   TYR A 180      11.057  22.273  13.592  1.00  7.82           N  
ANISOU 1449  N   TYR A 180     1191    772   1010   -154     60    235       N  
ATOM   1450  CA  TYR A 180      11.976  23.253  12.975  1.00  8.60           C  
ANISOU 1450  CA  TYR A 180     1322    894   1052   -241    109    188       C  
ATOM   1451  C   TYR A 180      12.982  22.562  12.075  1.00  8.42           C  
ANISOU 1451  C   TYR A 180     1207    977   1014   -134     71    238       C  
ATOM   1452  O   TYR A 180      13.192  22.981  10.912  1.00  9.01           O  
ANISOU 1452  O   TYR A 180     1275   1107   1042   -108    142    295       O  
ATOM   1453  CB  TYR A 180      12.612  24.098  14.098  1.00  9.85           C  
ANISOU 1453  CB  TYR A 180     1515    974   1254   -224     26    131       C  
ATOM   1454  CG  TYR A 180      13.338  25.332  13.638  1.00 10.94           C  
ANISOU 1454  CG  TYR A 180     1678    979   1499   -292    154     48       C  
ATOM   1455  CD1 TYR A 180      12.634  26.540  13.462  1.00 11.51           C  
ANISOU 1455  CD1 TYR A 180     1860   1197   1315   -226     55    378       C  
ATOM   1456  CD2 TYR A 180      14.700  25.363  13.415  1.00 15.35           C  
ANISOU 1456  CD2 TYR A 180     1764   1452   2616   -219    269    208       C  
ATOM   1457  CE1 TYR A 180      13.246  27.731  13.112  1.00 12.45           C  
ANISOU 1457  CE1 TYR A 180     2006   1261   1462   -313     60    281       C  
ATOM   1458  CE2 TYR A 180      15.340  26.568  13.044  1.00 16.53           C  
ANISOU 1458  CE2 TYR A 180     1867   1610   2802   -314    134    348       C  
ATOM   1459  CZ  TYR A 180      14.602  27.715  12.906  1.00 14.58           C  
ANISOU 1459  CZ  TYR A 180     1966   1334   2239   -408    184    295       C  
ATOM   1460  OH  TYR A 180      15.248  28.919  12.566  1.00 18.83           O  
ANISOU 1460  OH  TYR A 180     2571   1731   2854   -680    131    623       O  
ATOM   1461  N   GLY A 181      13.622  21.488  12.557  1.00  8.32           N  
ANISOU 1461  N   GLY A 181     1173   1014    975   -196     95    295       N  
ATOM   1462  CA  GLY A 181      14.593  20.748  11.779  1.00  8.71           C  
ANISOU 1462  CA  GLY A 181     1131   1138   1042    -93     77    292       C  
ATOM   1463  C   GLY A 181      13.977  20.050  10.588  1.00  7.67           C  
ANISOU 1463  C   GLY A 181     1002    918    993     22     95    222       C  
ATOM   1464  O   GLY A 181      14.581  19.961   9.508  1.00  8.79           O  
ANISOU 1464  O   GLY A 181     1179   1149   1013    -72    153    290       O  
ATOM   1465  N   SER A 182      12.736  19.554  10.741  1.00  7.74           N  
ANISOU 1465  N   SER A 182      995   1027    918    -68     25    240       N  
ATOM   1466  CA  SER A 182      12.079  18.912   9.602  1.00  7.88           C  
ANISOU 1466  CA  SER A 182     1088   1039    865    -22     70    228       C  
ATOM   1467  C   SER A 182      12.012  19.857   8.414  1.00  8.34           C  
ANISOU 1467  C   SER A 182     1111   1126    931     65    123    213       C  
ATOM   1468  O   SER A 182      12.163  19.451   7.250  1.00  9.17           O  
ANISOU 1468  O   SER A 182     1367   1170    947    -11     74    273       O  
ATOM   1469  CB  SER A 182      10.688  18.377   9.977  1.00  7.92           C  
ANISOU 1469  CB  SER A 182     1154    900    954   -103     70    219       C  
ATOM   1470  OG  SER A 182      10.794  17.333  10.938  1.00  8.48           O  
ANISOU 1470  OG  SER A 182     1281    967    973    -89    149    305       O  
ATOM   1471  N   ALA A 183      11.758  21.151   8.666  1.00  8.32           N  
ANISOU 1471  N   ALA A 183     1186   1059    917    -42    139    259       N  
ATOM   1472  CA  ALA A 183      11.740  22.162   7.601  1.00  8.94           C  
ANISOU 1472  CA  ALA A 183     1207   1111   1078    -65     77    357       C  
ATOM   1473  C   ALA A 183      13.124  22.566   7.134  1.00  9.78           C  
ANISOU 1473  C   ALA A 183     1328   1287   1101     21     98    370       C  
ATOM   1474  O   ALA A 183      13.428  22.554   5.921  1.00 11.18           O  
ANISOU 1474  O   ALA A 183     1526   1600   1122     -7    143    409       O  
ATOM   1475  CB  ALA A 183      10.967  23.390   8.087  1.00  9.87           C  
ANISOU 1475  CB  ALA A 183     1433   1153   1166    -47     48    470       C  
ATOM   1476  N   VAL A 184      14.014  22.967   8.045  1.00 10.53           N  
ANISOU 1476  N   VAL A 184     1315   1456   1231   -279    213    447       N  
ATOM   1477  CA  VAL A 184      15.291  23.584   7.636  1.00 11.37           C  
ANISOU 1477  CA  VAL A 184     1329   1488   1504   -289    190    382       C  
ATOM   1478  C   VAL A 184      16.363  22.588   7.300  1.00 13.46           C  
ANISOU 1478  C   VAL A 184     1704   1877   1535      2    435    410       C  
ATOM   1479  O   VAL A 184      17.254  22.914   6.463  1.00 20.03           O  
ANISOU 1479  O   VAL A 184     2379   2589   2642    132   1124    821       O  
ATOM   1480  CB AVAL A 184      15.772  24.646   8.666  0.77 13.45           C  
ANISOU 1480  CB AVAL A 184     1801   1735   1575   -213    142    293       C  
ATOM   1481  CG1AVAL A 184      14.655  25.663   8.946  0.77 14.72           C  
ANISOU 1481  CG1AVAL A 184     1885   1704   2002   -204    204    179       C  
ATOM   1482  CG2AVAL A 184      16.337  24.073   9.960  0.77 14.42           C  
ANISOU 1482  CG2AVAL A 184     1843   1859   1776   -157     37    378       C  
ATOM   1483  CB BVAL A 184      15.796  24.483   8.793  0.23 11.22           C  
ANISOU 1483  CB BVAL A 184     1364   1501   1399   -177    140    362       C  
ATOM   1484  CG1BVAL A 184      17.219  24.954   8.547  0.23 11.05           C  
ANISOU 1484  CG1BVAL A 184     1480   1374   1343   -426     52    264       C  
ATOM   1485  CG2BVAL A 184      14.878  25.677   9.019  0.23 11.17           C  
ANISOU 1485  CG2BVAL A 184     1344   1416   1482   -247    104    234       C  
ATOM   1486  N   LYS A 185      16.395  21.418   7.883  1.00 12.06           N  
ANISOU 1486  N   LYS A 185     1322   1690   1569    -70    202    313       N  
ATOM   1487  CA  LYS A 185      17.431  20.420   7.704  1.00 12.86           C  
ANISOU 1487  CA  LYS A 185     1344   1820   1721    -13    117    233       C  
ATOM   1488  C   LYS A 185      17.023  19.242   6.838  1.00 12.15           C  
ANISOU 1488  C   LYS A 185     1351   1858   1409     37    230    193       C  
ATOM   1489  O   LYS A 185      17.773  18.802   5.967  1.00 15.54           O  
ANISOU 1489  O   LYS A 185     1575   2612   1716     98    443    108       O  
ATOM   1490  CB ALYS A 185      17.933  19.860   9.048  0.51 13.06           C  
ANISOU 1490  CB ALYS A 185     1470   1823   1668    -21     37    191       C  
ATOM   1491  CG ALYS A 185      19.198  19.016   8.935  0.51 13.33           C  
ANISOU 1491  CG ALYS A 185     1694   1619   1753    -11     74    276       C  
ATOM   1492  CD ALYS A 185      19.745  18.606  10.298  0.51 14.86           C  
ANISOU 1492  CD ALYS A 185     1799   2151   1697    -32    122    323       C  
ATOM   1493  CE ALYS A 185      21.043  17.857  10.260  0.51 15.00           C  
ANISOU 1493  CE ALYS A 185     1759   1929   2013    -79     41    331       C  
ATOM   1494  NZ ALYS A 185      21.030  16.511   9.609  0.51 18.05           N  
ANISOU 1494  NZ ALYS A 185     2050   2255   2552   -323    332      9       N  
ATOM   1495  CB BLYS A 185      17.885  19.985   9.105  0.49 16.99           C  
ANISOU 1495  CB BLYS A 185     2005   2609   1840      6     -4    319       C  
ATOM   1496  CG BLYS A 185      18.870  18.844   9.177  0.49 21.39           C  
ANISOU 1496  CG BLYS A 185     2512   2822   2792    226     44    215       C  
ATOM   1497  CD BLYS A 185      19.463  18.699  10.575  0.49 25.20           C  
ANISOU 1497  CD BLYS A 185     3213   3506   2855    187    -79    317       C  
ATOM   1498  CE BLYS A 185      20.679  19.575  10.787  0.49 26.84           C  
ANISOU 1498  CE BLYS A 185     3463   3543   3193     31   -130    257       C  
ATOM   1499  NZ BLYS A 185      21.845  19.172   9.951  0.49 28.21           N  
ANISOU 1499  NZ BLYS A 185     3395   4042   3279   -133    -32    319       N  
ATOM   1500  N   VAL A 186      15.811  18.689   7.019  1.00 10.86           N  
ANISOU 1500  N   VAL A 186     1262   1516   1349    109    127    314       N  
ATOM   1501  CA  VAL A 186      15.348  17.504   6.318  1.00 10.66           C  
ANISOU 1501  CA  VAL A 186     1424   1559   1066    194    202    276       C  
ATOM   1502  C   VAL A 186      14.801  17.879   4.951  1.00 11.17           C  
ANISOU 1502  C   VAL A 186     1591   1646   1007    275    208    231       C  
ATOM   1503  O   VAL A 186      15.321  17.438   3.900  1.00 12.85           O  
ANISOU 1503  O   VAL A 186     1882   1900   1100    461    244    249       O  
ATOM   1504  CB  VAL A 186      14.346  16.708   7.180  1.00  9.76           C  
ANISOU 1504  CB  VAL A 186     1352   1276   1080     68     21    299       C  
ATOM   1505  CG1 VAL A 186      13.880  15.474   6.402  1.00 10.97           C  
ANISOU 1505  CG1 VAL A 186     1566   1353   1248    105   -112    155       C  
ATOM   1506  CG2 VAL A 186      14.965  16.308   8.506  1.00 11.06           C  
ANISOU 1506  CG2 VAL A 186     1727   1312   1163     39   -129    224       C  
ATOM   1507  N   ALA A 187      13.766  18.740   4.898  1.00 11.01           N  
ANISOU 1507  N   ALA A 187     1642   1612    931    314    188    453       N  
ATOM   1508  CA  ALA A 187      13.215  19.208   3.631  1.00 11.43           C  
ANISOU 1508  CA  ALA A 187     1574   1642   1126    265    152    347       C  
ATOM   1509  C   ALA A 187      14.152  20.174   2.917  1.00 11.74           C  
ANISOU 1509  C   ALA A 187     1622   1718   1121    359    231    444       C  
ATOM   1510  O   ALA A 187      14.198  20.211   1.673  1.00 14.41           O  
ANISOU 1510  O   ALA A 187     2051   2234   1191    474    283    388       O  
ATOM   1511  CB  ALA A 187      11.867  19.920   3.856  1.00 10.93           C  
ANISOU 1511  CB  ALA A 187     1562   1514   1078    158     83    281       C  
ATOM   1512  N   LYS A 188      14.864  21.002   3.670  1.00 12.44           N  
ANISOU 1512  N   LYS A 188     1481   1959   1285     55    247    495       N  
ATOM   1513  CA  LYS A 188      15.713  22.060   3.116  1.00 14.05           C  
ANISOU 1513  CA  LYS A 188     1636   2126   1577     96    373    632       C  
ATOM   1514  C   LYS A 188      14.849  23.048   2.319  1.00 13.15           C  
ANISOU 1514  C   LYS A 188     1495   2149   1351     20    333    605       C  
ATOM   1515  O   LYS A 188      15.106  23.384   1.139  1.00 14.96           O  
ANISOU 1515  O   LYS A 188     1994   2267   1424    139    414    662       O  
ATOM   1516  CB  LYS A 188      16.907  21.514   2.304  1.00 17.55           C  
ANISOU 1516  CB  LYS A 188     1756   2808   2106    197    575    658       C  
ATOM   1517  CG ALYS A 188      17.827  20.685   3.210  0.59 21.97           C  
ANISOU 1517  CG ALYS A 188     2399   3272   2678    385    153    742       C  
ATOM   1518  CD ALYS A 188      19.169  20.451   2.517  0.59 25.02           C  
ANISOU 1518  CD ALYS A 188     2696   3642   3167    212    463    419       C  
ATOM   1519  CE ALYS A 188      20.273  20.374   3.542  0.59 27.81           C  
ANISOU 1519  CE ALYS A 188     2932   4188   3447    132    289    388       C  
ATOM   1520  NZ ALYS A 188      20.135  19.300   4.555  0.59 27.53           N  
ANISOU 1520  NZ ALYS A 188     2700   4016   3747     60    501    443       N  
ATOM   1521  CG BLYS A 188      17.775  20.566   3.142  0.41 16.57           C  
ANISOU 1521  CG BLYS A 188     1335   2802   2160    184    541    506       C  
ATOM   1522  CD BLYS A 188      18.757  19.770   2.297  0.41 16.76           C  
ANISOU 1522  CD BLYS A 188     1736   2385   2248    101    450    215       C  
ATOM   1523  CE BLYS A 188      19.515  18.714   3.097  0.41 17.21           C  
ANISOU 1523  CE BLYS A 188     1792   2462   2286    230    410    109       C  
ATOM   1524  NZ BLYS A 188      18.622  17.552   3.461  0.41 15.05           N  
ANISOU 1524  NZ BLYS A 188     1893   2163   1662    501    622     75       N  
ATOM   1525  N   VAL A 189      13.797  23.572   2.959  1.00 11.47           N  
ANISOU 1525  N   VAL A 189     1354   1696   1308    -33    250    459       N  
ATOM   1526  CA  VAL A 189      12.897  24.550   2.350  1.00 11.28           C  
ANISOU 1526  CA  VAL A 189     1377   1611   1299   -117    247    455       C  
ATOM   1527  C   VAL A 189      13.705  25.720   1.784  1.00 12.00           C  
ANISOU 1527  C   VAL A 189     1649   1762   1148   -298    202    421       C  
ATOM   1528  O   VAL A 189      14.656  26.223   2.400  1.00 13.59           O  
ANISOU 1528  O   VAL A 189     1788   2029   1346   -465    172    481       O  
ATOM   1529  CB  VAL A 189      11.867  25.035   3.401  1.00 10.64           C  
ANISOU 1529  CB  VAL A 189     1469   1530   1042   -188    113    392       C  
ATOM   1530  CG1 VAL A 189      11.062  26.237   2.868  1.00 11.63           C  
ANISOU 1530  CG1 VAL A 189     1625   1503   1293    -64    248    431       C  
ATOM   1531  CG2 VAL A 189      10.940  23.899   3.817  1.00 10.61           C  
ANISOU 1531  CG2 VAL A 189     1394   1438   1198   -100    196    509       C  
ATOM   1532  N   THR A 190      13.304  26.145   0.566  1.00 12.75           N  
ANISOU 1532  N   THR A 190     1729   1893   1223   -212    157    551       N  
ATOM   1533  CA  THR A 190      13.987  27.222  -0.160  1.00 13.88           C  
ANISOU 1533  CA  THR A 190     2026   2021   1226   -287    261    594       C  
ATOM   1534  C   THR A 190      13.234  28.536  -0.078  1.00 14.27           C  
ANISOU 1534  C   THR A 190     2010   2091   1322   -224    298    593       C  
ATOM   1535  O   THR A 190      12.000  28.640   0.049  1.00 13.91           O  
ANISOU 1535  O   THR A 190     1972   1961   1351   -142    215    669       O  
ATOM   1536  CB  THR A 190      14.201  26.808  -1.629  1.00 14.51           C  
ANISOU 1536  CB  THR A 190     2068   2063   1382   -161    301    479       C  
ATOM   1537  OG1 THR A 190      12.906  26.414  -2.142  1.00 15.38           O  
ANISOU 1537  OG1 THR A 190     2088   2412   1343   -188    229    672       O  
ATOM   1538  CG2 THR A 190      15.221  25.697  -1.745  1.00 15.10           C  
ANISOU 1538  CG2 THR A 190     1948   2237   1553   -173    302    448       C  
ATOM   1539  N   GLN A 191      14.012  29.625  -0.300  1.00 15.90           N  
ANISOU 1539  N   GLN A 191     2195   2230   1615   -334    281    603       N  
ATOM   1540  CA  GLN A 191      13.432  30.956  -0.343  1.00 18.27           C  
ANISOU 1540  CA  GLN A 191     2502   2436   2002   -116     87    463       C  
ATOM   1541  C   GLN A 191      12.427  31.103  -1.484  1.00 15.44           C  
ANISOU 1541  C   GLN A 191     2182   1849   1835   -308    229    550       C  
ATOM   1542  O   GLN A 191      12.714  30.663  -2.616  1.00 16.96           O  
ANISOU 1542  O   GLN A 191     2455   2271   1719   -225    180    586       O  
ATOM   1543  CB  GLN A 191      14.543  32.020  -0.544  1.00 25.02           C  
ANISOU 1543  CB  GLN A 191     3183   3224   3098   -610    186    653       C  
ATOM   1544  CG AGLN A 191      13.994  33.409  -0.259  0.69 34.77           C  
ANISOU 1544  CG AGLN A 191     4745   4042   4423    317    256    457       C  
ATOM   1545  CD AGLN A 191      15.041  34.436   0.129  0.69 41.19           C  
ANISOU 1545  CD AGLN A 191     5402   4945   5302   -160    -71    381       C  
ATOM   1546  OE1AGLN A 191      16.157  34.415  -0.376  0.69 43.27           O  
ANISOU 1546  OE1AGLN A 191     5551   5297   5592    -63    100    329       O  
ATOM   1547  NE2AGLN A 191      14.658  35.342   1.025  0.69 43.51           N  
ANISOU 1547  NE2AGLN A 191     5714   5323   5496     49    115    297       N  
ATOM   1548  CG BGLN A 191      15.372  32.300   0.691  0.31 28.06           C  
ANISOU 1548  CG BGLN A 191     3771   3766   3125    -41    -20    378       C  
ATOM   1549  CD BGLN A 191      16.635  33.070   0.332  0.31 30.35           C  
ANISOU 1549  CD BGLN A 191     3913   4125   3492   -152     59    346       C  
ATOM   1550  OE1BGLN A 191      17.526  32.502  -0.301  0.31 31.34           O  
ANISOU 1550  OE1BGLN A 191     4010   4260   3639   -101    120    279       O  
ATOM   1551  NE2BGLN A 191      16.678  34.328   0.734  0.31 30.96           N  
ANISOU 1551  NE2BGLN A 191     4144   4116   3502    -60    141    367       N  
ATOM   1552  N   GLY A 192      11.271  31.665  -1.232  1.00 14.42           N  
ANISOU 1552  N   GLY A 192     2123   1750   1606   -296    106    622       N  
ATOM   1553  CA  GLY A 192      10.237  31.925  -2.224  1.00 14.97           C  
ANISOU 1553  CA  GLY A 192     2239   1864   1584   -189    111    634       C  
ATOM   1554  C   GLY A 192       9.338  30.747  -2.528  1.00 13.93           C  
ANISOU 1554  C   GLY A 192     2097   1791   1405    -66    179    531       C  
ATOM   1555  O   GLY A 192       8.386  30.872  -3.334  1.00 15.29           O  
ANISOU 1555  O   GLY A 192     2371   1846   1592     17     26    616       O  
ATOM   1556  N   SER A 193       9.518  29.615  -1.794  1.00 12.71           N  
ANISOU 1556  N   SER A 193     2165   1478   1187   -105    209    446       N  
ATOM   1557  CA  SER A 193       8.721  28.426  -2.071  1.00 12.13           C  
ANISOU 1557  CA  SER A 193     1822   1502   1284     44    140    414       C  
ATOM   1558  C   SER A 193       7.332  28.435  -1.413  1.00 11.34           C  
ANISOU 1558  C   SER A 193     1837   1453   1017    129     28    439       C  
ATOM   1559  O   SER A 193       7.028  29.291  -0.568  1.00 12.34           O  
ANISOU 1559  O   SER A 193     2044   1437   1205     -2    196    401       O  
ATOM   1560  CB  SER A 193       9.505  27.183  -1.592  1.00 12.18           C  
ANISOU 1560  CB  SER A 193     1655   1735   1238    169    119    391       C  
ATOM   1561  OG  SER A 193       9.667  27.195  -0.157  1.00 12.28           O  
ANISOU 1561  OG  SER A 193     1849   1557   1260     57    126    551       O  
ATOM   1562  N   THR A 194       6.510  27.479  -1.833  1.00 10.75           N  
ANISOU 1562  N   THR A 194     1763   1303   1017    136    173    357       N  
ATOM   1563  CA  THR A 194       5.183  27.242  -1.259  1.00 11.23           C  
ANISOU 1563  CA  THR A 194     1666   1327   1273    110      9    390       C  
ATOM   1564  C   THR A 194       5.208  25.914  -0.477  1.00 10.12           C  
ANISOU 1564  C   THR A 194     1614   1194   1036    186     85    243       C  
ATOM   1565  O   THR A 194       5.585  24.854  -1.024  1.00 10.69           O  
ANISOU 1565  O   THR A 194     1712   1380    971    262    193    233       O  
ATOM   1566  CB  THR A 194       4.079  27.195  -2.322  1.00 11.84           C  
ANISOU 1566  CB  THR A 194     1861   1393   1246    264    -58    374       C  
ATOM   1567  OG1 THR A 194       3.963  28.524  -2.890  1.00 13.09           O  
ANISOU 1567  OG1 THR A 194     2195   1557   1223    394    -54    503       O  
ATOM   1568  CG2 THR A 194       2.723  26.808  -1.779  1.00 12.54           C  
ANISOU 1568  CG2 THR A 194     1816   1349   1599    279    -98    446       C  
ATOM   1569  N   CYS A 195       4.781  25.983   0.809  1.00  9.40           N  
ANISOU 1569  N   CYS A 195     1557   1017    998    242    171    282       N  
ATOM   1570  CA  CYS A 195       4.768  24.845   1.709  1.00  9.15           C  
ANISOU 1570  CA  CYS A 195     1525   1002    949    168     32    261       C  
ATOM   1571  C   CYS A 195       3.339  24.531   2.167  1.00  9.69           C  
ANISOU 1571  C   CYS A 195     1475   1147   1062    313     15    264       C  
ATOM   1572  O   CYS A 195       2.530  25.460   2.327  1.00 10.77           O  
ANISOU 1572  O   CYS A 195     1585   1137   1370    317    188    252       O  
ATOM   1573  CB  CYS A 195       5.604  25.134   2.968  1.00  9.71           C  
ANISOU 1573  CB  CYS A 195     1401   1188   1100     81     43    326       C  
ATOM   1574  SG  CYS A 195       7.382  25.450   2.642  1.00  9.76           S  
ANISOU 1574  SG  CYS A 195     1413   1177   1117     79    114    335       S  
ATOM   1575  N   ALA A 196       3.053  23.270   2.439  1.00  8.71           N  
ANISOU 1575  N   ALA A 196     1199   1140    972    304    101    274       N  
ATOM   1576  CA  ALA A 196       1.793  22.843   3.068  1.00  8.88           C  
ANISOU 1576  CA  ALA A 196     1195   1139   1041    243     20    246       C  
ATOM   1577  C   ALA A 196       2.117  22.033   4.319  1.00  8.18           C  
ANISOU 1577  C   ALA A 196     1113    964   1031    205     57    342       C  
ATOM   1578  O   ALA A 196       2.936  21.092   4.253  1.00  9.55           O  
ANISOU 1578  O   ALA A 196     1399   1195   1033    351    115    266       O  
ATOM   1579  CB  ALA A 196       0.929  22.003   2.144  1.00 10.05           C  
ANISOU 1579  CB  ALA A 196     1389   1257   1172     75    -26    260       C  
ATOM   1580  N   VAL A 197       1.500  22.365   5.457  1.00  8.72           N  
ANISOU 1580  N   VAL A 197     1225   1072   1017    250     16    237       N  
ATOM   1581  CA  VAL A 197       1.772  21.712   6.750  1.00  7.92           C  
ANISOU 1581  CA  VAL A 197     1052    993    964    180     23    231       C  
ATOM   1582  C   VAL A 197       0.478  21.089   7.267  1.00  8.35           C  
ANISOU 1582  C   VAL A 197     1016   1085   1073    145     65    131       C  
ATOM   1583  O   VAL A 197      -0.470  21.822   7.580  1.00  9.06           O  
ANISOU 1583  O   VAL A 197     1143   1118   1182    230    118    157       O  
ATOM   1584  CB  VAL A 197       2.366  22.708   7.748  1.00  8.67           C  
ANISOU 1584  CB  VAL A 197     1253    992   1048    144     58    178       C  
ATOM   1585  CG1 VAL A 197       2.654  22.014   9.094  1.00  9.25           C  
ANISOU 1585  CG1 VAL A 197     1391   1065   1060    134     58    152       C  
ATOM   1586  CG2 VAL A 197       3.620  23.424   7.235  1.00  9.27           C  
ANISOU 1586  CG2 VAL A 197     1354   1068   1100     81     97    172       C  
ATOM   1587  N   PHE A 198       0.445  19.742   7.330  1.00  8.21           N  
ANISOU 1587  N   PHE A 198     1071   1017   1031     91    131    229       N  
ATOM   1588  CA  PHE A 198      -0.690  19.012   7.822  1.00  8.44           C  
ANISOU 1588  CA  PHE A 198     1088   1081   1040    112     89    242       C  
ATOM   1589  C   PHE A 198      -0.556  18.737   9.313  1.00  8.01           C  
ANISOU 1589  C   PHE A 198     1056    954   1032     15    -40    177       C  
ATOM   1590  O   PHE A 198       0.334  17.986   9.733  1.00  8.91           O  
ANISOU 1590  O   PHE A 198     1174   1116   1095    188     37    249       O  
ATOM   1591  CB  PHE A 198      -0.851  17.656   7.100  1.00  9.21           C  
ANISOU 1591  CB  PHE A 198     1188   1290   1022    118     61    118       C  
ATOM   1592  CG  PHE A 198      -1.238  17.752   5.630  1.00  9.99           C  
ANISOU 1592  CG  PHE A 198     1313   1395   1089    186     92     77       C  
ATOM   1593  CD1 PHE A 198      -0.406  18.221   4.630  1.00 10.54           C  
ANISOU 1593  CD1 PHE A 198     1504   1444   1056    171    157    -20       C  
ATOM   1594  CD2 PHE A 198      -2.508  17.331   5.247  1.00 13.64           C  
ANISOU 1594  CD2 PHE A 198     1626   2191   1365     36   -121    -24       C  
ATOM   1595  CE1 PHE A 198      -0.788  18.287   3.293  1.00 11.77           C  
ANISOU 1595  CE1 PHE A 198     1780   1471   1221    255    120     16       C  
ATOM   1596  CE2 PHE A 198      -2.895  17.386   3.924  1.00 15.00           C  
ANISOU 1596  CE2 PHE A 198     1669   2555   1475     50   -191    -33       C  
ATOM   1597  CZ  PHE A 198      -2.045  17.856   2.958  1.00 13.72           C  
ANISOU 1597  CZ  PHE A 198     1925   2000   1286    338   -194    120       C  
ATOM   1598  N   GLY A 199      -1.443  19.341  10.132  1.00  8.56           N  
ANISOU 1598  N   GLY A 199     1166   1100    987    243     40    180       N  
ATOM   1599  CA  GLY A 199      -1.418  19.219  11.586  1.00  8.32           C  
ANISOU 1599  CA  GLY A 199      988   1157   1015     66     42    182       C  
ATOM   1600  C   GLY A 199      -0.774  20.427  12.198  1.00  8.08           C  
ANISOU 1600  C   GLY A 199     1023   1023   1023      0      0      0       C  
ATOM   1601  O   GLY A 199       0.391  20.761  11.946  1.00  9.43           O  
ANISOU 1601  O   GLY A 199     1140   1266   1178     -3     95     58       O  
ATOM   1602  N   LEU A 200      -1.557  21.142  13.063  1.00  8.52           N  
ANISOU 1602  N   LEU A 200     1182   1060    994    111    155    145       N  
ATOM   1603  CA  LEU A 200      -1.179  22.423  13.631  1.00  8.51           C  
ANISOU 1603  CA  LEU A 200     1090   1138   1007    126     61    119       C  
ATOM   1604  C   LEU A 200      -1.063  22.388  15.147  1.00  9.03           C  
ANISOU 1604  C   LEU A 200     1174   1116   1142    103    181    169       C  
ATOM   1605  O   LEU A 200      -1.445  23.330  15.860  1.00 10.07           O  
ANISOU 1605  O   LEU A 200     1410   1204   1213    193     97    102       O  
ATOM   1606  CB  LEU A 200      -2.145  23.526  13.119  1.00  9.20           C  
ANISOU 1606  CB  LEU A 200     1046   1268   1181    128     87    267       C  
ATOM   1607  CG  LEU A 200      -2.229  23.650  11.583  1.00  9.88           C  
ANISOU 1607  CG  LEU A 200     1314   1219   1221    156    -26    302       C  
ATOM   1608  CD1 LEU A 200      -3.295  24.656  11.192  1.00 11.35           C  
ANISOU 1608  CD1 LEU A 200     1472   1352   1490    223    -96    335       C  
ATOM   1609  CD2 LEU A 200      -0.880  23.995  10.934  1.00 10.40           C  
ANISOU 1609  CD2 LEU A 200     1257   1458   1236     -7     25    230       C  
ATOM   1610  N   GLY A 201      -0.554  21.257  15.664  1.00  8.50           N  
ANISOU 1610  N   GLY A 201     1181   1015   1034     22     91    215       N  
ATOM   1611  CA  GLY A 201      -0.155  21.153  17.066  1.00  8.76           C  
ANISOU 1611  CA  GLY A 201     1232   1073   1024    156    157    180       C  
ATOM   1612  C   GLY A 201       1.229  21.687  17.328  1.00  8.22           C  
ANISOU 1612  C   GLY A 201     1242    892    991    119    180    169       C  
ATOM   1613  O   GLY A 201       1.793  22.414  16.486  1.00  9.20           O  
ANISOU 1613  O   GLY A 201     1405    964   1128    118    260    222       O  
ATOM   1614  N   GLY A 202       1.821  21.381  18.482  1.00  8.14           N  
ANISOU 1614  N   GLY A 202     1235    942    917     72    191    127       N  
ATOM   1615  CA  GLY A 202       3.137  21.942  18.810  1.00  8.77           C  
ANISOU 1615  CA  GLY A 202     1228   1042   1061     79    122     78       C  
ATOM   1616  C   GLY A 202       4.206  21.650  17.746  1.00  7.95           C  
ANISOU 1616  C   GLY A 202     1106    887   1026    -18    185    100       C  
ATOM   1617  O   GLY A 202       5.044  22.512  17.437  1.00  8.53           O  
ANISOU 1617  O   GLY A 202     1105    931   1204    -62    132     93       O  
ATOM   1618  N   VAL A 203       4.209  20.422  17.230  1.00  7.68           N  
ANISOU 1618  N   VAL A 203     1127    792   1000    -22    131    210       N  
ATOM   1619  CA  VAL A 203       5.218  20.068  16.197  1.00  7.54           C  
ANISOU 1619  CA  VAL A 203     1086    865    914      3     90    185       C  
ATOM   1620  C   VAL A 203       4.941  20.767  14.860  1.00  6.95           C  
ANISOU 1620  C   VAL A 203      900    735   1006   -113    108     92       C  
ATOM   1621  O   VAL A 203       5.866  21.343  14.254  1.00  7.75           O  
ANISOU 1621  O   VAL A 203     1032    841   1072    -53    134    233       O  
ATOM   1622  CB  VAL A 203       5.362  18.534  16.075  1.00  7.72           C  
ANISOU 1622  CB  VAL A 203     1066    868    998    -19    106    189       C  
ATOM   1623  CG1 VAL A 203       6.524  18.182  15.147  1.00  8.34           C  
ANISOU 1623  CG1 VAL A 203     1176    937   1055     19    116    202       C  
ATOM   1624  CG2 VAL A 203       5.567  17.882  17.435  1.00  8.47           C  
ANISOU 1624  CG2 VAL A 203     1049   1055   1116    -52      4    213       C  
ATOM   1625  N   GLY A 204       3.682  20.771  14.422  1.00  7.21           N  
ANISOU 1625  N   GLY A 204      995    785    961    -45    118    229       N  
ATOM   1626  CA  GLY A 204       3.344  21.449  13.143  1.00  7.83           C  
ANISOU 1626  CA  GLY A 204     1143    906    925     20     64    227       C  
ATOM   1627  C   GLY A 204       3.546  22.965  13.192  1.00  7.66           C  
ANISOU 1627  C   GLY A 204     1141    856    913    155     98    209       C  
ATOM   1628  O   GLY A 204       4.027  23.558  12.189  1.00  8.24           O  
ANISOU 1628  O   GLY A 204     1176    985    971     28    147    237       O  
ATOM   1629  N   LEU A 205       3.281  23.604  14.325  1.00  7.76           N  
ANISOU 1629  N   LEU A 205     1164    839    945    102    140    222       N  
ATOM   1630  CA  LEU A 205       3.587  25.026  14.469  1.00  7.69           C  
ANISOU 1630  CA  LEU A 205     1237    773    913    158     38    293       C  
ATOM   1631  C   LEU A 205       5.088  25.245  14.366  1.00  7.71           C  
ANISOU 1631  C   LEU A 205     1236    798    896     45     92    222       C  
ATOM   1632  O   LEU A 205       5.525  26.271  13.796  1.00  9.09           O  
ANISOU 1632  O   LEU A 205     1405    969   1081     49     81    287       O  
ATOM   1633  CB  LEU A 205       3.051  25.554  15.801  1.00  8.47           C  
ANISOU 1633  CB  LEU A 205     1287    898   1035     83    115    223       C  
ATOM   1634  CG  LEU A 205       1.536  25.646  15.947  1.00  8.81           C  
ANISOU 1634  CG  LEU A 205     1310   1002   1033    139     54    241       C  
ATOM   1635  CD1 LEU A 205       1.174  26.013  17.377  1.00 10.39           C  
ANISOU 1635  CD1 LEU A 205     1435   1463   1051    244    216    238       C  
ATOM   1636  CD2 LEU A 205       0.902  26.633  14.955  1.00  9.92           C  
ANISOU 1636  CD2 LEU A 205     1250   1281   1237    209    -76    281       C  
ATOM   1637  N   SER A 206       5.914  24.333  14.891  1.00  7.65           N  
ANISOU 1637  N   SER A 206     1126    862    919     58     -1    234       N  
ATOM   1638  CA  SER A 206       7.368  24.444  14.798  1.00  7.64           C  
ANISOU 1638  CA  SER A 206     1172    770    959    123    -10    123       C  
ATOM   1639  C   SER A 206       7.850  24.249  13.345  1.00  7.74           C  
ANISOU 1639  C   SER A 206     1124    848    969    -28     95    261       C  
ATOM   1640  O   SER A 206       8.828  24.896  12.902  1.00  8.23           O  
ANISOU 1640  O   SER A 206     1180    914   1034    -56     71    297       O  
ATOM   1641  CB  SER A 206       8.017  23.495  15.801  1.00  7.92           C  
ANISOU 1641  CB  SER A 206     1211    942    858    144    -25    167       C  
ATOM   1642  OG  SER A 206       7.650  23.825  17.129  1.00  8.60           O  
ANISOU 1642  OG  SER A 206     1371   1008    890    142     24    201       O  
ATOM   1643  N   VAL A 207       7.192  23.367  12.574  1.00  7.85           N  
ANISOU 1643  N   VAL A 207     1179    918    887     32     48    226       N  
ATOM   1644  CA  VAL A 207       7.450  23.257  11.124  1.00  7.66           C  
ANISOU 1644  CA  VAL A 207     1034    923    955    -34     95    259       C  
ATOM   1645  C   VAL A 207       7.155  24.610  10.439  1.00  7.67           C  
ANISOU 1645  C   VAL A 207     1157    904    853    -37     89    270       C  
ATOM   1646  O   VAL A 207       7.977  25.088   9.630  1.00  8.60           O  
ANISOU 1646  O   VAL A 207     1288    968   1011     -1    178    324       O  
ATOM   1647  CB  VAL A 207       6.602  22.142  10.460  1.00  7.46           C  
ANISOU 1647  CB  VAL A 207      972    900    960    -40     42    281       C  
ATOM   1648  CG1 VAL A 207       6.790  22.161   8.936  1.00  8.75           C  
ANISOU 1648  CG1 VAL A 207     1288   1002   1037    -69     -5    279       C  
ATOM   1649  CG2 VAL A 207       6.983  20.757  10.994  1.00  7.60           C  
ANISOU 1649  CG2 VAL A 207     1035    951    901     61     -4    162       C  
ATOM   1650  N   ILE A 208       6.014  25.251  10.752  1.00  7.88           N  
ANISOU 1650  N   ILE A 208     1237    802    953     16    114    263       N  
ATOM   1651  CA  ILE A 208       5.712  26.579  10.195  1.00  8.56           C  
ANISOU 1651  CA  ILE A 208     1285    917   1048      7      7    351       C  
ATOM   1652  C   ILE A 208       6.810  27.572  10.531  1.00  9.08           C  
ANISOU 1652  C   ILE A 208     1284   1113   1052    -25     67    330       C  
ATOM   1653  O   ILE A 208       7.290  28.335   9.661  1.00  9.82           O  
ANISOU 1653  O   ILE A 208     1514   1055   1162    -55    112    355       O  
ATOM   1654  CB  ILE A 208       4.321  27.092  10.630  1.00  8.66           C  
ANISOU 1654  CB  ILE A 208     1271    967   1051     48     51    286       C  
ATOM   1655  CG1 ILE A 208       3.217  26.208  10.049  1.00  9.43           C  
ANISOU 1655  CG1 ILE A 208     1242   1079   1261     30     26    363       C  
ATOM   1656  CG2 ILE A 208       4.132  28.564  10.260  1.00  9.86           C  
ANISOU 1656  CG2 ILE A 208     1511   1008   1228     82    120    291       C  
ATOM   1657  CD1 ILE A 208       1.820  26.491  10.569  1.00 11.59           C  
ANISOU 1657  CD1 ILE A 208     1414   1478   1513    149     43    384       C  
ATOM   1658  N   MET A 209       7.252  27.605  11.806  1.00  8.82           N  
ANISOU 1658  N   MET A 209     1553    831    967    -50      8    198       N  
ATOM   1659  CA  MET A 209       8.357  28.487  12.191  1.00  9.47           C  
ANISOU 1659  CA  MET A 209     1619    946   1032    -60     61    192       C  
ATOM   1660  C   MET A 209       9.570  28.256  11.304  1.00  9.61           C  
ANISOU 1660  C   MET A 209     1541   1012   1099   -215     78    232       C  
ATOM   1661  O   MET A 209      10.228  29.236  10.829  1.00 10.84           O  
ANISOU 1661  O   MET A 209     1778   1135   1207   -249     31    287       O  
ATOM   1662  CB  MET A 209       8.753  28.299  13.656  1.00  9.32           C  
ANISOU 1662  CB  MET A 209     1513    983   1046   -153     60    285       C  
ATOM   1663  CG  MET A 209       7.702  28.722  14.678  1.00 10.54           C  
ANISOU 1663  CG  MET A 209     1819   1120   1067    -54    133    219       C  
ATOM   1664  SD  MET A 209       8.232  28.225  16.349  1.00 10.13           S  
ANISOU 1664  SD  MET A 209     1703   1109   1037    -30    108    231       S  
ATOM   1665  CE  MET A 209       6.906  28.943  17.347  1.00 12.08           C  
ANISOU 1665  CE  MET A 209     1813   1509   1267    -38    168     72       C  
ATOM   1666  N   GLY A 210       9.953  27.003  11.075  1.00  9.25           N  
ANISOU 1666  N   GLY A 210     1400   1049   1064   -117    163    220       N  
ATOM   1667  CA  GLY A 210      11.107  26.700  10.224  1.00  9.80           C  
ANISOU 1667  CA  GLY A 210     1611   1088   1025    -92    153    222       C  
ATOM   1668  C   GLY A 210      10.899  27.096   8.749  1.00  9.50           C  
ANISOU 1668  C   GLY A 210     1367   1129   1114   -175     90    281       C  
ATOM   1669  O   GLY A 210      11.840  27.630   8.110  1.00 11.10           O  
ANISOU 1669  O   GLY A 210     1595   1316   1307   -217    158    353       O  
ATOM   1670  N   CYS A 211       9.712  26.870   8.195  1.00  9.24           N  
ANISOU 1670  N   CYS A 211     1358   1138   1016   -182     99    262       N  
ATOM   1671  CA  CYS A 211       9.442  27.279   6.815  1.00  9.82           C  
ANISOU 1671  CA  CYS A 211     1517   1201   1012   -112    162    320       C  
ATOM   1672  C   CYS A 211       9.569  28.804   6.685  1.00 10.96           C  
ANISOU 1672  C   CYS A 211     1646   1298   1219   -165     66    360       C  
ATOM   1673  O   CYS A 211      10.105  29.309   5.668  1.00 12.08           O  
ANISOU 1673  O   CYS A 211     1996   1402   1193   -240    128    480       O  
ATOM   1674  CB  CYS A 211       8.035  26.853   6.375  1.00  9.79           C  
ANISOU 1674  CB  CYS A 211     1591   1087   1041   -106     41    403       C  
ATOM   1675  SG  CYS A 211       7.805  25.054   6.183  1.00  8.80           S  
ANISOU 1675  SG  CYS A 211     1321   1063    960   -109     23    330       S  
ATOM   1676  N   LYS A 212       9.066  29.555   7.653  1.00 10.41           N  
ANISOU 1676  N   LYS A 212     1675   1067   1212   -188    -10    404       N  
ATOM   1677  CA  LYS A 212       9.150  31.023   7.599  1.00 12.24           C  
ANISOU 1677  CA  LYS A 212     2051   1100   1498    -70    -40    431       C  
ATOM   1678  C   LYS A 212      10.617  31.429   7.723  1.00 13.03           C  
ANISOU 1678  C   LYS A 212     2187   1220   1543   -358   -101    478       C  
ATOM   1679  O   LYS A 212      11.106  32.305   6.957  1.00 14.01           O  
ANISOU 1679  O   LYS A 212     2261   1421   1643   -482     88    602       O  
ATOM   1680  CB ALYS A 212       8.214  31.641   8.633  0.52 12.30           C  
ANISOU 1680  CB ALYS A 212     2022   1016   1635   -125    -48    282       C  
ATOM   1681  CG ALYS A 212       8.232  33.178   8.527  0.52 13.77           C  
ANISOU 1681  CG ALYS A 212     2066   1129   2037   -137    -59    133       C  
ATOM   1682  CD ALYS A 212       7.278  33.865   9.468  0.52 14.46           C  
ANISOU 1682  CD ALYS A 212     2245   1223   2028    -93    -45    110       C  
ATOM   1683  CE ALYS A 212       7.305  35.389   9.296  0.52 16.78           C  
ANISOU 1683  CE ALYS A 212     2593   1259   2525    101    -32    143       C  
ATOM   1684  NZ ALYS A 212       6.724  35.840   8.005  0.52 20.64           N  
ANISOU 1684  NZ ALYS A 212     3260   2086   2498   -172   -198    104       N  
ATOM   1685  CB BLYS A 212       8.381  31.664   8.763  0.48 14.56           C  
ANISOU 1685  CB BLYS A 212     2243   1458   1830     72     36    227       C  
ATOM   1686  CG BLYS A 212       8.671  33.178   8.804  0.48 16.99           C  
ANISOU 1686  CG BLYS A 212     2550   1572   2334    140   -234    194       C  
ATOM   1687  CD BLYS A 212       7.867  33.905   9.848  0.48 19.39           C  
ANISOU 1687  CD BLYS A 212     2630   2198   2538    261    -88    145       C  
ATOM   1688  CE BLYS A 212       8.007  35.425   9.666  0.48 21.58           C  
ANISOU 1688  CE BLYS A 212     3051   2233   2914     91    -58     68       C  
ATOM   1689  NZ BLYS A 212       6.903  36.086  10.420  0.48 22.11           N  
ANISOU 1689  NZ BLYS A 212     3114   2272   3017    199    -81     74       N  
ATOM   1690  N   ALA A 213      11.383  30.827   8.633  1.00 11.76           N  
ANISOU 1690  N   ALA A 213     1791   1310   1369   -335    -80    345       N  
ATOM   1691  CA  ALA A 213      12.809  31.136   8.811  1.00 12.61           C  
ANISOU 1691  CA  ALA A 213     1989   1514   1289   -537   -100    268       C  
ATOM   1692  C   ALA A 213      13.623  30.880   7.533  1.00 13.50           C  
ANISOU 1692  C   ALA A 213     2029   1684   1416   -579     92    240       C  
ATOM   1693  O   ALA A 213      14.619  31.608   7.258  1.00 16.31           O  
ANISOU 1693  O   ALA A 213     2298   2175   1726   -841    152    352       O  
ATOM   1694  CB  ALA A 213      13.399  30.374  10.008  1.00 14.13           C  
ANISOU 1694  CB  ALA A 213     2227   1744   1399   -499   -165    423       C  
ATOM   1695  N   ALA A 214      13.241  29.874   6.763  1.00 13.32           N  
ANISOU 1695  N   ALA A 214     1965   1785   1311   -408     87    201       N  
ATOM   1696  CA  ALA A 214      13.878  29.522   5.509  1.00 14.64           C  
ANISOU 1696  CA  ALA A 214     2233   1961   1370   -464    247    306       C  
ATOM   1697  C   ALA A 214      13.472  30.432   4.343  1.00 15.18           C  
ANISOU 1697  C   ALA A 214     2369   2005   1393   -552    263    291       C  
ATOM   1698  O   ALA A 214      14.001  30.267   3.224  1.00 18.73           O  
ANISOU 1698  O   ALA A 214     2967   2607   1543   -579    511    419       O  
ATOM   1699  CB  ALA A 214      13.533  28.063   5.191  1.00 15.50           C  
ANISOU 1699  CB  ALA A 214     2412   1998   1478   -365    391    154       C  
ATOM   1700  N   GLY A 215      12.506  31.323   4.542  1.00 15.03           N  
ANISOU 1700  N   GLY A 215     2344   1831   1537   -586    178    647       N  
ATOM   1701  CA  GLY A 215      12.156  32.282   3.494  1.00 16.20           C  
ANISOU 1701  CA  GLY A 215     2557   2029   1570   -689     60    732       C  
ATOM   1702  C   GLY A 215      11.002  31.834   2.608  1.00 14.89           C  
ANISOU 1702  C   GLY A 215     2533   1818   1307   -537    118    603       C  
ATOM   1703  O   GLY A 215      10.835  32.396   1.511  1.00 16.00           O  
ANISOU 1703  O   GLY A 215     2817   1800   1461   -256    171    764       O  
ATOM   1704  N   ALA A 216      10.185  30.841   2.990  1.00 14.09           N  
ANISOU 1704  N   ALA A 216     2347   1683   1323   -481    198    491       N  
ATOM   1705  CA  ALA A 216       9.039  30.470   2.175  1.00 12.60           C  
ANISOU 1705  CA  ALA A 216     1966   1361   1461   -168    274    403       C  
ATOM   1706  C   ALA A 216       8.135  31.681   1.898  1.00 13.28           C  
ANISOU 1706  C   ALA A 216     2174   1449   1423    -99    221    238       C  
ATOM   1707  O   ALA A 216       7.922  32.481   2.805  1.00 15.73           O  
ANISOU 1707  O   ALA A 216     2921   1432   1625    -27    258    186       O  
ATOM   1708  CB  ALA A 216       8.248  29.331   2.828  1.00 12.61           C  
ANISOU 1708  CB  ALA A 216     1961   1402   1430   -156    211    528       C  
ATOM   1709  N   ALA A 217       7.566  31.761   0.681  1.00 12.93           N  
ANISOU 1709  N   ALA A 217     2021   1436   1456     91    141    400       N  
ATOM   1710  CA  ALA A 217       6.626  32.831   0.367  1.00 13.46           C  
ANISOU 1710  CA  ALA A 217     2152   1351   1612     49    127    431       C  
ATOM   1711  C   ALA A 217       5.201  32.520   0.787  1.00 13.13           C  
ANISOU 1711  C   ALA A 217     2147   1360   1483    122    185    277       C  
ATOM   1712  O   ALA A 217       4.405  33.415   1.134  1.00 14.90           O  
ANISOU 1712  O   ALA A 217     2431   1317   1913    282    279    389       O  
ATOM   1713  CB  ALA A 217       6.618  33.084  -1.149  1.00 15.99           C  
ANISOU 1713  CB  ALA A 217     2567   1843   1665    204    232    675       C  
ATOM   1714  N   ARG A 218       4.806  31.237   0.783  1.00 11.75           N  
ANISOU 1714  N   ARG A 218     1892   1256   1315    125    125    304       N  
ATOM   1715  CA  ARG A 218       3.448  30.811   1.120  1.00 10.79           C  
ANISOU 1715  CA  ARG A 218     1824   1088   1186    253     54    347       C  
ATOM   1716  C   ARG A 218       3.563  29.592   2.016  1.00  9.90           C  
ANISOU 1716  C   ARG A 218     1669    975   1118    242     76    243       C  
ATOM   1717  O   ARG A 218       4.354  28.689   1.751  1.00 10.65           O  
ANISOU 1717  O   ARG A 218     1846   1082   1120    306    124    319       O  
ATOM   1718  CB  ARG A 218       2.597  30.458  -0.117  1.00 14.36           C  
ANISOU 1718  CB  ARG A 218     2580   1485   1392    344   -283    243       C  
ATOM   1719  CG  ARG A 218       2.187  31.638  -0.990  1.00 15.86           C  
ANISOU 1719  CG  ARG A 218     2534   1695   1797    359   -360    342       C  
ATOM   1720  CD  ARG A 218       1.335  31.238  -2.180  1.00 17.02           C  
ANISOU 1720  CD  ARG A 218     2531   2023   1913    357   -543    292       C  
ATOM   1721  NE  ARG A 218       0.025  30.689  -1.822  1.00 17.21           N  
ANISOU 1721  NE  ARG A 218     2562   2066   1912    404   -380    -32       N  
ATOM   1722  CZ  ARG A 218      -0.803  30.123  -2.710  1.00 15.53           C  
ANISOU 1722  CZ  ARG A 218     2609   1647   1645    448   -364    192       C  
ATOM   1723  NH1 ARG A 218      -0.410  29.995  -3.981  1.00 17.91           N  
ANISOU 1723  NH1 ARG A 218     2783   2420   1603    645   -314    207       N  
ATOM   1724  NH2 ARG A 218      -1.979  29.701  -2.325  1.00 17.44           N  
ANISOU 1724  NH2 ARG A 218     2851   2349   1424    147   -331    272       N  
ATOM   1725  N   ILE A 219       2.771  29.571   3.094  1.00 10.00           N  
ANISOU 1725  N   ILE A 219     1672   1007   1121    199     53    284       N  
ATOM   1726  CA  ILE A 219       2.758  28.468   4.065  1.00  9.28           C  
ANISOU 1726  CA  ILE A 219     1449    895   1181    165    -36    257       C  
ATOM   1727  C   ILE A 219       1.302  28.170   4.375  1.00  9.54           C  
ANISOU 1727  C   ILE A 219     1512   1073   1040    147     36    265       C  
ATOM   1728  O   ILE A 219       0.617  28.968   5.061  1.00 11.12           O  
ANISOU 1728  O   ILE A 219     1706   1256   1262    257    129    159       O  
ATOM   1729  CB  ILE A 219       3.535  28.773   5.351  1.00 10.21           C  
ANISOU 1729  CB  ILE A 219     1492   1186   1202    170    -54    273       C  
ATOM   1730  CG1 ILE A 219       5.008  29.149   5.066  1.00 10.70           C  
ANISOU 1730  CG1 ILE A 219     1551   1318   1197    131     24    341       C  
ATOM   1731  CG2 ILE A 219       3.496  27.555   6.281  1.00 11.45           C  
ANISOU 1731  CG2 ILE A 219     1784   1371   1196    161    -12    345       C  
ATOM   1732  CD1 ILE A 219       5.719  29.813   6.226  1.00 12.23           C  
ANISOU 1732  CD1 ILE A 219     1549   1615   1481    129     31     91       C  
ATOM   1733  N   ILE A 220       0.765  27.072   3.857  1.00  9.39           N  
ANISOU 1733  N   ILE A 220     1366   1079   1121    181    -45    188       N  
ATOM   1734  CA  ILE A 220      -0.643  26.704   3.948  1.00  9.13           C  
ANISOU 1734  CA  ILE A 220     1386    983   1099    273      2    195       C  
ATOM   1735  C   ILE A 220      -0.815  25.717   5.108  1.00  9.08           C  
ANISOU 1735  C   ILE A 220     1351   1021   1078    225      2    172       C  
ATOM   1736  O   ILE A 220      -0.295  24.576   5.040  1.00 10.08           O  
ANISOU 1736  O   ILE A 220     1480   1116   1233    384    140    260       O  
ATOM   1737  CB  ILE A 220      -1.192  26.123   2.633  1.00 10.11           C  
ANISOU 1737  CB  ILE A 220     1445   1182   1216    254   -132    168       C  
ATOM   1738  CG1 ILE A 220      -0.919  27.031   1.439  1.00 11.57           C  
ANISOU 1738  CG1 ILE A 220     1737   1468   1190    238    -20    185       C  
ATOM   1739  CG2 ILE A 220      -2.673  25.800   2.796  1.00 11.13           C  
ANISOU 1739  CG2 ILE A 220     1403   1473   1353    235    -94     96       C  
ATOM   1740  CD1 ILE A 220      -1.070  26.359   0.073  1.00 14.06           C  
ANISOU 1740  CD1 ILE A 220     1966   2183   1195    467    -47     91       C  
ATOM   1741  N   GLY A 221      -1.493  26.113   6.188  1.00  9.48           N  
ANISOU 1741  N   GLY A 221     1452   1100   1049    255     81    196       N  
ATOM   1742  CA  GLY A 221      -1.777  25.183   7.288  1.00  9.18           C  
ANISOU 1742  CA  GLY A 221     1368   1082   1040    251     14    237       C  
ATOM   1743  C   GLY A 221      -3.041  24.384   7.020  1.00  9.93           C  
ANISOU 1743  C   GLY A 221     1236   1230   1306    311      2    310       C  
ATOM   1744  O   GLY A 221      -4.030  24.914   6.485  1.00 12.77           O  
ANISOU 1744  O   GLY A 221     1391   1496   1964    356   -121    461       O  
ATOM   1745  N   VAL A 222      -3.034  23.081   7.356  1.00  8.83           N  
ANISOU 1745  N   VAL A 222     1055   1161   1139    169     22    193       N  
ATOM   1746  CA  VAL A 222      -4.158  22.196   7.123  1.00  9.55           C  
ANISOU 1746  CA  VAL A 222     1191   1366   1070    110    -29    188       C  
ATOM   1747  C   VAL A 222      -4.519  21.530   8.449  1.00  9.71           C  
ANISOU 1747  C   VAL A 222     1147   1370   1170    279      5    289       C  
ATOM   1748  O   VAL A 222      -3.676  20.838   9.066  1.00 10.46           O  
ANISOU 1748  O   VAL A 222     1167   1451   1357    156     86    437       O  
ATOM   1749  CB  VAL A 222      -3.817  21.124   6.054  1.00 10.11           C  
ANISOU 1749  CB  VAL A 222     1225   1541   1073    258   -103     91       C  
ATOM   1750  CG1 VAL A 222      -5.036  20.271   5.756  1.00 11.93           C  
ANISOU 1750  CG1 VAL A 222     1526   1620   1385    249   -282     86       C  
ATOM   1751  CG2 VAL A 222      -3.239  21.762   4.784  1.00 11.03           C  
ANISOU 1751  CG2 VAL A 222     1384   1663   1143    190    -19     83       C  
ATOM   1752  N   ASP A 223      -5.760  21.675   8.920  1.00  9.89           N  
ANISOU 1752  N   ASP A 223     1161   1473   1123    285    -29    307       N  
ATOM   1753  CA  ASP A 223      -6.196  21.025  10.156  1.00 10.23           C  
ANISOU 1753  CA  ASP A 223     1186   1395   1306    129    -10    285       C  
ATOM   1754  C   ASP A 223      -7.722  20.902  10.107  1.00  9.99           C  
ANISOU 1754  C   ASP A 223     1117   1462   1217    100    -23    199       C  
ATOM   1755  O   ASP A 223      -8.397  21.797   9.596  1.00 11.99           O  
ANISOU 1755  O   ASP A 223     1234   1842   1479    190     15    314       O  
ATOM   1756  CB  ASP A 223      -5.716  21.788  11.422  1.00 10.73           C  
ANISOU 1756  CB  ASP A 223     1318   1448   1312    195     14    204       C  
ATOM   1757  CG  ASP A 223      -5.562  20.962  12.682  1.00  9.94           C  
ANISOU 1757  CG  ASP A 223     1092   1415   1271     82      5    192       C  
ATOM   1758  OD1 ASP A 223      -6.610  20.356  13.083  1.00 10.72           O  
ANISOU 1758  OD1 ASP A 223     1054   1643   1377     96     16    383       O  
ATOM   1759  OD2 ASP A 223      -4.461  20.886  13.260  1.00 10.26           O  
ANISOU 1759  OD2 ASP A 223     1105   1567   1224    168     17    155       O  
ATOM   1760  N   ILE A 224      -8.269  19.823  10.684  1.00 11.63           N  
ANISOU 1760  N   ILE A 224     1193   1678   1547    100     84    309       N  
ATOM   1761  CA  ILE A 224      -9.712  19.659  10.829  1.00 12.43           C  
ANISOU 1761  CA  ILE A 224     1293   1849   1583    -77    134    134       C  
ATOM   1762  C   ILE A 224     -10.275  20.425  12.035  1.00 12.73           C  
ANISOU 1762  C   ILE A 224     1220   1982   1634     87    124    137       C  
ATOM   1763  O   ILE A 224     -11.530  20.540  12.140  1.00 14.37           O  
ANISOU 1763  O   ILE A 224     1242   2180   2037    124     80     52       O  
ATOM   1764  CB  ILE A 224     -10.141  18.183  10.888  1.00 14.01           C  
ANISOU 1764  CB  ILE A 224     1353   1881   2089    -79     70    183       C  
ATOM   1765  CG1 ILE A 224      -9.478  17.439  12.057  1.00 15.24           C  
ANISOU 1765  CG1 ILE A 224     1609   1912   2271     16    260    443       C  
ATOM   1766  CG2 ILE A 224      -9.895  17.482   9.557  1.00 16.23           C  
ANISOU 1766  CG2 ILE A 224     1761   2150   2257     15    151    -10       C  
ATOM   1767  CD1 ILE A 224      -9.999  16.017  12.314  1.00 18.44           C  
ANISOU 1767  CD1 ILE A 224     1965   2108   2935   -171    356    567       C  
ATOM   1768  N   ASN A 225      -9.442  20.985  12.901  1.00 12.51           N  
ANISOU 1768  N   ASN A 225     1441   1781   1532    190     64    208       N  
ATOM   1769  CA  ASN A 225      -9.863  21.795  14.014  1.00 12.97           C  
ANISOU 1769  CA  ASN A 225     1413   1852   1661    250     59    144       C  
ATOM   1770  C   ASN A 225      -9.549  23.259  13.712  1.00 12.50           C  
ANISOU 1770  C   ASN A 225     1270   1845   1633    245     28     28       C  
ATOM   1771  O   ASN A 225      -8.397  23.713  13.841  1.00 12.07           O  
ANISOU 1771  O   ASN A 225     1381   1668   1537    179     67    265       O  
ATOM   1772  CB  ASN A 225      -9.145  21.341  15.304  1.00 11.98           C  
ANISOU 1772  CB  ASN A 225     1416   1537   1599    171    228    273       C  
ATOM   1773  CG  ASN A 225      -9.630  22.133  16.503  1.00 13.39           C  
ANISOU 1773  CG  ASN A 225     1459   1974   1655    282    237    192       C  
ATOM   1774  OD1 ASN A 225     -10.414  23.102  16.388  1.00 15.12           O  
ANISOU 1774  OD1 ASN A 225     1887   2068   1788    429    339    103       O  
ATOM   1775  ND2 ASN A 225      -9.204  21.746  17.705  1.00 14.18           N  
ANISOU 1775  ND2 ASN A 225     1634   2154   1600    223    216    126       N  
ATOM   1776  N   LYS A 226     -10.581  24.039  13.295  1.00 13.45           N  
ANISOU 1776  N   LYS A 226     1493   1943   1672    393    -38    201       N  
ATOM   1777  CA  LYS A 226     -10.343  25.417  12.881  1.00 14.52           C  
ANISOU 1777  CA  LYS A 226     1611   1907   1998    443   -185    134       C  
ATOM   1778  C   LYS A 226      -9.889  26.303  14.021  1.00 13.56           C  
ANISOU 1778  C   LYS A 226     1351   1957   1844    360     70    123       C  
ATOM   1779  O   LYS A 226      -9.390  27.396  13.791  1.00 14.03           O  
ANISOU 1779  O   LYS A 226     1701   1946   1684    492      6    214       O  
ATOM   1780  CB ALYS A 226     -11.593  26.025  12.195  0.68 19.79           C  
ANISOU 1780  CB ALYS A 226     2094   2760   2667    663   -516    305       C  
ATOM   1781  CG ALYS A 226     -12.726  26.312  13.172  0.68 27.07           C  
ANISOU 1781  CG ALYS A 226     3048   3924   3314    297    190     -8       C  
ATOM   1782  CD ALYS A 226     -13.825  27.114  12.470  0.68 32.18           C  
ANISOU 1782  CD ALYS A 226     3929   4286   4012    525   -248    196       C  
ATOM   1783  CE ALYS A 226     -15.067  27.211  13.340  0.68 35.38           C  
ANISOU 1783  CE ALYS A 226     4224   4932   4289    505    -17     82       C  
ATOM   1784  NZ ALYS A 226     -15.550  25.877  13.785  0.68 37.93           N  
ANISOU 1784  NZ ALYS A 226     4692   5029   4691    363    -39    139       N  
ATOM   1785  CB BLYS A 226     -11.596  25.986  12.192  0.32 14.16           C  
ANISOU 1785  CB BLYS A 226     1436   2015   1929    460    -81    106       C  
ATOM   1786  CG BLYS A 226     -12.793  26.183  13.102  0.32 15.24           C  
ANISOU 1786  CG BLYS A 226     1458   2193   2142    341     22    127       C  
ATOM   1787  CD BLYS A 226     -14.042  26.586  12.324  0.32 17.31           C  
ANISOU 1787  CD BLYS A 226     1551   2634   2390    403    -35    150       C  
ATOM   1788  CE BLYS A 226     -13.902  27.892  11.570  0.32 20.14           C  
ANISOU 1788  CE BLYS A 226     2252   2736   2663    118    249    200       C  
ATOM   1789  NZ BLYS A 226     -15.126  28.218  10.775  0.32 22.65           N  
ANISOU 1789  NZ BLYS A 226     2562   3153   2891     53    -21    248       N  
ATOM   1790  N   ASP A 227     -10.096  25.865  15.292  1.00 13.60           N  
ANISOU 1790  N   ASP A 227     1288   2069   1812    432    166    127       N  
ATOM   1791  CA  ASP A 227      -9.586  26.639  16.411  1.00 13.96           C  
ANISOU 1791  CA  ASP A 227     1482   2146   1678    506    131    145       C  
ATOM   1792  C   ASP A 227      -8.051  26.718  16.449  1.00 13.01           C  
ANISOU 1792  C   ASP A 227     1499   1811   1635    299    102    -22       C  
ATOM   1793  O   ASP A 227      -7.497  27.583  17.121  1.00 13.87           O  
ANISOU 1793  O   ASP A 227     1521   1900   1847    358    190    -64       O  
ATOM   1794  CB  ASP A 227     -10.070  26.061  17.752  1.00 15.94           C  
ANISOU 1794  CB  ASP A 227     1910   2339   1808    452    370    101       C  
ATOM   1795  CG  ASP A 227     -11.557  26.073  17.954  1.00 20.85           C  
ANISOU 1795  CG  ASP A 227     2066   3268   2589    447    429    207       C  
ATOM   1796  OD1 ASP A 227     -12.270  26.839  17.264  1.00 22.91           O  
ANISOU 1796  OD1 ASP A 227     2039   3818   2849    743    580    384       O  
ATOM   1797  OD2 ASP A 227     -12.033  25.324  18.844  1.00 23.74           O  
ANISOU 1797  OD2 ASP A 227     2415   3755   2849    534    718    409       O  
ATOM   1798  N   LYS A 228      -7.342  25.885  15.658  1.00 11.61           N  
ANISOU 1798  N   LYS A 228     1366   1640   1407    364    165    168       N  
ATOM   1799  CA  LYS A 228      -5.874  25.909  15.573  1.00 10.63           C  
ANISOU 1799  CA  LYS A 228     1279   1506   1256    207    178    173       C  
ATOM   1800  C   LYS A 228      -5.358  26.954  14.575  1.00 10.42           C  
ANISOU 1800  C   LYS A 228     1320   1433   1205    316     11    202       C  
ATOM   1801  O   LYS A 228      -4.131  27.225  14.546  1.00 10.65           O  
ANISOU 1801  O   LYS A 228     1397   1383   1266    271    -50    246       O  
ATOM   1802  CB  LYS A 228      -5.383  24.512  15.087  1.00 10.80           C  
ANISOU 1802  CB  LYS A 228     1387   1419   1295    286     99    251       C  
ATOM   1803  CG ALYS A 228      -5.824  23.284  15.893  0.67 11.15           C  
ANISOU 1803  CG ALYS A 228     1345   1558   1334    125     -2    277       C  
ATOM   1804  CD ALYS A 228      -5.078  23.224  17.232  0.67 10.83           C  
ANISOU 1804  CD ALYS A 228     1453   1366   1294   -130      6    133       C  
ATOM   1805  CE ALYS A 228      -5.716  22.245  18.217  0.67 10.80           C  
ANISOU 1805  CE ALYS A 228     1360   1402   1343     43     36    254       C  
ATOM   1806  NZ ALYS A 228      -4.933  22.190  19.505  0.67 11.79           N  
ANISOU 1806  NZ ALYS A 228     1481   1688   1312    204     96    404       N  
ATOM   1807  CG BLYS A 228      -5.596  23.459  16.170  0.33  9.49           C  
ANISOU 1807  CG BLYS A 228     1141   1312   1152    224    -37    144       C  
ATOM   1808  CD BLYS A 228      -4.840  23.617  17.473  0.33  9.71           C  
ANISOU 1808  CD BLYS A 228     1163   1404   1123   -107    -11    142       C  
ATOM   1809  CE BLYS A 228      -5.253  22.574  18.493  0.33  8.41           C  
ANISOU 1809  CE BLYS A 228     1012   1287    895     23     -9    -38       C  
ATOM   1810  NZ BLYS A 228      -4.829  21.182  18.233  0.33 11.08           N  
ANISOU 1810  NZ BLYS A 228     1421   1355   1433    134     -4    -75       N  
ATOM   1811  N   PHE A 229      -6.229  27.604  13.785  1.00 10.96           N  
ANISOU 1811  N   PHE A 229     1352   1458   1355    385    129    212       N  
ATOM   1812  CA  PHE A 229      -5.780  28.481  12.696  1.00 11.09           C  
ANISOU 1812  CA  PHE A 229     1437   1435   1341    399    -67    318       C  
ATOM   1813  C   PHE A 229      -5.184  29.798  13.141  1.00 11.01           C  
ANISOU 1813  C   PHE A 229     1454   1418   1310    434    -11    219       C  
ATOM   1814  O   PHE A 229      -4.203  30.278  12.549  1.00 11.84           O  
ANISOU 1814  O   PHE A 229     1575   1518   1405    315     36    211       O  
ATOM   1815  CB  PHE A 229      -6.928  28.688  11.677  1.00 11.90           C  
ANISOU 1815  CB  PHE A 229     1425   1647   1448    438    -81    113       C  
ATOM   1816  CG  PHE A 229      -7.419  27.480  10.928  1.00 11.59           C  
ANISOU 1816  CG  PHE A 229     1386   1663   1355    349     -5    226       C  
ATOM   1817  CD1 PHE A 229      -6.710  26.285  10.918  1.00 11.80           C  
ANISOU 1817  CD1 PHE A 229     1660   1529   1296    405    -71    150       C  
ATOM   1818  CD2 PHE A 229      -8.575  27.553  10.154  1.00 12.52           C  
ANISOU 1818  CD2 PHE A 229     1474   1768   1517    282    -66    166       C  
ATOM   1819  CE1 PHE A 229      -7.145  25.197  10.182  1.00 12.02           C  
ANISOU 1819  CE1 PHE A 229     1527   1492   1547    288    -56    238       C  
ATOM   1820  CE2 PHE A 229      -9.014  26.473   9.413  1.00 14.01           C  
ANISOU 1820  CE2 PHE A 229     1645   1988   1691    294   -253    150       C  
ATOM   1821  CZ  PHE A 229      -8.290  25.292   9.419  1.00 12.89           C  
ANISOU 1821  CZ  PHE A 229     1549   1832   1518    214    -92    106       C  
ATOM   1822  N   ALA A 230      -5.781  30.398  14.193  1.00 11.59           N  
ANISOU 1822  N   ALA A 230     1570   1493   1342    408    -37    113       N  
ATOM   1823  CA  ALA A 230      -5.277  31.718  14.594  1.00 12.83           C  
ANISOU 1823  CA  ALA A 230     1744   1648   1481    234    117    -13       C  
ATOM   1824  C   ALA A 230      -3.807  31.682  14.981  1.00 11.57           C  
ANISOU 1824  C   ALA A 230     1707   1358   1333    288     31    118       C  
ATOM   1825  O   ALA A 230      -2.986  32.515  14.568  1.00 12.26           O  
ANISOU 1825  O   ALA A 230     1772   1374   1512    388     20    141       O  
ATOM   1826  CB  ALA A 230      -6.133  32.317  15.717  1.00 14.58           C  
ANISOU 1826  CB  ALA A 230     2194   1615   1731    581    200    -74       C  
ATOM   1827  N   LYS A 231      -3.413  30.679  15.819  1.00 11.38           N  
ANISOU 1827  N   LYS A 231     1675   1319   1329    351     20    154       N  
ATOM   1828  CA  LYS A 231      -2.014  30.600  16.241  1.00 11.20           C  
ANISOU 1828  CA  LYS A 231     1690   1379   1185    234     73    108       C  
ATOM   1829  C   LYS A 231      -1.107  30.236  15.061  1.00 10.23           C  
ANISOU 1829  C   LYS A 231     1388   1286   1213    315    -90    171       C  
ATOM   1830  O   LYS A 231       0.041  30.721  14.985  1.00 10.73           O  
ANISOU 1830  O   LYS A 231     1604   1228   1245    177    -70    146       O  
ATOM   1831  CB  LYS A 231      -1.871  29.569  17.383  1.00 11.39           C  
ANISOU 1831  CB  LYS A 231     1679   1396   1253    409    -30    154       C  
ATOM   1832  CG  LYS A 231      -0.455  29.376  17.875  1.00 12.64           C  
ANISOU 1832  CG  LYS A 231     1792   1700   1311    458    -15    315       C  
ATOM   1833  CD  LYS A 231       0.272  30.529  18.484  1.00 14.68           C  
ANISOU 1833  CD  LYS A 231     2094   1836   1647    209    -46    283       C  
ATOM   1834  CE  LYS A 231      -0.412  31.094  19.714  1.00 15.63           C  
ANISOU 1834  CE  LYS A 231     2421   1765   1753    294    -64    130       C  
ATOM   1835  NZ  LYS A 231      -0.431  30.145  20.857  1.00 14.38           N  
ANISOU 1835  NZ  LYS A 231     2015   1931   1519    424     37     65       N  
ATOM   1836  N   ALA A 232      -1.575  29.382  14.153  1.00 10.28           N  
ANISOU 1836  N   ALA A 232     1671   1128   1106    280     31    251       N  
ATOM   1837  CA  ALA A 232      -0.775  29.057  12.961  1.00 10.11           C  
ANISOU 1837  CA  ALA A 232     1498   1145   1198    241     59    214       C  
ATOM   1838  C   ALA A 232      -0.427  30.300  12.140  1.00 10.18           C  
ANISOU 1838  C   ALA A 232     1550   1051   1268    303    -34    230       C  
ATOM   1839  O   ALA A 232       0.725  30.490  11.713  1.00 10.43           O  
ANISOU 1839  O   ALA A 232     1541   1099   1323    216    -20    220       O  
ATOM   1840  CB  ALA A 232      -1.485  28.037  12.084  1.00 10.79           C  
ANISOU 1840  CB  ALA A 232     1577   1134   1388    240     10    141       C  
ATOM   1841  N   LYS A 233      -1.397  31.210  11.977  1.00 11.18           N  
ANISOU 1841  N   LYS A 233     1794   1189   1265    451      3    238       N  
ATOM   1842  CA  LYS A 233      -1.156  32.465  11.264  1.00 12.04           C  
ANISOU 1842  CA  LYS A 233     1934   1114   1525    384    -91    334       C  
ATOM   1843  C   LYS A 233      -0.192  33.345  12.047  1.00 12.46           C  
ANISOU 1843  C   LYS A 233     1853   1244   1638    346    -49    261       C  
ATOM   1844  O   LYS A 233       0.723  33.971  11.480  1.00 13.65           O  
ANISOU 1844  O   LYS A 233     2052   1393   1739    201    -14    324       O  
ATOM   1845  CB  LYS A 233      -2.460  33.206  10.920  1.00 13.54           C  
ANISOU 1845  CB  LYS A 233     2011   1344   1789    424    -91    282       C  
ATOM   1846  CG  LYS A 233      -3.248  32.500   9.821  1.00 14.74           C  
ANISOU 1846  CG  LYS A 233     2286   1369   1945    470   -209    287       C  
ATOM   1847  CD  LYS A 233      -4.594  33.144   9.476  1.00 18.63           C  
ANISOU 1847  CD  LYS A 233     2561   1905   2614    902   -262     84       C  
ATOM   1848  CE  LYS A 233      -5.083  32.517   8.164  1.00 22.94           C  
ANISOU 1848  CE  LYS A 233     3243   2425   3050    577   -702      1       C  
ATOM   1849  NZ  LYS A 233      -6.371  33.084   7.697  1.00 24.28           N  
ANISOU 1849  NZ  LYS A 233     3290   2946   2990    715   -438    277       N  
ATOM   1850  N   GLU A 234      -0.302  33.384  13.410  1.00 12.69           N  
ANISOU 1850  N   GLU A 234     2116   1114   1592    276    -26    182       N  
ATOM   1851  CA  GLU A 234       0.621  34.194  14.200  1.00 13.37           C  
ANISOU 1851  CA  GLU A 234     2009   1435   1636    136     -3    178       C  
ATOM   1852  C   GLU A 234       2.079  33.815  13.989  1.00 12.52           C  
ANISOU 1852  C   GLU A 234     1856   1285   1617      7    -90     54       C  
ATOM   1853  O   GLU A 234       2.973  34.663  14.011  1.00 15.59           O  
ANISOU 1853  O   GLU A 234     2051   1533   2340    -13    -88    -57       O  
ATOM   1854  CB AGLU A 234       0.301  34.076  15.706  0.68 15.84           C  
ANISOU 1854  CB AGLU A 234     2347   2001   1671    340     61    123       C  
ATOM   1855  CG AGLU A 234      -0.963  34.787  16.121  0.68 17.64           C  
ANISOU 1855  CG AGLU A 234     2454   2241   2008    406     76      8       C  
ATOM   1856  CD AGLU A 234      -1.392  34.618  17.562  0.68 22.13           C  
ANISOU 1856  CD AGLU A 234     3155   3147   2105    309    196   -133       C  
ATOM   1857  OE1AGLU A 234      -0.683  34.059  18.405  0.68 22.16           O  
ANISOU 1857  OE1AGLU A 234     3206   2989   2226    158     47   -143       O  
ATOM   1858  OE2AGLU A 234      -2.527  35.049  17.861  0.68 25.69           O  
ANISOU 1858  OE2AGLU A 234     3157   4036   2566    265    403   -238       O  
ATOM   1859  CB BGLU A 234       0.301  34.068  15.704  0.32 13.36           C  
ANISOU 1859  CB BGLU A 234     1864   1606   1605    335    -19     50       C  
ATOM   1860  CG BGLU A 234       1.305  34.674  16.668  0.32 14.88           C  
ANISOU 1860  CG BGLU A 234     2077   1848   1729    250   -119    -26       C  
ATOM   1861  CD BGLU A 234       1.103  34.292  18.131  0.32 15.24           C  
ANISOU 1861  CD BGLU A 234     1983   2052   1756    292   -242     91       C  
ATOM   1862  OE1BGLU A 234      -0.059  34.589  18.500  0.32 14.90           O  
ANISOU 1862  OE1BGLU A 234     2093   1901   1669    326   -189    -42       O  
ATOM   1863  OE2BGLU A 234       1.969  33.731  18.885  0.32 13.01           O  
ANISOU 1863  OE2BGLU A 234     2105   1571   1269    185   -216     56       O  
ATOM   1864  N   VAL A 235       2.372  32.500  13.815  1.00 11.39           N  
ANISOU 1864  N   VAL A 235     1801   1224   1304    144    -40    125       N  
ATOM   1865  CA  VAL A 235       3.751  32.058  13.630  1.00 11.64           C  
ANISOU 1865  CA  VAL A 235     1829   1295   1297    100    -27    136       C  
ATOM   1866  C   VAL A 235       4.202  31.920  12.192  1.00 11.46           C  
ANISOU 1866  C   VAL A 235     1793   1231   1331    -87   -101    188       C  
ATOM   1867  O   VAL A 235       5.359  31.525  11.949  1.00 12.19           O  
ANISOU 1867  O   VAL A 235     1864   1261   1505    -94    -47    167       O  
ATOM   1868  CB  VAL A 235       4.061  30.781  14.457  1.00 12.33           C  
ANISOU 1868  CB  VAL A 235     1915   1461   1308    147    -33    271       C  
ATOM   1869  CG1 VAL A 235       3.762  30.998  15.947  1.00 14.78           C  
ANISOU 1869  CG1 VAL A 235     2413   1861   1344    327   -113     76       C  
ATOM   1870  CG2 VAL A 235       3.289  29.576  13.937  1.00 11.45           C  
ANISOU 1870  CG2 VAL A 235     1895   1146   1309    191     99    390       C  
ATOM   1871  N   GLY A 236       3.342  32.257  11.223  1.00 11.28           N  
ANISOU 1871  N   GLY A 236     1600   1340   1344     49     35    219       N  
ATOM   1872  CA  GLY A 236       3.794  32.368   9.838  1.00 12.53           C  
ANISOU 1872  CA  GLY A 236     2062   1458   1242     25     52    205       C  
ATOM   1873  C   GLY A 236       2.889  31.791   8.779  1.00 11.65           C  
ANISOU 1873  C   GLY A 236     1806   1331   1291    111     25    176       C  
ATOM   1874  O   GLY A 236       3.187  32.002   7.569  1.00 12.54           O  
ANISOU 1874  O   GLY A 236     1956   1475   1332    166     94    211       O  
ATOM   1875  N   ALA A 237       1.806  31.067   9.069  1.00 10.50           N  
ANISOU 1875  N   ALA A 237     1723   1010   1257    224     10    141       N  
ATOM   1876  CA  ALA A 237       0.950  30.557   8.008  1.00 10.42           C  
ANISOU 1876  CA  ALA A 237     1738   1064   1158    197    -22    242       C  
ATOM   1877  C   ALA A 237       0.329  31.746   7.246  1.00 10.63           C  
ANISOU 1877  C   ALA A 237     1750   1116   1171    285     48     74       C  
ATOM   1878  O   ALA A 237      -0.145  32.712   7.870  1.00 12.41           O  
ANISOU 1878  O   ALA A 237     2249   1275   1190    444     -4    143       O  
ATOM   1879  CB  ALA A 237      -0.163  29.671   8.539  1.00 11.16           C  
ANISOU 1879  CB  ALA A 237     1661   1142   1438    236     10    258       C  
ATOM   1880  N   THR A 238       0.302  31.650   5.912  1.00 10.29           N  
ANISOU 1880  N   THR A 238     1690   1064   1155    247     23    228       N  
ATOM   1881  CA  THR A 238      -0.324  32.692   5.085  1.00 11.01           C  
ANISOU 1881  CA  THR A 238     1801   1081   1302    342     -6    246       C  
ATOM   1882  C   THR A 238      -1.774  32.412   4.827  1.00 11.15           C  
ANISOU 1882  C   THR A 238     1832   1146   1258    325    -59    274       C  
ATOM   1883  O   THR A 238      -2.554  33.348   4.487  1.00 13.97           O  
ANISOU 1883  O   THR A 238     2103   1392   1811    574   -261    202       O  
ATOM   1884  CB  THR A 238       0.458  32.852   3.760  1.00 12.22           C  
ANISOU 1884  CB  THR A 238     2151   1218   1274    472     49    285       C  
ATOM   1885  OG1 THR A 238       0.619  31.552   3.136  1.00 12.50           O  
ANISOU 1885  OG1 THR A 238     2115   1329   1307    476    225    272       O  
ATOM   1886  CG2 THR A 238       1.845  33.402   3.997  1.00 14.96           C  
ANISOU 1886  CG2 THR A 238     2392   1476   1814    155     -5    205       C  
ATOM   1887  N   GLU A 239      -2.258  31.187   4.972  1.00 12.13           N  
ANISOU 1887  N   GLU A 239     1562   1371   1678    130   -124    459       N  
ATOM   1888  CA  GLU A 239      -3.604  30.732   4.741  1.00 12.82           C  
ANISOU 1888  CA  GLU A 239     1603   1606   1664    -18   -129    537       C  
ATOM   1889  C   GLU A 239      -3.798  29.414   5.505  1.00 10.35           C  
ANISOU 1889  C   GLU A 239     1401   1322   1209    316    -14    212       C  
ATOM   1890  O   GLU A 239      -2.783  28.704   5.719  1.00 11.40           O  
ANISOU 1890  O   GLU A 239     1503   1491   1337    500    122    312       O  
ATOM   1891  CB AGLU A 239      -3.949  30.654   3.253  0.71 17.14           C  
ANISOU 1891  CB AGLU A 239     2264   2537   1712     42   -189    729       C  
ATOM   1892  CG AGLU A 239      -2.802  29.905   2.576  0.71 18.23           C  
ANISOU 1892  CG AGLU A 239     3071   2081   1777    302   -126    274       C  
ATOM   1893  CD AGLU A 239      -2.280  30.532   1.272  0.71 17.07           C  
ANISOU 1893  CD AGLU A 239     2734   1948   1804    496   -131    243       C  
ATOM   1894  OE1AGLU A 239      -3.136  30.532   0.360  0.71 19.10           O  
ANISOU 1894  OE1AGLU A 239     3150   2361   1745    424   -239    105       O  
ATOM   1895  OE2AGLU A 239      -1.128  31.056   1.046  0.71 16.44           O  
ANISOU 1895  OE2AGLU A 239     2197   2322   1729    981   -433     10       O  
ATOM   1896  CB BGLU A 239      -3.731  30.317   3.235  0.29 13.49           C  
ANISOU 1896  CB BGLU A 239     1765   1751   1610      6   -178    643       C  
ATOM   1897  CG BGLU A 239      -3.633  31.289   2.076  0.29 11.58           C  
ANISOU 1897  CG BGLU A 239     1801   1150   1449    314   -159    382       C  
ATOM   1898  CD BGLU A 239      -3.714  30.712   0.678  0.29 15.52           C  
ANISOU 1898  CD BGLU A 239     2262   1990   1643    200   -103     52       C  
ATOM   1899  OE1BGLU A 239      -2.849  29.898   0.269  0.29 15.92           O  
ANISOU 1899  OE1BGLU A 239     2546   2180   1322    380    -23    215       O  
ATOM   1900  OE2BGLU A 239      -4.592  31.092  -0.146  0.29 17.62           O  
ANISOU 1900  OE2BGLU A 239     2596   2030   2070    266   -376    127       O  
ATOM   1901  N   CYS A 240      -5.022  29.096   5.878  1.00 11.10           N  
ANISOU 1901  N   CYS A 240     1464   1326   1427    346    -28    287       N  
ATOM   1902  CA  CYS A 240      -5.351  27.831   6.518  1.00 10.60           C  
ANISOU 1902  CA  CYS A 240     1260   1332   1435    230    109    247       C  
ATOM   1903  C   CYS A 240      -6.600  27.238   5.877  1.00 11.60           C  
ANISOU 1903  C   CYS A 240     1281   1466   1660    291    -34    271       C  
ATOM   1904  O   CYS A 240      -7.554  27.975   5.549  1.00 14.26           O  
ANISOU 1904  O   CYS A 240     1703   1648   2068    478   -280    377       O  
ATOM   1905  CB  CYS A 240      -5.577  27.984   8.025  1.00 13.09           C  
ANISOU 1905  CB  CYS A 240     1628   1879   1466    241     25    217       C  
ATOM   1906  SG  CYS A 240      -4.086  28.334   8.987  1.00 14.12           S  
ANISOU 1906  SG  CYS A 240     1771   2293   1302    160    -45     81       S  
ATOM   1907  N   VAL A 241      -6.623  25.905   5.753  1.00 11.57           N  
ANISOU 1907  N   VAL A 241     1323   1497   1575    164    -72    276       N  
ATOM   1908  CA  VAL A 241      -7.733  25.193   5.166  1.00 12.15           C  
ANISOU 1908  CA  VAL A 241     1381   1609   1627    178    -44    225       C  
ATOM   1909  C   VAL A 241      -8.152  24.014   6.026  1.00 11.35           C  
ANISOU 1909  C   VAL A 241     1151   1710   1450    138    -40    245       C  
ATOM   1910  O   VAL A 241      -7.301  23.298   6.593  1.00 12.15           O  
ANISOU 1910  O   VAL A 241     1346   1734   1537    381      6    284       O  
ATOM   1911  CB  VAL A 241      -7.482  24.806   3.705  1.00 14.52           C  
ANISOU 1911  CB  VAL A 241     1807   2002   1708    -42     28    205       C  
ATOM   1912  CG1 VAL A 241      -7.275  26.007   2.782  1.00 16.66           C  
ANISOU 1912  CG1 VAL A 241     2125   2214   1992     66     10    346       C  
ATOM   1913  CG2 VAL A 241      -6.327  23.840   3.600  1.00 15.29           C  
ANISOU 1913  CG2 VAL A 241     1819   2265   1726     70    -79    146       C  
ATOM   1914  N   ASN A 242      -9.455  23.799   6.127  1.00 12.10           N  
ANISOU 1914  N   ASN A 242     1167   1770   1661     78   -149    189       N  
ATOM   1915  CA  ASN A 242     -10.052  22.674   6.848  1.00 12.72           C  
ANISOU 1915  CA  ASN A 242     1343   1940   1549    122    -33    235       C  
ATOM   1916  C   ASN A 242     -10.576  21.698   5.819  1.00 12.19           C  
ANISOU 1916  C   ASN A 242     1363   1797   1471     97      5    328       C  
ATOM   1917  O   ASN A 242     -11.575  22.025   5.128  1.00 13.24           O  
ANISOU 1917  O   ASN A 242     1339   1979   1711     52   -133    244       O  
ATOM   1918  CB  ASN A 242     -11.194  23.148   7.788  1.00 14.78           C  
ANISOU 1918  CB  ASN A 242     1420   2528   1667     99    -74     38       C  
ATOM   1919  CG  ASN A 242     -11.837  21.999   8.521  1.00 15.69           C  
ANISOU 1919  CG  ASN A 242     1506   2880   1576    -90      6     46       C  
ATOM   1920  OD1 ASN A 242     -11.606  20.801   8.286  1.00 16.51           O  
ANISOU 1920  OD1 ASN A 242     1607   2838   1826    -98    -71    272       O  
ATOM   1921  ND2 ASN A 242     -12.724  22.393   9.445  1.00 21.71           N  
ANISOU 1921  ND2 ASN A 242     2368   3718   2161     21    555    -45       N  
ATOM   1922  N   PRO A 243     -10.054  20.491   5.667  1.00 12.90           N  
ANISOU 1922  N   PRO A 243     1452   1845   1605    133    -42    356       N  
ATOM   1923  CA  PRO A 243     -10.557  19.520   4.720  1.00 13.69           C  
ANISOU 1923  CA  PRO A 243     1626   1772   1803     70     15    302       C  
ATOM   1924  C   PRO A 243     -12.061  19.251   4.825  1.00 14.63           C  
ANISOU 1924  C   PRO A 243     1679   1961   1920    -41   -186    189       C  
ATOM   1925  O   PRO A 243     -12.696  18.973   3.788  1.00 15.15           O  
ANISOU 1925  O   PRO A 243     1701   1948   2108    -23   -276    156       O  
ATOM   1926  CB  PRO A 243      -9.731  18.239   4.965  1.00 15.44           C  
ANISOU 1926  CB  PRO A 243     1786   1905   2177    256   -155    204       C  
ATOM   1927  CG  PRO A 243      -8.446  18.796   5.552  1.00 15.85           C  
ANISOU 1927  CG  PRO A 243     1732   2010   2280    187    -71    192       C  
ATOM   1928  CD  PRO A 243      -8.862  19.990   6.401  1.00 13.97           C  
ANISOU 1928  CD  PRO A 243     1468   2089   1749    217    -46    293       C  
ATOM   1929  N   GLN A 244     -12.649  19.367   6.009  1.00 15.98           N  
ANISOU 1929  N   GLN A 244     1613   2437   2021   -171    -13    440       N  
ATOM   1930  CA  GLN A 244     -14.096  19.127   6.182  1.00 18.70           C  
ANISOU 1930  CA  GLN A 244     1717   2898   2490   -195     33    409       C  
ATOM   1931  C   GLN A 244     -14.938  20.177   5.471  1.00 18.43           C  
ANISOU 1931  C   GLN A 244     1644   2728   2629    -74      4    213       C  
ATOM   1932  O   GLN A 244     -16.178  19.932   5.310  1.00 20.75           O  
ANISOU 1932  O   GLN A 244     1636   3313   2936   -147    -21    403       O  
ATOM   1933  CB AGLN A 244     -14.490  19.312   7.665  0.59 22.47           C  
ANISOU 1933  CB AGLN A 244     2318   3458   2762   -236    345    231       C  
ATOM   1934  CG AGLN A 244     -13.693  18.565   8.692  0.59 26.29           C  
ANISOU 1934  CG AGLN A 244     2869   3816   3305    -42    101    396       C  
ATOM   1935  CD AGLN A 244     -14.021  18.721  10.152  0.59 28.60           C  
ANISOU 1935  CD AGLN A 244     3204   4144   3519    -69    341    151       C  
ATOM   1936  OE1AGLN A 244     -14.283  19.784  10.714  0.59 29.02           O  
ANISOU 1936  OE1AGLN A 244     3329   4294   3403   -170    505     22       O  
ATOM   1937  NE2AGLN A 244     -13.965  17.583  10.847  0.59 29.75           N  
ANISOU 1937  NE2AGLN A 244     3350   4175   3778    -76    277    249       N  
ATOM   1938  CB BGLN A 244     -14.433  18.936   7.649  0.41 19.86           C  
ANISOU 1938  CB BGLN A 244     1933   3085   2528   -267     99    343       C  
ATOM   1939  CG BGLN A 244     -13.796  17.710   8.309  0.41 21.04           C  
ANISOU 1939  CG BGLN A 244     2229   3034   2730   -251     40    341       C  
ATOM   1940  CD BGLN A 244     -14.100  17.658   9.796  0.41 22.88           C  
ANISOU 1940  CD BGLN A 244     2581   3326   2788   -173    146    225       C  
ATOM   1941  OE1BGLN A 244     -14.708  18.573  10.360  0.41 25.08           O  
ANISOU 1941  OE1BGLN A 244     3035   3438   3054      7    132    152       O  
ATOM   1942  NE2BGLN A 244     -13.648  16.615  10.475  0.41 24.21           N  
ANISOU 1942  NE2BGLN A 244     2661   3409   3129   -105     67    268       N  
ATOM   1943  N   ASP A 245     -14.394  21.324   5.067  1.00 16.22           N  
ANISOU 1943  N   ASP A 245     1414   2479   2271    190    -70    144       N  
ATOM   1944  CA  ASP A 245     -15.189  22.356   4.398  1.00 15.78           C  
ANISOU 1944  CA  ASP A 245     1493   2197   2304     94   -198      8       C  
ATOM   1945  C   ASP A 245     -15.357  22.083   2.908  1.00 14.72           C  
ANISOU 1945  C   ASP A 245     1353   1983   2256     83   -113    104       C  
ATOM   1946  O   ASP A 245     -16.143  22.824   2.265  1.00 15.84           O  
ANISOU 1946  O   ASP A 245     1544   1997   2478    249   -153    166       O  
ATOM   1947  CB AASP A 245     -14.446  23.720   4.382  0.61 16.89           C  
ANISOU 1947  CB AASP A 245     1771   2198   2447     93    -92     14       C  
ATOM   1948  CG AASP A 245     -14.397  24.523   5.653  0.61 18.21           C  
ANISOU 1948  CG AASP A 245     2096   2531   2293    203   -117     74       C  
ATOM   1949  OD1AASP A 245     -15.165  24.168   6.570  0.61 21.23           O  
ANISOU 1949  OD1AASP A 245     2797   2853   2415     78    165    137       O  
ATOM   1950  OD2AASP A 245     -13.629  25.509   5.768  0.61 18.65           O  
ANISOU 1950  OD2AASP A 245     2011   2562   2514    273   -222     -2       O  
ATOM   1951  CB BASP A 245     -14.609  23.721   4.762  0.39 15.40           C  
ANISOU 1951  CB BASP A 245     1596   2080   2177    195    -83   -141       C  
ATOM   1952  CG BASP A 245     -14.680  24.124   6.221  0.39 16.23           C  
ANISOU 1952  CG BASP A 245     1871   2153   2145     83     17   -114       C  
ATOM   1953  OD1BASP A 245     -15.422  23.520   7.030  0.39 17.04           O  
ANISOU 1953  OD1BASP A 245     2240   1787   2447    111    106     -1       O  
ATOM   1954  OD2BASP A 245     -13.980  25.106   6.577  0.39 15.24           O  
ANISOU 1954  OD2BASP A 245     1778   2199   1814     12    105    -28       O  
ATOM   1955  N   TYR A 246     -14.663  21.099   2.343  1.00 13.38           N  
ANISOU 1955  N   TYR A 246     1451   1575   2059      3   -131    248       N  
ATOM   1956  CA  TYR A 246     -14.604  20.918   0.914  1.00 13.71           C  
ANISOU 1956  CA  TYR A 246     1553   1606   2050    100   -371    174       C  
ATOM   1957  C   TYR A 246     -15.310  19.657   0.427  1.00 15.11           C  
ANISOU 1957  C   TYR A 246     2172   1496   2072    -12   -341    203       C  
ATOM   1958  O   TYR A 246     -15.253  18.613   1.106  1.00 18.69           O  
ANISOU 1958  O   TYR A 246     2904   1646   2551   -107   -518    406       O  
ATOM   1959  CB  TYR A 246     -13.135  20.853   0.422  1.00 13.35           C  
ANISOU 1959  CB  TYR A 246     1830   1425   1816    174    -88    177       C  
ATOM   1960  CG  TYR A 246     -12.370  22.126   0.654  1.00 12.69           C  
ANISOU 1960  CG  TYR A 246     1612   1469   1742    186    -20    231       C  
ATOM   1961  CD1 TYR A 246     -11.782  22.398   1.884  1.00 14.24           C  
ANISOU 1961  CD1 TYR A 246     1504   1945   1960     21   -168    268       C  
ATOM   1962  CD2 TYR A 246     -12.252  23.097  -0.337  1.00 13.02           C  
ANISOU 1962  CD2 TYR A 246     1549   1710   1687    129     21    214       C  
ATOM   1963  CE1 TYR A 246     -11.126  23.589   2.122  1.00 15.26           C  
ANISOU 1963  CE1 TYR A 246     1595   2067   2136    -14    -52    124       C  
ATOM   1964  CE2 TYR A 246     -11.560  24.287  -0.119  1.00 13.74           C  
ANISOU 1964  CE2 TYR A 246     1421   1566   2235    258     41    262       C  
ATOM   1965  CZ  TYR A 246     -11.017  24.519   1.121  1.00 14.49           C  
ANISOU 1965  CZ  TYR A 246     1357   1752   2398     47     30    143       C  
ATOM   1966  OH  TYR A 246     -10.344  25.710   1.358  1.00 20.21           O  
ANISOU 1966  OH  TYR A 246     1983   2010   3685   -203    -89   -113       O  
ATOM   1967  N   LYS A 247     -15.877  19.687  -0.768  1.00 15.39           N  
ANISOU 1967  N   LYS A 247     1992   1626   2228   -177   -448    329       N  
ATOM   1968  CA  LYS A 247     -16.468  18.521  -1.416  1.00 17.83           C  
ANISOU 1968  CA  LYS A 247     2320   1848   2606   -382   -311    219       C  
ATOM   1969  C   LYS A 247     -15.392  17.740  -2.153  1.00 22.99           C  
ANISOU 1969  C   LYS A 247     3133   2739   2863      4     20     52       C  
ATOM   1970  O   LYS A 247     -15.601  16.547  -2.466  1.00 30.53           O  
ANISOU 1970  O   LYS A 247     4292   3181   4128   -389    332   -460       O  
ATOM   1971  CB  LYS A 247     -17.636  18.958  -2.321  1.00 20.39           C  
ANISOU 1971  CB  LYS A 247     2591   2361   2796   -386   -423    358       C  
ATOM   1972  CG  LYS A 247     -18.817  19.553  -1.581  1.00 22.96           C  
ANISOU 1972  CG  LYS A 247     2808   2531   3386   -115   -236    348       C  
ATOM   1973  CD ALYS A 247     -19.897  19.684  -2.685  0.55 26.70           C  
ANISOU 1973  CD ALYS A 247     3195   3403   3547   -145   -399    440       C  
ATOM   1974  CE ALYS A 247     -20.952  20.691  -2.309  0.55 30.15           C  
ANISOU 1974  CE ALYS A 247     3546   3835   4076    -30    114    261       C  
ATOM   1975  NZ ALYS A 247     -21.817  21.038  -3.486  0.55 32.30           N  
ANISOU 1975  NZ ALYS A 247     3748   4275   4250      1    -38    317       N  
ATOM   1976  CD BLYS A 247     -20.057  19.924  -2.380  0.45 22.61           C  
ANISOU 1976  CD BLYS A 247     2741   2622   3228    -56   -129    381       C  
ATOM   1977  CE BLYS A 247     -21.146  20.511  -1.499  0.45 23.51           C  
ANISOU 1977  CE BLYS A 247     2901   2821   3212     77   -114    333       C  
ATOM   1978  NZ BLYS A 247     -22.448  20.659  -2.238  0.45 24.94           N  
ANISOU 1978  NZ BLYS A 247     2788   3274   3412     78    -75    302       N  
ATOM   1979  N   LYS A 248     -14.223  18.243  -2.500  1.00 24.27           N  
ANISOU 1979  N   LYS A 248     2892   3272   3060    -64   -374    -96       N  
ATOM   1980  CA  LYS A 248     -13.168  17.531  -3.204  1.00 28.53           C  
ANISOU 1980  CA  LYS A 248     3247   3980   3612    361   -324   -294       C  
ATOM   1981  C   LYS A 248     -12.090  17.119  -2.195  1.00 21.62           C  
ANISOU 1981  C   LYS A 248     2562   2828   2826     29     62   -332       C  
ATOM   1982  O   LYS A 248     -11.958  17.771  -1.158  1.00 17.91           O  
ANISOU 1982  O   LYS A 248     1994   2280   2533    124   -192     76       O  
ATOM   1983  CB ALYS A 248     -12.476  18.410  -4.240  0.81 37.75           C  
ANISOU 1983  CB ALYS A 248     4623   5244   4477    -89    401    -26       C  
ATOM   1984  CG ALYS A 248     -13.242  19.313  -5.170  0.81 48.02           C  
ANISOU 1984  CG ALYS A 248     6042   6550   5654    669   -168    242       C  
ATOM   1985  CD ALYS A 248     -12.338  20.213  -5.990  0.81 54.46           C  
ANISOU 1985  CD ALYS A 248     6871   7430   6391    439    330    552       C  
ATOM   1986  CE ALYS A 248     -11.412  21.111  -5.209  0.81 58.60           C  
ANISOU 1986  CE ALYS A 248     7267   8168   6830    136     43    536       C  
ATOM   1987  NZ ALYS A 248     -12.033  22.354  -4.674  0.81 60.12           N  
ANISOU 1987  NZ ALYS A 248     7514   8309   7020    311    156    610       N  
ATOM   1988  CB BLYS A 248     -12.519  18.407  -4.269  0.19 35.43           C  
ANISOU 1988  CB BLYS A 248     4348   4593   4521     88    352    -34       C  
ATOM   1989  CG BLYS A 248     -13.377  18.793  -5.458  0.19 42.49           C  
ANISOU 1989  CG BLYS A 248     5194   5840   5112    451   -106     11       C  
ATOM   1990  CD BLYS A 248     -12.659  19.852  -6.286  0.19 48.06           C  
ANISOU 1990  CD BLYS A 248     5954   6260   6046    207    400    192       C  
ATOM   1991  CE BLYS A 248     -13.403  20.136  -7.579  0.19 51.23           C  
ANISOU 1991  CE BLYS A 248     6304   6890   6269    319    254    381       C  
ATOM   1992  NZ BLYS A 248     -13.552  18.910  -8.413  0.19 52.58           N  
ANISOU 1992  NZ BLYS A 248     6578   6964   6437    300    291    313       N  
ATOM   1993  N   PRO A 249     -11.259  16.134  -2.500  1.00 19.24           N  
ANISOU 1993  N   PRO A 249     2198   2664   2448    -28   -360   -258       N  
ATOM   1994  CA  PRO A 249     -10.158  15.763  -1.616  1.00 18.29           C  
ANISOU 1994  CA  PRO A 249     2091   2399   2459    -33   -241    -78       C  
ATOM   1995  C   PRO A 249      -9.184  16.928  -1.476  1.00 17.01           C  
ANISOU 1995  C   PRO A 249     1935   2343   2184     80   -293   -138       C  
ATOM   1996  O   PRO A 249      -8.888  17.665  -2.453  1.00 16.58           O  
ANISOU 1996  O   PRO A 249     1781   2399   2122     22   -320   -170       O  
ATOM   1997  CB  PRO A 249      -9.542  14.500  -2.219  1.00 22.13           C  
ANISOU 1997  CB  PRO A 249     2872   2488   3048    134   -317   -340       C  
ATOM   1998  CG  PRO A 249     -10.399  14.144  -3.383  1.00 24.60           C  
ANISOU 1998  CG  PRO A 249     3178   3069   3102    282   -401   -380       C  
ATOM   1999  CD  PRO A 249     -11.406  15.237  -3.652  1.00 21.11           C  
ANISOU 1999  CD  PRO A 249     2574   2774   2671     -9   -370   -404       C  
ATOM   2000  N   ILE A 250      -8.585  17.064  -0.293  1.00 16.56           N  
ANISOU 2000  N   ILE A 250     2116   2291   1883     31   -157    -54       N  
ATOM   2001  CA  ILE A 250      -7.719  18.242  -0.056  1.00 16.53           C  
ANISOU 2001  CA  ILE A 250     2042   2262   1979      1    -76    -85       C  
ATOM   2002  C   ILE A 250      -6.461  18.238  -0.923  1.00 15.25           C  
ANISOU 2002  C   ILE A 250     1969   2110   1714      9   -178    -84       C  
ATOM   2003  O   ILE A 250      -5.940  19.314  -1.209  1.00 15.09           O  
ANISOU 2003  O   ILE A 250     1736   2278   1720     63   -105    -10       O  
ATOM   2004  CB  ILE A 250      -7.482  18.481   1.444  1.00 16.65           C  
ANISOU 2004  CB  ILE A 250     2063   2230   2034     20    -22    -77       C  
ATOM   2005  CG1 ILE A 250      -7.108  19.942   1.771  1.00 16.88           C  
ANISOU 2005  CG1 ILE A 250     2222   2134   2059     20    121   -151       C  
ATOM   2006  CG2 ILE A 250      -6.422  17.547   1.949  1.00 17.34           C  
ANISOU 2006  CG2 ILE A 250     2022   2750   1816    213    157     16       C  
ATOM   2007  CD1 ILE A 250      -8.227  20.952   1.676  1.00 18.39           C  
ANISOU 2007  CD1 ILE A 250     2243   2247   2496     16    155    -86       C  
ATOM   2008  N   GLN A 251      -5.968  17.066  -1.388  1.00 16.04           N  
ANISOU 2008  N   GLN A 251     1937   2329   1827    320   -169     59       N  
ATOM   2009  CA  GLN A 251      -4.805  17.105  -2.292  1.00 16.51           C  
ANISOU 2009  CA  GLN A 251     1983   2391   1899    314   -126    114       C  
ATOM   2010  C   GLN A 251      -5.155  17.848  -3.579  1.00 15.89           C  
ANISOU 2010  C   GLN A 251     1878   2215   1945    337   -152     38       C  
ATOM   2011  O   GLN A 251      -4.298  18.519  -4.162  1.00 15.85           O  
ANISOU 2011  O   GLN A 251     1939   2289   1795    299   -242     -4       O  
ATOM   2012  CB AGLN A 251      -4.218  15.725  -2.598  0.53 18.28           C  
ANISOU 2012  CB AGLN A 251     2191   2408   2346    301   -187     -8       C  
ATOM   2013  CG AGLN A 251      -5.140  14.771  -3.334  0.53 20.36           C  
ANISOU 2013  CG AGLN A 251     2483   2432   2821    194   -294      9       C  
ATOM   2014  CD AGLN A 251      -6.070  13.974  -2.448  0.53 22.59           C  
ANISOU 2014  CD AGLN A 251     2541   2692   3350    175   -175    246       C  
ATOM   2015  OE1AGLN A 251      -6.382  14.282  -1.306  0.53 22.50           O  
ANISOU 2015  OE1AGLN A 251     2565   2448   3535    288   -320     54       O  
ATOM   2016  NE2AGLN A 251      -6.512  12.873  -3.067  0.53 25.97           N  
ANISOU 2016  NE2AGLN A 251     3117   3088   3662     58    -99    -81       N  
ATOM   2017  CB BGLN A 251      -4.243  15.712  -2.603  0.47 17.39           C  
ANISOU 2017  CB BGLN A 251     2144   2388   2075    253   -215    -46       C  
ATOM   2018  CG BGLN A 251      -5.147  14.775  -3.391  0.47 18.75           C  
ANISOU 2018  CG BGLN A 251     2445   2451   2228    179   -306    -38       C  
ATOM   2019  CD BGLN A 251      -4.807  13.311  -3.240  0.47 19.26           C  
ANISOU 2019  CD BGLN A 251     2588   2470   2259    175   -221    -15       C  
ATOM   2020  OE1BGLN A 251      -4.319  12.847  -2.202  0.47 19.20           O  
ANISOU 2020  OE1BGLN A 251     2591   2512   2191    154   -108     79       O  
ATOM   2021  NE2BGLN A 251      -4.990  12.538  -4.313  0.47 20.28           N  
ANISOU 2021  NE2BGLN A 251     2823   2503   2380    265   -328    -92       N  
ATOM   2022  N   GLU A 252      -6.386  17.732  -4.080  1.00 16.43           N  
ANISOU 2022  N   GLU A 252     1962   2455   1825    391   -235   -153       N  
ATOM   2023  CA  GLU A 252      -6.832  18.431  -5.289  1.00 17.25           C  
ANISOU 2023  CA  GLU A 252     2117   2419   2018    307   -154     -6       C  
ATOM   2024  C   GLU A 252      -6.934  19.927  -5.011  1.00 15.53           C  
ANISOU 2024  C   GLU A 252     1678   2393   1831    295   -157     48       C  
ATOM   2025  O   GLU A 252      -6.479  20.757  -5.795  1.00 15.39           O  
ANISOU 2025  O   GLU A 252     1806   2261   1780    358   -212    -23       O  
ATOM   2026  CB AGLU A 252      -8.195  17.889  -5.756  0.56 20.22           C  
ANISOU 2026  CB AGLU A 252     2256   3084   2344    125   -225     67       C  
ATOM   2027  CG AGLU A 252      -8.167  16.498  -6.338  0.56 24.39           C  
ANISOU 2027  CG AGLU A 252     3225   3202   2842    167    -41    -41       C  
ATOM   2028  CD AGLU A 252      -9.507  15.908  -6.738  0.56 28.31           C  
ANISOU 2028  CD AGLU A 252     3446   4008   3303    -80   -167     29       C  
ATOM   2029  OE1AGLU A 252     -10.490  16.660  -6.897  0.56 29.27           O  
ANISOU 2029  OE1AGLU A 252     3481   4232   3406    -25   -324    -90       O  
ATOM   2030  OE2AGLU A 252      -9.561  14.669  -6.890  0.56 29.88           O  
ANISOU 2030  OE2AGLU A 252     3738   4072   3542   -230   -202     56       O  
ATOM   2031  CB BGLU A 252      -8.164  17.831  -5.762  0.44 18.74           C  
ANISOU 2031  CB BGLU A 252     2196   2621   2301    172   -125    -79       C  
ATOM   2032  CG BGLU A 252      -8.652  18.370  -7.087  0.44 20.72           C  
ANISOU 2032  CG BGLU A 252     2638   2791   2444    235   -175     59       C  
ATOM   2033  CD BGLU A 252      -9.843  17.648  -7.684  0.44 22.60           C  
ANISOU 2033  CD BGLU A 252     2746   3094   2747     73   -181    -25       C  
ATOM   2034  OE1BGLU A 252     -10.307  16.648  -7.118  0.44 21.92           O  
ANISOU 2034  OE1BGLU A 252     2573   3153   2601   -124   -445   -158       O  
ATOM   2035  OE2BGLU A 252     -10.327  18.102  -8.755  0.44 23.78           O  
ANISOU 2035  OE2BGLU A 252     2930   3259   2846     24   -313     22       O  
ATOM   2036  N   VAL A 253      -7.517  20.277  -3.853  1.00 15.45           N  
ANISOU 2036  N   VAL A 253     1711   2308   1853    254   -119      7       N  
ATOM   2037  CA  VAL A 253      -7.627  21.679  -3.454  1.00 15.29           C  
ANISOU 2037  CA  VAL A 253     1726   2298   1787    309   -149     65       C  
ATOM   2038  C   VAL A 253      -6.270  22.355  -3.391  1.00 14.17           C  
ANISOU 2038  C   VAL A 253     1762   2017   1605    308     26     14       C  
ATOM   2039  O   VAL A 253      -6.019  23.435  -3.916  1.00 14.55           O  
ANISOU 2039  O   VAL A 253     1654   2248   1627    383     50    132       O  
ATOM   2040  CB  VAL A 253      -8.339  21.755  -2.085  1.00 16.51           C  
ANISOU 2040  CB  VAL A 253     1660   2615   1998    292      4    -84       C  
ATOM   2041  CG1 VAL A 253      -8.328  23.179  -1.543  1.00 17.44           C  
ANISOU 2041  CG1 VAL A 253     1836   2727   2063    226    129   -163       C  
ATOM   2042  CG2 VAL A 253      -9.759  21.227  -2.163  1.00 17.86           C  
ANISOU 2042  CG2 VAL A 253     1695   2858   2234    313     52    -22       C  
ATOM   2043  N   LEU A 254      -5.305  21.656  -2.701  1.00 12.84           N  
ANISOU 2043  N   LEU A 254     1540   1845   1493    365    150     70       N  
ATOM   2044  CA  LEU A 254      -3.961  22.221  -2.551  1.00 12.26           C  
ANISOU 2044  CA  LEU A 254     1596   1741   1322    389     69     36       C  
ATOM   2045  C   LEU A 254      -3.217  22.342  -3.878  1.00 11.47           C  
ANISOU 2045  C   LEU A 254     1450   1701   1205    352    -81    -21       C  
ATOM   2046  O   LEU A 254      -2.439  23.295  -4.070  1.00 12.35           O  
ANISOU 2046  O   LEU A 254     1647   1766   1278    379     28     62       O  
ATOM   2047  CB  LEU A 254      -3.152  21.418  -1.523  1.00 12.34           C  
ANISOU 2047  CB  LEU A 254     1587   1822   1279    404     18    -19       C  
ATOM   2048  CG  LEU A 254      -3.650  21.505  -0.079  1.00 12.51           C  
ANISOU 2048  CG  LEU A 254     1762   1627   1364    312     96    111       C  
ATOM   2049  CD1 LEU A 254      -3.048  20.382   0.756  1.00 14.02           C  
ANISOU 2049  CD1 LEU A 254     2047   1818   1461    313   -229     41       C  
ATOM   2050  CD2 LEU A 254      -3.296  22.858   0.536  1.00 14.13           C  
ANISOU 2050  CD2 LEU A 254     2180   1818   1371    434   -171    -36       C  
ATOM   2051  N   THR A 255      -3.388  21.360  -4.760  1.00 12.31           N  
ANISOU 2051  N   THR A 255     1475   1862   1339    379    -86    -82       N  
ATOM   2052  CA  THR A 255      -2.749  21.442  -6.089  1.00 13.18           C  
ANISOU 2052  CA  THR A 255     1792   1902   1313    375      4    -29       C  
ATOM   2053  C   THR A 255      -3.317  22.628  -6.863  1.00 13.09           C  
ANISOU 2053  C   THR A 255     1617   1971   1386    476     47   -131       C  
ATOM   2054  O   THR A 255      -2.551  23.381  -7.484  1.00 13.76           O  
ANISOU 2054  O   THR A 255     1839   1928   1463    568     24    146       O  
ATOM   2055  CB  THR A 255      -2.974  20.126  -6.864  1.00 13.70           C  
ANISOU 2055  CB  THR A 255     1822   1957   1425    544    -67   -116       C  
ATOM   2056  OG1 THR A 255      -2.318  19.060  -6.139  1.00 14.89           O  
ANISOU 2056  OG1 THR A 255     2037   2016   1603    655    -35    -70       O  
ATOM   2057  CG2 THR A 255      -2.425  20.138  -8.275  1.00 15.29           C  
ANISOU 2057  CG2 THR A 255     2186   2143   1479    622     28   -113       C  
ATOM   2058  N   GLU A 256      -4.623  22.886  -6.798  1.00 14.44           N  
ANISOU 2058  N   GLU A 256     1694   2205   1586    534    -85    105       N  
ATOM   2059  CA  GLU A 256      -5.218  24.039  -7.481  1.00 16.70           C  
ANISOU 2059  CA  GLU A 256     2075   2339   1930    600   -326    120       C  
ATOM   2060  C   GLU A 256      -4.697  25.343  -6.887  1.00 14.86           C  
ANISOU 2060  C   GLU A 256     1815   2183   1648    704    -84    201       C  
ATOM   2061  O   GLU A 256      -4.307  26.296  -7.580  1.00 15.99           O  
ANISOU 2061  O   GLU A 256     1911   2200   1967    714   -141    252       O  
ATOM   2062  CB AGLU A 256      -6.745  23.998  -7.326  0.62 21.89           C  
ANISOU 2062  CB AGLU A 256     2246   3189   2883    706   -229    290       C  
ATOM   2063  CG AGLU A 256      -7.484  22.925  -8.093  0.62 29.09           C  
ANISOU 2063  CG AGLU A 256     3784   3557   3713    292   -442      8       C  
ATOM   2064  CD AGLU A 256      -8.932  22.788  -7.639  0.62 35.67           C  
ANISOU 2064  CD AGLU A 256     4063   4859   4631    327    -77    264       C  
ATOM   2065  OE1AGLU A 256      -9.383  23.572  -6.770  0.62 36.83           O  
ANISOU 2065  OE1AGLU A 256     4040   4888   5067    413    -95     95       O  
ATOM   2066  OE2AGLU A 256      -9.616  21.870  -8.141  0.62 37.88           O  
ANISOU 2066  OE2AGLU A 256     4465   5001   4925    182    -60    133       O  
ATOM   2067  CB BGLU A 256      -6.742  23.900  -7.398  0.38 16.72           C  
ANISOU 2067  CB BGLU A 256     2102   2278   1973    345   -273    -65       C  
ATOM   2068  CG BGLU A 256      -7.495  25.029  -8.071  0.38 18.00           C  
ANISOU 2068  CG BGLU A 256     2265   2347   2227    319   -163    154       C  
ATOM   2069  CD BGLU A 256      -7.656  26.251  -7.197  0.38 20.00           C  
ANISOU 2069  CD BGLU A 256     2468   2641   2489    272   -120    -89       C  
ATOM   2070  OE1BGLU A 256      -7.548  26.172  -5.955  0.38 20.29           O  
ANISOU 2070  OE1BGLU A 256     2476   2747   2488    305    -16    -64       O  
ATOM   2071  OE2BGLU A 256      -7.869  27.366  -7.713  0.38 21.64           O  
ANISOU 2071  OE2BGLU A 256     2838   2720   2666    334    -47      6       O  
ATOM   2072  N   MET A 257      -4.656  25.438  -5.537  1.00 14.39           N  
ANISOU 2072  N   MET A 257     1841   2009   1616    727   -122     25       N  
ATOM   2073  CA  MET A 257      -4.225  26.647  -4.869  1.00 14.12           C  
ANISOU 2073  CA  MET A 257     1754   1909   1703    507    -77    208       C  
ATOM   2074  C   MET A 257      -2.814  27.098  -5.192  1.00 13.39           C  
ANISOU 2074  C   MET A 257     1682   1854   1550    552   -147    115       C  
ATOM   2075  O   MET A 257      -2.444  28.279  -5.270  1.00 16.06           O  
ANISOU 2075  O   MET A 257     1943   1915   2243    762    -46    102       O  
ATOM   2076  CB  MET A 257      -4.337  26.493  -3.331  1.00 15.56           C  
ANISOU 2076  CB  MET A 257     2241   1989   1684    767    232    100       C  
ATOM   2077  CG  MET A 257      -5.742  26.459  -2.764  1.00 16.44           C  
ANISOU 2077  CG  MET A 257     2259   2268   1718    564    213    297       C  
ATOM   2078  SD  MET A 257      -5.752  26.070  -0.993  1.00 16.28           S  
ANISOU 2078  SD  MET A 257     2627   1962   1598    666    200    161       S  
ATOM   2079  CE  MET A 257      -5.036  27.568  -0.276  1.00 18.13           C  
ANISOU 2079  CE  MET A 257     2575   2546   1768    319    115     62       C  
ATOM   2080  N   SER A 258      -1.930  26.071  -5.404  1.00 13.27           N  
ANISOU 2080  N   SER A 258     1702   1899   1442    607    -46     87       N  
ATOM   2081  CA  SER A 258      -0.514  26.240  -5.697  1.00 12.79           C  
ANISOU 2081  CA  SER A 258     1726   1761   1375    674    -58    148       C  
ATOM   2082  C   SER A 258      -0.211  26.171  -7.195  1.00 13.92           C  
ANISOU 2082  C   SER A 258     1860   1954   1476    639    -17    191       C  
ATOM   2083  O   SER A 258       0.954  26.112  -7.576  1.00 14.46           O  
ANISOU 2083  O   SER A 258     1953   2061   1479    583     51    389       O  
ATOM   2084  CB  SER A 258       0.286  25.155  -4.944  1.00 13.02           C  
ANISOU 2084  CB  SER A 258     1899   1773   1277    637   -122    115       C  
ATOM   2085  OG  SER A 258      -0.073  23.865  -5.365  1.00 12.51           O  
ANISOU 2085  OG  SER A 258     1827   1724   1200    758    -61    220       O  
ATOM   2086  N   ASN A 259      -1.235  26.279  -8.045  1.00 14.10           N  
ANISOU 2086  N   ASN A 259     2097   1947   1312    707   -112    148       N  
ATOM   2087  CA  ASN A 259      -1.020  26.349  -9.491  1.00 15.40           C  
ANISOU 2087  CA  ASN A 259     2303   2093   1457    711     34    175       C  
ATOM   2088  C   ASN A 259      -0.202  25.152  -9.978  1.00 14.93           C  
ANISOU 2088  C   ASN A 259     2303   2066   1302    656     98    130       C  
ATOM   2089  O   ASN A 259       0.649  25.282 -10.869  1.00 16.96           O  
ANISOU 2089  O   ASN A 259     2550   2425   1469    848    185    282       O  
ATOM   2090  CB  ASN A 259      -0.449  27.721  -9.872  1.00 18.09           C  
ANISOU 2090  CB  ASN A 259     2766   2276   1830    517   -141    393       C  
ATOM   2091  CG  ASN A 259      -1.430  28.871  -9.512  1.00 21.60           C  
ANISOU 2091  CG  ASN A 259     3077   2609   2519    690      3    296       C  
ATOM   2092  OD1 ASN A 259      -1.085  29.646  -8.620  1.00 26.79           O  
ANISOU 2092  OD1 ASN A 259     4131   2771   3278    816   -110      7       O  
ATOM   2093  ND2 ASN A 259      -2.584  28.843 -10.130  1.00 21.85           N  
ANISOU 2093  ND2 ASN A 259     2911   2468   2924    938     72    543       N  
ATOM   2094  N   GLY A 260      -0.535  23.943  -9.464  1.00 14.62           N  
ANISOU 2094  N   GLY A 260     2168   2103   1283    644    -18    188       N  
ATOM   2095  CA  GLY A 260       0.075  22.719  -9.930  1.00 14.60           C  
ANISOU 2095  CA  GLY A 260     2290   2061   1197    681    -73    172       C  
ATOM   2096  C   GLY A 260       0.823  21.874  -8.923  1.00 12.95           C  
ANISOU 2096  C   GLY A 260     1986   1778   1155    630     82    155       C  
ATOM   2097  O   GLY A 260       1.401  20.857  -9.329  1.00 13.59           O  
ANISOU 2097  O   GLY A 260     2104   1806   1254    559     82    -32       O  
ATOM   2098  N   GLY A 261       0.708  22.169  -7.623  1.00 11.98           N  
ANISOU 2098  N   GLY A 261     1747   1744   1059    676     39    189       N  
ATOM   2099  CA  GLY A 261       1.348  21.383  -6.543  1.00 11.11           C  
ANISOU 2099  CA  GLY A 261     1422   1566   1234    367    -75    212       C  
ATOM   2100  C   GLY A 261       2.340  22.216  -5.773  1.00 10.10           C  
ANISOU 2100  C   GLY A 261     1240   1446   1154    342     42    270       C  
ATOM   2101  O   GLY A 261       2.969  23.166  -6.274  1.00 11.63           O  
ANISOU 2101  O   GLY A 261     1732   1538   1149    304    129    289       O  
ATOM   2102  N   VAL A 262       2.502  21.886  -4.467  1.00 10.24           N  
ANISOU 2102  N   VAL A 262     1342   1477   1071    398      4    193       N  
ATOM   2103  CA  VAL A 262       3.390  22.639  -3.586  1.00 10.40           C  
ANISOU 2103  CA  VAL A 262     1404   1478   1069    259      6    283       C  
ATOM   2104  C   VAL A 262       4.869  22.228  -3.717  1.00  9.78           C  
ANISOU 2104  C   VAL A 262     1400   1334    981    217     75    272       C  
ATOM   2105  O   VAL A 262       5.174  21.088  -4.161  1.00 11.58           O  
ANISOU 2105  O   VAL A 262     1647   1566   1188    404    108    114       O  
ATOM   2106  CB  VAL A 262       2.922  22.578  -2.090  1.00 10.40           C  
ANISOU 2106  CB  VAL A 262     1435   1434   1082    422     42    267       C  
ATOM   2107  CG1 VAL A 262       1.474  23.043  -1.953  1.00 11.50           C  
ANISOU 2107  CG1 VAL A 262     1561   1610   1201    406     61    165       C  
ATOM   2108  CG2 VAL A 262       3.131  21.207  -1.450  1.00 10.98           C  
ANISOU 2108  CG2 VAL A 262     1555   1592   1025    448     87    350       C  
ATOM   2109  N   ASP A 263       5.806  23.088  -3.333  1.00  9.71           N  
ANISOU 2109  N   ASP A 263     1402   1199   1087    313     77    354       N  
ATOM   2110  CA  ASP A 263       7.232  22.737  -3.329  1.00  9.81           C  
ANISOU 2110  CA  ASP A 263     1440   1352    933    291     36    306       C  
ATOM   2111  C   ASP A 263       7.581  21.721  -2.228  1.00  8.95           C  
ANISOU 2111  C   ASP A 263     1335   1178    886    220     -7    167       C  
ATOM   2112  O   ASP A 263       8.372  20.784  -2.441  1.00 10.06           O  
ANISOU 2112  O   ASP A 263     1508   1340    976    327    129    257       O  
ATOM   2113  CB  ASP A 263       8.098  23.993  -3.172  1.00 10.44           C  
ANISOU 2113  CB  ASP A 263     1634   1364    969    202     90    263       C  
ATOM   2114  CG  ASP A 263       7.887  24.945  -4.361  1.00 11.17           C  
ANISOU 2114  CG  ASP A 263     1873   1380    992     49    182    247       C  
ATOM   2115  OD1 ASP A 263       8.368  24.595  -5.476  1.00 13.01           O  
ANISOU 2115  OD1 ASP A 263     2322   1590   1030    215    230    325       O  
ATOM   2116  OD2 ASP A 263       7.262  25.989  -4.151  1.00 13.55           O  
ANISOU 2116  OD2 ASP A 263     2457   1659   1030    395    292    425       O  
ATOM   2117  N   PHE A 264       7.014  21.938  -1.023  1.00  9.27           N  
ANISOU 2117  N   PHE A 264     1454   1197    870    218     62    268       N  
ATOM   2118  CA  PHE A 264       7.314  21.131   0.163  1.00  9.21           C  
ANISOU 2118  CA  PHE A 264     1358   1122   1019    230     51    306       C  
ATOM   2119  C   PHE A 264       6.049  20.840   0.951  1.00  8.92           C  
ANISOU 2119  C   PHE A 264     1258   1114   1016    256     94    240       C  
ATOM   2120  O   PHE A 264       5.312  21.808   1.258  1.00 10.23           O  
ANISOU 2120  O   PHE A 264     1464   1195   1227    296    264    376       O  
ATOM   2121  CB  PHE A 264       8.318  21.870   1.112  1.00  9.34           C  
ANISOU 2121  CB  PHE A 264     1347   1285    918    163    -21    279       C  
ATOM   2122  CG  PHE A 264       9.628  22.223   0.414  1.00  9.72           C  
ANISOU 2122  CG  PHE A 264     1418   1356    917     89     81    179       C  
ATOM   2123  CD1 PHE A 264      10.676  21.285   0.294  1.00 10.33           C  
ANISOU 2123  CD1 PHE A 264     1473   1285   1169    102     73    191       C  
ATOM   2124  CD2 PHE A 264       9.797  23.476  -0.176  1.00 10.44           C  
ANISOU 2124  CD2 PHE A 264     1531   1412   1025    138     73    267       C  
ATOM   2125  CE1 PHE A 264      11.827  21.611  -0.402  1.00 11.74           C  
ANISOU 2125  CE1 PHE A 264     1447   1594   1421    144    157    188       C  
ATOM   2126  CE2 PHE A 264      10.963  23.783  -0.871  1.00 11.40           C  
ANISOU 2126  CE2 PHE A 264     1513   1523   1296    -64    150    291       C  
ATOM   2127  CZ  PHE A 264      11.966  22.849  -0.994  1.00 12.05           C  
ANISOU 2127  CZ  PHE A 264     1646   1741   1190     60     21    246       C  
ATOM   2128  N   SER A 265       5.785  19.583   1.307  1.00  8.44           N  
ANISOU 2128  N   SER A 265     1209   1058    941    136    132    217       N  
ATOM   2129  CA  SER A 265       4.675  19.258   2.183  1.00  8.63           C  
ANISOU 2129  CA  SER A 265     1157   1134    989    215     80    317       C  
ATOM   2130  C   SER A 265       5.176  18.450   3.383  1.00  8.20           C  
ANISOU 2130  C   SER A 265     1148    881   1087    226     73    259       C  
ATOM   2131  O   SER A 265       6.222  17.809   3.335  1.00  8.28           O  
ANISOU 2131  O   SER A 265     1152   1025    971    276    111    218       O  
ATOM   2132  CB  SER A 265       3.560  18.517   1.497  1.00  9.20           C  
ANISOU 2132  CB  SER A 265     1205   1184   1104    208      7    277       C  
ATOM   2133  OG  SER A 265       4.032  17.244   1.089  1.00  9.87           O  
ANISOU 2133  OG  SER A 265     1249   1100   1401    267   -103     32       O  
ATOM   2134  N   PHE A 266       4.423  18.521   4.508  1.00  7.98           N  
ANISOU 2134  N   PHE A 266     1168    968    895    347     95    184       N  
ATOM   2135  CA  PHE A 266       4.795  17.906   5.762  1.00  7.71           C  
ANISOU 2135  CA  PHE A 266     1129    821    981     95     99    256       C  
ATOM   2136  C   PHE A 266       3.582  17.229   6.388  1.00  7.92           C  
ANISOU 2136  C   PHE A 266     1041    949   1020     93     58    178       C  
ATOM   2137  O   PHE A 266       2.519  17.861   6.549  1.00  8.97           O  
ANISOU 2137  O   PHE A 266     1144   1061   1206    207    124    241       O  
ATOM   2138  CB  PHE A 266       5.326  18.966   6.782  1.00  7.98           C  
ANISOU 2138  CB  PHE A 266     1063    966   1003    137     93    178       C  
ATOM   2139  CG  PHE A 266       6.514  19.734   6.250  1.00  7.52           C  
ANISOU 2139  CG  PHE A 266     1061    861    934     34     20     71       C  
ATOM   2140  CD1 PHE A 266       6.354  20.857   5.446  1.00  8.21           C  
ANISOU 2140  CD1 PHE A 266     1089   1004   1024     19     22    160       C  
ATOM   2141  CD2 PHE A 266       7.815  19.340   6.575  1.00  8.25           C  
ANISOU 2141  CD2 PHE A 266     1142   1062    930     43     52    139       C  
ATOM   2142  CE1 PHE A 266       7.444  21.524   4.957  1.00  9.13           C  
ANISOU 2142  CE1 PHE A 266     1284   1182   1005     -1     -6    256       C  
ATOM   2143  CE2 PHE A 266       8.925  20.013   6.088  1.00  9.17           C  
ANISOU 2143  CE2 PHE A 266     1277   1082   1125    -45     25    250       C  
ATOM   2144  CZ  PHE A 266       8.723  21.114   5.265  1.00  9.16           C  
ANISOU 2144  CZ  PHE A 266     1162   1284   1036    -47     48    237       C  
ATOM   2145  N   GLU A 267       3.710  15.950   6.756  1.00  7.34           N  
ANISOU 2145  N   GLU A 267     1030    807    954     63     73    157       N  
ATOM   2146  CA  GLU A 267       2.658  15.255   7.510  1.00  7.46           C  
ANISOU 2146  CA  GLU A 267      976    953    907     33     47    198       C  
ATOM   2147  C   GLU A 267       3.061  15.331   8.993  1.00  7.25           C  
ANISOU 2147  C   GLU A 267      983    898    875     48     91    198       C  
ATOM   2148  O   GLU A 267       4.118  14.789   9.355  1.00  8.29           O  
ANISOU 2148  O   GLU A 267     1075   1108    969    112    -12    233       O  
ATOM   2149  CB  GLU A 267       2.404  13.829   7.012  1.00  8.14           C  
ANISOU 2149  CB  GLU A 267     1224   1004    863     24     34    164       C  
ATOM   2150  CG  GLU A 267       1.038  13.258   7.434  1.00  9.13           C  
ANISOU 2150  CG  GLU A 267     1283   1072   1115     -8      3    153       C  
ATOM   2151  CD  GLU A 267       0.898  12.749   8.865  1.00  8.36           C  
ANISOU 2151  CD  GLU A 267     1137    891   1148     70     52     23       C  
ATOM   2152  OE1 GLU A 267       1.803  12.897   9.686  1.00  9.56           O  
ANISOU 2152  OE1 GLU A 267     1494   1104   1034    -13     46    204       O  
ATOM   2153  OE2 GLU A 267      -0.231  12.205   9.140  1.00 10.38           O  
ANISOU 2153  OE2 GLU A 267     1332   1250   1361    -51    103    186       O  
ATOM   2154  N   VAL A 268       2.276  16.004   9.815  1.00  7.21           N  
ANISOU 2154  N   VAL A 268      936    907    896     82     85    170       N  
ATOM   2155  CA  VAL A 268       2.578  16.270  11.223  1.00  7.46           C  
ANISOU 2155  CA  VAL A 268      987    890    958     12     15    190       C  
ATOM   2156  C   VAL A 268       1.396  15.903  12.120  1.00  7.92           C  
ANISOU 2156  C   VAL A 268     1132    962    915     -6    101    176       C  
ATOM   2157  O   VAL A 268       1.038  16.595  13.077  1.00  8.55           O  
ANISOU 2157  O   VAL A 268     1168   1073   1008    -48    135    136       O  
ATOM   2158  CB  VAL A 268       3.100  17.713  11.452  1.00  7.46           C  
ANISOU 2158  CB  VAL A 268     1035    890    911     18    113    208       C  
ATOM   2159  CG1 VAL A 268       4.000  17.690  12.689  1.00  8.28           C  
ANISOU 2159  CG1 VAL A 268     1232    836   1079     94    -17     93       C  
ATOM   2160  CG2 VAL A 268       3.826  18.292  10.233  1.00  8.12           C  
ANISOU 2160  CG2 VAL A 268     1205    920    962    -35     98    210       C  
ATOM   2161  N   ILE A 269       0.774  14.750  11.788  1.00  8.18           N  
ANISOU 2161  N   ILE A 269     1084   1028    994    -73     86    170       N  
ATOM   2162  CA  ILE A 269      -0.425  14.241  12.472  1.00  8.73           C  
ANISOU 2162  CA  ILE A 269     1071   1070   1176   -136     68    149       C  
ATOM   2163  C   ILE A 269      -0.186  12.821  13.024  1.00  8.53           C  
ANISOU 2163  C   ILE A 269     1149   1175    919   -178    110    200       C  
ATOM   2164  O   ILE A 269      -0.217  12.587  14.218  1.00  9.68           O  
ANISOU 2164  O   ILE A 269     1276   1351   1050     20    107    228       O  
ATOM   2165  CB  ILE A 269      -1.677  14.272  11.546  1.00  8.77           C  
ANISOU 2165  CB  ILE A 269     1045   1044   1242   -100    132    136       C  
ATOM   2166  CG1 ILE A 269      -1.949  15.651  10.946  1.00  9.40           C  
ANISOU 2166  CG1 ILE A 269     1126   1133   1311    126    158    157       C  
ATOM   2167  CG2 ILE A 269      -2.898  13.745  12.315  1.00  9.96           C  
ANISOU 2167  CG2 ILE A 269     1158   1200   1428   -163     64    231       C  
ATOM   2168  CD1 ILE A 269      -2.834  15.573   9.710  1.00 10.94           C  
ANISOU 2168  CD1 ILE A 269     1419   1396   1340    127     87    223       C  
ATOM   2169  N   GLY A 270       0.001  11.902  12.083  1.00  9.21           N  
ANISOU 2169  N   GLY A 270     1349   1040   1110    -53     79    247       N  
ATOM   2170  CA  GLY A 270       0.134  10.461  12.386  1.00 10.36           C  
ANISOU 2170  CA  GLY A 270     1641   1142   1152     22   -149    252       C  
ATOM   2171  C   GLY A 270      -1.003   9.649  11.803  1.00 10.70           C  
ANISOU 2171  C   GLY A 270     1672   1197   1196   -109     -1    226       C  
ATOM   2172  O   GLY A 270      -1.564   8.787  12.549  1.00 14.58           O  
ANISOU 2172  O   GLY A 270     2389   1571   1579   -558   -229    396       O  
ATOM   2173  N   ARG A 271      -1.393   9.877  10.562  1.00  9.94           N  
ANISOU 2173  N   ARG A 271     1319   1298   1159   -186     10    187       N  
ATOM   2174  CA  ARG A 271      -2.442   9.066   9.936  1.00 10.67           C  
ANISOU 2174  CA  ARG A 271     1497   1304   1253   -202     36     72       C  
ATOM   2175  C   ARG A 271      -1.898   8.560   8.596  1.00 10.10           C  
ANISOU 2175  C   ARG A 271     1392   1206   1239   -175     42    197       C  
ATOM   2176  O   ARG A 271      -1.299   9.317   7.829  1.00 10.71           O  
ANISOU 2176  O   ARG A 271     1392   1436   1241   -159     62    171       O  
ATOM   2177  CB  ARG A 271      -3.736   9.828   9.700  1.00 12.25           C  
ANISOU 2177  CB  ARG A 271     1481   1716   1458   -139    -20     24       C  
ATOM   2178  CG  ARG A 271      -4.456  10.295  10.953  1.00 14.91           C  
ANISOU 2178  CG  ARG A 271     1972   2099   1594      2     88    -41       C  
ATOM   2179  CD  ARG A 271      -5.650  11.181  10.559  1.00 17.65           C  
ANISOU 2179  CD  ARG A 271     2345   2307   2056    284    161    -60       C  
ATOM   2180  NE  ARG A 271      -6.615  10.463   9.738  1.00 21.79           N  
ANISOU 2180  NE  ARG A 271     2659   3104   2516     65    -62   -232       N  
ATOM   2181  CZ  ARG A 271      -7.632   9.743  10.163  1.00 27.27           C  
ANISOU 2181  CZ  ARG A 271     3187   3645   3528   -201    229    -77       C  
ATOM   2182  NH1 ARG A 271      -7.923   9.618  11.450  1.00 28.97           N  
ANISOU 2182  NH1 ARG A 271     3328   4063   3616   -323    444   -312       N  
ATOM   2183  NH2 ARG A 271      -8.362   9.164   9.219  1.00 29.88           N  
ANISOU 2183  NH2 ARG A 271     3513   4159   3682   -315    162   -306       N  
ATOM   2184  N   LEU A 272      -2.231   7.310   8.253  1.00 10.58           N  
ANISOU 2184  N   LEU A 272     1362   1248   1410   -134     43     34       N  
ATOM   2185  CA  LEU A 272      -1.773   6.768   6.964  1.00 12.13           C  
ANISOU 2185  CA  LEU A 272     1793   1445   1370   -157     -7     29       C  
ATOM   2186  C   LEU A 272      -2.383   7.560   5.809  1.00 10.81           C  
ANISOU 2186  C   LEU A 272     1376   1452   1280   -188     78     37       C  
ATOM   2187  O   LEU A 272      -1.669   7.867   4.802  1.00 12.73           O  
ANISOU 2187  O   LEU A 272     1616   1879   1342   -120    130    124       O  
ATOM   2188  CB  LEU A 272      -2.162   5.285   6.869  1.00 13.04           C  
ANISOU 2188  CB  LEU A 272     1870   1421   1662   -111     75    -12       C  
ATOM   2189  CG  LEU A 272      -1.603   4.381   7.939  1.00 14.71           C  
ANISOU 2189  CG  LEU A 272     2248   1425   1917     69    -45    -16       C  
ATOM   2190  CD1 LEU A 272      -2.189   2.973   7.731  1.00 18.65           C  
ANISOU 2190  CD1 LEU A 272     3041   1501   2546    -16   -283    139       C  
ATOM   2191  CD2 LEU A 272      -0.081   4.356   7.982  1.00 16.06           C  
ANISOU 2191  CD2 LEU A 272     2297   1905   1902    263    -17     35       C  
ATOM   2192  N   ASP A 273      -3.664   7.967   5.886  1.00 11.18           N  
ANISOU 2192  N   ASP A 273     1316   1638   1293   -222    -53     12       N  
ATOM   2193  CA  ASP A 273      -4.303   8.637   4.763  1.00 12.42           C  
ANISOU 2193  CA  ASP A 273     1472   1756   1490   -224    -64    265       C  
ATOM   2194  C   ASP A 273      -3.693  10.022   4.522  1.00 11.80           C  
ANISOU 2194  C   ASP A 273     1479   1687   1316   -157   -123    225       C  
ATOM   2195  O   ASP A 273      -3.472  10.394   3.351  1.00 13.31           O  
ANISOU 2195  O   ASP A 273     1613   2036   1410   -277   -177    297       O  
ATOM   2196  CB AASP A 273      -5.828   8.733   4.945  0.50 13.81           C  
ANISOU 2196  CB AASP A 273     1492   1913   1842   -289     24     61       C  
ATOM   2197  CG AASP A 273      -6.268   9.591   6.112  0.50 14.08           C  
ANISOU 2197  CG AASP A 273     1339   2021   1990   -212     28    -12       C  
ATOM   2198  OD1AASP A 273      -6.285   9.110   7.266  0.50 17.15           O  
ANISOU 2198  OD1AASP A 273     2089   2336   2091     33     -6     94       O  
ATOM   2199  OD2AASP A 273      -6.617  10.767   5.867  0.50 15.87           O  
ANISOU 2199  OD2AASP A 273     1563   2169   2299     61     68    -66       O  
ATOM   2200  CB BASP A 273      -5.825   8.725   4.879  0.50 14.61           C  
ANISOU 2200  CB BASP A 273     1533   2151   1867   -307     31    158       C  
ATOM   2201  CG BASP A 273      -6.393   9.308   6.144  0.50 16.28           C  
ANISOU 2201  CG BASP A 273     1878   2476   1833   -184     74    202       C  
ATOM   2202  OD1BASP A 273      -5.698   9.829   7.041  0.50 15.05           O  
ANISOU 2202  OD1BASP A 273     1697   2235   1787   -262    216    275       O  
ATOM   2203  OD2BASP A 273      -7.644   9.245   6.275  0.50 19.84           O  
ANISOU 2203  OD2BASP A 273     1874   3311   2355   -103    -15    277       O  
ATOM   2204  N   THR A 274      -3.381  10.771   5.587  1.00 10.55           N  
ANISOU 2204  N   THR A 274     1276   1504   1227   -132    -26    187       N  
ATOM   2205  CA  THR A 274      -2.765  12.097   5.395  1.00 10.48           C  
ANISOU 2205  CA  THR A 274     1324   1383   1276     33     58    260       C  
ATOM   2206  C   THR A 274      -1.325  11.981   4.949  1.00  9.87           C  
ANISOU 2206  C   THR A 274     1292   1288   1169    -25    -37    204       C  
ATOM   2207  O   THR A 274      -0.827  12.907   4.275  1.00 10.50           O  
ANISOU 2207  O   THR A 274     1290   1426   1274    -16     38    161       O  
ATOM   2208  CB  THR A 274      -2.949  12.974   6.656  1.00 11.18           C  
ANISOU 2208  CB  THR A 274     1285   1613   1351    103      9    192       C  
ATOM   2209  OG1 THR A 274      -2.649  12.235   7.846  1.00 11.35           O  
ANISOU 2209  OG1 THR A 274     1558   1443   1311    -30    106     69       O  
ATOM   2210  CG2 THR A 274      -4.392  13.479   6.793  1.00 13.80           C  
ANISOU 2210  CG2 THR A 274     1508   1920   1817    291     17     53       C  
ATOM   2211  N   MET A 275      -0.606  10.883   5.234  1.00  9.90           N  
ANISOU 2211  N   MET A 275     1268   1315   1179     10     -4    153       N  
ATOM   2212  CA  MET A 275       0.743  10.711   4.655  1.00  9.58           C  
ANISOU 2212  CA  MET A 275     1362   1148   1130     39     -7     47       C  
ATOM   2213  C   MET A 275       0.636  10.639   3.129  1.00  9.22           C  
ANISOU 2213  C   MET A 275     1232   1142   1127    -14     50    144       C  
ATOM   2214  O   MET A 275       1.453  11.263   2.417  1.00 10.58           O  
ANISOU 2214  O   MET A 275     1519   1351   1151    -36     98    100       O  
ATOM   2215  CB  MET A 275       1.411   9.467   5.262  1.00  9.52           C  
ANISOU 2215  CB  MET A 275     1313   1102   1201     11     -5     84       C  
ATOM   2216  CG  MET A 275       1.762   9.704   6.734  1.00  9.83           C  
ANISOU 2216  CG  MET A 275     1336   1179   1220      9     64     71       C  
ATOM   2217  SD  MET A 275       2.298   8.164   7.559  1.00 10.44           S  
ANISOU 2217  SD  MET A 275     1416   1186   1364     13    -22    262       S  
ATOM   2218  CE  MET A 275       2.277   8.774   9.275  1.00 12.90           C  
ANISOU 2218  CE  MET A 275     1744   1861   1297     96   -110    286       C  
ATOM   2219  N   VAL A 276      -0.302   9.878   2.606  1.00  9.88           N  
ANISOU 2219  N   VAL A 276     1379   1289   1085    -10    -65    103       N  
ATOM   2220  CA  VAL A 276      -0.468   9.742   1.137  1.00 11.10           C  
ANISOU 2220  CA  VAL A 276     1705   1371   1140   -101    -79     -5       C  
ATOM   2221  C   VAL A 276      -0.982  11.043   0.504  1.00 10.01           C  
ANISOU 2221  C   VAL A 276     1410   1327   1067     19    -14    -19       C  
ATOM   2222  O   VAL A 276      -0.483  11.482  -0.541  1.00 11.13           O  
ANISOU 2222  O   VAL A 276     1565   1523   1142     31    -53    107       O  
ATOM   2223  CB  VAL A 276      -1.320   8.526   0.757  1.00 13.03           C  
ANISOU 2223  CB  VAL A 276     1992   1485   1475   -228   -265      2       C  
ATOM   2224  CG1 VAL A 276      -1.421   8.438  -0.776  1.00 16.24           C  
ANISOU 2224  CG1 VAL A 276     2693   1880   1598   -254   -370    -19       C  
ATOM   2225  CG2 VAL A 276      -0.701   7.244   1.313  1.00 15.04           C  
ANISOU 2225  CG2 VAL A 276     2640   1489   1584    162    -23    -45       C  
ATOM   2226  N   THR A 277      -1.924  11.711   1.150  1.00 10.41           N  
ANISOU 2226  N   THR A 277     1345   1354   1255     88    -88     64       N  
ATOM   2227  CA  THR A 277      -2.448  13.007   0.690  1.00 11.24           C  
ANISOU 2227  CA  THR A 277     1222   1583   1465     44   -173    186       C  
ATOM   2228  C   THR A 277      -1.336  14.057   0.642  1.00  9.91           C  
ANISOU 2228  C   THR A 277     1193   1345   1225    135     48    100       C  
ATOM   2229  O   THR A 277      -1.225  14.827  -0.339  1.00 10.33           O  
ANISOU 2229  O   THR A 277     1299   1415   1211    212     15    135       O  
ATOM   2230  CB  THR A 277      -3.595  13.484   1.666  1.00 13.52           C  
ANISOU 2230  CB  THR A 277     1175   1639   2324    163    106    216       C  
ATOM   2231  OG1 THR A 277      -4.715  12.593   1.473  1.00 16.68           O  
ANISOU 2231  OG1 THR A 277     1710   2304   2324   -189    190    -56       O  
ATOM   2232  CG2 THR A 277      -4.034  14.902   1.409  1.00 15.65           C  
ANISOU 2232  CG2 THR A 277     1726   1977   2242    357     73    320       C  
ATOM   2233  N   ALA A 278      -0.506  14.119   1.698  1.00  9.48           N  
ANISOU 2233  N   ALA A 278     1125   1293   1183     83     59    109       N  
ATOM   2234  CA  ALA A 278       0.586  15.081   1.729  1.00  9.19           C  
ANISOU 2234  CA  ALA A 278     1291   1183   1019     11     41    141       C  
ATOM   2235  C   ALA A 278       1.565  14.822   0.586  1.00  8.81           C  
ANISOU 2235  C   ALA A 278     1249   1097   1001    126    -14    110       C  
ATOM   2236  O   ALA A 278       2.075  15.748  -0.057  1.00  9.21           O  
ANISOU 2236  O   ALA A 278     1205   1203   1093    175     68    144       O  
ATOM   2237  CB  ALA A 278       1.247  15.124   3.088  1.00  9.79           C  
ANISOU 2237  CB  ALA A 278     1471   1226   1022    132     75    112       C  
ATOM   2238  N   LEU A 279       1.885  13.538   0.311  1.00  9.31           N  
ANISOU 2238  N   LEU A 279     1305   1214   1018    209     25    100       N  
ATOM   2239  CA  LEU A 279       2.768  13.263  -0.838  1.00  9.33           C  
ANISOU 2239  CA  LEU A 279     1271   1253   1021    153     11     76       C  
ATOM   2240  C   LEU A 279       2.131  13.735  -2.152  1.00  9.19           C  
ANISOU 2240  C   LEU A 279     1235   1204   1054    164     73    141       C  
ATOM   2241  O   LEU A 279       2.788  14.382  -2.985  1.00 10.19           O  
ANISOU 2241  O   LEU A 279     1357   1364   1150    292     99    198       O  
ATOM   2242  CB  LEU A 279       3.062  11.740  -0.909  1.00 10.53           C  
ANISOU 2242  CB  LEU A 279     1600   1330   1069    246     -5     10       C  
ATOM   2243  CG  LEU A 279       3.879  11.333  -2.152  1.00 10.39           C  
ANISOU 2243  CG  LEU A 279     1483   1363   1102    317    -46    122       C  
ATOM   2244  CD1 LEU A 279       5.281  11.880  -2.106  1.00 10.45           C  
ANISOU 2244  CD1 LEU A 279     1479   1391   1101    340     74     84       C  
ATOM   2245  CD2 LEU A 279       3.903   9.799  -2.240  1.00 11.55           C  
ANISOU 2245  CD2 LEU A 279     1725   1366   1299    278    -31     25       C  
ATOM   2246  N   SER A 280       0.841  13.387  -2.339  1.00  9.93           N  
ANISOU 2246  N   SER A 280     1272   1382   1118    197    -90    135       N  
ATOM   2247  CA  SER A 280       0.170  13.722  -3.602  1.00 10.64           C  
ANISOU 2247  CA  SER A 280     1573   1419   1048    159   -116     21       C  
ATOM   2248  C   SER A 280       0.093  15.217  -3.871  1.00 10.72           C  
ANISOU 2248  C   SER A 280     1453   1562   1056    270   -147    100       C  
ATOM   2249  O   SER A 280       0.157  15.617  -5.048  1.00 12.35           O  
ANISOU 2249  O   SER A 280     1885   1684   1123    325   -142     87       O  
ATOM   2250  CB ASER A 280      -1.262  13.139  -3.486  0.51 11.45           C  
ANISOU 2250  CB ASER A 280     1586   1562   1204     17   -598    181       C  
ATOM   2251  OG ASER A 280      -1.204  11.727  -3.370  0.51 13.08           O  
ANISOU 2251  OG ASER A 280     1854   1598   1520     10   -149   -193       O  
ATOM   2252  CB BSER A 280      -1.233  13.099  -3.636  0.49 13.18           C  
ANISOU 2252  CB BSER A 280     1672   1632   1705     33   -240     79       C  
ATOM   2253  OG BSER A 280      -1.878  13.381  -4.868  0.49 16.01           O  
ANISOU 2253  OG BSER A 280     2005   2399   1680     72   -130    258       O  
ATOM   2254  N   CYS A 281      -0.035  16.059  -2.844  1.00  9.94           N  
ANISOU 2254  N   CYS A 281     1327   1403   1046    340     -3    146       N  
ATOM   2255  CA  CYS A 281      -0.185  17.498  -3.052  1.00 10.19           C  
ANISOU 2255  CA  CYS A 281     1312   1402   1160    348     22    216       C  
ATOM   2256  C   CYS A 281       1.102  18.224  -3.405  1.00 10.15           C  
ANISOU 2256  C   CYS A 281     1380   1307   1169    346    127    129       C  
ATOM   2257  O   CYS A 281       0.992  19.396  -3.802  1.00 11.03           O  
ANISOU 2257  O   CYS A 281     1501   1407   1284    349      0    195       O  
ATOM   2258  CB  CYS A 281      -0.879  18.123  -1.843  1.00 11.10           C  
ANISOU 2258  CB  CYS A 281     1470   1468   1280    404    117     76       C  
ATOM   2259  SG  CYS A 281       0.222  18.584  -0.454  1.00 10.51           S  
ANISOU 2259  SG  CYS A 281     1530   1388   1076    359    150    137       S  
ATOM   2260  N   CYS A 282       2.260  17.575  -3.272  1.00 10.44           N  
ANISOU 2260  N   CYS A 282     1332   1464   1172    391    137    265       N  
ATOM   2261  CA  CYS A 282       3.498  18.210  -3.738  1.00  9.98           C  
ANISOU 2261  CA  CYS A 282     1284   1255   1252    373     70    254       C  
ATOM   2262  C   CYS A 282       3.627  18.033  -5.272  1.00 10.24           C  
ANISOU 2262  C   CYS A 282     1282   1392   1218    163     77    121       C  
ATOM   2263  O   CYS A 282       3.089  17.076  -5.848  1.00 11.43           O  
ANISOU 2263  O   CYS A 282     1595   1447   1300    195    268    107       O  
ATOM   2264  CB  CYS A 282       4.750  17.839  -2.970  1.00 12.36           C  
ANISOU 2264  CB  CYS A 282     1444   1808   1443    417    102    542       C  
ATOM   2265  SG  CYS A 282       5.525  16.236  -3.212  1.00 11.30           S  
ANISOU 2265  SG  CYS A 282     1552   1564   1180    398     33    191       S  
ATOM   2266  N   GLN A 283       4.298  19.010  -5.903  1.00 10.18           N  
ANISOU 2266  N   GLN A 283     1473   1302   1093    263    162    113       N  
ATOM   2267  CA  GLN A 283       4.410  19.030  -7.382  1.00 10.43           C  
ANISOU 2267  CA  GLN A 283     1534   1387   1044    347    177     73       C  
ATOM   2268  C   GLN A 283       5.038  17.745  -7.890  1.00  9.86           C  
ANISOU 2268  C   GLN A 283     1254   1461   1031    384    105    131       C  
ATOM   2269  O   GLN A 283       6.054  17.244  -7.378  1.00 10.16           O  
ANISOU 2269  O   GLN A 283     1395   1517    946    403     59    208       O  
ATOM   2270  CB  GLN A 283       5.145  20.293  -7.811  1.00 11.17           C  
ANISOU 2270  CB  GLN A 283     1691   1460   1092    390    134    185       C  
ATOM   2271  CG  GLN A 283       4.880  20.745  -9.259  1.00 12.37           C  
ANISOU 2271  CG  GLN A 283     1916   1602   1180    361    142    326       C  
ATOM   2272  CD  GLN A 283       5.510  19.865 -10.317  1.00 12.15           C  
ANISOU 2272  CD  GLN A 283     1713   1763   1142    432     50    344       C  
ATOM   2273  OE1 GLN A 283       6.605  19.339 -10.077  1.00 12.02           O  
ANISOU 2273  OE1 GLN A 283     1717   1672   1178    470    176    233       O  
ATOM   2274  NE2 GLN A 283       4.868  19.686 -11.488  1.00 14.44           N  
ANISOU 2274  NE2 GLN A 283     2186   2050   1249    580    -19    192       N  
ATOM   2275  N   GLU A 284       4.441  17.167  -8.946  1.00 10.50           N  
ANISOU 2275  N   GLU A 284     1500   1511    977    380    -73    141       N  
ATOM   2276  CA  GLU A 284       4.769  15.800  -9.344  1.00 10.65           C  
ANISOU 2276  CA  GLU A 284     1442   1530   1073    335     58    121       C  
ATOM   2277  C   GLU A 284       6.189  15.591  -9.869  1.00 10.08           C  
ANISOU 2277  C   GLU A 284     1447   1477    905    307    -15     47       C  
ATOM   2278  O   GLU A 284       6.668  14.427  -9.824  1.00 11.22           O  
ANISOU 2278  O   GLU A 284     1619   1545   1100    443     29     73       O  
ATOM   2279  CB  GLU A 284       3.736  15.283 -10.380  1.00 11.70           C  
ANISOU 2279  CB  GLU A 284     1565   1685   1196    313    -83    171       C  
ATOM   2280  CG  GLU A 284       3.813  16.028 -11.710  1.00 12.74           C  
ANISOU 2280  CG  GLU A 284     1612   2126   1104    269    -56    122       C  
ATOM   2281  CD  GLU A 284       2.810  15.622 -12.765  1.00 15.21           C  
ANISOU 2281  CD  GLU A 284     1838   2603   1338    180    -95     -4       C  
ATOM   2282  OE1 GLU A 284       2.010  14.702 -12.556  1.00 18.98           O  
ANISOU 2282  OE1 GLU A 284     2603   3182   1428   -332   -227    255       O  
ATOM   2283  OE2 GLU A 284       2.804  16.251 -13.852  1.00 16.05           O  
ANISOU 2283  OE2 GLU A 284     1949   2872   1278    337   -105     29       O  
ATOM   2284  N   ALA A 285       6.815  16.607 -10.401  1.00 10.63           N  
ANISOU 2284  N   ALA A 285     1382   1608   1048    294     60    181       N  
ATOM   2285  CA  ALA A 285       8.161  16.535 -10.990  1.00 11.18           C  
ANISOU 2285  CA  ALA A 285     1443   1812    991    429     80    111       C  
ATOM   2286  C   ALA A 285       9.280  16.869 -10.017  1.00 11.06           C  
ANISOU 2286  C   ALA A 285     1487   1727    989    472     24    148       C  
ATOM   2287  O   ALA A 285      10.404  16.320 -10.141  1.00 12.26           O  
ANISOU 2287  O   ALA A 285     1610   1874   1174    466     71     44       O  
ATOM   2288  CB  ALA A 285       8.242  17.491 -12.191  1.00 11.65           C  
ANISOU 2288  CB  ALA A 285     1584   1911    933    355     95    181       C  
ATOM   2289  N   TYR A 286       9.056  17.781  -9.058  1.00 10.92           N  
ANISOU 2289  N   TYR A 286     1504   1780    864    437     50    107       N  
ATOM   2290  CA  TYR A 286      10.155  18.283  -8.216  1.00 11.30           C  
ANISOU 2290  CA  TYR A 286     1573   1720    999    207    110     48       C  
ATOM   2291  C   TYR A 286       9.733  18.472  -6.753  1.00  9.86           C  
ANISOU 2291  C   TYR A 286     1390   1343   1013    261      3    250       C  
ATOM   2292  O   TYR A 286      10.576  18.967  -5.975  1.00 11.06           O  
ANISOU 2292  O   TYR A 286     1507   1699    996    280      4    108       O  
ATOM   2293  CB  TYR A 286      10.775  19.558  -8.796  1.00 11.66           C  
ANISOU 2293  CB  TYR A 286     1722   1803    905    226    133    110       C  
ATOM   2294  CG  TYR A 286       9.781  20.687  -9.033  1.00 11.74           C  
ANISOU 2294  CG  TYR A 286     1848   1665    950    241    100    163       C  
ATOM   2295  CD1 TYR A 286       9.249  21.404  -7.965  1.00 12.46           C  
ANISOU 2295  CD1 TYR A 286     2008   1724   1000    225    137    136       C  
ATOM   2296  CD2 TYR A 286       9.414  21.081 -10.323  1.00 12.60           C  
ANISOU 2296  CD2 TYR A 286     2050   1740    999    287    164    178       C  
ATOM   2297  CE1 TYR A 286       8.354  22.432  -8.150  1.00 13.45           C  
ANISOU 2297  CE1 TYR A 286     2295   1737   1077    323     84    147       C  
ATOM   2298  CE2 TYR A 286       8.519  22.121 -10.527  1.00 13.00           C  
ANISOU 2298  CE2 TYR A 286     2271   1617   1050    208    -82    246       C  
ATOM   2299  CZ  TYR A 286       8.001  22.776  -9.438  1.00 13.09           C  
ANISOU 2299  CZ  TYR A 286     2215   1577   1183    290    -26    220       C  
ATOM   2300  OH  TYR A 286       7.106  23.813  -9.697  1.00 16.18           O  
ANISOU 2300  OH  TYR A 286     2771   1987   1388    606   -105    290       O  
ATOM   2301  N   GLY A 287       8.511  18.129  -6.383  1.00  9.96           N  
ANISOU 2301  N   GLY A 287     1412   1442    928    287     26    226       N  
ATOM   2302  CA  GLY A 287       8.060  18.291  -4.995  1.00  9.95           C  
ANISOU 2302  CA  GLY A 287     1597   1241    942    339    118    143       C  
ATOM   2303  C   GLY A 287       8.766  17.342  -4.022  1.00  9.68           C  
ANISOU 2303  C   GLY A 287     1345   1254   1079    356     99     63       C  
ATOM   2304  O   GLY A 287       9.261  16.281  -4.401  1.00 10.36           O  
ANISOU 2304  O   GLY A 287     1674   1345    916    460    127    200       O  
ATOM   2305  N   VAL A 288       8.752  17.783  -2.740  1.00  9.61           N  
ANISOU 2305  N   VAL A 288     1470   1261    921    433    110    214       N  
ATOM   2306  CA  VAL A 288       9.338  17.015  -1.619  1.00  9.47           C  
ANISOU 2306  CA  VAL A 288     1345   1207   1047    292     52    273       C  
ATOM   2307  C   VAL A 288       8.281  16.896  -0.500  1.00  8.80           C  
ANISOU 2307  C   VAL A 288     1274   1131    937    248     18    171       C  
ATOM   2308  O   VAL A 288       7.704  17.949  -0.151  1.00 10.66           O  
ANISOU 2308  O   VAL A 288     1722   1214   1114    358    223    259       O  
ATOM   2309  CB  VAL A 288      10.620  17.681  -1.087  1.00 10.26           C  
ANISOU 2309  CB  VAL A 288     1384   1544    970    190     88    309       C  
ATOM   2310  CG1 VAL A 288      11.165  16.957   0.145  1.00 12.53           C  
ANISOU 2310  CG1 VAL A 288     1594   2020   1147    217   -101    281       C  
ATOM   2311  CG2 VAL A 288      11.712  17.792  -2.151  1.00 11.85           C  
ANISOU 2311  CG2 VAL A 288     1552   1761   1189    277    232    331       C  
ATOM   2312  N   SER A 289       8.071  15.708   0.034  1.00  8.50           N  
ANISOU 2312  N   SER A 289     1293   1043    894    309     47    189       N  
ATOM   2313  CA  SER A 289       7.147  15.512   1.158  1.00  8.24           C  
ANISOU 2313  CA  SER A 289     1275    986    870    273     39    178       C  
ATOM   2314  C   SER A 289       7.890  14.807   2.307  1.00  8.27           C  
ANISOU 2314  C   SER A 289     1172    991    980    395     86    162       C  
ATOM   2315  O   SER A 289       8.579  13.815   2.067  1.00  9.01           O  
ANISOU 2315  O   SER A 289     1333   1157    933    470      9     99       O  
ATOM   2316  CB  SER A 289       5.909  14.731   0.763  1.00  9.07           C  
ANISOU 2316  CB  SER A 289     1340   1181    925    221     29    154       C  
ATOM   2317  OG  SER A 289       4.946  14.667   1.790  1.00  9.51           O  
ANISOU 2317  OG  SER A 289     1229   1384   1000    133     -4    144       O  
ATOM   2318  N   VAL A 290       7.726  15.330   3.523  1.00  7.82           N  
ANISOU 2318  N   VAL A 290     1146    974    854    318     14    140       N  
ATOM   2319  CA  VAL A 290       8.358  14.803   4.734  1.00  7.92           C  
ANISOU 2319  CA  VAL A 290     1146    888    974    277     20    239       C  
ATOM   2320  C   VAL A 290       7.326  14.275   5.717  1.00  7.75           C  
ANISOU 2320  C   VAL A 290     1030   1003    909    215     26    124       C  
ATOM   2321  O   VAL A 290       6.421  15.026   6.142  1.00  8.63           O  
ANISOU 2321  O   VAL A 290     1162   1080   1036    200     77    111       O  
ATOM   2322  CB  VAL A 290       9.249  15.869   5.402  1.00  8.66           C  
ANISOU 2322  CB  VAL A 290     1265   1085    940     76     70    186       C  
ATOM   2323  CG1 VAL A 290       9.926  15.288   6.659  1.00 10.16           C  
ANISOU 2323  CG1 VAL A 290     1324   1419   1118    209    -10    203       C  
ATOM   2324  CG2 VAL A 290      10.299  16.451   4.459  1.00  9.80           C  
ANISOU 2324  CG2 VAL A 290     1335   1277   1111     60     52    326       C  
ATOM   2325  N   ILE A 291       7.456  13.013   6.099  1.00  8.17           N  
ANISOU 2325  N   ILE A 291     1224   1003    877    209    137    208       N  
ATOM   2326  CA  ILE A 291       6.652  12.419   7.181  1.00  8.02           C  
ANISOU 2326  CA  ILE A 291     1034   1033    980    125     51    214       C  
ATOM   2327  C   ILE A 291       7.318  12.672   8.540  1.00  7.69           C  
ANISOU 2327  C   ILE A 291      968   1004    949    116     30    246       C  
ATOM   2328  O   ILE A 291       8.482  12.314   8.755  1.00  8.39           O  
ANISOU 2328  O   ILE A 291      969   1203   1016    189     59    150       O  
ATOM   2329  CB  ILE A 291       6.460  10.904   7.002  1.00  8.29           C  
ANISOU 2329  CB  ILE A 291     1126   1097    928    163    -21    267       C  
ATOM   2330  CG1 ILE A 291       5.918  10.528   5.608  1.00  9.71           C  
ANISOU 2330  CG1 ILE A 291     1355   1242   1091     51    -27    179       C  
ATOM   2331  CG2 ILE A 291       5.587  10.354   8.112  1.00  9.22           C  
ANISOU 2331  CG2 ILE A 291     1361   1082   1058    -37     64    219       C  
ATOM   2332  CD1 ILE A 291       5.719   9.034   5.386  1.00 11.08           C  
ANISOU 2332  CD1 ILE A 291     1716   1256   1239      6      0    118       C  
ATOM   2333  N   VAL A 292       6.541  13.313   9.413  1.00  7.37           N  
ANISOU 2333  N   VAL A 292      932    981    886     24     23    191       N  
ATOM   2334  CA  VAL A 292       6.905  13.568  10.831  1.00  7.68           C  
ANISOU 2334  CA  VAL A 292     1046    935    937    110     57    208       C  
ATOM   2335  C   VAL A 292       5.999  12.822  11.789  1.00  7.38           C  
ANISOU 2335  C   VAL A 292     1110    747    947    162    137    159       C  
ATOM   2336  O   VAL A 292       6.432  12.340  12.858  1.00  8.43           O  
ANISOU 2336  O   VAL A 292     1161   1062    980    156     91    232       O  
ATOM   2337  CB  VAL A 292       6.928  15.082  11.134  1.00  8.33           C  
ANISOU 2337  CB  VAL A 292     1196    925   1044    -12    158    141       C  
ATOM   2338  CG1 VAL A 292       7.449  15.360  12.543  1.00  9.26           C  
ANISOU 2338  CG1 VAL A 292     1192   1115   1210    120     24     67       C  
ATOM   2339  CG2 VAL A 292       7.704  15.867  10.090  1.00  9.85           C  
ANISOU 2339  CG2 VAL A 292     1329   1185   1228    -32    110    258       C  
ATOM   2340  N   GLY A 293       4.681  12.726  11.500  1.00  8.44           N  
ANISOU 2340  N   GLY A 293     1143   1106    959     34     98    240       N  
ATOM   2341  CA  GLY A 293       3.753  12.065  12.412  1.00  8.44           C  
ANISOU 2341  CA  GLY A 293     1083   1056   1069     26    166    191       C  
ATOM   2342  C   GLY A 293       4.040  10.587  12.609  1.00  8.33           C  
ANISOU 2342  C   GLY A 293     1255    960    948    -29     79    126       C  
ATOM   2343  O   GLY A 293       4.511   9.896  11.707  1.00  9.63           O  
ANISOU 2343  O   GLY A 293     1493   1063   1103     72    128    135       O  
ATOM   2344  N   VAL A 294       3.632  10.089  13.795  1.00  9.16           N  
ANISOU 2344  N   VAL A 294     1511    955   1015     59    119    235       N  
ATOM   2345  CA  VAL A 294       3.777   8.668  14.167  1.00 10.16           C  
ANISOU 2345  CA  VAL A 294     1693    930   1239     29     39    188       C  
ATOM   2346  C   VAL A 294       2.427   7.955  13.964  1.00 10.74           C  
ANISOU 2346  C   VAL A 294     1940    794   1347   -123   -203    410       C  
ATOM   2347  O   VAL A 294       1.476   8.273  14.558  1.00 14.85           O  
ANISOU 2347  O   VAL A 294     1751   1402   2491    -57    -94    628       O  
ATOM   2348  CB  VAL A 294       4.213   8.540  15.634  1.00 10.95           C  
ANISOU 2348  CB  VAL A 294     1730   1157   1272     93    -87    291       C  
ATOM   2349  CG1 VAL A 294       4.165   7.102  16.141  1.00 12.69           C  
ANISOU 2349  CG1 VAL A 294     2148   1239   1435     99    -48    338       C  
ATOM   2350  CG2 VAL A 294       5.607   9.129  15.839  1.00 14.21           C  
ANISOU 2350  CG2 VAL A 294     1867   1536   1995     18   -356    324       C  
ATOM   2351  N  APRO A 295       2.237   6.954  13.067  0.56 12.29           N  
ANISOU 2351  N  APRO A 295     1840   1170   1659   -177   -192    148       N  
ATOM   2352  CA APRO A 295       0.917   6.328  12.919  0.56 11.65           C  
ANISOU 2352  CA APRO A 295     1718   1177   1533    -26    -59    169       C  
ATOM   2353  C  APRO A 295       0.743   5.115  13.828  0.56 10.76           C  
ANISOU 2353  C  APRO A 295     1528   1188   1371    -16     37    127       C  
ATOM   2354  O  APRO A 295       1.684   4.679  14.497  0.56 11.06           O  
ANISOU 2354  O  APRO A 295     1505   1237   1462     18     76    110       O  
ATOM   2355  CB APRO A 295       0.930   5.858  11.449  0.56 14.65           C  
ANISOU 2355  CB APRO A 295     2222   1713   1632    -24    -75    -23       C  
ATOM   2356  CG APRO A 295       2.361   5.418  11.287  0.56 15.83           C  
ANISOU 2356  CG APRO A 295     2184   1961   1868    -77   -164    -28       C  
ATOM   2357  CD APRO A 295       3.231   6.345  12.065  0.56 14.04           C  
ANISOU 2357  CD APRO A 295     1705   1716   1914    199   -164    118       C  
ATOM   2358  N  BPRO A 295       2.854   6.926  13.040  0.44 11.48           N  
ANISOU 2358  N  BPRO A 295     1756    979   1629   -238   -210    308       N  
ATOM   2359  CA BPRO A 295       1.783   6.076  12.504  0.44 11.51           C  
ANISOU 2359  CA BPRO A 295     1729   1160   1485   -259   -145    105       C  
ATOM   2360  C  BPRO A 295       1.451   4.965  13.480  0.44 10.55           C  
ANISOU 2360  C  BPRO A 295     1572    998   1440    -14   -157    108       C  
ATOM   2361  O  BPRO A 295       2.283   4.572  14.312  0.44 10.87           O  
ANISOU 2361  O  BPRO A 295     1530   1074   1527    -71    -94    280       O  
ATOM   2362  CB BPRO A 295       2.308   5.468  11.187  0.44 13.56           C  
ANISOU 2362  CB BPRO A 295     2146   1432   1574   -277   -166   -214       C  
ATOM   2363  CG BPRO A 295       3.727   5.163  11.619  0.44 12.20           C  
ANISOU 2363  CG BPRO A 295     2124   1097   1414   -102     72   -369       C  
ATOM   2364  CD BPRO A 295       4.135   6.441  12.346  0.44 11.24           C  
ANISOU 2364  CD BPRO A 295     1935   1056   1281   -359   -233   -151       C  
ATOM   2365  N  APRO A 296      -0.439   4.513  13.847  0.56 11.48           N  
ANISOU 2365  N  APRO A 296     1589   1285   1488    -90     -5    203       N  
ATOM   2366  CA APRO A 296      -0.715   3.322  14.669  0.56 12.06           C  
ANISOU 2366  CA APRO A 296     1850   1250   1483   -171     25    198       C  
ATOM   2367  C  APRO A 296       0.236   2.185  14.344  0.56 11.95           C  
ANISOU 2367  C  APRO A 296     1788   1393   1360   -180    -67     53       C  
ATOM   2368  O  APRO A 296       0.381   1.851  13.163  0.56 12.15           O  
ANISOU 2368  O  APRO A 296     1698   1584   1333    -56     65    194       O  
ATOM   2369  CB APRO A 296      -2.180   2.940  14.381  0.56 14.47           C  
ANISOU 2369  CB APRO A 296     1791   1854   1853    -69     20     17       C  
ATOM   2370  CG APRO A 296      -2.734   4.265  13.903  0.56 14.58           C  
ANISOU 2370  CG APRO A 296     1843   1694   2004   -142   -164    -84       C  
ATOM   2371  CD APRO A 296      -1.632   4.958  13.144  0.56 12.81           C  
ANISOU 2371  CD APRO A 296     1734   1327   1807     -3   -251     29       C  
ATOM   2372  N  BPRO A 296       0.233   4.451  13.392  0.44 11.14           N  
ANISOU 2372  N  BPRO A 296     1518   1202   1511      3     69    -27       N  
ATOM   2373  CA BPRO A 296      -0.228   3.381  14.264  0.44 11.31           C  
ANISOU 2373  CA BPRO A 296     1603   1287   1407    103    160     -4       C  
ATOM   2374  C  BPRO A 296       0.669   2.164  14.112  0.44  9.96           C  
ANISOU 2374  C  BPRO A 296     1668    968   1146   -140    148    103       C  
ATOM   2375  O  BPRO A 296       1.018   1.731  13.015  0.44  8.60           O  
ANISOU 2375  O  BPRO A 296     1144    941   1182   -109    148    125       O  
ATOM   2376  CB BPRO A 296      -1.695   3.086  13.919  0.44 13.59           C  
ANISOU 2376  CB BPRO A 296     1580   1785   1798    -26    307     80       C  
ATOM   2377  CG BPRO A 296      -1.851   3.755  12.576  0.44 14.96           C  
ANISOU 2377  CG BPRO A 296     1737   2000   1948   -120   -156    117       C  
ATOM   2378  CD BPRO A 296      -0.797   4.832  12.421  0.44 12.52           C  
ANISOU 2378  CD BPRO A 296     1545   1466   1745    167     35     17       C  
ATOM   2379  CA  ASP A 297       1.811   0.479  15.273  1.00 12.57           C  
ANISOU 2379  CA  ASP A 297     2019   1302   1457   -212    -27    204       C  
ATOM   2380  C   ASP A 297       1.469  -0.620  14.285  1.00 12.60           C  
ANISOU 2380  C   ASP A 297     1943   1279   1564   -137   -105    200       C  
ATOM   2381  O   ASP A 297       0.362  -1.142  14.213  1.00 13.76           O  
ANISOU 2381  O   ASP A 297     2201   1325   1703   -460    -62    169       O  
ATOM   2382  CB  ASP A 297       1.942  -0.180  16.667  1.00 13.75           C  
ANISOU 2382  CB  ASP A 297     2281   1441   1502   -216    -34    230       C  
ATOM   2383  CG  ASP A 297       3.024  -1.236  16.655  1.00 15.23           C  
ANISOU 2383  CG  ASP A 297     2253   1581   1952   -191    -65     70       C  
ATOM   2384  OD1 ASP A 297       4.233  -0.857  16.636  1.00 16.56           O  
ANISOU 2384  OD1 ASP A 297     2261   1968   2062   -215   -134    158       O  
ATOM   2385  OD2 ASP A 297       2.757  -2.465  16.650  1.00 16.35           O  
ANISOU 2385  OD2 ASP A 297     2661   1526   2025   -160   -112    235       O  
ATOM   2386  N  AASP A 297       0.804   1.532  15.363  0.56 12.77           N  
ANISOU 2386  N  AASP A 297     2069   1230   1551   -234    -89    311       N  
ATOM   2387  N  BASP A 297       0.889   1.577  15.301  0.44 12.02           N  
ANISOU 2387  N  BASP A 297     2054   1088   1423   -245   -126    329       N  
ATOM   2388  N   SER A 298       2.489  -0.976  13.488  1.00 15.05           N  
ANISOU 2388  N   SER A 298     2139   1791   1788   -165     45    156       N  
ATOM   2389  CA  SER A 298       2.502  -2.090  12.560  1.00 18.33           C  
ANISOU 2389  CA  SER A 298     2701   2186   2079     76    -75    -69       C  
ATOM   2390  C   SER A 298       1.524  -1.982  11.423  1.00 19.46           C  
ANISOU 2390  C   SER A 298     2787   2531   2075    101   -122   -243       C  
ATOM   2391  O   SER A 298       1.349  -2.979  10.688  1.00 24.91           O  
ANISOU 2391  O   SER A 298     3702   2839   2924    133   -410   -669       O  
ATOM   2392  CB  SER A 298       2.315  -3.413  13.333  1.00 18.59           C  
ANISOU 2392  CB  SER A 298     2736   2172   2155    -39    -20   -115       C  
ATOM   2393  OG  SER A 298       3.403  -3.638  14.236  1.00 21.07           O  
ANISOU 2393  OG  SER A 298     3165   2167   2673    102   -344    199       O  
ATOM   2394  N   GLN A 299       0.914  -0.861  11.136  1.00 16.42           N  
ANISOU 2394  N   GLN A 299     2494   2160   1584   -389     99    104       N  
ATOM   2395  CA  GLN A 299      -0.031  -0.697  10.033  1.00 16.06           C  
ANISOU 2395  CA  GLN A 299     2375   2157   1568   -353     95     93       C  
ATOM   2396  C   GLN A 299       0.643  -0.197   8.764  1.00 15.61           C  
ANISOU 2396  C   GLN A 299     2353   2120   1457   -493     36     27       C  
ATOM   2397  O   GLN A 299       1.484   0.712   8.829  1.00 18.01           O  
ANISOU 2397  O   GLN A 299     2939   2245   1660   -797    176     28       O  
ATOM   2398  CB AGLN A 299      -1.166   0.239  10.440  0.73 17.86           C  
ANISOU 2398  CB AGLN A 299     2424   2325   2038   -241     92    204       C  
ATOM   2399  CG AGLN A 299      -1.950  -0.337  11.631  0.73 21.33           C  
ANISOU 2399  CG AGLN A 299     2836   2953   2315   -487    328    157       C  
ATOM   2400  CD AGLN A 299      -3.257   0.398  11.826  0.73 25.04           C  
ANISOU 2400  CD AGLN A 299     3119   3299   3095   -186     76     -3       C  
ATOM   2401  OE1AGLN A 299      -3.849   0.934  10.883  0.73 27.78           O  
ANISOU 2401  OE1AGLN A 299     3465   3667   3423   -116     79    386       O  
ATOM   2402  NE2AGLN A 299      -3.759   0.426  13.057  0.73 26.20           N  
ANISOU 2402  NE2AGLN A 299     3162   3491   3301   -252    316   -247       N  
ATOM   2403  CB BGLN A 299      -1.108   0.321  10.431  0.27 15.57           C  
ANISOU 2403  CB BGLN A 299     2143   2111   1660   -369     50    214       C  
ATOM   2404  CG BGLN A 299      -1.914  -0.040  11.672  0.27 15.87           C  
ANISOU 2404  CG BGLN A 299     2032   2200   1797   -361    140    120       C  
ATOM   2405  CD BGLN A 299      -2.494  -1.439  11.547  0.27 15.75           C  
ANISOU 2405  CD BGLN A 299     2010   2093   1880   -241     -3    137       C  
ATOM   2406  OE1BGLN A 299      -2.059  -2.327  12.283  0.27 17.87           O  
ANISOU 2406  OE1BGLN A 299     2402   2141   2247   -105     12    255       O  
ATOM   2407  NE2BGLN A 299      -3.433  -1.561  10.624  0.27 14.36           N  
ANISOU 2407  NE2BGLN A 299     1798   1655   2001   -480     41    161       N  
ATOM   2408  N   ASN A 300       0.293  -0.764   7.621  1.00 15.81           N  
ANISOU 2408  N   ASN A 300     2307   2178   1523   -482    108      3       N  
ATOM   2409  CA  ASN A 300       0.841  -0.377   6.329  1.00 15.38           C  
ANISOU 2409  CA  ASN A 300     2028   2166   1650   -259    197     50       C  
ATOM   2410  C   ASN A 300      -0.124   0.541   5.592  1.00 16.07           C  
ANISOU 2410  C   ASN A 300     1960   2239   1908    -88    261     67       C  
ATOM   2411  O   ASN A 300      -1.344   0.432   5.697  1.00 18.80           O  
ANISOU 2411  O   ASN A 300     2059   2670   2414   -183    -12    -30       O  
ATOM   2412  CB  ASN A 300       1.083  -1.610   5.448  1.00 17.21           C  
ANISOU 2412  CB  ASN A 300     2447   2154   1939   -148     93     19       C  
ATOM   2413  CG  ASN A 300       2.361  -2.373   5.744  1.00 19.28           C  
ANISOU 2413  CG  ASN A 300     2714   2000   2611    -61   -107    106       C  
ATOM   2414  OD1 ASN A 300       3.063  -2.197   6.714  1.00 21.71           O  
ANISOU 2414  OD1 ASN A 300     2698   2590   2961   -139   -257    314       O  
ATOM   2415  ND2 ASN A 300       2.797  -3.181   4.772  1.00 23.73           N  
ANISOU 2415  ND2 ASN A 300     3153   2862   3000    223     56   -104       N  
ATOM   2416  N   LEU A 301       0.436   1.465   4.800  1.00 15.94           N  
ANISOU 2416  N   LEU A 301     1968   2453   1637     36    219    172       N  
ATOM   2417  CA  LEU A 301      -0.309   2.342   3.910  1.00 16.63           C  
ANISOU 2417  CA  LEU A 301     1969   2650   1699    188    233     88       C  
ATOM   2418  C   LEU A 301      -0.297   1.705   2.497  1.00 15.96           C  
ANISOU 2418  C   LEU A 301     1987   2345   1731    165    206     99       C  
ATOM   2419  O   LEU A 301       0.558   0.892   2.170  1.00 15.57           O  
ANISOU 2419  O   LEU A 301     2246   1978   1692    144     48    -64       O  
ATOM   2420  CB  LEU A 301       0.214   3.777   3.852  1.00 17.38           C  
ANISOU 2420  CB  LEU A 301     2364   2506   1733    325    229   -100       C  
ATOM   2421  CG  LEU A 301       1.643   4.103   3.433  1.00 15.56           C  
ANISOU 2421  CG  LEU A 301     2333   2050   1528    237     34     26       C  
ATOM   2422  CD1 LEU A 301       1.852   4.008   1.909  1.00 15.73           C  
ANISOU 2422  CD1 LEU A 301     2409   1947   1619    106     31     77       C  
ATOM   2423  CD2 LEU A 301       2.077   5.500   3.903  1.00 17.50           C  
ANISOU 2423  CD2 LEU A 301     2812   2203   1635    312   -289   -183       C  
ATOM   2424  N   SER A 302      -1.243   2.105   1.662  1.00 17.44           N  
ANISOU 2424  N   SER A 302     2003   2974   1648    252    217     42       N  
ATOM   2425  CA  SER A 302      -1.333   1.725   0.253  1.00 17.21           C  
ANISOU 2425  CA  SER A 302     2265   2640   1632   -100     77    196       C  
ATOM   2426  C   SER A 302      -1.120   2.959  -0.608  1.00 15.55           C  
ANISOU 2426  C   SER A 302     1918   2368   1622    -65     82     -7       C  
ATOM   2427  O   SER A 302      -1.729   4.026  -0.352  1.00 17.01           O  
ANISOU 2427  O   SER A 302     1985   2740   1738    105    155    -52       O  
ATOM   2428  CB ASER A 302      -2.725   1.122   0.001  0.78 20.82           C  
ANISOU 2428  CB ASER A 302     2550   3079   2281   -385     39     20       C  
ATOM   2429  OG ASER A 302      -2.928   0.861  -1.381  0.78 21.70           O  
ANISOU 2429  OG ASER A 302     2548   3424   2275   -468    264    -65       O  
ATOM   2430  CB BSER A 302      -2.703   1.108  -0.037  0.22 17.91           C  
ANISOU 2430  CB BSER A 302     2343   2632   1829   -123     28    148       C  
ATOM   2431  OG BSER A 302      -2.754  -0.229   0.420  0.22 18.66           O  
ANISOU 2431  OG BSER A 302     2440   2686   1964    -76     64    265       O  
ATOM   2432  N   MET A 303      -0.263   2.913  -1.627  1.00 14.42           N  
ANISOU 2432  N   MET A 303     1700   2137   1644    -93     49     34       N  
ATOM   2433  CA  MET A 303      -0.018   4.061  -2.509  1.00 13.81           C  
ANISOU 2433  CA  MET A 303     1698   1921   1629     87     88    -97       C  
ATOM   2434  C   MET A 303       0.379   3.605  -3.911  1.00 13.84           C  
ANISOU 2434  C   MET A 303     1584   2005   1667    -14     47   -108       C  
ATOM   2435  O   MET A 303       0.865   2.484  -4.099  1.00 14.90           O  
ANISOU 2435  O   MET A 303     1845   2105   1712     58      4   -175       O  
ATOM   2436  CB  MET A 303       1.021   5.028  -1.949  1.00 14.13           C  
ANISOU 2436  CB  MET A 303     1921   1839   1608     86    103   -127       C  
ATOM   2437  CG  MET A 303       2.419   4.489  -1.717  1.00 14.25           C  
ANISOU 2437  CG  MET A 303     1984   2052   1378    104    -17    -48       C  
ATOM   2438  SD  MET A 303       3.496   4.456  -3.176  1.00 13.31           S  
ANISOU 2438  SD  MET A 303     1667   1856   1535    142     26    -98       S  
ATOM   2439  CE  MET A 303       3.836   6.202  -3.423  1.00 14.99           C  
ANISOU 2439  CE  MET A 303     2188   1888   1618     55     -3    -30       C  
ATOM   2440  N   ASN A 304       0.179   4.490  -4.890  1.00 15.03           N  
ANISOU 2440  N   ASN A 304     1680   2388   1644      8     74     39       N  
ATOM   2441  CA  ASN A 304       0.580   4.212  -6.291  1.00 15.57           C  
ANISOU 2441  CA  ASN A 304     1796   2470   1650    -64    123    -37       C  
ATOM   2442  C   ASN A 304       1.964   4.745  -6.542  1.00 13.10           C  
ANISOU 2442  C   ASN A 304     1744   1860   1373     27    -19   -154       C  
ATOM   2443  O   ASN A 304       2.213   5.954  -6.433  1.00 13.23           O  
ANISOU 2443  O   ASN A 304     1754   1815   1458    166     46    -90       O  
ATOM   2444  CB  ASN A 304      -0.464   4.867  -7.220  1.00 19.66           C  
ANISOU 2444  CB  ASN A 304     2144   3240   2086     48    -73    138       C  
ATOM   2445  CG  ASN A 304      -0.245   4.512  -8.668  1.00 21.94           C  
ANISOU 2445  CG  ASN A 304     2538   3706   2094     -4   -130     93       C  
ATOM   2446  OD1 ASN A 304       0.872   4.366  -9.119  1.00 20.97           O  
ANISOU 2446  OD1 ASN A 304     2489   3631   1847   -278   -174    -64       O  
ATOM   2447  ND2 ASN A 304      -1.283   4.316  -9.501  1.00 26.12           N  
ANISOU 2447  ND2 ASN A 304     2802   4589   2534   -192   -311    101       N  
ATOM   2448  N   PRO A 305       2.951   3.895  -6.881  1.00 13.92           N  
ANISOU 2448  N   PRO A 305     1864   1764   1661     56     55   -144       N  
ATOM   2449  CA  PRO A 305       4.327   4.327  -7.086  1.00 13.42           C  
ANISOU 2449  CA  PRO A 305     1729   1789   1580    134     23     17       C  
ATOM   2450  C   PRO A 305       4.543   5.289  -8.252  1.00 12.16           C  
ANISOU 2450  C   PRO A 305     1462   1628   1529    150    117   -124       C  
ATOM   2451  O   PRO A 305       5.592   5.936  -8.366  1.00 12.39           O  
ANISOU 2451  O   PRO A 305     1617   1592   1497    135    149   -178       O  
ATOM   2452  CB  PRO A 305       5.167   3.042  -7.252  1.00 16.50           C  
ANISOU 2452  CB  PRO A 305     2153   1911   2206    278    174     11       C  
ATOM   2453  CG  PRO A 305       4.145   2.073  -7.714  1.00 17.53           C  
ANISOU 2453  CG  PRO A 305     2541   2002   2119     81    299   -218       C  
ATOM   2454  CD  PRO A 305       2.813   2.442  -7.086  1.00 15.70           C  
ANISOU 2454  CD  PRO A 305     2261   1828   1876    -48    165   -138       C  
ATOM   2455  N   MET A 306       3.535   5.460  -9.141  1.00 13.14           N  
ANISOU 2455  N   MET A 306     1676   1895   1423    106     20   -231       N  
ATOM   2456  CA  MET A 306       3.626   6.469 -10.181  1.00 13.69           C  
ANISOU 2456  CA  MET A 306     1846   1908   1448    154   -192   -173       C  
ATOM   2457  C   MET A 306       3.733   7.875  -9.576  1.00 12.36           C  
ANISOU 2457  C   MET A 306     1540   1827   1331    177    -78    -47       C  
ATOM   2458  O   MET A 306       4.295   8.789 -10.197  1.00 12.99           O  
ANISOU 2458  O   MET A 306     1733   1947   1255    339    -69     58       O  
ATOM   2459  CB AMET A 306       2.367   6.479 -11.079  0.66 18.32           C  
ANISOU 2459  CB AMET A 306     2152   2959   1850    217   -386   -129       C  
ATOM   2460  CG AMET A 306       2.296   5.376 -12.111  0.66 23.92           C  
ANISOU 2460  CG AMET A 306     3291   3385   2414    135   -479   -430       C  
ATOM   2461  SD AMET A 306       3.769   5.294 -13.138  0.66 28.76           S  
ANISOU 2461  SD AMET A 306     3723   4174   3031    587   -131   -474       S  
ATOM   2462  CE AMET A 306       3.999   7.027 -13.572  0.66 22.19           C  
ANISOU 2462  CE AMET A 306     2440   4440   1552    294   -482    102       C  
ATOM   2463  CB BMET A 306       2.450   6.275 -11.144  0.34 13.79           C  
ANISOU 2463  CB BMET A 306     1931   2261   1047    -30      8   -338       C  
ATOM   2464  CG BMET A 306       2.475   4.888 -11.817  0.34 17.09           C  
ANISOU 2464  CG BMET A 306     2766   2194   1533   -139    -64   -280       C  
ATOM   2465  SD BMET A 306       1.184   4.793 -13.082  0.34 19.42           S  
ANISOU 2465  SD BMET A 306     2937   2697   1747   -292   -201    -89       S  
ATOM   2466  CE BMET A 306       1.486   3.181 -13.775  0.34 20.17           C  
ANISOU 2466  CE BMET A 306     3130   2715   1819   -220   -195   -160       C  
ATOM   2467  N   LEU A 307       3.299   8.058  -8.281  1.00 12.09           N  
ANISOU 2467  N   LEU A 307     1631   1705   1257    303    -10    -37       N  
ATOM   2468  CA  LEU A 307       3.491   9.346  -7.622  1.00 11.40           C  
ANISOU 2468  CA  LEU A 307     1520   1619   1192    362    -28    -66       C  
ATOM   2469  C   LEU A 307       4.961   9.685  -7.500  1.00 10.71           C  
ANISOU 2469  C   LEU A 307     1544   1445   1081    225     45     -7       C  
ATOM   2470  O   LEU A 307       5.360  10.862  -7.505  1.00 10.92           O  
ANISOU 2470  O   LEU A 307     1396   1514   1237    219     56     54       O  
ATOM   2471  CB  LEU A 307       2.842   9.353  -6.212  1.00 12.00           C  
ANISOU 2471  CB  LEU A 307     1505   1672   1383    139    123     -6       C  
ATOM   2472  CG  LEU A 307       1.299   9.340  -6.161  1.00 13.32           C  
ANISOU 2472  CG  LEU A 307     1582   1920   1559    395    184      0       C  
ATOM   2473  CD1 LEU A 307       0.862   9.202  -4.702  1.00 14.89           C  
ANISOU 2473  CD1 LEU A 307     1733   2206   1719    159    462     32       C  
ATOM   2474  CD2 LEU A 307       0.721  10.604  -6.772  1.00 14.75           C  
ANISOU 2474  CD2 LEU A 307     1568   1948   2089    330    175    176       C  
ATOM   2475  N   LEU A 308       5.829   8.651  -7.315  1.00 10.37           N  
ANISOU 2475  N   LEU A 308     1416   1445   1077    267     47     67       N  
ATOM   2476  CA  LEU A 308       7.257   8.839  -7.221  1.00  9.64           C  
ANISOU 2476  CA  LEU A 308     1423   1352    890    233     71     56       C  
ATOM   2477  C   LEU A 308       7.959   8.879  -8.591  1.00  9.60           C  
ANISOU 2477  C   LEU A 308     1375   1228   1044    243     51     59       C  
ATOM   2478  O   LEU A 308       8.904   9.646  -8.801  1.00  9.98           O  
ANISOU 2478  O   LEU A 308     1404   1399    990    262    -15     96       O  
ATOM   2479  CB  LEU A 308       7.900   7.755  -6.314  1.00 10.26           C  
ANISOU 2479  CB  LEU A 308     1436   1408   1055    282     86     78       C  
ATOM   2480  CG  LEU A 308       7.379   7.741  -4.881  1.00 11.65           C  
ANISOU 2480  CG  LEU A 308     1723   1756    947    322      1    133       C  
ATOM   2481  CD1 LEU A 308       7.937   6.554  -4.132  1.00 14.83           C  
ANISOU 2481  CD1 LEU A 308     2169   1977   1490    594    158    273       C  
ATOM   2482  CD2 LEU A 308       7.723   9.019  -4.132  1.00 15.38           C  
ANISOU 2482  CD2 LEU A 308     2858   1915   1072      7    107     70       C  
ATOM   2483  N   LEU A 309       7.533   8.015  -9.527  1.00 10.03           N  
ANISOU 2483  N   LEU A 309     1350   1447   1013    169     68    -15       N  
ATOM   2484  CA  LEU A 309       8.184   7.912 -10.839  1.00 10.46           C  
ANISOU 2484  CA  LEU A 309     1461   1507   1006    234     83     -6       C  
ATOM   2485  C   LEU A 309       8.270   9.230 -11.570  1.00 10.13           C  
ANISOU 2485  C   LEU A 309     1320   1587    944    372     -6    -23       C  
ATOM   2486  O   LEU A 309       9.229   9.511 -12.313  1.00 11.48           O  
ANISOU 2486  O   LEU A 309     1647   1681   1033    367    119     62       O  
ATOM   2487  CB ALEU A 309       7.486   6.832 -11.698  0.63 11.99           C  
ANISOU 2487  CB ALEU A 309     1490   1757   1307    192     15   -121       C  
ATOM   2488  CG ALEU A 309       8.010   5.424 -11.422  0.63 13.90           C  
ANISOU 2488  CG ALEU A 309     1701   1808   1771    177     82    -76       C  
ATOM   2489  CD1ALEU A 309       6.999   4.348 -11.800  0.63 16.05           C  
ANISOU 2489  CD1ALEU A 309     1732   2227   2140    -36     88   -150       C  
ATOM   2490  CD2ALEU A 309       9.293   5.122 -12.185  0.63 13.35           C  
ANISOU 2490  CD2ALEU A 309     1713   1713   1646    242     50   -116       C  
ATOM   2491  CB BLEU A 309       7.522   6.837 -11.724  0.37 10.63           C  
ANISOU 2491  CB BLEU A 309     1419   1541   1077    281    -25      8       C  
ATOM   2492  CG BLEU A 309       8.388   6.334 -12.883  0.37 11.16           C  
ANISOU 2492  CG BLEU A 309     1569   1758    915    210    -27     55       C  
ATOM   2493  CD1BLEU A 309       9.572   5.524 -12.361  0.37 10.86           C  
ANISOU 2493  CD1BLEU A 309     1465   1421   1242    240    202     87       C  
ATOM   2494  CD2BLEU A 309       7.571   5.541 -13.897  0.37 12.45           C  
ANISOU 2494  CD2BLEU A 309     1803   1699   1228    154    -48    -89       C  
ATOM   2495  N   SER A 310       7.262  10.118 -11.438  1.00 10.39           N  
ANISOU 2495  N   SER A 310     1453   1454   1040    372    -52    101       N  
ATOM   2496  CA  SER A 310       7.287  11.425 -12.095  1.00 10.65           C  
ANISOU 2496  CA  SER A 310     1448   1558   1040    361    -23    204       C  
ATOM   2497  C   SER A 310       8.390  12.353 -11.620  1.00 10.67           C  
ANISOU 2497  C   SER A 310     1560   1510    983    296     87    125       C  
ATOM   2498  O   SER A 310       8.753  13.306 -12.312  1.00 11.07           O  
ANISOU 2498  O   SER A 310     1551   1586   1069    274      5    201       O  
ATOM   2499  CB  SER A 310       5.920  12.110 -11.977  1.00 11.73           C  
ANISOU 2499  CB  SER A 310     1518   1702   1239    406   -136     73       C  
ATOM   2500  OG  SER A 310       5.459  12.146 -10.626  1.00 12.95           O  
ANISOU 2500  OG  SER A 310     1573   1947   1399    642     18    167       O  
ATOM   2501  N   GLY A 311       8.886  12.111 -10.365  1.00 10.23           N  
ANISOU 2501  N   GLY A 311     1512   1475    900    294     91    133       N  
ATOM   2502  CA  GLY A 311       9.966  12.941  -9.848  1.00 10.29           C  
ANISOU 2502  CA  GLY A 311     1383   1530    996    326     43    182       C  
ATOM   2503  C   GLY A 311       9.844  13.322  -8.364  1.00  9.53           C  
ANISOU 2503  C   GLY A 311     1308   1231   1083    183    -13    216       C  
ATOM   2504  O   GLY A 311      10.816  13.879  -7.839  1.00 11.89           O  
ANISOU 2504  O   GLY A 311     1566   1773   1177    -16    135      8       O  
ATOM   2505  N   ARG A 312       8.756  13.041  -7.680  1.00  9.87           N  
ANISOU 2505  N   ARG A 312     1432   1386    933    324     74    120       N  
ATOM   2506  CA  ARG A 312       8.629  13.393  -6.259  1.00  9.43           C  
ANISOU 2506  CA  ARG A 312     1471   1162    950    393    167    153       C  
ATOM   2507  C   ARG A 312       9.693  12.679  -5.409  1.00 10.03           C  
ANISOU 2507  C   ARG A 312     1520   1324    968    425    145     77       C  
ATOM   2508  O   ARG A 312      10.132  11.567  -5.694  1.00 11.11           O  
ANISOU 2508  O   ARG A 312     1846   1398    978    486   -114     64       O  
ATOM   2509  CB  ARG A 312       7.247  13.011  -5.721  1.00  9.91           C  
ANISOU 2509  CB  ARG A 312     1444   1371    948    346     33    100       C  
ATOM   2510  CG  ARG A 312       6.065  13.833  -6.284  1.00 10.21           C  
ANISOU 2510  CG  ARG A 312     1494   1401    985    386     30    203       C  
ATOM   2511  CD  ARG A 312       4.774  13.433  -5.588  1.00 10.22           C  
ANISOU 2511  CD  ARG A 312     1381   1384   1118    361      2     18       C  
ATOM   2512  NE  ARG A 312       3.573  14.161  -6.058  1.00 11.07           N  
ANISOU 2512  NE  ARG A 312     1584   1524   1097    504     -9     50       N  
ATOM   2513  CZ  ARG A 312       2.845  13.817  -7.131  1.00 10.70           C  
ANISOU 2513  CZ  ARG A 312     1506   1395   1164    349     14     98       C  
ATOM   2514  NH1 ARG A 312       3.211  12.832  -7.949  1.00 11.14           N  
ANISOU 2514  NH1 ARG A 312     1479   1546   1209    393    -23     23       N  
ATOM   2515  NH2 ARG A 312       1.755  14.524  -7.456  1.00 11.56           N  
ANISOU 2515  NH2 ARG A 312     1539   1720   1133    454    -49     42       N  
ATOM   2516  N   THR A 313      10.012  13.337  -4.284  1.00  9.93           N  
ANISOU 2516  N   THR A 313     1583   1286    905    435    -21    177       N  
ATOM   2517  CA  THR A 313      10.865  12.808  -3.213  1.00 10.19           C  
ANISOU 2517  CA  THR A 313     1645   1259    967    452    -39    223       C  
ATOM   2518  C   THR A 313      10.032  12.667  -1.949  1.00 10.18           C  
ANISOU 2518  C   THR A 313     1600   1262   1005    532    -16    147       C  
ATOM   2519  O   THR A 313       9.353  13.635  -1.533  1.00 12.09           O  
ANISOU 2519  O   THR A 313     2214   1424    955    718    143    193       O  
ATOM   2520  CB  THR A 313      12.031  13.776  -2.972  1.00 10.49           C  
ANISOU 2520  CB  THR A 313     1569   1345   1072    414    -88    156       C  
ATOM   2521  OG1 THR A 313      12.805  13.936  -4.175  1.00 12.00           O  
ANISOU 2521  OG1 THR A 313     1466   1763   1332    308     37     46       O  
ATOM   2522  CG2 THR A 313      12.953  13.294  -1.863  1.00 13.88           C  
ANISOU 2522  CG2 THR A 313     1942   1962   1370    500   -436    193       C  
ATOM   2523  N   TRP A 314      10.113  11.498  -1.313  1.00  9.96           N  
ANISOU 2523  N   TRP A 314     1608   1269    908    453     64    151       N  
ATOM   2524  CA  TRP A 314       9.375  11.205  -0.076  1.00 10.30           C  
ANISOU 2524  CA  TRP A 314     1557   1418    937    491     65    177       C  
ATOM   2525  C   TRP A 314      10.413  10.817   0.982  1.00 10.71           C  
ANISOU 2525  C   TRP A 314     1580   1476   1012    676     19     74       C  
ATOM   2526  O   TRP A 314      11.232   9.918   0.767  1.00 13.11           O  
ANISOU 2526  O   TRP A 314     2080   1807   1095   1023    -33     77       O  
ATOM   2527  CB  TRP A 314       8.416  10.053  -0.307  1.00 11.23           C  
ANISOU 2527  CB  TRP A 314     1659   1392   1216    528     43     92       C  
ATOM   2528  CG  TRP A 314       7.236   9.969   0.612  1.00  9.64           C  
ANISOU 2528  CG  TRP A 314     1466   1197   1000    404   -142    132       C  
ATOM   2529  CD1 TRP A 314       6.744  10.910   1.510  1.00  9.76           C  
ANISOU 2529  CD1 TRP A 314     1391   1182   1136    295    -44    117       C  
ATOM   2530  CD2 TRP A 314       6.261   8.911   0.613  1.00  9.97           C  
ANISOU 2530  CD2 TRP A 314     1506   1283    997    286   -148     96       C  
ATOM   2531  NE1 TRP A 314       5.559  10.492   2.061  1.00 10.05           N  
ANISOU 2531  NE1 TRP A 314     1426   1278   1113    219    -55     31       N  
ATOM   2532  CE2 TRP A 314       5.237   9.264   1.517  1.00 10.59           C  
ANISOU 2532  CE2 TRP A 314     1597   1269   1158    211    -70     71       C  
ATOM   2533  CE3 TRP A 314       6.181   7.679  -0.072  1.00 11.07           C  
ANISOU 2533  CE3 TRP A 314     1674   1387   1143    363   -199     17       C  
ATOM   2534  CZ2 TRP A 314       4.142   8.453   1.755  1.00 12.04           C  
ANISOU 2534  CZ2 TRP A 314     1779   1536   1260     77    -37     34       C  
ATOM   2535  CZ3 TRP A 314       5.107   6.873   0.181  1.00 12.47           C  
ANISOU 2535  CZ3 TRP A 314     1928   1469   1342    252   -177    -59       C  
ATOM   2536  CH2 TRP A 314       4.075   7.240   1.069  1.00 13.01           C  
ANISOU 2536  CH2 TRP A 314     1933   1559   1451    106   -101     26       C  
ATOM   2537  N   LYS A 315      10.393  11.455   2.142  1.00  9.75           N  
ANISOU 2537  N   LYS A 315     1352   1457    896    556    -79    184       N  
ATOM   2538  CA  LYS A 315      11.349  11.135   3.209  1.00 10.33           C  
ANISOU 2538  CA  LYS A 315     1258   1660   1008    299    -85    199       C  
ATOM   2539  C   LYS A 315      10.654  11.231   4.568  1.00  8.54           C  
ANISOU 2539  C   LYS A 315     1197   1078    971    258    -93    192       C  
ATOM   2540  O   LYS A 315       9.567  11.811   4.645  1.00  9.55           O  
ANISOU 2540  O   LYS A 315     1292   1293   1045    458     24    271       O  
ATOM   2541  CB ALYS A 315      12.680  11.761   2.995  0.59 10.15           C  
ANISOU 2541  CB ALYS A 315     1308   1373   1174    270     39    -37       C  
ATOM   2542  CG ALYS A 315      12.463  13.253   3.264  0.59 10.13           C  
ANISOU 2542  CG ALYS A 315     1463   1234   1152    -37    -45   -195       C  
ATOM   2543  CD ALYS A 315      13.489  14.178   2.606  0.59 14.36           C  
ANISOU 2543  CD ALYS A 315     1783   2013   1660    -76     90    120       C  
ATOM   2544  CE ALYS A 315      14.899  13.919   3.085  0.59 15.09           C  
ANISOU 2544  CE ALYS A 315     1884   2123   1726    180    108    -35       C  
ATOM   2545  NZ ALYS A 315      15.869  14.932   2.570  0.59 17.99           N  
ANISOU 2545  NZ ALYS A 315     1953   2326   2556    -20     65     13       N  
ATOM   2546  CB BLYS A 315      12.247  12.426   3.290  0.41 11.76           C  
ANISOU 2546  CB BLYS A 315     1437   1823   1208    184    -50    213       C  
ATOM   2547  CG BLYS A 315      13.207  12.842   2.203  0.41 13.21           C  
ANISOU 2547  CG BLYS A 315     1526   2029   1464   -109    -50    290       C  
ATOM   2548  CD BLYS A 315      13.998  14.110   2.493  0.41 15.56           C  
ANISOU 2548  CD BLYS A 315     1872   2244   1797   -181    -50    -26       C  
ATOM   2549  CE BLYS A 315      15.013  14.453   1.412  0.41 17.97           C  
ANISOU 2549  CE BLYS A 315     2314   2543   1970    -44    129    252       C  
ATOM   2550  NZ BLYS A 315      15.501  15.840   1.662  0.41 19.65           N  
ANISOU 2550  NZ BLYS A 315     2783   2516   2165     -8     23     99       N  
ATOM   2551  N   GLY A 316      11.276  10.685   5.594  1.00  8.99           N  
ANISOU 2551  N   GLY A 316     1353   1193    871    317    -83    144       N  
ATOM   2552  CA  GLY A 316      10.833  10.933   6.968  1.00  8.36           C  
ANISOU 2552  CA  GLY A 316     1209   1170    798    200     18     73       C  
ATOM   2553  C   GLY A 316      12.047  11.235   7.829  1.00  7.73           C  
ANISOU 2553  C   GLY A 316     1036    913    988    255     19    191       C  
ATOM   2554  O   GLY A 316      13.190  11.125   7.377  1.00  8.42           O  
ANISOU 2554  O   GLY A 316     1162   1084    953     72    103    194       O  
ATOM   2555  N   ALA A 317      11.815  11.593   9.101  1.00  8.09           N  
ANISOU 2555  N   ALA A 317     1135   1030    910    150     55     91       N  
ATOM   2556  CA  ALA A 317      12.943  11.788  10.013  1.00  8.07           C  
ANISOU 2556  CA  ALA A 317     1150   1016    901    -65     96    155       C  
ATOM   2557  C   ALA A 317      12.444  11.779  11.465  1.00  7.65           C  
ANISOU 2557  C   ALA A 317     1061    832   1015     -6     20    205       C  
ATOM   2558  O   ALA A 317      11.276  12.078  11.746  1.00  8.19           O  
ANISOU 2558  O   ALA A 317     1098   1059    956      1     -5    124       O  
ATOM   2559  CB  ALA A 317      13.615  13.149   9.771  1.00 10.64           C  
ANISOU 2559  CB  ALA A 317     1591   1148   1304   -148    220     88       C  
ATOM   2560  N   ILE A 318      13.384  11.449  12.342  1.00  7.85           N  
ANISOU 2560  N   ILE A 318     1129    951    903     21     47    233       N  
ATOM   2561  CA  ILE A 318      13.229  11.545  13.790  1.00  7.62           C  
ANISOU 2561  CA  ILE A 318     1133    906    858    -73     15    120       C  
ATOM   2562  C   ILE A 318      13.958  12.782  14.282  1.00  7.30           C  
ANISOU 2562  C   ILE A 318     1088    753    935    -94     97    291       C  
ATOM   2563  O   ILE A 318      15.090  13.094  13.836  1.00  8.04           O  
ANISOU 2563  O   ILE A 318     1076    954   1027     10    103    163       O  
ATOM   2564  CB  ILE A 318      13.814  10.278  14.495  1.00  9.43           C  
ANISOU 2564  CB  ILE A 318     1674    895   1014     31    -47    283       C  
ATOM   2565  CG1 ILE A 318      13.188   9.004  13.987  1.00 12.04           C  
ANISOU 2565  CG1 ILE A 318     2110   1196   1268   -136   -276    310       C  
ATOM   2566  CG2 ILE A 318      13.708  10.397  16.001  1.00 10.31           C  
ANISOU 2566  CG2 ILE A 318     1720   1131   1067     34   -213    134       C  
ATOM   2567  CD1 ILE A 318      11.737   8.912  14.230  1.00 15.28           C  
ANISOU 2567  CD1 ILE A 318     2073   1870   1862   -274   -249    194       C  
ATOM   2568  N   PHE A 319      13.338  13.536  15.187  1.00  6.99           N  
ANISOU 2568  N   PHE A 319      956    815    885      8     -7    224       N  
ATOM   2569  CA  PHE A 319      13.976  14.666  15.876  1.00  7.37           C  
ANISOU 2569  CA  PHE A 319      980    835    987     27    104    122       C  
ATOM   2570  C   PHE A 319      14.545  15.692  14.888  1.00  7.52           C  
ANISOU 2570  C   PHE A 319     1042    815   1001     -5      6     91       C  
ATOM   2571  O   PHE A 319      15.615  16.292  15.090  1.00  8.43           O  
ANISOU 2571  O   PHE A 319     1095   1069   1041    -75    -20    287       O  
ATOM   2572  CB  PHE A 319      15.035  14.186  16.897  1.00  8.08           C  
ANISOU 2572  CB  PHE A 319     1069    910   1092    -95      7    147       C  
ATOM   2573  CG  PHE A 319      15.481  15.244  17.892  1.00  7.06           C  
ANISOU 2573  CG  PHE A 319      911    824    945    -85     83    208       C  
ATOM   2574  CD1 PHE A 319      14.548  15.809  18.769  1.00  7.68           C  
ANISOU 2574  CD1 PHE A 319     1039    832   1047    -74    106    196       C  
ATOM   2575  CD2 PHE A 319      16.820  15.620  18.021  1.00  8.01           C  
ANISOU 2575  CD2 PHE A 319     1069    934   1040    -62      6    158       C  
ATOM   2576  CE1 PHE A 319      14.944  16.754  19.697  1.00  8.21           C  
ANISOU 2576  CE1 PHE A 319     1120   1050    948     12     83    110       C  
ATOM   2577  CE2 PHE A 319      17.205  16.543  18.984  1.00  9.13           C  
ANISOU 2577  CE2 PHE A 319     1091   1159   1219   -157     71    167       C  
ATOM   2578  CZ  PHE A 319      16.276  17.108  19.822  1.00  8.51           C  
ANISOU 2578  CZ  PHE A 319     1189   1010   1037    -48     69     93       C  
ATOM   2579  N   GLY A 320      13.783  15.939  13.784  1.00  7.89           N  
ANISOU 2579  N   GLY A 320     1130    936    931     19     27    211       N  
ATOM   2580  CA  GLY A 320      14.180  16.989  12.835  1.00  8.71           C  
ANISOU 2580  CA  GLY A 320     1231   1041   1039     20     53    256       C  
ATOM   2581  C   GLY A 320      15.480  16.746  12.095  1.00  7.97           C  
ANISOU 2581  C   GLY A 320     1202    976    852    -18     65    268       C  
ATOM   2582  O   GLY A 320      16.019  17.693  11.499  1.00  9.21           O  
ANISOU 2582  O   GLY A 320     1266   1115   1117    -26     73    320       O  
ATOM   2583  N   GLY A 321      15.990  15.513  12.115  1.00  8.10           N  
ANISOU 2583  N   GLY A 321     1064   1057    956      0     74    229       N  
ATOM   2584  CA  GLY A 321      17.295  15.202  11.524  1.00  8.54           C  
ANISOU 2584  CA  GLY A 321     1213   1104    929     57    156    183       C  
ATOM   2585  C   GLY A 321      18.500  15.668  12.327  1.00  8.53           C  
ANISOU 2585  C   GLY A 321     1055   1111   1074     -6    141    274       C  
ATOM   2586  O   GLY A 321      19.631  15.427  11.873  1.00 10.58           O  
ANISOU 2586  O   GLY A 321     1235   1565   1220    -67    205     44       O  
ATOM   2587  N   PHE A 322      18.309  16.270  13.489  1.00  8.54           N  
ANISOU 2587  N   PHE A 322     1087   1060   1098     -2     83    177       N  
ATOM   2588  CA  PHE A 322      19.449  16.777  14.260  1.00  8.55           C  
ANISOU 2588  CA  PHE A 322     1135   1079   1036   -157     86    233       C  
ATOM   2589  C   PHE A 322      20.241  15.691  14.964  1.00  8.63           C  
ANISOU 2589  C   PHE A 322     1090   1097   1094   -181     29    193       C  
ATOM   2590  O   PHE A 322      19.644  14.853  15.681  1.00  8.68           O  
ANISOU 2590  O   PHE A 322     1009   1104   1186   -178     31    264       O  
ATOM   2591  CB  PHE A 322      18.935  17.774  15.314  1.00  9.11           C  
ANISOU 2591  CB  PHE A 322     1157   1067   1238   -132    -26    157       C  
ATOM   2592  CG  PHE A 322      18.465  19.114  14.822  1.00  9.05           C  
ANISOU 2592  CG  PHE A 322     1135   1048   1255   -131     25    115       C  
ATOM   2593  CD1 PHE A 322      19.383  19.957  14.182  1.00 12.95           C  
ANISOU 2593  CD1 PHE A 322     1408   1236   2276   -184    232    365       C  
ATOM   2594  CD2 PHE A 322      17.156  19.549  14.998  1.00  9.41           C  
ANISOU 2594  CD2 PHE A 322     1175   1156   1246    -77    -65    129       C  
ATOM   2595  CE1 PHE A 322      18.996  21.219  13.745  1.00 13.89           C  
ANISOU 2595  CE1 PHE A 322     1549   1411   2319   -126    257    507       C  
ATOM   2596  CE2 PHE A 322      16.775  20.820  14.554  1.00  9.71           C  
ANISOU 2596  CE2 PHE A 322     1198   1223   1267   -120   -118    145       C  
ATOM   2597  CZ  PHE A 322      17.695  21.639  13.924  1.00 11.84           C  
ANISOU 2597  CZ  PHE A 322     1558   1166   1775   -124    104    299       C  
ATOM   2598  N   LYS A 323      21.569  15.700  14.843  1.00  8.66           N  
ANISOU 2598  N   LYS A 323     1068   1157   1066    -53     58    208       N  
ATOM   2599  CA  LYS A 323      22.459  14.910  15.695  1.00  8.86           C  
ANISOU 2599  CA  LYS A 323     1023   1105   1238   -167     36    198       C  
ATOM   2600  C   LYS A 323      22.252  15.463  17.119  1.00  8.71           C  
ANISOU 2600  C   LYS A 323     1133    993   1184    -20     -6    233       C  
ATOM   2601  O   LYS A 323      22.517  16.660  17.363  1.00  9.86           O  
ANISOU 2601  O   LYS A 323     1461   1067   1218   -160      8    199       O  
ATOM   2602  CB  LYS A 323      23.918  14.992  15.234  1.00  9.87           C  
ANISOU 2602  CB  LYS A 323     1014   1359   1376    -59     78    153       C  
ATOM   2603  CG  LYS A 323      24.152  14.308  13.893  1.00 10.86           C  
ANISOU 2603  CG  LYS A 323     1290   1426   1409     12    224    107       C  
ATOM   2604  CD  LYS A 323      25.596  14.387  13.443  1.00 12.66           C  
ANISOU 2604  CD  LYS A 323     1355   1736   1720    -36    185     53       C  
ATOM   2605  CE  LYS A 323      25.892  13.706  12.111  1.00 13.89           C  
ANISOU 2605  CE  LYS A 323     1737   1830   1712    -13    512    145       C  
ATOM   2606  NZ  LYS A 323      25.894  12.233  12.198  1.00 13.42           N  
ANISOU 2606  NZ  LYS A 323     1630   1799   1669    105    336     68       N  
ATOM   2607  N   SER A 324      21.705  14.680  18.031  1.00  8.59           N  
ANISOU 2607  N   SER A 324     1060   1010   1194   -113     71    217       N  
ATOM   2608  CA  SER A 324      21.084  15.221  19.216  1.00  9.22           C  
ANISOU 2608  CA  SER A 324     1246   1121   1137   -125     20    122       C  
ATOM   2609  C   SER A 324      22.003  15.949  20.190  1.00  8.51           C  
ANISOU 2609  C   SER A 324     1110   1080   1045    -82    153     79       C  
ATOM   2610  O   SER A 324      21.666  17.057  20.655  1.00  9.41           O  
ANISOU 2610  O   SER A 324     1254   1102   1220   -111     13     98       O  
ATOM   2611  CB  SER A 324      20.252  14.140  19.908  1.00  9.23           C  
ANISOU 2611  CB  SER A 324     1181   1088   1237   -125     96    140       C  
ATOM   2612  OG  SER A 324      21.161  13.097  20.276  1.00  9.62           O  
ANISOU 2612  OG  SER A 324     1263   1158   1233    -64     99    232       O  
ATOM   2613  N   LYS A 325      23.121  15.327  20.553  1.00  8.97           N  
ANISOU 2613  N   LYS A 325     1011   1176   1220   -180    -26     96       N  
ATOM   2614  CA  LYS A 325      23.980  15.876  21.599  1.00  9.08           C  
ANISOU 2614  CA  LYS A 325     1142   1146   1163   -131   -112     12       C  
ATOM   2615  C   LYS A 325      24.783  17.069  21.064  1.00  9.81           C  
ANISOU 2615  C   LYS A 325     1174   1241   1311   -170   -105     38       C  
ATOM   2616  O   LYS A 325      25.001  18.030  21.805  1.00 11.20           O  
ANISOU 2616  O   LYS A 325     1365   1347   1542   -308   -177     30       O  
ATOM   2617  CB  LYS A 325      24.867  14.773  22.202  1.00 10.14           C  
ANISOU 2617  CB  LYS A 325     1186   1315   1353   -133   -140    217       C  
ATOM   2618  CG  LYS A 325      25.642  15.205  23.456  1.00 10.42           C  
ANISOU 2618  CG  LYS A 325     1323   1403   1234    -90     -9    203       C  
ATOM   2619  CD  LYS A 325      26.043  14.029  24.337  1.00 10.46           C  
ANISOU 2619  CD  LYS A 325     1222   1392   1359   -116   -116    136       C  
ATOM   2620  CE  LYS A 325      26.835  14.485  25.570  1.00 11.97           C  
ANISOU 2620  CE  LYS A 325     1255   1744   1551   -202   -205    162       C  
ATOM   2621  NZ  LYS A 325      26.832  13.419  26.624  1.00 12.51           N  
ANISOU 2621  NZ  LYS A 325     1507   1711   1534    -86   -184    260       N  
ATOM   2622  N   ASP A 326      25.168  17.061  19.780  1.00 10.62           N  
ANISOU 2622  N   ASP A 326     1215   1371   1450   -246     84    171       N  
ATOM   2623  CA  ASP A 326      25.823  18.234  19.189  1.00 11.22           C  
ANISOU 2623  CA  ASP A 326     1098   1426   1740   -256     -9    259       C  
ATOM   2624  C   ASP A 326      24.812  19.365  19.073  1.00 10.78           C  
ANISOU 2624  C   ASP A 326     1192   1247   1658   -282     58    218       C  
ATOM   2625  O   ASP A 326      25.150  20.553  19.276  1.00 13.63           O  
ANISOU 2625  O   ASP A 326     1662   1355   2162   -395    -81     75       O  
ATOM   2626  CB  ASP A 326      26.310  17.906  17.777  1.00 14.24           C  
ANISOU 2626  CB  ASP A 326     1643   1785   1981   -316    320    263       C  
ATOM   2627  CG  ASP A 326      27.494  16.961  17.667  1.00 16.46           C  
ANISOU 2627  CG  ASP A 326     1751   1945   2559   -378    429    273       C  
ATOM   2628  OD1 ASP A 326      28.253  16.856  18.635  1.00 20.15           O  
ANISOU 2628  OD1 ASP A 326     1877   2855   2924    217    380    477       O  
ATOM   2629  OD2 ASP A 326      27.664  16.351  16.586  1.00 20.11           O  
ANISOU 2629  OD2 ASP A 326     2345   2298   3000   -406    949     44       O  
ATOM   2630  N   SER A 327      23.557  19.102  18.711  1.00  9.80           N  
ANISOU 2630  N   SER A 327     1079   1202   1443   -243     27    144       N  
ATOM   2631  CA  SER A 327      22.616  20.141  18.324  1.00  9.67           C  
ANISOU 2631  CA  SER A 327     1272   1040   1361   -225     74    154       C  
ATOM   2632  C   SER A 327      21.861  20.803  19.461  1.00  9.30           C  
ANISOU 2632  C   SER A 327     1270    993   1271   -186     14    110       C  
ATOM   2633  O   SER A 327      21.617  22.018  19.419  1.00 10.35           O  
ANISOU 2633  O   SER A 327     1532    974   1426   -260    126    113       O  
ATOM   2634  CB  SER A 327      21.590  19.617  17.318  1.00 10.48           C  
ANISOU 2634  CB  SER A 327     1359   1185   1439   -107     43     34       C  
ATOM   2635  OG  SER A 327      22.197  19.074  16.166  1.00 10.92           O  
ANISOU 2635  OG  SER A 327     1423   1450   1277   -170    120     74       O  
ATOM   2636  N   VAL A 328      21.466  20.024  20.484  1.00  9.21           N  
ANISOU 2636  N   VAL A 328     1263    968   1268   -156     54    132       N  
ATOM   2637  CA  VAL A 328      20.653  20.591  21.559  1.00  9.37           C  
ANISOU 2637  CA  VAL A 328     1439    926   1196   -156     10     90       C  
ATOM   2638  C   VAL A 328      21.296  21.792  22.252  1.00  9.67           C  
ANISOU 2638  C   VAL A 328     1304   1105   1265    -81      9     33       C  
ATOM   2639  O   VAL A 328      20.625  22.828  22.439  1.00  9.96           O  
ANISOU 2639  O   VAL A 328     1367   1001   1418   -232     88    113       O  
ATOM   2640  CB  VAL A 328      20.146  19.480  22.508  1.00  8.92           C  
ANISOU 2640  CB  VAL A 328     1250    926   1215   -119    -38    149       C  
ATOM   2641  CG1 VAL A 328      19.678  20.033  23.848  1.00 10.62           C  
ANISOU 2641  CG1 VAL A 328     1543   1116   1377   -196    106    130       C  
ATOM   2642  CG2 VAL A 328      18.982  18.737  21.837  1.00 10.25           C  
ANISOU 2642  CG2 VAL A 328     1300   1115   1479   -119    -36    115       C  
ATOM   2643  N   PRO A 329      22.591  21.762  22.609  1.00  9.76           N  
ANISOU 2643  N   PRO A 329     1389    995   1326   -233    -98     78       N  
ATOM   2644  CA  PRO A 329      23.200  22.922  23.267  1.00 10.83           C  
ANISOU 2644  CA  PRO A 329     1537   1157   1422   -240    -86     22       C  
ATOM   2645  C   PRO A 329      23.232  24.156  22.374  1.00 10.03           C  
ANISOU 2645  C   PRO A 329     1197   1133   1480   -225    -52     -4       C  
ATOM   2646  O   PRO A 329      23.050  25.286  22.847  1.00 10.95           O  
ANISOU 2646  O   PRO A 329     1507   1137   1517   -290    -19     22       O  
ATOM   2647  CB  PRO A 329      24.613  22.475  23.685  1.00 11.86           C  
ANISOU 2647  CB  PRO A 329     1603   1297   1607   -119   -156    176       C  
ATOM   2648  CG  PRO A 329      24.436  20.960  23.803  1.00 11.56           C  
ANISOU 2648  CG  PRO A 329     1443   1337   1612    -73   -137    -33       C  
ATOM   2649  CD  PRO A 329      23.506  20.598  22.638  1.00 10.84           C  
ANISOU 2649  CD  PRO A 329     1318   1254   1549   -163   -133     81       C  
ATOM   2650  N   LYS A 330      23.438  23.959  21.069  1.00 10.48           N  
ANISOU 2650  N   LYS A 330     1363   1078   1539   -363    126    156       N  
ATOM   2651  CA  LYS A 330      23.466  25.055  20.090  1.00 11.37           C  
ANISOU 2651  CA  LYS A 330     1502   1243   1576   -257     70    222       C  
ATOM   2652  C   LYS A 330      22.061  25.648  19.918  1.00 10.47           C  
ANISOU 2652  C   LYS A 330     1436   1104   1438   -292     76     58       C  
ATOM   2653  O   LYS A 330      21.898  26.877  19.824  1.00 11.77           O  
ANISOU 2653  O   LYS A 330     1647   1108   1719   -438    137    148       O  
ATOM   2654  CB ALYS A 330      24.064  24.575  18.770  0.61 14.35           C  
ANISOU 2654  CB ALYS A 330     1827   1875   1750   -283    267     73       C  
ATOM   2655  CG ALYS A 330      23.995  25.581  17.643  0.61 17.27           C  
ANISOU 2655  CG ALYS A 330     2442   2338   1782    -63    289    150       C  
ATOM   2656  CD ALYS A 330      24.741  26.881  17.928  0.61 20.70           C  
ANISOU 2656  CD ALYS A 330     2755   2664   2446   -277    229     86       C  
ATOM   2657  CE ALYS A 330      24.910  27.638  16.603  0.61 23.02           C  
ANISOU 2657  CE ALYS A 330     3206   2937   2604   -397    384    227       C  
ATOM   2658  NZ ALYS A 330      24.741  29.103  16.758  0.61 23.57           N  
ANISOU 2658  NZ ALYS A 330     3389   3025   2542   -160    409    234       N  
ATOM   2659  CB BLYS A 330      23.974  24.521  18.743  0.39 11.89           C  
ANISOU 2659  CB BLYS A 330     1620   1379   1521   -183    198    351       C  
ATOM   2660  CG BLYS A 330      25.436  24.149  18.711  0.39 13.47           C  
ANISOU 2660  CG BLYS A 330     1748   1499   1873     45    147    285       C  
ATOM   2661  CD BLYS A 330      25.866  23.426  17.442  0.39 17.96           C  
ANISOU 2661  CD BLYS A 330     2392   2274   2159    183    409     61       C  
ATOM   2662  CE BLYS A 330      27.356  23.123  17.527  0.39 20.68           C  
ANISOU 2662  CE BLYS A 330     2504   2830   2525    322    264     98       C  
ATOM   2663  NZ BLYS A 330      28.160  24.374  17.550  0.39 23.27           N  
ANISOU 2663  NZ BLYS A 330     2964   3019   2859    125    320     12       N  
ATOM   2664  N   LEU A 331      21.009  24.816  19.886  1.00 10.05           N  
ANISOU 2664  N   LEU A 331     1334   1090   1395   -266    102    158       N  
ATOM   2665  CA  LEU A 331      19.648  25.296  19.817  1.00  9.52           C  
ANISOU 2665  CA  LEU A 331     1321    964   1330   -360     65    281       C  
ATOM   2666  C   LEU A 331      19.298  26.119  21.070  1.00  9.31           C  
ANISOU 2666  C   LEU A 331     1206    901   1431   -258     -5    259       C  
ATOM   2667  O   LEU A 331      18.658  27.178  20.964  1.00  9.81           O  
ANISOU 2667  O   LEU A 331     1422    890   1415   -199    -23    157       O  
ATOM   2668  CB  LEU A 331      18.655  24.124  19.636  1.00  9.70           C  
ANISOU 2668  CB  LEU A 331     1382    999   1307   -351     78    200       C  
ATOM   2669  CG  LEU A 331      18.711  23.490  18.229  1.00 11.01           C  
ANISOU 2669  CG  LEU A 331     1606   1225   1352   -261      4     56       C  
ATOM   2670  CD1 LEU A 331      18.090  22.088  18.247  1.00 12.56           C  
ANISOU 2670  CD1 LEU A 331     1756   1410   1607   -588     26    -80       C  
ATOM   2671  CD2 LEU A 331      18.007  24.366  17.202  1.00 15.03           C  
ANISOU 2671  CD2 LEU A 331     2387   1677   1647    191   -320    -38       C  
ATOM   2672  N   VAL A 332      19.728  25.657  22.265  1.00 10.10           N  
ANISOU 2672  N   VAL A 332     1457    975   1404   -394    -64    152       N  
ATOM   2673  CA  VAL A 332      19.500  26.465  23.464  1.00 10.03           C  
ANISOU 2673  CA  VAL A 332     1503    878   1428   -255    -85    139       C  
ATOM   2674  C   VAL A 332      20.250  27.819  23.357  1.00 10.63           C  
ANISOU 2674  C   VAL A 332     1610    953   1477   -191   -106    132       C  
ATOM   2675  O   VAL A 332      19.676  28.860  23.692  1.00 11.18           O  
ANISOU 2675  O   VAL A 332     1707    943   1599   -282    -90     97       O  
ATOM   2676  CB  VAL A 332      19.924  25.702  24.736  1.00  9.95           C  
ANISOU 2676  CB  VAL A 332     1520    905   1357   -284     -5    185       C  
ATOM   2677  CG1 VAL A 332      19.938  26.650  25.931  1.00 12.21           C  
ANISOU 2677  CG1 VAL A 332     1949   1214   1477   -271    -95    102       C  
ATOM   2678  CG2 VAL A 332      18.987  24.518  24.994  1.00 10.58           C  
ANISOU 2678  CG2 VAL A 332     1552   1041   1428   -350      5    247       C  
ATOM   2679  N   ALA A 333      21.495  27.813  22.896  1.00 10.97           N  
ANISOU 2679  N   ALA A 333     1623    968   1575   -415    -79    107       N  
ATOM   2680  CA  ALA A 333      22.231  29.089  22.733  1.00 11.77           C  
ANISOU 2680  CA  ALA A 333     1631   1073   1769   -412   -101     72       C  
ATOM   2681  C   ALA A 333      21.500  30.010  21.784  1.00 11.55           C  
ANISOU 2681  C   ALA A 333     1774    977   1637   -343    119    126       C  
ATOM   2682  O   ALA A 333      21.396  31.245  22.050  1.00 12.61           O  
ANISOU 2682  O   ALA A 333     1943   1030   1820   -389     46    -11       O  
ATOM   2683  CB  ALA A 333      23.643  28.785  22.250  1.00 12.96           C  
ANISOU 2683  CB  ALA A 333     1735   1175   2014   -514    127    207       C  
ATOM   2684  N   ASP A 334      20.959  29.490  20.680  1.00 11.67           N  
ANISOU 2684  N   ASP A 334     1735   1111   1587   -358     46    215       N  
ATOM   2685  CA  ASP A 334      20.223  30.318  19.728  1.00 11.45           C  
ANISOU 2685  CA  ASP A 334     1694   1104   1552   -382     78    198       C  
ATOM   2686  C   ASP A 334      18.944  30.872  20.339  1.00 11.08           C  
ANISOU 2686  C   ASP A 334     1906    996   1309   -224    136    184       C  
ATOM   2687  O   ASP A 334      18.595  32.049  20.109  1.00 11.90           O  
ANISOU 2687  O   ASP A 334     2042    944   1537   -271    177    130       O  
ATOM   2688  CB  ASP A 334      19.960  29.524  18.442  1.00 13.87           C  
ANISOU 2688  CB  ASP A 334     2220   1410   1640    -53     34    100       C  
ATOM   2689  CG  ASP A 334      21.201  29.317  17.577  1.00 18.08           C  
ANISOU 2689  CG  ASP A 334     2612   2289   1969     34    282    -38       C  
ATOM   2690  OD1 ASP A 334      22.247  29.935  17.804  1.00 21.49           O  
ANISOU 2690  OD1 ASP A 334     2761   2804   2598   -321    802    242       O  
ATOM   2691  OD2 ASP A 334      21.115  28.468  16.661  1.00 24.30           O  
ANISOU 2691  OD2 ASP A 334     3532   3445   2256    402     77   -492       O  
ATOM   2692  N   PHE A 335      18.231  30.077  21.167  1.00 10.57           N  
ANISOU 2692  N   PHE A 335     1673    904   1439   -289     68    173       N  
ATOM   2693  CA  PHE A 335      17.074  30.562  21.895  1.00 10.41           C  
ANISOU 2693  CA  PHE A 335     1746    801   1407   -221     79    222       C  
ATOM   2694  C   PHE A 335      17.451  31.730  22.820  1.00 10.62           C  
ANISOU 2694  C   PHE A 335     1586    929   1522   -223     79    191       C  
ATOM   2695  O   PHE A 335      16.734  32.748  22.881  1.00 11.52           O  
ANISOU 2695  O   PHE A 335     1931    914   1533   -203    159    226       O  
ATOM   2696  CB  PHE A 335      16.434  29.416  22.706  1.00 10.78           C  
ANISOU 2696  CB  PHE A 335     1751    887   1457   -305    129    227       C  
ATOM   2697  CG  PHE A 335      15.320  29.901  23.609  1.00 11.07           C  
ANISOU 2697  CG  PHE A 335     1847    808   1550   -239    146    127       C  
ATOM   2698  CD1 PHE A 335      14.094  30.285  23.057  1.00 13.19           C  
ANISOU 2698  CD1 PHE A 335     1722   1164   2124   -308    208     28       C  
ATOM   2699  CD2 PHE A 335      15.511  30.028  24.971  1.00 13.41           C  
ANISOU 2699  CD2 PHE A 335     2186   1269   1639   -119    253    365       C  
ATOM   2700  CE1 PHE A 335      13.082  30.747  23.895  1.00 14.08           C  
ANISOU 2700  CE1 PHE A 335     1668   1433   2248   -343    233     95       C  
ATOM   2701  CE2 PHE A 335      14.503  30.503  25.812  1.00 14.90           C  
ANISOU 2701  CE2 PHE A 335     2377   1598   1687   -258    382    226       C  
ATOM   2702  CZ  PHE A 335      13.288  30.838  25.250  1.00 15.36           C  
ANISOU 2702  CZ  PHE A 335     2113   1515   2207   -353    493    162       C  
ATOM   2703  N   MET A 336      18.568  31.565  23.547  1.00 10.92           N  
ANISOU 2703  N   MET A 336     1758    876   1517   -358    -45    138       N  
ATOM   2704  CA  MET A 336      18.991  32.633  24.476  1.00 12.51           C  
ANISOU 2704  CA  MET A 336     2259    904   1590   -292   -109    130       C  
ATOM   2705  C   MET A 336      19.336  33.917  23.732  1.00 12.38           C  
ANISOU 2705  C   MET A 336     2145    955   1602   -460     80     61       C  
ATOM   2706  O   MET A 336      19.205  35.003  24.335  1.00 15.71           O  
ANISOU 2706  O   MET A 336     3115   1116   1737   -480    314     70       O  
ATOM   2707  CB AMET A 336      20.199  32.122  25.278  0.78 13.31           C  
ANISOU 2707  CB AMET A 336     2198   1194   1664   -375    -83    237       C  
ATOM   2708  CG AMET A 336      19.992  30.963  26.254  0.78 12.98           C  
ANISOU 2708  CG AMET A 336     2254   1071   1607   -301    -45    155       C  
ATOM   2709  SD AMET A 336      18.713  31.249  27.501  0.78 13.94           S  
ANISOU 2709  SD AMET A 336     2566   1252   1477   -535    151    294       S  
ATOM   2710  CE AMET A 336      19.595  32.309  28.669  0.78 16.90           C  
ANISOU 2710  CE AMET A 336     2910   1821   1690   -588     98   -118       C  
ATOM   2711  CB BMET A 336      20.033  32.144  25.455  0.22 14.18           C  
ANISOU 2711  CB BMET A 336     2221   1367   1797   -165   -182     87       C  
ATOM   2712  CG BMET A 336      19.336  31.150  26.411  0.22 15.28           C  
ANISOU 2712  CG BMET A 336     2448   1456   1903   -262   -109     70       C  
ATOM   2713  SD BMET A 336      20.610  30.430  27.447  0.22 17.75           S  
ANISOU 2713  SD BMET A 336     2830   1799   2115   -133   -318    140       S  
ATOM   2714  CE BMET A 336      20.865  31.761  28.618  0.22 17.13           C  
ANISOU 2714  CE BMET A 336     2518   1895   2094   -221   -384    113       C  
ATOM   2715  N   ALA A 337      19.749  33.829  22.471  1.00 12.44           N  
ANISOU 2715  N   ALA A 337     2310    876   1542   -554      5     83       N  
ATOM   2716  CA  ALA A 337      20.051  34.979  21.608  1.00 12.36           C  
ANISOU 2716  CA  ALA A 337     1969   1035   1694   -461     41    212       C  
ATOM   2717  C   ALA A 337      18.848  35.390  20.788  1.00 11.55           C  
ANISOU 2717  C   ALA A 337     1964   1101   1324   -513    104    140       C  
ATOM   2718  O   ALA A 337      18.944  36.197  19.818  1.00 13.91           O  
ANISOU 2718  O   ALA A 337     2497   1178   1609   -508    294    301       O  
ATOM   2719  CB  ALA A 337      21.283  34.674  20.763  1.00 13.96           C  
ANISOU 2719  CB  ALA A 337     2113   1386   1806   -582    170    136       C  
ATOM   2720  N   LYS A 338      17.632  34.918  21.100  1.00 11.83           N  
ANISOU 2720  N   LYS A 338     1847   1037   1611   -333     83    179       N  
ATOM   2721  CA  LYS A 338      16.384  35.316  20.493  1.00 12.58           C  
ANISOU 2721  CA  LYS A 338     1897   1208   1674   -375     78    207       C  
ATOM   2722  C   LYS A 338      16.314  34.997  19.005  1.00 11.90           C  
ANISOU 2722  C   LYS A 338     1812   1196   1513   -167    102    324       C  
ATOM   2723  O   LYS A 338      15.679  35.692  18.188  1.00 14.08           O  
ANISOU 2723  O   LYS A 338     2548   1157   1644      9    -17    267       O  
ATOM   2724  CB ALYS A 338      16.123  36.813  20.746  0.59 15.02           C  
ANISOU 2724  CB ALYS A 338     2172   1468   2067    -36    -35     -3       C  
ATOM   2725  CG ALYS A 338      15.728  37.050  22.190  0.59 17.80           C  
ANISOU 2725  CG ALYS A 338     2454   2174   2137    -77     66    -16       C  
ATOM   2726  CD ALYS A 338      14.804  38.218  22.446  0.59 19.37           C  
ANISOU 2726  CD ALYS A 338     2610   2282   2467    -78    204   -144       C  
ATOM   2727  CE ALYS A 338      13.338  37.823  22.357  0.59 20.52           C  
ANISOU 2727  CE ALYS A 338     2653   2625   2518   -256    246   -109       C  
ATOM   2728  NZ ALYS A 338      12.418  38.995  22.400  0.59 21.00           N  
ANISOU 2728  NZ ALYS A 338     2720   2686   2574   -255    410    -35       N  
ATOM   2729  CB BLYS A 338      16.096  36.790  20.781  0.41 12.26           C  
ANISOU 2729  CB BLYS A 338     1754   1381   1522   -124      7     84       C  
ATOM   2730  CG BLYS A 338      16.211  37.290  22.202  0.41 12.35           C  
ANISOU 2730  CG BLYS A 338     1643   1543   1508    -54     18     70       C  
ATOM   2731  CD BLYS A 338      15.403  36.541  23.236  0.41 12.59           C  
ANISOU 2731  CD BLYS A 338     1658   1680   1445    -84     13     51       C  
ATOM   2732  CE BLYS A 338      15.652  37.007  24.665  0.41 12.45           C  
ANISOU 2732  CE BLYS A 338     1680   1633   1416    -57     48     81       C  
ATOM   2733  NZ BLYS A 338      14.794  36.285  25.649  0.41 12.75           N  
ANISOU 2733  NZ BLYS A 338     1690   1673   1482   -149     89     16       N  
ATOM   2734  N   LYS A 339      16.925  33.901  18.557  1.00 11.84           N  
ANISOU 2734  N   LYS A 339     1910   1035   1552   -306     92    228       N  
ATOM   2735  CA  LYS A 339      16.893  33.498  17.138  1.00 12.57           C  
ANISOU 2735  CA  LYS A 339     1958   1303   1514   -405     63    262       C  
ATOM   2736  C   LYS A 339      15.582  32.799  16.752  1.00 11.82           C  
ANISOU 2736  C   LYS A 339     1980   1172   1340   -383    109    110       C  
ATOM   2737  O   LYS A 339      15.249  32.729  15.559  1.00 14.38           O  
ANISOU 2737  O   LYS A 339     2466   1545   1454   -699    -15    397       O  
ATOM   2738  CB  LYS A 339      18.108  32.670  16.747  1.00 13.91           C  
ANISOU 2738  CB  LYS A 339     2090   1568   1627   -216     72    136       C  
ATOM   2739  CG  LYS A 339      19.440  33.331  16.975  1.00 14.63           C  
ANISOU 2739  CG  LYS A 339     2053   1663   1841   -180    113    108       C  
ATOM   2740  CD  LYS A 339      19.630  34.686  16.310  1.00 16.17           C  
ANISOU 2740  CD  LYS A 339     2308   1799   2037   -373    139    146       C  
ATOM   2741  CE  LYS A 339      21.045  35.217  16.512  1.00 18.18           C  
ANISOU 2741  CE  LYS A 339     2296   2250   2362   -432    242    141       C  
ATOM   2742  NZ  LYS A 339      21.213  36.611  15.978  1.00 20.09           N  
ANISOU 2742  NZ  LYS A 339     2860   2358   2414   -719    477    162       N  
ATOM   2743  N   PHE A 340      14.834  32.289  17.741  1.00 10.85           N  
ANISOU 2743  N   PHE A 340     1724   1054   1346   -343    -15    229       N  
ATOM   2744  CA  PHE A 340      13.515  31.712  17.555  1.00 10.78           C  
ANISOU 2744  CA  PHE A 340     1665   1008   1422   -156    -81    157       C  
ATOM   2745  C   PHE A 340      12.761  31.879  18.884  1.00 10.83           C  
ANISOU 2745  C   PHE A 340     1952    820   1342   -213    -25    232       C  
ATOM   2746  O   PHE A 340      13.379  32.188  19.909  1.00 13.30           O  
ANISOU 2746  O   PHE A 340     2332   1256   1465   -252   -174    163       O  
ATOM   2747  CB  PHE A 340      13.537  30.249  17.126  1.00 10.71           C  
ANISOU 2747  CB  PHE A 340     1802   1021   1248   -310    -10    157       C  
ATOM   2748  CG  PHE A 340      14.287  29.306  18.032  1.00 10.58           C  
ANISOU 2748  CG  PHE A 340     1691    906   1424   -221    -20     72       C  
ATOM   2749  CD1 PHE A 340      13.635  28.745  19.143  1.00 10.42           C  
ANISOU 2749  CD1 PHE A 340     1564   1003   1393   -235    -28    162       C  
ATOM   2750  CD2 PHE A 340      15.608  28.960  17.794  1.00 12.04           C  
ANISOU 2750  CD2 PHE A 340     1718   1134   1723   -352    108    133       C  
ATOM   2751  CE1 PHE A 340      14.304  27.836  19.954  1.00 10.77           C  
ANISOU 2751  CE1 PHE A 340     1546   1097   1451   -310    -83     98       C  
ATOM   2752  CE2 PHE A 340      16.268  28.072  18.626  1.00 12.01           C  
ANISOU 2752  CE2 PHE A 340     1688   1288   1587   -324     24     51       C  
ATOM   2753  CZ  PHE A 340      15.619  27.517  19.713  1.00 10.75           C  
ANISOU 2753  CZ  PHE A 340     1518   1150   1417   -349   -158     66       C  
ATOM   2754  N   ALA A 341      11.445  31.726  18.858  1.00 11.92           N  
ANISOU 2754  N   ALA A 341     1958   1155   1417   -162     87    312       N  
ATOM   2755  CA  ALA A 341      10.577  31.856  20.037  1.00 11.99           C  
ANISOU 2755  CA  ALA A 341     1967   1033   1555   -214    126    258       C  
ATOM   2756  C   ALA A 341       9.938  30.506  20.397  1.00 11.31           C  
ANISOU 2756  C   ALA A 341     1927   1075   1296   -265    138    175       C  
ATOM   2757  O   ALA A 341       9.608  29.719  19.517  1.00 13.40           O  
ANISOU 2757  O   ALA A 341     2413   1457   1222   -408    158    213       O  
ATOM   2758  CB  ALA A 341       9.452  32.849  19.745  1.00 13.71           C  
ANISOU 2758  CB  ALA A 341     2072   1395   1741    -84    169    401       C  
ATOM   2759  N   LEU A 342       9.738  30.291  21.706  1.00 10.17           N  
ANISOU 2759  N   LEU A 342     1716    888   1262   -117     16    172       N  
ATOM   2760  CA  LEU A 342       9.075  29.116  22.249  1.00  9.82           C  
ANISOU 2760  CA  LEU A 342     1586    906   1238   -189    -44    267       C  
ATOM   2761  C   LEU A 342       7.715  29.411  22.887  1.00 10.08           C  
ANISOU 2761  C   LEU A 342     1573   1001   1256   -104    -89    214       C  
ATOM   2762  O   LEU A 342       6.805  28.565  22.900  1.00 10.91           O  
ANISOU 2762  O   LEU A 342     1641   1161   1345   -126     46    191       O  
ATOM   2763  CB  LEU A 342       9.984  28.364  23.248  1.00  9.90           C  
ANISOU 2763  CB  LEU A 342     1602   1009   1151   -188    -37    151       C  
ATOM   2764  CG  LEU A 342      11.231  27.740  22.650  1.00  9.62           C  
ANISOU 2764  CG  LEU A 342     1486    956   1215   -263     64    221       C  
ATOM   2765  CD1 LEU A 342      12.160  27.187  23.728  1.00 10.24           C  
ANISOU 2765  CD1 LEU A 342     1568   1052   1273    -37    -14    121       C  
ATOM   2766  CD2 LEU A 342      10.912  26.667  21.592  1.00 10.81           C  
ANISOU 2766  CD2 LEU A 342     1673   1107   1328   -108     52     38       C  
ATOM   2767  N   ASP A 343       7.505  30.666  23.388  1.00 11.20           N  
ANISOU 2767  N   ASP A 343     1802   1092   1362    -53     76    126       N  
ATOM   2768  CA  ASP A 343       6.229  31.028  24.019  1.00 11.61           C  
ANISOU 2768  CA  ASP A 343     1842   1175   1395    -40     83    143       C  
ATOM   2769  C   ASP A 343       4.991  30.762  23.143  1.00 10.71           C  
ANISOU 2769  C   ASP A 343     1611   1101   1359     69    159    126       C  
ATOM   2770  O   ASP A 343       3.968  30.374  23.682  1.00 11.42           O  
ANISOU 2770  O   ASP A 343     1614   1186   1538    118     77    186       O  
ATOM   2771  CB  ASP A 343       6.229  32.479  24.477  1.00 14.71           C  
ANISOU 2771  CB  ASP A 343     2473   1365   1751    244     17   -184       C  
ATOM   2772  CG  ASP A 343       7.004  32.741  25.742  1.00 20.01           C  
ANISOU 2772  CG  ASP A 343     3404   2188   2010    129   -218   -496       C  
ATOM   2773  OD1 ASP A 343       7.439  31.783  26.414  1.00 20.96           O  
ANISOU 2773  OD1 ASP A 343     3420   2614   1931    524   -333   -517       O  
ATOM   2774  OD2 ASP A 343       7.165  33.934  26.089  1.00 24.12           O  
ANISOU 2774  OD2 ASP A 343     4069   2366   2730     57   -451   -650       O  
ATOM   2775  N   PRO A 344       5.029  30.921  21.816  1.00 10.80           N  
ANISOU 2775  N   PRO A 344     1583   1202   1320    -86     14    283       N  
ATOM   2776  CA  PRO A 344       3.816  30.635  21.042  1.00 11.55           C  
ANISOU 2776  CA  PRO A 344     1570   1365   1455    -52     23    303       C  
ATOM   2777  C   PRO A 344       3.328  29.196  21.180  1.00 11.06           C  
ANISOU 2777  C   PRO A 344     1661   1232   1309     87    -26    212       C  
ATOM   2778  O   PRO A 344       2.132  28.935  20.933  1.00 11.99           O  
ANISOU 2778  O   PRO A 344     1682   1283   1592     69   -114    239       O  
ATOM   2779  CB  PRO A 344       4.226  30.931  19.572  1.00 11.77           C  
ANISOU 2779  CB  PRO A 344     1703   1404   1365    -25    -83    254       C  
ATOM   2780  CG  PRO A 344       5.293  31.979  19.747  1.00 13.06           C  
ANISOU 2780  CG  PRO A 344     1914   1439   1611    -96    -92    387       C  
ATOM   2781  CD  PRO A 344       6.083  31.504  20.966  1.00 11.56           C  
ANISOU 2781  CD  PRO A 344     1814   1309   1269   -108     79    265       C  
ATOM   2782  N   LEU A 345       4.200  28.237  21.535  1.00 10.04           N  
ANISOU 2782  N   LEU A 345     1403   1177   1234     56    -41    176       N  
ATOM   2783  CA  LEU A 345       3.805  26.854  21.689  1.00  9.57           C  
ANISOU 2783  CA  LEU A 345     1466   1105   1065      1    -40    189       C  
ATOM   2784  C   LEU A 345       3.154  26.573  23.051  1.00 10.31           C  
ANISOU 2784  C   LEU A 345     1591   1152   1174     34    -57    191       C  
ATOM   2785  O   LEU A 345       2.458  25.534  23.179  1.00 10.13           O  
ANISOU 2785  O   LEU A 345     1480   1147   1224     16     81    137       O  
ATOM   2786  CB  LEU A 345       5.034  25.933  21.536  1.00  9.67           C  
ANISOU 2786  CB  LEU A 345     1355   1243   1076     41    -24    106       C  
ATOM   2787  CG  LEU A 345       5.849  26.123  20.246  1.00  9.89           C  
ANISOU 2787  CG  LEU A 345     1571   1139   1049   -162     33     30       C  
ATOM   2788  CD1 LEU A 345       7.061  25.189  20.218  1.00 12.64           C  
ANISOU 2788  CD1 LEU A 345     1830   1557   1415    162     74    -49       C  
ATOM   2789  CD2 LEU A 345       5.000  25.929  18.994  1.00 10.87           C  
ANISOU 2789  CD2 LEU A 345     1437   1499   1193   -157     36     88       C  
ATOM   2790  N   ILE A 346       3.388  27.403  24.064  1.00  9.73           N  
ANISOU 2790  N   ILE A 346     1617   1044   1034     83    167    164       N  
ATOM   2791  CA  ILE A 346       2.960  27.137  25.429  1.00 10.47           C  
ANISOU 2791  CA  ILE A 346     1561   1205   1214    107    238    261       C  
ATOM   2792  C   ILE A 346       1.612  27.785  25.701  1.00 10.74           C  
ANISOU 2792  C   ILE A 346     1610   1072   1399    192    165    211       C  
ATOM   2793  O   ILE A 346       1.502  29.022  25.750  1.00 13.53           O  
ANISOU 2793  O   ILE A 346     1935   1178   2028    243    304    183       O  
ATOM   2794  CB  ILE A 346       4.005  27.635  26.446  1.00 11.65           C  
ANISOU 2794  CB  ILE A 346     1980   1171   1276     66     79    192       C  
ATOM   2795  CG1 ILE A 346       5.363  26.968  26.204  1.00 12.63           C  
ANISOU 2795  CG1 ILE A 346     1824   1570   1404    -31      2    166       C  
ATOM   2796  CG2 ILE A 346       3.490  27.368  27.871  1.00 12.99           C  
ANISOU 2796  CG2 ILE A 346     2245   1484   1208    210     87    197       C  
ATOM   2797  CD1 ILE A 346       6.549  27.553  26.961  1.00 14.19           C  
ANISOU 2797  CD1 ILE A 346     1956   1841   1594     10   -212     71       C  
ATOM   2798  N   THR A 347       0.569  26.976  25.797  1.00 10.18           N  
ANISOU 2798  N   THR A 347     1424   1232   1214    212     91     98       N  
ATOM   2799  CA  THR A 347      -0.800  27.471  26.011  1.00 10.85           C  
ANISOU 2799  CA  THR A 347     1451   1495   1177    298     94     70       C  
ATOM   2800  C   THR A 347      -1.251  27.314  27.436  1.00 11.33           C  
ANISOU 2800  C   THR A 347     1656   1351   1298    384    150    128       C  
ATOM   2801  O   THR A 347      -2.237  27.982  27.835  1.00 12.36           O  
ANISOU 2801  O   THR A 347     1755   1533   1408    431    151    166       O  
ATOM   2802  CB ATHR A 347      -1.865  26.780  25.123  0.53 11.49           C  
ANISOU 2802  CB ATHR A 347     1663   1399   1303    174      1    230       C  
ATOM   2803  OG1ATHR A 347      -1.800  25.345  25.292  0.53 11.62           O  
ANISOU 2803  OG1ATHR A 347     1708   1485   1222    293    101     93       O  
ATOM   2804  CG2ATHR A 347      -1.740  27.073  23.636  0.53 10.99           C  
ANISOU 2804  CG2ATHR A 347     1477   1378   1320    388     42    146       C  
ATOM   2805  CB BTHR A 347      -1.710  26.849  24.938  0.47  9.97           C  
ANISOU 2805  CB BTHR A 347     1479   1216   1093    176    145    202       C  
ATOM   2806  OG1BTHR A 347      -1.676  25.424  25.073  0.47 10.44           O  
ANISOU 2806  OG1BTHR A 347     1614   1304   1050    228     77     31       O  
ATOM   2807  CG2BTHR A 347      -1.196  27.258  23.549  0.47 10.51           C  
ANISOU 2807  CG2BTHR A 347     1721   1297    973    -10     79    147       C  
ATOM   2808  N   HIS A 348      -0.693  26.378  28.208  1.00 10.71           N  
ANISOU 2808  N   HIS A 348     1658   1368   1042    294    154     37       N  
ATOM   2809  CA  HIS A 348      -1.133  26.043  29.557  1.00 10.75           C  
ANISOU 2809  CA  HIS A 348     1466   1478   1140     69    164    118       C  
ATOM   2810  C   HIS A 348       0.085  25.660  30.394  1.00 10.45           C  
ANISOU 2810  C   HIS A 348     1484   1334   1151     93    264     50       C  
ATOM   2811  O   HIS A 348       1.052  25.050  29.879  1.00 10.50           O  
ANISOU 2811  O   HIS A 348     1506   1383   1101    153    155     62       O  
ATOM   2812  CB AHIS A 348      -2.122  24.851  29.497  0.71 11.35           C  
ANISOU 2812  CB AHIS A 348     1370   1684   1259     92    137    143       C  
ATOM   2813  CG AHIS A 348      -3.382  25.140  28.718  0.71 11.02           C  
ANISOU 2813  CG AHIS A 348     1388   1559   1241    128     68     82       C  
ATOM   2814  ND1AHIS A 348      -3.417  25.147  27.334  0.71 10.47           N  
ANISOU 2814  ND1AHIS A 348     1364   1367   1245    154    151     91       N  
ATOM   2815  CD2AHIS A 348      -4.633  25.470  29.176  0.71 12.35           C  
ANISOU 2815  CD2AHIS A 348     1540   1721   1431     62    240     96       C  
ATOM   2816  CE1AHIS A 348      -4.657  25.499  26.984  0.71 11.00           C  
ANISOU 2816  CE1AHIS A 348     1266   1409   1505    207    206    101       C  
ATOM   2817  NE2AHIS A 348      -5.408  25.698  28.065  0.71 12.49           N  
ANISOU 2817  NE2AHIS A 348     1684   1612   1448    154    116     32       N  
ATOM   2818  CB BHIS A 348      -2.083  24.839  29.535  0.29 12.42           C  
ANISOU 2818  CB BHIS A 348     1581   1635   1505      3    159    125       C  
ATOM   2819  CG BHIS A 348      -3.412  24.952  28.864  0.29 13.78           C  
ANISOU 2819  CG BHIS A 348     1658   1893   1686     86     66    100       C  
ATOM   2820  ND1BHIS A 348      -3.590  24.852  27.498  0.29 14.09           N  
ANISOU 2820  ND1BHIS A 348     1799   1850   1703     72    109     65       N  
ATOM   2821  CD2BHIS A 348      -4.651  25.152  29.390  0.29 13.93           C  
ANISOU 2821  CD2BHIS A 348     1695   1849   1747    -21    159    265       C  
ATOM   2822  CE1BHIS A 348      -4.873  25.004  27.216  0.29 14.04           C  
ANISOU 2822  CE1BHIS A 348     1741   1850   1743    -13    116     87       C  
ATOM   2823  NE2BHIS A 348      -5.547  25.180  28.348  0.29 14.06           N  
ANISOU 2823  NE2BHIS A 348     1674   1882   1787      9    145    156       N  
ATOM   2824  N   VAL A 349       0.022  25.954  31.691  1.00 10.52           N  
ANISOU 2824  N   VAL A 349     1485   1450   1064    192    178     84       N  
ATOM   2825  CA  VAL A 349       1.026  25.528  32.668  1.00 11.17           C  
ANISOU 2825  CA  VAL A 349     1620   1452   1172    314    186     92       C  
ATOM   2826  C   VAL A 349       0.284  24.865  33.833  1.00 11.70           C  
ANISOU 2826  C   VAL A 349     1832   1587   1026    394    186      4       C  
ATOM   2827  O   VAL A 349      -0.778  25.359  34.277  1.00 13.85           O  
ANISOU 2827  O   VAL A 349     2053   1907   1303    564    346    199       O  
ATOM   2828  CB  VAL A 349       1.917  26.708  33.110  1.00 13.01           C  
ANISOU 2828  CB  VAL A 349     1897   1696   1351    140      1     38       C  
ATOM   2829  CG1 VAL A 349       2.799  27.204  31.962  1.00 13.73           C  
ANISOU 2829  CG1 VAL A 349     2089   1592   1534    116     69     93       C  
ATOM   2830  CG2 VAL A 349       1.129  27.891  33.722  1.00 15.64           C  
ANISOU 2830  CG2 VAL A 349     2393   1860   1687    245    236    -70       C  
ATOM   2831  N   LEU A 350       0.812  23.738  34.315  1.00 11.02           N  
ANISOU 2831  N   LEU A 350     1605   1524   1058    258    144     42       N  
ATOM   2832  CA  LEU A 350       0.231  23.020  35.465  1.00 10.77           C  
ANISOU 2832  CA  LEU A 350     1433   1547   1111    118     90     64       C  
ATOM   2833  C   LEU A 350       1.353  22.422  36.319  1.00 10.39           C  
ANISOU 2833  C   LEU A 350     1484   1371   1091    145    133     47       C  
ATOM   2834  O   LEU A 350       2.444  22.118  35.792  1.00 11.19           O  
ANISOU 2834  O   LEU A 350     1509   1617   1125    181    139     58       O  
ATOM   2835  CB  LEU A 350      -0.638  21.844  34.956  1.00 11.29           C  
ANISOU 2835  CB  LEU A 350     1565   1500   1226     34    160     54       C  
ATOM   2836  CG  LEU A 350      -1.976  22.148  34.286  1.00 12.71           C  
ANISOU 2836  CG  LEU A 350     1547   1808   1474    -35    121      6       C  
ATOM   2837  CD1 LEU A 350      -2.601  20.880  33.714  1.00 12.92           C  
ANISOU 2837  CD1 LEU A 350     1627   1860   1421    -61     93     40       C  
ATOM   2838  CD2 LEU A 350      -2.960  22.782  35.254  1.00 14.39           C  
ANISOU 2838  CD2 LEU A 350     1613   2154   1699     30    147   -142       C  
ATOM   2839  N   PRO A 351       1.109  22.196  37.602  1.00 10.19           N  
ANISOU 2839  N   PRO A 351     1414   1442   1017    120    136    -10       N  
ATOM   2840  CA  PRO A 351       2.059  21.378  38.376  1.00 10.74           C  
ANISOU 2840  CA  PRO A 351     1595   1409   1077    165     75      9       C  
ATOM   2841  C   PRO A 351       2.021  19.943  37.867  1.00 10.70           C  
ANISOU 2841  C   PRO A 351     1508   1475   1082     19     72    122       C  
ATOM   2842  O   PRO A 351       0.992  19.456  37.400  1.00 10.69           O  
ANISOU 2842  O   PRO A 351     1545   1404   1114     50     80    126       O  
ATOM   2843  CB  PRO A 351       1.562  21.514  39.816  1.00 12.25           C  
ANISOU 2843  CB  PRO A 351     1835   1677   1141    247    184     11       C  
ATOM   2844  CG  PRO A 351       0.077  21.688  39.635  1.00 12.70           C  
ANISOU 2844  CG  PRO A 351     1801   1918   1107     90    140    147       C  
ATOM   2845  CD  PRO A 351      -0.106  22.521  38.371  1.00 11.23           C  
ANISOU 2845  CD  PRO A 351     1391   1682   1195     82    100     50       C  
ATOM   2846  N   PHE A 352       3.141  19.237  38.078  1.00 10.63           N  
ANISOU 2846  N   PHE A 352     1612   1334   1091    113     32     56       N  
ATOM   2847  CA  PHE A 352       3.250  17.817  37.725  1.00 10.90           C  
ANISOU 2847  CA  PHE A 352     1582   1475   1083     58     -4     13       C  
ATOM   2848  C   PHE A 352       2.099  16.982  38.257  1.00 11.30           C  
ANISOU 2848  C   PHE A 352     1637   1427   1229     50     67     76       C  
ATOM   2849  O   PHE A 352       1.624  16.045  37.597  1.00 11.10           O  
ANISOU 2849  O   PHE A 352     1577   1466   1173    -52     16    154       O  
ATOM   2850  CB  PHE A 352       4.601  17.283  38.185  1.00 11.53           C  
ANISOU 2850  CB  PHE A 352     1564   1273   1545     54    -76     33       C  
ATOM   2851  CG  PHE A 352       4.813  15.795  38.018  1.00 12.23           C  
ANISOU 2851  CG  PHE A 352     1687   1235   1726      6    -92    155       C  
ATOM   2852  CD1 PHE A 352       4.862  15.239  36.745  1.00 13.82           C  
ANISOU 2852  CD1 PHE A 352     1731   1597   1922    141   -179   -191       C  
ATOM   2853  CD2 PHE A 352       4.984  14.993  39.128  1.00 15.39           C  
ANISOU 2853  CD2 PHE A 352     2157   1572   2118    -32    -70    367       C  
ATOM   2854  CE1 PHE A 352       5.060  13.856  36.598  1.00 16.04           C  
ANISOU 2854  CE1 PHE A 352     1998   1685   2413     -7   -355   -244       C  
ATOM   2855  CE2 PHE A 352       5.177  13.617  38.987  1.00 17.13           C  
ANISOU 2855  CE2 PHE A 352     2285   1670   2553     82   -149    340       C  
ATOM   2856  CZ  PHE A 352       5.222  13.078  37.721  1.00 17.73           C  
ANISOU 2856  CZ  PHE A 352     2305   1618   2812   -143   -305     30       C  
ATOM   2857  N   GLU A 353       1.648  17.282  39.497  1.00 11.17           N  
ANISOU 2857  N   GLU A 353     1716   1431   1096   -150    100    133       N  
ATOM   2858  CA  GLU A 353       0.587  16.510  40.131  1.00 12.00           C  
ANISOU 2858  CA  GLU A 353     1717   1695   1149   -102    100    193       C  
ATOM   2859  C   GLU A 353      -0.707  16.541  39.346  1.00 12.03           C  
ANISOU 2859  C   GLU A 353     1562   1712   1295    -98    160    188       C  
ATOM   2860  O   GLU A 353      -1.582  15.676  39.558  1.00 13.72           O  
ANISOU 2860  O   GLU A 353     1780   2106   1327   -281     53    366       O  
ATOM   2861  CB  GLU A 353       0.403  16.993  41.588  1.00 12.58           C  
ANISOU 2861  CB  GLU A 353     1733   1828   1219      9     72    173       C  
ATOM   2862  CG  GLU A 353       1.590  16.735  42.484  1.00 14.04           C  
ANISOU 2862  CG  GLU A 353     1996   2133   1205     42    -45    103       C  
ATOM   2863  CD  GLU A 353       2.817  17.576  42.252  1.00 13.12           C  
ANISOU 2863  CD  GLU A 353     1913   1991   1082    152     48    -99       C  
ATOM   2864  OE1 GLU A 353       2.676  18.734  41.758  1.00 13.19           O  
ANISOU 2864  OE1 GLU A 353     1737   1977   1299      1     79     52       O  
ATOM   2865  OE2 GLU A 353       3.936  17.072  42.536  1.00 15.59           O  
ANISOU 2865  OE2 GLU A 353     2083   2504   1336    310     52    242       O  
ATOM   2866  N   LYS A 354      -0.908  17.537  38.456  1.00 11.97           N  
ANISOU 2866  N   LYS A 354     1633   1717   1198      9    138    149       N  
ATOM   2867  CA  LYS A 354      -2.094  17.642  37.633  1.00 11.56           C  
ANISOU 2867  CA  LYS A 354     1510   1725   1157    -36    184    129       C  
ATOM   2868  C   LYS A 354      -1.834  17.137  36.207  1.00 11.37           C  
ANISOU 2868  C   LYS A 354     1568   1658   1093     34    189    267       C  
ATOM   2869  O   LYS A 354      -2.521  17.520  35.229  1.00 11.88           O  
ANISOU 2869  O   LYS A 354     1503   1789   1223    125    192    263       O  
ATOM   2870  CB  LYS A 354      -2.601  19.091  37.633  1.00 12.72           C  
ANISOU 2870  CB  LYS A 354     1742   1813   1280     33    274     83       C  
ATOM   2871  CG  LYS A 354      -3.173  19.496  39.000  1.00 14.05           C  
ANISOU 2871  CG  LYS A 354     1837   2152   1349     19    296    109       C  
ATOM   2872  CD  LYS A 354      -3.740  20.906  39.049  1.00 16.80           C  
ANISOU 2872  CD  LYS A 354     2251   2268   1863    187    324    137       C  
ATOM   2873  CE  LYS A 354      -4.462  21.167  40.372  1.00 20.86           C  
ANISOU 2873  CE  LYS A 354     3108   2825   1994    203    457   -198       C  
ATOM   2874  NZ  LYS A 354      -5.232  22.432  40.381  1.00 25.20           N  
ANISOU 2874  NZ  LYS A 354     3571   3120   2884    412    423    -51       N  
ATOM   2875  N   ILE A 355      -0.932  16.155  36.035  1.00 11.02           N  
ANISOU 2875  N   ILE A 355     1558   1594   1035     -7     96    158       N  
ATOM   2876  CA  ILE A 355      -0.638  15.573  34.732  1.00 10.47           C  
ANISOU 2876  CA  ILE A 355     1295   1572   1113     51     94    247       C  
ATOM   2877  C   ILE A 355      -1.898  15.060  34.028  1.00 10.49           C  
ANISOU 2877  C   ILE A 355     1281   1553   1153     25    127    253       C  
ATOM   2878  O   ILE A 355      -2.010  15.255  32.799  1.00 10.45           O  
ANISOU 2878  O   ILE A 355     1298   1512   1159    -39    121    246       O  
ATOM   2879  CB  ILE A 355       0.404  14.425  34.874  1.00 10.75           C  
ANISOU 2879  CB  ILE A 355     1396   1547   1142      5     55    164       C  
ATOM   2880  CG1 ILE A 355       0.842  13.878  33.508  1.00 10.72           C  
ANISOU 2880  CG1 ILE A 355     1528   1395   1150     49     46    133       C  
ATOM   2881  CG2 ILE A 355       0.006  13.304  35.847  1.00 13.11           C  
ANISOU 2881  CG2 ILE A 355     1945   1718   1318     53    175    248       C  
ATOM   2882  CD1 ILE A 355       2.124  13.069  33.534  1.00 13.17           C  
ANISOU 2882  CD1 ILE A 355     1865   1792   1345    339    -50    171       C  
ATOM   2883  N   ASN A 356      -2.832  14.392  34.724  1.00 11.03           N  
ANISOU 2883  N   ASN A 356     1347   1704   1140    -39    183    303       N  
ATOM   2884  CA  ASN A 356      -4.012  13.887  34.003  1.00 11.02           C  
ANISOU 2884  CA  ASN A 356     1477   1609   1100    -13    228    203       C  
ATOM   2885  C   ASN A 356      -4.879  15.007  33.419  1.00 11.26           C  
ANISOU 2885  C   ASN A 356     1390   1695   1195     -6     85    199       C  
ATOM   2886  O   ASN A 356      -5.339  14.851  32.260  1.00 11.99           O  
ANISOU 2886  O   ASN A 356     1495   1832   1231    -78    129    245       O  
ATOM   2887  CB  ASN A 356      -4.801  12.931  34.906  1.00 12.04           C  
ANISOU 2887  CB  ASN A 356     1538   1803   1234    -13    295    249       C  
ATOM   2888  CG  ASN A 356      -4.056  11.611  35.084  1.00 11.99           C  
ANISOU 2888  CG  ASN A 356     1500   1703   1354   -118    189    300       C  
ATOM   2889  OD1 ASN A 356      -3.594  10.995  34.100  1.00 13.19           O  
ANISOU 2889  OD1 ASN A 356     1892   1697   1424     38    322    376       O  
ATOM   2890  ND2 ASN A 356      -3.943  11.113  36.320  1.00 13.54           N  
ANISOU 2890  ND2 ASN A 356     1872   1740   1534    170    259    396       N  
ATOM   2891  N   GLU A 357      -5.067  16.117  34.119  1.00 11.16           N  
ANISOU 2891  N   GLU A 357     1297   1743   1202     17    150    234       N  
ATOM   2892  CA  GLU A 357      -5.767  17.275  33.535  1.00 12.37           C  
ANISOU 2892  CA  GLU A 357     1579   1820   1302    231    131    237       C  
ATOM   2893  C   GLU A 357      -5.026  17.780  32.292  1.00 11.71           C  
ANISOU 2893  C   GLU A 357     1316   1922   1210     68     80    126       C  
ATOM   2894  O   GLU A 357      -5.645  18.192  31.304  1.00 12.45           O  
ANISOU 2894  O   GLU A 357     1360   1955   1414    134    120    266       O  
ATOM   2895  CB AGLU A 357      -5.855  18.386  34.600  0.64 13.80           C  
ANISOU 2895  CB AGLU A 357     1792   2207   1242    253    418     67       C  
ATOM   2896  CG AGLU A 357      -6.473  19.670  34.075  0.64 16.19           C  
ANISOU 2896  CG AGLU A 357     2067   2226   1859    318    262     40       C  
ATOM   2897  CD AGLU A 357      -6.610  20.838  35.023  0.64 19.72           C  
ANISOU 2897  CD AGLU A 357     2437   2583   2473    370    387   -267       C  
ATOM   2898  OE1AGLU A 357      -6.272  20.706  36.198  0.64 20.79           O  
ANISOU 2898  OE1AGLU A 357     2546   2877   2474    308    465   -427       O  
ATOM   2899  OE2AGLU A 357      -7.024  21.917  34.518  0.64 23.78           O  
ANISOU 2899  OE2AGLU A 357     3247   2522   3265    455    346   -158       O  
ATOM   2900  CB BGLU A 357      -5.849  18.361  34.608  0.36 14.09           C  
ANISOU 2900  CB BGLU A 357     1835   1982   1538    294    106     41       C  
ATOM   2901  CG BGLU A 357      -6.748  17.975  35.768  0.36 15.53           C  
ANISOU 2901  CG BGLU A 357     1908   2165   1826    216    234     42       C  
ATOM   2902  CD BGLU A 357      -6.625  18.943  36.939  0.36 17.80           C  
ANISOU 2902  CD BGLU A 357     2382   2499   1881    122    133    -71       C  
ATOM   2903  OE1BGLU A 357      -6.943  20.110  36.630  0.36 18.65           O  
ANISOU 2903  OE1BGLU A 357     2643   2337   2107    -14    314   -142       O  
ATOM   2904  OE2BGLU A 357      -6.239  18.555  38.066  0.36 16.16           O  
ANISOU 2904  OE2BGLU A 357     2079   2576   1484    -46    278   -327       O  
ATOM   2905  N   GLY A 358      -3.683  17.758  32.319  1.00 10.89           N  
ANISOU 2905  N   GLY A 358     1323   1682   1133     29    199    177       N  
ATOM   2906  CA  GLY A 358      -2.898  18.174  31.148  1.00 11.37           C  
ANISOU 2906  CA  GLY A 358     1514   1650   1156     67    236    213       C  
ATOM   2907  C   GLY A 358      -3.147  17.269  29.938  1.00  9.99           C  
ANISOU 2907  C   GLY A 358     1099   1497   1198    -21    129    242       C  
ATOM   2908  O   GLY A 358      -3.210  17.742  28.782  1.00 10.85           O  
ANISOU 2908  O   GLY A 358     1315   1555   1251    -44     75    185       O  
ATOM   2909  N   PHE A 359      -3.243  15.965  30.155  1.00  9.94           N  
ANISOU 2909  N   PHE A 359     1190   1501   1087     54     88    208       N  
ATOM   2910  CA  PHE A 359      -3.608  15.055  29.049  1.00 10.70           C  
ANISOU 2910  CA  PHE A 359     1383   1361   1322      5     46    201       C  
ATOM   2911  C   PHE A 359      -5.056  15.293  28.576  1.00 11.52           C  
ANISOU 2911  C   PHE A 359     1395   1678   1304      3     16    111       C  
ATOM   2912  O   PHE A 359      -5.331  15.204  27.361  1.00 12.23           O  
ANISOU 2912  O   PHE A 359     1632   1708   1305    -35     -9    214       O  
ATOM   2913  CB  PHE A 359      -3.334  13.581  29.376  1.00 10.32           C  
ANISOU 2913  CB  PHE A 359     1265   1407   1248    -42     96    243       C  
ATOM   2914  CG  PHE A 359      -1.885  13.192  29.183  1.00  9.93           C  
ANISOU 2914  CG  PHE A 359     1317   1357   1098   -124    148    216       C  
ATOM   2915  CD1 PHE A 359      -0.899  13.522  30.096  1.00 10.42           C  
ANISOU 2915  CD1 PHE A 359     1313   1503   1144     16     81    216       C  
ATOM   2916  CD2 PHE A 359      -1.480  12.569  28.003  1.00 10.06           C  
ANISOU 2916  CD2 PHE A 359     1375   1317   1132   -192     66    143       C  
ATOM   2917  CE1 PHE A 359       0.431  13.215  29.878  1.00 10.16           C  
ANISOU 2917  CE1 PHE A 359     1375   1359   1127      9    154    276       C  
ATOM   2918  CE2 PHE A 359      -0.148  12.269  27.772  1.00 10.94           C  
ANISOU 2918  CE2 PHE A 359     1442   1569   1146    -88     41    181       C  
ATOM   2919  CZ  PHE A 359       0.821  12.589  28.704  1.00  9.95           C  
ANISOU 2919  CZ  PHE A 359     1252   1322   1207     -9    104    210       C  
ATOM   2920  N   ASP A 360      -5.973  15.577  29.518  1.00 11.87           N  
ANISOU 2920  N   ASP A 360     1260   1836   1412    -84     70    208       N  
ATOM   2921  CA  ASP A 360      -7.340  15.901  29.121  1.00 13.04           C  
ANISOU 2921  CA  ASP A 360     1392   1901   1663     57     74    421       C  
ATOM   2922  C   ASP A 360      -7.379  17.110  28.199  1.00 11.99           C  
ANISOU 2922  C   ASP A 360     1373   1815   1367    -26     57    259       C  
ATOM   2923  O   ASP A 360      -8.139  17.149  27.202  1.00 13.13           O  
ANISOU 2923  O   ASP A 360     1272   2171   1545   -111     98    349       O  
ATOM   2924  CB  ASP A 360      -8.217  16.156  30.367  1.00 15.40           C  
ANISOU 2924  CB  ASP A 360     1573   2470   1810      0    252    445       C  
ATOM   2925  CG  ASP A 360      -8.455  15.058  31.366  1.00 18.88           C  
ANISOU 2925  CG  ASP A 360     2416   2674   2083    -52    338    415       C  
ATOM   2926  OD1 ASP A 360      -8.313  13.890  30.981  1.00 20.19           O  
ANISOU 2926  OD1 ASP A 360     2478   2500   2695   -152    314    409       O  
ATOM   2927  OD2 ASP A 360      -8.849  15.313  32.552  1.00 23.46           O  
ANISOU 2927  OD2 ASP A 360     2955   3603   2355    110    639    365       O  
ATOM   2928  N   LEU A 361      -6.594  18.152  28.495  1.00 11.71           N  
ANISOU 2928  N   LEU A 361     1385   1766   1299     50    158    160       N  
ATOM   2929  CA  LEU A 361      -6.511  19.343  27.654  1.00 11.99           C  
ANISOU 2929  CA  LEU A 361     1422   1706   1427    136    222    202       C  
ATOM   2930  C   LEU A 361      -6.020  18.993  26.250  1.00 12.29           C  
ANISOU 2930  C   LEU A 361     1438   1756   1475    185    137    248       C  
ATOM   2931  O   LEU A 361      -6.520  19.543  25.254  1.00 13.66           O  
ANISOU 2931  O   LEU A 361     1449   2209   1530    401    127    292       O  
ATOM   2932  CB  LEU A 361      -5.594  20.386  28.282  1.00 12.50           C  
ANISOU 2932  CB  LEU A 361     1656   1605   1489     96    328    199       C  
ATOM   2933  CG  LEU A 361      -6.110  21.154  29.505  1.00 13.89           C  
ANISOU 2933  CG  LEU A 361     1986   1770   1521    332    203     85       C  
ATOM   2934  CD1 LEU A 361      -4.972  21.834  30.247  1.00 16.08           C  
ANISOU 2934  CD1 LEU A 361     2208   1951   1953    251    -22     95       C  
ATOM   2935  CD2 LEU A 361      -7.144  22.198  29.044  1.00 16.31           C  
ANISOU 2935  CD2 LEU A 361     2105   2112   1982    525     60     55       C  
ATOM   2936  N   LEU A 362      -4.992  18.142  26.123  1.00 10.73           N  
ANISOU 2936  N   LEU A 362     1262   1604   1213     88    134    198       N  
ATOM   2937  CA  LEU A 362      -4.503  17.750  24.799  1.00 10.41           C  
ANISOU 2937  CA  LEU A 362     1305   1428   1224    -61     56     93       C  
ATOM   2938  C   LEU A 362      -5.588  17.015  24.024  1.00 10.10           C  
ANISOU 2938  C   LEU A 362     1148   1468   1223     13     54    111       C  
ATOM   2939  O   LEU A 362      -5.892  17.337  22.840  1.00 11.68           O  
ANISOU 2939  O   LEU A 362     1318   1856   1266    -76     11    231       O  
ATOM   2940  CB  LEU A 362      -3.266  16.848  24.937  1.00 10.99           C  
ANISOU 2940  CB  LEU A 362     1300   1587   1287    -76     36     54       C  
ATOM   2941  CG  LEU A 362      -2.645  16.402  23.594  1.00 12.34           C  
ANISOU 2941  CG  LEU A 362     1427   1927   1336     53     -9    -13       C  
ATOM   2942  CD1 LEU A 362      -1.960  17.557  22.865  1.00 14.78           C  
ANISOU 2942  CD1 LEU A 362     1716   2276   1626    -96    361     68       C  
ATOM   2943  CD2 LEU A 362      -1.688  15.236  23.801  1.00 15.57           C  
ANISOU 2943  CD2 LEU A 362     1990   2288   1639    449     36   -224       C  
ATOM   2944  N   ARG A 363      -6.212  16.031  24.684  1.00 11.64           N  
ANISOU 2944  N   ARG A 363     1457   1507   1459   -157     89    201       N  
ATOM   2945  CA  ARG A 363      -7.207  15.177  24.015  1.00 12.26           C  
ANISOU 2945  CA  ARG A 363     1409   1813   1437   -204     24    241       C  
ATOM   2946  C   ARG A 363      -8.449  15.951  23.591  1.00 13.55           C  
ANISOU 2946  C   ARG A 363     1493   2040   1615   -182    -67    200       C  
ATOM   2947  O   ARG A 363      -9.081  15.568  22.582  1.00 15.28           O  
ANISOU 2947  O   ARG A 363     1580   2444   1782   -282   -304    307       O  
ATOM   2948  CB  ARG A 363      -7.596  14.004  24.923  1.00 12.79           C  
ANISOU 2948  CB  ARG A 363     1342   1926   1591   -248     16    324       C  
ATOM   2949  CG  ARG A 363      -6.453  13.035  25.186  1.00 12.65           C  
ANISOU 2949  CG  ARG A 363     1563   1680   1565   -164    -19    294       C  
ATOM   2950  CD  ARG A 363      -6.783  12.099  26.350  1.00 14.97           C  
ANISOU 2950  CD  ARG A 363     1497   2209   1984    -57     89    672       C  
ATOM   2951  NE  ARG A 363      -5.631  11.232  26.625  1.00 14.38           N  
ANISOU 2951  NE  ARG A 363     1610   2074   1778    -25    191    336       N  
ATOM   2952  CZ  ARG A 363      -5.289  10.759  27.798  1.00 13.88           C  
ANISOU 2952  CZ  ARG A 363     1437   2092   1745   -160    154    372       C  
ATOM   2953  NH1 ARG A 363      -6.048  11.026  28.891  1.00 16.87           N  
ANISOU 2953  NH1 ARG A 363     1812   2752   1847   -109    310    376       N  
ATOM   2954  NH2 ARG A 363      -4.178  10.056  27.955  1.00 14.21           N  
ANISOU 2954  NH2 ARG A 363     1705   2015   1680    -31    218    343       N  
ATOM   2955  N   SER A 364      -8.847  16.989  24.302  1.00 12.98           N  
ANISOU 2955  N   SER A 364     1272   2074   1585     12     47    287       N  
ATOM   2956  CA  SER A 364     -10.019  17.784  23.942  1.00 14.39           C  
ANISOU 2956  CA  SER A 364     1508   2202   1755    140     74    395       C  
ATOM   2957  C   SER A 364      -9.791  18.697  22.758  1.00 14.34           C  
ANISOU 2957  C   SER A 364     1462   2271   1716     18     70    472       C  
ATOM   2958  O   SER A 364     -10.755  19.325  22.279  1.00 16.39           O  
ANISOU 2958  O   SER A 364     1467   2742   2019    189     60    529       O  
ATOM   2959  CB  SER A 364     -10.451  18.638  25.132  1.00 16.46           C  
ANISOU 2959  CB  SER A 364     1751   2637   1866    411    166    291       C  
ATOM   2960  OG  SER A 364      -9.524  19.707  25.322  1.00 17.26           O  
ANISOU 2960  OG  SER A 364     1819   2864   1876    384     77    156       O  
ATOM   2961  N   GLY A 365      -8.538  18.893  22.339  1.00 13.36           N  
ANISOU 2961  N   GLY A 365     1421   2064   1591    -36     63    371       N  
ATOM   2962  CA  GLY A 365      -8.208  19.845  21.303  1.00 13.81           C  
ANISOU 2962  CA  GLY A 365     1689   2119   1439     24    142    331       C  
ATOM   2963  C   GLY A 365      -7.859  21.234  21.789  1.00 13.45           C  
ANISOU 2963  C   GLY A 365     1524   2006   1579    223    155    344       C  
ATOM   2964  O   GLY A 365      -7.492  22.082  20.950  1.00 15.74           O  
ANISOU 2964  O   GLY A 365     2068   2073   1839    225    242    472       O  
ATOM   2965  N   GLU A 366      -7.959  21.490  23.106  1.00 13.73           N  
ANISOU 2965  N   GLU A 366     1461   2183   1573    119      2    194       N  
ATOM   2966  CA  GLU A 366      -7.804  22.837  23.631  1.00 15.22           C  
ANISOU 2966  CA  GLU A 366     1728   2214   1840    110    182     65       C  
ATOM   2967  C   GLU A 366      -6.368  23.305  23.699  1.00 15.29           C  
ANISOU 2967  C   GLU A 366     1732   1989   2089    193    -99    310       C  
ATOM   2968  O   GLU A 366      -6.080  24.509  23.490  1.00 21.81           O  
ANISOU 2968  O   GLU A 366     2271   2042   3974    237   -670    448       O  
ATOM   2969  CB AGLU A 366      -8.453  23.007  25.024  0.50 16.17           C  
ANISOU 2969  CB AGLU A 366     1597   2504   2041     44    344    -60       C  
ATOM   2970  CG AGLU A 366      -8.244  24.392  25.605  0.50 18.50           C  
ANISOU 2970  CG AGLU A 366     1982   2496   2552    231     70   -151       C  
ATOM   2971  CD AGLU A 366      -8.789  24.674  26.988  0.50 19.55           C  
ANISOU 2971  CD AGLU A 366     1988   2835   2605     84    146   -105       C  
ATOM   2972  OE1AGLU A 366      -9.655  23.874  27.423  0.50 20.72           O  
ANISOU 2972  OE1AGLU A 366     1834   3058   2980     -9     67   -109       O  
ATOM   2973  OE2AGLU A 366      -8.349  25.685  27.615  0.50 18.52           O  
ANISOU 2973  OE2AGLU A 366     1514   2772   2752    375    249   -268       O  
ATOM   2974  CB BGLU A 366      -8.448  22.904  25.029  0.50 19.43           C  
ANISOU 2974  CB BGLU A 366     2488   2814   2082    128    467    -32       C  
ATOM   2975  CG BGLU A 366      -9.929  22.580  25.175  0.50 23.07           C  
ANISOU 2975  CG BGLU A 366     2576   3160   3031     75    410    -94       C  
ATOM   2976  CD BGLU A 366     -10.304  22.454  26.656  0.50 25.62           C  
ANISOU 2976  CD BGLU A 366     3161   3453   3122     23    481     56       C  
ATOM   2977  OE1BGLU A 366     -10.358  23.557  27.247  0.50 27.28           O  
ANISOU 2977  OE1BGLU A 366     3303   3574   3489    -59    388   -132       O  
ATOM   2978  OE2BGLU A 366     -10.487  21.376  27.275  0.50 22.78           O  
ANISOU 2978  OE2BGLU A 366     2667   3496   2493    -63    796    -97       O  
ATOM   2979  N   SER A 367      -5.402  22.465  23.997  1.00 11.80           N  
ANISOU 2979  N   SER A 367     1481   1618   1383     71    186    147       N  
ATOM   2980  CA  SER A 367      -4.037  22.901  24.178  1.00 10.83           C  
ANISOU 2980  CA  SER A 367     1440   1492   1185    171    181     70       C  
ATOM   2981  C   SER A 367      -3.159  22.669  22.956  1.00  9.37           C  
ANISOU 2981  C   SER A 367     1198   1259   1102    135     93    176       C  
ATOM   2982  O   SER A 367      -3.414  21.834  22.103  1.00 10.59           O  
ANISOU 2982  O   SER A 367     1323   1493   1206     49    155     75       O  
ATOM   2983  CB  SER A 367      -3.420  22.174  25.399  1.00 11.14           C  
ANISOU 2983  CB  SER A 367     1688   1436   1110    114    261     74       C  
ATOM   2984  OG  SER A 367      -3.469  20.779  25.138  1.00 11.16           O  
ANISOU 2984  OG  SER A 367     1660   1379   1200      5     53    231       O  
ATOM   2985  N   ILE A 368      -2.014  23.378  22.985  1.00  9.17           N  
ANISOU 2985  N   ILE A 368     1278   1152   1054    135    103     85       N  
ATOM   2986  CA  ILE A 368      -0.837  23.082  22.125  1.00  8.77           C  
ANISOU 2986  CA  ILE A 368     1162   1122   1049    126     92    204       C  
ATOM   2987  C   ILE A 368       0.122  22.338  23.052  1.00  8.84           C  
ANISOU 2987  C   ILE A 368     1365   1014    979     63     53    179       C  
ATOM   2988  O   ILE A 368      -0.008  21.110  23.216  1.00 10.03           O  
ANISOU 2988  O   ILE A 368     1500   1115   1194    102     16    225       O  
ATOM   2989  CB  ILE A 368      -0.249  24.309  21.438  1.00  9.37           C  
ANISOU 2989  CB  ILE A 368     1451   1010   1099    127     59    237       C  
ATOM   2990  CG1 ILE A 368      -1.306  24.934  20.512  1.00 10.91           C  
ANISOU 2990  CG1 ILE A 368     1562   1429   1154    163     24    233       C  
ATOM   2991  CG2 ILE A 368       1.042  23.984  20.667  1.00  9.66           C  
ANISOU 2991  CG2 ILE A 368     1592   1185    892     45    107    104       C  
ATOM   2992  CD1 ILE A 368      -1.700  24.082  19.310  1.00 11.36           C  
ANISOU 2992  CD1 ILE A 368     1606   1386   1325    -23   -134    236       C  
ATOM   2993  N   ARG A 369       0.987  23.041  23.788  1.00  9.25           N  
ANISOU 2993  N   ARG A 369     1419   1082   1013    110    -20    196       N  
ATOM   2994  CA  ARG A 369       1.793  22.424  24.842  1.00  9.19           C  
ANISOU 2994  CA  ARG A 369     1403   1101    987    180     82    242       C  
ATOM   2995  C   ARG A 369       1.385  22.928  26.220  1.00  9.22           C  
ANISOU 2995  C   ARG A 369     1359   1096   1049     57     62    220       C  
ATOM   2996  O   ARG A 369       1.328  24.141  26.500  1.00 10.18           O  
ANISOU 2996  O   ARG A 369     1629   1138   1101    181     78    184       O  
ATOM   2997  CB  ARG A 369       3.310  22.687  24.623  1.00  9.62           C  
ANISOU 2997  CB  ARG A 369     1427   1108   1120    207     44    162       C  
ATOM   2998  CG  ARG A 369       3.932  21.875  23.492  1.00  9.61           C  
ANISOU 2998  CG  ARG A 369     1335   1098   1218     82    203    195       C  
ATOM   2999  CD  ARG A 369       3.905  20.392  23.821  1.00  9.34           C  
ANISOU 2999  CD  ARG A 369     1323   1081   1144     63     -9    111       C  
ATOM   3000  NE  ARG A 369       4.867  19.596  23.063  1.00  8.96           N  
ANISOU 3000  NE  ARG A 369     1213   1055   1136    -62     39    146       N  
ATOM   3001  CZ  ARG A 369       4.598  18.868  21.969  1.00  9.53           C  
ANISOU 3001  CZ  ARG A 369     1400   1132   1087   -180    246    175       C  
ATOM   3002  NH1 ARG A 369       3.410  18.838  21.389  1.00 11.32           N  
ANISOU 3002  NH1 ARG A 369     1635   1545   1121   -291      4    279       N  
ATOM   3003  NH2 ARG A 369       5.615  18.161  21.463  1.00  9.70           N  
ANISOU 3003  NH2 ARG A 369     1518   1094   1075   -193    309    230       N  
ATOM   3004  N   THR A 370       1.098  21.961  27.098  1.00  9.55           N  
ANISOU 3004  N   THR A 370     1399   1187   1042     12     27    174       N  
ATOM   3005  CA  THR A 370       1.064  22.141  28.554  1.00  9.35           C  
ANISOU 3005  CA  THR A 370     1370   1217    964     52     83    101       C  
ATOM   3006  C   THR A 370       2.472  21.800  29.083  1.00  9.15           C  
ANISOU 3006  C   THR A 370     1330   1190    959     43    119     94       C  
ATOM   3007  O   THR A 370       2.990  20.702  28.785  1.00 10.20           O  
ANISOU 3007  O   THR A 370     1523   1194   1158     97     42     95       O  
ATOM   3008  CB  THR A 370       0.007  21.263  29.223  1.00 10.03           C  
ANISOU 3008  CB  THR A 370     1391   1296   1125    -20     56     86       C  
ATOM   3009  OG1 THR A 370      -1.298  21.651  28.785  1.00 11.80           O  
ANISOU 3009  OG1 THR A 370     1357   1643   1485    123    181    118       O  
ATOM   3010  CG2 THR A 370       0.054  21.385  30.752  1.00 12.43           C  
ANISOU 3010  CG2 THR A 370     1766   1779   1180    -46    243    139       C  
ATOM   3011  N   ILE A 371       3.053  22.691  29.868  1.00  9.00           N  
ANISOU 3011  N   ILE A 371     1296   1105   1019     56     26    133       N  
ATOM   3012  CA  ILE A 371       4.309  22.470  30.559  1.00  9.21           C  
ANISOU 3012  CA  ILE A 371     1281   1195   1023     46     76    113       C  
ATOM   3013  C   ILE A 371       4.000  22.112  32.013  1.00  9.46           C  
ANISOU 3013  C   ILE A 371     1536   1169    890    108     43    -44       C  
ATOM   3014  O   ILE A 371       3.305  22.884  32.717  1.00 10.68           O  
ANISOU 3014  O   ILE A 371     1624   1305   1129    136    249     24       O  
ATOM   3015  CB  ILE A 371       5.306  23.649  30.484  1.00 10.01           C  
ANISOU 3015  CB  ILE A 371     1311   1264   1229      4     22    216       C  
ATOM   3016  CG1 ILE A 371       5.524  24.078  29.025  1.00 11.77           C  
ANISOU 3016  CG1 ILE A 371     1624   1493   1353    -99     15    364       C  
ATOM   3017  CG2 ILE A 371       6.602  23.322  31.206  1.00  9.96           C  
ANISOU 3017  CG2 ILE A 371     1302   1268   1215    -78    -61     61       C  
ATOM   3018  CD1 ILE A 371       6.013  23.036  28.075  1.00 12.61           C  
ANISOU 3018  CD1 ILE A 371     1742   1810   1239     68    124    385       C  
ATOM   3019  N   LEU A 372       4.496  20.977  32.476  1.00  9.63           N  
ANISOU 3019  N   LEU A 372     1427   1257    974     76    159    148       N  
ATOM   3020  CA  LEU A 372       4.376  20.524  33.871  1.00  9.26           C  
ANISOU 3020  CA  LEU A 372     1270   1208   1042     13    187    168       C  
ATOM   3021  C   LEU A 372       5.645  20.880  34.654  1.00  9.74           C  
ANISOU 3021  C   LEU A 372     1321   1263   1115    101    148     95       C  
ATOM   3022  O   LEU A 372       6.776  20.621  34.220  1.00 10.19           O  
ANISOU 3022  O   LEU A 372     1297   1438   1137      8     44    -35       O  
ATOM   3023  CB  LEU A 372       4.227  19.000  33.916  1.00  9.59           C  
ANISOU 3023  CB  LEU A 372     1284   1289   1072     10     87     93       C  
ATOM   3024  CG  LEU A 372       3.015  18.432  33.148  1.00 10.11           C  
ANISOU 3024  CG  LEU A 372     1321   1331   1190   -112    128    136       C  
ATOM   3025  CD1 LEU A 372       3.036  16.902  33.253  1.00 11.04           C  
ANISOU 3025  CD1 LEU A 372     1423   1357   1413   -166    147    121       C  
ATOM   3026  CD2 LEU A 372       1.702  18.984  33.672  1.00 11.51           C  
ANISOU 3026  CD2 LEU A 372     1326   1708   1340   -112     82     38       C  
ATOM   3027  N   THR A 373       5.449  21.478  35.851  1.00 10.46           N  
ANISOU 3027  N   THR A 373     1444   1445   1086     70     16    -75       N  
ATOM   3028  CA  THR A 373       6.564  21.836  36.742  1.00 10.64           C  
ANISOU 3028  CA  THR A 373     1466   1387   1188    -82     23    -48       C  
ATOM   3029  C   THR A 373       6.581  20.940  37.983  1.00 10.27           C  
ANISOU 3029  C   THR A 373     1355   1343   1205     -4     60    -48       C  
ATOM   3030  O   THR A 373       5.542  20.738  38.651  1.00 11.59           O  
ANISOU 3030  O   THR A 373     1376   1646   1382     15     67     -1       O  
ATOM   3031  CB ATHR A 373       6.547  23.335  37.088  0.69 11.76           C  
ANISOU 3031  CB ATHR A 373     1647   1465   1358   -168     22    -85       C  
ATOM   3032  OG1ATHR A 373       5.201  23.752  37.312  0.69 13.61           O  
ANISOU 3032  OG1ATHR A 373     1806   1672   1694     -2      5   -158       O  
ATOM   3033  CG2ATHR A 373       7.189  24.176  35.988  0.69 12.97           C  
ANISOU 3033  CG2ATHR A 373     1605   1722   1601   -129     43    225       C  
ATOM   3034  CB BTHR A 373       6.314  23.283  37.235  0.31 10.49           C  
ANISOU 3034  CB BTHR A 373     1335   1326   1327     26   -104     41       C  
ATOM   3035  OG1BTHR A 373       6.392  24.179  36.121  0.31 11.35           O  
ANISOU 3035  OG1BTHR A 373     1328   1350   1633    172     -2    267       O  
ATOM   3036  CG2BTHR A 373       7.322  23.667  38.306  0.31 11.09           C  
ANISOU 3036  CG2BTHR A 373     1550   1223   1440     24   -276     53       C  
ATOM   3037  N   PHE A 374       7.768  20.435  38.327  1.00 10.56           N  
ANISOU 3037  N   PHE A 374     1477   1382   1152     75     77     62       N  
ATOM   3038  CA  PHE A 374       7.982  19.579  39.484  1.00 10.82           C  
ANISOU 3038  CA  PHE A 374     1562   1328   1221    102     57    121       C  
ATOM   3039  C   PHE A 374       8.133  20.374  40.780  1.00 11.19           C  
ANISOU 3039  C   PHE A 374     1564   1452   1235    139     30    109       C  
ATOM   3040  O   PHE A 374       8.449  21.584  40.742  1.00 13.30           O  
ANISOU 3040  O   PHE A 374     2115   1641   1296    -39    210    -54       O  
ATOM   3041  CB  PHE A 374       9.211  18.679  39.250  1.00 11.63           C  
ANISOU 3041  CB  PHE A 374     1501   1585   1331     80    -80      1       C  
ATOM   3042  CG  PHE A 374       8.969  17.672  38.165  1.00 11.06           C  
ANISOU 3042  CG  PHE A 374     1540   1357   1304    103    -61    108       C  
ATOM   3043  CD1 PHE A 374       8.399  16.444  38.454  1.00 11.38           C  
ANISOU 3043  CD1 PHE A 374     1546   1279   1499    179   -172    134       C  
ATOM   3044  CD2 PHE A 374       9.303  17.930  36.832  1.00 11.55           C  
ANISOU 3044  CD2 PHE A 374     1605   1409   1375     55      3     22       C  
ATOM   3045  CE1 PHE A 374       8.182  15.515  37.453  1.00 12.15           C  
ANISOU 3045  CE1 PHE A 374     1612   1361   1645    170   -145     64       C  
ATOM   3046  CE2 PHE A 374       9.048  17.014  35.823  1.00 12.70           C  
ANISOU 3046  CE2 PHE A 374     1763   1494   1569     58    -99    -42       C  
ATOM   3047  CZ  PHE A 374       8.500  15.798  36.135  1.00 12.55           C  
ANISOU 3047  CZ  PHE A 374     1638   1524   1607    125   -216    -91       C  
ATOM   3048  OXT PHE A 374       8.007  19.738  41.867  1.00 14.16           O  
ANISOU 3048  OXT PHE A 374     2168   1857   1356    210     96    202       O  
TER    3049      PHE A 374                                                      
ATOM   3050  N   SER B   1      11.398  13.653 -54.595  1.00 57.15           N  
ANISOU 3050  N   SER B   1     7297   7873   6543    -91     12    155       N  
ATOM   3051  CA  SER B   1      10.984  14.696 -53.620  1.00 56.38           C  
ANISOU 3051  CA  SER B   1     7126   7864   6430   -282     25    112       C  
ATOM   3052  C   SER B   1       9.854  14.222 -52.716  1.00 50.19           C  
ANISOU 3052  C   SER B   1     6843   6825   5402    112   -211    -46       C  
ATOM   3053  O   SER B   1       8.805  13.816 -53.214  1.00 46.54           O  
ANISOU 3053  O   SER B   1     6687   6604   4392    146    183     30       O  
ATOM   3054  CB  SER B   1      10.511  15.972 -54.330  1.00 59.20           C  
ANISOU 3054  CB  SER B   1     7689   7900   6904   -335   -194    206       C  
ATOM   3055  OG  SER B   1       9.529  16.639 -53.544  1.00 60.68           O  
ANISOU 3055  OG  SER B   1     7663   8095   7297   -258   -141    216       O  
ATOM   3056  N   THR B   2      10.060  14.298 -51.394  1.00 40.89           N  
ANISOU 3056  N   THR B   2     5064   5569   4904   -116    425    149       N  
ATOM   3057  CA  THR B   2       8.975  13.891 -50.488  1.00 31.61           C  
ANISOU 3057  CA  THR B   2     4358   4345   3309     74   -289    -84       C  
ATOM   3058  C   THR B   2       8.433  15.089 -49.720  1.00 26.81           C  
ANISOU 3058  C   THR B   2     3624   4234   2329   -255   -266    159       C  
ATOM   3059  O   THR B   2       7.307  15.038 -49.213  1.00 23.71           O  
ANISOU 3059  O   THR B   2     3513   3963   1532     21   -433    419       O  
ATOM   3060  CB  THR B   2       9.399  12.772 -49.521  1.00 27.13           C  
ANISOU 3060  CB  THR B   2     3676   4116   2517   -160     61   -332       C  
ATOM   3061  OG1 THR B   2      10.600  13.139 -48.841  1.00 24.26           O  
ANISOU 3061  OG1 THR B   2     3448   4060   1708   -146    396   -236       O  
ATOM   3062  CG2 THR B   2       9.640  11.458 -50.265  1.00 26.95           C  
ANISOU 3062  CG2 THR B   2     3713   3969   2560     -8    134   -204       C  
ATOM   3063  N   ALA B   3       9.185  16.175 -49.636  1.00 24.88           N  
ANISOU 3063  N   ALA B   3     3875   3883   1694   -169     21    414       N  
ATOM   3064  CA  ALA B   3       8.761  17.341 -48.870  1.00 25.82           C  
ANISOU 3064  CA  ALA B   3     3709   3693   2407   -232    -33    260       C  
ATOM   3065  C   ALA B   3       7.407  17.877 -49.274  1.00 25.64           C  
ANISOU 3065  C   ALA B   3     3778   3640   2325   -127    -54    224       C  
ATOM   3066  O   ALA B   3       7.122  18.044 -50.488  1.00 27.82           O  
ANISOU 3066  O   ALA B   3     4484   3842   2244   -100   -194    398       O  
ATOM   3067  CB  ALA B   3       9.832  18.431 -48.886  1.00 26.06           C  
ANISOU 3067  CB  ALA B   3     3788   3748   2367   -320     18    122       C  
ATOM   3068  N   GLY B   4       6.483  18.080 -48.354  1.00 25.05           N  
ANISOU 3068  N   GLY B   4     3754   3537   2228     63   -160    173       N  
ATOM   3069  CA  GLY B   4       5.150  18.592 -48.559  1.00 24.59           C  
ANISOU 3069  CA  GLY B   4     3745   3308   2290      8   -191    282       C  
ATOM   3070  C   GLY B   4       4.131  17.578 -49.037  1.00 23.70           C  
ANISOU 3070  C   GLY B   4     3459   3274   2270    108   -157    334       C  
ATOM   3071  O   GLY B   4       2.939  17.853 -49.208  1.00 25.73           O  
ANISOU 3071  O   GLY B   4     3611   3515   2652    203   -368    437       O  
ATOM   3072  N   LYS B   5       4.572  16.340 -49.206  1.00 21.67           N  
ANISOU 3072  N   LYS B   5     3282   3192   1761     86   -388    289       N  
ATOM   3073  CA  LYS B   5       3.747  15.252 -49.690  1.00 22.80           C  
ANISOU 3073  CA  LYS B   5     3349   3384   1931     -2   -398    162       C  
ATOM   3074  C   LYS B   5       3.535  14.177 -48.646  1.00 21.35           C  
ANISOU 3074  C   LYS B   5     2983   3291   1838     -6   -466     96       C  
ATOM   3075  O   LYS B   5       4.382  13.985 -47.726  1.00 21.53           O  
ANISOU 3075  O   LYS B   5     3078   3424   1677     33   -518    178       O  
ATOM   3076  CB  LYS B   5       4.469  14.571 -50.888  1.00 26.39           C  
ANISOU 3076  CB  LYS B   5     3865   3973   2188    125   -282    -81       C  
ATOM   3077  CG  LYS B   5       4.723  15.551 -52.033  1.00 30.50           C  
ANISOU 3077  CG  LYS B   5     4370   4233   2986    -65   -317    343       C  
ATOM   3078  CD  LYS B   5       5.417  14.888 -53.208  1.00 34.46           C  
ANISOU 3078  CD  LYS B   5     4578   4839   3678     19   -171   -178       C  
ATOM   3079  CE  LYS B   5       5.667  15.895 -54.331  1.00 38.18           C  
ANISOU 3079  CE  LYS B   5     5086   5082   4338   -164   -135    141       C  
ATOM   3080  NZ  LYS B   5       6.551  15.292 -55.374  1.00 40.29           N  
ANISOU 3080  NZ  LYS B   5     5251   5376   4679   -174     67     21       N  
ATOM   3081  N   VAL B   6       2.464  13.438 -48.757  1.00 20.27           N  
ANISOU 3081  N   VAL B   6     2899   3300   1503     25   -283     96       N  
ATOM   3082  CA  VAL B   6       2.214  12.249 -47.961  1.00 19.22           C  
ANISOU 3082  CA  VAL B   6     2628   3128   1549      6   -153   -105       C  
ATOM   3083  C   VAL B   6       3.273  11.224 -48.339  1.00 18.54           C  
ANISOU 3083  C   VAL B   6     2662   2973   1411     -9   -366   -233       C  
ATOM   3084  O   VAL B   6       3.585  11.042 -49.554  1.00 21.70           O  
ANISOU 3084  O   VAL B   6     3253   3530   1462     69   -177   -194       O  
ATOM   3085  CB  VAL B   6       0.788  11.714 -48.188  1.00 20.77           C  
ANISOU 3085  CB  VAL B   6     2620   3414   1857     31   -287   -142       C  
ATOM   3086  CG1 VAL B   6       0.596  10.341 -47.570  1.00 22.41           C  
ANISOU 3086  CG1 VAL B   6     2833   3515   2168     21   -318    -35       C  
ATOM   3087  CG2 VAL B   6      -0.259  12.694 -47.674  1.00 23.30           C  
ANISOU 3087  CG2 VAL B   6     2792   3804   2255    213   -351   -348       C  
ATOM   3088  N   ILE B   7       3.892  10.544 -47.393  1.00 18.09           N  
ANISOU 3088  N   ILE B   7     2517   2782   1574    134   -123    -63       N  
ATOM   3089  CA  ILE B   7       4.809   9.441 -47.600  1.00 16.19           C  
ANISOU 3089  CA  ILE B   7     2194   2794   1165     13   -155   -105       C  
ATOM   3090  C   ILE B   7       4.155   8.085 -47.315  1.00 17.13           C  
ANISOU 3090  C   ILE B   7     2362   2797   1350    -54    -48   -380       C  
ATOM   3091  O   ILE B   7       3.529   7.926 -46.253  1.00 19.40           O  
ANISOU 3091  O   ILE B   7     2719   3152   1500    -42    225   -551       O  
ATOM   3092  CB  ILE B   7       6.085   9.591 -46.736  1.00 16.62           C  
ANISOU 3092  CB  ILE B   7     2179   2626   1508    -25   -201   -215       C  
ATOM   3093  CG1 ILE B   7       7.017  10.707 -47.244  1.00 16.94           C  
ANISOU 3093  CG1 ILE B   7     2283   2882   1270     -8    -23   -127       C  
ATOM   3094  CG2 ILE B   7       6.897   8.292 -46.666  1.00 18.15           C  
ANISOU 3094  CG2 ILE B   7     2390   2702   1805     45   -287   -182       C  
ATOM   3095  CD1 ILE B   7       8.246  10.931 -46.364  1.00 18.50           C  
ANISOU 3095  CD1 ILE B   7     2442   3084   1502    -46   -108   -306       C  
ATOM   3096  N   LYS B   8       4.305   7.116 -48.225  1.00 17.16           N  
ANISOU 3096  N   LYS B   8     2250   2802   1469    -13    -80   -480       N  
ATOM   3097  CA  LYS B   8       3.908   5.750 -47.953  1.00 16.71           C  
ANISOU 3097  CA  LYS B   8     2166   2637   1547    123    -95   -625       C  
ATOM   3098  C   LYS B   8       5.173   4.992 -47.597  1.00 16.90           C  
ANISOU 3098  C   LYS B   8     2189   2834   1397    214     -5   -593       C  
ATOM   3099  O   LYS B   8       6.163   5.059 -48.365  1.00 19.17           O  
ANISOU 3099  O   LYS B   8     2278   3503   1501    335     70   -486       O  
ATOM   3100  CB ALYS B   8       3.201   5.045 -49.132  0.71 19.53           C  
ANISOU 3100  CB ALYS B   8     2781   2880   1759     72   -339   -724       C  
ATOM   3101  CG ALYS B   8       1.719   5.381 -49.199  0.71 22.77           C  
ANISOU 3101  CG ALYS B   8     2899   3287   2468    275    -16   -432       C  
ATOM   3102  CD ALYS B   8       1.013   4.686 -50.371  0.71 25.67           C  
ANISOU 3102  CD ALYS B   8     3471   3549   2735    115   -210   -460       C  
ATOM   3103  CE ALYS B   8      -0.467   4.524 -50.029  0.71 30.17           C  
ANISOU 3103  CE ALYS B   8     3713   4172   3578    175    218   -283       C  
ATOM   3104  NZ ALYS B   8      -1.263   3.956 -51.153  0.71 32.86           N  
ANISOU 3104  NZ ALYS B   8     4127   4656   3703     44      8   -214       N  
ATOM   3105  CB BLYS B   8       3.169   5.138 -49.152  0.29 16.86           C  
ANISOU 3105  CB BLYS B   8     2238   2545   1622    148   -246   -458       C  
ATOM   3106  CG BLYS B   8       1.910   5.914 -49.527  0.29 17.44           C  
ANISOU 3106  CG BLYS B   8     2276   2546   1803    191   -148   -228       C  
ATOM   3107  CD BLYS B   8       1.116   5.225 -50.631  0.29 18.21           C  
ANISOU 3107  CD BLYS B   8     2477   2545   1895    193   -305   -121       C  
ATOM   3108  CE BLYS B   8      -0.277   5.841 -50.767  0.29 19.78           C  
ANISOU 3108  CE BLYS B   8     2549   2775   2189    280   -157    -15       C  
ATOM   3109  NZ BLYS B   8      -1.078   5.147 -51.814  0.29 20.23           N  
ANISOU 3109  NZ BLYS B   8     2594   2762   2329    259   -303    102       N  
ATOM   3110  N   CYS B   9       5.204   4.309 -46.454  1.00 16.36           N  
ANISOU 3110  N   CYS B   9     1775   3041   1399    154   -162   -483       N  
ATOM   3111  CA  CYS B   9       6.395   3.587 -46.007  1.00 16.36           C  
ANISOU 3111  CA  CYS B   9     2040   2729   1448    275    -29   -548       C  
ATOM   3112  C   CYS B   9       6.001   2.455 -45.097  1.00 15.97           C  
ANISOU 3112  C   CYS B   9     1992   2615   1462     48   -213   -656       C  
ATOM   3113  O   CYS B   9       4.822   2.294 -44.724  1.00 16.76           O  
ANISOU 3113  O   CYS B   9     1893   2649   1828     67   -129   -730       O  
ATOM   3114  CB  CYS B   9       7.370   4.536 -45.277  1.00 15.83           C  
ANISOU 3114  CB  CYS B   9     1873   2670   1471    192    134   -452       C  
ATOM   3115  SG  CYS B   9       6.723   5.165 -43.676  1.00 15.48           S  
ANISOU 3115  SG  CYS B   9     1780   2753   1350     44    -25   -607       S  
ATOM   3116  N   LYS B  10       6.958   1.620 -44.667  1.00 16.60           N  
ANISOU 3116  N   LYS B  10     2163   2654   1490    158   -213   -679       N  
ATOM   3117  CA  LYS B  10       6.679   0.495 -43.786  1.00 17.62           C  
ANISOU 3117  CA  LYS B  10     2267   2640   1787    220   -261   -518       C  
ATOM   3118  C   LYS B  10       6.772   0.905 -42.301  1.00 16.37           C  
ANISOU 3118  C   LYS B  10     2144   2348   1729     -5    -53   -524       C  
ATOM   3119  O   LYS B  10       7.598   1.782 -41.937  1.00 16.63           O  
ANISOU 3119  O   LYS B  10     2076   2589   1655    -56     92   -575       O  
ATOM   3120  CB ALYS B  10       7.188  -0.795 -44.438  0.67 22.29           C  
ANISOU 3120  CB ALYS B  10     2968   2730   2773    191     -8   -502       C  
ATOM   3121  CG ALYS B  10       6.838  -0.914 -45.910  0.67 22.83           C  
ANISOU 3121  CG ALYS B  10     3023   2933   2719    282   -260   -132       C  
ATOM   3122  CD ALYS B  10       5.854  -0.432 -47.000  0.67 12.95           C  
ANISOU 3122  CD ALYS B  10     2288   1740    892   -121    407   -641       C  
ATOM   3123  CE ALYS B  10       4.764  -1.457 -47.186  0.67 19.89           C  
ANISOU 3123  CE ALYS B  10     2731   1989   2838   -205    186   -145       C  
ATOM   3124  NZ ALYS B  10       4.901  -2.901 -47.010  0.67  9.97           N  
ANISOU 3124  NZ ALYS B  10     1191   1563   1035   -111    310   -357       N  
ATOM   3125  CB BLYS B  10       7.978  -0.331 -43.990  0.33 13.50           C  
ANISOU 3125  CB BLYS B  10     2194   2057    878     93   -228   -655       C  
ATOM   3126  CG BLYS B  10       7.934  -1.764 -43.646  0.33 11.90           C  
ANISOU 3126  CG BLYS B  10     1483   2212    825    191     52   -196       C  
ATOM   3127  CD BLYS B  10       9.328  -2.327 -43.983  0.33  9.03           C  
ANISOU 3127  CD BLYS B  10     1647   1411    374    585    132    144       C  
ATOM   3128  CE BLYS B  10       9.633  -2.319 -45.508  0.33  8.52           C  
ANISOU 3128  CE BLYS B  10     1438   1310    489    471    385    431       C  
ATOM   3129  NZ BLYS B  10      10.570  -3.471 -45.768  0.33  7.71           N  
ANISOU 3129  NZ BLYS B  10     1394   1104    431    356    203    171       N  
ATOM   3130  N   ALA B  11       5.930   0.356 -41.458  1.00 15.94           N  
ANISOU 3130  N   ALA B  11     2044   2386   1628   -122   -255   -461       N  
ATOM   3131  CA  ALA B  11       5.947   0.576 -40.009  1.00 15.44           C  
ANISOU 3131  CA  ALA B  11     1792   2367   1707     18   -205   -507       C  
ATOM   3132  C   ALA B  11       5.514  -0.712 -39.316  1.00 16.01           C  
ANISOU 3132  C   ALA B  11     1917   2353   1813     -3   -198   -538       C  
ATOM   3133  O   ALA B  11       4.903  -1.604 -39.941  1.00 18.18           O  
ANISOU 3133  O   ALA B  11     2322   2511   2074   -336   -358   -492       O  
ATOM   3134  CB  ALA B  11       5.071   1.757 -39.573  1.00 15.90           C  
ANISOU 3134  CB  ALA B  11     1838   2471   1733    122   -260   -505       C  
ATOM   3135  N   ALA B  12       5.765  -0.812 -38.003  1.00 14.91           N  
ANISOU 3135  N   ALA B  12     1565   2437   1662   -163     83   -487       N  
ATOM   3136  CA  ALA B  12       5.328  -1.935 -37.185  1.00 15.54           C  
ANISOU 3136  CA  ALA B  12     1739   2429   1739   -195     60   -453       C  
ATOM   3137  C   ALA B  12       4.106  -1.468 -36.399  1.00 15.52           C  
ANISOU 3137  C   ALA B  12     1701   2465   1731   -263     54   -567       C  
ATOM   3138  O   ALA B  12       4.227  -0.681 -35.442  1.00 17.90           O  
ANISOU 3138  O   ALA B  12     1930   2855   2018   -325    160   -939       O  
ATOM   3139  CB  ALA B  12       6.442  -2.386 -36.245  1.00 17.25           C  
ANISOU 3139  CB  ALA B  12     1893   2647   2013   -129    -32   -163       C  
ATOM   3140  N   VAL B  13       2.914  -1.857 -36.857  1.00 15.98           N  
ANISOU 3140  N   VAL B  13     1664   2553   1853   -271     58   -603       N  
ATOM   3141  CA  VAL B  13       1.651  -1.452 -36.233  1.00 15.53           C  
ANISOU 3141  CA  VAL B  13     1608   2435   1856   -218    -15   -462       C  
ATOM   3142  C   VAL B  13       1.221  -2.485 -35.209  1.00 15.56           C  
ANISOU 3142  C   VAL B  13     1756   2330   1827   -217     35   -515       C  
ATOM   3143  O   VAL B  13       1.313  -3.689 -35.451  1.00 17.32           O  
ANISOU 3143  O   VAL B  13     2182   2376   2024   -375    342   -688       O  
ATOM   3144  CB  VAL B  13       0.553  -1.276 -37.309  1.00 16.88           C  
ANISOU 3144  CB  VAL B  13     1850   2672   1890    -98   -132   -436       C  
ATOM   3145  CG1 VAL B  13      -0.794  -0.910 -36.688  1.00 18.96           C  
ANISOU 3145  CG1 VAL B  13     1998   2828   2379     61    -90   -590       C  
ATOM   3146  CG2 VAL B  13       0.955  -0.238 -38.351  1.00 18.87           C  
ANISOU 3146  CG2 VAL B  13     2054   3033   2081   -272   -120   -278       C  
ATOM   3147  N   LEU B  14       0.818  -2.043 -34.001  1.00 15.69           N  
ANISOU 3147  N   LEU B  14     1799   2400   1764   -255      4   -553       N  
ATOM   3148  CA  LEU B  14       0.241  -2.896 -32.970  1.00 16.14           C  
ANISOU 3148  CA  LEU B  14     1910   2384   1839   -121    -65   -461       C  
ATOM   3149  C   LEU B  14      -1.268  -2.628 -32.926  1.00 15.98           C  
ANISOU 3149  C   LEU B  14     1864   2334   1874   -242     50   -351       C  
ATOM   3150  O   LEU B  14      -1.740  -1.557 -32.537  1.00 16.08           O  
ANISOU 3150  O   LEU B  14     1545   2485   2081   -248     15   -448       O  
ATOM   3151  CB  LEU B  14       0.857  -2.624 -31.593  1.00 15.40           C  
ANISOU 3151  CB  LEU B  14     1784   2306   1760   -130     41   -516       C  
ATOM   3152  CG  LEU B  14       0.381  -3.593 -30.509  1.00 16.54           C  
ANISOU 3152  CG  LEU B  14     1958   2539   1789   -122    -63   -374       C  
ATOM   3153  CD1 LEU B  14       0.929  -5.002 -30.698  1.00 18.00           C  
ANISOU 3153  CD1 LEU B  14     2125   2595   2119    -73   -112   -435       C  
ATOM   3154  CD2 LEU B  14       0.748  -3.072 -29.118  1.00 18.37           C  
ANISOU 3154  CD2 LEU B  14     2431   2700   1848     17    -59   -445       C  
ATOM   3155  N   TRP B  15      -2.026  -3.590 -33.487  1.00 17.13           N  
ANISOU 3155  N   TRP B  15     1641   2726   2144   -237   -134   -401       N  
ATOM   3156  CA  TRP B  15      -3.475  -3.426 -33.608  1.00 17.58           C  
ANISOU 3156  CA  TRP B  15     1684   2744   2251   -306   -105   -371       C  
ATOM   3157  C   TRP B  15      -4.228  -3.716 -32.321  1.00 17.92           C  
ANISOU 3157  C   TRP B  15     1976   2562   2272   -138    -48   -156       C  
ATOM   3158  O   TRP B  15      -5.331  -3.164 -32.113  1.00 20.32           O  
ANISOU 3158  O   TRP B  15     1987   2978   2755   -129    -28   -150       O  
ATOM   3159  CB  TRP B  15      -4.021  -4.324 -34.742  1.00 18.93           C  
ANISOU 3159  CB  TRP B  15     1998   2918   2278   -270   -130   -534       C  
ATOM   3160  CG  TRP B  15      -3.617  -3.883 -36.113  1.00 18.87           C  
ANISOU 3160  CG  TRP B  15     2077   2780   2315   -313   -215   -465       C  
ATOM   3161  CD1 TRP B  15      -2.618  -4.433 -36.894  1.00 19.90           C  
ANISOU 3161  CD1 TRP B  15     2047   3224   2289   -262   -196   -407       C  
ATOM   3162  CD2 TRP B  15      -4.203  -2.862 -36.909  1.00 18.27           C  
ANISOU 3162  CD2 TRP B  15     2039   2705   2196   -344   -216   -483       C  
ATOM   3163  NE1 TRP B  15      -2.569  -3.792 -38.118  1.00 19.70           N  
ANISOU 3163  NE1 TRP B  15     2115   2943   2428   -425   -177   -413       N  
ATOM   3164  CE2 TRP B  15      -3.509  -2.810 -38.148  1.00 18.88           C  
ANISOU 3164  CE2 TRP B  15     2112   2876   2186   -383   -252   -456       C  
ATOM   3165  CE3 TRP B  15      -5.224  -1.917 -36.697  1.00 18.90           C  
ANISOU 3165  CE3 TRP B  15     2279   2724   2179   -205   -346   -526       C  
ATOM   3166  CZ2 TRP B  15      -3.848  -1.923 -39.156  1.00 19.75           C  
ANISOU 3166  CZ2 TRP B  15     2186   2883   2437   -408   -277   -361       C  
ATOM   3167  CZ3 TRP B  15      -5.560  -1.029 -37.709  1.00 19.46           C  
ANISOU 3167  CZ3 TRP B  15     2209   2911   2276   -263   -303   -392       C  
ATOM   3168  CH2 TRP B  15      -4.854  -1.029 -38.925  1.00 19.70           C  
ANISOU 3168  CH2 TRP B  15     2371   2963   2151   -263   -415   -368       C  
ATOM   3169  N   GLU B  16      -3.733  -4.609 -31.480  1.00 18.44           N  
ANISOU 3169  N   GLU B  16     2037   2667   2301   -142    -70   -108       N  
ATOM   3170  CA  GLU B  16      -4.369  -4.982 -30.216  1.00 20.77           C  
ANISOU 3170  CA  GLU B  16     2443   3016   2432      3     60     52       C  
ATOM   3171  C   GLU B  16      -3.316  -5.556 -29.263  1.00 19.06           C  
ANISOU 3171  C   GLU B  16     2266   2526   2451   -161     89     74       C  
ATOM   3172  O   GLU B  16      -2.222  -5.947 -29.698  1.00 18.09           O  
ANISOU 3172  O   GLU B  16     2189   2490   2194   -301    -47    -80       O  
ATOM   3173  CB AGLU B  16      -5.583  -5.887 -30.351  0.77 25.11           C  
ANISOU 3173  CB AGLU B  16     2792   3458   3291   -236   -120     65       C  
ATOM   3174  CG AGLU B  16      -5.312  -7.263 -30.864  0.77 27.47           C  
ANISOU 3174  CG AGLU B  16     3278   3665   3494    -30   -150   -153       C  
ATOM   3175  CD AGLU B  16      -6.574  -8.110 -31.034  0.77 28.72           C  
ANISOU 3175  CD AGLU B  16     3358   3724   3830   -131    -88   -108       C  
ATOM   3176  OE1AGLU B  16      -7.096  -8.649 -30.049  0.77 28.16           O  
ANISOU 3176  OE1AGLU B  16     3228   3625   3846   -372   -311   -147       O  
ATOM   3177  OE2AGLU B  16      -7.041  -8.215 -32.184  0.77 29.96           O  
ANISOU 3177  OE2AGLU B  16     3701   3720   3964   -211   -233   -155       O  
ATOM   3178  CB BGLU B  16      -5.467  -6.020 -30.479  0.22 24.23           C  
ANISOU 3178  CB BGLU B  16     2820   3302   3086   -204    -87    180       C  
ATOM   3179  CG BGLU B  16      -5.208  -7.038 -31.566  0.22 27.71           C  
ANISOU 3179  CG BGLU B  16     3601   3663   3266     92     41     79       C  
ATOM   3180  CD BGLU B  16      -6.351  -7.993 -31.837  0.22 30.21           C  
ANISOU 3180  CD BGLU B  16     3865   3978   3635   -105   -107     90       C  
ATOM   3181  OE1BGLU B  16      -7.505  -7.710 -31.450  0.22 30.25           O  
ANISOU 3181  OE1BGLU B  16     3963   3884   3645   -104     -4     88       O  
ATOM   3182  OE2BGLU B  16      -6.111  -9.055 -32.451  0.22 31.00           O  
ANISOU 3182  OE2BGLU B  16     3928   4055   3795    -55    -27     29       O  
ATOM   3183  N   GLU B  17      -3.622  -5.575 -27.963  1.00 17.85           N  
ANISOU 3183  N   GLU B  17     1954   2439   2392     44     33   -192       N  
ATOM   3184  CA  GLU B  17      -2.661  -6.099 -26.997  1.00 17.83           C  
ANISOU 3184  CA  GLU B  17     2025   2462   2287     51     84   -267       C  
ATOM   3185  C   GLU B  17      -2.389  -7.578 -27.266  1.00 17.14           C  
ANISOU 3185  C   GLU B  17     2126   2348   2040   -183    -99   -272       C  
ATOM   3186  O   GLU B  17      -3.228  -8.303 -27.808  1.00 17.12           O  
ANISOU 3186  O   GLU B  17     1993   2496   2016   -351     87   -240       O  
ATOM   3187  CB AGLU B  17      -3.129  -5.940 -25.539  0.54 18.95           C  
ANISOU 3187  CB AGLU B  17     2293   2573   2333     19    215   -391       C  
ATOM   3188  CG AGLU B  17      -4.317  -6.770 -25.104  0.54 20.12           C  
ANISOU 3188  CG AGLU B  17     2334   2855   2456    -73    240   -338       C  
ATOM   3189  CD AGLU B  17      -4.509  -6.984 -23.615  0.54 23.02           C  
ANISOU 3189  CD AGLU B  17     2949   3282   2514    -36    271   -270       C  
ATOM   3190  OE1AGLU B  17      -3.902  -6.273 -22.771  0.54 22.93           O  
ANISOU 3190  OE1AGLU B  17     2902   3553   2258     71    329   -306       O  
ATOM   3191  OE2AGLU B  17      -5.278  -7.905 -23.218  0.54 24.35           O  
ANISOU 3191  OE2AGLU B  17     3091   3495   2668   -159    346   -322       O  
ATOM   3192  CB BGLU B  17      -3.142  -5.929 -25.555  0.46 20.86           C  
ANISOU 3192  CB BGLU B  17     2449   3085   2390    -44    200   -234       C  
ATOM   3193  CG BGLU B  17      -3.367  -4.521 -25.055  0.46 23.92           C  
ANISOU 3193  CG BGLU B  17     2851   3119   3118    -37     22   -301       C  
ATOM   3194  CD BGLU B  17      -3.894  -4.456 -23.632  0.46 26.51           C  
ANISOU 3194  CD BGLU B  17     3243   3587   3244    -42    191   -213       C  
ATOM   3195  OE1BGLU B  17      -4.364  -5.494 -23.125  0.46 27.37           O  
ANISOU 3195  OE1BGLU B  17     3490   3568   3342     -5    333   -191       O  
ATOM   3196  OE2BGLU B  17      -3.860  -3.380 -22.989  0.46 25.55           O  
ANISOU 3196  OE2BGLU B  17     2835   3614   3259    -26    294   -294       O  
ATOM   3197  N   LYS B  18      -1.234  -8.060 -26.814  1.00 17.46           N  
ANISOU 3197  N   LYS B  18     2125   2509   1999    -97     12   -311       N  
ATOM   3198  CA  LYS B  18      -0.888  -9.466 -26.794  1.00 18.07           C  
ANISOU 3198  CA  LYS B  18     2323   2598   1945     17    -22   -307       C  
ATOM   3199  C   LYS B  18      -0.889 -10.081 -28.199  1.00 16.77           C  
ANISOU 3199  C   LYS B  18     2258   2307   1807   -239   -122   -185       C  
ATOM   3200  O   LYS B  18      -1.269 -11.256 -28.343  1.00 19.31           O  
ANISOU 3200  O   LYS B  18     3020   2351   1966   -271    100   -250       O  
ATOM   3201  CB  LYS B  18      -1.807 -10.195 -25.794  1.00 20.25           C  
ANISOU 3201  CB  LYS B  18     2594   2741   2361   -112     99   -250       C  
ATOM   3202  CG  LYS B  18      -1.593  -9.777 -24.333  1.00 25.38           C  
ANISOU 3202  CG  LYS B  18     3284   3732   2628    -65    -57   -534       C  
ATOM   3203  CD  LYS B  18      -2.459 -10.540 -23.336  1.00 31.28           C  
ANISOU 3203  CD  LYS B  18     3884   4385   3616    -73    243     65       C  
ATOM   3204  CE  LYS B  18      -2.231  -9.994 -21.916  1.00 36.44           C  
ANISOU 3204  CE  LYS B  18     4562   5287   3995    108     47   -334       C  
ATOM   3205  NZ  LYS B  18      -2.906 -10.874 -20.912  1.00 39.54           N  
ANISOU 3205  NZ  LYS B  18     5091   5379   4555    -69    103   -116       N  
ATOM   3206  N   LYS B  19      -0.480  -9.364 -29.233  1.00 16.52           N  
ANISOU 3206  N   LYS B  19     2056   2324   1898   -317    146   -321       N  
ATOM   3207  CA  LYS B  19      -0.295  -9.841 -30.595  1.00 16.00           C  
ANISOU 3207  CA  LYS B  19     1989   2283   1808   -268    144   -246       C  
ATOM   3208  C   LYS B  19       1.066  -9.386 -31.119  1.00 17.03           C  
ANISOU 3208  C   LYS B  19     2041   2362   2066   -425    189   -459       C  
ATOM   3209  O   LYS B  19       1.600  -8.373 -30.641  1.00 17.75           O  
ANISOU 3209  O   LYS B  19     2115   2393   2235   -407    172   -668       O  
ATOM   3210  CB  LYS B  19      -1.344  -9.208 -31.535  1.00 16.23           C  
ANISOU 3210  CB  LYS B  19     2088   2060   2020   -296    127    -76       C  
ATOM   3211  CG  LYS B  19      -2.785  -9.600 -31.238  1.00 16.54           C  
ANISOU 3211  CG  LYS B  19     2070   2106   2108   -128    259   -177       C  
ATOM   3212  CD  LYS B  19      -3.063 -11.083 -31.457  1.00 19.29           C  
ANISOU 3212  CD  LYS B  19     2462   2257   2612   -321    337   -113       C  
ATOM   3213  CE  LYS B  19      -4.569 -11.324 -31.223  1.00 22.15           C  
ANISOU 3213  CE  LYS B  19     2459   2989   2969    -80    312   -124       C  
ATOM   3214  NZ  LYS B  19      -4.907 -12.752 -31.405  1.00 23.81           N  
ANISOU 3214  NZ  LYS B  19     2737   3173   3138   -339    311   -274       N  
ATOM   3215  N   PRO B  20       1.625 -10.070 -32.109  1.00 18.33           N  
ANISOU 3215  N   PRO B  20     2133   2629   2200   -529    219   -660       N  
ATOM   3216  CA  PRO B  20       2.854  -9.625 -32.755  1.00 17.12           C  
ANISOU 3216  CA  PRO B  20     2005   2524   1977   -354    181   -501       C  
ATOM   3217  C   PRO B  20       2.616  -8.298 -33.447  1.00 17.14           C  
ANISOU 3217  C   PRO B  20     2036   2545   1933   -276    223   -561       C  
ATOM   3218  O   PRO B  20       1.494  -7.933 -33.795  1.00 18.25           O  
ANISOU 3218  O   PRO B  20     2063   2541   2331   -397    139   -563       O  
ATOM   3219  CB  PRO B  20       3.141 -10.689 -33.858  1.00 18.14           C  
ANISOU 3219  CB  PRO B  20     1975   2588   2330   -382    241   -694       C  
ATOM   3220  CG  PRO B  20       2.383 -11.890 -33.338  1.00 19.87           C  
ANISOU 3220  CG  PRO B  20     2313   2515   2721   -454    295   -720       C  
ATOM   3221  CD  PRO B  20       1.106 -11.311 -32.703  1.00 18.94           C  
ANISOU 3221  CD  PRO B  20     2329   2319   2549   -461    378   -611       C  
ATOM   3222  N   PHE B  21       3.687  -7.499 -33.689  1.00 16.94           N  
ANISOU 3222  N   PHE B  21     1976   2515   1946   -321     54   -586       N  
ATOM   3223  CA  PHE B  21       3.601  -6.292 -34.492  1.00 17.49           C  
ANISOU 3223  CA  PHE B  21     1973   2458   2213   -319     33   -534       C  
ATOM   3224  C   PHE B  21       3.302  -6.720 -35.946  1.00 17.03           C  
ANISOU 3224  C   PHE B  21     1975   2307   2189   -281    116   -573       C  
ATOM   3225  O   PHE B  21       3.859  -7.736 -36.429  1.00 18.70           O  
ANISOU 3225  O   PHE B  21     2200   2601   2305    -90    124   -592       O  
ATOM   3226  CB  PHE B  21       4.939  -5.553 -34.443  1.00 17.73           C  
ANISOU 3226  CB  PHE B  21     2063   2442   2230   -385    212   -480       C  
ATOM   3227  CG  PHE B  21       5.264  -4.959 -33.085  1.00 15.74           C  
ANISOU 3227  CG  PHE B  21     1694   2036   2250   -451    165   -386       C  
ATOM   3228  CD1 PHE B  21       4.713  -3.740 -32.716  1.00 16.39           C  
ANISOU 3228  CD1 PHE B  21     1967   2172   2087   -355    107   -500       C  
ATOM   3229  CD2 PHE B  21       6.061  -5.642 -32.185  1.00 16.62           C  
ANISOU 3229  CD2 PHE B  21     1796   2075   2443   -314     90   -506       C  
ATOM   3230  CE1 PHE B  21       4.940  -3.228 -31.445  1.00 16.09           C  
ANISOU 3230  CE1 PHE B  21     1857   2289   1966   -349     60   -386       C  
ATOM   3231  CE2 PHE B  21       6.325  -5.113 -30.921  1.00 16.83           C  
ANISOU 3231  CE2 PHE B  21     1696   2215   2484   -119   -111   -403       C  
ATOM   3232  CZ  PHE B  21       5.748  -3.903 -30.547  1.00 16.19           C  
ANISOU 3232  CZ  PHE B  21     1878   2188   2086   -233     92   -474       C  
ATOM   3233  N   SER B  22       2.519  -5.919 -36.640  1.00 17.16           N  
ANISOU 3233  N   SER B  22     2094   2440   1987   -384    123   -448       N  
ATOM   3234  CA  SER B  22       2.206  -6.126 -38.056  1.00 17.66           C  
ANISOU 3234  CA  SER B  22     2278   2361   2069   -378   -121   -615       C  
ATOM   3235  C   SER B  22       3.050  -5.163 -38.876  1.00 16.99           C  
ANISOU 3235  C   SER B  22     2227   2471   1760   -121   -101   -415       C  
ATOM   3236  O   SER B  22       2.820  -3.949 -38.838  1.00 17.59           O  
ANISOU 3236  O   SER B  22     2169   2520   1993   -156   -110   -418       O  
ATOM   3237  CB  SER B  22       0.724  -5.821 -38.280  1.00 20.37           C  
ANISOU 3237  CB  SER B  22     2428   2862   2452   -267   -274   -592       C  
ATOM   3238  OG  SER B  22       0.364  -6.110 -39.634  1.00 24.16           O  
ANISOU 3238  OG  SER B  22     3035   3432   2711   -186   -495   -926       O  
ATOM   3239  N   ILE B  23       3.998  -5.671 -39.667  1.00 18.04           N  
ANISOU 3239  N   ILE B  23     2483   2409   1963   -138     46   -524       N  
ATOM   3240  CA  ILE B  23       4.886  -4.849 -40.480  1.00 18.05           C  
ANISOU 3240  CA  ILE B  23     2440   2588   1830    -41   -160   -292       C  
ATOM   3241  C   ILE B  23       4.237  -4.610 -41.836  1.00 17.47           C  
ANISOU 3241  C   ILE B  23     2327   2497   1812    -69   -214   -363       C  
ATOM   3242  O   ILE B  23       4.100  -5.520 -42.687  1.00 20.20           O  
ANISOU 3242  O   ILE B  23     2584   2925   2165    288   -383   -722       O  
ATOM   3243  CB  ILE B  23       6.276  -5.518 -40.663  1.00 19.65           C  
ANISOU 3243  CB  ILE B  23     2524   2887   2054     52   -105   -134       C  
ATOM   3244  CG1 ILE B  23       6.892  -5.833 -39.307  1.00 22.43           C  
ANISOU 3244  CG1 ILE B  23     3031   3221   2272    205   -314   -104       C  
ATOM   3245  CG2 ILE B  23       7.175  -4.601 -41.484  1.00 22.89           C  
ANISOU 3245  CG2 ILE B  23     2643   3359   2693   -114    -95    194       C  
ATOM   3246  CD1 ILE B  23       7.866  -6.979 -39.315  1.00 25.63           C  
ANISOU 3246  CD1 ILE B  23     3496   3486   2757    480   -518   -183       C  
ATOM   3247  N   GLU B  24       3.721  -3.428 -42.064  1.00 17.21           N  
ANISOU 3247  N   GLU B  24     2372   2491   1675    -41   -315   -405       N  
ATOM   3248  CA  GLU B  24       2.932  -3.123 -43.264  1.00 16.58           C  
ANISOU 3248  CA  GLU B  24     2115   2539   1647     75   -187   -425       C  
ATOM   3249  C   GLU B  24       3.001  -1.669 -43.637  1.00 16.66           C  
ANISOU 3249  C   GLU B  24     2134   2500   1697     14   -213   -478       C  
ATOM   3250  O   GLU B  24       3.549  -0.852 -42.863  1.00 17.35           O  
ANISOU 3250  O   GLU B  24     2146   2705   1742    -27   -326   -517       O  
ATOM   3251  CB  GLU B  24       1.485  -3.579 -43.019  1.00 18.16           C  
ANISOU 3251  CB  GLU B  24     2199   2815   1887      7    -33   -469       C  
ATOM   3252  CG  GLU B  24       0.786  -2.869 -41.861  1.00 18.43           C  
ANISOU 3252  CG  GLU B  24     2172   2790   2040    -54     52   -507       C  
ATOM   3253  CD  GLU B  24      -0.634  -3.406 -41.691  1.00 19.93           C  
ANISOU 3253  CD  GLU B  24     2201   2957   2416    -49    100   -502       C  
ATOM   3254  OE1 GLU B  24      -1.466  -3.073 -42.564  1.00 22.40           O  
ANISOU 3254  OE1 GLU B  24     2414   3482   2617    -78    -72   -603       O  
ATOM   3255  OE2 GLU B  24      -0.940  -4.107 -40.703  1.00 21.08           O  
ANISOU 3255  OE2 GLU B  24     2250   3365   2396   -385    -68   -521       O  
ATOM   3256  N   GLU B  25       2.479  -1.306 -44.799  1.00 15.77           N  
ANISOU 3256  N   GLU B  25     1903   2517   1572    170   -134   -611       N  
ATOM   3257  CA  GLU B  25       2.465   0.041 -45.312  1.00 16.58           C  
ANISOU 3257  CA  GLU B  25     2233   2589   1479     72    -76   -563       C  
ATOM   3258  C   GLU B  25       1.523   0.953 -44.512  1.00 15.86           C  
ANISOU 3258  C   GLU B  25     1899   2507   1621     25    -88   -478       C  
ATOM   3259  O   GLU B  25       0.363   0.617 -44.236  1.00 18.26           O  
ANISOU 3259  O   GLU B  25     1871   3247   1822   -104   -113   -862       O  
ATOM   3260  CB  GLU B  25       2.014   0.056 -46.797  1.00 17.80           C  
ANISOU 3260  CB  GLU B  25     2293   2956   1514    184   -177   -689       C  
ATOM   3261  CG  GLU B  25       2.000   1.452 -47.405  1.00 20.74           C  
ANISOU 3261  CG  GLU B  25     2943   2959   1979     61    -90   -539       C  
ATOM   3262  CD  GLU B  25       1.566   1.354 -48.899  1.00 24.59           C  
ANISOU 3262  CD  GLU B  25     3608   3401   2334    357   -423   -338       C  
ATOM   3263  OE1 GLU B  25       0.358   1.224 -49.154  1.00 27.84           O  
ANISOU 3263  OE1 GLU B  25     3940   3703   2935    106   -905   -422       O  
ATOM   3264  OE2 GLU B  25       2.470   1.431 -49.713  1.00 26.25           O  
ANISOU 3264  OE2 GLU B  25     4458   3569   1946    898   -181   -269       O  
ATOM   3265  N   VAL B  26       2.046   2.111 -44.165  1.00 15.45           N  
ANISOU 3265  N   VAL B  26     1694   2537   1637     22   -164   -485       N  
ATOM   3266  CA  VAL B  26       1.296   3.193 -43.543  1.00 15.59           C  
ANISOU 3266  CA  VAL B  26     1841   2588   1496    158   -196   -435       C  
ATOM   3267  C   VAL B  26       1.476   4.456 -44.368  1.00 15.83           C  
ANISOU 3267  C   VAL B  26     1842   2587   1585     75    -87   -447       C  
ATOM   3268  O   VAL B  26       2.387   4.552 -45.218  1.00 16.79           O  
ANISOU 3268  O   VAL B  26     1959   2811   1608     69     -4   -431       O  
ATOM   3269  CB  VAL B  26       1.753   3.465 -42.076  1.00 16.00           C  
ANISOU 3269  CB  VAL B  26     1767   2688   1623     71   -178   -632       C  
ATOM   3270  CG1 VAL B  26       1.548   2.230 -41.230  1.00 17.09           C  
ANISOU 3270  CG1 VAL B  26     1883   2824   1786    -10   -228   -580       C  
ATOM   3271  CG2 VAL B  26       3.188   3.974 -42.001  1.00 16.05           C  
ANISOU 3271  CG2 VAL B  26     1931   2552   1614   -124   -177   -373       C  
ATOM   3272  N   GLU B  27       0.633   5.469 -44.180  1.00 15.43           N  
ANISOU 3272  N   GLU B  27     1862   2558   1441    151   -204   -455       N  
ATOM   3273  C   GLU B  27       1.123   7.758 -43.659  1.00 15.65           C  
ANISOU 3273  C   GLU B  27     1944   2632   1371     75   -151   -337       C  
ATOM   3274  O   GLU B  27       0.482   7.800 -42.592  1.00 16.91           O  
ANISOU 3274  O   GLU B  27     1957   2916   1554    -85    -16   -532       O  
ATOM   3275  CA AGLU B  27       0.755   6.778 -44.774  0.55 15.56           C  
ANISOU 3275  CA AGLU B  27     1823   2650   1440    107   -238   -404       C  
ATOM   3276  CB AGLU B  27      -0.527   7.254 -45.469  0.55 16.98           C  
ANISOU 3276  CB AGLU B  27     1927   2956   1570    120   -457   -564       C  
ATOM   3277  CG AGLU B  27      -0.912   6.279 -46.604  0.55 17.09           C  
ANISOU 3277  CG AGLU B  27     1940   2999   1553    -40   -423   -538       C  
ATOM   3278  CD AGLU B  27      -1.777   5.167 -46.071  0.55 20.13           C  
ANISOU 3278  CD AGLU B  27     2589   3060   2001    -39   -302   -148       C  
ATOM   3279  OE1AGLU B  27      -2.584   5.439 -45.152  0.55 24.52           O  
ANISOU 3279  OE1AGLU B  27     3168   3698   2449    198     47   -278       O  
ATOM   3280  OE2AGLU B  27      -1.690   4.011 -46.532  0.55 23.80           O  
ANISOU 3280  OE2AGLU B  27     3134   3277   2632     79   -100   -377       O  
ATOM   3281  CA BGLU B  27       0.731   6.778 -44.773  0.45 17.05           C  
ANISOU 3281  CA BGLU B  27     2232   2628   1619     23   -128   -418       C  
ATOM   3282  CB BGLU B  27      -0.596   7.239 -45.378  0.45 20.99           C  
ANISOU 3282  CB BGLU B  27     2390   3252   2331    213   -216   -230       C  
ATOM   3283  CG BGLU B  27      -1.086   6.442 -46.588  0.45 24.07           C  
ANISOU 3283  CG BGLU B  27     3001   3532   2613    -86   -204   -371       C  
ATOM   3284  CD BGLU B  27      -2.465   6.957 -46.991  0.45 26.63           C  
ANISOU 3284  CD BGLU B  27     3140   3849   3131     27   -253   -179       C  
ATOM   3285  OE1BGLU B  27      -3.463   6.467 -46.430  0.45 27.07           O  
ANISOU 3285  OE1BGLU B  27     3112   3975   3200    104   -220   -132       O  
ATOM   3286  OE2BGLU B  27      -2.542   7.864 -47.839  0.45 28.35           O  
ANISOU 3286  OE2BGLU B  27     3299   3973   3501     40   -169      7       O  
ATOM   3287  N   VAL B  28       2.156   8.539 -43.897  1.00 14.91           N  
ANISOU 3287  N   VAL B  28     1863   2570   1232    107   -164   -322       N  
ATOM   3288  CA  VAL B  28       2.687   9.545 -42.969  1.00 14.66           C  
ANISOU 3288  CA  VAL B  28     1796   2507   1267     98   -115   -325       C  
ATOM   3289  C   VAL B  28       2.499  10.948 -43.556  1.00 15.75           C  
ANISOU 3289  C   VAL B  28     2098   2561   1327    125   -172   -230       C  
ATOM   3290  O   VAL B  28       3.067  11.286 -44.629  1.00 16.05           O  
ANISOU 3290  O   VAL B  28     2188   2577   1334     54   -160   -202       O  
ATOM   3291  CB  VAL B  28       4.184   9.313 -42.681  1.00 14.78           C  
ANISOU 3291  CB  VAL B  28     1867   2388   1360    162    -74   -288       C  
ATOM   3292  CG1 VAL B  28       4.669  10.278 -41.588  1.00 15.58           C  
ANISOU 3292  CG1 VAL B  28     2156   2375   1390    181   -285   -197       C  
ATOM   3293  CG2 VAL B  28       4.446   7.868 -42.281  1.00 15.17           C  
ANISOU 3293  CG2 VAL B  28     1909   2444   1413    192    -92   -315       C  
ATOM   3294  N   ALA B  29       1.635  11.756 -42.942  1.00 15.25           N  
ANISOU 3294  N   ALA B  29     2015   2507   1273    106   -125   -131       N  
ATOM   3295  CA  ALA B  29       1.338  13.096 -43.431  1.00 15.25           C  
ANISOU 3295  CA  ALA B  29     1999   2465   1330    168   -209   -130       C  
ATOM   3296  C   ALA B  29       2.556  13.993 -43.303  1.00 15.45           C  
ANISOU 3296  C   ALA B  29     1940   2469   1460    155   -204     24       C  
ATOM   3297  O   ALA B  29       3.458  13.758 -42.473  1.00 16.31           O  
ANISOU 3297  O   ALA B  29     1962   2835   1402    262   -167     -4       O  
ATOM   3298  CB  ALA B  29       0.171  13.645 -42.601  1.00 17.20           C  
ANISOU 3298  CB  ALA B  29     2141   2582   1811    348   -164   -277       C  
ATOM   3299  N   PRO B  30       2.609  15.067 -44.087  1.00 16.06           N  
ANISOU 3299  N   PRO B  30     2236   2646   1221    -39   -228     83       N  
ATOM   3300  CA  PRO B  30       3.688  16.046 -43.943  1.00 16.35           C  
ANISOU 3300  CA  PRO B  30     2290   2664   1257    -95   -151    178       C  
ATOM   3301  C   PRO B  30       3.521  16.801 -42.617  1.00 16.33           C  
ANISOU 3301  C   PRO B  30     2138   2633   1435    151    -90     82       C  
ATOM   3302  O   PRO B  30       2.452  16.896 -42.002  1.00 17.68           O  
ANISOU 3302  O   PRO B  30     2232   2828   1659    191   -101     24       O  
ATOM   3303  CB  PRO B  30       3.545  16.943 -45.179  1.00 18.62           C  
ANISOU 3303  CB  PRO B  30     2667   2843   1564   -176   -221    338       C  
ATOM   3304  CG  PRO B  30       2.120  16.756 -45.610  1.00 20.09           C  
ANISOU 3304  CG  PRO B  30     2739   3085   1809   -106   -364    334       C  
ATOM   3305  CD  PRO B  30       1.659  15.402 -45.168  1.00 17.88           C  
ANISOU 3305  CD  PRO B  30     2241   2933   1621     -1   -397    141       C  
ATOM   3306  N   PRO B  31       4.612  17.377 -42.139  1.00 15.80           N  
ANISOU 3306  N   PRO B  31     2211   2520   1274    129    -27     81       N  
ATOM   3307  CA  PRO B  31       4.600  18.118 -40.860  1.00 15.43           C  
ANISOU 3307  CA  PRO B  31     2097   2393   1373    221      0     -6       C  
ATOM   3308  C   PRO B  31       3.810  19.412 -40.968  1.00 15.93           C  
ANISOU 3308  C   PRO B  31     2205   2465   1383    223   -153     76       C  
ATOM   3309  O   PRO B  31       3.946  20.144 -41.979  1.00 18.06           O  
ANISOU 3309  O   PRO B  31     2648   2712   1503    181     -3    220       O  
ATOM   3310  CB  PRO B  31       6.092  18.386 -40.540  1.00 16.10           C  
ANISOU 3310  CB  PRO B  31     2218   2522   1378     69    -34     87       C  
ATOM   3311  CG  PRO B  31       6.720  18.395 -41.919  1.00 16.32           C  
ANISOU 3311  CG  PRO B  31     2287   2545   1371     52     -4     41       C  
ATOM   3312  CD  PRO B  31       5.939  17.361 -42.725  1.00 15.93           C  
ANISOU 3312  CD  PRO B  31     2105   2597   1352    115   -156    126       C  
ATOM   3313  N   LYS B  32       3.022  19.714 -39.948  1.00 16.20           N  
ANISOU 3313  N   LYS B  32     2374   2287   1493    275    -55     53       N  
ATOM   3314  CA  LYS B  32       2.316  20.987 -39.824  1.00 17.00           C  
ANISOU 3314  CA  LYS B  32     2181   2549   1730    423   -133    148       C  
ATOM   3315  C   LYS B  32       3.262  21.967 -39.154  1.00 17.62           C  
ANISOU 3315  C   LYS B  32     2634   2539   1523    414   -232     48       C  
ATOM   3316  O   LYS B  32       4.481  21.696 -38.933  1.00 18.28           O  
ANISOU 3316  O   LYS B  32     2637   2781   1527    260   -291    -33       O  
ATOM   3317  CB ALYS B  32       1.036  20.852 -38.986  0.58 18.21           C  
ANISOU 3317  CB ALYS B  32     2355   2662   1902    370     26    114       C  
ATOM   3318  CG ALYS B  32       0.013  19.810 -39.409  0.58 19.97           C  
ANISOU 3318  CG ALYS B  32     2309   2820   2458    267    -42    248       C  
ATOM   3319  CD ALYS B  32      -1.248  19.927 -38.562  0.58 20.68           C  
ANISOU 3319  CD ALYS B  32     2545   2877   2435    339     63    148       C  
ATOM   3320  CE ALYS B  32      -2.355  18.939 -38.858  0.58 22.15           C  
ANISOU 3320  CE ALYS B  32     2762   3076   2579    236   -223     79       C  
ATOM   3321  NZ ALYS B  32      -3.476  19.037 -37.853  0.58 23.56           N  
ANISOU 3321  NZ ALYS B  32     2936   3589   2426    289   -299    -87       N  
ATOM   3322  CB BLYS B  32       0.926  20.739 -39.221  0.42 17.55           C  
ANISOU 3322  CB BLYS B  32     2292   2610   1767    253    -58     18       C  
ATOM   3323  CG BLYS B  32       0.039  19.869 -40.138  0.42 18.74           C  
ANISOU 3323  CG BLYS B  32     2385   2717   2018    107   -103    -35       C  
ATOM   3324  CD BLYS B  32      -1.411  19.923 -39.686  0.42 19.47           C  
ANISOU 3324  CD BLYS B  32     2397   2909   2092     89   -146    -22       C  
ATOM   3325  CE BLYS B  32      -2.307  18.868 -40.315  0.42 21.44           C  
ANISOU 3325  CE BLYS B  32     2757   2891   2499    -77    -97    -64       C  
ATOM   3326  NZ BLYS B  32      -3.748  19.246 -40.240  0.42 22.86           N  
ANISOU 3326  NZ BLYS B  32     2871   3102   2714     77   -100    147       N  
ATOM   3327  N   ALA B  33       2.755  23.146 -38.803  1.00 18.91           N  
ANISOU 3327  N   ALA B  33     2585   2513   2088    454   -455     86       N  
ATOM   3328  CA  ALA B  33       3.547  24.149 -38.132  1.00 20.06           C  
ANISOU 3328  CA  ALA B  33     2608   2610   2404    363   -508     86       C  
ATOM   3329  C   ALA B  33       4.148  23.545 -36.854  1.00 18.16           C  
ANISOU 3329  C   ALA B  33     2591   2346   1964     58   -205     -2       C  
ATOM   3330  O   ALA B  33       3.534  22.785 -36.084  1.00 19.03           O  
ANISOU 3330  O   ALA B  33     2827   2426   1980    175   -108     21       O  
ATOM   3331  CB  ALA B  33       2.756  25.396 -37.756  1.00 22.38           C  
ANISOU 3331  CB  ALA B  33     2937   2740   2824    485   -423     15       C  
ATOM   3332  N   HIS B  34       5.397  23.863 -36.677  1.00 15.87           N  
ANISOU 3332  N   HIS B  34     2538   2004   1487     94   -150    111       N  
ATOM   3333  CA  HIS B  34       6.194  23.474 -35.510  1.00 15.15           C  
ANISOU 3333  CA  HIS B  34     2281   2065   1410     86   -182     86       C  
ATOM   3334  C   HIS B  34       6.356  21.957 -35.381  1.00 14.03           C  
ANISOU 3334  C   HIS B  34     2080   2022   1228    132    -45     80       C  
ATOM   3335  O   HIS B  34       6.577  21.481 -34.242  1.00 14.98           O  
ANISOU 3335  O   HIS B  34     2256   2159   1276    382   -272     43       O  
ATOM   3336  CB  HIS B  34       5.676  24.121 -34.216  1.00 17.02           C  
ANISOU 3336  CB  HIS B  34     2659   2203   1605    206   -186    -45       C  
ATOM   3337  CG  HIS B  34       5.787  25.620 -34.313  1.00 19.33           C  
ANISOU 3337  CG  HIS B  34     3145   2308   1891     85    -60   -151       C  
ATOM   3338  ND1 HIS B  34       6.954  26.333 -34.252  1.00 24.02           N  
ANISOU 3338  ND1 HIS B  34     3547   2863   2718   -160     50     30       N  
ATOM   3339  CD2 HIS B  34       4.771  26.487 -34.506  1.00 21.63           C  
ANISOU 3339  CD2 HIS B  34     3316   2528   2373    278     72   -111       C  
ATOM   3340  CE1 HIS B  34       6.668  27.624 -34.388  1.00 23.25           C  
ANISOU 3340  CE1 HIS B  34     3474   2805   2555   -102    154    152       C  
ATOM   3341  NE2 HIS B  34       5.373  27.738 -34.562  1.00 24.84           N  
ANISOU 3341  NE2 HIS B  34     3592   2877   2969    -30    156    101       N  
ATOM   3342  N   GLU B  35       6.333  21.226 -36.486  1.00 13.86           N  
ANISOU 3342  N   GLU B  35     1986   1980   1300    109   -159     37       N  
ATOM   3343  CA  GLU B  35       6.511  19.786 -36.491  1.00 13.53           C  
ANISOU 3343  CA  GLU B  35     2050   1990   1099    169    -26     65       C  
ATOM   3344  C   GLU B  35       7.672  19.415 -37.414  1.00 13.72           C  
ANISOU 3344  C   GLU B  35     1957   2124   1132    109    -34     60       C  
ATOM   3345  O   GLU B  35       8.121  20.193 -38.285  1.00 14.11           O  
ANISOU 3345  O   GLU B  35     2012   2207   1143    108    -54    119       O  
ATOM   3346  CB  GLU B  35       5.253  19.046 -36.945  1.00 13.96           C  
ANISOU 3346  CB  GLU B  35     1943   1983   1376    235     41     96       C  
ATOM   3347  CG  GLU B  35       4.043  19.309 -36.050  1.00 14.22           C  
ANISOU 3347  CG  GLU B  35     2039   2072   1293    106     76     84       C  
ATOM   3348  CD  GLU B  35       2.752  18.697 -36.529  1.00 14.79           C  
ANISOU 3348  CD  GLU B  35     2031   2094   1496     39     52    -21       C  
ATOM   3349  OE1 GLU B  35       2.733  18.058 -37.618  1.00 15.67           O  
ANISOU 3349  OE1 GLU B  35     2231   2316   1407     55    -67     -6       O  
ATOM   3350  OE2 GLU B  35       1.698  18.862 -35.849  1.00 16.64           O  
ANISOU 3350  OE2 GLU B  35     2017   2739   1567     17     22   -253       O  
ATOM   3351  N   VAL B  36       8.229  18.216 -37.199  1.00 13.22           N  
ANISOU 3351  N   VAL B  36     1912   2045   1065    145     61    -55       N  
ATOM   3352  CA  VAL B  36       9.435  17.724 -37.870  1.00 13.06           C  
ANISOU 3352  CA  VAL B  36     1713   2154   1095     -2     17     66       C  
ATOM   3353  C   VAL B  36       9.215  16.308 -38.360  1.00 12.44           C  
ANISOU 3353  C   VAL B  36     1759   1954   1015    166     70    152       C  
ATOM   3354  O   VAL B  36       8.848  15.448 -37.537  1.00 13.74           O  
ANISOU 3354  O   VAL B  36     2091   2077   1053    -38      9    155       O  
ATOM   3355  CB  VAL B  36      10.640  17.759 -36.891  1.00 12.89           C  
ANISOU 3355  CB  VAL B  36     1736   1991   1169     64    -29    -37       C  
ATOM   3356  CG1 VAL B  36      11.925  17.223 -37.547  1.00 14.54           C  
ANISOU 3356  CG1 VAL B  36     1857   2250   1418     97    107     18       C  
ATOM   3357  CG2 VAL B  36      10.870  19.149 -36.319  1.00 13.83           C  
ANISOU 3357  CG2 VAL B  36     1983   2112   1158    -57     19     -4       C  
ATOM   3358  N   ARG B  37       9.450  16.034 -39.648  1.00 13.38           N  
ANISOU 3358  N   ARG B  37     1951   2115   1017     87     17     32       N  
ATOM   3359  CA  ARG B  37       9.331  14.668 -40.159  1.00 12.72           C  
ANISOU 3359  CA  ARG B  37     1784   2052    997    -32     42    165       C  
ATOM   3360  C   ARG B  37      10.736  14.072 -40.304  1.00 12.73           C  
ANISOU 3360  C   ARG B  37     1837   2036    964    -72    -41    -31       C  
ATOM   3361  O   ARG B  37      11.637  14.723 -40.892  1.00 13.68           O  
ANISOU 3361  O   ARG B  37     1910   2168   1121    -29    132     46       O  
ATOM   3362  CB  ARG B  37       8.528  14.616 -41.469  1.00 13.54           C  
ANISOU 3362  CB  ARG B  37     1973   2193    980    112    -86    -57       C  
ATOM   3363  CG  ARG B  37       8.289  13.186 -41.959  1.00 13.26           C  
ANISOU 3363  CG  ARG B  37     1805   2186   1048    111    -47     33       C  
ATOM   3364  CD  ARG B  37       7.088  13.068 -42.900  1.00 14.22           C  
ANISOU 3364  CD  ARG B  37     1937   2433   1035    144   -106     47       C  
ATOM   3365  NE  ARG B  37       7.358  13.767 -44.159  1.00 14.60           N  
ANISOU 3365  NE  ARG B  37     2054   2479   1013    -84   -151    -62       N  
ATOM   3366  CZ  ARG B  37       6.545  13.826 -45.220  1.00 14.93           C  
ANISOU 3366  CZ  ARG B  37     2041   2583   1048    -99   -122     -1       C  
ATOM   3367  NH1 ARG B  37       5.353  13.260 -45.175  1.00 15.41           N  
ANISOU 3367  NH1 ARG B  37     1995   2748   1114      1   -100    121       N  
ATOM   3368  NH2 ARG B  37       6.941  14.442 -46.334  1.00 16.64           N  
ANISOU 3368  NH2 ARG B  37     2452   2798   1075    -70     54     95       N  
ATOM   3369  N   ILE B  38      10.944  12.898 -39.715  1.00 12.90           N  
ANISOU 3369  N   ILE B  38     1691   2062   1147    -17     82     39       N  
ATOM   3370  CA  ILE B  38      12.228  12.249 -39.571  1.00 13.68           C  
ANISOU 3370  CA  ILE B  38     1951   2067   1180    118     28    -77       C  
ATOM   3371  C   ILE B  38      12.274  10.886 -40.256  1.00 12.22           C  
ANISOU 3371  C   ILE B  38     1646   1863   1136     22     61     10       C  
ATOM   3372  O   ILE B  38      11.376  10.076 -40.072  1.00 13.73           O  
ANISOU 3372  O   ILE B  38     1749   2173   1295   -190    141   -100       O  
ATOM   3373  CB  ILE B  38      12.589  12.074 -38.053  1.00 13.82           C  
ANISOU 3373  CB  ILE B  38     1828   2219   1204     -1     92    -40       C  
ATOM   3374  CG1 ILE B  38      12.411  13.326 -37.209  1.00 14.73           C  
ANISOU 3374  CG1 ILE B  38     1925   2496   1177   -138     94   -176       C  
ATOM   3375  CG2 ILE B  38      13.999  11.521 -37.915  1.00 16.86           C  
ANISOU 3375  CG2 ILE B  38     2075   3032   1300    369    -82   -337       C  
ATOM   3376  CD1 ILE B  38      12.427  13.083 -35.710  1.00 14.61           C  
ANISOU 3376  CD1 ILE B  38     2010   2454   1088    -40    222   -249       C  
ATOM   3377  N   LYS B  39      13.329  10.681 -41.048  1.00 13.43           N  
ANISOU 3377  N   LYS B  39     1826   2119   1158     59    134    -11       N  
ATOM   3378  CA  LYS B  39      13.630   9.360 -41.617  1.00 13.48           C  
ANISOU 3378  CA  LYS B  39     1836   2087   1201    -59    138     53       C  
ATOM   3379  C   LYS B  39      14.428   8.595 -40.523  1.00 13.47           C  
ANISOU 3379  C   LYS B  39     1685   2156   1275   -116    149     70       C  
ATOM   3380  O   LYS B  39      15.541   8.992 -40.136  1.00 14.48           O  
ANISOU 3380  O   LYS B  39     1748   2366   1389   -225    146    -23       O  
ATOM   3381  CB  LYS B  39      14.498   9.449 -42.887  1.00 14.66           C  
ANISOU 3381  CB  LYS B  39     2030   2340   1201     62    208     16       C  
ATOM   3382  CG  LYS B  39      14.676   8.069 -43.520  1.00 16.66           C  
ANISOU 3382  CG  LYS B  39     2544   2371   1414     22    217    -66       C  
ATOM   3383  CD  LYS B  39      15.563   8.045 -44.748  1.00 19.88           C  
ANISOU 3383  CD  LYS B  39     3006   2794   1756     56    485    -93       C  
ATOM   3384  CE  LYS B  39      15.474   6.648 -45.399  1.00 23.28           C  
ANISOU 3384  CE  LYS B  39     3821   2941   2084     93    535   -253       C  
ATOM   3385  NZ  LYS B  39      16.508   6.477 -46.455  1.00 25.50           N  
ANISOU 3385  NZ  LYS B  39     3896   3372   2422    154    709     47       N  
ATOM   3386  N   MET B  40      13.845   7.517 -39.991  1.00 14.09           N  
ANISOU 3386  N   MET B  40     1937   2147   1271   -262    -89     78       N  
ATOM   3387  CA  MET B  40      14.494   6.738 -38.934  1.00 13.49           C  
ANISOU 3387  CA  MET B  40     1838   2017   1270    -57     44     17       C  
ATOM   3388  C   MET B  40      15.654   5.900 -39.476  1.00 14.04           C  
ANISOU 3388  C   MET B  40     1945   2141   1248    -72    166   -144       C  
ATOM   3389  O   MET B  40      15.606   5.376 -40.611  1.00 15.63           O  
ANISOU 3389  O   MET B  40     2311   2359   1270   -178    128   -222       O  
ATOM   3390  CB AMET B  40      13.501   5.805 -38.240  0.52 13.68           C  
ANISOU 3390  CB AMET B  40     1736   2183   1278   -150      3      8       C  
ATOM   3391  CG AMET B  40      12.435   6.429 -37.336  0.52 14.60           C  
ANISOU 3391  CG AMET B  40     1955   2180   1411    -28    -14    -15       C  
ATOM   3392  SD AMET B  40      12.966   7.175 -35.785  0.52 14.54           S  
ANISOU 3392  SD AMET B  40     2197   2193   1135   -248     81    176       S  
ATOM   3393  CE AMET B  40      13.473   8.813 -36.248  0.52 17.49           C  
ANISOU 3393  CE AMET B  40     2530   2222   1893   -332    -66     66       C  
ATOM   3394  CB BMET B  40      13.361   5.953 -38.279  0.47 15.07           C  
ANISOU 3394  CB BMET B  40     1845   2411   1469   -139     74     29       C  
ATOM   3395  CG BMET B  40      12.270   6.913 -37.753  0.47 17.44           C  
ANISOU 3395  CG BMET B  40     2015   2681   1929    201    -88     60       C  
ATOM   3396  SD BMET B  40      12.885   8.316 -36.787  0.47 19.00           S  
ANISOU 3396  SD BMET B  40     2151   3045   2023    181   -319    -18       S  
ATOM   3397  CE BMET B  40      14.064   7.469 -35.748  0.47 10.18           C  
ANISOU 3397  CE BMET B  40     1301   1979    588   -246    308    -13       C  
ATOM   3398  N   VAL B  41      16.750   5.828 -38.707  1.00 13.86           N  
ANISOU 3398  N   VAL B  41     1760   2232   1274    -13    242    -59       N  
ATOM   3399  CA  VAL B  41      17.940   5.082 -39.083  1.00 13.12           C  
ANISOU 3399  CA  VAL B  41     1841   1956   1188    -97    230   -102       C  
ATOM   3400  C   VAL B  41      18.144   3.866 -38.194  1.00 13.36           C  
ANISOU 3400  C   VAL B  41     1874   1930   1272    175    364   -151       C  
ATOM   3401  O   VAL B  41      18.410   2.751 -38.677  1.00 14.65           O  
ANISOU 3401  O   VAL B  41     2366   1807   1394   -101    712   -141       O  
ATOM   3402  CB  VAL B  41      19.195   5.977 -39.161  1.00 13.75           C  
ANISOU 3402  CB  VAL B  41     1805   2118   1303    -43    299     11       C  
ATOM   3403  CG1 VAL B  41      20.470   5.150 -39.381  1.00 16.22           C  
ANISOU 3403  CG1 VAL B  41     1965   2225   1972     49    495   -118       C  
ATOM   3404  CG2 VAL B  41      19.032   7.002 -40.285  1.00 14.90           C  
ANISOU 3404  CG2 VAL B  41     2100   2189   1372   -229    424    172       C  
ATOM   3405  N   ALA B  42      17.970   4.029 -36.851  1.00 12.40           N  
ANISOU 3405  N   ALA B  42     1679   1864   1168   -149    285    -77       N  
ATOM   3406  CA  ALA B  42      18.141   2.925 -35.919  1.00 12.16           C  
ANISOU 3406  CA  ALA B  42     1565   1761   1293     -1    317    -52       C  
ATOM   3407  C   ALA B  42      17.200   3.134 -34.707  1.00 11.17           C  
ANISOU 3407  C   ALA B  42     1461   1528   1254     18    270   -102       C  
ATOM   3408  O   ALA B  42      17.007   4.279 -34.292  1.00 12.29           O  
ANISOU 3408  O   ALA B  42     1812   1650   1208     18    374    -62       O  
ATOM   3409  CB  ALA B  42      19.586   2.834 -35.425  1.00 14.23           C  
ANISOU 3409  CB  ALA B  42     1566   2238   1602    104    374     12       C  
ATOM   3410  N   THR B  43      16.655   2.056 -34.166  1.00 11.20           N  
ANISOU 3410  N   THR B  43     1531   1579   1145    -75    288   -140       N  
ATOM   3411  CA  THR B  43      15.800   2.124 -32.975  1.00 11.50           C  
ANISOU 3411  CA  THR B  43     1513   1712   1146    130    297   -162       C  
ATOM   3412  C   THR B  43      16.054   0.897 -32.102  1.00 11.40           C  
ANISOU 3412  C   THR B  43     1465   1561   1305     66    308   -208       C  
ATOM   3413  O   THR B  43      16.171  -0.221 -32.576  1.00 12.38           O  
ANISOU 3413  O   THR B  43     1805   1608   1292     22    303   -142       O  
ATOM   3414  CB  THR B  43      14.330   2.309 -33.399  1.00 11.72           C  
ANISOU 3414  CB  THR B  43     1480   1754   1220    115    255   -255       C  
ATOM   3415  OG1 THR B  43      13.500   2.552 -32.231  1.00 12.45           O  
ANISOU 3415  OG1 THR B  43     1469   1908   1353    107    322   -192       O  
ATOM   3416  CG2 THR B  43      13.743   1.123 -34.155  1.00 13.53           C  
ANISOU 3416  CG2 THR B  43     1546   2110   1486   -103    231   -342       C  
ATOM   3417  N   GLY B  44      16.110   1.138 -30.769  1.00 11.45           N  
ANISOU 3417  N   GLY B  44     1510   1612   1230   -177    231    -79       N  
ATOM   3418  CA  GLY B  44      16.288   0.049 -29.827  1.00 11.23           C  
ANISOU 3418  CA  GLY B  44     1386   1655   1228   -129    143   -106       C  
ATOM   3419  C   GLY B  44      15.003  -0.571 -29.328  1.00 11.45           C  
ANISOU 3419  C   GLY B  44     1331   1590   1430   -107    180   -140       C  
ATOM   3420  O   GLY B  44      13.929   0.079 -29.350  1.00 13.73           O  
ANISOU 3420  O   GLY B  44     1533   1883   1800    131    343    -51       O  
ATOM   3421  N   ILE B  45      15.084  -1.811 -28.885  1.00 11.54           N  
ANISOU 3421  N   ILE B  45     1459   1598   1329    -34    261   -151       N  
ATOM   3422  CA  ILE B  45      13.939  -2.512 -28.272  1.00 11.67           C  
ANISOU 3422  CA  ILE B  45     1524   1668   1244    -10    358     -8       C  
ATOM   3423  C   ILE B  45      14.071  -2.387 -26.748  1.00 11.35           C  
ANISOU 3423  C   ILE B  45     1428   1587   1298     20    168    -51       C  
ATOM   3424  O   ILE B  45      14.959  -2.987 -26.113  1.00 12.13           O  
ANISOU 3424  O   ILE B  45     1489   1742   1378     82    151    -96       O  
ATOM   3425  CB  ILE B  45      13.895  -3.973 -28.745  1.00 12.53           C  
ANISOU 3425  CB  ILE B  45     1593   1653   1516    -82    188    -87       C  
ATOM   3426  CG1 ILE B  45      13.605  -4.020 -30.259  1.00 13.71           C  
ANISOU 3426  CG1 ILE B  45     1873   1832   1505   -136    159   -195       C  
ATOM   3427  CG2 ILE B  45      12.839  -4.748 -27.959  1.00 13.40           C  
ANISOU 3427  CG2 ILE B  45     1801   1790   1501   -325     88    -19       C  
ATOM   3428  CD1 ILE B  45      13.623  -5.426 -30.848  1.00 13.98           C  
ANISOU 3428  CD1 ILE B  45     1965   1935   1411   -192     57   -220       C  
ATOM   3429  N   CYS B  46      13.222  -1.542 -26.167  1.00 11.19           N  
ANISOU 3429  N   CYS B  46     1347   1694   1210    141    137    -46       N  
ATOM   3430  CA  CYS B  46      13.201  -1.300 -24.712  1.00 11.11           C  
ANISOU 3430  CA  CYS B  46     1359   1625   1236     81    161   -144       C  
ATOM   3431  C   CYS B  46      12.042  -2.059 -24.072  1.00 10.79           C  
ANISOU 3431  C   CYS B  46     1286   1653   1159    115    183   -161       C  
ATOM   3432  O   CYS B  46      10.947  -2.220 -24.663  1.00 11.94           O  
ANISOU 3432  O   CYS B  46     1535   1711   1291     37     42   -174       O  
ATOM   3433  CB  CYS B  46      13.069   0.222 -24.508  1.00 11.19           C  
ANISOU 3433  CB  CYS B  46     1438   1588   1224    -59    101    -58       C  
ATOM   3434  SG  CYS B  46      12.830   0.707 -22.737  1.00 10.74           S  
ANISOU 3434  SG  CYS B  46     1349   1567   1165    -20     77    -73       S  
ATOM   3435  N   ARG B  47      12.177  -2.460 -22.803  1.00 10.87           N  
ANISOU 3435  N   ARG B  47     1351   1464   1314     72     73    -59       N  
ATOM   3436  CA  ARG B  47      11.063  -3.131 -22.101  1.00 10.79           C  
ANISOU 3436  CA  ARG B  47     1392   1373   1336     -6     57    -98       C  
ATOM   3437  C   ARG B  47       9.799  -2.263 -22.085  1.00 10.53           C  
ANISOU 3437  C   ARG B  47     1333   1508   1158    -39    128     42       C  
ATOM   3438  O   ARG B  47       8.700  -2.852 -22.075  1.00 11.63           O  
ANISOU 3438  O   ARG B  47     1304   1677   1436   -115    124     -5       O  
ATOM   3439  CB  ARG B  47      11.555  -3.536 -20.692  1.00 11.25           C  
ANISOU 3439  CB  ARG B  47     1295   1597   1381    -24     67   -108       C  
ATOM   3440  CG  ARG B  47      10.473  -4.254 -19.893  1.00 11.80           C  
ANISOU 3440  CG  ARG B  47     1488   1526   1470   -128      9    -33       C  
ATOM   3441  CD  ARG B  47      10.029  -5.579 -20.456  1.00 13.35           C  
ANISOU 3441  CD  ARG B  47     1571   1708   1791   -126    119   -186       C  
ATOM   3442  NE  ARG B  47      11.057  -6.596 -20.404  1.00 13.43           N  
ANISOU 3442  NE  ARG B  47     1828   1677   1598    -10    -15    -60       N  
ATOM   3443  CZ  ARG B  47      10.858  -7.901 -20.616  1.00 15.22           C  
ANISOU 3443  CZ  ARG B  47     2161   1827   1794    -81    -79   -208       C  
ATOM   3444  NH1 ARG B  47       9.687  -8.329 -21.067  1.00 16.27           N  
ANISOU 3444  NH1 ARG B  47     2364   1950   1867   -284   -165    -96       N  
ATOM   3445  NH2 ARG B  47      11.861  -8.746 -20.381  1.00 16.96           N  
ANISOU 3445  NH2 ARG B  47     2500   1896   2048    188    106   -110       N  
ATOM   3446  N   SER B  48       9.898  -0.925 -22.050  1.00 10.69           N  
ANISOU 3446  N   SER B  48     1422   1522   1118     31    152     12       N  
ATOM   3447  CA  SER B  48       8.645  -0.170 -22.062  1.00 10.97           C  
ANISOU 3447  CA  SER B  48     1235   1613   1319    -16     21    -76       C  
ATOM   3448  C   SER B  48       7.836  -0.377 -23.349  1.00 11.27           C  
ANISOU 3448  C   SER B  48     1192   1851   1240      1     70    -85       C  
ATOM   3449  O   SER B  48       6.590  -0.264 -23.296  1.00 12.07           O  
ANISOU 3449  O   SER B  48     1284   1932   1369    -18      4   -276       O  
ATOM   3450  CB  SER B  48       8.887   1.320 -21.896  1.00 10.54           C  
ANISOU 3450  CB  SER B  48     1431   1572   1000     79    -12     23       C  
ATOM   3451  OG  SER B  48       9.358   1.613 -20.581  1.00 11.62           O  
ANISOU 3451  OG  SER B  48     1571   1694   1151     -7    -82    -33       O  
ATOM   3452  N   ASP B  49       8.478  -0.604 -24.505  1.00 11.32           N  
ANISOU 3452  N   ASP B  49     1383   1806   1114    -31      7   -203       N  
ATOM   3453  CA  ASP B  49       7.705  -0.954 -25.705  1.00 11.55           C  
ANISOU 3453  CA  ASP B  49     1344   1851   1193    -90    -48   -134       C  
ATOM   3454  C   ASP B  49       6.976  -2.264 -25.525  1.00 12.06           C  
ANISOU 3454  C   ASP B  49     1402   1859   1322    -36     25   -260       C  
ATOM   3455  O   ASP B  49       5.809  -2.411 -25.942  1.00 12.57           O  
ANISOU 3455  O   ASP B  49     1453   1923   1399    -92     26   -179       O  
ATOM   3456  CB  ASP B  49       8.625  -0.991 -26.946  1.00 12.10           C  
ANISOU 3456  CB  ASP B  49     1596   1813   1190    -87     39   -253       C  
ATOM   3457  CG  ASP B  49       9.373   0.311 -27.154  1.00 11.49           C  
ANISOU 3457  CG  ASP B  49     1465   1858   1044     10     -7   -124       C  
ATOM   3458  OD1 ASP B  49       8.694   1.349 -27.373  1.00 11.89           O  
ANISOU 3458  OD1 ASP B  49     1528   1813   1178    -40     49    -78       O  
ATOM   3459  OD2 ASP B  49      10.627   0.278 -27.094  1.00 12.77           O  
ANISOU 3459  OD2 ASP B  49     1498   1931   1421    -87     91   -167       O  
ATOM   3460  N   ASP B  50       7.629  -3.258 -24.903  1.00 11.70           N  
ANISOU 3460  N   ASP B  50     1279   1856   1309   -171     42   -138       N  
ATOM   3461  CA  ASP B  50       6.972  -4.522 -24.587  1.00 12.35           C  
ANISOU 3461  CA  ASP B  50     1366   1871   1457   -210     56   -128       C  
ATOM   3462  C   ASP B  50       5.810  -4.340 -23.606  1.00 11.37           C  
ANISOU 3462  C   ASP B  50     1330   1582   1409    -88     30   -111       C  
ATOM   3463  O   ASP B  50       4.807  -5.062 -23.704  1.00 13.71           O  
ANISOU 3463  O   ASP B  50     1552   2054   1604   -347     81   -193       O  
ATOM   3464  CB  ASP B  50       7.985  -5.504 -24.030  1.00 12.54           C  
ANISOU 3464  CB  ASP B  50     1427   1877   1462   -115    146   -188       C  
ATOM   3465  CG  ASP B  50       7.389  -6.874 -23.759  1.00 14.41           C  
ANISOU 3465  CG  ASP B  50     1949   1869   1659   -142     91   -184       C  
ATOM   3466  OD1 ASP B  50       6.971  -7.516 -24.753  1.00 16.38           O  
ANISOU 3466  OD1 ASP B  50     2437   1951   1838   -174    -69   -199       O  
ATOM   3467  OD2 ASP B  50       7.333  -7.282 -22.566  1.00 15.78           O  
ANISOU 3467  OD2 ASP B  50     2250   1932   1814   -174     32    -75       O  
ATOM   3468  N   HIS B  51       5.910  -3.407 -22.655  1.00 11.86           N  
ANISOU 3468  N   HIS B  51     1454   1778   1276   -159    116   -138       N  
ATOM   3469  CA  HIS B  51       4.796  -3.142 -21.731  1.00 12.88           C  
ANISOU 3469  CA  HIS B  51     1555   2042   1298    -78     71   -193       C  
ATOM   3470  C   HIS B  51       3.512  -2.739 -22.461  1.00 13.41           C  
ANISOU 3470  C   HIS B  51     1521   2102   1473   -166     60   -158       C  
ATOM   3471  O   HIS B  51       2.393  -3.008 -21.979  1.00 15.05           O  
ANISOU 3471  O   HIS B  51     1643   2505   1570   -274    162   -299       O  
ATOM   3472  CB  HIS B  51       5.167  -2.049 -20.713  1.00 13.02           C  
ANISOU 3472  CB  HIS B  51     1409   2099   1438    -20    -32   -229       C  
ATOM   3473  CG  HIS B  51       6.202  -2.443 -19.695  1.00 12.12           C  
ANISOU 3473  CG  HIS B  51     1368   1936   1301    -54     86   -231       C  
ATOM   3474  ND1 HIS B  51       6.467  -3.734 -19.291  1.00 12.85           N  
ANISOU 3474  ND1 HIS B  51     1409   2029   1444   -110    116   -152       N  
ATOM   3475  CD2 HIS B  51       6.982  -1.611 -18.936  1.00 11.76           C  
ANISOU 3475  CD2 HIS B  51     1445   1761   1264     -3    -33    -98       C  
ATOM   3476  CE1 HIS B  51       7.368  -3.683 -18.328  1.00 12.66           C  
ANISOU 3476  CE1 HIS B  51     1587   1870   1351    -24     91    -90       C  
ATOM   3477  NE2 HIS B  51       7.673  -2.411 -18.075  1.00 12.52           N  
ANISOU 3477  NE2 HIS B  51     1527   1825   1403     -2     63     25       N  
ATOM   3478  N   VAL B  52       3.628  -2.083 -23.629  1.00 13.29           N  
ANISOU 3478  N   VAL B  52     1469   2163   1419     21     18   -165       N  
ATOM   3479  CA  VAL B  52       2.444  -1.753 -24.428  1.00 14.52           C  
ANISOU 3479  CA  VAL B  52     1505   2359   1654     50   -151   -241       C  
ATOM   3480  C   VAL B  52       1.801  -3.036 -24.956  1.00 14.84           C  
ANISOU 3480  C   VAL B  52     1411   2487   1741    -63   -144   -342       C  
ATOM   3481  O   VAL B  52       0.578  -3.204 -24.923  1.00 17.27           O  
ANISOU 3481  O   VAL B  52     1469   2956   2136    -35   -129   -552       O  
ATOM   3482  CB  VAL B  52       2.791  -0.833 -25.617  1.00 15.23           C  
ANISOU 3482  CB  VAL B  52     1751   2286   1749    201   -154   -168       C  
ATOM   3483  CG1 VAL B  52       1.540  -0.539 -26.446  1.00 17.32           C  
ANISOU 3483  CG1 VAL B  52     1912   2766   1903    221   -271   -248       C  
ATOM   3484  CG2 VAL B  52       3.405   0.481 -25.166  1.00 16.09           C  
ANISOU 3484  CG2 VAL B  52     1915   2358   1842     90   -187    -70       C  
ATOM   3485  N   VAL B  53       2.620  -3.975 -25.428  1.00 15.53           N  
ANISOU 3485  N   VAL B  53     1758   2408   1734   -149    -71   -531       N  
ATOM   3486  CA  VAL B  53       2.118  -5.251 -25.919  1.00 15.65           C  
ANISOU 3486  CA  VAL B  53     1672   2386   1890   -219   -112   -439       C  
ATOM   3487  C   VAL B  53       1.431  -6.061 -24.825  1.00 16.85           C  
ANISOU 3487  C   VAL B  53     2037   2478   1885   -249     18   -471       C  
ATOM   3488  O   VAL B  53       0.359  -6.653 -25.015  1.00 19.06           O  
ANISOU 3488  O   VAL B  53     2162   2901   2178   -404     -3   -601       O  
ATOM   3489  CB  VAL B  53       3.250  -6.081 -26.572  1.00 16.11           C  
ANISOU 3489  CB  VAL B  53     1851   2481   1791   -202   -113   -482       C  
ATOM   3490  CG1 VAL B  53       2.684  -7.381 -27.150  1.00 18.20           C  
ANISOU 3490  CG1 VAL B  53     2334   2421   2158   -254    -62   -523       C  
ATOM   3491  CG2 VAL B  53       3.970  -5.274 -27.645  1.00 16.83           C  
ANISOU 3491  CG2 VAL B  53     1943   2686   1765   -113   -125   -359       C  
ATOM   3492  N   SER B  54       2.059  -6.106 -23.646  1.00 17.10           N  
ANISOU 3492  N   SER B  54     1940   2729   1829   -403     79   -354       N  
ATOM   3493  CA  SER B  54       1.532  -6.922 -22.569  1.00 17.46           C  
ANISOU 3493  CA  SER B  54     2152   2642   1841   -357     13   -276       C  
ATOM   3494  C   SER B  54       0.376  -6.306 -21.806  1.00 18.73           C  
ANISOU 3494  C   SER B  54     2117   2858   2141   -409    138   -370       C  
ATOM   3495  O   SER B  54      -0.262  -7.002 -21.001  1.00 23.24           O  
ANISOU 3495  O   SER B  54     2550   3497   2784   -613    541   -199       O  
ATOM   3496  CB  SER B  54       2.675  -7.250 -21.596  1.00 17.36           C  
ANISOU 3496  CB  SER B  54     2288   2466   1842   -405     13    -75       C  
ATOM   3497  OG  SER B  54       3.058  -6.116 -20.829  1.00 18.00           O  
ANISOU 3497  OG  SER B  54     2259   2511   2068   -257    -19   -258       O  
ATOM   3498  N   GLY B  55       0.090  -5.039 -21.975  1.00 18.96           N  
ANISOU 3498  N   GLY B  55     2016   2943   2245   -349    253   -314       N  
ATOM   3499  CA  GLY B  55      -0.971  -4.382 -21.219  1.00 20.58           C  
ANISOU 3499  CA  GLY B  55     2160   3220   2441   -318    319   -382       C  
ATOM   3500  C   GLY B  55      -0.466  -3.793 -19.902  1.00 21.00           C  
ANISOU 3500  C   GLY B  55     2353   3318   2306   -171    174   -288       C  
ATOM   3501  O   GLY B  55      -1.287  -3.281 -19.115  1.00 23.69           O  
ANISOU 3501  O   GLY B  55     2702   3812   2485   -199    397   -395       O  
ATOM   3502  N   THR B  56       0.815  -3.920 -19.570  1.00 19.63           N  
ANISOU 3502  N   THR B  56     2307   3177   1974   -366    213   -363       N  
ATOM   3503  CA  THR B  56       1.389  -3.292 -18.370  1.00 17.22           C  
ANISOU 3503  CA  THR B  56     1905   2735   1904   -275    181   -172       C  
ATOM   3504  C   THR B  56       1.280  -1.773 -18.461  1.00 17.41           C  
ANISOU 3504  C   THR B  56     2065   2756   1796   -141    197   -210       C  
ATOM   3505  O   THR B  56       1.025  -1.108 -17.439  1.00 17.49           O  
ANISOU 3505  O   THR B  56     1915   2915   1814   -320    308   -232       O  
ATOM   3506  CB  THR B  56       2.870  -3.756 -18.227  1.00 17.65           C  
ANISOU 3506  CB  THR B  56     1925   2713   2068   -199    169   -147       C  
ATOM   3507  OG1 THR B  56       2.872  -5.134 -17.819  1.00 23.06           O  
ANISOU 3507  OG1 THR B  56     2477   2876   3408    -73    -36    -10       O  
ATOM   3508  CG2 THR B  56       3.660  -2.935 -17.216  1.00 18.48           C  
ANISOU 3508  CG2 THR B  56     2369   2966   1685   -175    218   -212       C  
ATOM   3509  N   LEU B  57       1.528  -1.199 -19.646  1.00 16.05           N  
ANISOU 3509  N   LEU B  57     1761   2515   1821     28     83    -87       N  
ATOM   3510  C   LEU B  57       0.275   0.502 -20.782  1.00 17.05           C  
ANISOU 3510  C   LEU B  57     2046   2722   1712    236     11   -235       C  
ATOM   3511  O   LEU B  57       0.211  -0.005 -21.931  1.00 19.51           O  
ANISOU 3511  O   LEU B  57     2183   3321   1907    297     -4   -530       O  
ATOM   3512  CA ALEU B  57       1.494   0.232 -19.901  0.62 15.46           C  
ANISOU 3512  CA ALEU B  57     1765   2525   1585     72    166   -120       C  
ATOM   3513  CB ALEU B  57       2.789   0.633 -20.633  0.62 16.46           C  
ANISOU 3513  CB ALEU B  57     1895   2382   1979     24    331   -147       C  
ATOM   3514  CG ALEU B  57       3.120   2.117 -20.799  0.62 15.70           C  
ANISOU 3514  CG ALEU B  57     1950   2413   1603    -26    321   -212       C  
ATOM   3515  CD1ALEU B  57       4.579   2.217 -21.254  0.62 16.34           C  
ANISOU 3515  CD1ALEU B  57     1914   2382   1911     46    340   -113       C  
ATOM   3516  CD2ALEU B  57       2.168   2.852 -21.732  0.62 16.50           C  
ANISOU 3516  CD2ALEU B  57     2019   2489   1762     48    258   -151       C  
ATOM   3517  CA BLEU B  57       1.468   0.239 -19.867  0.38 16.67           C  
ANISOU 3517  CA BLEU B  57     2008   2546   1778    135     29    -90       C  
ATOM   3518  CB BLEU B  57       2.781   0.753 -20.472  0.38 18.37           C  
ANISOU 3518  CB BLEU B  57     2238   2620   2121    -11    138    -25       C  
ATOM   3519  CG BLEU B  57       2.846   2.218 -20.913  0.38 19.38           C  
ANISOU 3519  CG BLEU B  57     2480   2677   2208     51    102     41       C  
ATOM   3520  CD1BLEU B  57       2.604   3.143 -19.730  0.38 19.48           C  
ANISOU 3520  CD1BLEU B  57     2553   2641   2208     25     88     53       C  
ATOM   3521  CD2BLEU B  57       4.187   2.530 -21.573  0.38 20.23           C  
ANISOU 3521  CD2BLEU B  57     2479   2872   2337    -72     71     63       C  
ATOM   3522  N   VAL B  58      -0.702   1.260 -20.283  1.00 17.31           N  
ANISOU 3522  N   VAL B  58     2103   2833   1639    195    167    -74       N  
ATOM   3523  CA  VAL B  58      -1.916   1.573 -21.024  1.00 18.22           C  
ANISOU 3523  CA  VAL B  58     2126   2870   1927    108     97   -116       C  
ATOM   3524  C   VAL B  58      -1.732   2.840 -21.856  1.00 18.91           C  
ANISOU 3524  C   VAL B  58     2356   2855   1974     95    -44   -140       C  
ATOM   3525  O   VAL B  58      -1.410   3.897 -21.323  1.00 20.17           O  
ANISOU 3525  O   VAL B  58     2803   2883   1977     96   -253   -178       O  
ATOM   3526  CB  VAL B  58      -3.108   1.731 -20.042  1.00 20.20           C  
ANISOU 3526  CB  VAL B  58     2558   2558   2558      0      0      0       C  
ATOM   3527  CG1 VAL B  58      -4.370   2.211 -20.744  1.00 23.25           C  
ANISOU 3527  CG1 VAL B  58     2393   3810   2633    462     34    -80       C  
ATOM   3528  CG2 VAL B  58      -3.364   0.384 -19.390  1.00 21.39           C  
ANISOU 3528  CG2 VAL B  58     2195   3516   2415    -86    171    -18       C  
ATOM   3529  N   THR B  59      -1.994   2.704 -23.156  1.00 17.56           N  
ANISOU 3529  N   THR B  59     2074   2771   1828     66     84   -140       N  
ATOM   3530  CA  THR B  59      -1.943   3.835 -24.108  1.00 17.25           C  
ANISOU 3530  CA  THR B  59     1985   2659   1912    111      2   -171       C  
ATOM   3531  C   THR B  59      -2.931   3.516 -25.223  1.00 16.15           C  
ANISOU 3531  C   THR B  59     1991   2454   1691     67    109   -245       C  
ATOM   3532  O   THR B  59      -3.157   2.327 -25.487  1.00 17.14           O  
ANISOU 3532  O   THR B  59     2203   2458   1851     -2    165   -229       O  
ATOM   3533  CB  THR B  59      -0.505   4.074 -24.631  1.00 17.77           C  
ANISOU 3533  CB  THR B  59     1914   2661   2176    155     34   -329       C  
ATOM   3534  OG1 THR B  59      -0.363   5.346 -25.265  1.00 17.67           O  
ANISOU 3534  OG1 THR B  59     1822   2635   2257     -2     -5   -445       O  
ATOM   3535  CG2 THR B  59      -0.052   2.922 -25.535  1.00 18.63           C  
ANISOU 3535  CG2 THR B  59     1961   2652   2467    196    190   -386       C  
ATOM   3536  N   PRO B  60      -3.532   4.476 -25.900  1.00 15.27           N  
ANISOU 3536  N   PRO B  60     1748   2392   1663     39    114   -240       N  
ATOM   3537  CA  PRO B  60      -4.537   4.141 -26.926  1.00 14.93           C  
ANISOU 3537  CA  PRO B  60     1559   2315   1797    -59    162   -186       C  
ATOM   3538  C   PRO B  60      -3.998   3.295 -28.055  1.00 15.86           C  
ANISOU 3538  C   PRO B  60     1702   2453   1872    -44    181   -230       C  
ATOM   3539  O   PRO B  60      -2.922   3.552 -28.624  1.00 15.81           O  
ANISOU 3539  O   PRO B  60     1593   2694   1721     29    127   -304       O  
ATOM   3540  CB  PRO B  60      -5.074   5.510 -27.405  1.00 15.96           C  
ANISOU 3540  CB  PRO B  60     1765   2641   1657    206     38    -92       C  
ATOM   3541  CG  PRO B  60      -4.882   6.361 -26.172  1.00 16.30           C  
ANISOU 3541  CG  PRO B  60     1865   2456   1871     91     64   -108       C  
ATOM   3542  CD  PRO B  60      -3.527   5.902 -25.627  1.00 15.85           C  
ANISOU 3542  CD  PRO B  60     1832   2433   1758    119     69    -74       C  
ATOM   3543  N   LEU B  61      -4.773   2.264 -28.448  1.00 16.71           N  
ANISOU 3543  N   LEU B  61     1788   2598   1961   -146    321   -319       N  
ATOM   3544  CA  LEU B  61      -4.504   1.375 -29.576  1.00 16.75           C  
ANISOU 3544  CA  LEU B  61     1943   2393   2029   -124     93   -324       C  
ATOM   3545  C   LEU B  61      -5.537   1.596 -30.673  1.00 16.78           C  
ANISOU 3545  C   LEU B  61     1752   2567   2056    -64    102   -448       C  
ATOM   3546  O   LEU B  61      -6.674   2.061 -30.390  1.00 18.83           O  
ANISOU 3546  O   LEU B  61     1836   3061   2257    -16    146   -463       O  
ATOM   3547  CB ALEU B  61      -4.558  -0.074 -29.051  0.65 17.18           C  
ANISOU 3547  CB ALEU B  61     1911   2366   2252   -135   -112   -271       C  
ATOM   3548  CG ALEU B  61      -3.704  -0.427 -27.825  0.65 16.81           C  
ANISOU 3548  CG ALEU B  61     1974   2376   2038   -142     79    -94       C  
ATOM   3549  CD1ALEU B  61      -3.828  -1.884 -27.406  0.65 19.07           C  
ANISOU 3549  CD1ALEU B  61     2416   2461   2369   -242    -10    -17       C  
ATOM   3550  CD2ALEU B  61      -2.235  -0.133 -28.132  0.65 17.78           C  
ANISOU 3550  CD2ALEU B  61     1915   2433   2409   -162    -96    -80       C  
ATOM   3551  CB BLEU B  61      -4.404  -0.087 -29.176  0.35 18.74           C  
ANISOU 3551  CB BLEU B  61     2269   2447   2404    -62     34   -221       C  
ATOM   3552  CG BLEU B  61      -3.002  -0.651 -28.919  0.35 20.22           C  
ANISOU 3552  CG BLEU B  61     2434   2652   2598    102      5    -97       C  
ATOM   3553  CD1BLEU B  61      -2.301   0.026 -27.754  0.35 20.51           C  
ANISOU 3553  CD1BLEU B  61     2491   2716   2584      9     52   -106       C  
ATOM   3554  CD2BLEU B  61      -3.121  -2.143 -28.652  0.35 20.45           C  
ANISOU 3554  CD2BLEU B  61     2490   2624   2658     55     63   -171       C  
ATOM   3555  N   PRO B  62      -5.240   1.318 -31.946  1.00 16.94           N  
ANISOU 3555  N   PRO B  62     1559   2935   1944     48   -154   -441       N  
ATOM   3556  CA  PRO B  62      -3.967   0.824 -32.445  1.00 15.55           C  
ANISOU 3556  CA  PRO B  62     1499   2562   1846   -155   -119   -443       C  
ATOM   3557  C   PRO B  62      -2.875   1.896 -32.394  1.00 13.90           C  
ANISOU 3557  C   PRO B  62     1502   2222   1558    -22   -101   -213       C  
ATOM   3558  O   PRO B  62      -3.188   3.077 -32.418  1.00 14.76           O  
ANISOU 3558  O   PRO B  62     1407   2370   1830    -53     -1   -265       O  
ATOM   3559  CB  PRO B  62      -4.257   0.434 -33.931  1.00 16.81           C  
ANISOU 3559  CB  PRO B  62     1697   2749   1941   -161   -184   -534       C  
ATOM   3560  CG  PRO B  62      -5.348   1.400 -34.272  1.00 18.68           C  
ANISOU 3560  CG  PRO B  62     2092   3126   1879    123   -131   -417       C  
ATOM   3561  CD  PRO B  62      -6.217   1.563 -33.044  1.00 17.66           C  
ANISOU 3561  CD  PRO B  62     1802   3022   1886    105   -170   -520       C  
ATOM   3562  N   VAL B  63      -1.610   1.421 -32.394  1.00 14.32           N  
ANISOU 3562  N   VAL B  63     1373   2430   1637   -147   -104   -411       N  
ATOM   3563  CA  VAL B  63      -0.509   2.366 -32.174  1.00 13.77           C  
ANISOU 3563  CA  VAL B  63     1504   2255   1471   -148     -3   -309       C  
ATOM   3564  C   VAL B  63       0.779   1.992 -32.900  1.00 13.72           C  
ANISOU 3564  C   VAL B  63     1580   2085   1547   -128     16   -405       C  
ATOM   3565  O   VAL B  63       1.008   0.806 -33.163  1.00 13.72           O  
ANISOU 3565  O   VAL B  63     1468   2032   1711   -184     -3   -338       O  
ATOM   3566  CB  VAL B  63      -0.192   2.427 -30.626  1.00 14.07           C  
ANISOU 3566  CB  VAL B  63     1492   2332   1522   -132     21   -217       C  
ATOM   3567  CG1 VAL B  63       0.417   1.143 -30.102  1.00 14.35           C  
ANISOU 3567  CG1 VAL B  63     1516   2318   1617   -191    -42   -310       C  
ATOM   3568  CG2 VAL B  63       0.711   3.580 -30.233  1.00 13.65           C  
ANISOU 3568  CG2 VAL B  63     1580   2136   1469    -18     93   -297       C  
ATOM   3569  N   ILE B  64       1.599   2.989 -33.225  1.00 12.75           N  
ANISOU 3569  N   ILE B  64     1401   2062   1383    -14     11   -324       N  
ATOM   3570  CA  ILE B  64       2.985   2.782 -33.641  1.00 13.63           C  
ANISOU 3570  CA  ILE B  64     1404   2428   1349   -215     52   -204       C  
ATOM   3571  C   ILE B  64       3.856   3.106 -32.393  1.00 12.48           C  
ANISOU 3571  C   ILE B  64     1323   2100   1318    -79     80   -190       C  
ATOM   3572  O   ILE B  64       3.959   4.257 -31.983  1.00 12.72           O  
ANISOU 3572  O   ILE B  64     1502   2105   1225    -64    -42   -185       O  
ATOM   3573  CB  ILE B  64       3.409   3.610 -34.854  1.00 14.04           C  
ANISOU 3573  CB  ILE B  64     1462   2504   1367   -204     31   -195       C  
ATOM   3574  CG1 ILE B  64       2.585   3.151 -36.085  1.00 17.54           C  
ANISOU 3574  CG1 ILE B  64     1922   3172   1569   -115   -155   -215       C  
ATOM   3575  CG2 ILE B  64       4.908   3.459 -35.141  1.00 14.35           C  
ANISOU 3575  CG2 ILE B  64     1497   2490   1466    -25    149   -317       C  
ATOM   3576  CD1 ILE B  64       2.734   4.012 -37.318  1.00 18.03           C  
ANISOU 3576  CD1 ILE B  64     2232   3032   1589     80    -30   -330       C  
ATOM   3577  N   ALA B  65       4.417   2.062 -31.792  1.00 12.04           N  
ANISOU 3577  N   ALA B  65     1370   1922   1283   -215     61   -235       N  
ATOM   3578  CA  ALA B  65       5.273   2.206 -30.602  1.00 12.04           C  
ANISOU 3578  CA  ALA B  65     1232   2029   1314   -260     86   -174       C  
ATOM   3579  C   ALA B  65       6.697   2.572 -31.002  1.00 11.47           C  
ANISOU 3579  C   ALA B  65     1310   1893   1154   -126    167   -271       C  
ATOM   3580  O   ALA B  65       6.936   3.007 -32.160  1.00 12.59           O  
ANISOU 3580  O   ALA B  65     1406   2145   1232    -71    133   -134       O  
ATOM   3581  CB  ALA B  65       5.172   0.955 -29.749  1.00 13.48           C  
ANISOU 3581  CB  ALA B  65     1574   2113   1436   -116    -59   -143       C  
ATOM   3582  N   GLY B  66       7.645   2.450 -30.064  1.00 11.77           N  
ANISOU 3582  N   GLY B  66     1314   1923   1237   -153    109   -129       N  
ATOM   3583  CA  GLY B  66       9.024   2.854 -30.318  1.00 12.05           C  
ANISOU 3583  CA  GLY B  66     1476   1889   1212   -254    115    -29       C  
ATOM   3584  C   GLY B  66       9.279   4.242 -29.747  1.00 10.88           C  
ANISOU 3584  C   GLY B  66     1268   1728   1139    -94    138     49       C  
ATOM   3585  O   GLY B  66       8.566   5.210 -30.060  1.00 12.73           O  
ANISOU 3585  O   GLY B  66     1469   2088   1279    178    167     66       O  
ATOM   3586  N   HIS B  67      10.316   4.351 -28.906  1.00 11.51           N  
ANISOU 3586  N   HIS B  67     1333   1816   1224     37     92    -87       N  
ATOM   3587  CA  HIS B  67      10.696   5.597 -28.284  1.00 11.49           C  
ANISOU 3587  CA  HIS B  67     1332   1679   1352    122     -1    -77       C  
ATOM   3588  C   HIS B  67      12.195   5.817 -28.103  1.00 11.78           C  
ANISOU 3588  C   HIS B  67     1372   1668   1437     48    161   -234       C  
ATOM   3589  O   HIS B  67      12.588   6.910 -27.623  1.00 14.22           O  
ANISOU 3589  O   HIS B  67     1364   1820   2220    -22    255   -404       O  
ATOM   3590  CB  HIS B  67       9.979   5.760 -26.896  1.00 11.82           C  
ANISOU 3590  CB  HIS B  67     1382   1625   1482     36    129   -113       C  
ATOM   3591  CG  HIS B  67      10.402   4.729 -25.910  1.00 11.68           C  
ANISOU 3591  CG  HIS B  67     1418   1581   1438     78    169   -187       C  
ATOM   3592  ND1 HIS B  67      10.020   3.393 -25.978  1.00 11.57           N  
ANISOU 3592  ND1 HIS B  67     1248   1633   1515     59    252   -166       N  
ATOM   3593  CD2 HIS B  67      11.204   4.794 -24.809  1.00 12.78           C  
ANISOU 3593  CD2 HIS B  67     1306   1591   1960    131   -111   -113       C  
ATOM   3594  CE1 HIS B  67      10.593   2.720 -24.986  1.00 11.77           C  
ANISOU 3594  CE1 HIS B  67     1283   1575   1613      5     75   -282       C  
ATOM   3595  NE2 HIS B  67      11.317   3.543 -24.241  1.00 12.49           N  
ANISOU 3595  NE2 HIS B  67     1424   1606   1717    152   -121   -222       N  
ATOM   3596  N   GLU B  68      13.032   4.850 -28.423  1.00 10.36           N  
ANISOU 3596  N   GLU B  68     1248   1564   1124      2    153   -118       N  
ATOM   3597  CA  GLU B  68      14.508   4.908 -28.261  1.00 10.27           C  
ANISOU 3597  CA  GLU B  68     1329   1467   1106      5    128   -138       C  
ATOM   3598  C   GLU B  68      15.100   4.866 -29.682  1.00  9.93           C  
ANISOU 3598  C   GLU B  68     1195   1481   1095    -25     61   -133       C  
ATOM   3599  O   GLU B  68      15.111   3.772 -30.283  1.00 11.17           O  
ANISOU 3599  O   GLU B  68     1568   1541   1135     -1    164   -133       O  
ATOM   3600  CB  GLU B  68      14.943   3.697 -27.437  1.00 10.95           C  
ANISOU 3600  CB  GLU B  68     1391   1658   1112     69     97    -97       C  
ATOM   3601  CG  GLU B  68      16.438   3.609 -27.153  1.00 11.76           C  
ANISOU 3601  CG  GLU B  68     1424   1787   1256     18    201     19       C  
ATOM   3602  CD  GLU B  68      16.758   2.427 -26.246  1.00 12.55           C  
ANISOU 3602  CD  GLU B  68     1707   1730   1331    168    258    -59       C  
ATOM   3603  OE1 GLU B  68      16.934   1.296 -26.765  1.00 14.36           O  
ANISOU 3603  OE1 GLU B  68     2356   1696   1402     97    191    -88       O  
ATOM   3604  OE2 GLU B  68      16.782   2.616 -24.999  1.00 13.87           O  
ANISOU 3604  OE2 GLU B  68     2143   1946   1180    282     19    -71       O  
ATOM   3605  N   ALA B  69      15.520   5.981 -30.273  1.00 10.64           N  
ANISOU 3605  N   ALA B  69     1408   1589   1047     66    116    -73       N  
ATOM   3606  CA  ALA B  69      15.891   5.949 -31.710  1.00 10.28           C  
ANISOU 3606  CA  ALA B  69     1411   1495    999     92     88    -91       C  
ATOM   3607  C   ALA B  69      16.751   7.136 -32.085  1.00 10.56           C  
ANISOU 3607  C   ALA B  69     1315   1729    970     26     88    -77       C  
ATOM   3608  O   ALA B  69      16.937   8.102 -31.347  1.00 11.25           O  
ANISOU 3608  O   ALA B  69     1551   1632   1090   -113    244     14       O  
ATOM   3609  CB  ALA B  69      14.603   5.967 -32.549  1.00 10.85           C  
ANISOU 3609  CB  ALA B  69     1425   1601   1098     18     78   -111       C  
ATOM   3610  N   ALA B  70      17.237   7.077 -33.342  1.00 11.09           N  
ANISOU 3610  N   ALA B  70     1576   1604   1035    -18    198     30       N  
ATOM   3611  CA  ALA B  70      17.952   8.164 -33.965  1.00 11.77           C  
ANISOU 3611  CA  ALA B  70     1712   1716   1042    -85    189    -12       C  
ATOM   3612  C   ALA B  70      17.691   8.164 -35.479  1.00 11.31           C  
ANISOU 3612  C   ALA B  70     1464   1745   1088     50     94    -62       C  
ATOM   3613  O   ALA B  70      17.482   7.121 -36.076  1.00 12.42           O  
ANISOU 3613  O   ALA B  70     1802   1802   1116     12    196    -44       O  
ATOM   3614  CB  ALA B  70      19.441   8.190 -33.679  1.00 14.37           C  
ANISOU 3614  CB  ALA B  70     1808   2445   1207    -83    251    -85       C  
ATOM   3615  N   GLY B  71      17.658   9.352 -36.099  1.00 11.86           N  
ANISOU 3615  N   GLY B  71     1699   1765   1043     12    149    -54       N  
ATOM   3616  CA  GLY B  71      17.436   9.433 -37.542  1.00 12.18           C  
ANISOU 3616  CA  GLY B  71     1683   1824   1120    -37    143     17       C  
ATOM   3617  C   GLY B  71      17.893  10.765 -38.122  1.00 12.09           C  
ANISOU 3617  C   GLY B  71     1642   1843   1110   -122    227    -33       C  
ATOM   3618  O   GLY B  71      18.724  11.466 -37.526  1.00 12.42           O  
ANISOU 3618  O   GLY B  71     1702   1953   1065   -198    294    -44       O  
ATOM   3619  N   ILE B  72      17.405  11.055 -39.340  1.00 13.01           N  
ANISOU 3619  N   ILE B  72     1929   1935   1079   -101    195     60       N  
ATOM   3620  CA  ILE B  72      17.802  12.197 -40.146  1.00 12.51           C  
ANISOU 3620  CA  ILE B  72     1798   1894   1061    -99    196     51       C  
ATOM   3621  C   ILE B  72      16.564  12.999 -40.533  1.00 12.18           C  
ANISOU 3621  C   ILE B  72     1695   1910   1021   -172    269    109       C  
ATOM   3622  O   ILE B  72      15.589  12.425 -41.047  1.00 13.84           O  
ANISOU 3622  O   ILE B  72     1773   2163   1323   -173      5    -24       O  
ATOM   3623  CB  ILE B  72      18.610  11.779 -41.412  1.00 15.35           C  
ANISOU 3623  CB  ILE B  72     2153   2394   1286    152    473    225       C  
ATOM   3624  CG1 ILE B  72      19.906  11.039 -41.000  1.00 17.27           C  
ANISOU 3624  CG1 ILE B  72     2424   2607   1529    380    559    330       C  
ATOM   3625  CG2 ILE B  72      18.923  12.988 -42.298  1.00 15.65           C  
ANISOU 3625  CG2 ILE B  72     2247   2346   1355    -30    523     86       C  
ATOM   3626  CD1 ILE B  72      20.610  10.286 -42.118  1.00 20.59           C  
ANISOU 3626  CD1 ILE B  72     3080   2934   1809    296    805    175       C  
ATOM   3627  N   VAL B  73      16.557  14.306 -40.313  1.00 12.66           N  
ANISOU 3627  N   VAL B  73     1953   1902    954    -28    168    171       N  
ATOM   3628  CA  VAL B  73      15.398  15.118 -40.678  1.00 12.82           C  
ANISOU 3628  CA  VAL B  73     1866   2068    936    -24    173    156       C  
ATOM   3629  C   VAL B  73      15.134  15.124 -42.188  1.00 12.98           C  
ANISOU 3629  C   VAL B  73     1821   2095   1014     20    224    226       C  
ATOM   3630  O   VAL B  73      16.038  15.443 -42.986  1.00 14.26           O  
ANISOU 3630  O   VAL B  73     1928   2459   1030    -76    215    216       O  
ATOM   3631  CB  VAL B  73      15.563  16.574 -40.191  1.00 13.79           C  
ANISOU 3631  CB  VAL B  73     2252   2016    972     13     87    260       C  
ATOM   3632  CG1 VAL B  73      14.392  17.451 -40.599  1.00 13.53           C  
ANISOU 3632  CG1 VAL B  73     2001   2187    952     13     82     76       C  
ATOM   3633  CG2 VAL B  73      15.738  16.600 -38.661  1.00 14.53           C  
ANISOU 3633  CG2 VAL B  73     2156   2345   1019   -113     77    165       C  
ATOM   3634  N   GLU B  74      13.914  14.797 -42.583  1.00 14.13           N  
ANISOU 3634  N   GLU B  74     1965   2447    958   -144    231    137       N  
ATOM   3635  CA  GLU B  74      13.489  14.815 -43.999  1.00 14.23           C  
ANISOU 3635  CA  GLU B  74     1867   2493   1048    -20    150    102       C  
ATOM   3636  C   GLU B  74      12.865  16.158 -44.347  1.00 14.52           C  
ANISOU 3636  C   GLU B  74     2241   2379    897    -37    132     48       C  
ATOM   3637  O   GLU B  74      13.138  16.682 -45.443  1.00 16.66           O  
ANISOU 3637  O   GLU B  74     2504   2735   1092     -6    184    389       O  
ATOM   3638  CB  GLU B  74      12.518  13.648 -44.250  1.00 14.71           C  
ANISOU 3638  CB  GLU B  74     2097   2443   1049    -80    105    101       C  
ATOM   3639  CG  GLU B  74      11.816  13.666 -45.618  1.00 15.60           C  
ANISOU 3639  CG  GLU B  74     2174   2544   1208   -128     36    174       C  
ATOM   3640  CD  GLU B  74      10.503  14.406 -45.637  1.00 16.41           C  
ANISOU 3640  CD  GLU B  74     2138   2883   1212   -115      5     12       C  
ATOM   3641  OE1 GLU B  74       9.971  14.735 -44.534  1.00 15.68           O  
ANISOU 3641  OE1 GLU B  74     2072   2667   1218   -112     -1   -102       O  
ATOM   3642  OE2 GLU B  74       9.923  14.614 -46.741  1.00 18.12           O  
ANISOU 3642  OE2 GLU B  74     2394   3279   1214    -61    -39    166       O  
ATOM   3643  N   SER B  75      12.061  16.762 -43.472  1.00 14.45           N  
ANISOU 3643  N   SER B  75     2173   2300   1017     49     44     21       N  
ATOM   3644  CA  SER B  75      11.438  18.058 -43.747  1.00 14.51           C  
ANISOU 3644  CA  SER B  75     2185   2192   1136    -95     -7     -9       C  
ATOM   3645  C   SER B  75      10.940  18.664 -42.435  1.00 14.79           C  
ANISOU 3645  C   SER B  75     2296   2210   1115     16    154     85       C  
ATOM   3646  O   SER B  75      10.749  17.956 -41.403  1.00 15.18           O  
ANISOU 3646  O   SER B  75     2372   2320   1075    -98     95    115       O  
ATOM   3647  CB  SER B  75      10.274  17.953 -44.737  1.00 15.61           C  
ANISOU 3647  CB  SER B  75     2156   2456   1320     46    -73     65       C  
ATOM   3648  OG  SER B  75       9.141  17.234 -44.237  1.00 15.72           O  
ANISOU 3648  OG  SER B  75     2207   2497   1269    -71    -23     43       O  
ATOM   3649  N   ILE B  76      10.760  19.974 -42.434  1.00 15.27           N  
ANISOU 3649  N   ILE B  76     2389   2286   1126     48    131    165       N  
ATOM   3650  CA  ILE B  76      10.288  20.730 -41.278  1.00 15.22           C  
ANISOU 3650  CA  ILE B  76     2215   2353   1214    -31     84    151       C  
ATOM   3651  C   ILE B  76       9.063  21.549 -41.658  1.00 15.78           C  
ANISOU 3651  C   ILE B  76     2253   2508   1236    -34     -7    208       C  
ATOM   3652  O   ILE B  76       8.960  22.018 -42.813  1.00 17.98           O  
ANISOU 3652  O   ILE B  76     2623   2949   1258    207    -23    387       O  
ATOM   3653  CB  ILE B  76      11.371  21.654 -40.683  1.00 15.79           C  
ANISOU 3653  CB  ILE B  76     2316   2323   1359   -126     30    220       C  
ATOM   3654  CG1 ILE B  76      11.856  22.704 -41.691  1.00 16.48           C  
ANISOU 3654  CG1 ILE B  76     2430   2443   1387   -150    217    174       C  
ATOM   3655  CG2 ILE B  76      12.542  20.827 -40.159  1.00 15.50           C  
ANISOU 3655  CG2 ILE B  76     2203   2375   1312   -129    110    148       C  
ATOM   3656  CD1 ILE B  76      12.805  23.720 -41.072  1.00 17.55           C  
ANISOU 3656  CD1 ILE B  76     2563   2592   1514   -254    149    157       C  
ATOM   3657  N   GLY B  77       8.151  21.730 -40.707  1.00 16.39           N  
ANISOU 3657  N   GLY B  77     2316   2480   1430    125     99    369       N  
ATOM   3658  CA  GLY B  77       6.991  22.559 -40.859  1.00 17.70           C  
ANISOU 3658  CA  GLY B  77     2391   2858   1476    159   -206    143       C  
ATOM   3659  C   GLY B  77       7.349  24.016 -40.620  1.00 19.46           C  
ANISOU 3659  C   GLY B  77     2892   2845   1656     54   -250    142       C  
ATOM   3660  O   GLY B  77       8.469  24.416 -40.235  1.00 19.84           O  
ANISOU 3660  O   GLY B  77     3057   2650   1830    207   -405    192       O  
ATOM   3661  N   GLU B  78       6.323  24.838 -40.951  1.00 22.90           N  
ANISOU 3661  N   GLU B  78     3387   3218   2095    323   -405    215       N  
ATOM   3662  C   GLU B  78       6.827  26.548 -39.299  1.00 22.89           C  
ANISOU 3662  C   GLU B  78     3200   2934   2563    -56    -66    242       C  
ATOM   3663  O   GLU B  78       6.289  25.982 -38.338  1.00 22.63           O  
ANISOU 3663  O   GLU B  78     3177   3235   2188    -56   -103     27       O  
ATOM   3664  CA AGLU B  78       6.490  26.265 -40.765  0.62 25.88           C  
ANISOU 3664  CA AGLU B  78     3818   3375   2639   -106   -193    122       C  
ATOM   3665  CB AGLU B  78       5.172  26.973 -41.104  0.62 32.32           C  
ANISOU 3665  CB AGLU B  78     3979   4720   3583    243   -192     58       C  
ATOM   3666  CG AGLU B  78       5.276  28.475 -41.271  0.62 40.22           C  
ANISOU 3666  CG AGLU B  78     5550   5006   4724   -159    121    262       C  
ATOM   3667  CD AGLU B  78       3.946  29.072 -41.707  0.62 45.01           C  
ANISOU 3667  CD AGLU B  78     5680   5922   5500     40    117    488       C  
ATOM   3668  OE1AGLU B  78       3.330  28.518 -42.637  0.62 45.96           O  
ANISOU 3668  OE1AGLU B  78     5915   5925   5621     34    109    383       O  
ATOM   3669  OE2AGLU B  78       3.541  30.084 -41.099  0.62 45.95           O  
ANISOU 3669  OE2AGLU B  78     5872   5996   5592     21    102    388       O  
ATOM   3670  CA BGLU B  78       6.395  26.273 -40.741  0.38 25.83           C  
ANISOU 3670  CA BGLU B  78     3812   3328   2675    -72   -213    158       C  
ATOM   3671  CB BGLU B  78       5.024  26.938 -40.940  0.38 32.13           C  
ANISOU 3671  CB BGLU B  78     3970   4567   3670    185   -209    311       C  
ATOM   3672  CG BGLU B  78       4.974  28.414 -40.575  0.38 39.20           C  
ANISOU 3672  CG BGLU B  78     5344   4707   4843      9   -216    220       C  
ATOM   3673  CD BGLU B  78       3.776  28.769 -39.714  0.38 43.70           C  
ANISOU 3673  CD BGLU B  78     5768   5288   5550    116    211    222       C  
ATOM   3674  OE1BGLU B  78       2.635  28.750 -40.223  0.38 44.36           O  
ANISOU 3674  OE1BGLU B  78     5894   5421   5539    116    119    206       O  
ATOM   3675  OE2BGLU B  78       3.993  29.056 -38.513  0.38 44.16           O  
ANISOU 3675  OE2BGLU B  78     5784   5345   5650     78    107    182       O  
ATOM   3676  N   GLY B  79       7.732  27.474 -39.127  1.00 19.77           N  
ANISOU 3676  N   GLY B  79     2941   2592   1978    190    -95    312       N  
ATOM   3677  CA  GLY B  79       8.079  27.965 -37.808  1.00 17.92           C  
ANISOU 3677  CA  GLY B  79     2620   2115   2074     91   -171    216       C  
ATOM   3678  C   GLY B  79       9.192  27.237 -37.096  1.00 16.61           C  
ANISOU 3678  C   GLY B  79     2490   2057   1765     18    -95    146       C  
ATOM   3679  O   GLY B  79       9.606  27.724 -36.019  1.00 18.71           O  
ANISOU 3679  O   GLY B  79     3072   2199   1839   -141   -122    -53       O  
ATOM   3680  N   VAL B  80       9.668  26.100 -37.560  1.00 15.61           N  
ANISOU 3680  N   VAL B  80     2381   1992   1556    -13   -211    146       N  
ATOM   3681  CA  VAL B  80      10.737  25.324 -36.912  1.00 14.47           C  
ANISOU 3681  CA  VAL B  80     2072   1980   1447   -140   -167     96       C  
ATOM   3682  C   VAL B  80      12.060  26.039 -37.018  1.00 14.98           C  
ANISOU 3682  C   VAL B  80     2138   2174   1378   -168    108     76       C  
ATOM   3683  O   VAL B  80      12.443  26.487 -38.109  1.00 17.03           O  
ANISOU 3683  O   VAL B  80     2537   2553   1381   -391     44    235       O  
ATOM   3684  CB  VAL B  80      10.836  23.913 -37.507  1.00 13.77           C  
ANISOU 3684  CB  VAL B  80     2002   1988   1243   -133     41    135       C  
ATOM   3685  CG1 VAL B  80      12.077  23.168 -37.043  1.00 14.70           C  
ANISOU 3685  CG1 VAL B  80     2136   2105   1343    -76     75    249       C  
ATOM   3686  CG2 VAL B  80       9.582  23.103 -37.213  1.00 13.88           C  
ANISOU 3686  CG2 VAL B  80     2055   1860   1357   -157     -5    103       C  
ATOM   3687  N   THR B  81      12.765  26.155 -35.892  1.00 15.05           N  
ANISOU 3687  N   THR B  81     2282   1973   1463   -317    -44    154       N  
ATOM   3688  CA  THR B  81      14.038  26.880 -35.828  1.00 16.10           C  
ANISOU 3688  CA  THR B  81     2295   2271   1551   -270    -54    170       C  
ATOM   3689  C   THR B  81      15.206  26.078 -35.277  1.00 16.49           C  
ANISOU 3689  C   THR B  81     2259   2467   1539   -149    -43     54       C  
ATOM   3690  O   THR B  81      16.345  26.579 -35.314  1.00 21.09           O  
ANISOU 3690  O   THR B  81     2545   3139   2327   -483     24    236       O  
ATOM   3691  CB  THR B  81      13.899  28.172 -34.975  1.00 17.61           C  
ANISOU 3691  CB  THR B  81     2603   2345   1742   -251    -31     98       C  
ATOM   3692  OG1 THR B  81      13.470  27.788 -33.656  1.00 17.94           O  
ANISOU 3692  OG1 THR B  81     2903   2347   1568   -356    -82    -27       O  
ATOM   3693  CG2 THR B  81      12.933  29.161 -35.606  1.00 18.54           C  
ANISOU 3693  CG2 THR B  81     2956   2115   1975   -263   -168      4       C  
ATOM   3694  N   THR B  82      14.987  24.897 -34.695  1.00 16.37           N  
ANISOU 3694  N   THR B  82     2462   2361   1395     25     11     49       N  
ATOM   3695  CA  THR B  82      15.996  24.149 -33.979  1.00 16.25           C  
ANISOU 3695  CA  THR B  82     2229   2541   1406     34    129     -6       C  
ATOM   3696  C   THR B  82      16.653  23.009 -34.706  1.00 15.39           C  
ANISOU 3696  C   THR B  82     1975   2372   1500    -60     99     31       C  
ATOM   3697  O   THR B  82      17.667  22.451 -34.274  1.00 16.18           O  
ANISOU 3697  O   THR B  82     2066   2509   1573     70     78    -50       O  
ATOM   3698  CB  THR B  82      15.435  23.654 -32.596  1.00 16.22           C  
ANISOU 3698  CB  THR B  82     2527   2355   1280    118     43    101       C  
ATOM   3699  OG1 THR B  82      14.379  22.715 -32.766  1.00 17.33           O  
ANISOU 3699  OG1 THR B  82     2404   2868   1311    -61     73    307       O  
ATOM   3700  CG2 THR B  82      15.029  24.847 -31.741  1.00 19.81           C  
ANISOU 3700  CG2 THR B  82     2943   2946   1636    302     71   -217       C  
ATOM   3701  N   VAL B  83      16.100  22.599 -35.837  1.00 15.13           N  
ANISOU 3701  N   VAL B  83     2039   2284   1425   -181    127    -23       N  
ATOM   3702  CA  VAL B  83      16.612  21.553 -36.707  1.00 15.10           C  
ANISOU 3702  CA  VAL B  83     2064   2288   1384     38    158     98       C  
ATOM   3703  C   VAL B  83      16.347  21.970 -38.168  1.00 15.21           C  
ANISOU 3703  C   VAL B  83     2248   2156   1373     76    141     80       C  
ATOM   3704  O   VAL B  83      15.439  22.788 -38.414  1.00 15.65           O  
ANISOU 3704  O   VAL B  83     2366   2229   1350    107    207    132       O  
ATOM   3705  CB  VAL B  83      16.011  20.164 -36.398  1.00 14.93           C  
ANISOU 3705  CB  VAL B  83     2132   2180   1359     72     86     39       C  
ATOM   3706  CG1 VAL B  83      16.221  19.682 -34.951  1.00 17.38           C  
ANISOU 3706  CG1 VAL B  83     2346   2819   1438    197    -27    203       C  
ATOM   3707  CG2 VAL B  83      14.521  20.110 -36.709  1.00 16.38           C  
ANISOU 3707  CG2 VAL B  83     2176   2470   1577   -136    111     89       C  
ATOM   3708  N   ARG B  84      17.079  21.369 -39.095  1.00 16.12           N  
ANISOU 3708  N   ARG B  84     2480   2304   1339     12    232     99       N  
ATOM   3709  CA  ARG B  84      16.914  21.591 -40.528  1.00 16.01           C  
ANISOU 3709  CA  ARG B  84     2591   2205   1287    -51    172    149       C  
ATOM   3710  C   ARG B  84      16.990  20.254 -41.259  1.00 15.44           C  
ANISOU 3710  C   ARG B  84     2406   2131   1329    -21    239    202       C  
ATOM   3711  O   ARG B  84      17.616  19.295 -40.770  1.00 14.93           O  
ANISOU 3711  O   ARG B  84     2235   2360   1080    -89    185    163       O  
ATOM   3712  CB AARG B  84      18.104  22.419 -41.077  0.51 19.12           C  
ANISOU 3712  CB AARG B  84     2814   2769   1681   -251    280    204       C  
ATOM   3713  CG AARG B  84      18.121  23.859 -40.613  0.51 22.85           C  
ANISOU 3713  CG AARG B  84     3618   3054   2010    -18     72   -163       C  
ATOM   3714  CD AARG B  84      19.398  24.591 -41.008  0.51 29.75           C  
ANISOU 3714  CD AARG B  84     3808   4311   3183   -264    181    256       C  
ATOM   3715  NE AARG B  84      19.361  25.917 -40.379  0.51 35.18           N  
ANISOU 3715  NE AARG B  84     4823   4553   3989     84     32     12       N  
ATOM   3716  CZ AARG B  84      20.337  26.809 -40.334  0.51 38.26           C  
ANISOU 3716  CZ AARG B  84     4978   5080   4478   -155   -116    134       C  
ATOM   3717  NH1AARG B  84      21.522  26.584 -40.877  0.51 37.76           N  
ANISOU 3717  NH1AARG B  84     5080   4944   4325   -164    -64     22       N  
ATOM   3718  NH2AARG B  84      20.109  27.960 -39.713  0.51 39.69           N  
ANISOU 3718  NH2AARG B  84     5180   5167   4732    -63    -72     75       N  
ATOM   3719  CB BARG B  84      17.882  22.596 -41.137  0.49 16.94           C  
ANISOU 3719  CB BARG B  84     2599   2188   1649   -105    219    129       C  
ATOM   3720  CG BARG B  84      19.305  22.124 -41.341  0.49 18.55           C  
ANISOU 3720  CG BARG B  84     2644   2136   2268     38     71     51       C  
ATOM   3721  CD BARG B  84      20.079  23.181 -42.123  0.49 20.99           C  
ANISOU 3721  CD BARG B  84     2886   2480   2609    -54    173    248       C  
ATOM   3722  NE BARG B  84      21.438  22.838 -42.561  0.49 21.70           N  
ANISOU 3722  NE BARG B  84     2806   2347   3092    -70    167    230       N  
ATOM   3723  CZ BARG B  84      22.384  22.550 -41.657  0.49 23.50           C  
ANISOU 3723  CZ BARG B  84     2993   2922   3015   -135     66    140       C  
ATOM   3724  NH1BARG B  84      22.063  22.520 -40.373  0.49 25.11           N  
ANISOU 3724  NH1BARG B  84     3158   3371   3012    -54    114    281       N  
ATOM   3725  NH2BARG B  84      23.641  22.226 -41.948  0.49 23.74           N  
ANISOU 3725  NH2BARG B  84     2959   2743   3318   -274    170    318       N  
ATOM   3726  N   PRO B  85      16.462  20.178 -42.483  1.00 15.11           N  
ANISOU 3726  N   PRO B  85     2426   2011   1303      3    166    186       N  
ATOM   3727  CA  PRO B  85      16.578  18.962 -43.291  1.00 14.41           C  
ANISOU 3727  CA  PRO B  85     2175   2147   1154    -38    107    193       C  
ATOM   3728  C   PRO B  85      18.031  18.511 -43.410  1.00 13.64           C  
ANISOU 3728  C   PRO B  85     2041   1948   1193   -162    243    138       C  
ATOM   3729  O   PRO B  85      18.964  19.323 -43.617  1.00 14.74           O  
ANISOU 3729  O   PRO B  85     2184   2148   1269   -318    219    257       O  
ATOM   3730  CB  PRO B  85      15.974  19.339 -44.666  1.00 16.13           C  
ANISOU 3730  CB  PRO B  85     2686   2237   1205    -20     56    327       C  
ATOM   3731  CG  PRO B  85      15.006  20.434 -44.284  1.00 16.91           C  
ANISOU 3731  CG  PRO B  85     2482   2350   1594    -41     -2    326       C  
ATOM   3732  CD  PRO B  85      15.691  21.220 -43.170  1.00 15.83           C  
ANISOU 3732  CD  PRO B  85     2340   2249   1426    112    149    207       C  
ATOM   3733  N   GLY B  86      18.274  17.211 -43.206  1.00 14.23           N  
ANISOU 3733  N   GLY B  86     2183   2148   1074     65    169    241       N  
ATOM   3734  CA  GLY B  86      19.595  16.596 -43.255  1.00 14.41           C  
ANISOU 3734  CA  GLY B  86     2095   2265   1113    -11    272    311       C  
ATOM   3735  C   GLY B  86      20.261  16.461 -41.898  1.00 14.73           C  
ANISOU 3735  C   GLY B  86     2182   2264   1149    -84    227    170       C  
ATOM   3736  O   GLY B  86      21.283  15.742 -41.779  1.00 15.35           O  
ANISOU 3736  O   GLY B  86     2256   2316   1262      5    354    258       O  
ATOM   3737  N   ASP B  87      19.765  17.123 -40.851  1.00 13.86           N  
ANISOU 3737  N   ASP B  87     1940   2170   1157    -31    225    214       N  
ATOM   3738  CA  ASP B  87      20.352  17.010 -39.514  1.00 14.31           C  
ANISOU 3738  CA  ASP B  87     2163   2123   1149    -11     89    241       C  
ATOM   3739  C   ASP B  87      20.131  15.620 -38.902  1.00 12.90           C  
ANISOU 3739  C   ASP B  87     1788   2083   1029    -97    150     69       C  
ATOM   3740  O   ASP B  87      19.058  15.062 -39.051  1.00 13.69           O  
ANISOU 3740  O   ASP B  87     1833   2137   1232   -117     57    162       O  
ATOM   3741  CB  ASP B  87      19.811  18.048 -38.535  1.00 14.79           C  
ANISOU 3741  CB  ASP B  87     2311   2039   1269    -78     -1    166       C  
ATOM   3742  CG  ASP B  87      20.233  19.497 -38.743  1.00 16.20           C  
ANISOU 3742  CG  ASP B  87     2335   2151   1669   -133    131    201       C  
ATOM   3743  OD1 ASP B  87      21.222  19.706 -39.486  1.00 17.69           O  
ANISOU 3743  OD1 ASP B  87     2512   2320   1889   -296    201    286       O  
ATOM   3744  OD2 ASP B  87      19.564  20.372 -38.150  1.00 16.58           O  
ANISOU 3744  OD2 ASP B  87     2579   2129   1592    -93   -133     45       O  
ATOM   3745  N   LYS B  88      21.146  15.148 -38.165  1.00 12.56           N  
ANISOU 3745  N   LYS B  88     1677   1929   1164    -55    252    209       N  
ATOM   3746  CA  LYS B  88      20.954  13.969 -37.316  1.00 12.66           C  
ANISOU 3746  CA  LYS B  88     1707   2011   1094    -46    292    272       C  
ATOM   3747  C   LYS B  88      20.230  14.407 -36.028  1.00 12.28           C  
ANISOU 3747  C   LYS B  88     1809   1701   1154   -136    217     44       C  
ATOM   3748  O   LYS B  88      20.517  15.473 -35.481  1.00 12.19           O  
ANISOU 3748  O   LYS B  88     1695   1810   1126   -142    258    126       O  
ATOM   3749  CB  LYS B  88      22.298  13.326 -36.983  1.00 12.45           C  
ANISOU 3749  CB  LYS B  88     1786   1839   1106    -89    262    167       C  
ATOM   3750  CG  LYS B  88      22.931  12.588 -38.158  1.00 13.33           C  
ANISOU 3750  CG  LYS B  88     1871   2085   1109    -25    312    186       C  
ATOM   3751  CD  LYS B  88      24.261  11.949 -37.852  1.00 14.38           C  
ANISOU 3751  CD  LYS B  88     1794   2226   1442    -95    204    100       C  
ATOM   3752  CE  LYS B  88      24.756  11.097 -39.021  1.00 15.45           C  
ANISOU 3752  CE  LYS B  88     1884   2545   1441     66    231    202       C  
ATOM   3753  NZ  LYS B  88      26.158  10.613 -38.781  1.00 16.09           N  
ANISOU 3753  NZ  LYS B  88     1975   2518   1621    154    325     80       N  
ATOM   3754  N   VAL B  89      19.250  13.607 -35.599  1.00 12.07           N  
ANISOU 3754  N   VAL B  89     1758   1797   1032   -121    214     42       N  
ATOM   3755  CA  VAL B  89      18.384  13.907 -34.467  1.00 11.71           C  
ANISOU 3755  CA  VAL B  89     1717   1688   1044     15    207     47       C  
ATOM   3756  C   VAL B  89      18.020  12.671 -33.663  1.00 10.76           C  
ANISOU 3756  C   VAL B  89     1546   1617    924     -5    101     24       C  
ATOM   3757  O   VAL B  89      18.030  11.543 -34.156  1.00 11.85           O  
ANISOU 3757  O   VAL B  89     1885   1670    947   -103    318      5       O  
ATOM   3758  CB  VAL B  89      17.059  14.577 -34.932  1.00 12.38           C  
ANISOU 3758  CB  VAL B  89     1785   1868   1050      0    156     44       C  
ATOM   3759  CG1 VAL B  89      17.266  15.992 -35.468  1.00 13.36           C  
ANISOU 3759  CG1 VAL B  89     1952   1938   1187    -48    120    153       C  
ATOM   3760  CG2 VAL B  89      16.322  13.723 -35.960  1.00 13.81           C  
ANISOU 3760  CG2 VAL B  89     1873   2116   1256    -12    -27    108       C  
ATOM   3761  N   ILE B  90      17.685  12.926 -32.395  1.00 11.18           N  
ANISOU 3761  N   ILE B  90     1634   1611   1002   -123    287     55       N  
ATOM   3762  CA  ILE B  90      17.112  11.923 -31.475  1.00 10.73           C  
ANISOU 3762  CA  ILE B  90     1571   1501   1005    -24    135     93       C  
ATOM   3763  C   ILE B  90      15.742  12.423 -31.022  1.00 10.45           C  
ANISOU 3763  C   ILE B  90     1493   1551    927    -47    127     45       C  
ATOM   3764  O   ILE B  90      15.630  13.515 -30.442  1.00 11.46           O  
ANISOU 3764  O   ILE B  90     1599   1679   1078    -62     71    -59       O  
ATOM   3765  CB  ILE B  90      18.058  11.653 -30.265  1.00 10.87           C  
ANISOU 3765  CB  ILE B  90     1343   1662   1127     14    124    171       C  
ATOM   3766  CG1 ILE B  90      19.307  10.906 -30.776  1.00 12.02           C  
ANISOU 3766  CG1 ILE B  90     1567   1891   1109    117    109     71       C  
ATOM   3767  CG2 ILE B  90      17.345  10.862 -29.158  1.00 11.00           C  
ANISOU 3767  CG2 ILE B  90     1440   1698   1041     14    125    187       C  
ATOM   3768  CD1 ILE B  90      20.402  10.704 -29.729  1.00 13.08           C  
ANISOU 3768  CD1 ILE B  90     1690   2003   1277     77     67    170       C  
ATOM   3769  N   PRO B  91      14.669  11.667 -31.250  1.00 10.50           N  
ANISOU 3769  N   PRO B  91     1351   1683    955      7    109     38       N  
ATOM   3770  CA  PRO B  91      13.331  11.991 -30.702  1.00 10.92           C  
ANISOU 3770  CA  PRO B  91     1353   1729   1068     13    126     48       C  
ATOM   3771  C   PRO B  91      13.349  11.943 -29.177  1.00 10.86           C  
ANISOU 3771  C   PRO B  91     1498   1513   1116     89    148    147       C  
ATOM   3772  O   PRO B  91      14.045  11.070 -28.599  1.00 11.01           O  
ANISOU 3772  O   PRO B  91     1621   1604    958    141    222    108       O  
ATOM   3773  CB  PRO B  91      12.375  10.924 -31.284  1.00 13.70           C  
ANISOU 3773  CB  PRO B  91     1695   2231   1279    -70     57   -251       C  
ATOM   3774  CG  PRO B  91      13.142  10.307 -32.418  1.00 14.58           C  
ANISOU 3774  CG  PRO B  91     1738   2142   1659      3    237   -315       C  
ATOM   3775  CD  PRO B  91      14.620  10.422 -32.047  1.00 12.97           C  
ANISOU 3775  CD  PRO B  91     1721   1903   1302    129     83   -183       C  
ATOM   3776  N   LEU B  92      12.590  12.818 -28.521  1.00 10.14           N  
ANISOU 3776  N   LEU B  92     1338   1641    873     77     32     73       N  
ATOM   3777  CA  LEU B  92      12.562  12.960 -27.061  1.00 10.34           C  
ANISOU 3777  CA  LEU B  92     1521   1525    881     42     46      1       C  
ATOM   3778  C   LEU B  92      11.201  12.511 -26.515  1.00 10.17           C  
ANISOU 3778  C   LEU B  92     1477   1398    991    132     39    -36       C  
ATOM   3779  O   LEU B  92      10.208  13.228 -26.699  1.00 11.85           O  
ANISOU 3779  O   LEU B  92     1571   1761   1169    244    107    254       O  
ATOM   3780  CB  LEU B  92      12.823  14.424 -26.688  1.00 10.64           C  
ANISOU 3780  CB  LEU B  92     1478   1567    998     18     41    116       C  
ATOM   3781  CG  LEU B  92      14.097  15.039 -27.299  1.00 10.95           C  
ANISOU 3781  CG  LEU B  92     1536   1593   1030    -20     89      9       C  
ATOM   3782  CD1 LEU B  92      14.151  16.530 -26.948  1.00 12.01           C  
ANISOU 3782  CD1 LEU B  92     1943   1617   1005     -1    123     72       C  
ATOM   3783  CD2 LEU B  92      15.349  14.321 -26.873  1.00 12.07           C  
ANISOU 3783  CD2 LEU B  92     1628   1722   1234     56    154     65       C  
ATOM   3784  N   PHE B  93      11.134  11.351 -25.875  1.00 10.12           N  
ANISOU 3784  N   PHE B  93     1439   1455    951    151    103     23       N  
ATOM   3785  CA  PHE B  93       9.848  10.857 -25.347  1.00 10.42           C  
ANISOU 3785  CA  PHE B  93     1269   1616   1074     80    -26     15       C  
ATOM   3786  C   PHE B  93       9.378  11.699 -24.148  1.00 10.51           C  
ANISOU 3786  C   PHE B  93     1347   1733    912     40     33    173       C  
ATOM   3787  O   PHE B  93       8.161  11.735 -23.869  1.00 12.12           O  
ANISOU 3787  O   PHE B  93     1518   1912   1177    181    127     76       O  
ATOM   3788  CB  PHE B  93       9.883   9.373 -25.036  1.00 10.93           C  
ANISOU 3788  CB  PHE B  93     1499   1563   1090    166      4     16       C  
ATOM   3789  CG  PHE B  93      10.607   8.917 -23.795  1.00 10.42           C  
ANISOU 3789  CG  PHE B  93     1384   1548   1026     57     48    115       C  
ATOM   3790  CD1 PHE B  93      10.003   9.021 -22.527  1.00 10.40           C  
ANISOU 3790  CD1 PHE B  93     1271   1565   1117     92     91     47       C  
ATOM   3791  CD2 PHE B  93      11.878   8.390 -23.856  1.00 11.10           C  
ANISOU 3791  CD2 PHE B  93     1404   1499   1315    105     44     68       C  
ATOM   3792  CE1 PHE B  93      10.680   8.621 -21.382  1.00 11.13           C  
ANISOU 3792  CE1 PHE B  93     1469   1654   1107    125     13     95       C  
ATOM   3793  CE2 PHE B  93      12.566   7.995 -22.722  1.00 11.87           C  
ANISOU 3793  CE2 PHE B  93     1398   1709   1403    161     12     95       C  
ATOM   3794  CZ  PHE B  93      11.959   8.091 -21.476  1.00 11.74           C  
ANISOU 3794  CZ  PHE B  93     1492   1639   1329    124   -155     83       C  
ATOM   3795  N   THR B  94      10.296  12.377 -23.471  1.00 10.89           N  
ANISOU 3795  N   THR B  94     1518   1604   1015     65     43    -16       N  
ATOM   3796  CA  THR B  94       9.970  13.440 -22.513  1.00 11.89           C  
ANISOU 3796  CA  THR B  94     1813   1706   1000    121     69    -17       C  
ATOM   3797  C   THR B  94      10.234  14.753 -23.228  1.00 11.06           C  
ANISOU 3797  C   THR B  94     1579   1528   1095    112     35   -198       C  
ATOM   3798  O   THR B  94      11.421  14.997 -23.550  1.00 11.97           O  
ANISOU 3798  O   THR B  94     1551   1832   1167     75    112     21       O  
ATOM   3799  CB  THR B  94      10.806  13.306 -21.209  1.00 13.31           C  
ANISOU 3799  CB  THR B  94     2313   1633   1111    111   -129    -26       C  
ATOM   3800  OG1 THR B  94      10.613  11.998 -20.653  1.00 15.35           O  
ANISOU 3800  OG1 THR B  94     2810   1844   1180     28   -134    157       O  
ATOM   3801  CG2 THR B  94      10.397  14.372 -20.206  1.00 15.34           C  
ANISOU 3801  CG2 THR B  94     2884   1931   1015     95   -104   -152       C  
ATOM   3802  N   PRO B  95       9.266  15.602 -23.509  1.00 12.06           N  
ANISOU 3802  N   PRO B  95     1788   1768   1029    281     77      8       N  
ATOM   3803  CA  PRO B  95       9.532  16.855 -24.225  1.00 12.40           C  
ANISOU 3803  CA  PRO B  95     1825   1876   1012    144     39     99       C  
ATOM   3804  C   PRO B  95      10.301  17.846 -23.358  1.00 11.89           C  
ANISOU 3804  C   PRO B  95     1933   1550   1033    320     47    109       C  
ATOM   3805  O   PRO B  95      10.447  17.659 -22.128  1.00 12.58           O  
ANISOU 3805  O   PRO B  95     2014   1755   1012    328    -26    140       O  
ATOM   3806  CB  PRO B  95       8.170  17.429 -24.616  1.00 14.28           C  
ANISOU 3806  CB  PRO B  95     2171   1878   1375    335   -255     34       C  
ATOM   3807  CG  PRO B  95       7.164  16.476 -24.086  1.00 16.78           C  
ANISOU 3807  CG  PRO B  95     2192   2319   1864    463     40    386       C  
ATOM   3808  CD  PRO B  95       7.836  15.444 -23.217  1.00 13.45           C  
ANISOU 3808  CD  PRO B  95     1778   2088   1246    322    -64    -21       C  
ATOM   3809  N   GLN B  96      10.726  18.958 -23.957  1.00 12.53           N  
ANISOU 3809  N   GLN B  96     2121   1626   1013    166     76     32       N  
ATOM   3810  CA  GLN B  96      11.254  20.099 -23.201  1.00 12.91           C  
ANISOU 3810  CA  GLN B  96     2199   1666   1040    238    -12    -11       C  
ATOM   3811  C   GLN B  96      10.754  21.397 -23.860  1.00 14.28           C  
ANISOU 3811  C   GLN B  96     2484   1770   1172    243     29    -42       C  
ATOM   3812  O   GLN B  96      11.394  21.951 -24.777  1.00 15.77           O  
ANISOU 3812  O   GLN B  96     2939   1864   1189    369     29    192       O  
ATOM   3813  CB  GLN B  96      12.773  20.131 -23.071  1.00 12.56           C  
ANISOU 3813  CB  GLN B  96     2205   1464   1104    245    200    -44       C  
ATOM   3814  CG  GLN B  96      13.268  21.224 -22.137  1.00 13.62           C  
ANISOU 3814  CG  GLN B  96     2220   1772   1182    167    -18    -96       C  
ATOM   3815  CD  GLN B  96      14.743  21.242 -21.887  1.00 13.40           C  
ANISOU 3815  CD  GLN B  96     2270   1588   1235     99   -123     82       C  
ATOM   3816  OE1 GLN B  96      15.509  20.366 -22.321  1.00 13.89           O  
ANISOU 3816  OE1 GLN B  96     2251   1694   1332    131     -6     91       O  
ATOM   3817  NE2 GLN B  96      15.179  22.227 -21.089  1.00 14.58           N  
ANISOU 3817  NE2 GLN B  96     2319   1733   1488    114    -96    -98       N  
ATOM   3818  N   CYS B  97       9.588  21.895 -23.429  1.00 14.87           N  
ANISOU 3818  N   CYS B  97     2466   2107   1076    536   -276    -51       N  
ATOM   3819  CA  CYS B  97       9.040  23.118 -24.057  1.00 16.29           C  
ANISOU 3819  CA  CYS B  97     2838   2123   1230    458   -390     87       C  
ATOM   3820  C   CYS B  97       9.865  24.343 -23.716  1.00 17.16           C  
ANISOU 3820  C   CYS B  97     3036   2048   1435    370   -378    140       C  
ATOM   3821  O   CYS B  97       9.803  25.382 -24.453  1.00 19.49           O  
ANISOU 3821  O   CYS B  97     3669   2174   1562    577   -234    256       O  
ATOM   3822  CB  CYS B  97       7.568  23.249 -23.722  1.00 17.97           C  
ANISOU 3822  CB  CYS B  97     2989   2586   1252    609   -262     99       C  
ATOM   3823  SG  CYS B  97       7.111  23.925 -22.084  1.00 17.68           S  
ANISOU 3823  SG  CYS B  97     2972   2330   1415   1082   -447   -129       S  
ATOM   3824  N   GLY B  98      10.483  24.375 -22.538  1.00 17.09           N  
ANISOU 3824  N   GLY B  98     3002   2152   1340    312   -224    -13       N  
ATOM   3825  CA  GLY B  98      11.268  25.533 -22.122  1.00 18.23           C  
ANISOU 3825  CA  GLY B  98     3437   2132   1356     77    -56     40       C  
ATOM   3826  C   GLY B  98      10.492  26.655 -21.450  1.00 19.00           C  
ANISOU 3826  C   GLY B  98     3323   2304   1592    100   -140      0       C  
ATOM   3827  O   GLY B  98      11.114  27.652 -21.042  1.00 21.85           O  
ANISOU 3827  O   GLY B  98     3744   2243   2314     51   -190   -215       O  
ATOM   3828  N   LYS B  99       9.177  26.523 -21.388  1.00 17.83           N  
ANISOU 3828  N   LYS B  99     3215   1923   1637    360     24    197       N  
ATOM   3829  CA  LYS B  99       8.308  27.637 -20.970  1.00 22.62           C  
ANISOU 3829  CA  LYS B  99     3524   2452   2619    543    226    -62       C  
ATOM   3830  C   LYS B  99       7.406  27.302 -19.790  1.00 21.93           C  
ANISOU 3830  C   LYS B  99     3452   2354   2528    594    120     35       C  
ATOM   3831  O   LYS B  99       6.879  28.241 -19.158  1.00 24.43           O  
ANISOU 3831  O   LYS B  99     3984   2606   2692    626    244   -118       O  
ATOM   3832  CB ALYS B  99       7.536  28.167 -22.201  0.51 23.58           C  
ANISOU 3832  CB ALYS B  99     3448   2677   2834    473    163    115       C  
ATOM   3833  CG ALYS B  99       8.414  28.822 -23.266  0.51 25.28           C  
ANISOU 3833  CG ALYS B  99     3447   3124   3035    334    273     88       C  
ATOM   3834  CD ALYS B  99       7.707  29.187 -24.554  0.51 27.05           C  
ANISOU 3834  CD ALYS B  99     3586   3467   3226    238     77     99       C  
ATOM   3835  CE ALYS B  99       8.579  30.089 -25.430  0.51 28.69           C  
ANISOU 3835  CE ALYS B  99     3733   3696   3473    102    226     78       C  
ATOM   3836  NZ ALYS B  99       7.882  30.469 -26.693  0.51 29.22           N  
ANISOU 3836  NZ ALYS B  99     3822   3680   3601     98    170    198       N  
ATOM   3837  CB BLYS B  99       7.402  28.076 -22.135  0.49 28.24           C  
ANISOU 3837  CB BLYS B  99     3983   3517   3231    580   -236    -77       C  
ATOM   3838  CG BLYS B  99       8.066  28.920 -23.215  0.49 34.80           C  
ANISOU 3838  CG BLYS B  99     4884   4493   3844     15    285    -36       C  
ATOM   3839  CD BLYS B  99       6.988  29.641 -24.017  0.49 38.99           C  
ANISOU 3839  CD BLYS B  99     5105   5331   4379    240    -25   -142       C  
ATOM   3840  CE BLYS B  99       7.502  30.906 -24.679  0.49 42.21           C  
ANISOU 3840  CE BLYS B  99     5662   5609   4765   -105    134   -107       C  
ATOM   3841  NZ BLYS B  99       6.377  31.811 -25.059  0.49 43.32           N  
ANISOU 3841  NZ BLYS B  99     5758   5778   4925    -41    110    -40       N  
ATOM   3842  N   CYS B 100       7.189  26.029 -19.429  1.00 17.86           N  
ANISOU 3842  N   CYS B 100     3010   2270   1506    579    113    -49       N  
ATOM   3843  CA  CYS B 100       6.342  25.647 -18.314  1.00 16.66           C  
ANISOU 3843  CA  CYS B 100     2336   2181   1812    529   -116    143       C  
ATOM   3844  C   CYS B 100       7.067  25.711 -16.963  1.00 15.39           C  
ANISOU 3844  C   CYS B 100     2383   1881   1585    297    101   -208       C  
ATOM   3845  O   CYS B 100       8.290  25.881 -16.924  1.00 15.53           O  
ANISOU 3845  O   CYS B 100     2491   2005   1406    363    -17     43       O  
ATOM   3846  CB  CYS B 100       5.728  24.258 -18.493  1.00 17.34           C  
ANISOU 3846  CB  CYS B 100     2546   2195   1847    559   -190    -22       C  
ATOM   3847  SG  CYS B 100       6.854  22.867 -18.218  1.00 14.50           S  
ANISOU 3847  SG  CYS B 100     2092   2010   1409    576   -201   -188       S  
ATOM   3848  N   ARG B 101       6.323  25.620 -15.854  1.00 16.65           N  
ANISOU 3848  N   ARG B 101     2485   2230   1610    361     95   -278       N  
ATOM   3849  CA  ARG B 101       6.932  25.757 -14.525  1.00 18.09           C  
ANISOU 3849  CA  ARG B 101     2668   2676   1530    535    183   -285       C  
ATOM   3850  C   ARG B 101       8.021  24.726 -14.267  1.00 15.49           C  
ANISOU 3850  C   ARG B 101     2305   2198   1382    223    183   -272       C  
ATOM   3851  O   ARG B 101       9.007  24.965 -13.581  1.00 16.33           O  
ANISOU 3851  O   ARG B 101     2384   2189   1631    193    197   -406       O  
ATOM   3852  CB AARG B 101       5.897  25.768 -13.392  0.56 18.69           C  
ANISOU 3852  CB AARG B 101     2810   2676   1616    393    329   -261       C  
ATOM   3853  CG AARG B 101       6.402  26.356 -12.083  0.56 19.15           C  
ANISOU 3853  CG AARG B 101     2902   2702   1673    387    156   -134       C  
ATOM   3854  CD AARG B 101       5.268  26.641 -11.119  0.56 18.65           C  
ANISOU 3854  CD AARG B 101     2727   2406   1954    121    258    -10       C  
ATOM   3855  NE AARG B 101       4.653  25.458 -10.556  0.56 18.68           N  
ANISOU 3855  NE AARG B 101     2675   2319   2104    231    208    138       N  
ATOM   3856  CZ AARG B 101       3.767  25.376  -9.575  0.56 17.23           C  
ANISOU 3856  CZ AARG B 101     2645   1971   1932    154    110    228       C  
ATOM   3857  NH1AARG B 101       3.368  26.472  -8.935  0.56 18.23           N  
ANISOU 3857  NH1AARG B 101     2572   2302   2053    295     47     18       N  
ATOM   3858  NH2AARG B 101       3.270  24.193  -9.142  0.56 13.22           N  
ANISOU 3858  NH2AARG B 101     2212   1669   1140    439   -251    507       N  
ATOM   3859  CB BARG B 101       5.851  25.624 -13.419  0.44 21.79           C  
ANISOU 3859  CB BARG B 101     2912   3294   2072    349    397   -237       C  
ATOM   3860  CG BARG B 101       5.394  24.226 -13.100  0.44 27.81           C  
ANISOU 3860  CG BARG B 101     3720   3414   3431    155    -83     -2       C  
ATOM   3861  CD BARG B 101       4.402  23.971 -11.990  0.44 33.48           C  
ANISOU 3861  CD BARG B 101     4033   4615   4075    248    224    285       C  
ATOM   3862  NE BARG B 101       4.501  24.889 -10.898  0.44 37.91           N  
ANISOU 3862  NE BARG B 101     4764   4944   4697    104    -64    -51       N  
ATOM   3863  CZ BARG B 101       4.035  25.011  -9.677  0.44 40.55           C  
ANISOU 3863  CZ BARG B 101     5112   5495   4799    214     23     63       C  
ATOM   3864  NH1BARG B 101       3.232  24.141  -9.091  0.44 39.87           N  
ANISOU 3864  NH1BARG B 101     5142   5270   4737    221   -107     63       N  
ATOM   3865  NH2BARG B 101       4.411  26.099  -8.995  0.44 41.29           N  
ANISOU 3865  NH2BARG B 101     5206   5545   4936    127    -32     59       N  
ATOM   3866  N   VAL B 102       7.838  23.492 -14.800  1.00 13.98           N  
ANISOU 3866  N   VAL B 102     1990   2012   1311    255     35   -191       N  
ATOM   3867  CA  VAL B 102       8.805  22.399 -14.628  1.00 13.37           C  
ANISOU 3867  CA  VAL B 102     2033   1960   1087    170     38    -42       C  
ATOM   3868  C   VAL B 102      10.066  22.666 -15.419  1.00 12.81           C  
ANISOU 3868  C   VAL B 102     2007   1782   1079    131     41    -87       C  
ATOM   3869  O   VAL B 102      11.199  22.569 -14.936  1.00 12.88           O  
ANISOU 3869  O   VAL B 102     2052   1799   1041     99     98     53       O  
ATOM   3870  CB  VAL B 102       8.177  21.052 -14.963  1.00 13.38           C  
ANISOU 3870  CB  VAL B 102     2000   1987   1097     60      9    132       C  
ATOM   3871  CG1 VAL B 102       9.193  19.927 -14.876  1.00 14.80           C  
ANISOU 3871  CG1 VAL B 102     2177   2115   1332    180    -37    106       C  
ATOM   3872  CG2 VAL B 102       6.995  20.742 -14.037  1.00 14.62           C  
ANISOU 3872  CG2 VAL B 102     2075   2299   1180    -20    101    137       C  
ATOM   3873  N   CYS B 103       9.897  23.080 -16.730  1.00 12.49           N  
ANISOU 3873  N   CYS B 103     2017   1549   1178     -5    101    117       N  
ATOM   3874  CA  CYS B 103      11.081  23.380 -17.536  1.00 12.95           C  
ANISOU 3874  CA  CYS B 103     2058   1661   1200    156     58    204       C  
ATOM   3875  C   CYS B 103      11.914  24.528 -16.964  1.00 13.07           C  
ANISOU 3875  C   CYS B 103     2095   1705   1167     58     73    276       C  
ATOM   3876  O   CYS B 103      13.143  24.541 -17.110  1.00 14.49           O  
ANISOU 3876  O   CYS B 103     2287   1969   1250     25    187    186       O  
ATOM   3877  CB  CYS B 103      10.706  23.721 -18.980  1.00 13.82           C  
ANISOU 3877  CB  CYS B 103     2311   1733   1208    186     22    176       C  
ATOM   3878  SG  CYS B 103      10.231  22.238 -19.967  1.00 13.05           S  
ANISOU 3878  SG  CYS B 103     2367   1695    895    492    -35     14       S  
ATOM   3879  N   LYS B 104      11.236  25.501 -16.280  1.00 15.11           N  
ANISOU 3879  N   LYS B 104     2796   1724   1220     83    226    165       N  
ATOM   3880  CA  LYS B 104      11.936  26.610 -15.657  1.00 17.11           C  
ANISOU 3880  CA  LYS B 104     2780   2117   1606    -50     67     63       C  
ATOM   3881  C   LYS B 104      12.557  26.284 -14.298  1.00 16.96           C  
ANISOU 3881  C   LYS B 104     2948   1940   1556   -218     63    116       C  
ATOM   3882  O   LYS B 104      13.405  27.047 -13.796  1.00 19.62           O  
ANISOU 3882  O   LYS B 104     3390   2268   1795   -531    -20     44       O  
ATOM   3883  CB  LYS B 104      10.994  27.829 -15.522  1.00 19.81           C  
ANISOU 3883  CB  LYS B 104     3111   2268   2148     73    154    -23       C  
ATOM   3884  CG  LYS B 104      10.576  28.395 -16.888  1.00 24.59           C  
ANISOU 3884  CG  LYS B 104     3873   2900   2571    -41   -163    296       C  
ATOM   3885  CD  LYS B 104       9.614  29.565 -16.660  1.00 31.91           C  
ANISOU 3885  CD  LYS B 104     4234   3824   4067    355    -29   -128       C  
ATOM   3886  CE  LYS B 104       9.356  30.328 -17.948  1.00 37.20           C  
ANISOU 3886  CE  LYS B 104     4969   4899   4265      3   -126    254       C  
ATOM   3887  NZ  LYS B 104       8.698  31.633 -17.616  1.00 40.63           N  
ANISOU 3887  NZ  LYS B 104     5294   5276   4867    270      2     95       N  
ATOM   3888  N   HIS B 105      12.241  25.141 -13.703  1.00 15.59           N  
ANISOU 3888  N   HIS B 105     2669   2052   1203   -198    172    124       N  
ATOM   3889  CA  HIS B 105      12.774  24.761 -12.376  1.00 15.01           C  
ANISOU 3889  CA  HIS B 105     2376   2053   1273   -127     -6    -42       C  
ATOM   3890  C   HIS B 105      14.125  24.121 -12.589  1.00 16.26           C  
ANISOU 3890  C   HIS B 105     2354   2219   1606    -66    203    -24       C  
ATOM   3891  O   HIS B 105      14.366  23.358 -13.444  1.00 19.63           O  
ANISOU 3891  O   HIS B 105     2617   3169   1670    224    305   -528       O  
ATOM   3892  CB  HIS B 105      11.799  23.753 -11.736  1.00 15.40           C  
ANISOU 3892  CB  HIS B 105     2446   2153   1250     10    274      1       C  
ATOM   3893  CG  HIS B 105      12.080  23.447 -10.286  1.00 16.15           C  
ANISOU 3893  CG  HIS B 105     2243   2498   1394     84    158    111       C  
ATOM   3894  ND1 HIS B 105      13.104  22.593  -9.903  1.00 19.03           N  
ANISOU 3894  ND1 HIS B 105     2378   3162   1692    266    260    346       N  
ATOM   3895  CD2 HIS B 105      11.417  23.850  -9.180  1.00 16.23           C  
ANISOU 3895  CD2 HIS B 105     2372   2555   1239     18    155    200       C  
ATOM   3896  CE1 HIS B 105      13.027  22.523  -8.567  1.00 19.25           C  
ANISOU 3896  CE1 HIS B 105     2415   3233   1667    305    126    339       C  
ATOM   3897  NE2 HIS B 105      12.066  23.306  -8.107  1.00 17.70           N  
ANISOU 3897  NE2 HIS B 105     2566   2772   1388    136     23    184       N  
ATOM   3898  N  APRO B 106      14.987  24.414 -11.520  0.59 17.69           N  
ANISOU 3898  N  APRO B 106     2395   2285   2040   -130     45    -65       N  
ATOM   3899  CA APRO B 106      16.369  23.949 -11.652  0.59 19.06           C  
ANISOU 3899  CA APRO B 106     2446   2570   2227   -120    -72    -86       C  
ATOM   3900  C  APRO B 106      16.570  22.448 -11.738  0.59 19.63           C  
ANISOU 3900  C  APRO B 106     2629   2643   2186    -30     44   -281       C  
ATOM   3901  O  APRO B 106      17.556  21.948 -12.312  0.59 22.97           O  
ANISOU 3901  O  APRO B 106     2618   3291   2818    182    114   -337       O  
ATOM   3902  CB APRO B 106      17.199  24.478 -10.458  0.59 19.87           C  
ANISOU 3902  CB APRO B 106     2522   2613   2416   -199   -156   -142       C  
ATOM   3903  CG APRO B 106      16.233  25.256  -9.647  0.59 20.31           C  
ANISOU 3903  CG APRO B 106     2573   2882   2261   -150   -200   -167       C  
ATOM   3904  CD APRO B 106      14.871  25.254 -10.222  0.59 18.77           C  
ANISOU 3904  CD APRO B 106     2558   2404   2169   -112   -115   -195       C  
ATOM   3905  N  BPRO B 106      15.136  24.541 -11.728  0.41 17.98           N  
ANISOU 3905  N  BPRO B 106     2308   2521   2002    -29     95    -46       N  
ATOM   3906  CA BPRO B 106      16.453  23.919 -11.987  0.41 18.67           C  
ANISOU 3906  CA BPRO B 106     2345   2599   2151    -24     27   -115       C  
ATOM   3907  C  BPRO B 106      16.487  22.405 -11.896  0.41 18.81           C  
ANISOU 3907  C  BPRO B 106     2453   2595   2099     18    -25   -235       C  
ATOM   3908  O  BPRO B 106      17.320  21.808 -12.628  0.41 20.46           O  
ANISOU 3908  O  BPRO B 106     2454   2989   2329    121     56   -291       O  
ATOM   3909  CB BPRO B 106      17.507  24.579 -11.093  0.41 19.32           C  
ANISOU 3909  CB BPRO B 106     2297   2727   2318    -37     -2    -90       C  
ATOM   3910  CG BPRO B 106      16.804  25.806 -10.601  0.41 19.75           C  
ANISOU 3910  CG BPRO B 106     2452   2708   2345     34     -1    -24       C  
ATOM   3911  CD BPRO B 106      15.322  25.599 -10.636  0.41 19.13           C  
ANISOU 3911  CD BPRO B 106     2484   2505   2279    -67     22   -114       C  
ATOM   3912  N   GLU B 107      15.690  21.697 -11.095  1.00 18.25           N  
ANISOU 3912  N   GLU B 107     2513   2524   1899      3   -247   -133       N  
ATOM   3913  CA  GLU B 107      15.833  20.252 -10.985  1.00 22.33           C  
ANISOU 3913  CA  GLU B 107     3048   2586   2852     53   -148    -85       C  
ATOM   3914  C   GLU B 107      14.858  19.479 -11.873  1.00 23.03           C  
ANISOU 3914  C   GLU B 107     2820   2996   2935    179   -227   -172       C  
ATOM   3915  O   GLU B 107      15.284  18.483 -12.514  1.00 25.76           O  
ANISOU 3915  O   GLU B 107     3360   3231   3196    125    -98   -332       O  
ATOM   3916  CB AGLU B 107      15.706  19.826  -9.520  0.75 28.07           C  
ANISOU 3916  CB AGLU B 107     3961   3556   3147    169    -23    289       C  
ATOM   3917  CG AGLU B 107      16.667  20.518  -8.557  0.75 34.48           C  
ANISOU 3917  CG AGLU B 107     4555   4501   4046   -130   -378     33       C  
ATOM   3918  CD AGLU B 107      18.106  20.224  -8.941  0.75 39.08           C  
ANISOU 3918  CD AGLU B 107     4787   5424   4636     49   -135     30       C  
ATOM   3919  OE1AGLU B 107      18.438  19.025  -9.018  0.75 40.60           O  
ANISOU 3919  OE1AGLU B 107     5015   5426   4984    -28   -196     30       O  
ATOM   3920  OE2AGLU B 107      18.852  21.201  -9.165  0.75 41.12           O  
ANISOU 3920  OE2AGLU B 107     5170   5515   4937   -111   -167     77       O  
ATOM   3921  CB BGLU B 107      15.629  19.754  -9.543  0.25 23.55           C  
ANISOU 3921  CB BGLU B 107     3042   2966   2940     20   -159     91       C  
ATOM   3922  CG BGLU B 107      15.642  20.672  -8.364  0.25 24.86           C  
ANISOU 3922  CG BGLU B 107     3262   3164   3017     43    -22     21       C  
ATOM   3923  CD BGLU B 107      15.509  20.139  -6.958  0.25 25.38           C  
ANISOU 3923  CD BGLU B 107     3314   3309   3020     33    -27     50       C  
ATOM   3924  OE1BGLU B 107      14.388  19.843  -6.465  0.25 22.21           O  
ANISOU 3924  OE1BGLU B 107     3261   2895   2282     64   -270    328       O  
ATOM   3925  OE2BGLU B 107      16.603  20.054  -6.337  0.25 25.79           O  
ANISOU 3925  OE2BGLU B 107     3448   3419   2931    -17   -108     27       O  
ATOM   3926  N   GLY B 108      13.678  19.994 -12.100  1.00 17.45           N  
ANISOU 3926  N   GLY B 108     2395   2568   1667     18     82   -606       N  
ATOM   3927  CA  GLY B 108      12.627  19.178 -12.735  1.00 17.18           C  
ANISOU 3927  CA  GLY B 108     2254   2584   1688     -2    219   -560       C  
ATOM   3928  C   GLY B 108      12.863  18.928 -14.217  1.00 14.05           C  
ANISOU 3928  C   GLY B 108     1935   1846   1557    187    118   -152       C  
ATOM   3929  O   GLY B 108      13.433  19.761 -14.910  1.00 15.83           O  
ANISOU 3929  O   GLY B 108     2351   1911   1755   -121    -46    -93       O  
ATOM   3930  N   ASN B 109      12.344  17.813 -14.710  1.00 12.48           N  
ANISOU 3930  N   ASN B 109     1838   1705   1198    144    132    -88       N  
ATOM   3931  CA  ASN B 109      12.454  17.488 -16.134  1.00 11.17           C  
ANISOU 3931  CA  ASN B 109     1548   1570   1126    257     82     40       C  
ATOM   3932  C   ASN B 109      11.149  16.968 -16.693  1.00 10.85           C  
ANISOU 3932  C   ASN B 109     1539   1556   1029    280    128     26       C  
ATOM   3933  O   ASN B 109      11.106  16.770 -17.955  1.00 11.70           O  
ANISOU 3933  O   ASN B 109     1778   1693    975    187    137     46       O  
ATOM   3934  CB  ASN B 109      13.562  16.468 -16.431  1.00 11.77           C  
ANISOU 3934  CB  ASN B 109     1632   1490   1350    223    163     53       C  
ATOM   3935  CG  ASN B 109      13.218  15.034 -16.086  1.00 10.83           C  
ANISOU 3935  CG  ASN B 109     1424   1512   1180    266     86    190       C  
ATOM   3936  OD1 ASN B 109      12.472  14.819 -15.122  1.00 13.84           O  
ANISOU 3936  OD1 ASN B 109     2040   1638   1580    144    509    102       O  
ATOM   3937  ND2 ASN B 109      13.709  14.081 -16.854  1.00 11.23           N  
ANISOU 3937  ND2 ASN B 109     1631   1508   1127    105    150    158       N  
ATOM   3938  N   PHE B 110      10.109  16.712 -15.913  1.00 11.69           N  
ANISOU 3938  N   PHE B 110     1465   1981    997    176     90     53       N  
ATOM   3939  CA  PHE B 110       8.872  16.124 -16.408  1.00 11.94           C  
ANISOU 3939  CA  PHE B 110     1466   2095    974    205     96    -57       C  
ATOM   3940  C   PHE B 110       7.949  17.198 -16.960  1.00 12.59           C  
ANISOU 3940  C   PHE B 110     1631   2047   1106    212     -9    -92       C  
ATOM   3941  O   PHE B 110       6.968  17.626 -16.357  1.00 13.88           O  
ANISOU 3941  O   PHE B 110     1765   2369   1140    373    -66   -198       O  
ATOM   3942  CB  PHE B 110       8.253  15.250 -15.309  1.00 12.86           C  
ANISOU 3942  CB  PHE B 110     1621   2201   1064     32    -17     11       C  
ATOM   3943  CG  PHE B 110       7.139  14.330 -15.741  1.00 12.75           C  
ANISOU 3943  CG  PHE B 110     1656   1989   1200     21     -7    134       C  
ATOM   3944  CD1 PHE B 110       7.283  13.415 -16.782  1.00 15.84           C  
ANISOU 3944  CD1 PHE B 110     1836   2224   1959    173    224   -283       C  
ATOM   3945  CD2 PHE B 110       5.916  14.332 -15.087  1.00 13.98           C  
ANISOU 3945  CD2 PHE B 110     1758   2181   1374    -49     80    118       C  
ATOM   3946  CE1 PHE B 110       6.260  12.560 -17.141  1.00 16.90           C  
ANISOU 3946  CE1 PHE B 110     1808   2550   2063    196     81   -353       C  
ATOM   3947  CE2 PHE B 110       4.894  13.472 -15.430  1.00 14.07           C  
ANISOU 3947  CE2 PHE B 110     1547   2408   1392     49    119    127       C  
ATOM   3948  CZ  PHE B 110       5.048  12.576 -16.466  1.00 15.37           C  
ANISOU 3948  CZ  PHE B 110     1692   2165   1984    115     24    -81       C  
ATOM   3949  N   CYS B 111       8.322  17.688 -18.169  1.00 11.94           N  
ANISOU 3949  N   CYS B 111     1620   1851   1066    318    -64    -33       N  
ATOM   3950  CA  CYS B 111       7.643  18.800 -18.828  1.00 11.92           C  
ANISOU 3950  CA  CYS B 111     1810   1691   1026    295    -75    -52       C  
ATOM   3951  C   CYS B 111       6.146  18.563 -18.867  1.00 12.83           C  
ANISOU 3951  C   CYS B 111     1851   1947   1075    296    -41    -10       C  
ATOM   3952  O   CYS B 111       5.664  17.482 -19.214  1.00 13.25           O  
ANISOU 3952  O   CYS B 111     1936   1924   1176    334   -269    -19       O  
ATOM   3953  CB  CYS B 111       8.214  18.920 -20.260  1.00 11.96           C  
ANISOU 3953  CB  CYS B 111     1902   1609   1035    462   -110     -4       C  
ATOM   3954  SG  CYS B 111       7.377  20.112 -21.348  1.00 13.02           S  
ANISOU 3954  SG  CYS B 111     2047   1913    986    556   -134    -47       S  
ATOM   3955  N   LEU B 112       5.351  19.631 -18.608  1.00 13.64           N  
ANISOU 3955  N   LEU B 112     1986   1987   1208    380    -79   -158       N  
ATOM   3956  CA  LEU B 112       3.904  19.526 -18.573  1.00 15.63           C  
ANISOU 3956  CA  LEU B 112     1956   2613   1370    369    -70   -337       C  
ATOM   3957  C   LEU B 112       3.269  19.235 -19.920  1.00 14.80           C  
ANISOU 3957  C   LEU B 112     1837   2401   1385    343    -53   -162       C  
ATOM   3958  O   LEU B 112       2.084  18.846 -19.929  1.00 16.35           O  
ANISOU 3958  O   LEU B 112     1812   3009   1390    398    -36   -269       O  
ATOM   3959  CB  LEU B 112       3.356  20.796 -17.893  1.00 17.93           C  
ANISOU 3959  CB  LEU B 112     2205   2797   1810    417    111   -440       C  
ATOM   3960  CG  LEU B 112       3.732  20.867 -16.391  1.00 20.17           C  
ANISOU 3960  CG  LEU B 112     2552   3232   1878    331    110   -455       C  
ATOM   3961  CD1 LEU B 112       3.442  22.206 -15.760  1.00 23.89           C  
ANISOU 3961  CD1 LEU B 112     3541   3173   2362    106    245   -513       C  
ATOM   3962  CD2 LEU B 112       3.001  19.781 -15.644  1.00 19.16           C  
ANISOU 3962  CD2 LEU B 112     2594   2899   1789    597   -140   -341       C  
ATOM   3963  N   LYS B 113       3.989  19.332 -21.024  1.00 14.02           N  
ANISOU 3963  N   LYS B 113     1848   2233   1247    438   -115   -211       N  
ATOM   3964  CA  LYS B 113       3.451  18.943 -22.347  1.00 14.93           C  
ANISOU 3964  CA  LYS B 113     2118   2318   1237    405   -195   -213       C  
ATOM   3965  C   LYS B 113       3.619  17.456 -22.614  1.00 14.01           C  
ANISOU 3965  C   LYS B 113     1823   2231   1270    386   -160    -59       C  
ATOM   3966  O   LYS B 113       3.237  16.977 -23.730  1.00 14.68           O  
ANISOU 3966  O   LYS B 113     2056   2241   1279    440   -261   -176       O  
ATOM   3967  CB  LYS B 113       4.135  19.731 -23.471  1.00 17.17           C  
ANISOU 3967  CB  LYS B 113     2659   2549   1316    216   -227    -84       C  
ATOM   3968  CG ALYS B 113       3.787  21.218 -23.355  0.51 21.06           C  
ANISOU 3968  CG ALYS B 113     3348   2590   2063    163   -218    -95       C  
ATOM   3969  CD ALYS B 113       2.317  21.489 -23.593  0.51 26.46           C  
ANISOU 3969  CD ALYS B 113     3320   3608   3124    127    -44   -215       C  
ATOM   3970  CE ALYS B 113       2.060  22.845 -24.227  0.51 29.99           C  
ANISOU 3970  CE ALYS B 113     4112   3795   3489     38     14     23       C  
ATOM   3971  NZ ALYS B 113       0.605  23.070 -24.491  0.51 32.30           N  
ANISOU 3971  NZ ALYS B 113     4171   4153   3950     96    -15      5       N  
ATOM   3972  CG BLYS B 113       4.296  21.219 -23.345  0.49 19.03           C  
ANISOU 3972  CG BLYS B 113     2836   2514   1880    290   -311     65       C  
ATOM   3973  CD BLYS B 113       2.984  21.971 -23.333  0.49 21.50           C  
ANISOU 3973  CD BLYS B 113     2654   2946   2568    206   -245   -144       C  
ATOM   3974  CE BLYS B 113       3.206  23.432 -23.716  0.49 24.89           C  
ANISOU 3974  CE BLYS B 113     3115   3110   3230    289   -179    193       C  
ATOM   3975  NZ BLYS B 113       4.044  24.167 -22.732  0.49 28.16           N  
ANISOU 3975  NZ BLYS B 113     3358   3671   3670    187   -326    -14       N  
ATOM   3976  N   ASN B 114       4.108  16.652 -21.674  1.00 13.48           N  
ANISOU 3976  N   ASN B 114     1701   2152   1268    407   -172    -22       N  
ATOM   3977  CA  ASN B 114       4.266  15.219 -21.860  1.00 13.35           C  
ANISOU 3977  CA  ASN B 114     1751   2071   1250    345    -73     36       C  
ATOM   3978  C   ASN B 114       2.978  14.494 -22.188  1.00 13.72           C  
ANISOU 3978  C   ASN B 114     1690   2208   1316    363     41   -184       C  
ATOM   3979  O   ASN B 114       1.867  14.917 -21.790  1.00 14.82           O  
ANISOU 3979  O   ASN B 114     1698   2400   1533    455    -64   -308       O  
ATOM   3980  CB  ASN B 114       4.925  14.587 -20.602  1.00 13.49           C  
ANISOU 3980  CB  ASN B 114     1775   2115   1237    318    -75     27       C  
ATOM   3981  CG  ASN B 114       3.957  14.392 -19.443  1.00 13.50           C  
ANISOU 3981  CG  ASN B 114     1900   2065   1165    301    -50     11       C  
ATOM   3982  OD1 ASN B 114       3.171  13.435 -19.453  1.00 14.50           O  
ANISOU 3982  OD1 ASN B 114     1913   2177   1421    289   -143   -130       O  
ATOM   3983  ND2 ASN B 114       3.991  15.315 -18.479  1.00 14.26           N  
ANISOU 3983  ND2 ASN B 114     2103   2075   1238    337    -87    -11       N  
ATOM   3984  N   ASP B 115       3.098  13.347 -22.913  1.00 13.58           N  
ANISOU 3984  N   ASP B 115     1763   2162   1237    302    -20   -180       N  
ATOM   3985  CA  ASP B 115       1.998  12.448 -23.182  1.00 14.25           C  
ANISOU 3985  CA  ASP B 115     1876   2209   1328    252     47   -206       C  
ATOM   3986  C   ASP B 115       2.158  11.175 -22.351  1.00 15.46           C  
ANISOU 3986  C   ASP B 115     2118   2199   1555    231    -10   -194       C  
ATOM   3987  O   ASP B 115       1.699  10.098 -22.759  1.00 18.42           O  
ANISOU 3987  O   ASP B 115     2585   2354   2060    -65   -206    -75       O  
ATOM   3988  CB  ASP B 115       1.878  12.112 -24.690  1.00 14.41           C  
ANISOU 3988  CB  ASP B 115     1738   2375   1364    138     86   -271       C  
ATOM   3989  CG  ASP B 115       0.557  11.462 -25.058  1.00 15.78           C  
ANISOU 3989  CG  ASP B 115     1830   2580   1584     71    130   -417       C  
ATOM   3990  OD1 ASP B 115      -0.479  11.960 -24.525  1.00 16.44           O  
ANISOU 3990  OD1 ASP B 115     1729   2780   1739     25    216   -365       O  
ATOM   3991  OD2 ASP B 115       0.529  10.502 -25.871  1.00 16.59           O  
ANISOU 3991  OD2 ASP B 115     2046   2767   1489    -42     72   -481       O  
ATOM   3992  N   LEU B 116       2.809  11.243 -21.174  1.00 14.96           N  
ANISOU 3992  N   LEU B 116     1777   2338   1570    184     26    -79       N  
ATOM   3993  CA  LEU B 116       3.015  10.065 -20.346  1.00 16.20           C  
ANISOU 3993  CA  LEU B 116     2027   2444   1683    344     53    -14       C  
ATOM   3994  C   LEU B 116       1.980   9.906 -19.235  1.00 19.71           C  
ANISOU 3994  C   LEU B 116     2618   2871   2000     51    329   -143       C  
ATOM   3995  O   LEU B 116       1.520   8.795 -18.995  1.00 22.80           O  
ANISOU 3995  O   LEU B 116     2989   3090   2582   -162    521   -120       O  
ATOM   3996  CB  LEU B 116       4.420  10.160 -19.707  1.00 16.44           C  
ANISOU 3996  CB  LEU B 116     2085   2732   1429    242    123    -33       C  
ATOM   3997  CG  LEU B 116       5.611   9.654 -20.512  1.00 17.42           C  
ANISOU 3997  CG  LEU B 116     2104   2823   1693    308     17   -102       C  
ATOM   3998  CD1 LEU B 116       5.874  10.509 -21.736  1.00 20.75           C  
ANISOU 3998  CD1 LEU B 116     2296   3245   2343    119    227    331       C  
ATOM   3999  CD2 LEU B 116       6.878   9.525 -19.678  1.00 19.59           C  
ANISOU 3999  CD2 LEU B 116     2096   3194   2155    451    -93   -312       C  
ATOM   4000  N   SER B 117       1.631  10.996 -18.550  1.00 19.66           N  
ANISOU 4000  N   SER B 117     2405   3070   1995    188    509   -208       N  
ATOM   4001  CA  SER B 117       0.683  10.919 -17.434  1.00 24.15           C  
ANISOU 4001  CA  SER B 117     3113   3773   2290    193    787   -461       C  
ATOM   4002  C   SER B 117      -0.706  10.444 -17.755  1.00 27.85           C  
ANISOU 4002  C   SER B 117     3481   4197   2902     41    274   -390       C  
ATOM   4003  O   SER B 117      -1.311   9.700 -16.947  1.00 31.41           O  
ANISOU 4003  O   SER B 117     4155   4925   2856   -189    351   -189       O  
ATOM   4004  CB  SER B 117       0.566  12.345 -16.815  1.00 24.35           C  
ANISOU 4004  CB  SER B 117     2895   4066   2291    200    796   -772       C  
ATOM   4005  OG  SER B 117       1.716  12.506 -16.038  1.00 27.15           O  
ANISOU 4005  OG  SER B 117     3309   4421   2587    268    451   -309       O  
ATOM   4006  N   MET B 118      -1.311  10.932 -18.819  1.00 26.50           N  
ANISOU 4006  N   MET B 118     3737   4108   2222    353    357  -1004       N  
ATOM   4007  CA  MET B 118      -2.679  10.585 -19.217  1.00 31.32           C  
ANISOU 4007  CA  MET B 118     4151   4685   3066   -312      3   -365       C  
ATOM   4008  C   MET B 118      -2.657  10.554 -20.764  1.00 26.79           C  
ANISOU 4008  C   MET B 118     3555   3728   2895   -114     73   -468       C  
ATOM   4009  O   MET B 118      -2.916  11.517 -21.468  1.00 25.51           O  
ANISOU 4009  O   MET B 118     3559   3773   2361     51     54   -816       O  
ATOM   4010  CB  MET B 118      -3.687  11.602 -18.704  1.00 38.81           C  
ANISOU 4010  CB  MET B 118     4785   5159   4803    175    -31   -440       C  
ATOM   4011  CG  MET B 118      -3.952  11.552 -17.201  1.00 46.14           C  
ANISOU 4011  CG  MET B 118     6070   6480   4983   -144   -122    -64       C  
ATOM   4012  SD  MET B 118      -5.194  12.672 -16.578  1.00 51.13           S  
ANISOU 4012  SD  MET B 118     6530   7136   5760    222     89   -150       S  
ATOM   4013  CE  MET B 118      -4.424  14.265 -16.813  1.00 51.15           C  
ANISOU 4013  CE  MET B 118     6540   7170   5724    182     29   -105       C  
ATOM   4014  N   PRO B 119      -2.133   9.462 -21.262  1.00 23.65           N  
ANISOU 4014  N   PRO B 119     3145   3699   2143   -211    163   -218       N  
ATOM   4015  CA  PRO B 119      -1.802   9.381 -22.704  1.00 23.29           C  
ANISOU 4015  CA  PRO B 119     3173   3574   2103   -127    171   -270       C  
ATOM   4016  C   PRO B 119      -2.992   9.533 -23.620  1.00 22.89           C  
ANISOU 4016  C   PRO B 119     3035   3508   2155   -326    164   -418       C  
ATOM   4017  O   PRO B 119      -4.028   8.871 -23.462  1.00 26.13           O  
ANISOU 4017  O   PRO B 119     3218   4250   2461   -609    431   -576       O  
ATOM   4018  CB  PRO B 119      -1.093   8.034 -22.893  1.00 24.88           C  
ANISOU 4018  CB  PRO B 119     3151   3695   2609    -54     -7   -362       C  
ATOM   4019  CG  PRO B 119      -1.657   7.259 -21.738  1.00 27.96           C  
ANISOU 4019  CG  PRO B 119     3861   3647   3114   -175    202   -212       C  
ATOM   4020  CD  PRO B 119      -1.718   8.256 -20.584  1.00 26.08           C  
ANISOU 4020  CD  PRO B 119     3522   3614   2774   -231     52   -138       C  
ATOM   4021  N   ARG B 120      -2.808  10.411 -24.596  1.00 19.87           N  
ANISOU 4021  N   ARG B 120     2104   3501   1946   -143    205   -439       N  
ATOM   4022  CA  ARG B 120      -3.777  10.656 -25.651  1.00 19.26           C  
ANISOU 4022  CA  ARG B 120     2112   3364   1840    -93    222   -346       C  
ATOM   4023  C   ARG B 120      -3.307   9.913 -26.934  1.00 17.09           C  
ANISOU 4023  C   ARG B 120     1728   2999   1767   -136    121   -358       C  
ATOM   4024  O   ARG B 120      -4.129   9.620 -27.804  1.00 17.45           O  
ANISOU 4024  O   ARG B 120     1742   3001   1888    -58     78   -514       O  
ATOM   4025  CB  ARG B 120      -3.905  12.129 -26.025  1.00 23.55           C  
ANISOU 4025  CB  ARG B 120     2828   3491   2628    164      9   -206       C  
ATOM   4026  CG  ARG B 120      -4.426  13.191 -25.078  1.00 26.49           C  
ANISOU 4026  CG  ARG B 120     3463   3597   3005    133     38   -329       C  
ATOM   4027  CD  ARG B 120      -4.542  14.533 -25.794  1.00 28.03           C  
ANISOU 4027  CD  ARG B 120     3618   3668   3364    198     13   -146       C  
ATOM   4028  NE  ARG B 120      -3.265  15.259 -25.920  1.00 27.70           N  
ANISOU 4028  NE  ARG B 120     3698   3610   3217    202    267   -231       N  
ATOM   4029  CZ  ARG B 120      -3.128  16.402 -26.585  1.00 28.29           C  
ANISOU 4029  CZ  ARG B 120     3880   3661   3208    215    268   -272       C  
ATOM   4030  NH1 ARG B 120      -4.183  16.966 -27.168  1.00 29.92           N  
ANISOU 4030  NH1 ARG B 120     4400   4085   2884    355    -56   -364       N  
ATOM   4031  NH2 ARG B 120      -1.954  17.010 -26.645  1.00 28.03           N  
ANISOU 4031  NH2 ARG B 120     3735   3938   2977    341    644    -55       N  
ATOM   4032  N   GLY B 121      -1.992   9.639 -27.116  1.00 15.87           N  
ANISOU 4032  N   GLY B 121     1781   2774   1474    131      7   -423       N  
ATOM   4033  CA  GLY B 121      -1.537   9.002 -28.362  1.00 15.18           C  
ANISOU 4033  CA  GLY B 121     1801   2424   1542     94     97   -337       C  
ATOM   4034  C   GLY B 121      -1.688   9.876 -29.587  1.00 14.57           C  
ANISOU 4034  C   GLY B 121     1566   2404   1564     74     21   -326       C  
ATOM   4035  O   GLY B 121      -1.996   9.393 -30.699  1.00 15.31           O  
ANISOU 4035  O   GLY B 121     1622   2549   1647    264   -113   -457       O  
ATOM   4036  N   THR B 122      -1.432  11.164 -29.472  1.00 14.30           N  
ANISOU 4036  N   THR B 122     1527   2394   1511    121    -72   -197       N  
ATOM   4037  CA  THR B 122      -1.544  12.119 -30.554  1.00 15.01           C  
ANISOU 4037  CA  THR B 122     1720   2355   1629    164    -22   -130       C  
ATOM   4038  C   THR B 122      -0.323  13.046 -30.596  1.00 14.90           C  
ANISOU 4038  C   THR B 122     1746   2287   1627    205    -44   -131       C  
ATOM   4039  O   THR B 122       0.566  12.994 -29.715  1.00 15.77           O  
ANISOU 4039  O   THR B 122     1729   2617   1646    239    -26   -223       O  
ATOM   4040  CB  THR B 122      -2.800  13.009 -30.378  1.00 17.34           C  
ANISOU 4040  CB  THR B 122     1740   2719   2131    268     14   -242       C  
ATOM   4041  OG1 THR B 122      -2.665  13.820 -29.197  1.00 18.11           O  
ANISOU 4041  OG1 THR B 122     2018   2585   2278    449    366   -385       O  
ATOM   4042  CG2 THR B 122      -4.101  12.217 -30.266  1.00 18.50           C  
ANISOU 4042  CG2 THR B 122     1817   2701   2511    210    -84   -123       C  
ATOM   4043  N   MET B 123      -0.272  13.920 -31.582  1.00 15.10           N  
ANISOU 4043  N   MET B 123     1786   2452   1500     94     61   -149       N  
ATOM   4044  CA  MET B 123       0.620  15.046 -31.653  1.00 14.79           C  
ANISOU 4044  CA  MET B 123     1698   2492   1428    131     79   -170       C  
ATOM   4045  C   MET B 123       0.139  16.062 -30.598  1.00 15.55           C  
ANISOU 4045  C   MET B 123     1910   2523   1473    201    223    -53       C  
ATOM   4046  O   MET B 123      -0.987  15.969 -30.045  1.00 16.86           O  
ANISOU 4046  O   MET B 123     1940   2843   1622    208    190   -257       O  
ATOM   4047  CB  MET B 123       0.579  15.716 -33.039  1.00 16.45           C  
ANISOU 4047  CB  MET B 123     2209   2631   1409     75    111   -197       C  
ATOM   4048  CG  MET B 123       1.021  14.807 -34.168  1.00 16.75           C  
ANISOU 4048  CG  MET B 123     2258   2344   1763     25    255   -257       C  
ATOM   4049  SD  MET B 123       2.764  14.373 -34.172  1.00 17.49           S  
ANISOU 4049  SD  MET B 123     2500   2254   1891    340    656    -64       S  
ATOM   4050  CE  MET B 123       3.516  15.965 -34.498  1.00 16.85           C  
ANISOU 4050  CE  MET B 123     2264   2524   1615     56    -21   -158       C  
ATOM   4051  N   GLN B 124       0.911  17.126 -30.395  1.00 15.82           N  
ANISOU 4051  N   GLN B 124     2009   2665   1337    117     36   -236       N  
ATOM   4052  CA  GLN B 124       0.453  18.177 -29.454  1.00 16.35           C  
ANISOU 4052  CA  GLN B 124     2178   2592   1443    158     59   -235       C  
ATOM   4053  C   GLN B 124      -0.905  18.771 -29.806  1.00 17.69           C  
ANISOU 4053  C   GLN B 124     2228   2825   1667    285    128   -272       C  
ATOM   4054  O   GLN B 124      -1.681  19.120 -28.892  1.00 18.64           O  
ANISOU 4054  O   GLN B 124     2241   3022   1819    311    123   -494       O  
ATOM   4055  CB  GLN B 124       1.478  19.282 -29.297  1.00 16.15           C  
ANISOU 4055  CB  GLN B 124     2171   2610   1355    177     64   -117       C  
ATOM   4056  CG  GLN B 124       2.765  18.928 -28.574  1.00 17.01           C  
ANISOU 4056  CG  GLN B 124     2417   2554   1494    357   -121   -142       C  
ATOM   4057  CD  GLN B 124       2.542  18.649 -27.089  1.00 18.00           C  
ANISOU 4057  CD  GLN B 124     2472   2878   1490    471    -90   -156       C  
ATOM   4058  OE1 GLN B 124       1.751  19.305 -26.409  1.00 20.83           O  
ANISOU 4058  OE1 GLN B 124     3261   3116   1537    809    107   -148       O  
ATOM   4059  NE2 GLN B 124       3.275  17.660 -26.584  1.00 17.12           N  
ANISOU 4059  NE2 GLN B 124     2286   2769   1448    327   -146   -187       N  
ATOM   4060  N   ASP B 125      -1.259  18.841 -31.110  1.00 17.51           N  
ANISOU 4060  N   ASP B 125     2223   2658   1773    374     17   -152       N  
ATOM   4061  CA  ASP B 125      -2.530  19.425 -31.532  1.00 18.06           C  
ANISOU 4061  CA  ASP B 125     2214   2660   1988    329     -3    -58       C  
ATOM   4062  C   ASP B 125      -3.713  18.481 -31.395  1.00 17.73           C  
ANISOU 4062  C   ASP B 125     2170   2672   1893    343     -8    -57       C  
ATOM   4063  O   ASP B 125      -4.841  18.857 -31.787  1.00 19.89           O  
ANISOU 4063  O   ASP B 125     2347   3063   2146    692   -108   -145       O  
ATOM   4064  CB AASP B 125      -2.434  20.094 -32.914  0.58 18.22           C  
ANISOU 4064  CB AASP B 125     2529   2433   1959    360     60   -145       C  
ATOM   4065  CG AASP B 125      -2.394  19.183 -34.115  0.58 17.05           C  
ANISOU 4065  CG AASP B 125     2331   2257   1889    273     63    -38       C  
ATOM   4066  OD1AASP B 125      -2.342  17.954 -33.896  0.58 16.05           O  
ANISOU 4066  OD1AASP B 125     2091   2207   1799    216     78   -107       O  
ATOM   4067  OD2AASP B 125      -2.380  19.644 -35.277  0.58 16.98           O  
ANISOU 4067  OD2AASP B 125     2394   2165   1892     98     38      5       O  
ATOM   4068  CB BASP B 125      -2.468  19.832 -33.017  0.42 17.94           C  
ANISOU 4068  CB BASP B 125     2365   2509   1941    290     54   -163       C  
ATOM   4069  CG BASP B 125      -2.582  18.703 -34.021  0.42 17.19           C  
ANISOU 4069  CG BASP B 125     2280   2294   1957     96     60    -57       C  
ATOM   4070  OD1BASP B 125      -2.547  17.501 -33.677  0.42 16.53           O  
ANISOU 4070  OD1BASP B 125     2080   2238   1962    126    155   -111       O  
ATOM   4071  OD2BASP B 125      -2.691  19.024 -35.230  0.42 17.35           O  
ANISOU 4071  OD2BASP B 125     2278   2369   1944      4   -159   -107       O  
ATOM   4072  N   GLY B 126      -3.596  17.284 -30.834  1.00 17.07           N  
ANISOU 4072  N   GLY B 126     2171   2567   1747    245      3   -170       N  
ATOM   4073  CA  GLY B 126      -4.670  16.341 -30.600  1.00 17.79           C  
ANISOU 4073  CA  GLY B 126     2221   2597   1943    285    150   -265       C  
ATOM   4074  C   GLY B 126      -5.056  15.506 -31.813  1.00 17.42           C  
ANISOU 4074  C   GLY B 126     1958   2744   1915    349      9   -221       C  
ATOM   4075  O   GLY B 126      -6.055  14.768 -31.725  1.00 19.05           O  
ANISOU 4075  O   GLY B 126     2160   3133   1946    164    129   -297       O  
ATOM   4076  N   THR B 127      -4.251  15.544 -32.883  1.00 17.84           N  
ANISOU 4076  N   THR B 127     2131   2838   1811    539     38   -264       N  
ATOM   4077  CA  THR B 127      -4.529  14.753 -34.085  1.00 16.84           C  
ANISOU 4077  CA  THR B 127     1827   2644   1926    300    -85   -160       C  
ATOM   4078  C   THR B 127      -3.355  13.805 -34.358  1.00 16.46           C  
ANISOU 4078  C   THR B 127     1804   2805   1644    331    -89   -262       C  
ATOM   4079  O   THR B 127      -2.277  13.908 -33.749  1.00 17.73           O  
ANISOU 4079  O   THR B 127     1870   3075   1789    438   -226   -477       O  
ATOM   4080  CB  THR B 127      -4.818  15.632 -35.307  1.00 18.18           C  
ANISOU 4080  CB  THR B 127     2047   2903   1958    330    -18    -72       C  
ATOM   4081  OG1 THR B 127      -3.611  16.292 -35.726  1.00 18.64           O  
ANISOU 4081  OG1 THR B 127     2168   3149   1763    363    121     54       O  
ATOM   4082  CG2 THR B 127      -5.907  16.673 -35.041  1.00 19.97           C  
ANISOU 4082  CG2 THR B 127     2151   3025   2412    443    -39      5       C  
ATOM   4083  N   SER B 128      -3.542  12.887 -35.315  1.00 16.31           N  
ANISOU 4083  N   SER B 128     1643   2840   1713    430    -61   -297       N  
ATOM   4084  CA  SER B 128      -2.529  11.921 -35.693  1.00 15.47           C  
ANISOU 4084  CA  SER B 128     1694   2560   1622    294     -8   -249       C  
ATOM   4085  C   SER B 128      -2.044  12.126 -37.119  1.00 15.78           C  
ANISOU 4085  C   SER B 128     1783   2667   1547    281    -99   -110       C  
ATOM   4086  O   SER B 128      -2.859  12.510 -38.013  1.00 18.14           O  
ANISOU 4086  O   SER B 128     1881   3425   1584    529   -232   -249       O  
ATOM   4087  CB  SER B 128      -3.113  10.499 -35.621  1.00 17.28           C  
ANISOU 4087  CB  SER B 128     2114   2735   1716     13    271   -140       C  
ATOM   4088  OG  SER B 128      -2.228   9.583 -36.259  1.00 18.78           O  
ANISOU 4088  OG  SER B 128     2473   2771   1893     40    256   -320       O  
ATOM   4089  N   ARG B 129      -0.770  11.888 -37.385  1.00 14.59           N  
ANISOU 4089  N   ARG B 129     1734   2596   1212    304   -199   -262       N  
ATOM   4090  CA  ARG B 129      -0.157  11.957 -38.703  1.00 14.04           C  
ANISOU 4090  CA  ARG B 129     1773   2300   1261     90   -141   -126       C  
ATOM   4091  C   ARG B 129      -0.083  10.606 -39.425  1.00 13.84           C  
ANISOU 4091  C   ARG B 129     1510   2408   1340     72   -126   -239       C  
ATOM   4092  O   ARG B 129       0.406  10.580 -40.575  1.00 15.55           O  
ANISOU 4092  O   ARG B 129     1971   2567   1369     36    -46   -189       O  
ATOM   4093  CB  ARG B 129       1.263  12.548 -38.626  1.00 13.82           C  
ANISOU 4093  CB  ARG B 129     1786   2192   1271     11   -122   -136       C  
ATOM   4094  CG  ARG B 129       1.300  13.935 -37.999  1.00 15.02           C  
ANISOU 4094  CG  ARG B 129     1941   2256   1510     39      4   -205       C  
ATOM   4095  CD  ARG B 129       0.857  15.063 -38.974  1.00 15.70           C  
ANISOU 4095  CD  ARG B 129     1990   2442   1535    -31   -102    -70       C  
ATOM   4096  NE  ARG B 129       0.628  16.256 -38.121  1.00 17.92           N  
ANISOU 4096  NE  ARG B 129     2304   2629   1874    -41    125   -272       N  
ATOM   4097  CZ  ARG B 129      -0.516  16.422 -37.455  1.00 19.17           C  
ANISOU 4097  CZ  ARG B 129     2332   2753   2199    -66    237   -300       C  
ATOM   4098  NH1 ARG B 129      -1.570  15.646 -37.631  1.00 19.81           N  
ANISOU 4098  NH1 ARG B 129     2320   2977   2229   -110    277   -467       N  
ATOM   4099  NH2 ARG B 129      -0.573  17.426 -36.581  1.00 19.07           N  
ANISOU 4099  NH2 ARG B 129     2232   2681   2334     36    180   -315       N  
ATOM   4100  N   PHE B 130      -0.610   9.538 -38.825  1.00 14.28           N  
ANISOU 4100  N   PHE B 130     1705   2484   1236    -52   -131   -305       N  
ATOM   4101  CA  PHE B 130      -0.529   8.209 -39.377  1.00 14.35           C  
ANISOU 4101  CA  PHE B 130     1438   2459   1554     85   -184   -205       C  
ATOM   4102  C   PHE B 130      -1.898   7.621 -39.750  1.00 14.87           C  
ANISOU 4102  C   PHE B 130     1530   2584   1535     14    -92   -340       C  
ATOM   4103  O   PHE B 130      -2.876   7.721 -39.010  1.00 16.01           O  
ANISOU 4103  O   PHE B 130     1523   2943   1617     70   -175   -307       O  
ATOM   4104  CB  PHE B 130       0.033   7.245 -38.301  1.00 14.82           C  
ANISOU 4104  CB  PHE B 130     1652   2500   1480     70   -167   -163       C  
ATOM   4105  CG  PHE B 130       1.450   7.497 -37.850  1.00 14.77           C  
ANISOU 4105  CG  PHE B 130     1613   2537   1463   -163    -71   -291       C  
ATOM   4106  CD1 PHE B 130       2.518   7.496 -38.720  1.00 16.95           C  
ANISOU 4106  CD1 PHE B 130     1751   3168   1522    -63    -63     -2       C  
ATOM   4107  CD2 PHE B 130       1.690   7.736 -36.493  1.00 15.11           C  
ANISOU 4107  CD2 PHE B 130     1643   2622   1476     47   -181   -194       C  
ATOM   4108  CE1 PHE B 130       3.827   7.697 -38.284  1.00 17.57           C  
ANISOU 4108  CE1 PHE B 130     1751   3333   1589   -185    -87     82       C  
ATOM   4109  CE2 PHE B 130       3.003   7.928 -36.039  1.00 16.06           C  
ANISOU 4109  CE2 PHE B 130     1726   2591   1785     51   -319    -61       C  
ATOM   4110  CZ  PHE B 130       4.042   7.919 -36.931  1.00 17.16           C  
ANISOU 4110  CZ  PHE B 130     1800   3046   1672   -163   -327    123       C  
ATOM   4111  N   THR B 131      -1.930   6.972 -40.922  1.00 15.69           N  
ANISOU 4111  N   THR B 131     1664   2756   1542     95   -232   -394       N  
ATOM   4112  CA  THR B 131      -3.091   6.177 -41.332  1.00 16.73           C  
ANISOU 4112  CA  THR B 131     1763   2726   1870     39   -250   -353       C  
ATOM   4113  C   THR B 131      -2.614   4.799 -41.794  1.00 16.40           C  
ANISOU 4113  C   THR B 131     1746   2802   1683     57   -154   -379       C  
ATOM   4114  O   THR B 131      -1.499   4.678 -42.345  1.00 19.16           O  
ANISOU 4114  O   THR B 131     1985   3270   2024     -1     88   -442       O  
ATOM   4115  CB ATHR B 131      -4.019   6.812 -42.365  0.51 18.18           C  
ANISOU 4115  CB ATHR B 131     1923   2889   2097    138   -309   -182       C  
ATOM   4116  OG1ATHR B 131      -3.221   7.228 -43.459  0.51 18.96           O  
ANISOU 4116  OG1ATHR B 131     2152   3008   2042    204   -277    -91       O  
ATOM   4117  CG2ATHR B 131      -4.786   7.990 -41.779  0.51 17.51           C  
ANISOU 4117  CG2ATHR B 131     1902   2867   1883     71   -249   -203       C  
ATOM   4118  CB BTHR B 131      -3.738   6.893 -42.554  0.49 17.91           C  
ANISOU 4118  CB BTHR B 131     1958   2713   2133    132   -226   -128       C  
ATOM   4119  OG1BTHR B 131      -3.922   8.292 -42.247  0.49 18.99           O  
ANISOU 4119  OG1BTHR B 131     2098   2788   2330    207   -345   -262       O  
ATOM   4120  CG2BTHR B 131      -5.093   6.321 -42.948  0.49 18.02           C  
ANISOU 4120  CG2BTHR B 131     2099   2563   2184     78   -262   -294       C  
ATOM   4121  N   CYS B 132      -3.416   3.769 -41.625  1.00 17.26           N  
ANISOU 4121  N   CYS B 132     1758   2898   1901     25   -214   -533       N  
ATOM   4122  CA  CYS B 132      -3.088   2.414 -42.040  1.00 18.25           C  
ANISOU 4122  CA  CYS B 132     1958   2905   2072     45   -290   -436       C  
ATOM   4123  C   CYS B 132      -4.390   1.713 -42.433  1.00 19.84           C  
ANISOU 4123  C   CYS B 132     2056   3272   2210     24   -345   -538       C  
ATOM   4124  O   CYS B 132      -5.305   1.658 -41.611  1.00 19.69           O  
ANISOU 4124  O   CYS B 132     1873   3402   2208   -162   -441   -578       O  
ATOM   4125  CB  CYS B 132      -2.318   1.626 -40.969  1.00 17.30           C  
ANISOU 4125  CB  CYS B 132     1923   2820   1829     61   -193   -487       C  
ATOM   4126  SG  CYS B 132      -1.793  -0.028 -41.509  1.00 17.03           S  
ANISOU 4126  SG  CYS B 132     1766   2888   1818    -52   -249   -641       S  
ATOM   4127  N   ARG B 133      -4.476   1.265 -43.681  1.00 21.05           N  
ANISOU 4127  N   ARG B 133     2254   3363   2380     53   -458   -744       N  
ATOM   4128  CA  ARG B 133      -5.686   0.618 -44.201  1.00 23.08           C  
ANISOU 4128  CA  ARG B 133     2582   3535   2651   -128   -613   -619       C  
ATOM   4129  C   ARG B 133      -6.912   1.526 -44.033  1.00 23.59           C  
ANISOU 4129  C   ARG B 133     2775   3659   2528     -3   -473   -652       C  
ATOM   4130  O   ARG B 133      -8.001   1.025 -43.701  1.00 27.44           O  
ANISOU 4130  O   ARG B 133     2867   4221   3338   -236   -545   -751       O  
ATOM   4131  CB  ARG B 133      -5.940  -0.715 -43.535  1.00 23.48           C  
ANISOU 4131  CB  ARG B 133     2477   3500   2946   -442   -592   -671       C  
ATOM   4132  CG  ARG B 133      -4.817  -1.712 -43.409  1.00 26.49           C  
ANISOU 4132  CG  ARG B 133     2924   3653   3487   -219   -663   -497       C  
ATOM   4133  CD  ARG B 133      -5.285  -3.031 -42.847  1.00 29.64           C  
ANISOU 4133  CD  ARG B 133     3494   3966   3802   -348   -482   -274       C  
ATOM   4134  NE  ARG B 133      -4.232  -3.852 -42.289  1.00 29.25           N  
ANISOU 4134  NE  ARG B 133     3461   4048   3604   -342   -640   -558       N  
ATOM   4135  CZ  ARG B 133      -4.367  -5.045 -41.753  1.00 32.64           C  
ANISOU 4135  CZ  ARG B 133     4168   4192   4040   -206   -287   -303       C  
ATOM   4136  NH1 ARG B 133      -5.573  -5.635 -41.769  1.00 34.78           N  
ANISOU 4136  NH1 ARG B 133     4316   4466   4434   -367   -179   -288       N  
ATOM   4137  NH2 ARG B 133      -3.360  -5.708 -41.216  1.00 31.19           N  
ANISOU 4137  NH2 ARG B 133     3833   4041   3977   -540   -323   -367       N  
ATOM   4138  N   GLY B 134      -6.719   2.828 -44.207  1.00 23.79           N  
ANISOU 4138  N   GLY B 134     2837   3707   2494    144   -804   -562       N  
ATOM   4139  CA  GLY B 134      -7.801   3.795 -44.092  1.00 26.56           C  
ANISOU 4139  CA  GLY B 134     3174   3961   2958    427   -540   -558       C  
ATOM   4140  C   GLY B 134      -8.160   4.181 -42.668  1.00 27.25           C  
ANISOU 4140  C   GLY B 134     3334   4071   2950    310   -503   -504       C  
ATOM   4141  O   GLY B 134      -9.122   4.940 -42.483  1.00 29.83           O  
ANISOU 4141  O   GLY B 134     3624   4621   3090    632   -607   -687       O  
ATOM   4142  N   LYS B 135      -7.493   3.631 -41.661  1.00 24.25           N  
ANISOU 4142  N   LYS B 135     2622   3937   2656    181   -357   -665       N  
ATOM   4143  CA  LYS B 135      -7.804   3.956 -40.274  1.00 23.99           C  
ANISOU 4143  CA  LYS B 135     2581   3795   2738     80   -189   -582       C  
ATOM   4144  C   LYS B 135      -6.636   4.753 -39.652  1.00 21.10           C  
ANISOU 4144  C   LYS B 135     2373   3240   2404    142   -116   -355       C  
ATOM   4145  O   LYS B 135      -5.510   4.589 -39.875  1.00 20.46           O  
ANISOU 4145  O   LYS B 135     2175   3435   2164    177   -142   -687       O  
ATOM   4146  CB  LYS B 135      -7.864   2.668 -39.443  1.00 30.53           C  
ANISOU 4146  CB  LYS B 135     3804   4422   3375    294   -146    -14       C  
ATOM   4147  CG  LYS B 135      -8.647   1.486 -39.993  1.00 39.62           C  
ANISOU 4147  CG  LYS B 135     5438   4877   4740   -152   -396   -362       C  
ATOM   4148  CD  LYS B 135     -10.097   1.519 -39.550  1.00 46.08           C  
ANISOU 4148  CD  LYS B 135     5644   5889   5976    -12   -184   -224       C  
ATOM   4149  CE  LYS B 135     -10.233   1.205 -38.070  1.00 50.80           C  
ANISOU 4149  CE  LYS B 135     6799   6415   6088      6   -266    -94       C  
ATOM   4150  NZ  LYS B 135     -11.656   1.073 -37.645  1.00 52.98           N  
ANISOU 4150  NZ  LYS B 135     6841   6761   6528     24   -204    -44       N  
ATOM   4151  N  APRO B 136      -7.213   5.583 -38.687  0.52 20.18           N  
ANISOU 4151  N  APRO B 136     2196   3190   2281    111   -210   -274       N  
ATOM   4152  CA APRO B 136      -6.254   6.371 -37.895  0.52 18.88           C  
ANISOU 4152  CA APRO B 136     2169   2882   2121    154   -107   -209       C  
ATOM   4153  C  APRO B 136      -5.472   5.473 -36.946  0.52 17.18           C  
ANISOU 4153  C  APRO B 136     1945   2649   1932    -81     32   -161       C  
ATOM   4154  O  APRO B 136      -5.958   4.499 -36.358  0.52 15.93           O  
ANISOU 4154  O  APRO B 136     1533   2646   1874   -212   -193   -228       O  
ATOM   4155  CB APRO B 136      -7.018   7.439 -37.110  0.52 19.56           C  
ANISOU 4155  CB APRO B 136     2221   2993   2219    256     -3   -169       C  
ATOM   4156  CG APRO B 136      -8.397   6.884 -37.050  0.52 20.84           C  
ANISOU 4156  CG APRO B 136     2381   3127   2411    107    122   -112       C  
ATOM   4157  CD APRO B 136      -8.625   5.931 -38.164  0.52 21.21           C  
ANISOU 4157  CD APRO B 136     2354   3185   2520    155     -3   -149       C  
ATOM   4158  N  BPRO B 136      -7.101   5.874 -38.941  0.48 19.15           N  
ANISOU 4158  N  BPRO B 136     1989   3028   2259     79   -179   -214       N  
ATOM   4159  CA BPRO B 136      -6.075   6.655 -38.204  0.48 18.16           C  
ANISOU 4159  CA BPRO B 136     2033   2673   2195    124    -95   -179       C  
ATOM   4160  C  BPRO B 136      -5.375   5.817 -37.134  0.48 17.36           C  
ANISOU 4160  C  BPRO B 136     1872   2641   2084     48      7   -150       C  
ATOM   4161  O  BPRO B 136      -6.060   5.081 -36.412  0.48 16.86           O  
ANISOU 4161  O  BPRO B 136     1875   2193   2339     64   -191     10       O  
ATOM   4162  CB BPRO B 136      -6.762   7.857 -37.542  0.48 19.12           C  
ANISOU 4162  CB BPRO B 136     2255   2775   2234    278    -73   -114       C  
ATOM   4163  CG BPRO B 136      -8.184   7.784 -37.984  0.48 19.83           C  
ANISOU 4163  CG BPRO B 136     2261   2799   2473    210    -20   -175       C  
ATOM   4164  CD BPRO B 136      -8.487   6.470 -38.605  0.48 19.46           C  
ANISOU 4164  CD BPRO B 136     2178   2817   2400    156    -22   -146       C  
ATOM   4165  CA  ILE B 137      -3.282   5.100 -35.952  1.00 15.76           C  
ANISOU 4165  CA  ILE B 137     1864   2519   1604     -9   -199   -399       C  
ATOM   4166  C   ILE B 137      -2.681   6.056 -34.908  1.00 14.96           C  
ANISOU 4166  C   ILE B 137     1789   2378   1516    -18   -103   -349       C  
ATOM   4167  O   ILE B 137      -2.219   7.133 -35.270  1.00 15.40           O  
ANISOU 4167  O   ILE B 137     1861   2452   1539     22   -112   -252       O  
ATOM   4168  CB  ILE B 137      -2.152   4.333 -36.671  1.00 16.20           C  
ANISOU 4168  CB  ILE B 137     1818   2713   1622    -60   -144   -410       C  
ATOM   4169  CG1 ILE B 137      -2.671   3.513 -37.872  1.00 17.21           C  
ANISOU 4169  CG1 ILE B 137     2057   2793   1689   -253   -108   -533       C  
ATOM   4170  CG2 ILE B 137      -1.344   3.462 -35.704  1.00 16.30           C  
ANISOU 4170  CG2 ILE B 137     1718   2810   1665   -156    -93   -374       C  
ATOM   4171  CD1 ILE B 137      -3.602   2.376 -37.477  1.00 17.99           C  
ANISOU 4171  CD1 ILE B 137     2114   2887   1836   -312    -26   -623       C  
ATOM   4172  N  AILE B 137      -4.175   5.826 -36.826  0.52 16.23           N  
ANISOU 4172  N  AILE B 137     1837   2677   1654    127   -183   -429       N  
ATOM   4173  N  BILE B 137      -4.050   5.880 -36.941  0.48 16.10           N  
ANISOU 4173  N  BILE B 137     1841   2559   1715    139   -162   -418       N  
ATOM   4174  N   HIS B 138      -2.687   5.652 -33.625  1.00 14.14           N  
ANISOU 4174  N   HIS B 138     1540   2355   1477    -11   -120   -330       N  
ATOM   4175  CA  HIS B 138      -2.139   6.518 -32.575  1.00 13.85           C  
ANISOU 4175  CA  HIS B 138     1476   2367   1419    -16    -78   -378       C  
ATOM   4176  C   HIS B 138      -0.604   6.583 -32.591  1.00 13.74           C  
ANISOU 4176  C   HIS B 138     1524   2196   1499     36    -78   -303       C  
ATOM   4177  O   HIS B 138       0.091   5.640 -32.976  1.00 13.80           O  
ANISOU 4177  O   HIS B 138     1455   2215   1574    -22    -69   -333       O  
ATOM   4178  CB AHIS B 138      -2.548   5.934 -31.189  0.53 13.98           C  
ANISOU 4178  CB AHIS B 138     1446   2274   1593     12     10   -289       C  
ATOM   4179  CG AHIS B 138      -4.032   5.979 -30.938  0.53 14.56           C  
ANISOU 4179  CG AHIS B 138     1434   2084   2015     79     13   -186       C  
ATOM   4180  ND1AHIS B 138      -4.904   4.921 -31.103  0.53 15.48           N  
ANISOU 4180  ND1AHIS B 138     1647   2122   2113    -48    -19     14       N  
ATOM   4181  CD2AHIS B 138      -4.769   7.018 -30.458  0.53 14.84           C  
ANISOU 4181  CD2AHIS B 138     1541   2011   2085     87     64   -141       C  
ATOM   4182  CE1AHIS B 138      -6.130   5.314 -30.766  0.53 17.04           C  
ANISOU 4182  CE1AHIS B 138     1842   2210   2423     16     91   -129       C  
ATOM   4183  NE2AHIS B 138      -6.096   6.570 -30.398  0.53 15.76           N  
ANISOU 4183  NE2AHIS B 138     1647   2146   2194    -43    133    -83       N  
ATOM   4184  CB BHIS B 138      -2.575   6.116 -31.154  0.47 13.70           C  
ANISOU 4184  CB BHIS B 138     1435   2248   1523    -64     12   -321       C  
ATOM   4185  CG BHIS B 138      -4.015   6.458 -30.890  0.47 13.77           C  
ANISOU 4185  CG BHIS B 138     1480   1991   1762     86     32   -139       C  
ATOM   4186  ND1BHIS B 138      -5.042   5.563 -31.088  0.47 15.15           N  
ANISOU 4186  ND1BHIS B 138     1621   1994   2141     36     28   -126       N  
ATOM   4187  CD2BHIS B 138      -4.589   7.583 -30.398  0.47 13.16           C  
ANISOU 4187  CD2BHIS B 138     1550   2022   1429     -2     66   -268       C  
ATOM   4188  CE1BHIS B 138      -6.204   6.134 -30.763  0.47 14.39           C  
ANISOU 4188  CE1BHIS B 138     1495   2148   1823    -36    -32   -172       C  
ATOM   4189  NE2BHIS B 138      -5.957   7.361 -30.341  0.47 15.61           N  
ANISOU 4189  NE2BHIS B 138     1622   2090   2218    126     30    -75       N  
ATOM   4190  N   HIS B 139      -0.110   7.719 -32.100  1.00 13.30           N  
ANISOU 4190  N   HIS B 139     1423   2236   1393    -96   -124   -233       N  
ATOM   4191  C   HIS B 139       1.569   7.374 -30.372  1.00 12.35           C  
ANISOU 4191  C   HIS B 139     1334   2061   1299    -60     39   -113       C  
ATOM   4192  O   HIS B 139       0.612   7.033 -29.641  1.00 13.36           O  
ANISOU 4192  O   HIS B 139     1360   2322   1393    -12     11    -58       O  
ATOM   4193  CA AHIS B 139       1.285   7.988 -31.762  0.59 12.56           C  
ANISOU 4193  CA AHIS B 139     1409   2069   1293    -53    -60   -177       C  
ATOM   4194  CB AHIS B 139       1.585   9.499 -31.818  0.59 13.19           C  
ANISOU 4194  CB AHIS B 139     1543   2047   1423   -100    -75    -98       C  
ATOM   4195  CG AHIS B 139       1.540  10.220 -33.130  0.59 13.91           C  
ANISOU 4195  CG AHIS B 139     1680   2219   1386     71    -90    -73       C  
ATOM   4196  ND1AHIS B 139       2.655  10.735 -33.775  0.59 13.77           N  
ANISOU 4196  ND1AHIS B 139     1736   2084   1412     12   -123    -60       N  
ATOM   4197  CD2AHIS B 139       0.487  10.569 -33.940  0.59 13.79           C  
ANISOU 4197  CD2AHIS B 139     1789   2121   1329     77   -126    -46       C  
ATOM   4198  CE1AHIS B 139       2.271  11.312 -34.918  0.59 13.79           C  
ANISOU 4198  CE1AHIS B 139     1641   2095   1504    -80    -47     42       C  
ATOM   4199  NE2AHIS B 139       0.953  11.238 -35.054  0.59 13.13           N  
ANISOU 4199  NE2AHIS B 139     1686   1846   1456     65   -147    -57       N  
ATOM   4200  CA BHIS B 139       1.299   7.885 -31.775  0.41 12.22           C  
ANISOU 4200  CA BHIS B 139     1409   1943   1291    -85    -84   -167       C  
ATOM   4201  CB BHIS B 139       1.652   9.378 -31.769  0.41 11.18           C  
ANISOU 4201  CB BHIS B 139     1384   1877    987    -72    -40    -69       C  
ATOM   4202  CG BHIS B 139       1.422   9.941 -33.139  0.41 10.30           C  
ANISOU 4202  CG BHIS B 139     1345   1579    989     -5    -69    -66       C  
ATOM   4203  ND1BHIS B 139       2.479  10.520 -33.814  0.41 10.98           N  
ANISOU 4203  ND1BHIS B 139     1412   1662   1098    -51    -69    -14       N  
ATOM   4204  CD2BHIS B 139       0.333  10.048 -33.948  0.41 10.90           C  
ANISOU 4204  CD2BHIS B 139     1396   1771    973    -38   -116   -147       C  
ATOM   4205  CE1BHIS B 139       2.045  10.950 -34.997  0.41 10.22           C  
ANISOU 4205  CE1BHIS B 139     1296   1615    972    -51    -74   -244       C  
ATOM   4206  NE2BHIS B 139       0.749  10.684 -35.101  0.41 10.54           N  
ANISOU 4206  NE2BHIS B 139     1415   1570   1020   -260   -100   -271       N  
ATOM   4207  N   PHE B 140       2.839   7.291 -29.987  1.00 12.12           N  
ANISOU 4207  N   PHE B 140     1351   2079   1175     56     17   -222       N  
ATOM   4208  CA  PHE B 140       3.282   6.753 -28.692  1.00 11.69           C  
ANISOU 4208  CA  PHE B 140     1265   1930   1245    -63     67   -100       C  
ATOM   4209  C   PHE B 140       4.328   7.677 -28.102  1.00 11.50           C  
ANISOU 4209  C   PHE B 140     1299   1833   1237    -19    107   -167       C  
ATOM   4210  O   PHE B 140       5.411   7.876 -28.710  1.00 12.25           O  
ANISOU 4210  O   PHE B 140     1432   2076   1146     22    159    -79       O  
ATOM   4211  CB  PHE B 140       3.897   5.357 -28.834  1.00 12.22           C  
ANISOU 4211  CB  PHE B 140     1505   1822   1314    -95     57   -118       C  
ATOM   4212  CG  PHE B 140       4.384   4.742 -27.535  1.00 12.45           C  
ANISOU 4212  CG  PHE B 140     1438   1957   1336     15     -6   -118       C  
ATOM   4213  CD1 PHE B 140       3.511   4.601 -26.447  1.00 13.48           C  
ANISOU 4213  CD1 PHE B 140     1408   2294   1420    -45     -5     55       C  
ATOM   4214  CD2 PHE B 140       5.687   4.275 -27.403  1.00 13.21           C  
ANISOU 4214  CD2 PHE B 140     1508   2075   1436     42     48   -185       C  
ATOM   4215  CE1 PHE B 140       3.970   4.027 -25.268  1.00 14.61           C  
ANISOU 4215  CE1 PHE B 140     1651   2360   1539    -65    -16     62       C  
ATOM   4216  CE2 PHE B 140       6.130   3.702 -26.229  1.00 14.69           C  
ANISOU 4216  CE2 PHE B 140     1668   2249   1665    123    -36    -45       C  
ATOM   4217  CZ  PHE B 140       5.262   3.574 -25.149  1.00 15.29           C  
ANISOU 4217  CZ  PHE B 140     1614   2536   1660    -55    -81     89       C  
ATOM   4218  N   LEU B 141       4.021   8.302 -26.966  1.00 11.92           N  
ANISOU 4218  N   LEU B 141     1281   1985   1261     17     71   -238       N  
ATOM   4219  CA  LEU B 141       4.899   9.239 -26.252  1.00 11.91           C  
ANISOU 4219  CA  LEU B 141     1432   1899   1195     11    201   -246       C  
ATOM   4220  C   LEU B 141       5.399  10.374 -27.147  1.00 11.78           C  
ANISOU 4220  C   LEU B 141     1321   1901   1256     43    150   -166       C  
ATOM   4221  O   LEU B 141       6.488  10.912 -26.931  1.00 12.41           O  
ANISOU 4221  O   LEU B 141     1455   2075   1186    -54     87   -267       O  
ATOM   4222  CB  LEU B 141       6.066   8.495 -25.600  1.00 12.36           C  
ANISOU 4222  CB  LEU B 141     1545   1861   1289    -56     82   -113       C  
ATOM   4223  CG  LEU B 141       5.774   7.198 -24.841  1.00 13.39           C  
ANISOU 4223  CG  LEU B 141     1795   1979   1315     25     43     13       C  
ATOM   4224  CD1 LEU B 141       7.064   6.679 -24.223  1.00 15.33           C  
ANISOU 4224  CD1 LEU B 141     1979   2268   1576     69   -199     58       C  
ATOM   4225  CD2 LEU B 141       4.710   7.348 -23.771  1.00 16.11           C  
ANISOU 4225  CD2 LEU B 141     1834   2712   1576   -257    167   -103       C  
ATOM   4226  N   GLY B 142       4.616  10.768 -28.168  1.00 12.41           N  
ANISOU 4226  N   GLY B 142     1457   1952   1304    192     84    -14       N  
ATOM   4227  CA  GLY B 142       5.058  11.819 -29.088  1.00 13.59           C  
ANISOU 4227  CA  GLY B 142     1694   2033   1435    254    272    -12       C  
ATOM   4228  C   GLY B 142       6.209  11.400 -29.976  1.00 14.19           C  
ANISOU 4228  C   GLY B 142     1832   1861   1699    273    460     71       C  
ATOM   4229  O   GLY B 142       6.785  12.267 -30.668  1.00 21.10           O  
ANISOU 4229  O   GLY B 142     3057   2179   2779    468   1347    434       O  
ATOM   4230  N   THR B 143       6.599  10.133 -30.042  1.00 10.76           N  
ANISOU 4230  N   THR B 143     1318   1688   1082    -16    153   -130       N  
ATOM   4231  CA  THR B 143       7.773   9.692 -30.807  1.00 11.49           C  
ANISOU 4231  CA  THR B 143     1428   1654   1283    119    102   -239       C  
ATOM   4232  C   THR B 143       7.476   8.657 -31.874  1.00 12.00           C  
ANISOU 4232  C   THR B 143     1561   1958   1040     -4    140   -188       C  
ATOM   4233  O   THR B 143       7.900   8.909 -33.031  1.00 17.23           O  
ANISOU 4233  O   THR B 143     2893   2460   1195   -613     -2    -83       O  
ATOM   4234  CB  THR B 143       8.896   9.192 -29.850  1.00 11.88           C  
ANISOU 4234  CB  THR B 143     1450   1820   1244    -11     54   -203       C  
ATOM   4235  OG1 THR B 143       8.454   8.073 -29.065  1.00 12.24           O  
ANISOU 4235  OG1 THR B 143     1618   1990   1043    167    -77     -6       O  
ATOM   4236  CG2 THR B 143       9.427  10.271 -28.918  1.00 12.41           C  
ANISOU 4236  CG2 THR B 143     1619   1948   1147   -136     95   -310       C  
ATOM   4237  N   SER B 144       6.893   7.518 -31.619  1.00 11.63           N  
ANISOU 4237  N   SER B 144     1557   1818   1045     18     82   -181       N  
ATOM   4238  CA  SER B 144       6.545   6.511 -32.629  1.00 11.59           C  
ANISOU 4238  CA  SER B 144     1524   1770   1109    165    114   -194       C  
ATOM   4239  C   SER B 144       7.692   6.187 -33.581  1.00 11.79           C  
ANISOU 4239  C   SER B 144     1503   1919   1057     86    102    -84       C  
ATOM   4240  O   SER B 144       7.644   6.462 -34.799  1.00 13.58           O  
ANISOU 4240  O   SER B 144     1761   2341   1057    239    138    -48       O  
ATOM   4241  CB  SER B 144       5.287   6.957 -33.416  1.00 12.67           C  
ANISOU 4241  CB  SER B 144     1395   2231   1189    -48     67   -157       C  
ATOM   4242  OG  SER B 144       4.131   6.898 -32.566  1.00 12.83           O  
ANISOU 4242  OG  SER B 144     1389   2251   1235    112    143   -160       O  
ATOM   4243  N   THR B 145       8.730   5.553 -33.037  1.00 12.27           N  
ANISOU 4243  N   THR B 145     1527   1941   1195    161    152    -40       N  
ATOM   4244  CA  THR B 145       9.976   5.316 -33.781  1.00 11.77           C  
ANISOU 4244  CA  THR B 145     1317   1780   1375   -165    166   -183       C  
ATOM   4245  C   THR B 145      10.004   4.010 -34.535  1.00 12.38           C  
ANISOU 4245  C   THR B 145     1552   1880   1274      8    232   -215       C  
ATOM   4246  O   THR B 145      10.959   3.773 -35.308  1.00 13.51           O  
ANISOU 4246  O   THR B 145     1463   2337   1333    -46    238   -315       O  
ATOM   4247  CB  THR B 145      11.219   5.444 -32.875  1.00 12.33           C  
ANISOU 4247  CB  THR B 145     1551   1891   1245    -49     66   -117       C  
ATOM   4248  OG1 THR B 145      11.259   4.333 -31.965  1.00 12.86           O  
ANISOU 4248  OG1 THR B 145     1423   2235   1230     71    111    -12       O  
ATOM   4249  CG2 THR B 145      11.173   6.734 -32.070  1.00 12.60           C  
ANISOU 4249  CG2 THR B 145     1598   1905   1285    -31     91   -101       C  
ATOM   4250  N   PHE B 146       8.985   3.154 -34.382  1.00 12.49           N  
ANISOU 4250  N   PHE B 146     1636   1935   1175   -106    190   -210       N  
ATOM   4251  CA  PHE B 146       8.926   1.894 -35.138  1.00 13.07           C  
ANISOU 4251  CA  PHE B 146     1519   1963   1485   -122    132   -234       C  
ATOM   4252  C   PHE B 146       8.256   2.096 -36.505  1.00 13.55           C  
ANISOU 4252  C   PHE B 146     1786   1928   1434   -229     80   -339       C  
ATOM   4253  O   PHE B 146       7.314   1.413 -36.903  1.00 14.55           O  
ANISOU 4253  O   PHE B 146     1617   2341   1569   -103    113   -509       O  
ATOM   4254  CB  PHE B 146       8.196   0.815 -34.349  1.00 14.03           C  
ANISOU 4254  CB  PHE B 146     1756   2086   1487   -146    216   -304       C  
ATOM   4255  CG  PHE B 146       8.864   0.321 -33.075  1.00 12.94           C  
ANISOU 4255  CG  PHE B 146     1450   1815   1651     -2    246   -235       C  
ATOM   4256  CD1 PHE B 146      10.203   0.502 -32.792  1.00 14.53           C  
ANISOU 4256  CD1 PHE B 146     1595   2286   1639     56    -11   -459       C  
ATOM   4257  CD2 PHE B 146       8.098  -0.407 -32.158  1.00 14.04           C  
ANISOU 4257  CD2 PHE B 146     1811   2008   1515   -119    164   -296       C  
ATOM   4258  CE1 PHE B 146      10.778   0.021 -31.629  1.00 14.15           C  
ANISOU 4258  CE1 PHE B 146     1670   1993   1714     34    175   -245       C  
ATOM   4259  CE2 PHE B 146       8.670  -0.902 -31.000  1.00 14.09           C  
ANISOU 4259  CE2 PHE B 146     1708   2076   1569   -121    187   -286       C  
ATOM   4260  CZ  PHE B 146      10.000  -0.686 -30.705  1.00 13.96           C  
ANISOU 4260  CZ  PHE B 146     1682   2054   1567    -41    157   -350       C  
ATOM   4261  N   SER B 147       8.811   3.030 -37.282  1.00 13.96           N  
ANISOU 4261  N   SER B 147     1633   2242   1431   -276      5   -204       N  
ATOM   4262  CA  SER B 147       8.337   3.397 -38.607  1.00 14.52           C  
ANISOU 4262  CA  SER B 147     1743   2528   1246   -217     49   -416       C  
ATOM   4263  C   SER B 147       9.490   3.999 -39.397  1.00 14.60           C  
ANISOU 4263  C   SER B 147     1838   2472   1237   -253     40   -339       C  
ATOM   4264  O   SER B 147      10.337   4.716 -38.860  1.00 15.33           O  
ANISOU 4264  O   SER B 147     1974   2614   1238   -410    234   -423       O  
ATOM   4265  CB  SER B 147       7.224   4.443 -38.527  1.00 15.18           C  
ANISOU 4265  CB  SER B 147     1648   2637   1483   -242     43   -280       C  
ATOM   4266  OG  SER B 147       6.720   4.782 -39.824  1.00 16.05           O  
ANISOU 4266  OG  SER B 147     1900   2786   1411   -100      9   -456       O  
ATOM   4267  N   GLN B 148       9.529   3.747 -40.735  1.00 14.46           N  
ANISOU 4267  N   GLN B 148     1799   2419   1277   -139    191   -441       N  
ATOM   4268  CA  GLN B 148      10.607   4.334 -41.541  1.00 13.44           C  
ANISOU 4268  CA  GLN B 148     1740   2114   1254     20    160   -391       C  
ATOM   4269  C   GLN B 148      10.592   5.845 -41.471  1.00 12.75           C  
ANISOU 4269  C   GLN B 148     1686   2138   1020    -65    -95   -353       C  
ATOM   4270  O   GLN B 148      11.670   6.486 -41.605  1.00 13.39           O  
ANISOU 4270  O   GLN B 148     1734   2241   1114   -106     34   -322       O  
ATOM   4271  CB AGLN B 148      10.480   3.755 -42.967  0.72 14.95           C  
ANISOU 4271  CB AGLN B 148     1986   2524   1170     60     63   -514       C  
ATOM   4272  CG AGLN B 148      10.890   2.291 -43.137  0.72 17.28           C  
ANISOU 4272  CG AGLN B 148     2158   2620   1789    132    101   -529       C  
ATOM   4273  CD AGLN B 148      10.809   1.804 -44.589  0.72 18.88           C  
ANISOU 4273  CD AGLN B 148     2531   2898   1746    453      8   -492       C  
ATOM   4274  OE1AGLN B 148       9.969   2.348 -45.340  0.72 20.78           O  
ANISOU 4274  OE1AGLN B 148     2375   3460   2062    595   -162   -720       O  
ATOM   4275  NE2AGLN B 148      11.719   0.909 -45.033  0.72 15.35           N  
ANISOU 4275  NE2AGLN B 148     2162   2351   1318    102   -248   -544       N  
ATOM   4276  CB BGLN B 148      10.531   3.922 -43.014  0.28 14.73           C  
ANISOU 4276  CB BGLN B 148     2054   2312   1230    239    141   -188       C  
ATOM   4277  CG BGLN B 148      11.677   2.941 -43.182  0.28 17.49           C  
ANISOU 4277  CG BGLN B 148     2367   2502   1776    514    315    159       C  
ATOM   4278  CD BGLN B 148      13.048   3.570 -43.389  0.28 19.43           C  
ANISOU 4278  CD BGLN B 148     2418   2991   1974    485    446    654       C  
ATOM   4279  OE1BGLN B 148      13.640   2.907 -44.251  0.28 16.85           O  
ANISOU 4279  OE1BGLN B 148     2514   1934   1955    467   -169    500       O  
ATOM   4280  NE2BGLN B 148      13.602   4.600 -42.702  0.28 12.30           N  
ANISOU 4280  NE2BGLN B 148     1621   2309    741   1125    951    682       N  
ATOM   4281  N   TYR B 149       9.402   6.453 -41.339  1.00 14.25           N  
ANISOU 4281  N   TYR B 149     1747   2414   1254    -19     60   -289       N  
ATOM   4282  CA  TYR B 149       9.288   7.893 -41.135  1.00 14.31           C  
ANISOU 4282  CA  TYR B 149     1812   2363   1263   -222    150    -95       C  
ATOM   4283  C   TYR B 149       8.316   8.139 -39.965  1.00 13.30           C  
ANISOU 4283  C   TYR B 149     1874   2072   1108   -133     50   -168       C  
ATOM   4284  O   TYR B 149       7.301   7.468 -39.837  1.00 14.96           O  
ANISOU 4284  O   TYR B 149     1908   2467   1310   -272    112   -435       O  
ATOM   4285  CB  TYR B 149       8.783   8.658 -42.373  1.00 15.94           C  
ANISOU 4285  CB  TYR B 149     2227   2635   1196    -24    115   -160       C  
ATOM   4286  CG  TYR B 149       9.752   8.684 -43.546  1.00 14.54           C  
ANISOU 4286  CG  TYR B 149     1824   2505   1197    -60    -36   -244       C  
ATOM   4287  CD1 TYR B 149       9.789   7.584 -44.421  1.00 16.58           C  
ANISOU 4287  CD1 TYR B 149     2235   2681   1385    -13     70   -389       C  
ATOM   4288  CD2 TYR B 149      10.608   9.735 -43.775  1.00 15.65           C  
ANISOU 4288  CD2 TYR B 149     2228   2355   1363    -57    -71    -17       C  
ATOM   4289  CE1 TYR B 149      10.665   7.558 -45.507  1.00 18.02           C  
ANISOU 4289  CE1 TYR B 149     2506   2913   1429   -165    206   -182       C  
ATOM   4290  CE2 TYR B 149      11.467   9.724 -44.869  1.00 17.81           C  
ANISOU 4290  CE2 TYR B 149     2339   2826   1600   -138     48    -13       C  
ATOM   4291  CZ  TYR B 149      11.501   8.631 -45.704  1.00 18.04           C  
ANISOU 4291  CZ  TYR B 149     2410   2907   1538    -66    274    -80       C  
ATOM   4292  OH  TYR B 149      12.332   8.560 -46.815  1.00 21.10           O  
ANISOU 4292  OH  TYR B 149     2695   3488   1834   -164    594   -105       O  
ATOM   4293  N   THR B 150       8.621   9.136 -39.142  1.00 12.97           N  
ANISOU 4293  N   THR B 150     1732   2038   1158    105    150   -264       N  
ATOM   4294  CA  THR B 150       7.729   9.601 -38.098  1.00 12.26           C  
ANISOU 4294  CA  THR B 150     1562   2033   1063     19    168   -177       C  
ATOM   4295  C   THR B 150       7.632  11.119 -38.150  1.00 12.08           C  
ANISOU 4295  C   THR B 150     1451   2018   1119     -3    -34   -154       C  
ATOM   4296  O   THR B 150       8.473  11.763 -38.794  1.00 13.77           O  
ANISOU 4296  O   THR B 150     1810   2092   1329     20    141    -33       O  
ATOM   4297  CB  THR B 150       8.151   9.099 -36.713  1.00 12.31           C  
ANISOU 4297  CB  THR B 150     1478   2000   1201     26    180     69       C  
ATOM   4298  OG1 THR B 150       7.073   9.433 -35.808  1.00 13.05           O  
ANISOU 4298  OG1 THR B 150     1504   2239   1217      0    112    -10       O  
ATOM   4299  CG2 THR B 150       9.451   9.699 -36.230  1.00 12.77           C  
ANISOU 4299  CG2 THR B 150     1569   2119   1162    -23     88    -38       C  
ATOM   4300  N   VAL B 151       6.643  11.699 -37.488  1.00 12.66           N  
ANISOU 4300  N   VAL B 151     1697   2008   1105     93    102    -96       N  
ATOM   4301  CA  VAL B 151       6.454  13.136 -37.362  1.00 12.65           C  
ANISOU 4301  CA  VAL B 151     1752   1969   1088    185     40    -69       C  
ATOM   4302  C   VAL B 151       6.391  13.428 -35.835  1.00 12.52           C  
ANISOU 4302  C   VAL B 151     1760   1860   1135     52     99     28       C  
ATOM   4303  O   VAL B 151       5.614  12.764 -35.145  1.00 13.20           O  
ANISOU 4303  O   VAL B 151     1786   2117   1113     29    144      2       O  
ATOM   4304  CB  VAL B 151       5.196  13.664 -38.063  1.00 13.79           C  
ANISOU 4304  CB  VAL B 151     1794   2258   1186    110    -60     16       C  
ATOM   4305  CG1 VAL B 151       5.119  15.177 -37.937  1.00 15.28           C  
ANISOU 4305  CG1 VAL B 151     2181   2332   1292    445   -216    -76       C  
ATOM   4306  CG2 VAL B 151       5.168  13.252 -39.543  1.00 14.55           C  
ANISOU 4306  CG2 VAL B 151     1920   2388   1221    244    -63     28       C  
ATOM   4307  N   VAL B 152       7.195  14.381 -35.393  1.00 12.14           N  
ANISOU 4307  N   VAL B 152     1806   1849    958     86     86     31       N  
ATOM   4308  CA  VAL B 152       7.236  14.736 -33.973  1.00 12.59           C  
ANISOU 4308  CA  VAL B 152     1875   1935    975     61     53    -27       C  
ATOM   4309  C   VAL B 152       7.114  16.238 -33.826  1.00 13.57           C  
ANISOU 4309  C   VAL B 152     2240   1901   1017     30    -40    -71       C  
ATOM   4310  O   VAL B 152       7.459  17.010 -34.738  1.00 15.95           O  
ANISOU 4310  O   VAL B 152     2882   2036   1142    164    187     90       O  
ATOM   4311  CB  VAL B 152       8.536  14.250 -33.302  1.00 13.64           C  
ANISOU 4311  CB  VAL B 152     1975   2043   1163    101    -77    -38       C  
ATOM   4312  CG1 VAL B 152       8.714  12.741 -33.405  1.00 14.78           C  
ANISOU 4312  CG1 VAL B 152     1994   2080   1540    105   -117     14       C  
ATOM   4313  CG2 VAL B 152       9.754  14.975 -33.771  1.00 15.41           C  
ANISOU 4313  CG2 VAL B 152     2129   2254   1472     29    114   -127       C  
ATOM   4314  N   ASP B 153       6.593  16.706 -32.698  1.00 13.22           N  
ANISOU 4314  N   ASP B 153     2112   1817   1092    149     17     -4       N  
ATOM   4315  CA  ASP B 153       6.586  18.121 -32.371  1.00 12.94           C  
ANISOU 4315  CA  ASP B 153     2068   1822   1027    115    -18    123       C  
ATOM   4316  C   ASP B 153       8.015  18.599 -32.151  1.00 12.00           C  
ANISOU 4316  C   ASP B 153     1930   1684    943    192     30      5       C  
ATOM   4317  O   ASP B 153       8.885  17.832 -31.650  1.00 13.07           O  
ANISOU 4317  O   ASP B 153     2003   1857   1106    286     36     93       O  
ATOM   4318  CB  ASP B 153       5.700  18.343 -31.144  1.00 13.54           C  
ANISOU 4318  CB  ASP B 153     2066   1973   1106    245     -2    131       C  
ATOM   4319  CG  ASP B 153       4.230  18.088 -31.490  1.00 14.50           C  
ANISOU 4319  CG  ASP B 153     2114   2099   1297    195    -69   -107       C  
ATOM   4320  OD1 ASP B 153       3.595  18.985 -32.119  1.00 16.31           O  
ANISOU 4320  OD1 ASP B 153     2284   2478   1435    329   -165     65       O  
ATOM   4321  OD2 ASP B 153       3.662  17.032 -31.120  1.00 15.57           O  
ANISOU 4321  OD2 ASP B 153     2082   2290   1544     51    -45   -120       O  
ATOM   4322  N   GLU B 154       8.318  19.860 -32.477  1.00 12.89           N  
ANISOU 4322  N   GLU B 154     2034   1837   1027     69    -80    113       N  
ATOM   4323  CA  GLU B 154       9.651  20.400 -32.295  1.00 12.37           C  
ANISOU 4323  CA  GLU B 154     1899   1832    968    179    -12    154       C  
ATOM   4324  C   GLU B 154      10.189  20.249 -30.872  1.00 12.08           C  
ANISOU 4324  C   GLU B 154     1844   1857    889    237     34     86       C  
ATOM   4325  O   GLU B 154      11.392  19.996 -30.678  1.00 13.79           O  
ANISOU 4325  O   GLU B 154     1945   2230   1065    301     44    185       O  
ATOM   4326  CB  GLU B 154       9.693  21.870 -32.779  1.00 13.57           C  
ANISOU 4326  CB  GLU B 154     2092   1919   1144     82    -35    219       C  
ATOM   4327  CG  GLU B 154      11.071  22.480 -32.723  1.00 14.07           C  
ANISOU 4327  CG  GLU B 154     2078   2013   1256     34   -141    160       C  
ATOM   4328  CD  GLU B 154      11.130  23.905 -33.253  1.00 13.69           C  
ANISOU 4328  CD  GLU B 154     1981   1994   1227     13    -16     49       C  
ATOM   4329  OE1 GLU B 154      10.123  24.626 -33.289  1.00 15.31           O  
ANISOU 4329  OE1 GLU B 154     2163   2185   1468     92    116    392       O  
ATOM   4330  OE2 GLU B 154      12.264  24.302 -33.616  1.00 16.53           O  
ANISOU 4330  OE2 GLU B 154     2116   2689   1474     37      6    479       O  
ATOM   4331  N   ILE B 155       9.343  20.427 -29.840  1.00 12.35           N  
ANISOU 4331  N   ILE B 155     1926   1860    906    358    -10     99       N  
ATOM   4332  CA  ILE B 155       9.763  20.262 -28.439  1.00 12.55           C  
ANISOU 4332  CA  ILE B 155     2036   1839    895    327    -13     57       C  
ATOM   4333  C   ILE B 155      10.120  18.824 -28.068  1.00 11.91           C  
ANISOU 4333  C   ILE B 155     1772   1804    949    252     18    138       C  
ATOM   4334  O   ILE B 155      10.632  18.569 -26.940  1.00 13.07           O  
ANISOU 4334  O   ILE B 155     2057   1996    915    296    -31    117       O  
ATOM   4335  CB  ILE B 155       8.696  20.817 -27.462  1.00 13.04           C  
ANISOU 4335  CB  ILE B 155     1910   1996   1051    406    -32     36       C  
ATOM   4336  CG1 ILE B 155       7.372  20.062 -27.560  1.00 13.72           C  
ANISOU 4336  CG1 ILE B 155     1929   2165   1120    308     -4    -70       C  
ATOM   4337  CG2 ILE B 155       8.514  22.307 -27.660  1.00 13.38           C  
ANISOU 4337  CG2 ILE B 155     1947   2015   1122    194    -87     82       C  
ATOM   4338  CD1 ILE B 155       6.395  20.326 -26.410  1.00 14.57           C  
ANISOU 4338  CD1 ILE B 155     1914   2262   1359    487     59    -69       C  
ATOM   4339  N   SER B 156       9.896  17.879 -28.974  1.00 12.30           N  
ANISOU 4339  N   SER B 156     2018   1780    874    230     17    131       N  
ATOM   4340  CA  SER B 156      10.184  16.472 -28.816  1.00 12.17           C  
ANISOU 4340  CA  SER B 156     1899   1796    928    280     36     67       C  
ATOM   4341  C   SER B 156      11.290  15.974 -29.781  1.00 11.91           C  
ANISOU 4341  C   SER B 156     1771   1767    988    168     65     43       C  
ATOM   4342  O   SER B 156      11.363  14.774 -30.073  1.00 12.55           O  
ANISOU 4342  O   SER B 156     1909   1809   1051    266    101    103       O  
ATOM   4343  CB  SER B 156       8.926  15.625 -28.988  1.00 13.09           C  
ANISOU 4343  CB  SER B 156     1912   1960   1101    241    143    145       C  
ATOM   4344  OG  SER B 156       7.932  15.871 -27.970  1.00 15.36           O  
ANISOU 4344  OG  SER B 156     2077   2036   1724    220    443    107       O  
ATOM   4345  N   VAL B 157      12.210  16.874 -30.155  1.00 11.77           N  
ANISOU 4345  N   VAL B 157     1656   1688   1128    177     73    -51       N  
ATOM   4346  CA  VAL B 157      13.363  16.444 -30.990  1.00 12.61           C  
ANISOU 4346  CA  VAL B 157     1645   2083   1062     70    230   -165       C  
ATOM   4347  C   VAL B 157      14.597  17.270 -30.622  1.00 12.24           C  
ANISOU 4347  C   VAL B 157     1655   1919   1077    145    138    -49       C  
ATOM   4348  O   VAL B 157      14.491  18.477 -30.385  1.00 13.70           O  
ANISOU 4348  O   VAL B 157     1929   1907   1368    142    -58    -17       O  
ATOM   4349  CB AVAL B 157      13.050  16.368 -32.491  0.79 14.71           C  
ANISOU 4349  CB AVAL B 157     1998   2507   1083    276    209   -112       C  
ATOM   4350  CG1AVAL B 157      12.908  17.773 -33.027  0.79 16.06           C  
ANISOU 4350  CG1AVAL B 157     2354   2531   1218    439    440   -131       C  
ATOM   4351  CG2AVAL B 157      14.178  15.667 -33.262  0.79 13.61           C  
ANISOU 4351  CG2AVAL B 157     2081   1967   1123    100    232   -204       C  
ATOM   4352  CB BVAL B 157      13.054  16.617 -32.491  0.21 12.49           C  
ANISOU 4352  CB BVAL B 157     1558   2025   1162    195     94    -16       C  
ATOM   4353  CG1BVAL B 157      12.387  17.956 -32.779  0.21 12.82           C  
ANISOU 4353  CG1BVAL B 157     1617   2050   1202    136    123    185       C  
ATOM   4354  CG2BVAL B 157      14.287  16.473 -33.388  0.21 11.70           C  
ANISOU 4354  CG2BVAL B 157     1597   1851    998    113     53   -141       C  
ATOM   4355  N   ALA B 158      15.765  16.618 -30.575  1.00 12.00           N  
ANISOU 4355  N   ALA B 158     1598   1761   1200     90     41    -10       N  
ATOM   4356  CA  ALA B 158      17.047  17.282 -30.379  1.00 12.78           C  
ANISOU 4356  CA  ALA B 158     1702   1958   1197     21     13     71       C  
ATOM   4357  C   ALA B 158      18.003  17.021 -31.532  1.00 12.70           C  
ANISOU 4357  C   ALA B 158     1867   1745   1213    -80     12      6       C  
ATOM   4358  O   ALA B 158      18.170  15.889 -31.990  1.00 12.48           O  
ANISOU 4358  O   ALA B 158     1903   1728   1110    -71    167     35       O  
ATOM   4359  CB  ALA B 158      17.750  16.812 -29.080  1.00 14.31           C  
ANISOU 4359  CB  ALA B 158     1659   2536   1241     87    -26     38       C  
ATOM   4360  N   LYS B 159      18.688  18.083 -31.974  1.00 13.00           N  
ANISOU 4360  N   LYS B 159     1935   1596   1409     23    168     63       N  
ATOM   4361  CA  LYS B 159      19.765  18.025 -32.973  1.00 14.17           C  
ANISOU 4361  CA  LYS B 159     1952   2078   1353   -125    161    113       C  
ATOM   4362  C   LYS B 159      21.046  17.502 -32.334  1.00 13.29           C  
ANISOU 4362  C   LYS B 159     2073   1893   1083    -87    214     85       C  
ATOM   4363  O   LYS B 159      21.416  17.969 -31.237  1.00 14.42           O  
ANISOU 4363  O   LYS B 159     2099   2139   1242     -1    118    -43       O  
ATOM   4364  CB  LYS B 159      20.047  19.433 -33.537  1.00 15.42           C  
ANISOU 4364  CB  LYS B 159     2025   2226   1608    -54     52    289       C  
ATOM   4365  CG  LYS B 159      21.130  19.416 -34.617  1.00 17.00           C  
ANISOU 4365  CG  LYS B 159     2296   2533   1631   -108    163    489       C  
ATOM   4366  CD  LYS B 159      21.420  20.821 -35.143  1.00 18.97           C  
ANISOU 4366  CD  LYS B 159     2658   2636   1914   -157     64    484       C  
ATOM   4367  CE  LYS B 159      22.562  20.806 -36.154  1.00 21.11           C  
ANISOU 4367  CE  LYS B 159     3053   3011   1956    -84    274    194       C  
ATOM   4368  NZ  LYS B 159      22.912  22.214 -36.577  1.00 26.23           N  
ANISOU 4368  NZ  LYS B 159     3809   3304   2853   -253    242    444       N  
ATOM   4369  N   ILE B 160      21.757  16.589 -32.984  1.00 13.14           N  
ANISOU 4369  N   ILE B 160     1773   1898   1321    -56    166     42       N  
ATOM   4370  CA  ILE B 160      22.977  15.989 -32.453  1.00 13.22           C  
ANISOU 4370  CA  ILE B 160     1928   1954   1141    -69    144     40       C  
ATOM   4371  C   ILE B 160      24.117  16.073 -33.476  1.00 14.29           C  
ANISOU 4371  C   ILE B 160     2005   2138   1288    -91    206     69       C  
ATOM   4372  O   ILE B 160      23.914  16.454 -34.655  1.00 15.08           O  
ANISOU 4372  O   ILE B 160     2111   2329   1288   -265    253     69       O  
ATOM   4373  CB  ILE B 160      22.734  14.541 -31.998  1.00 13.50           C  
ANISOU 4373  CB  ILE B 160     1921   1904   1306    -23    147      9       C  
ATOM   4374  CG1 ILE B 160      22.384  13.608 -33.158  1.00 13.54           C  
ANISOU 4374  CG1 ILE B 160     1908   1874   1363   -161     56     -3       C  
ATOM   4375  CG2 ILE B 160      21.675  14.484 -30.887  1.00 13.37           C  
ANISOU 4375  CG2 ILE B 160     1957   1810   1312   -245    202    -32       C  
ATOM   4376  CD1 ILE B 160      22.502  12.143 -32.847  1.00 13.99           C  
ANISOU 4376  CD1 ILE B 160     1859   1892   1565    -45    250     94       C  
ATOM   4377  N   ASP B 161      25.337  15.754 -33.026  1.00 15.19           N  
ANISOU 4377  N   ASP B 161     1921   2344   1505    -76    270    117       N  
ATOM   4378  CA  ASP B 161      26.562  15.842 -33.835  1.00 17.09           C  
ANISOU 4378  CA  ASP B 161     2135   2655   1702   -174    398   -130       C  
ATOM   4379  C   ASP B 161      26.350  15.167 -35.170  1.00 16.05           C  
ANISOU 4379  C   ASP B 161     2091   2349   1658   -240    336    -71       C  
ATOM   4380  O   ASP B 161      26.013  13.978 -35.256  1.00 15.46           O  
ANISOU 4380  O   ASP B 161     1932   2382   1561   -220    488    -66       O  
ATOM   4381  CB  ASP B 161      27.725  15.214 -33.070  1.00 20.06           C  
ANISOU 4381  CB  ASP B 161     2242   3323   2058   -136    185   -111       C  
ATOM   4382  CG  ASP B 161      29.127  15.315 -33.624  1.00 22.39           C  
ANISOU 4382  CG  ASP B 161     2462   3657   2388   -234    331    -72       C  
ATOM   4383  OD1 ASP B 161      29.343  15.428 -34.851  1.00 22.12           O  
ANISOU 4383  OD1 ASP B 161     2172   3913   2320   -176    206   -128       O  
ATOM   4384  OD2 ASP B 161      30.079  15.220 -32.804  1.00 26.69           O  
ANISOU 4384  OD2 ASP B 161     2716   4531   2893    -99    185    179       O  
ATOM   4385  N   ALA B 162      26.694  15.836 -36.285  1.00 16.92           N  
ANISOU 4385  N   ALA B 162     2188   2491   1751   -317    405    -26       N  
ATOM   4386  CA  ALA B 162      26.567  15.286 -37.628  1.00 16.50           C  
ANISOU 4386  CA  ALA B 162     2244   2403   1624    -67    381    143       C  
ATOM   4387  C   ALA B 162      27.442  14.063 -37.880  1.00 15.57           C  
ANISOU 4387  C   ALA B 162     2020   2357   1538   -179    389    157       C  
ATOM   4388  O   ALA B 162      27.156  13.309 -38.825  1.00 16.83           O  
ANISOU 4388  O   ALA B 162     2111   2643   1642   -220    334     13       O  
ATOM   4389  CB  ALA B 162      26.886  16.358 -38.692  1.00 17.87           C  
ANISOU 4389  CB  ALA B 162     2357   2624   1807   -243    324    236       C  
ATOM   4390  N   ALA B 163      28.509  13.874 -37.106  1.00 16.35           N  
ANISOU 4390  N   ALA B 163     1898   2558   1758   -301    387    249       N  
ATOM   4391  CA  ALA B 163      29.396  12.727 -37.281  1.00 17.37           C  
ANISOU 4391  CA  ALA B 163     2109   2514   1976   -209    356    225       C  
ATOM   4392  C   ALA B 163      29.035  11.551 -36.393  1.00 17.26           C  
ANISOU 4392  C   ALA B 163     2158   2592   1807   -139    404    192       C  
ATOM   4393  O   ALA B 163      29.700  10.500 -36.373  1.00 19.10           O  
ANISOU 4393  O   ALA B 163     2336   2787   2132    -31    538    275       O  
ATOM   4394  CB  ALA B 163      30.863  13.106 -36.988  1.00 19.35           C  
ANISOU 4394  CB  ALA B 163     2186   2944   2221   -282    393    330       C  
ATOM   4395  N   SER B 164      27.899  11.615 -35.649  1.00 16.86           N  
ANISOU 4395  N   SER B 164     2200   2549   1655   -304    465    247       N  
ATOM   4396  CA  SER B 164      27.668  10.498 -34.692  1.00 18.13           C  
ANISOU 4396  CA  SER B 164     2291   2548   2050   -280    328    397       C  
ATOM   4397  C   SER B 164      27.110   9.257 -35.345  1.00 15.57           C  
ANISOU 4397  C   SER B 164     1586   2449   1881   -151    482    294       C  
ATOM   4398  O   SER B 164      26.370   9.277 -36.346  1.00 16.37           O  
ANISOU 4398  O   SER B 164     2008   2435   1776     42    376    285       O  
ATOM   4399  CB  SER B 164      26.950  10.919 -33.430  1.00 23.00           C  
ANISOU 4399  CB  SER B 164     2910   3293   2536     60    569    376       C  
ATOM   4400  OG  SER B 164      25.759  11.506 -33.812  1.00 24.26           O  
ANISOU 4400  OG  SER B 164     2750   4124   2341    295   1050   1235       O  
ATOM   4401  N   PRO B 165      27.467   8.106 -34.787  1.00 14.97           N  
ANISOU 4401  N   PRO B 165     1563   2422   1703   -115    402    175       N  
ATOM   4402  CA  PRO B 165      27.028   6.800 -35.308  1.00 15.75           C  
ANISOU 4402  CA  PRO B 165     1809   2442   1735    -77    377     88       C  
ATOM   4403  C   PRO B 165      25.633   6.494 -34.802  1.00 14.13           C  
ANISOU 4403  C   PRO B 165     1744   2200   1423    -51    332     48       C  
ATOM   4404  O   PRO B 165      25.442   6.160 -33.612  1.00 15.55           O  
ANISOU 4404  O   PRO B 165     1946   2538   1426    -32    429     36       O  
ATOM   4405  CB  PRO B 165      28.094   5.811 -34.815  1.00 16.82           C  
ANISOU 4405  CB  PRO B 165     1899   2683   1807     35    393    185       C  
ATOM   4406  CG  PRO B 165      28.599   6.451 -33.544  1.00 17.15           C  
ANISOU 4406  CG  PRO B 165     1909   2627   1978    142    201    199       C  
ATOM   4407  CD  PRO B 165      28.481   7.952 -33.728  1.00 16.94           C  
ANISOU 4407  CD  PRO B 165     1879   2572   1984   -109    212    256       C  
ATOM   4408  N   LEU B 166      24.629   6.619 -35.664  1.00 14.46           N  
ANISOU 4408  N   LEU B 166     1666   2281   1548    -59    388    -28       N  
ATOM   4409  CA  LEU B 166      23.235   6.488 -35.237  1.00 13.35           C  
ANISOU 4409  CA  LEU B 166     1659   1849   1563    -91    332     -9       C  
ATOM   4410  C   LEU B 166      22.828   5.139 -34.685  1.00 13.33           C  
ANISOU 4410  C   LEU B 166     1819   1819   1426     -7    320    -25       C  
ATOM   4411  O   LEU B 166      21.959   5.067 -33.784  1.00 14.08           O  
ANISOU 4411  O   LEU B 166     1569   2220   1561    -92    356    -73       O  
ATOM   4412  CB  LEU B 166      22.300   6.943 -36.362  1.00 15.31           C  
ANISOU 4412  CB  LEU B 166     2068   1919   1831     39    182      9       C  
ATOM   4413  CG  LEU B 166      22.463   8.395 -36.811  1.00 16.27           C  
ANISOU 4413  CG  LEU B 166     2125   2005   2053   -135    196    153       C  
ATOM   4414  CD1 LEU B 166      21.387   8.792 -37.805  1.00 19.38           C  
ANISOU 4414  CD1 LEU B 166     2187   2167   3008   -311   -210    416       C  
ATOM   4415  CD2 LEU B 166      22.498   9.380 -35.631  1.00 19.62           C  
ANISOU 4415  CD2 LEU B 166     2692   2326   2435   -295    531   -126       C  
ATOM   4416  N   GLU B 167      23.500   4.082 -35.124  1.00 13.45           N  
ANISOU 4416  N   GLU B 167     1776   1925   1411     42    348   -142       N  
ATOM   4417  CA  GLU B 167      23.251   2.727 -34.626  1.00 14.95           C  
ANISOU 4417  CA  GLU B 167     2171   2047   1461    126    249    -35       C  
ATOM   4418  C   GLU B 167      23.757   2.546 -33.203  1.00 13.76           C  
ANISOU 4418  C   GLU B 167     1612   2092   1526     83    178   -124       C  
ATOM   4419  O   GLU B 167      23.452   1.531 -32.589  1.00 16.93           O  
ANISOU 4419  O   GLU B 167     2375   2181   1878    -92    -35    -43       O  
ATOM   4420  CB AGLU B 167      23.840   1.679 -35.571  0.63 16.20           C  
ANISOU 4420  CB AGLU B 167     2335   2236   1585    254    234   -164       C  
ATOM   4421  CG AGLU B 167      25.308   1.397 -35.507  0.63 18.66           C  
ANISOU 4421  CG AGLU B 167     2356   2605   2129    356    304   -263       C  
ATOM   4422  CD AGLU B 167      26.280   2.424 -36.012  0.63 20.01           C  
ANISOU 4422  CD AGLU B 167     2623   2753   2227    302    399   -189       C  
ATOM   4423  OE1AGLU B 167      25.907   3.499 -36.522  0.63 20.60           O  
ANISOU 4423  OE1AGLU B 167     2661   2832   2332    453    625   -136       O  
ATOM   4424  OE2AGLU B 167      27.520   2.179 -35.911  0.63 23.51           O  
ANISOU 4424  OE2AGLU B 167     2723   3438   2771    500    331   -168       O  
ATOM   4425  CB BGLU B 167      23.969   1.769 -35.596  0.37 17.40           C  
ANISOU 4425  CB BGLU B 167     2372   2278   1961    215    329   -227       C  
ATOM   4426  CG BGLU B 167      23.497   1.866 -37.029  0.37 20.17           C  
ANISOU 4426  CG BGLU B 167     2688   2840   2137    155    121   -195       C  
ATOM   4427  CD BGLU B 167      24.111   2.905 -37.936  0.37 23.46           C  
ANISOU 4427  CD BGLU B 167     2980   3217   2715    -40    353    -45       C  
ATOM   4428  OE1BGLU B 167      24.890   3.788 -37.510  0.37 23.69           O  
ANISOU 4428  OE1BGLU B 167     3015   3315   2671     28    326   -257       O  
ATOM   4429  OE2BGLU B 167      23.791   2.838 -39.153  0.37 26.57           O  
ANISOU 4429  OE2BGLU B 167     3396   3891   2807     42    205     12       O  
ATOM   4430  N   LYS B 168      24.520   3.480 -32.661  1.00 13.31           N  
ANISOU 4430  N   LYS B 168     1636   2011   1410    -59    334    -72       N  
ATOM   4431  CA  LYS B 168      24.932   3.440 -31.254  1.00 13.84           C  
ANISOU 4431  CA  LYS B 168     1664   2113   1480     35    276    -98       C  
ATOM   4432  C   LYS B 168      24.181   4.502 -30.424  1.00 12.49           C  
ANISOU 4432  C   LYS B 168     1572   1926   1248    131    127     25       C  
ATOM   4433  O   LYS B 168      23.617   4.202 -29.355  1.00 13.11           O  
ANISOU 4433  O   LYS B 168     1525   2136   1321     80    198     15       O  
ATOM   4434  CB ALYS B 168      26.435   3.802 -31.165  0.67 15.48           C  
ANISOU 4434  CB ALYS B 168     1664   2424   1794    187    226   -190       C  
ATOM   4435  CG ALYS B 168      27.428   3.033 -32.022  0.67 17.02           C  
ANISOU 4435  CG ALYS B 168     2126   2515   1825    240    439   -157       C  
ATOM   4436  CD ALYS B 168      27.448   1.548 -31.701  0.67 18.51           C  
ANISOU 4436  CD ALYS B 168     2462   2570   2001    232    332   -132       C  
ATOM   4437  CE ALYS B 168      28.489   0.858 -32.605  0.67 19.01           C  
ANISOU 4437  CE ALYS B 168     2712   2750   1759    331    381    -71       C  
ATOM   4438  NZ ALYS B 168      28.517  -0.595 -32.267  0.67 20.33           N  
ANISOU 4438  NZ ALYS B 168     3001   2742   1981    233    463   -245       N  
ATOM   4439  CB BLYS B 168      26.436   3.593 -31.067  0.34 14.09           C  
ANISOU 4439  CB BLYS B 168     1652   2142   1559    147    280   -145       C  
ATOM   4440  CG BLYS B 168      27.209   2.425 -31.680  0.34 14.45           C  
ANISOU 4440  CG BLYS B 168     1871   1941   1678    149    267    -96       C  
ATOM   4441  CD BLYS B 168      28.691   2.733 -31.600  0.34 15.71           C  
ANISOU 4441  CD BLYS B 168     1923   2350   1696     17    256   -188       C  
ATOM   4442  CE BLYS B 168      29.477   1.824 -32.528  0.34 16.35           C  
ANISOU 4442  CE BLYS B 168     2029   2410   1772     15    231   -323       C  
ATOM   4443  NZ BLYS B 168      29.351   0.395 -32.203  0.34 16.77           N  
ANISOU 4443  NZ BLYS B 168     2257   2433   1680     48    387   -348       N  
ATOM   4444  N   VAL B 169      24.170   5.762 -30.911  1.00 12.26           N  
ANISOU 4444  N   VAL B 169     1592   1791   1277    -37    202    -44       N  
ATOM   4445  CA  VAL B 169      23.642   6.866 -30.090  1.00 12.74           C  
ANISOU 4445  CA  VAL B 169     1608   1946   1286    -38    161    -23       C  
ATOM   4446  C   VAL B 169      22.132   6.852 -29.961  1.00 12.16           C  
ANISOU 4446  C   VAL B 169     1552   1838   1230   -123    163    -81       C  
ATOM   4447  O   VAL B 169      21.608   7.521 -29.038  1.00 12.26           O  
ANISOU 4447  O   VAL B 169     1766   1682   1211   -106    262      6       O  
ATOM   4448  CB  VAL B 169      24.144   8.255 -30.509  1.00 13.65           C  
ANISOU 4448  CB  VAL B 169     1790   1892   1505   -141    241   -111       C  
ATOM   4449  CG1 VAL B 169      25.659   8.356 -30.427  1.00 16.35           C  
ANISOU 4449  CG1 VAL B 169     1833   2449   1932   -329    319   -203       C  
ATOM   4450  CG2 VAL B 169      23.650   8.660 -31.896  1.00 14.89           C  
ANISOU 4450  CG2 VAL B 169     2080   2137   1439   -200    332     41       C  
ATOM   4451  N   CYS B 170      21.369   6.036 -30.708  1.00 11.04           N  
ANISOU 4451  N   CYS B 170     1379   1631   1184   -117    167     58       N  
ATOM   4452  CA  CYS B 170      19.960   5.819 -30.417  1.00 10.86           C  
ANISOU 4452  CA  CYS B 170     1305   1707   1115    -34    158     25       C  
ATOM   4453  C   CYS B 170      19.729   5.440 -28.943  1.00 10.44           C  
ANISOU 4453  C   CYS B 170     1340   1482   1143     70     94    -55       C  
ATOM   4454  O   CYS B 170      18.672   5.805 -28.385  1.00 10.78           O  
ANISOU 4454  O   CYS B 170     1279   1603   1214      0     87     77       O  
ATOM   4455  CB  CYS B 170      19.350   4.745 -31.344  1.00 11.85           C  
ANISOU 4455  CB  CYS B 170     1452   1787   1264   -234     57     90       C  
ATOM   4456  SG  CYS B 170      20.190   3.139 -31.324  1.00 13.15           S  
ANISOU 4456  SG  CYS B 170     1912   1814   1271    -24     69   -133       S  
ATOM   4457  N   LEU B 171      20.669   4.756 -28.272  1.00 10.26           N  
ANISOU 4457  N   LEU B 171     1268   1538   1092      5    184     -5       N  
ATOM   4458  CA  LEU B 171      20.520   4.396 -26.864  1.00 11.00           C  
ANISOU 4458  CA  LEU B 171     1499   1648   1034     33    200     72       C  
ATOM   4459  C   LEU B 171      20.443   5.582 -25.923  1.00 10.64           C  
ANISOU 4459  C   LEU B 171     1367   1584   1091    117     88    225       C  
ATOM   4460  O   LEU B 171      19.917   5.475 -24.785  1.00 11.41           O  
ANISOU 4460  O   LEU B 171     1548   1705   1083     29    148    106       O  
ATOM   4461  CB  LEU B 171      21.640   3.429 -26.444  1.00 12.31           C  
ANISOU 4461  CB  LEU B 171     1625   1707   1345     39    153     51       C  
ATOM   4462  CG  LEU B 171      21.590   2.073 -27.139  1.00 14.55           C  
ANISOU 4462  CG  LEU B 171     2131   1827   1569    134    147   -160       C  
ATOM   4463  CD1 LEU B 171      22.837   1.283 -26.761  1.00 20.31           C  
ANISOU 4463  CD1 LEU B 171     2871   2395   2453    539   -501   -403       C  
ATOM   4464  CD2 LEU B 171      20.298   1.344 -26.814  1.00 20.35           C  
ANISOU 4464  CD2 LEU B 171     2926   2071   2736   -240    872   -382       C  
ATOM   4465  N   ILE B 172      20.969   6.739 -26.323  1.00 10.30           N  
ANISOU 4465  N   ILE B 172     1399   1495   1022     89    162     96       N  
ATOM   4466  CA  ILE B 172      20.870   7.972 -25.549  1.00  9.90           C  
ANISOU 4466  CA  ILE B 172     1337   1424   1002     45     -9     94       C  
ATOM   4467  C   ILE B 172      19.417   8.483 -25.550  1.00 10.58           C  
ANISOU 4467  C   ILE B 172     1314   1598   1108     72     51     74       C  
ATOM   4468  O   ILE B 172      19.010   9.235 -24.650  1.00 11.36           O  
ANISOU 4468  O   ILE B 172     1535   1650   1132     56     84     27       O  
ATOM   4469  CB  ILE B 172      21.908   8.997 -26.061  1.00 10.86           C  
ANISOU 4469  CB  ILE B 172     1410   1650   1066    -74     21     86       C  
ATOM   4470  CG1 ILE B 172      23.320   8.506 -25.691  1.00 12.20           C  
ANISOU 4470  CG1 ILE B 172     1465   1812   1358     61    165    154       C  
ATOM   4471  CG2 ILE B 172      21.673  10.399 -25.562  1.00 12.12           C  
ANISOU 4471  CG2 ILE B 172     1659   1674   1273   -118    144    182       C  
ATOM   4472  CD1 ILE B 172      24.465   9.188 -26.393  1.00 13.93           C  
ANISOU 4472  CD1 ILE B 172     1573   2153   1565   -141    249     27       C  
ATOM   4473  N   GLY B 173      18.563   8.006 -26.476  1.00 10.60           N  
ANISOU 4473  N   GLY B 173     1280   1628   1117    108     91    125       N  
ATOM   4474  CA  GLY B 173      17.140   8.332 -26.476  1.00 10.79           C  
ANISOU 4474  CA  GLY B 173     1235   1678   1186     38     76    113       C  
ATOM   4475  C   GLY B 173      16.338   7.640 -25.354  1.00 10.26           C  
ANISOU 4475  C   GLY B 173     1394   1446   1057    146     57     -3       C  
ATOM   4476  O   GLY B 173      15.181   8.041 -25.117  1.00 10.58           O  
ANISOU 4476  O   GLY B 173     1355   1557   1107    125     95    115       O  
ATOM   4477  N   CYS B 174      16.869   6.616 -24.697  1.00  9.95           N  
ANISOU 4477  N   CYS B 174     1358   1474    946     39    121     40       N  
ATOM   4478  CA  CYS B 174      16.140   6.092 -23.554  1.00 10.18           C  
ANISOU 4478  CA  CYS B 174     1331   1599    936     43    159     48       C  
ATOM   4479  C   CYS B 174      17.069   5.380 -22.564  1.00  9.84           C  
ANISOU 4479  C   CYS B 174     1344   1463    930     75    187     39       C  
ATOM   4480  O   CYS B 174      17.352   5.929 -21.478  1.00 10.25           O  
ANISOU 4480  O   CYS B 174     1387   1518    988     99     74     46       O  
ATOM   4481  CB  CYS B 174      14.958   5.180 -23.898  1.00 10.09           C  
ANISOU 4481  CB  CYS B 174     1395   1530    908     27    135     61       C  
ATOM   4482  SG  CYS B 174      14.196   4.639 -22.308  1.00 10.36           S  
ANISOU 4482  SG  CYS B 174     1339   1611    987   -136     97     13       S  
ATOM   4483  N   GLY B 175      17.552   4.180 -22.874  1.00  9.93           N  
ANISOU 4483  N   GLY B 175     1368   1482    924     38    140     31       N  
ATOM   4484  CA  GLY B 175      18.068   3.334 -21.815  1.00 10.56           C  
ANISOU 4484  CA  GLY B 175     1493   1396   1123     57     73      1       C  
ATOM   4485  C   GLY B 175      19.348   3.800 -21.145  1.00  9.82           C  
ANISOU 4485  C   GLY B 175     1262   1441   1029    157    134    -20       C  
ATOM   4486  O   GLY B 175      19.466   3.717 -19.903  1.00 10.72           O  
ANISOU 4486  O   GLY B 175     1380   1605   1087     61     38     98       O  
ATOM   4487  N   PHE B 176      20.311   4.253 -21.945  1.00 10.29           N  
ANISOU 4487  N   PHE B 176     1362   1474   1073     66    161     63       N  
ATOM   4488  CA  PHE B 176      21.570   4.720 -21.373  1.00 10.56           C  
ANISOU 4488  CA  PHE B 176     1241   1644   1128     88    200    100       C  
ATOM   4489  C   PHE B 176      21.310   5.932 -20.477  1.00 10.45           C  
ANISOU 4489  C   PHE B 176     1332   1633   1005     92     20     61       C  
ATOM   4490  O   PHE B 176      21.723   6.005 -19.297  1.00 10.98           O  
ANISOU 4490  O   PHE B 176     1348   1771   1051     96     58    129       O  
ATOM   4491  CB  PHE B 176      22.670   5.056 -22.410  1.00 10.74           C  
ANISOU 4491  CB  PHE B 176     1263   1625   1191    168    186    133       C  
ATOM   4492  CG  PHE B 176      23.839   5.735 -21.756  1.00 11.61           C  
ANISOU 4492  CG  PHE B 176     1280   1884   1248    109    229    -15       C  
ATOM   4493  CD1 PHE B 176      24.786   4.977 -21.058  1.00 12.67           C  
ANISOU 4493  CD1 PHE B 176     1432   2036   1347    203    113    -80       C  
ATOM   4494  CD2 PHE B 176      23.958   7.096 -21.704  1.00 11.86           C  
ANISOU 4494  CD2 PHE B 176     1464   1840   1202    127    291    174       C  
ATOM   4495  CE1 PHE B 176      25.832   5.575 -20.344  1.00 13.17           C  
ANISOU 4495  CE1 PHE B 176     1503   2194   1307     28    253     83       C  
ATOM   4496  CE2 PHE B 176      24.980   7.721 -21.022  1.00 12.98           C  
ANISOU 4496  CE2 PHE B 176     1678   1818   1437   -151    329    263       C  
ATOM   4497  CZ  PHE B 176      25.919   6.957 -20.329  1.00 13.22           C  
ANISOU 4497  CZ  PHE B 176     1408   2233   1383   -126    280     53       C  
ATOM   4498  N   SER B 177      20.640   6.959 -21.028  1.00 10.01           N  
ANISOU 4498  N   SER B 177     1270   1471   1064    102    107     48       N  
ATOM   4499  CA  SER B 177      20.460   8.217 -20.309  1.00 10.80           C  
ANISOU 4499  CA  SER B 177     1499   1566   1037    171     46     57       C  
ATOM   4500  C   SER B 177      19.661   7.986 -19.027  1.00  9.01           C  
ANISOU 4500  C   SER B 177     1158   1264   1002    171    -14     34       C  
ATOM   4501  O   SER B 177      19.951   8.580 -17.970  1.00 10.10           O  
ANISOU 4501  O   SER B 177     1445   1352   1039     80    -33     34       O  
ATOM   4502  CB  SER B 177      19.794   9.233 -21.215  1.00 10.49           C  
ANISOU 4502  CB  SER B 177     1467   1513   1007    138    180    145       C  
ATOM   4503  OG  SER B 177      20.568   9.370 -22.410  1.00 11.67           O  
ANISOU 4503  OG  SER B 177     1502   1755   1178     41    162    251       O  
ATOM   4504  N   THR B 178      18.618   7.160 -19.128  1.00  9.67           N  
ANISOU 4504  N   THR B 178     1245   1355   1074     41     36     63       N  
ATOM   4505  CA  THR B 178      17.785   6.867 -17.944  1.00  9.56           C  
ANISOU 4505  CA  THR B 178     1305   1314   1012    182     19     72       C  
ATOM   4506  C   THR B 178      18.634   6.269 -16.847  1.00  9.22           C  
ANISOU 4506  C   THR B 178     1304   1189   1010    131    104    108       C  
ATOM   4507  O   THR B 178      18.603   6.712 -15.663  1.00  9.75           O  
ANISOU 4507  O   THR B 178     1284   1400   1018    168     65     54       O  
ATOM   4508  CB  THR B 178      16.595   5.981 -18.307  1.00  9.30           C  
ANISOU 4508  CB  THR B 178     1174   1316   1044    189     60     79       C  
ATOM   4509  OG1 THR B 178      15.739   6.650 -19.241  1.00  9.81           O  
ANISOU 4509  OG1 THR B 178     1175   1480   1074    122    -24     71       O  
ATOM   4510  CG2 THR B 178      15.806   5.612 -17.055  1.00 10.68           C  
ANISOU 4510  CG2 THR B 178     1503   1654    902    137     44     -1       C  
ATOM   4511  N   GLY B 179      19.368   5.192 -17.154  1.00  9.78           N  
ANISOU 4511  N   GLY B 179     1315   1365   1036    212     56     57       N  
ATOM   4512  CA  GLY B 179      20.081   4.539 -16.059  1.00  9.15           C  
ANISOU 4512  CA  GLY B 179     1218   1241   1017     58     88     60       C  
ATOM   4513  C   GLY B 179      21.218   5.378 -15.514  1.00  9.96           C  
ANISOU 4513  C   GLY B 179     1135   1550   1100    110     91     39       C  
ATOM   4514  O   GLY B 179      21.387   5.490 -14.280  1.00 10.05           O  
ANISOU 4514  O   GLY B 179     1334   1408   1076    121    -17    132       O  
ATOM   4515  N   TYR B 180      22.026   5.945 -16.416  1.00 10.22           N  
ANISOU 4515  N   TYR B 180     1267   1554   1061     34    102     44       N  
ATOM   4516  CA  TYR B 180      23.175   6.754 -16.029  1.00 10.84           C  
ANISOU 4516  CA  TYR B 180     1355   1656   1109    -58    169     13       C  
ATOM   4517  C   TYR B 180      22.733   7.929 -15.182  1.00  9.92           C  
ANISOU 4517  C   TYR B 180     1337   1448    986    113     10    139       C  
ATOM   4518  O   TYR B 180      23.304   8.216 -14.106  1.00 10.61           O  
ANISOU 4518  O   TYR B 180     1332   1548   1152     57    -92    140       O  
ATOM   4519  CB  TYR B 180      23.973   7.176 -17.260  1.00 11.85           C  
ANISOU 4519  CB  TYR B 180     1486   1761   1258    -35    252      1       C  
ATOM   4520  CG  TYR B 180      25.362   7.725 -17.026  1.00 13.80           C  
ANISOU 4520  CG  TYR B 180     1597   2194   1451   -207    345    -33       C  
ATOM   4521  CD1 TYR B 180      26.440   6.839 -16.908  1.00 15.03           C  
ANISOU 4521  CD1 TYR B 180     1745   2391   1576    -71    129    108       C  
ATOM   4522  CD2 TYR B 180      25.631   9.074 -16.984  1.00 18.82           C  
ANISOU 4522  CD2 TYR B 180     2038   2304   2808   -192    204    -23       C  
ATOM   4523  CE1 TYR B 180      27.748   7.287 -16.778  1.00 16.82           C  
ANISOU 4523  CE1 TYR B 180     1820   2602   1968   -145    132    173       C  
ATOM   4524  CE2 TYR B 180      26.950   9.542 -16.835  1.00 19.74           C  
ANISOU 4524  CE2 TYR B 180     2078   2299   3122   -227     82    -59       C  
ATOM   4525  CZ  TYR B 180      27.969   8.631 -16.720  1.00 18.44           C  
ANISOU 4525  CZ  TYR B 180     1854   2612   2542   -196     30      9       C  
ATOM   4526  OH  TYR B 180      29.290   9.076 -16.623  1.00 21.67           O  
ANISOU 4526  OH  TYR B 180     2029   2823   3381   -374    -94     22       O  
ATOM   4527  N   GLY B 181      21.711   8.687 -15.649  1.00  9.93           N  
ANISOU 4527  N   GLY B 181     1322   1387   1064     33      1    123       N  
ATOM   4528  CA  GLY B 181      21.197   9.820 -14.898  1.00 10.11           C  
ANISOU 4528  CA  GLY B 181     1287   1430   1123    -60     -8    -31       C  
ATOM   4529  C   GLY B 181      20.574   9.437 -13.565  1.00 10.03           C  
ANISOU 4529  C   GLY B 181     1376   1329   1105     60    -43    131       C  
ATOM   4530  O   GLY B 181      20.688  10.158 -12.547  1.00 10.48           O  
ANISOU 4530  O   GLY B 181     1518   1294   1171     34    -18    137       O  
ATOM   4531  N   SER B 182      19.872   8.301 -13.517  1.00  9.53           N  
ANISOU 4531  N   SER B 182     1203   1329   1090     28     16     74       N  
ATOM   4532  CA  SER B 182      19.294   7.852 -12.238  1.00  9.67           C  
ANISOU 4532  CA  SER B 182     1288   1359   1029     90    -30     83       C  
ATOM   4533  C   SER B 182      20.359   7.755 -11.164  1.00  9.65           C  
ANISOU 4533  C   SER B 182     1293   1298   1075     41      0    101       C  
ATOM   4534  O   SER B 182      20.107   8.092  -9.992  1.00 10.18           O  
ANISOU 4534  O   SER B 182     1468   1323   1078    127    -59     90       O  
ATOM   4535  CB  SER B 182      18.512   6.543 -12.398  1.00 10.46           C  
ANISOU 4535  CB  SER B 182     1295   1488   1191     51    -10     55       C  
ATOM   4536  OG  SER B 182      17.373   6.715 -13.235  1.00 10.54           O  
ANISOU 4536  OG  SER B 182     1304   1570   1130     83    -48     72       O  
ATOM   4537  N   ALA B 183      21.565   7.277 -11.523  1.00 10.30           N  
ANISOU 4537  N   ALA B 183     1317   1437   1157    168    -70     54       N  
ATOM   4538  CA  ALA B 183      22.686   7.220 -10.597  1.00 10.25           C  
ANISOU 4538  CA  ALA B 183     1277   1503   1113    103    -49    -50       C  
ATOM   4539  C   ALA B 183      23.322   8.579 -10.330  1.00 11.36           C  
ANISOU 4539  C   ALA B 183     1481   1581   1255     21   -119     42       C  
ATOM   4540  O   ALA B 183      23.500   8.983  -9.154  1.00 12.35           O  
ANISOU 4540  O   ALA B 183     1650   1721   1323    -13    -97    -12       O  
ATOM   4541  CB  ALA B 183      23.760   6.249 -11.100  1.00 10.97           C  
ANISOU 4541  CB  ALA B 183     1225   1617   1327     91    -99    -44       C  
ATOM   4542  N   VAL B 184      23.726   9.305 -11.390  1.00 12.35           N  
ANISOU 4542  N   VAL B 184     1792   1540   1362    -25   -109    144       N  
ATOM   4543  CA  VAL B 184      24.575  10.490 -11.192  1.00 13.85           C  
ANISOU 4543  CA  VAL B 184     1787   1787   1687   -179     65     71       C  
ATOM   4544  C   VAL B 184      23.792  11.745 -10.873  1.00 14.27           C  
ANISOU 4544  C   VAL B 184     1942   1728   1751   -121   -115    -38       C  
ATOM   4545  O   VAL B 184      24.327  12.664 -10.183  1.00 20.31           O  
ANISOU 4545  O   VAL B 184     2471   2275   2972   -192   -505   -649       O  
ATOM   4546  CB AVAL B 184      25.545  10.722 -12.377  0.67 13.76           C  
ANISOU 4546  CB AVAL B 184     1874   1802   1552   -102     -8    196       C  
ATOM   4547  CG1AVAL B 184      26.353   9.460 -12.708  0.67 15.20           C  
ANISOU 4547  CG1AVAL B 184     1722   2111   1941     26     54     45       C  
ATOM   4548  CG2AVAL B 184      24.881  11.198 -13.670  0.67 13.37           C  
ANISOU 4548  CG2AVAL B 184     1644   1906   1531   -111    -19     69       C  
ATOM   4549  CB BVAL B 184      25.493  10.704 -12.412  0.33 14.80           C  
ANISOU 4549  CB BVAL B 184     1942   2002   1681    -79     81    119       C  
ATOM   4550  CG1BVAL B 184      26.230  12.027 -12.328  0.33 16.13           C  
ANISOU 4550  CG1BVAL B 184     2038   2190   1899   -238     51    -13       C  
ATOM   4551  CG2BVAL B 184      26.504   9.566 -12.540  0.33 15.75           C  
ANISOU 4551  CG2BVAL B 184     1883   2165   1936    -35    134     42       C  
ATOM   4552  N   LYS B 185      22.563  11.875 -11.320  1.00 13.44           N  
ANISOU 4552  N   LYS B 185     1813   1619   1674   -106      4     28       N  
ATOM   4553  CA  LYS B 185      21.746  13.090 -11.142  1.00 13.82           C  
ANISOU 4553  CA  LYS B 185     1983   1545   1723    -51    -31     82       C  
ATOM   4554  C   LYS B 185      20.627  12.918 -10.129  1.00 12.54           C  
ANISOU 4554  C   LYS B 185     1894   1363   1509    105    -87     51       C  
ATOM   4555  O   LYS B 185      20.400  13.825  -9.303  1.00 15.99           O  
ANISOU 4555  O   LYS B 185     2528   1734   1814    -63     92   -262       O  
ATOM   4556  CB  LYS B 185      21.143  13.489 -12.507  1.00 15.85           C  
ANISOU 4556  CB  LYS B 185     2237   1906   1880     39    -66    234       C  
ATOM   4557  CG ALYS B 185      20.186  14.671 -12.456  0.53 16.24           C  
ANISOU 4557  CG ALYS B 185     2389   1822   1960     27    100    285       C  
ATOM   4558  CD ALYS B 185      19.797  15.245 -13.810  0.53 17.02           C  
ANISOU 4558  CD ALYS B 185     2430   2214   1825     31    -63     91       C  
ATOM   4559  CE ALYS B 185      19.406  16.709 -13.777  0.53 18.80           C  
ANISOU 4559  CE ALYS B 185     2519   2248   2376     27      1    127       C  
ATOM   4560  NZ ALYS B 185      18.080  17.021 -13.197  0.53 20.49           N  
ANISOU 4560  NZ ALYS B 185     2694   2726   2367    -34    138   -176       N  
ATOM   4561  CG BLYS B 185      20.654  14.924 -12.611  0.47 18.33           C  
ANISOU 4561  CG BLYS B 185     2392   2181   2390    261    -62    111       C  
ATOM   4562  CD BLYS B 185      20.385  15.307 -14.071  0.47 20.80           C  
ANISOU 4562  CD BLYS B 185     2718   2762   2424     65   -261    126       C  
ATOM   4563  CE BLYS B 185      19.579  16.590 -14.178  0.47 22.50           C  
ANISOU 4563  CE BLYS B 185     3093   2713   2742     84   -123    224       C  
ATOM   4564  NZ BLYS B 185      20.210  17.692 -13.391  0.47 22.81           N  
ANISOU 4564  NZ BLYS B 185     3257   2442   2969      4   -349    476       N  
ATOM   4565  N   VAL B 186      19.878  11.806 -10.130  1.00 11.79           N  
ANISOU 4565  N   VAL B 186     1655   1378   1449    118    -82     99       N  
ATOM   4566  CA  VAL B 186      18.731  11.598  -9.253  1.00 11.35           C  
ANISOU 4566  CA  VAL B 186     1647   1377   1289    257    -76     50       C  
ATOM   4567  C   VAL B 186      19.180  11.139  -7.867  1.00 11.81           C  
ANISOU 4567  C   VAL B 186     1683   1541   1265    377   -133    -81       C  
ATOM   4568  O   VAL B 186      18.960  11.821  -6.841  1.00 13.38           O  
ANISOU 4568  O   VAL B 186     2147   1710   1226    446   -158   -119       O  
ATOM   4569  CB  VAL B 186      17.709  10.639  -9.891  1.00 10.53           C  
ANISOU 4569  CB  VAL B 186     1454   1501   1047    224     -8    237       C  
ATOM   4570  CG1 VAL B 186      16.514  10.481  -8.945  1.00 11.15           C  
ANISOU 4570  CG1 VAL B 186     1521   1521   1193    201     86    127       C  
ATOM   4571  CG2 VAL B 186      17.243  11.183 -11.249  1.00 12.00           C  
ANISOU 4571  CG2 VAL B 186     1621   1857   1082    390     -8    242       C  
ATOM   4572  N   ALA B 187      19.880   9.995  -7.779  1.00 11.75           N  
ANISOU 4572  N   ALA B 187     1806   1522   1137    391   -165    -50       N  
ATOM   4573  CA  ALA B 187      20.421   9.533  -6.499  1.00 11.59           C  
ANISOU 4573  CA  ALA B 187     1744   1469   1189    216   -182     60       C  
ATOM   4574  C   ALA B 187      21.600  10.373  -6.037  1.00 12.00           C  
ANISOU 4574  C   ALA B 187     1782   1496   1281    229   -173     16       C  
ATOM   4575  O   ALA B 187      21.785  10.538  -4.802  1.00 14.38           O  
ANISOU 4575  O   ALA B 187     2140   1994   1330    457   -303   -112       O  
ATOM   4576  CB  ALA B 187      20.917   8.086  -6.647  1.00 11.73           C  
ANISOU 4576  CB  ALA B 187     1633   1566   1256    135   -178    113       C  
ATOM   4577  N   LYS B 188      22.422  10.876  -6.936  1.00 12.72           N  
ANISOU 4577  N   LYS B 188     1888   1528   1419     61   -171     71       N  
ATOM   4578  CA  LYS B 188      23.662  11.585  -6.616  1.00 13.75           C  
ANISOU 4578  CA  LYS B 188     2045   1383   1795     42   -254     69       C  
ATOM   4579  C   LYS B 188      24.592  10.664  -5.812  1.00 13.39           C  
ANISOU 4579  C   LYS B 188     1997   1418   1672    -63   -389     19       C  
ATOM   4580  O   LYS B 188      25.069  10.988  -4.712  1.00 14.64           O  
ANISOU 4580  O   LYS B 188     2161   1691   1712     -7   -402   -122       O  
ATOM   4581  CB ALYS B 188      23.478  12.972  -6.007  0.62 18.10           C  
ANISOU 4581  CB ALYS B 188     2690   1611   2575     75   -341   -191       C  
ATOM   4582  CG ALYS B 188      22.911  13.939  -7.080  0.62 21.59           C  
ANISOU 4582  CG ALYS B 188     3011   2315   2878    148   -488    123       C  
ATOM   4583  CD ALYS B 188      22.612  15.289  -6.462  0.62 24.71           C  
ANISOU 4583  CD ALYS B 188     3292   2669   3427    227   -253   -186       C  
ATOM   4584  CE ALYS B 188      22.463  16.366  -7.519  0.62 27.12           C  
ANISOU 4584  CE ALYS B 188     3717   2963   3625     92   -242     -2       C  
ATOM   4585  NZ ALYS B 188      21.311  16.189  -8.439  0.62 26.57           N  
ANISOU 4585  NZ ALYS B 188     3540   2645   3911    112   -243   -154       N  
ATOM   4586  CB BLYS B 188      23.277  12.872  -5.840  0.38 13.96           C  
ANISOU 4586  CB BLYS B 188     2099   1303   1903     70   -326     58       C  
ATOM   4587  CG BLYS B 188      22.333  13.792  -6.635  0.38 13.46           C  
ANISOU 4587  CG BLYS B 188     1844   1393   1876    104   -152     88       C  
ATOM   4588  CD BLYS B 188      22.014  15.112  -5.968  0.38 15.69           C  
ANISOU 4588  CD BLYS B 188     2220   1481   2260     78   -104    -50       C  
ATOM   4589  CE BLYS B 188      20.976  15.891  -6.774  0.38 17.27           C  
ANISOU 4589  CE BLYS B 188     2339   1847   2378    159   -219    -83       C  
ATOM   4590  NZ BLYS B 188      19.681  15.148  -6.899  0.38 17.51           N  
ANISOU 4590  NZ BLYS B 188     2285   2043   2324    209   -299   -292       N  
ATOM   4591  N   VAL B 189      24.881   9.499  -6.395  1.00 12.00           N  
ANISOU 4591  N   VAL B 189     1685   1454   1421    -62   -179     65       N  
ATOM   4592  CA  VAL B 189      25.802   8.525  -5.769  1.00 11.45           C  
ANISOU 4592  CA  VAL B 189     1493   1438   1419    -25    -58    102       C  
ATOM   4593  C   VAL B 189      27.128   9.190  -5.398  1.00 12.12           C  
ANISOU 4593  C   VAL B 189     1581   1644   1381   -115     -5    160       C  
ATOM   4594  O   VAL B 189      27.702   9.962  -6.198  1.00 13.43           O  
ANISOU 4594  O   VAL B 189     1803   1770   1529   -326   -106    165       O  
ATOM   4595  CB  VAL B 189      26.012   7.343  -6.736  1.00 11.17           C  
ANISOU 4595  CB  VAL B 189     1430   1591   1221    -27    -83     98       C  
ATOM   4596  CG1 VAL B 189      27.106   6.391  -6.244  1.00 12.20           C  
ANISOU 4596  CG1 VAL B 189     1534   1581   1519    -29   -132     28       C  
ATOM   4597  CG2 VAL B 189      24.709   6.572  -6.952  1.00 11.73           C  
ANISOU 4597  CG2 VAL B 189     1523   1513   1420    -77    -91    -24       C  
ATOM   4598  N   THR B 190      27.651   8.852  -4.212  1.00 12.65           N  
ANISOU 4598  N   THR B 190     1575   1664   1566   -221   -180    199       N  
ATOM   4599  CA  THR B 190      28.887   9.442  -3.699  1.00 13.29           C  
ANISOU 4599  CA  THR B 190     1798   1639   1612   -273   -240     81       C  
ATOM   4600  C   THR B 190      30.085   8.513  -3.790  1.00 13.45           C  
ANISOU 4600  C   THR B 190     1804   1788   1520   -266   -186    -73       C  
ATOM   4601  O   THR B 190      29.992   7.264  -3.833  1.00 13.13           O  
ANISOU 4601  O   THR B 190     1648   1707   1632    -86   -242     58       O  
ATOM   4602  CB  THR B 190      28.656   9.844  -2.217  1.00 13.34           C  
ANISOU 4602  CB  THR B 190     1862   1594   1612   -226   -224     63       C  
ATOM   4603  OG1 THR B 190      28.143   8.688  -1.530  1.00 13.98           O  
ANISOU 4603  OG1 THR B 190     2001   1770   1540   -124   -208    141       O  
ATOM   4604  CG2 THR B 190      27.707  11.024  -2.127  1.00 15.08           C  
ANISOU 4604  CG2 THR B 190     2092   1883   1755     34   -209    -67       C  
ATOM   4605  N   GLN B 191      31.278   9.125  -3.783  1.00 15.60           N  
ANISOU 4605  N   GLN B 191     1898   2103   1928   -350   -316     25       N  
ATOM   4606  CA  GLN B 191      32.514   8.358  -3.825  1.00 17.95           C  
ANISOU 4606  CA  GLN B 191     2155   2341   2325   -101   -168    178       C  
ATOM   4607  C   GLN B 191      32.655   7.498  -2.566  1.00 15.54           C  
ANISOU 4607  C   GLN B 191     1814   2094   1997     17   -234   -101       C  
ATOM   4608  O   GLN B 191      32.412   7.948  -1.443  1.00 16.55           O  
ANISOU 4608  O   GLN B 191     2010   2281   1997   -111   -252    -67       O  
ATOM   4609  CB AGLN B 191      33.716   9.313  -3.890  0.50 22.09           C  
ANISOU 4609  CB AGLN B 191     2714   2831   2848   -548   -128    118       C  
ATOM   4610  CG AGLN B 191      35.052   8.625  -3.680  0.50 28.19           C  
ANISOU 4610  CG AGLN B 191     3190   3743   3779    -42   -131    214       C  
ATOM   4611  CD AGLN B 191      35.542   7.857  -4.883  0.50 32.18           C  
ANISOU 4611  CD AGLN B 191     3850   4372   4006   -184     17    -96       C  
ATOM   4612  OE1AGLN B 191      36.052   6.737  -4.779  0.50 33.76           O  
ANISOU 4612  OE1AGLN B 191     3943   4588   4295    -42    -15     88       O  
ATOM   4613  NE2AGLN B 191      35.390   8.470  -6.053  0.50 33.45           N  
ANISOU 4613  NE2AGLN B 191     4053   4479   4180   -105    -27     53       N  
ATOM   4614  CB BGLN B 191      33.723   9.295  -3.933  0.50 19.98           C  
ANISOU 4614  CB BGLN B 191     2172   2679   2740   -219   -237     28       C  
ATOM   4615  CG BGLN B 191      33.762  10.086  -5.236  0.50 24.63           C  
ANISOU 4615  CG BGLN B 191     3140   3408   2810      3   -155    199       C  
ATOM   4616  CD BGLN B 191      34.949  11.040  -5.246  0.50 29.10           C  
ANISOU 4616  CD BGLN B 191     3526   3952   3578   -327    -62    150       C  
ATOM   4617  OE1BGLN B 191      36.082  10.593  -5.077  0.50 29.94           O  
ANISOU 4617  OE1BGLN B 191     3498   4158   3718   -365    -44    131       O  
ATOM   4618  NE2BGLN B 191      34.654  12.320  -5.415  0.50 31.11           N  
ANISOU 4618  NE2BGLN B 191     3753   4047   4022   -217   -108    143       N  
ATOM   4619  N   GLY B 192      33.027   6.230  -2.764  1.00 13.75           N  
ANISOU 4619  N   GLY B 192     1533   1982   1709   -104   -219     44       N  
ATOM   4620  CA  GLY B 192      33.253   5.311  -1.686  1.00 14.12           C  
ANISOU 4620  CA  GLY B 192     1616   2030   1720   -107   -259     -4       C  
ATOM   4621  C   GLY B 192      32.003   4.587  -1.202  1.00 13.49           C  
ANISOU 4621  C   GLY B 192     1599   1949   1577    -51   -237     41       C  
ATOM   4622  O   GLY B 192      32.108   3.746  -0.287  1.00 15.16           O  
ANISOU 4622  O   GLY B 192     1786   2173   1802    -41   -315    202       O  
ATOM   4623  N   SER B 193      30.821   4.861  -1.771  1.00 12.82           N  
ANISOU 4623  N   SER B 193     1485   1835   1551   -105   -192     16       N  
ATOM   4624  CA  SER B 193      29.565   4.282  -1.314  1.00 11.67           C  
ANISOU 4624  CA  SER B 193     1318   1650   1466     72    -55     38       C  
ATOM   4625  C   SER B 193      29.321   2.864  -1.788  1.00 10.82           C  
ANISOU 4625  C   SER B 193     1235   1548   1327     39   -122     19       C  
ATOM   4626  O   SER B 193      30.019   2.331  -2.678  1.00 12.52           O  
ANISOU 4626  O   SER B 193     1435   1854   1467    182    -32     -6       O  
ATOM   4627  CB  SER B 193      28.403   5.204  -1.771  1.00 12.64           C  
ANISOU 4627  CB  SER B 193     1661   1600   1540    127   -127     19       C  
ATOM   4628  OG  SER B 193      28.272   5.207  -3.188  1.00 12.79           O  
ANISOU 4628  OG  SER B 193     1500   1870   1492    111   -241     86       O  
ATOM   4629  N   THR B 194      28.310   2.230  -1.185  1.00 10.88           N  
ANISOU 4629  N   THR B 194     1233   1412   1489     68   -199     29       N  
ATOM   4630  CA  THR B 194      27.818   0.914  -1.563  1.00 10.44           C  
ANISOU 4630  CA  THR B 194     1173   1341   1452    124    -63     56       C  
ATOM   4631  C   THR B 194      26.434   1.061  -2.213  1.00 10.34           C  
ANISOU 4631  C   THR B 194     1272   1344   1314    261    -27     -1       C  
ATOM   4632  O   THR B 194      25.514   1.649  -1.598  1.00 10.95           O  
ANISOU 4632  O   THR B 194     1351   1528   1280    247    -26    -85       O  
ATOM   4633  CB  THR B 194      27.748  -0.045  -0.359  1.00 11.47           C  
ANISOU 4633  CB  THR B 194     1304   1642   1413    139   -181    162       C  
ATOM   4634  OG1 THR B 194      29.109  -0.308   0.093  1.00 12.74           O  
ANISOU 4634  OG1 THR B 194     1471   1993   1376    284   -204    227       O  
ATOM   4635  CG2 THR B 194      27.124  -1.367  -0.715  1.00 12.41           C  
ANISOU 4635  CG2 THR B 194     1231   1604   1882    217   -202    113       C  
ATOM   4636  N   CYS B 195      26.286   0.519  -3.426  1.00  9.74           N  
ANISOU 4636  N   CYS B 195     1155   1345   1202    288   -113    -64       N  
ATOM   4637  CA  CYS B 195      25.056   0.579  -4.194  1.00  9.59           C  
ANISOU 4637  CA  CYS B 195     1115   1282   1245    194    -35     77       C  
ATOM   4638  C   CYS B 195      24.483  -0.817  -4.452  1.00  9.70           C  
ANISOU 4638  C   CYS B 195     1224   1181   1282    178    -57     86       C  
ATOM   4639  O   CYS B 195      25.290  -1.766  -4.587  1.00 11.24           O  
ANISOU 4639  O   CYS B 195     1336   1275   1662    224   -109   -128       O  
ATOM   4640  CB  CYS B 195      25.331   1.207  -5.573  1.00 10.36           C  
ANISOU 4640  CB  CYS B 195     1300   1333   1305     68     -6     18       C  
ATOM   4641  SG  CYS B 195      25.917   2.949  -5.494  1.00 10.14           S  
ANISOU 4641  SG  CYS B 195     1264   1325   1264     93     27    121       S  
ATOM   4642  N   ALA B 196      23.170  -0.940  -4.543  1.00  9.57           N  
ANISOU 4642  N   ALA B 196     1196   1207   1234    174    -49    -36       N  
ATOM   4643  CA  ALA B 196      22.499  -2.167  -4.968  1.00  9.74           C  
ANISOU 4643  CA  ALA B 196     1262   1191   1247    200    -26     63       C  
ATOM   4644  C   ALA B 196      21.594  -1.845  -6.156  1.00  9.51           C  
ANISOU 4644  C   ALA B 196     1326   1054   1232    291      0     94       C  
ATOM   4645  O   ALA B 196      20.795  -0.900  -6.084  1.00 10.07           O  
ANISOU 4645  O   ALA B 196     1310   1235   1282    340    -55    -35       O  
ATOM   4646  CB  ALA B 196      21.649  -2.771  -3.853  1.00 10.82           C  
ANISOU 4646  CB  ALA B 196     1598   1380   1134    138    -63    193       C  
ATOM   4647  N   VAL B 197      21.717  -2.616  -7.248  1.00  9.69           N  
ANISOU 4647  N   VAL B 197     1256   1188   1238    272   -118     51       N  
ATOM   4648  CA  VAL B 197      20.969  -2.386  -8.480  1.00  9.50           C  
ANISOU 4648  CA  VAL B 197     1234   1244   1133    273    -61     39       C  
ATOM   4649  C   VAL B 197      20.090  -3.599  -8.774  1.00  9.61           C  
ANISOU 4649  C   VAL B 197     1271   1184   1197    254    -59    -15       C  
ATOM   4650  O   VAL B 197      20.641  -4.681  -9.044  1.00 10.39           O  
ANISOU 4650  O   VAL B 197     1293   1203   1453    258    -34    -23       O  
ATOM   4651  CB  VAL B 197      21.901  -2.073  -9.672  1.00 10.26           C  
ANISOU 4651  CB  VAL B 197     1322   1315   1260    187    -29    -39       C  
ATOM   4652  CG1 VAL B 197      21.103  -1.814 -10.952  1.00 11.20           C  
ANISOU 4652  CG1 VAL B 197     1483   1501   1273    169    -36     78       C  
ATOM   4653  CG2 VAL B 197      22.819  -0.906  -9.324  1.00 11.44           C  
ANISOU 4653  CG2 VAL B 197     1435   1595   1315      3     33     22       C  
ATOM   4654  N   PHE B 198      18.765  -3.461  -8.705  1.00  9.38           N  
ANISOU 4654  N   PHE B 198     1186   1114   1266    132     16     10       N  
ATOM   4655  CA  PHE B 198      17.815  -4.510  -8.971  1.00 10.04           C  
ANISOU 4655  CA  PHE B 198     1304   1264   1247    123     29     11       C  
ATOM   4656  C   PHE B 198      17.395  -4.468 -10.436  1.00  9.82           C  
ANISOU 4656  C   PHE B 198     1334   1125   1273    157     23    -10       C  
ATOM   4657  O   PHE B 198      16.742  -3.511 -10.872  1.00 10.20           O  
ANISOU 4657  O   PHE B 198     1444   1204   1229    274    -35     -6       O  
ATOM   4658  CB  PHE B 198      16.572  -4.379  -8.067  1.00 10.01           C  
ANISOU 4658  CB  PHE B 198     1419   1102   1284     48     99     34       C  
ATOM   4659  CG  PHE B 198      16.805  -4.606  -6.596  1.00 10.47           C  
ANISOU 4659  CG  PHE B 198     1429   1272   1278    196     48      9       C  
ATOM   4660  CD1 PHE B 198      17.460  -3.722  -5.772  1.00 11.46           C  
ANISOU 4660  CD1 PHE B 198     1431   1639   1285    147      6    -67       C  
ATOM   4661  CD2 PHE B 198      16.290  -5.760  -6.016  1.00 13.86           C  
ANISOU 4661  CD2 PHE B 198     2245   1592   1430    -69    174    174       C  
ATOM   4662  CE1 PHE B 198      17.630  -3.956  -4.410  1.00 13.10           C  
ANISOU 4662  CE1 PHE B 198     1758   1839   1381    255     65     33       C  
ATOM   4663  CE2 PHE B 198      16.448  -6.023  -4.657  1.00 15.02           C  
ANISOU 4663  CE2 PHE B 198     2442   1636   1628     -4    146    364       C  
ATOM   4664  CZ  PHE B 198      17.099  -5.096  -3.864  1.00 14.25           C  
ANISOU 4664  CZ  PHE B 198     2043   1901   1469    265    122    137       C  
ATOM   4665  N   GLY B 199      17.780  -5.507 -11.192  1.00  9.91           N  
ANISOU 4665  N   GLY B 199     1384   1160   1220    262     50     36       N  
ATOM   4666  CA  GLY B 199      17.473  -5.615 -12.618  1.00 11.18           C  
ANISOU 4666  CA  GLY B 199     1646   1393   1208    139      5    104       C  
ATOM   4667  C   GLY B 199      18.686  -5.231 -13.442  1.00 10.81           C  
ANISOU 4667  C   GLY B 199     1450   1278   1379     57    -74   -157       C  
ATOM   4668  O   GLY B 199      19.186  -4.109 -13.370  1.00 11.46           O  
ANISOU 4668  O   GLY B 199     1599   1378   1377     59    130    -95       O  
ATOM   4669  N   LEU B 200      19.205  -6.190 -14.247  1.00 10.23           N  
ANISOU 4669  N   LEU B 200     1402   1227   1258     95     80    -53       N  
ATOM   4670  CA  LEU B 200      20.434  -6.054 -15.014  1.00 10.79           C  
ANISOU 4670  CA  LEU B 200     1511   1278   1310     95     59    -26       C  
ATOM   4671  C   LEU B 200      20.217  -6.111 -16.518  1.00 11.74           C  
ANISOU 4671  C   LEU B 200     1581   1508   1369    160    142   -126       C  
ATOM   4672  O   LEU B 200      20.984  -6.714 -17.280  1.00 13.49           O  
ANISOU 4672  O   LEU B 200     1964   1677   1483    327    285   -154       O  
ATOM   4673  CB  LEU B 200      21.464  -7.108 -14.510  1.00 11.47           C  
ANISOU 4673  CB  LEU B 200     1582   1305   1472    206     63     16       C  
ATOM   4674  CG  LEU B 200      21.727  -7.077 -12.992  1.00 11.79           C  
ANISOU 4674  CG  LEU B 200     1446   1542   1493    204     26    -37       C  
ATOM   4675  CD1 LEU B 200      22.641  -8.247 -12.604  1.00 12.77           C  
ANISOU 4675  CD1 LEU B 200     1525   1641   1686    186    -78     75       C  
ATOM   4676  CD2 LEU B 200      22.337  -5.755 -12.538  1.00 13.34           C  
ANISOU 4676  CD2 LEU B 200     1744   1661   1663    172   -176    -55       C  
ATOM   4677  N   GLY B 201      19.142  -5.471 -16.991  1.00 10.98           N  
ANISOU 4677  N   GLY B 201     1342   1552   1279    112    149   -101       N  
ATOM   4678  CA  GLY B 201      18.904  -5.224 -18.410  1.00 11.22           C  
ANISOU 4678  CA  GLY B 201     1429   1492   1343    195    162    -47       C  
ATOM   4679  C   GLY B 201      19.625  -3.962 -18.874  1.00 10.77           C  
ANISOU 4679  C   GLY B 201     1115   1660   1316    130     38    -65       C  
ATOM   4680  O   GLY B 201      20.514  -3.448 -18.185  1.00 10.99           O  
ANISOU 4680  O   GLY B 201     1264   1589   1323    174     19   -104       O  
ATOM   4681  N   GLY B 202      19.244  -3.453 -20.045  1.00 10.81           N  
ANISOU 4681  N   GLY B 202     1206   1615   1288     45    -14    -95       N  
ATOM   4682  CA  GLY B 202      19.920  -2.290 -20.593  1.00 10.98           C  
ANISOU 4682  CA  GLY B 202     1435   1490   1246     95     65   -119       C  
ATOM   4683  C   GLY B 202      19.919  -1.095 -19.652  1.00 10.34           C  
ANISOU 4683  C   GLY B 202     1266   1407   1255    158     29    -73       C  
ATOM   4684  O   GLY B 202      20.915  -0.356 -19.524  1.00 11.03           O  
ANISOU 4684  O   GLY B 202     1402   1499   1289    104    178   -145       O  
ATOM   4685  N   VAL B 203      18.765  -0.858 -18.993  1.00 10.19           N  
ANISOU 4685  N   VAL B 203     1245   1467   1159    135     31   -126       N  
ATOM   4686  CA  VAL B 203      18.680   0.281 -18.086  1.00  9.92           C  
ANISOU 4686  CA  VAL B 203     1138   1427   1203     95    -24   -132       C  
ATOM   4687  C   VAL B 203      19.485   0.034 -16.814  1.00  9.97           C  
ANISOU 4687  C   VAL B 203     1313   1308   1166     32    116   -114       C  
ATOM   4688  O   VAL B 203      20.269   0.921 -16.387  1.00  9.68           O  
ANISOU 4688  O   VAL B 203     1171   1352   1156    102     82     10       O  
ATOM   4689  CB  VAL B 203      17.210   0.666 -17.804  1.00  9.75           C  
ANISOU 4689  CB  VAL B 203     1068   1527   1111     95     97    -11       C  
ATOM   4690  CG1 VAL B 203      17.120   1.934 -16.964  1.00 10.82           C  
ANISOU 4690  CG1 VAL B 203     1262   1500   1348    127    -29    -13       C  
ATOM   4691  CG2 VAL B 203      16.414   0.856 -19.104  1.00 10.75           C  
ANISOU 4691  CG2 VAL B 203     1300   1513   1273    151     -2     90       C  
ATOM   4692  N   GLY B 204      19.399  -1.147 -16.219  1.00  9.42           N  
ANISOU 4692  N   GLY B 204     1166   1174   1238    123     -4   -123       N  
ATOM   4693  CA  GLY B 204      20.154  -1.441 -14.988  1.00  9.78           C  
ANISOU 4693  CA  GLY B 204     1141   1328   1246     78      3    -30       C  
ATOM   4694  C   GLY B 204      21.656  -1.450 -15.197  1.00  9.67           C  
ANISOU 4694  C   GLY B 204     1209   1269   1196      1     26    -37       C  
ATOM   4695  O   GLY B 204      22.436  -0.989 -14.333  1.00  9.83           O  
ANISOU 4695  O   GLY B 204     1180   1387   1167    150    -12    -33       O  
ATOM   4696  N   LEU B 205      22.113  -1.935 -16.373  1.00  9.46           N  
ANISOU 4696  N   LEU B 205     1113   1330   1151    153    -61    -78       N  
ATOM   4697  CA  LEU B 205      23.543  -1.868 -16.669  1.00  9.95           C  
ANISOU 4697  CA  LEU B 205     1173   1458   1149    152    -44     27       C  
ATOM   4698  C   LEU B 205      24.026  -0.435 -16.772  1.00  9.50           C  
ANISOU 4698  C   LEU B 205     1090   1516   1003    128     60     41       C  
ATOM   4699  O   LEU B 205      25.159  -0.103 -16.379  1.00 10.57           O  
ANISOU 4699  O   LEU B 205     1247   1521   1248    101    -20    -40       O  
ATOM   4700  CB  LEU B 205      23.868  -2.611 -17.975  1.00 11.28           C  
ANISOU 4700  CB  LEU B 205     1567   1405   1313    193     -3    -93       C  
ATOM   4701  CG  LEU B 205      23.735  -4.130 -17.929  1.00 11.68           C  
ANISOU 4701  CG  LEU B 205     1415   1502   1521    188     16   -109       C  
ATOM   4702  CD1 LEU B 205      23.946  -4.701 -19.318  1.00 14.60           C  
ANISOU 4702  CD1 LEU B 205     2274   1664   1608    321    -16   -282       C  
ATOM   4703  CD2 LEU B 205      24.701  -4.795 -16.955  1.00 13.67           C  
ANISOU 4703  CD2 LEU B 205     1737   1761   1696    206   -141    -12       C  
ATOM   4704  N   SER B 206      23.165   0.465 -17.299  1.00  9.56           N  
ANISOU 4704  N   SER B 206     1047   1375   1210    142     65    -21       N  
ATOM   4705  CA  SER B 206      23.471   1.890 -17.386  1.00  9.66           C  
ANISOU 4705  CA  SER B 206     1188   1385   1098    140     58     -6       C  
ATOM   4706  C   SER B 206      23.549   2.537 -15.994  1.00  9.77           C  
ANISOU 4706  C   SER B 206     1180   1334   1197     49     36    -21       C  
ATOM   4707  O   SER B 206      24.371   3.421 -15.754  1.00  9.99           O  
ANISOU 4707  O   SER B 206     1260   1367   1169     97    -35     47       O  
ATOM   4708  CB  SER B 206      22.510   2.575 -18.349  1.00  9.87           C  
ANISOU 4708  CB  SER B 206     1162   1578   1009    201     99     60       C  
ATOM   4709  OG  SER B 206      22.624   2.025 -19.662  1.00 10.77           O  
ANISOU 4709  OG  SER B 206     1406   1563   1124    245     59     66       O  
ATOM   4710  N   VAL B 207      22.667   2.097 -15.064  1.00  9.42           N  
ANISOU 4710  N   VAL B 207     1198   1332   1048    194    -12     26       N  
ATOM   4711  CA  VAL B 207      22.769   2.518 -13.649  1.00  9.05           C  
ANISOU 4711  CA  VAL B 207     1095   1292   1051    148    102      6       C  
ATOM   4712  C   VAL B 207      24.137   2.087 -13.083  1.00  9.32           C  
ANISOU 4712  C   VAL B 207     1074   1334   1134    115     63      9       C  
ATOM   4713  O   VAL B 207      24.822   2.896 -12.435  1.00  9.94           O  
ANISOU 4713  O   VAL B 207     1234   1363   1179     88    -29     90       O  
ATOM   4714  CB  VAL B 207      21.627   1.927 -12.785  1.00  9.41           C  
ANISOU 4714  CB  VAL B 207     1109   1297   1170     66      7    119       C  
ATOM   4715  CG1 VAL B 207      21.832   2.218 -11.301  1.00 10.96           C  
ANISOU 4715  CG1 VAL B 207     1508   1541   1114    181     57    154       C  
ATOM   4716  CG2 VAL B 207      20.255   2.451 -13.210  1.00 10.40           C  
ANISOU 4716  CG2 VAL B 207     1185   1440   1325    162     90    107       C  
ATOM   4717  N   ILE B 208      24.574   0.857 -13.341  1.00 10.06           N  
ANISOU 4717  N   ILE B 208     1228   1455   1138    166     -4      5       N  
ATOM   4718  CA  ILE B 208      25.893   0.415 -12.880  1.00 10.00           C  
ANISOU 4718  CA  ILE B 208     1202   1367   1229    143    -97     91       C  
ATOM   4719  C   ILE B 208      26.994   1.304 -13.440  1.00  9.89           C  
ANISOU 4719  C   ILE B 208     1240   1294   1223     23    -11     24       C  
ATOM   4720  O   ILE B 208      27.905   1.742 -12.712  1.00 10.93           O  
ANISOU 4720  O   ILE B 208     1158   1645   1350    -51     -8     84       O  
ATOM   4721  CB  ILE B 208      26.153  -1.059 -13.200  1.00 10.20           C  
ANISOU 4721  CB  ILE B 208     1206   1391   1278     75     -1     74       C  
ATOM   4722  CG1 ILE B 208      25.200  -1.955 -12.372  1.00 11.08           C  
ANISOU 4722  CG1 ILE B 208     1255   1471   1485     86   -114    234       C  
ATOM   4723  CG2 ILE B 208      27.612  -1.462 -12.957  1.00 11.41           C  
ANISOU 4723  CG2 ILE B 208     1399   1523   1412    194     17    104       C  
ATOM   4724  CD1 ILE B 208      25.238  -3.420 -12.750  1.00 13.67           C  
ANISOU 4724  CD1 ILE B 208     1710   1495   1988    146   -154     58       C  
ATOM   4725  N   MET B 209      26.951   1.596 -14.759  1.00 10.05           N  
ANISOU 4725  N   MET B 209     1250   1353   1215     -9    142    -70       N  
ATOM   4726  CA  MET B 209      27.924   2.507 -15.361  1.00 10.52           C  
ANISOU 4726  CA  MET B 209     1185   1537   1274    120    106     81       C  
ATOM   4727  C   MET B 209      27.984   3.829 -14.605  1.00 10.72           C  
ANISOU 4727  C   MET B 209     1278   1655   1138    -20     -4     34       C  
ATOM   4728  O   MET B 209      29.081   4.346 -14.317  1.00 11.95           O  
ANISOU 4728  O   MET B 209     1303   1816   1423    -35    -23    -61       O  
ATOM   4729  CB  MET B 209      27.592   2.763 -16.829  1.00 11.82           C  
ANISOU 4729  CB  MET B 209     1379   1805   1308    131    150     56       C  
ATOM   4730  CG  MET B 209      27.762   1.580 -17.754  1.00 12.08           C  
ANISOU 4730  CG  MET B 209     1415   1820   1353    171     91     -6       C  
ATOM   4731  SD  MET B 209      27.221   2.034 -19.430  1.00 12.67           S  
ANISOU 4731  SD  MET B 209     1638   1938   1240    154    103    -30       S  
ATOM   4732  CE  MET B 209      27.663   0.550 -20.364  1.00 14.42           C  
ANISOU 4732  CE  MET B 209     1855   2134   1489    108    229   -150       C  
ATOM   4733  N   GLY B 210      26.828   4.399 -14.275  1.00 10.96           N  
ANISOU 4733  N   GLY B 210     1332   1603   1230     17    -15     45       N  
ATOM   4734  CA  GLY B 210      26.803   5.664 -13.548  1.00 11.77           C  
ANISOU 4734  CA  GLY B 210     1505   1651   1317     54     87     16       C  
ATOM   4735  C   GLY B 210      27.314   5.554 -12.112  1.00 10.65           C  
ANISOU 4735  C   GLY B 210     1365   1379   1301    -77     54    108       C  
ATOM   4736  O   GLY B 210      28.047   6.446 -11.665  1.00 11.99           O  
ANISOU 4736  O   GLY B 210     1536   1591   1427   -193    -79    236       O  
ATOM   4737  N   CYS B 211      26.979   4.462 -11.403  1.00 10.42           N  
ANISOU 4737  N   CYS B 211     1372   1431   1158    -84    -25    177       N  
ATOM   4738  CA  CYS B 211      27.519   4.280 -10.048  1.00 10.68           C  
ANISOU 4738  CA  CYS B 211     1267   1496   1296    -64   -171    126       C  
ATOM   4739  C   CYS B 211      29.048   4.193 -10.089  1.00 11.62           C  
ANISOU 4739  C   CYS B 211     1297   1693   1425   -205    -79    120       C  
ATOM   4740  O   CYS B 211      29.730   4.746  -9.204  1.00 13.03           O  
ANISOU 4740  O   CYS B 211     1484   2055   1410   -197   -185    165       O  
ATOM   4741  CB  CYS B 211      26.929   3.024  -9.401  1.00 10.57           C  
ANISOU 4741  CB  CYS B 211     1204   1555   1258    -33   -131     44       C  
ATOM   4742  SG  CYS B 211      25.162   3.077  -9.000  1.00  9.95           S  
ANISOU 4742  SG  CYS B 211     1230   1453   1097     39    -22    141       S  
ATOM   4743  N   LYS B 212      29.619   3.473 -11.047  1.00 12.27           N  
ANISOU 4743  N   LYS B 212     1304   1833   1526     21   -101    115       N  
ATOM   4744  CA  LYS B 212      31.076   3.318 -11.161  1.00 13.54           C  
ANISOU 4744  CA  LYS B 212     1314   2002   1831    -11    -34     80       C  
ATOM   4745  C   LYS B 212      31.662   4.683 -11.502  1.00 13.33           C  
ANISOU 4745  C   LYS B 212     1390   2025   1651   -145   -122     91       C  
ATOM   4746  O   LYS B 212      32.704   5.123 -10.931  1.00 14.25           O  
ANISOU 4746  O   LYS B 212     1421   2177   1816   -213   -148    169       O  
ATOM   4747  CB ALYS B 212      31.414   2.304 -12.257  0.51 17.27           C  
ANISOU 4747  CB ALYS B 212     2021   2466   2075    101      5   -109       C  
ATOM   4748  CG ALYS B 212      32.864   2.157 -12.705  0.51 21.44           C  
ANISOU 4748  CG ALYS B 212     2213   3214   2721     49    208    -84       C  
ATOM   4749  CD ALYS B 212      33.666   1.289 -11.760  0.51 24.77           C  
ANISOU 4749  CD ALYS B 212     2926   3509   2977    105    -22     79       C  
ATOM   4750  CE ALYS B 212      34.993   0.834 -12.367  0.51 26.33           C  
ANISOU 4750  CE ALYS B 212     2958   3838   3207    112     43     23       C  
ATOM   4751  NZ ALYS B 212      35.564  -0.321 -11.634  0.51 26.28           N  
ANISOU 4751  NZ ALYS B 212     2919   3933   3133    144    182     69       N  
ATOM   4752  CB BLYS B 212      31.485   2.289 -12.210  0.49 13.21           C  
ANISOU 4752  CB BLYS B 212     1141   2088   1790    156     55    167       C  
ATOM   4753  CG BLYS B 212      33.027   2.237 -12.282  0.49 14.05           C  
ANISOU 4753  CG BLYS B 212     1201   2085   2053    323     73     69       C  
ATOM   4754  CD BLYS B 212      33.444   1.103 -13.194  0.49 15.28           C  
ANISOU 4754  CD BLYS B 212     1669   2147   1991    319     15    -35       C  
ATOM   4755  CE BLYS B 212      34.977   1.062 -13.302  0.49 18.59           C  
ANISOU 4755  CE BLYS B 212     1769   2918   2377    232    163     64       C  
ATOM   4756  NZ BLYS B 212      35.387  -0.055 -14.185  0.49 21.33           N  
ANISOU 4756  NZ BLYS B 212     2387   3116   2603    341    133    -70       N  
ATOM   4757  N   ALA B 213      31.076   5.445 -12.432  1.00 12.65           N  
ANISOU 4757  N   ALA B 213     1472   1853   1481   -191     -7    187       N  
ATOM   4758  CA  ALA B 213      31.580   6.782 -12.797  1.00 13.72           C  
ANISOU 4758  CA  ALA B 213     1648   1906   1661   -312      7    140       C  
ATOM   4759  C   ALA B 213      31.598   7.738 -11.621  1.00 14.63           C  
ANISOU 4759  C   ALA B 213     1857   2150   1553   -394     15    124       C  
ATOM   4760  O   ALA B 213      32.435   8.639 -11.531  1.00 16.70           O  
ANISOU 4760  O   ALA B 213     2117   2406   1822   -554    -19    175       O  
ATOM   4761  CB  ALA B 213      30.781   7.345 -13.963  1.00 14.50           C  
ANISOU 4761  CB  ALA B 213     1644   2146   1719   -491   -104    184       C  
ATOM   4762  N   ALA B 214      30.652   7.617 -10.705  1.00 13.76           N  
ANISOU 4762  N   ALA B 214     1850   1889   1490   -364      5     49       N  
ATOM   4763  CA  ALA B 214      30.502   8.420  -9.509  1.00 15.04           C  
ANISOU 4763  CA  ALA B 214     1926   2055   1732   -316     18   -142       C  
ATOM   4764  C   ALA B 214      31.460   7.990  -8.397  1.00 15.42           C  
ANISOU 4764  C   ALA B 214     1902   2195   1761   -459     10    -82       C  
ATOM   4765  O   ALA B 214      31.548   8.657  -7.340  1.00 17.97           O  
ANISOU 4765  O   ALA B 214     2319   2740   1767   -403   -212   -140       O  
ATOM   4766  CB  ALA B 214      29.053   8.375  -9.018  1.00 15.22           C  
ANISOU 4766  CB  ALA B 214     1853   2288   1642   -365    -62   -214       C  
ATOM   4767  N   GLY B 215      32.200   6.898  -8.574  1.00 14.79           N  
ANISOU 4767  N   GLY B 215     1943   2167   1508   -383   -127     78       N  
ATOM   4768  CA  GLY B 215      33.182   6.490  -7.585  1.00 16.41           C  
ANISOU 4768  CA  GLY B 215     1918   2451   1866   -403   -227    313       C  
ATOM   4769  C   GLY B 215      32.697   5.539  -6.502  1.00 14.18           C  
ANISOU 4769  C   GLY B 215     1617   2181   1588   -221   -116    103       C  
ATOM   4770  O   GLY B 215      33.423   5.395  -5.498  1.00 15.51           O  
ANISOU 4770  O   GLY B 215     1824   2397   1673   -243   -231     88       O  
ATOM   4771  N   ALA B 216      31.564   4.861  -6.711  1.00 13.50           N  
ANISOU 4771  N   ALA B 216     1548   1977   1605   -135   -162     14       N  
ATOM   4772  CA  ALA B 216      31.136   3.893  -5.705  1.00 12.85           C  
ANISOU 4772  CA  ALA B 216     1463   1856   1566    -23    -89    -53       C  
ATOM   4773  C   ALA B 216      32.243   2.844  -5.482  1.00 13.11           C  
ANISOU 4773  C   ALA B 216     1413   1898   1669    -49    -57   -139       C  
ATOM   4774  O   ALA B 216      32.890   2.391  -6.441  1.00 15.98           O  
ANISOU 4774  O   ALA B 216     1647   2528   1898    156    131   -138       O  
ATOM   4775  CB  ALA B 216      29.849   3.214  -6.165  1.00 13.02           C  
ANISOU 4775  CB  ALA B 216     1314   2105   1526    151   -149    -44       C  
ATOM   4776  N   ALA B 217      32.369   2.389  -4.229  1.00 13.16           N  
ANISOU 4776  N   ALA B 217     1315   1956   1730    202   -138    -32       N  
ATOM   4777  CA  ALA B 217      33.341   1.347  -3.903  1.00 14.22           C  
ANISOU 4777  CA  ALA B 217     1328   2012   2064    165   -212     33       C  
ATOM   4778  C   ALA B 217      32.817  -0.062  -4.151  1.00 13.30           C  
ANISOU 4778  C   ALA B 217     1289   1924   1840    237   -169    -47       C  
ATOM   4779  O   ALA B 217      33.567  -1.015  -4.453  1.00 15.79           O  
ANISOU 4779  O   ALA B 217     1528   2169   2302    411   -122   -208       O  
ATOM   4780  CB  ALA B 217      33.817   1.454  -2.456  1.00 16.68           C  
ANISOU 4780  CB  ALA B 217     1779   2322   2238    247   -448    -75       C  
ATOM   4781  N   ARG B 218      31.508  -0.262  -3.952  1.00 12.46           N  
ANISOU 4781  N   ARG B 218     1339   1775   1621    208    -63   -164       N  
ATOM   4782  CA  ARG B 218      30.836  -1.556  -4.064  1.00 11.49           C  
ANISOU 4782  CA  ARG B 218     1345   1646   1374    260   -164    -59       C  
ATOM   4783  C   ARG B 218      29.545  -1.337  -4.857  1.00 10.73           C  
ANISOU 4783  C   ARG B 218     1210   1508   1357    248     12   -115       C  
ATOM   4784  O   ARG B 218      28.779  -0.398  -4.566  1.00 11.25           O  
ANISOU 4784  O   ARG B 218     1315   1552   1406    269    -17     10       O  
ATOM   4785  CB  ARG B 218      30.533  -2.210  -2.722  1.00 13.20           C  
ANISOU 4785  CB  ARG B 218     1409   2184   1424    347    -43    -13       C  
ATOM   4786  CG  ARG B 218      31.736  -2.651  -1.896  1.00 15.61           C  
ANISOU 4786  CG  ARG B 218     1745   2436   1751    340   -158    445       C  
ATOM   4787  CD  ARG B 218      31.330  -3.291  -0.583  1.00 16.91           C  
ANISOU 4787  CD  ARG B 218     2214   2472   1741    337    -74    513       C  
ATOM   4788  NE  ARG B 218      30.582  -4.549  -0.709  1.00 16.64           N  
ANISOU 4788  NE  ARG B 218     2071   2351   1900    530     39    348       N  
ATOM   4789  CZ  ARG B 218      30.030  -5.193   0.338  1.00 16.67           C  
ANISOU 4789  CZ  ARG B 218     2073   2528   1733    582    -47    325       C  
ATOM   4790  NH1 ARG B 218      30.072  -4.683   1.556  1.00 17.48           N  
ANISOU 4790  NH1 ARG B 218     2269   2604   1769    783     88    227       N  
ATOM   4791  NH2 ARG B 218      29.401  -6.330   0.105  1.00 18.53           N  
ANISOU 4791  NH2 ARG B 218     2164   3109   1769    210   -167    129       N  
ATOM   4792  N   ILE B 219      29.286  -2.223  -5.813  1.00 10.71           N  
ANISOU 4792  N   ILE B 219     1247   1501   1321    317   -102    -31       N  
ATOM   4793  CA  ILE B 219      28.075  -2.159  -6.653  1.00  9.92           C  
ANISOU 4793  CA  ILE B 219     1025   1429   1313    287     35     99       C  
ATOM   4794  C   ILE B 219      27.539  -3.593  -6.735  1.00 10.34           C  
ANISOU 4794  C   ILE B 219     1255   1358   1315    326    -43     77       C  
ATOM   4795  O   ILE B 219      28.159  -4.440  -7.416  1.00 12.24           O  
ANISOU 4795  O   ILE B 219     1413   1612   1626    311     97   -181       O  
ATOM   4796  CB  ILE B 219      28.336  -1.569  -8.052  1.00 10.87           C  
ANISOU 4796  CB  ILE B 219     1460   1460   1209    276     62     13       C  
ATOM   4797  CG1 ILE B 219      28.926  -0.143  -7.993  1.00 11.28           C  
ANISOU 4797  CG1 ILE B 219     1510   1518   1258    253     35     91       C  
ATOM   4798  CG2 ILE B 219      27.028  -1.534  -8.856  1.00 12.47           C  
ANISOU 4798  CG2 ILE B 219     1627   1732   1380    213    -37    -17       C  
ATOM   4799  CD1 ILE B 219      29.551   0.320  -9.294  1.00 13.22           C  
ANISOU 4799  CD1 ILE B 219     1891   1694   1439    259    208    225       C  
ATOM   4800  N   ILE B 220      26.427  -3.893  -6.057  1.00  9.92           N  
ANISOU 4800  N   ILE B 220     1224   1236   1309    170   -108     23       N  
ATOM   4801  CA  ILE B 220      25.864  -5.228  -5.966  1.00 10.29           C  
ANISOU 4801  CA  ILE B 220     1287   1236   1385    188      9     21       C  
ATOM   4802  C   ILE B 220      24.719  -5.379  -6.961  1.00 10.64           C  
ANISOU 4802  C   ILE B 220     1331   1215   1495    272    -45    -53       C  
ATOM   4803  O   ILE B 220      23.687  -4.665  -6.846  1.00 11.39           O  
ANISOU 4803  O   ILE B 220     1372   1402   1553    354    -79    -79       O  
ATOM   4804  CB  ILE B 220      25.352  -5.523  -4.524  1.00 10.93           C  
ANISOU 4804  CB  ILE B 220     1455   1387   1313    362    -11     69       C  
ATOM   4805  CG1 ILE B 220      26.443  -5.288  -3.473  1.00 12.49           C  
ANISOU 4805  CG1 ILE B 220     1704   1551   1492    132    -94     86       C  
ATOM   4806  CG2 ILE B 220      24.834  -6.962  -4.441  1.00 12.28           C  
ANISOU 4806  CG2 ILE B 220     1664   1459   1542    365     32     19       C  
ATOM   4807  CD1 ILE B 220      25.928  -5.218  -2.039  1.00 13.75           C  
ANISOU 4807  CD1 ILE B 220     2071   1630   1524    152      3     53       C  
ATOM   4808  N   GLY B 221      24.903  -6.190  -8.010  1.00 10.69           N  
ANISOU 4808  N   GLY B 221     1314   1431   1318    333    -46    -47       N  
ATOM   4809  CA  GLY B 221      23.820  -6.440  -8.944  1.00 10.77           C  
ANISOU 4809  CA  GLY B 221     1291   1400   1401    197    -71      3       C  
ATOM   4810  C   GLY B 221      22.884  -7.534  -8.459  1.00 11.05           C  
ANISOU 4810  C   GLY B 221     1443   1177   1578    296    -60     57       C  
ATOM   4811  O   GLY B 221      23.343  -8.526  -7.835  1.00 13.89           O  
ANISOU 4811  O   GLY B 221     1737   1365   2178    325   -232    224       O  
ATOM   4812  N   VAL B 222      21.580  -7.358  -8.658  1.00 10.30           N  
ANISOU 4812  N   VAL B 222     1367   1220   1325    223     58     40       N  
ATOM   4813  CA  VAL B 222      20.555  -8.294  -8.193  1.00 10.99           C  
ANISOU 4813  CA  VAL B 222     1412   1327   1436    169    -22     17       C  
ATOM   4814  C   VAL B 222      19.706  -8.705  -9.381  1.00 11.05           C  
ANISOU 4814  C   VAL B 222     1513   1306   1381    180   -152     98       C  
ATOM   4815  O   VAL B 222      19.068  -7.826 -10.008  1.00 11.98           O  
ANISOU 4815  O   VAL B 222     1687   1282   1584    240   -225     68       O  
ATOM   4816  CB  VAL B 222      19.681  -7.703  -7.054  1.00 10.80           C  
ANISOU 4816  CB  VAL B 222     1407   1319   1379    114     64     14       C  
ATOM   4817  CG1 VAL B 222      18.691  -8.729  -6.528  1.00 12.72           C  
ANISOU 4817  CG1 VAL B 222     1704   1305   1824     53     69    116       C  
ATOM   4818  CG2 VAL B 222      20.520  -7.112  -5.910  1.00 11.77           C  
ANISOU 4818  CG2 VAL B 222     1631   1409   1433    175    -75      0       C  
ATOM   4819  N   ASP B 223      19.627  -9.979  -9.717  1.00 11.68           N  
ANISOU 4819  N   ASP B 223     1710   1314   1414    239   -105      0       N  
ATOM   4820  CA  ASP B 223      18.756 -10.423 -10.819  1.00 12.34           C  
ANISOU 4820  CA  ASP B 223     1867   1358   1465     53   -121     71       C  
ATOM   4821  C   ASP B 223      18.454 -11.900 -10.565  1.00 11.82           C  
ANISOU 4821  C   ASP B 223     1822   1301   1370    122   -116   -100       C  
ATOM   4822  O   ASP B 223      19.290 -12.667 -10.061  1.00 13.22           O  
ANISOU 4822  O   ASP B 223     1989   1327   1708     82   -214     29       O  
ATOM   4823  CB  ASP B 223      19.442 -10.192 -12.197  1.00 12.18           C  
ANISOU 4823  CB  ASP B 223     1581   1507   1537    118   -153     32       C  
ATOM   4824  CG  ASP B 223      18.497 -10.053 -13.378  1.00 11.61           C  
ANISOU 4824  CG  ASP B 223     1477   1398   1537     31   -139     25       C  
ATOM   4825  OD1 ASP B 223      17.706 -11.016 -13.608  1.00 12.28           O  
ANISOU 4825  OD1 ASP B 223     1758   1289   1618     -5   -173     36       O  
ATOM   4826  OD2 ASP B 223      18.532  -8.988 -14.053  1.00 12.05           O  
ANISOU 4826  OD2 ASP B 223     1731   1361   1489     56   -141     31       O  
ATOM   4827  N   ILE B 224      17.257 -12.338 -10.959  1.00 12.78           N  
ANISOU 4827  N   ILE B 224     1871   1234   1749    -71    -89     41       N  
ATOM   4828  CA  ILE B 224      16.867 -13.760 -10.945  1.00 14.22           C  
ANISOU 4828  CA  ILE B 224     2035   1436   1930   -148    -60    -37       C  
ATOM   4829  C   ILE B 224      17.398 -14.501 -12.158  1.00 15.11           C  
ANISOU 4829  C   ILE B 224     2124   1514   2105     59     -2    -64       C  
ATOM   4830  O   ILE B 224      17.289 -15.773 -12.140  1.00 17.03           O  
ANISOU 4830  O   ILE B 224     2408   1503   2559    -75     74   -122       O  
ATOM   4831  CB  ILE B 224      15.332 -13.941 -10.857  1.00 16.06           C  
ANISOU 4831  CB  ILE B 224     2038   1735   2327    -90   -118     56       C  
ATOM   4832  CG1 ILE B 224      14.580 -13.273 -12.003  1.00 17.16           C  
ANISOU 4832  CG1 ILE B 224     2203   1870   2448     -3   -244     22       C  
ATOM   4833  CG2 ILE B 224      14.826 -13.494  -9.493  1.00 17.10           C  
ANISOU 4833  CG2 ILE B 224     2067   1991   2439   -129   -148   -100       C  
ATOM   4834  CD1 ILE B 224      13.100 -13.600 -12.139  1.00 19.88           C  
ANISOU 4834  CD1 ILE B 224     2201   2157   3197    132   -279    -99       C  
ATOM   4835  N   ASN B 225      17.971 -13.855 -13.154  1.00 14.49           N  
ANISOU 4835  N   ASN B 225     2068   1629   1809    104   -142   -151       N  
ATOM   4836  CA  ASN B 225      18.593 -14.512 -14.306  1.00 14.86           C  
ANISOU 4836  CA  ASN B 225     2235   1556   1853     18    -85   -248       C  
ATOM   4837  C   ASN B 225      20.111 -14.359 -14.170  1.00 14.59           C  
ANISOU 4837  C   ASN B 225     2166   1526   1850    117     95    -36       C  
ATOM   4838  O   ASN B 225      20.713 -13.316 -14.502  1.00 14.04           O  
ANISOU 4838  O   ASN B 225     1978   1634   1722    145    -19    -14       O  
ATOM   4839  CB  ASN B 225      18.096 -13.850 -15.599  1.00 15.69           C  
ANISOU 4839  CB  ASN B 225     2421   1701   1840     97   -150   -258       C  
ATOM   4840  CG  ASN B 225      18.644 -14.544 -16.836  1.00 16.70           C  
ANISOU 4840  CG  ASN B 225     2523   1887   1934    305   -266   -327       C  
ATOM   4841  OD1 ASN B 225      19.500 -15.444 -16.696  1.00 18.27           O  
ANISOU 4841  OD1 ASN B 225     2689   2030   2222    496   -340   -416       O  
ATOM   4842  ND2 ASN B 225      18.225 -14.140 -18.022  1.00 18.61           N  
ANISOU 4842  ND2 ASN B 225     2690   2445   1937    548   -285   -446       N  
ATOM   4843  N   LYS B 226      20.788 -15.446 -13.718  1.00 15.68           N  
ANISOU 4843  N   LYS B 226     2305   1661   1992    277     21   -119       N  
ATOM   4844  CA  LYS B 226      22.233 -15.395 -13.512  1.00 16.26           C  
ANISOU 4844  CA  LYS B 226     2373   1641   2166    361     -5     50       C  
ATOM   4845  C   LYS B 226      23.041 -15.225 -14.796  1.00 15.01           C  
ANISOU 4845  C   LYS B 226     2210   1409   2085    191    -52    -85       C  
ATOM   4846  O   LYS B 226      24.227 -14.852 -14.731  1.00 15.97           O  
ANISOU 4846  O   LYS B 226     2271   1681   2116    323    -53    -18       O  
ATOM   4847  CB  LYS B 226      22.704 -16.641 -12.749  1.00 19.83           C  
ANISOU 4847  CB  LYS B 226     2912   1965   2659    447    -39    281       C  
ATOM   4848  CG ALYS B 226      22.863 -17.853 -13.677  0.59 24.47           C  
ANISOU 4848  CG ALYS B 226     3744   2286   3269    280    -30    -55       C  
ATOM   4849  CD ALYS B 226      24.350 -18.093 -13.903  0.59 30.62           C  
ANISOU 4849  CD ALYS B 226     3823   3617   4195    139    107    -62       C  
ATOM   4850  CE ALYS B 226      24.680 -18.654 -15.274  0.59 33.50           C  
ANISOU 4850  CE ALYS B 226     4543   3934   4251     55    109   -176       C  
ATOM   4851  NZ ALYS B 226      26.163 -18.677 -15.476  0.59 34.12           N  
ANISOU 4851  NZ ALYS B 226     4572   4015   4375     71    184   -299       N  
ATOM   4852  CG BLYS B 226      22.517 -17.938 -13.516  0.41 20.46           C  
ANISOU 4852  CG BLYS B 226     2830   2127   2817    295    117    116       C  
ATOM   4853  CD BLYS B 226      23.097 -19.108 -12.719  0.41 21.37           C  
ANISOU 4853  CD BLYS B 226     3006   2188   2925    388    183    183       C  
ATOM   4854  CE BLYS B 226      22.707 -20.417 -13.397  0.41 23.23           C  
ANISOU 4854  CE BLYS B 226     3218   2510   3098    215     10     63       C  
ATOM   4855  NZ BLYS B 226      23.291 -20.499 -14.761  0.41 25.10           N  
ANISOU 4855  NZ BLYS B 226     3385   2927   3224    217    148    191       N  
ATOM   4856  N   ASP B 227      22.429 -15.443 -15.981  1.00 15.44           N  
ANISOU 4856  N   ASP B 227     2314   1526   2027    282     16   -118       N  
ATOM   4857  CA  ASP B 227      23.112 -15.187 -17.225  1.00 16.01           C  
ANISOU 4857  CA  ASP B 227     2287   1733   2064    258     83   -266       C  
ATOM   4858  C   ASP B 227      23.447 -13.708 -17.442  1.00 15.45           C  
ANISOU 4858  C   ASP B 227     2325   1754   1791    207     35   -152       C  
ATOM   4859  O   ASP B 227      24.279 -13.369 -18.279  1.00 16.66           O  
ANISOU 4859  O   ASP B 227     2452   1760   2119    288    202   -131       O  
ATOM   4860  CB  ASP B 227      22.320 -15.705 -18.412  1.00 18.98           C  
ANISOU 4860  CB  ASP B 227     2868   2224   2120    184    -61   -423       C  
ATOM   4861  CG  ASP B 227      22.137 -17.199 -18.498  1.00 23.96           C  
ANISOU 4861  CG  ASP B 227     3561   2421   3121     40    -20   -371       C  
ATOM   4862  OD1 ASP B 227      22.886 -17.931 -17.831  1.00 26.65           O  
ANISOU 4862  OD1 ASP B 227     4239   2396   3492    167   -215   -312       O  
ATOM   4863  OD2 ASP B 227      21.226 -17.600 -19.253  1.00 26.69           O  
ANISOU 4863  OD2 ASP B 227     3973   2878   3292   -123   -126   -486       O  
ATOM   4864  N   LYS B 228      22.820 -12.810 -16.657  1.00 14.50           N  
ANISOU 4864  N   LYS B 228     2222   1525   1764    256   -163   -116       N  
ATOM   4865  CA  LYS B 228      23.044 -11.382 -16.733  1.00 14.16           C  
ANISOU 4865  CA  LYS B 228     1945   1463   1974    159    -82    -53       C  
ATOM   4866  C   LYS B 228      24.276 -10.925 -15.936  1.00 13.23           C  
ANISOU 4866  C   LYS B 228     1942   1398   1687    385   -128    -13       C  
ATOM   4867  O   LYS B 228      24.755  -9.780 -16.086  1.00 13.74           O  
ANISOU 4867  O   LYS B 228     1864   1577   1780    284   -222    -71       O  
ATOM   4868  CB ALYS B 228      21.796 -10.618 -16.232  0.68 15.41           C  
ANISOU 4868  CB ALYS B 228     2013   1890   1952    374   -127    -95       C  
ATOM   4869  CG ALYS B 228      20.519 -10.808 -17.048  0.68 16.70           C  
ANISOU 4869  CG ALYS B 228     2283   2106   1957    262   -286    -62       C  
ATOM   4870  CD ALYS B 228      20.549 -10.183 -18.435  0.68 17.17           C  
ANISOU 4870  CD ALYS B 228     2481   1986   2056    120   -236     44       C  
ATOM   4871  CE ALYS B 228      19.374 -10.514 -19.338  0.68 15.47           C  
ANISOU 4871  CE ALYS B 228     2146   1841   1889    447     28   -233       C  
ATOM   4872  NZ ALYS B 228      18.110  -9.764 -19.051  0.68 16.54           N  
ANISOU 4872  NZ ALYS B 228     2022   2213   2051    415    159    -43       N  
ATOM   4873  CB BLYS B 228      21.802 -10.663 -16.163  0.32 13.75           C  
ANISOU 4873  CB BLYS B 228     1846   1617   1761    219   -190    -28       C  
ATOM   4874  CG BLYS B 228      20.485 -11.011 -16.845  0.32 13.61           C  
ANISOU 4874  CG BLYS B 228     1902   1637   1632    118   -187     74       C  
ATOM   4875  CD BLYS B 228      20.471 -10.567 -18.304  0.32 14.55           C  
ANISOU 4875  CD BLYS B 228     2015   1856   1658    125   -206    120       C  
ATOM   4876  CE BLYS B 228      19.177 -10.971 -18.994  0.32 14.26           C  
ANISOU 4876  CE BLYS B 228     1966   1723   1729     70   -150    160       C  
ATOM   4877  NZ BLYS B 228      19.040 -10.281 -20.303  0.32 14.08           N  
ANISOU 4877  NZ BLYS B 228     2023   1695   1632    295   -146     51       N  
ATOM   4878  N   PHE B 229      24.851 -11.810 -15.114  1.00 13.29           N  
ANISOU 4878  N   PHE B 229     1868   1555   1626    366   -102    -23       N  
ATOM   4879  CA  PHE B 229      25.890 -11.403 -14.161  1.00 13.07           C  
ANISOU 4879  CA  PHE B 229     1635   1624   1707    322    -56     52       C  
ATOM   4880  C   PHE B 229      27.232 -11.047 -14.781  1.00 12.60           C  
ANISOU 4880  C   PHE B 229     1661   1673   1455    317    -50     39       C  
ATOM   4881  O   PHE B 229      27.936 -10.097 -14.363  1.00 13.85           O  
ANISOU 4881  O   PHE B 229     1811   1663   1787    346    -89     -5       O  
ATOM   4882  CB  PHE B 229      26.046 -12.458 -13.060  1.00 13.77           C  
ANISOU 4882  CB  PHE B 229     1988   1559   1685    303    -86      5       C  
ATOM   4883  CG  PHE B 229      24.864 -12.652 -12.134  1.00 13.54           C  
ANISOU 4883  CG  PHE B 229     1942   1522   1680    336   -101     48       C  
ATOM   4884  CD1 PHE B 229      23.775 -11.774 -12.078  1.00 13.57           C  
ANISOU 4884  CD1 PHE B 229     1849   1660   1648    375   -126    228       C  
ATOM   4885  CD2 PHE B 229      24.885 -13.719 -11.224  1.00 14.68           C  
ANISOU 4885  CD2 PHE B 229     2048   1683   1847    304     13    175       C  
ATOM   4886  CE1 PHE B 229      22.748 -11.966 -11.183  1.00 14.04           C  
ANISOU 4886  CE1 PHE B 229     1940   1780   1616    387   -104    127       C  
ATOM   4887  CE2 PHE B 229      23.847 -13.914 -10.330  1.00 15.27           C  
ANISOU 4887  CE2 PHE B 229     2040   1680   2084    173    -33    194       C  
ATOM   4888  CZ  PHE B 229      22.767 -13.033 -10.308  1.00 14.34           C  
ANISOU 4888  CZ  PHE B 229     1977   1682   1789    149   -138    115       C  
ATOM   4889  N   ALA B 230      27.662 -11.807 -15.813  1.00 13.80           N  
ANISOU 4889  N   ALA B 230     1757   1810   1675    397     30    -87       N  
ATOM   4890  CA  ALA B 230      28.978 -11.548 -16.399  1.00 14.83           C  
ANISOU 4890  CA  ALA B 230     1961   1959   1714    413    172     -7       C  
ATOM   4891  C   ALA B 230      29.102 -10.146 -16.958  1.00 13.69           C  
ANISOU 4891  C   ALA B 230     1834   1885   1481    390    111    -67       C  
ATOM   4892  O   ALA B 230      30.092  -9.428 -16.728  1.00 14.92           O  
ANISOU 4892  O   ALA B 230     1775   2051   1843    509    125   -220       O  
ATOM   4893  CB  ALA B 230      29.374 -12.600 -17.452  1.00 16.99           C  
ANISOU 4893  CB  ALA B 230     2292   2053   2109    566    318   -152       C  
ATOM   4894  N   LYS B 231      28.072  -9.709 -17.731  1.00 13.97           N  
ANISOU 4894  N   LYS B 231     1931   1804   1573    563    100   -133       N  
ATOM   4895  CA  LYS B 231      28.104  -8.381 -18.323  1.00 13.69           C  
ANISOU 4895  CA  LYS B 231     1824   1812   1566    424    -46   -139       C  
ATOM   4896  C   LYS B 231      28.013  -7.317 -17.227  1.00 12.30           C  
ANISOU 4896  C   LYS B 231     1613   1685   1373    397    -61    -43       C  
ATOM   4897  O   LYS B 231      28.649  -6.257 -17.304  1.00 14.02           O  
ANISOU 4897  O   LYS B 231     1819   1920   1589    249    136   -177       O  
ATOM   4898  CB  LYS B 231      26.990  -8.199 -19.352  1.00 14.39           C  
ANISOU 4898  CB  LYS B 231     2006   2025   1435    393    -60   -166       C  
ATOM   4899  CG  LYS B 231      26.943  -6.845 -20.005  1.00 16.22           C  
ANISOU 4899  CG  LYS B 231     2397   2064   1702    434   -130    -54       C  
ATOM   4900  CD  LYS B 231      28.128  -6.378 -20.797  1.00 19.51           C  
ANISOU 4900  CD  LYS B 231     2606   2696   2110    167     18     87       C  
ATOM   4901  CE  LYS B 231      28.479  -7.212 -22.018  1.00 20.92           C  
ANISOU 4901  CE  LYS B 231     2647   3096   2205    457    197    114       C  
ATOM   4902  NZ  LYS B 231      27.391  -7.205 -23.029  1.00 20.98           N  
ANISOU 4902  NZ  LYS B 231     3002   2851   2118    476     70     37       N  
ATOM   4903  N   ALA B 232      27.229  -7.554 -16.173  1.00 12.79           N  
ANISOU 4903  N   ALA B 232     1620   1706   1534    368     43    -11       N  
ATOM   4904  CA  ALA B 232      27.147  -6.609 -15.047  1.00 12.33           C  
ANISOU 4904  CA  ALA B 232     1421   1742   1522    361     54    -38       C  
ATOM   4905  C   ALA B 232      28.522  -6.358 -14.434  1.00 12.47           C  
ANISOU 4905  C   ALA B 232     1538   1683   1516    306      1     -4       C  
ATOM   4906  O   ALA B 232      28.917  -5.213 -14.144  1.00 12.82           O  
ANISOU 4906  O   ALA B 232     1575   1759   1538    276    -28     51       O  
ATOM   4907  CB  ALA B 232      26.133  -7.085 -14.036  1.00 12.57           C  
ANISOU 4907  CB  ALA B 232     1542   1595   1640    283    129    -82       C  
ATOM   4908  N   LYS B 233      29.301  -7.433 -14.224  1.00 13.17           N  
ANISOU 4908  N   LYS B 233     1487   1777   1740    402     72   -134       N  
ATOM   4909  CA  LYS B 233      30.670  -7.292 -13.706  1.00 13.60           C  
ANISOU 4909  CA  LYS B 233     1403   1890   1876    419     48    -78       C  
ATOM   4910  C   LYS B 233      31.573  -6.551 -14.678  1.00 14.16           C  
ANISOU 4910  C   LYS B 233     1554   1954   1873    308    -48    -13       C  
ATOM   4911  O   LYS B 233      32.385  -5.676 -14.292  1.00 14.86           O  
ANISOU 4911  O   LYS B 233     1692   2060   1896    281     34    -75       O  
ATOM   4912  CB  LYS B 233      31.239  -8.675 -13.311  1.00 16.17           C  
ANISOU 4912  CB  LYS B 233     1866   2046   2230    558     47     35       C  
ATOM   4913  CG  LYS B 233      30.563  -9.225 -12.048  1.00 17.65           C  
ANISOU 4913  CG  LYS B 233     2135   2249   2324    526     49    232       C  
ATOM   4914  CD  LYS B 233      31.115 -10.581 -11.579  1.00 20.76           C  
ANISOU 4914  CD  LYS B 233     2556   2501   2828    776     44    293       C  
ATOM   4915  CE  LYS B 233      30.643 -10.807 -10.132  1.00 25.15           C  
ANISOU 4915  CE  LYS B 233     3039   3524   2991    536    179    467       C  
ATOM   4916  NZ  LYS B 233      31.033 -12.131  -9.602  1.00 27.23           N  
ANISOU 4916  NZ  LYS B 233     3486   3778   3083    666    -53    474       N  
ATOM   4917  N   GLU B 234      31.455  -6.807 -15.997  1.00 14.51           N  
ANISOU 4917  N   GLU B 234     1506   2195   1812    356     66    -40       N  
ATOM   4918  CA  GLU B 234      32.276  -6.105 -16.988  1.00 15.30           C  
ANISOU 4918  CA  GLU B 234     1763   2182   1870    208    140    -26       C  
ATOM   4919  C   GLU B 234      32.108  -4.597 -16.909  1.00 15.05           C  
ANISOU 4919  C   GLU B 234     1728   2170   1822    190    104     16       C  
ATOM   4920  O   GLU B 234      33.083  -3.865 -17.125  1.00 18.10           O  
ANISOU 4920  O   GLU B 234     1848   2467   2564    127    332     94       O  
ATOM   4921  CB AGLU B 234      31.980  -6.549 -18.431  0.62 16.94           C  
ANISOU 4921  CB AGLU B 234     2135   2498   1802    271    219    -43       C  
ATOM   4922  CG AGLU B 234      32.540  -7.925 -18.730  0.62 18.66           C  
ANISOU 4922  CG AGLU B 234     2381   2592   2118    412    152    -93       C  
ATOM   4923  CD AGLU B 234      32.138  -8.481 -20.078  0.62 22.03           C  
ANISOU 4923  CD AGLU B 234     3044   3096   2230    346    223   -327       C  
ATOM   4924  OE1AGLU B 234      31.543  -7.778 -20.910  0.62 22.53           O  
ANISOU 4924  OE1AGLU B 234     3222   3172   2167    280    268   -294       O  
ATOM   4925  OE2AGLU B 234      32.400  -9.694 -20.311  0.62 24.82           O  
ANISOU 4925  OE2AGLU B 234     3701   2958   2769     58     66   -375       O  
ATOM   4926  CB BGLU B 234      31.921  -6.571 -18.415  0.38 17.14           C  
ANISOU 4926  CB BGLU B 234     2176   2430   1908    289    141   -118       C  
ATOM   4927  CG BGLU B 234      32.483  -5.743 -19.550  0.38 19.36           C  
ANISOU 4927  CG BGLU B 234     2542   2633   2180    280    301     32       C  
ATOM   4928  CD BGLU B 234      31.926  -6.045 -20.928  0.38 20.76           C  
ANISOU 4928  CD BGLU B 234     2737   2827   2322    225    128     41       C  
ATOM   4929  OE1BGLU B 234      31.958  -7.254 -21.232  0.38 21.72           O  
ANISOU 4929  OE1BGLU B 234     3019   2852   2381    199    323     70       O  
ATOM   4930  OE2BGLU B 234      31.493  -5.156 -21.709  0.38 19.18           O  
ANISOU 4930  OE2BGLU B 234     2399   2703   2184    345    260    -74       O  
ATOM   4931  N   VAL B 235      30.886  -4.097 -16.628  1.00 14.26           N  
ANISOU 4931  N   VAL B 235     1738   2126   1555    276     90    122       N  
ATOM   4932  CA  VAL B 235      30.617  -2.661 -16.590  1.00 14.85           C  
ANISOU 4932  CA  VAL B 235     1873   2068   1701    226     72     42       C  
ATOM   4933  C   VAL B 235      30.710  -2.062 -15.181  1.00 13.38           C  
ANISOU 4933  C   VAL B 235     1586   1903   1596    224    142    169       C  
ATOM   4934  O   VAL B 235      30.528  -0.838 -15.022  1.00 14.17           O  
ANISOU 4934  O   VAL B 235     1866   1902   1615    107    156    154       O  
ATOM   4935  CB  VAL B 235      29.296  -2.268 -17.278  1.00 14.69           C  
ANISOU 4935  CB  VAL B 235     1889   2053   1641    228     12     38       C  
ATOM   4936  CG1 VAL B 235      29.340  -2.717 -18.749  1.00 16.91           C  
ANISOU 4936  CG1 VAL B 235     2191   2557   1677    213     53     41       C  
ATOM   4937  CG2 VAL B 235      28.086  -2.798 -16.551  1.00 14.19           C  
ANISOU 4937  CG2 VAL B 235     1617   2060   1715    353    -84    -26       C  
ATOM   4938  N   GLY B 236      31.065  -2.863 -14.165  1.00 13.06           N  
ANISOU 4938  N   GLY B 236     1606   1815   1542    145     67    109       N  
ATOM   4939  CA  GLY B 236      31.399  -2.312 -12.853  1.00 13.81           C  
ANISOU 4939  CA  GLY B 236     1749   1941   1555    179     41     95       C  
ATOM   4940  C   GLY B 236      30.838  -2.989 -11.631  1.00 12.35           C  
ANISOU 4940  C   GLY B 236     1435   1708   1550    188      6     70       C  
ATOM   4941  O   GLY B 236      31.228  -2.614 -10.505  1.00 13.49           O  
ANISOU 4941  O   GLY B 236     1627   1810   1689    136    -27    -76       O  
ATOM   4942  N   ALA B 237      29.961  -3.970 -11.756  1.00 11.88           N  
ANISOU 4942  N   ALA B 237     1406   1626   1483    272     35     15       N  
ATOM   4943  CA  ALA B 237      29.477  -4.649 -10.542  1.00 11.46           C  
ANISOU 4943  CA  ALA B 237     1396   1579   1378    355     -1     48       C  
ATOM   4944  C   ALA B 237      30.643  -5.349  -9.834  1.00 11.88           C  
ANISOU 4944  C   ALA B 237     1414   1588   1510    427     25    -49       C  
ATOM   4945  O   ALA B 237      31.442  -6.017 -10.507  1.00 14.11           O  
ANISOU 4945  O   ALA B 237     1694   2121   1545    774     30    -63       O  
ATOM   4946  CB  ALA B 237      28.363  -5.647 -10.817  1.00 12.62           C  
ANISOU 4946  CB  ALA B 237     1537   1668   1591    185     21     99       C  
ATOM   4947  N   THR B 238      30.699  -5.245  -8.512  1.00 11.54           N  
ANISOU 4947  N   THR B 238     1362   1584   1441    391    -18    -42       N  
ATOM   4948  CA  THR B 238      31.724  -5.935  -7.727  1.00 12.45           C  
ANISOU 4948  CA  THR B 238     1412   1639   1681    375    -50     61       C  
ATOM   4949  C   THR B 238      31.256  -7.293  -7.274  1.00 12.13           C  
ANISOU 4949  C   THR B 238     1423   1635   1551    392      2    169       C  
ATOM   4950  O   THR B 238      32.096  -8.161  -6.942  1.00 15.62           O  
ANISOU 4950  O   THR B 238     1827   2133   1975    808    -23    184       O  
ATOM   4951  CB  THR B 238      32.128  -5.060  -6.521  1.00 13.72           C  
ANISOU 4951  CB  THR B 238     1510   1993   1709    544    -49   -104       C  
ATOM   4952  OG1 THR B 238      30.942  -4.643  -5.801  1.00 13.58           O  
ANISOU 4952  OG1 THR B 238     1673   1929   1560    662    -68   -203       O  
ATOM   4953  CG2 THR B 238      32.867  -3.822  -6.921  1.00 16.31           C  
ANISOU 4953  CG2 THR B 238     1810   2289   2097    181    -48   -212       C  
ATOM   4954  N   GLU B 239      29.965  -7.565  -7.218  1.00 13.99           N  
ANISOU 4954  N   GLU B 239     1552   1721   2043    163   -145    280       N  
ATOM   4955  CA  GLU B 239      29.340  -8.786  -6.756  1.00 14.45           C  
ANISOU 4955  CA  GLU B 239     1716   1826   1948    -31   -353    296       C  
ATOM   4956  C   GLU B 239      27.930  -8.861  -7.379  1.00 12.03           C  
ANISOU 4956  C   GLU B 239     1541   1402   1625    239    -65     47       C  
ATOM   4957  O   GLU B 239      27.350  -7.795  -7.635  1.00 12.61           O  
ANISOU 4957  O   GLU B 239     1593   1451   1747    408   -264    -90       O  
ATOM   4958  CB AGLU B 239      29.294  -8.866  -5.222  0.63 18.24           C  
ANISOU 4958  CB AGLU B 239     2450   2468   2013    -76   -619    335       C  
ATOM   4959  CG AGLU B 239      28.899  -7.517  -4.646  0.63 20.08           C  
ANISOU 4959  CG AGLU B 239     2428   2978   2223    353   -264     34       C  
ATOM   4960  CD AGLU B 239      29.790  -6.993  -3.527  0.63 18.04           C  
ANISOU 4960  CD AGLU B 239     2296   2569   1989    659   -200     12       C  
ATOM   4961  OE1AGLU B 239      29.774  -7.732  -2.511  0.63 19.43           O  
ANISOU 4961  OE1AGLU B 239     2466   3170   1745    238     45     56       O  
ATOM   4962  OE2AGLU B 239      30.528  -5.962  -3.454  0.63 16.79           O  
ANISOU 4962  OE2AGLU B 239     2555   2241   1584    916     60    263       O  
ATOM   4963  CB BGLU B 239      29.059  -8.679  -5.232  0.37 16.32           C  
ANISOU 4963  CB BGLU B 239     2010   2189   2002   -140   -370    300       C  
ATOM   4964  CG BGLU B 239      30.235  -8.620  -4.269  0.37 15.39           C  
ANISOU 4964  CG BGLU B 239     1718   2074   2055     47   -220    209       C  
ATOM   4965  CD BGLU B 239      29.751  -8.821  -2.837  0.37 18.85           C  
ANISOU 4965  CD BGLU B 239     2140   2894   2127     82    -48    125       C  
ATOM   4966  OE1BGLU B 239      29.263  -7.811  -2.289  0.37 17.47           O  
ANISOU 4966  OE1BGLU B 239     1881   3064   1692    105   -298     85       O  
ATOM   4967  OE2BGLU B 239      29.850  -9.969  -2.317  0.37 19.94           O  
ANISOU 4967  OE2BGLU B 239     2105   3243   2229    253    176    347       O  
ATOM   4968  N   CYS B 240      27.430 -10.065  -7.570  1.00 11.82           N  
ANISOU 4968  N   CYS B 240     1399   1379   1713    253    -14      2       N  
ATOM   4969  CA  CYS B 240      26.057 -10.262  -8.036  1.00 12.89           C  
ANISOU 4969  CA  CYS B 240     1534   1587   1777    151     41    -23       C  
ATOM   4970  C   CYS B 240      25.344 -11.305  -7.197  1.00 13.06           C  
ANISOU 4970  C   CYS B 240     1727   1393   1841    226   -133    110       C  
ATOM   4971  O   CYS B 240      25.969 -12.324  -6.805  1.00 15.93           O  
ANISOU 4971  O   CYS B 240     1965   1691   2395    447   -280    265       O  
ATOM   4972  CB  CYS B 240      25.996 -10.684  -9.509  1.00 15.11           C  
ANISOU 4972  CB  CYS B 240     2346   1683   1713    170   -139    -30       C  
ATOM   4973  SG  CYS B 240      26.443  -9.362 -10.659  1.00 15.86           S  
ANISOU 4973  SG  CYS B 240     2625   1898   1504    158    -43     -9       S  
ATOM   4974  N   VAL B 241      24.054 -11.135  -6.897  1.00 12.67           N  
ANISOU 4974  N   VAL B 241     1706   1320   1787    134    -48    125       N  
ATOM   4975  CA  VAL B 241      23.254 -12.061  -6.117  1.00 13.66           C  
ANISOU 4975  CA  VAL B 241     1737   1601   1851    140    -30    187       C  
ATOM   4976  C   VAL B 241      21.949 -12.348  -6.828  1.00 12.40           C  
ANISOU 4976  C   VAL B 241     1713   1275   1723    127    -39    126       C  
ATOM   4977  O   VAL B 241      21.283 -11.456  -7.394  1.00 13.02           O  
ANISOU 4977  O   VAL B 241     1872   1308   1768    239   -205     57       O  
ATOM   4978  CB  VAL B 241      23.048 -11.639  -4.652  1.00 15.83           C  
ANISOU 4978  CB  VAL B 241     2152   1920   1943     33   -141     38       C  
ATOM   4979  CG1 VAL B 241      24.402 -11.565  -3.941  1.00 18.01           C  
ANISOU 4979  CG1 VAL B 241     2322   2484   2038    -27   -234     99       C  
ATOM   4980  CG2 VAL B 241      22.314 -10.334  -4.582  1.00 17.18           C  
ANISOU 4980  CG2 VAL B 241     2266   1962   2299     70     53    230       C  
ATOM   4981  N   ASN B 242      21.519 -13.610  -6.729  1.00 13.83           N  
ANISOU 4981  N   ASN B 242     1928   1339   1990    192    -11    307       N  
ATOM   4982  CA  ASN B 242      20.238 -14.086  -7.253  1.00 14.07           C  
ANISOU 4982  CA  ASN B 242     2170   1542   1635    174   -210    121       C  
ATOM   4983  C   ASN B 242      19.309 -14.365  -6.085  1.00 13.81           C  
ANISOU 4983  C   ASN B 242     2002   1354   1889    160   -139     84       C  
ATOM   4984  O   ASN B 242      19.610 -15.330  -5.330  1.00 14.47           O  
ANISOU 4984  O   ASN B 242     1923   1583   1991     58   -264    264       O  
ATOM   4985  CB  ASN B 242      20.446 -15.359  -8.081  1.00 16.16           C  
ANISOU 4985  CB  ASN B 242     2488   1625   2027     46   -110     66       C  
ATOM   4986  CG  ASN B 242      19.155 -15.900  -8.628  1.00 17.60           C  
ANISOU 4986  CG  ASN B 242     2708   1823   2156   -144   -156   -118       C  
ATOM   4987  OD1 ASN B 242      18.023 -15.527  -8.278  1.00 16.80           O  
ANISOU 4987  OD1 ASN B 242     2534   1763   2086   -317   -294     88       O  
ATOM   4988  ND2 ASN B 242      19.345 -16.904  -9.509  1.00 23.14           N  
ANISOU 4988  ND2 ASN B 242     3475   2676   2641    -52   -136   -653       N  
ATOM   4989  N   PRO B 243      18.205 -13.666  -5.874  1.00 14.01           N  
ANISOU 4989  N   PRO B 243     1879   1523   1922    147   -183    202       N  
ATOM   4990  CA  PRO B 243      17.298 -13.941  -4.768  1.00 14.70           C  
ANISOU 4990  CA  PRO B 243     1974   1706   1907     85   -127     59       C  
ATOM   4991  C   PRO B 243      16.820 -15.387  -4.647  1.00 15.22           C  
ANISOU 4991  C   PRO B 243     1982   1800   2001     16   -140    271       C  
ATOM   4992  O   PRO B 243      16.564 -15.876  -3.545  1.00 16.20           O  
ANISOU 4992  O   PRO B 243     2069   1859   2228     90    -42    374       O  
ATOM   4993  CB  PRO B 243      16.088 -13.009  -5.001  1.00 16.21           C  
ANISOU 4993  CB  PRO B 243     2110   1784   2265    141   -146    285       C  
ATOM   4994  CG  PRO B 243      16.735 -11.884  -5.782  1.00 17.35           C  
ANISOU 4994  CG  PRO B 243     2046   1987   2558    189     59    365       C  
ATOM   4995  CD  PRO B 243      17.768 -12.531  -6.697  1.00 14.63           C  
ANISOU 4995  CD  PRO B 243     2004   1562   1994    118   -265    238       C  
ATOM   4996  N   GLN B 244      16.713 -16.088  -5.785  1.00 16.99           N  
ANISOU 4996  N   GLN B 244     2406   1825   2223   -144   -231    134       N  
ATOM   4997  CA  GLN B 244      16.256 -17.482  -5.747  1.00 19.56           C  
ANISOU 4997  CA  GLN B 244     2784   1953   2695   -220   -336    210       C  
ATOM   4998  C   GLN B 244      17.272 -18.409  -5.094  1.00 19.05           C  
ANISOU 4998  C   GLN B 244     2780   1902   2557   -124   -223    228       C  
ATOM   4999  O   GLN B 244      16.909 -19.566  -4.754  1.00 21.56           O  
ANISOU 4999  O   GLN B 244     3216   2048   2926   -322   -251    313       O  
ATOM   5000  CB AGLN B 244      16.132 -18.020  -7.194  0.51 22.13           C  
ANISOU 5000  CB AGLN B 244     3133   2485   2790   -273   -126    -14       C  
ATOM   5001  CG AGLN B 244      15.281 -17.197  -8.126  0.51 23.38           C  
ANISOU 5001  CG AGLN B 244     3190   2652   3042   -152   -184     -7       C  
ATOM   5002  CD AGLN B 244      15.106 -17.652  -9.554  0.51 24.57           C  
ANISOU 5002  CD AGLN B 244     3349   2802   3186   -231    -95   -195       C  
ATOM   5003  OE1AGLN B 244      14.014 -17.403 -10.091  0.51 25.93           O  
ANISOU 5003  OE1AGLN B 244     3475   2941   3435    -97   -139    -65       O  
ATOM   5004  NE2AGLN B 244      16.116 -18.192 -10.214  0.51 22.70           N  
ANISOU 5004  NE2AGLN B 244     3328   2355   2943   -332   -252   -400       N  
ATOM   5005  CB BGLN B 244      15.735 -17.900  -7.119  0.49 22.84           C  
ANISOU 5005  CB BGLN B 244     3214   2735   2730   -263   -241     47       C  
ATOM   5006  CG BGLN B 244      14.526 -17.052  -7.531  0.49 25.00           C  
ANISOU 5006  CG BGLN B 244     3275   2983   3240   -158   -158    197       C  
ATOM   5007  CD BGLN B 244      13.987 -17.369  -8.907  0.49 27.21           C  
ANISOU 5007  CD BGLN B 244     3646   3428   3265   -284   -120     89       C  
ATOM   5008  OE1BGLN B 244      12.997 -16.762  -9.330  0.49 28.50           O  
ANISOU 5008  OE1BGLN B 244     3686   3546   3597   -285   -168    148       O  
ATOM   5009  NE2BGLN B 244      14.629 -18.303  -9.602  0.49 27.87           N  
ANISOU 5009  NE2BGLN B 244     3739   3479   3373   -170   -185     96       N  
ATOM   5010  N   ASP B 245      18.515 -17.991  -4.862  1.00 17.31           N  
ANISOU 5010  N   ASP B 245     2694   1612   2272     62   -238    130       N  
ATOM   5011  CA  ASP B 245      19.539 -18.833  -4.249  1.00 17.18           C  
ANISOU 5011  CA  ASP B 245     2375   1745   2409     61    -21    218       C  
ATOM   5012  C   ASP B 245      19.451 -18.842  -2.733  1.00 14.96           C  
ANISOU 5012  C   ASP B 245     1970   1377   2336    -47     84    348       C  
ATOM   5013  O   ASP B 245      20.193 -19.610  -2.076  1.00 16.49           O  
ANISOU 5013  O   ASP B 245     2109   1547   2610     41     64    499       O  
ATOM   5014  CB  ASP B 245      20.962 -18.372  -4.657  1.00 18.64           C  
ANISOU 5014  CB  ASP B 245     2395   1834   2853    274    183    221       C  
ATOM   5015  CG  ASP B 245      21.369 -18.679  -6.089  1.00 22.31           C  
ANISOU 5015  CG  ASP B 245     3023   2533   2920    246    369    244       C  
ATOM   5016  OD1 ASP B 245      20.663 -19.426  -6.803  1.00 24.27           O  
ANISOU 5016  OD1 ASP B 245     3428   2761   3032    239    562   -156       O  
ATOM   5017  OD2 ASP B 245      22.434 -18.157  -6.529  1.00 24.31           O  
ANISOU 5017  OD2 ASP B 245     3213   2548   3476    429    665    448       O  
ATOM   5018  N   TYR B 246      18.620 -17.974  -2.120  1.00 15.08           N  
ANISOU 5018  N   TYR B 246     1911   1662   2155      4    122    382       N  
ATOM   5019  CA  TYR B 246      18.596 -17.737  -0.697  1.00 14.38           C  
ANISOU 5019  CA  TYR B 246     1638   1748   2079     58    181    378       C  
ATOM   5020  C   TYR B 246      17.301 -18.197  -0.028  1.00 16.32           C  
ANISOU 5020  C   TYR B 246     1636   2355   2212     77    150    504       C  
ATOM   5021  O   TYR B 246      16.210 -18.121  -0.609  1.00 19.70           O  
ANISOU 5021  O   TYR B 246     1698   3320   2465     72     88    745       O  
ATOM   5022  CB ATYR B 246      18.747 -16.236  -0.391  0.60 14.42           C  
ANISOU 5022  CB ATYR B 246     1595   1787   2097     60    117    254       C  
ATOM   5023  CG ATYR B 246      20.132 -15.729  -0.718  0.60 12.30           C  
ANISOU 5023  CG ATYR B 246     1499   1504   1671    159      7    148       C  
ATOM   5024  CD1ATYR B 246      20.436 -15.315  -2.014  0.60 13.70           C  
ANISOU 5024  CD1ATYR B 246     1871   1591   1742    111     13    252       C  
ATOM   5025  CD2ATYR B 246      21.113 -15.674   0.252  0.60 12.73           C  
ANISOU 5025  CD2ATYR B 246     1526   1533   1776    254    -90     17       C  
ATOM   5026  CE1ATYR B 246      21.697 -14.849  -2.345  0.60 14.52           C  
ANISOU 5026  CE1ATYR B 246     1968   1776   1771   -118    -82    139       C  
ATOM   5027  CE2ATYR B 246      22.382 -15.201  -0.065  0.60 11.94           C  
ANISOU 5027  CE2ATYR B 246     1697   1316   1526    150    -21    -76       C  
ATOM   5028  CZ ATYR B 246      22.662 -14.801  -1.358  0.60 13.21           C  
ANISOU 5028  CZ ATYR B 246     1858   1400   1763    -54    -44    180       C  
ATOM   5029  OH ATYR B 246      23.921 -14.323  -1.666  0.60 16.21           O  
ANISOU 5029  OH ATYR B 246     1978   2015   2166    -43    160    262       O  
ATOM   5030  CB BTYR B 246      18.844 -16.238  -0.420  0.40 14.66           C  
ANISOU 5030  CB BTYR B 246     1730   1791   2050     64     89    275       C  
ATOM   5031  CG BTYR B 246      20.160 -15.717  -0.955  0.40 13.37           C  
ANISOU 5031  CG BTYR B 246     1649   1667   1765    161     55    147       C  
ATOM   5032  CD1BTYR B 246      20.278 -15.291  -2.279  0.40 13.99           C  
ANISOU 5032  CD1BTYR B 246     1876   1653   1786     52     31    189       C  
ATOM   5033  CD2BTYR B 246      21.296 -15.642  -0.164  0.40 13.43           C  
ANISOU 5033  CD2BTYR B 246     1744   1811   1548    167     48    100       C  
ATOM   5034  CE1BTYR B 246      21.478 -14.813  -2.780  0.40 13.74           C  
ANISOU 5034  CE1BTYR B 246     1740   1792   1690    -79   -163      2       C  
ATOM   5035  CE2BTYR B 246      22.502 -15.164  -0.647  0.40 13.09           C  
ANISOU 5035  CE2BTYR B 246     1681   1661   1632    159     -5     45       C  
ATOM   5036  CZ BTYR B 246      22.594 -14.757  -1.965  0.40 12.71           C  
ANISOU 5036  CZ BTYR B 246     1673   1583   1573     81    -90    -39       C  
ATOM   5037  OH BTYR B 246      23.781 -14.279  -2.475  0.40 14.78           O  
ANISOU 5037  OH BTYR B 246     1962   1692   1962   -155    -81    178       O  
ATOM   5038  N   LYS B 247      17.433 -18.655   1.211  1.00 16.15           N  
ANISOU 5038  N   LYS B 247     1731   2135   2269    -44    115    668       N  
ATOM   5039  CA  LYS B 247      16.292 -19.056   2.024  1.00 18.78           C  
ANISOU 5039  CA  LYS B 247     2067   2696   2375   -202    264    602       C  
ATOM   5040  C   LYS B 247      15.674 -17.846   2.719  1.00 23.45           C  
ANISOU 5040  C   LYS B 247     2920   3249   2742    -66    199    -14       C  
ATOM   5041  O   LYS B 247      14.531 -17.933   3.208  1.00 30.98           O  
ANISOU 5041  O   LYS B 247     3240   4472   4058   -442    556   -285       O  
ATOM   5042  CB  LYS B 247      16.655 -20.194   3.007  1.00 20.90           C  
ANISOU 5042  CB  LYS B 247     2400   2918   2622   -360    -21    707       C  
ATOM   5043  CG  LYS B 247      17.113 -21.468   2.319  1.00 22.75           C  
ANISOU 5043  CG  LYS B 247     2508   3088   3047   -183     32    607       C  
ATOM   5044  CD  LYS B 247      17.386 -22.564   3.383  1.00 25.74           C  
ANISOU 5044  CD  LYS B 247     2906   3391   3482   -249     -8    839       C  
ATOM   5045  CE  LYS B 247      17.932 -23.790   2.698  1.00 29.43           C  
ANISOU 5045  CE  LYS B 247     3380   3772   4029    -33    133    521       C  
ATOM   5046  NZ  LYS B 247      18.268 -24.857   3.705  1.00 32.88           N  
ANISOU 5046  NZ  LYS B 247     3859   4076   4559    119    157    874       N  
ATOM   5047  N   LYS B 248      16.303 -16.701   2.861  1.00 22.31           N  
ANISOU 5047  N   LYS B 248     2955   2813   2710    203    458    426       N  
ATOM   5048  CA  LYS B 248      15.716 -15.520   3.520  1.00 24.78           C  
ANISOU 5048  CA  LYS B 248     3396   2925   3094    404    424    359       C  
ATOM   5049  C   LYS B 248      15.492 -14.420   2.490  1.00 20.92           C  
ANISOU 5049  C   LYS B 248     2713   2588   2648    113    507    190       C  
ATOM   5050  O   LYS B 248      16.041 -14.485   1.373  1.00 17.95           O  
ANISOU 5050  O   LYS B 248     2490   1930   2399    172    321    215       O  
ATOM   5051  CB  LYS B 248      16.586 -15.076   4.690  1.00 32.61           C  
ANISOU 5051  CB  LYS B 248     4502   4079   3810    320   -117    -33       C  
ATOM   5052  CG ALYS B 248      17.853 -14.356   4.302  0.60 37.16           C  
ANISOU 5052  CG ALYS B 248     4886   4749   4485    140    266    175       C  
ATOM   5053  CD ALYS B 248      18.667 -13.741   5.424  0.60 41.20           C  
ANISOU 5053  CD ALYS B 248     5540   5300   4815    -79    173   -174       C  
ATOM   5054  CE ALYS B 248      19.633 -14.692   6.087  0.60 43.31           C  
ANISOU 5054  CE ALYS B 248     5854   5470   5131    143    208    -81       C  
ATOM   5055  NZ ALYS B 248      20.950 -14.072   6.417  0.60 43.77           N  
ANISOU 5055  NZ ALYS B 248     5941   5409   5280    155    103   -171       N  
ATOM   5056  CG BLYS B 248      17.940 -14.484   4.450  0.40 37.41           C  
ANISOU 5056  CG BLYS B 248     4896   4625   4693    -10    269     34       C  
ATOM   5057  CD BLYS B 248      18.969 -14.916   5.478  0.40 40.93           C  
ANISOU 5057  CD BLYS B 248     5185   5130   5238     93      3    198       C  
ATOM   5058  CE BLYS B 248      18.769 -14.385   6.878  0.40 43.31           C  
ANISOU 5058  CE BLYS B 248     5600   5416   5441    -23    250     21       C  
ATOM   5059  NZ BLYS B 248      19.846 -14.857   7.803  0.40 43.99           N  
ANISOU 5059  NZ BLYS B 248     5743   5512   5458     20    188      0       N  
ATOM   5060  N   PRO B 249      14.636 -13.455   2.789  1.00 19.16           N  
ANISOU 5060  N   PRO B 249     2483   2324   2472     54    343    461       N  
ATOM   5061  CA  PRO B 249      14.340 -12.356   1.861  1.00 18.14           C  
ANISOU 5061  CA  PRO B 249     2314   2145   2433    -30    160    348       C  
ATOM   5062  C   PRO B 249      15.609 -11.588   1.478  1.00 16.45           C  
ANISOU 5062  C   PRO B 249     2345   1896   2008   -101     -4    251       C  
ATOM   5063  O   PRO B 249      16.497 -11.361   2.348  1.00 16.09           O  
ANISOU 5063  O   PRO B 249     2267   1818   2028     -9     27    282       O  
ATOM   5064  CB  PRO B 249      13.317 -11.472   2.579  1.00 20.85           C  
ANISOU 5064  CB  PRO B 249     2513   2400   3010    134    243    165       C  
ATOM   5065  CG  PRO B 249      12.820 -12.321   3.707  1.00 23.06           C  
ANISOU 5065  CG  PRO B 249     3042   2789   2930    371    359    266       C  
ATOM   5066  CD  PRO B 249      13.855 -13.377   4.035  1.00 21.21           C  
ANISOU 5066  CD  PRO B 249     2737   2678   2645    241    420    229       C  
ATOM   5067  N   ILE B 250      15.718 -11.189   0.207  1.00 15.88           N  
ANISOU 5067  N   ILE B 250     2009   2117   1909     -6     49    152       N  
ATOM   5068  CA  ILE B 250      16.945 -10.528  -0.245  1.00 15.33           C  
ANISOU 5068  CA  ILE B 250     2247   1675   1903   -119     93     29       C  
ATOM   5069  C   ILE B 250      17.204  -9.204   0.461  1.00 14.75           C  
ANISOU 5069  C   ILE B 250     2157   1613   1833     18    117     98       C  
ATOM   5070  O   ILE B 250      18.374  -8.836   0.585  1.00 14.98           O  
ANISOU 5070  O   ILE B 250     2128   1845   1717     78      1     36       O  
ATOM   5071  CB  ILE B 250      17.065 -10.466  -1.786  1.00 16.59           C  
ANISOU 5071  CB  ILE B 250     2357   1982   1965    160    208     15       C  
ATOM   5072  CG1 ILE B 250      18.510 -10.388  -2.307  1.00 17.02           C  
ANISOU 5072  CG1 ILE B 250     2285   2101   2081    152    153   -176       C  
ATOM   5073  CG2 ILE B 250      16.223  -9.335  -2.304  1.00 18.28           C  
ANISOU 5073  CG2 ILE B 250     2896   1935   2113    211   -205   -129       C  
ATOM   5074  CD1 ILE B 250      19.353 -11.628  -2.152  1.00 18.40           C  
ANISOU 5074  CD1 ILE B 250     2129   2256   2607    111    -54   -110       C  
ATOM   5075  N   GLN B 251      16.193  -8.510   0.991  1.00 15.60           N  
ANISOU 5075  N   GLN B 251     2198   1757   1973    204    -34    107       N  
ATOM   5076  CA  GLN B 251      16.486  -7.270   1.734  1.00 15.35           C  
ANISOU 5076  CA  GLN B 251     2227   1718   1887    226    -53    138       C  
ATOM   5077  C   GLN B 251      17.357  -7.593   2.956  1.00 15.39           C  
ANISOU 5077  C   GLN B 251     2247   1751   1848     31    -63    123       C  
ATOM   5078  O   GLN B 251      18.216  -6.786   3.352  1.00 15.49           O  
ANISOU 5078  O   GLN B 251     2113   1789   1985     48     80    103       O  
ATOM   5079  CB AGLN B 251      15.146  -6.630   2.123  0.51 17.94           C  
ANISOU 5079  CB AGLN B 251     2364   2188   2265    342     46     95       C  
ATOM   5080  CG AGLN B 251      14.089  -7.661   2.561  0.51 20.83           C  
ANISOU 5080  CG AGLN B 251     2771   2485   2658    115     90    226       C  
ATOM   5081  CD AGLN B 251      13.196  -8.121   1.437  0.51 21.37           C  
ANISOU 5081  CD AGLN B 251     2956   2437   2726    130     21     47       C  
ATOM   5082  OE1AGLN B 251      13.303  -8.799   0.403  0.51 18.00           O  
ANISOU 5082  OE1AGLN B 251     2440   1847   2553    463     47    409       O  
ATOM   5083  NE2AGLN B 251      11.965  -7.564   1.573  0.51 25.49           N  
ANISOU 5083  NE2AGLN B 251     3106   3129   3449    298    152    119       N  
ATOM   5084  CB BGLN B 251      15.252  -6.453   2.128  0.49 14.37           C  
ANISOU 5084  CB BGLN B 251     2132   1698   1629    188     55    302       C  
ATOM   5085  CG BGLN B 251      14.337  -7.065   3.183  0.49 13.44           C  
ANISOU 5085  CG BGLN B 251     1971   1734   1401    119     32     39       C  
ATOM   5086  CD BGLN B 251      12.937  -6.492   3.270  0.49 15.76           C  
ANISOU 5086  CD BGLN B 251     2042   2063   1882    173     58    148       C  
ATOM   5087  OE1BGLN B 251      12.340  -6.481   4.359  0.49 18.70           O  
ANISOU 5087  OE1BGLN B 251     2395   2549   2163    132    338    166       O  
ATOM   5088  NE2BGLN B 251      12.395  -6.033   2.161  0.49 14.23           N  
ANISOU 5088  NE2BGLN B 251     1722   1916   1770    180     93     52       N  
ATOM   5089  N   GLU B 252      17.120  -8.728   3.628  1.00 15.20           N  
ANISOU 5089  N   GLU B 252     2092   1828   1856      0    -23    158       N  
ATOM   5090  CA  GLU B 252      17.929  -9.133   4.785  1.00 15.94           C  
ANISOU 5090  CA  GLU B 252     2277   1848   1933    125    -80    274       C  
ATOM   5091  C   GLU B 252      19.353  -9.482   4.366  1.00 14.78           C  
ANISOU 5091  C   GLU B 252     2320   1598   1699    136    -80    259       C  
ATOM   5092  O   GLU B 252      20.341  -9.097   4.999  1.00 15.36           O  
ANISOU 5092  O   GLU B 252     2459   1640   1736    115   -117    136       O  
ATOM   5093  CB AGLU B 252      17.315 -10.345   5.501  0.65 17.95           C  
ANISOU 5093  CB AGLU B 252     2687   2151   1983    -50    -50    348       C  
ATOM   5094  CG AGLU B 252      15.980 -10.047   6.149  0.65 21.78           C  
ANISOU 5094  CG AGLU B 252     2953   2974   2349    179    125     -6       C  
ATOM   5095  CD AGLU B 252      15.333 -11.278   6.770  0.65 26.18           C  
ANISOU 5095  CD AGLU B 252     3598   3436   2914   -116    192    240       C  
ATOM   5096  OE1AGLU B 252      16.051 -12.253   7.060  0.65 27.00           O  
ANISOU 5096  OE1AGLU B 252     3780   3473   3006   -108    326    430       O  
ATOM   5097  OE2AGLU B 252      14.098 -11.266   6.971  0.65 29.81           O  
ANISOU 5097  OE2AGLU B 252     3661   4257   3409   -362    276    325       O  
ATOM   5098  CB BGLU B 252      17.251 -10.311   5.490  0.35 17.78           C  
ANISOU 5098  CB BGLU B 252     2528   2077   2149   -101     43    211       C  
ATOM   5099  CG BGLU B 252      17.904 -10.764   6.777  0.35 19.79           C  
ANISOU 5099  CG BGLU B 252     2786   2542   2191     18    -61    118       C  
ATOM   5100  CD BGLU B 252      17.067 -11.764   7.556  0.35 21.31           C  
ANISOU 5100  CD BGLU B 252     2941   2804   2352    -98    102    114       C  
ATOM   5101  OE1BGLU B 252      15.908 -12.023   7.182  0.35 21.53           O  
ANISOU 5101  OE1BGLU B 252     2963   2824   2393   -175    176    262       O  
ATOM   5102  OE2BGLU B 252      17.589 -12.292   8.563  0.35 22.37           O  
ANISOU 5102  OE2BGLU B 252     3098   3009   2391   -137     89    261       O  
ATOM   5103  N   VAL B 253      19.484 -10.226   3.254  1.00 14.66           N  
ANISOU 5103  N   VAL B 253     2204   1595   1771    291   -114    170       N  
ATOM   5104  CA  VAL B 253      20.792 -10.567   2.704  1.00 14.12           C  
ANISOU 5104  CA  VAL B 253     2072   1458   1837    151   -130    149       C  
ATOM   5105  C   VAL B 253      21.634  -9.333   2.419  1.00 13.36           C  
ANISOU 5105  C   VAL B 253     2137   1252   1688    223    -99    -20       C  
ATOM   5106  O   VAL B 253      22.808  -9.198   2.787  1.00 14.11           O  
ANISOU 5106  O   VAL B 253     2196   1315   1850    312    -19    -40       O  
ATOM   5107  CB  VAL B 253      20.621 -11.433   1.440  1.00 15.28           C  
ANISOU 5107  CB  VAL B 253     2354   1450   2001    163   -143    -39       C  
ATOM   5108  CG1 VAL B 253      21.964 -11.700   0.770  1.00 17.26           C  
ANISOU 5108  CG1 VAL B 253     2488   1744   2325    186    -50   -229       C  
ATOM   5109  CG2 VAL B 253      19.878 -12.736   1.733  1.00 17.32           C  
ANISOU 5109  CG2 VAL B 253     2796   1480   2303    112   -132    126       C  
ATOM   5110  N   LEU B 254      21.004  -8.364   1.698  1.00 13.07           N  
ANISOU 5110  N   LEU B 254     2079   1288   1600    288     16     52       N  
ATOM   5111  CA  LEU B 254      21.720  -7.145   1.324  1.00 12.18           C  
ANISOU 5111  CA  LEU B 254     1644   1429   1555    298     79     60       C  
ATOM   5112  C   LEU B 254      22.069  -6.273   2.529  1.00 11.50           C  
ANISOU 5112  C   LEU B 254     1559   1315   1497    303     45    135       C  
ATOM   5113  O   LEU B 254      23.135  -5.656   2.536  1.00 11.94           O  
ANISOU 5113  O   LEU B 254     1763   1199   1575    241     16    -61       O  
ATOM   5114  CB  LEU B 254      20.909  -6.329   0.302  1.00 12.32           C  
ANISOU 5114  CB  LEU B 254     1643   1523   1514    379    -19     51       C  
ATOM   5115  CG  LEU B 254      20.774  -7.006  -1.070  1.00 13.78           C  
ANISOU 5115  CG  LEU B 254     1931   1899   1406    329    -13    100       C  
ATOM   5116  CD1 LEU B 254      19.657  -6.351  -1.853  1.00 14.07           C  
ANISOU 5116  CD1 LEU B 254     1734   2019   1591    159    -63    120       C  
ATOM   5117  CD2 LEU B 254      22.081  -6.942  -1.856  1.00 15.15           C  
ANISOU 5117  CD2 LEU B 254     1862   2299   1597    356    -86     35       C  
ATOM   5118  N   THR B 255      21.208  -6.238   3.532  1.00 12.11           N  
ANISOU 5118  N   THR B 255     1761   1365   1475    252     53     92       N  
ATOM   5119  CA  THR B 255      21.514  -5.482   4.774  1.00 12.76           C  
ANISOU 5119  CA  THR B 255     1864   1534   1448    462    -31     60       C  
ATOM   5120  C   THR B 255      22.727  -6.104   5.459  1.00 12.25           C  
ANISOU 5120  C   THR B 255     1888   1293   1474    367    -48    152       C  
ATOM   5121  O   THR B 255      23.644  -5.411   5.913  1.00 13.27           O  
ANISOU 5121  O   THR B 255     1986   1487   1570    396   -112     34       O  
ATOM   5122  CB  THR B 255      20.271  -5.451   5.679  1.00 13.32           C  
ANISOU 5122  CB  THR B 255     1953   1514   1592    462     44     23       C  
ATOM   5123  OG1 THR B 255      19.225  -4.715   5.011  1.00 13.84           O  
ANISOU 5123  OG1 THR B 255     1917   1667   1676    494     95     34       O  
ATOM   5124  CG2 THR B 255      20.509  -4.775   7.022  1.00 14.35           C  
ANISOU 5124  CG2 THR B 255     2145   1847   1462    345     -7     68       C  
ATOM   5125  N   GLU B 256      22.759  -7.451   5.557  1.00 13.95           N  
ANISOU 5125  N   GLU B 256     2099   1445   1758    431   -129     22       N  
ATOM   5126  CA  GLU B 256      23.929  -8.105   6.182  1.00 15.07           C  
ANISOU 5126  CA  GLU B 256     2033   1737   1958    379    -99    204       C  
ATOM   5127  C   GLU B 256      25.200  -7.890   5.384  1.00 13.70           C  
ANISOU 5127  C   GLU B 256     2071   1298   1837    524   -120    -44       C  
ATOM   5128  O   GLU B 256      26.287  -7.578   5.907  1.00 14.48           O  
ANISOU 5128  O   GLU B 256     2191   1503   1808    520   -199    116       O  
ATOM   5129  CB AGLU B 256      23.631  -9.590   6.379  0.51 14.13           C  
ANISOU 5129  CB AGLU B 256     1901   1668   1797    382   -143     54       C  
ATOM   5130  CG AGLU B 256      23.313 -10.366   5.120  0.51 14.32           C  
ANISOU 5130  CG AGLU B 256     1960   1620   1860    250   -178     66       C  
ATOM   5131  CD AGLU B 256      24.443 -11.192   4.542  0.51 13.62           C  
ANISOU 5131  CD AGLU B 256     1674   1584   1917    131   -274    102       C  
ATOM   5132  OE1AGLU B 256      25.628 -10.880   4.764  0.51 11.01           O  
ANISOU 5132  OE1AGLU B 256     1344   1026   1812    457   -116    170       O  
ATOM   5133  OE2AGLU B 256      24.155 -12.203   3.858  0.51 13.27           O  
ANISOU 5133  OE2AGLU B 256     2343    902   1796    418   -285    410       O  
ATOM   5134  CB BGLU B 256      23.565  -9.561   6.404  0.49 17.76           C  
ANISOU 5134  CB BGLU B 256     2568   1881   2300    238    106     56       C  
ATOM   5135  CG BGLU B 256      24.706 -10.360   7.006  0.49 21.50           C  
ANISOU 5135  CG BGLU B 256     2666   2814   2687    493     17    143       C  
ATOM   5136  CD BGLU B 256      24.234 -11.725   7.438  0.49 25.31           C  
ANISOU 5136  CD BGLU B 256     3362   3067   3188    143    128    135       C  
ATOM   5137  OE1BGLU B 256      23.122 -12.173   7.106  0.49 26.66           O  
ANISOU 5137  OE1BGLU B 256     3423   3262   3447     57     70    198       O  
ATOM   5138  OE2BGLU B 256      25.091 -12.321   8.149  0.49 27.09           O  
ANISOU 5138  OE2BGLU B 256     3631   3387   3276    362    178    313       O  
ATOM   5139  N   MET B 257      25.139  -8.003   4.033  1.00 13.23           N  
ANISOU 5139  N   MET B 257     1842   1431   1754    366     27     92       N  
ATOM   5140  CA  MET B 257      26.311  -7.843   3.187  1.00 13.72           C  
ANISOU 5140  CA  MET B 257     1777   1519   1916    374    -34    -12       C  
ATOM   5141  C   MET B 257      26.980  -6.484   3.301  1.00 13.28           C  
ANISOU 5141  C   MET B 257     1823   1462   1762    391    -50     69       C  
ATOM   5142  O   MET B 257      28.198  -6.310   3.175  1.00 15.10           O  
ANISOU 5142  O   MET B 257     1844   1542   2350    611     25    138       O  
ATOM   5143  CB  MET B 257      26.006  -8.054   1.672  1.00 15.32           C  
ANISOU 5143  CB  MET B 257     2145   1743   1933    548     26    -81       C  
ATOM   5144  CG  MET B 257      25.657  -9.489   1.313  1.00 16.07           C  
ANISOU 5144  CG  MET B 257     2188   1849   2069    777   -182   -146       C  
ATOM   5145  SD  MET B 257      25.087  -9.639  -0.382  1.00 16.76           S  
ANISOU 5145  SD  MET B 257     2131   2312   1927    549   -141   -321       S  
ATOM   5146  CE  MET B 257      26.589  -9.216  -1.293  1.00 18.42           C  
ANISOU 5146  CE  MET B 257     2418   2307   2275    111    -90   -210       C  
ATOM   5147  N   SER B 258      26.122  -5.459   3.504  1.00 12.72           N  
ANISOU 5147  N   SER B 258     1801   1437   1596    474   -185     92       N  
ATOM   5148  CA  SER B 258      26.523  -4.064   3.612  1.00 12.55           C  
ANISOU 5148  CA  SER B 258     1732   1511   1526    391    -85    136       C  
ATOM   5149  C   SER B 258      26.711  -3.619   5.057  1.00 12.78           C  
ANISOU 5149  C   SER B 258     1855   1476   1526    420    -24    169       C  
ATOM   5150  O   SER B 258      26.846  -2.407   5.307  1.00 13.71           O  
ANISOU 5150  O   SER B 258     2005   1528   1674    521   -229    114       O  
ATOM   5151  CB  SER B 258      25.500  -3.157   2.901  1.00 11.67           C  
ANISOU 5151  CB  SER B 258     1624   1379   1432    393    -64     -9       C  
ATOM   5152  OG  SER B 258      24.214  -3.315   3.477  1.00 11.82           O  
ANISOU 5152  OG  SER B 258     1612   1415   1466    535    -69    146       O  
ATOM   5153  N   ASN B 259      26.769  -4.553   6.020  1.00 13.11           N  
ANISOU 5153  N   ASN B 259     1913   1571   1497    506   -195    175       N  
ATOM   5154  CA  ASN B 259      27.030  -4.205   7.423  1.00 13.90           C  
ANISOU 5154  CA  ASN B 259     2003   1596   1684    363   -287    -39       C  
ATOM   5155  C   ASN B 259      26.020  -3.161   7.899  1.00 13.28           C  
ANISOU 5155  C   ASN B 259     1910   1628   1510    351   -265     49       C  
ATOM   5156  O   ASN B 259      26.400  -2.262   8.668  1.00 16.05           O  
ANISOU 5156  O   ASN B 259     2504   1889   1703    442   -370   -143       O  
ATOM   5157  CB  ASN B 259      28.510  -3.811   7.582  1.00 15.98           C  
ANISOU 5157  CB  ASN B 259     2038   2001   2034    368   -357    -77       C  
ATOM   5158  CG  ASN B 259      29.453  -4.995   7.266  1.00 18.26           C  
ANISOU 5158  CG  ASN B 259     2467   2188   2283    529   -239    -58       C  
ATOM   5159  OD1 ASN B 259      29.446  -6.018   7.962  1.00 22.19           O  
ANISOU 5159  OD1 ASN B 259     2889   2365   3179    688   -432    271       O  
ATOM   5160  ND2 ASN B 259      30.203  -4.871   6.188  1.00 22.47           N  
ANISOU 5160  ND2 ASN B 259     2634   2991   2912    803    133     69       N  
ATOM   5161  N   GLY B 260      24.751  -3.373   7.573  1.00 12.04           N  
ANISOU 5161  N   GLY B 260     1824   1407   1344    344   -181     88       N  
ATOM   5162  CA  GLY B 260      23.663  -2.567   8.081  1.00 13.07           C  
ANISOU 5162  CA  GLY B 260     1961   1642   1362    440   -108     89       C  
ATOM   5163  C   GLY B 260      22.811  -1.805   7.077  1.00 11.14           C  
ANISOU 5163  C   GLY B 260     1834   1111   1286    368    -35     40       C  
ATOM   5164  O   GLY B 260      21.954  -1.000   7.505  1.00 12.41           O  
ANISOU 5164  O   GLY B 260     1929   1407   1380    454     50    -65       O  
ATOM   5165  N   GLY B 261      22.954  -2.024   5.778  1.00 10.86           N  
ANISOU 5165  N   GLY B 261     1649   1262   1215    513    -47    114       N  
ATOM   5166  CA  GLY B 261      22.141  -1.381   4.731  1.00  9.94           C  
ANISOU 5166  CA  GLY B 261     1392   1250   1135    439    -36     50       C  
ATOM   5167  C   GLY B 261      23.025  -0.632   3.753  1.00  9.63           C  
ANISOU 5167  C   GLY B 261     1381   1054   1225    206    -73    -36       C  
ATOM   5168  O   GLY B 261      24.094  -0.137   4.083  1.00 10.95           O  
ANISOU 5168  O   GLY B 261     1480   1399   1281    157    -48     23       O  
ATOM   5169  N   VAL B 262      22.559  -0.566   2.495  1.00  9.98           N  
ANISOU 5169  N   VAL B 262     1466   1150   1176    239    -79    218       N  
ATOM   5170  CA  VAL B 262      23.320   0.089   1.429  1.00  9.95           C  
ANISOU 5170  CA  VAL B 262     1284   1247   1248    315    -19    156       C  
ATOM   5171  C   VAL B 262      23.093   1.608   1.451  1.00  9.91           C  
ANISOU 5171  C   VAL B 262     1342   1253   1172    218     -7    164       C  
ATOM   5172  O   VAL B 262      22.096   2.155   1.955  1.00 10.68           O  
ANISOU 5172  O   VAL B 262     1542   1226   1290    269    112    106       O  
ATOM   5173  CB  VAL B 262      23.002  -0.489   0.019  1.00 10.36           C  
ANISOU 5173  CB  VAL B 262     1428   1245   1265    227    -44    138       C  
ATOM   5174  CG1 VAL B 262      23.237  -1.994   0.005  1.00 11.55           C  
ANISOU 5174  CG1 VAL B 262     1612   1327   1448    305      8     50       C  
ATOM   5175  CG2 VAL B 262      21.587  -0.149  -0.456  1.00 10.50           C  
ANISOU 5175  CG2 VAL B 262     1479   1279   1230    266    -63    -36       C  
ATOM   5176  N   ASP B 263      24.043   2.354   0.857  1.00  9.43           N  
ANISOU 5176  N   ASP B 263     1311   1167   1106    241   -111     88       N  
ATOM   5177  CA  ASP B 263      23.904   3.795   0.707  1.00  9.71           C  
ANISOU 5177  CA  ASP B 263     1512   1217    960    214   -124     80       C  
ATOM   5178  C   ASP B 263      22.822   4.175  -0.321  1.00  9.08           C  
ANISOU 5178  C   ASP B 263     1336   1050   1065    194    -79    147       C  
ATOM   5179  O   ASP B 263      22.048   5.139  -0.115  1.00  9.83           O  
ANISOU 5179  O   ASP B 263     1498   1117   1119    216   -136     37       O  
ATOM   5180  CB  ASP B 263      25.234   4.435   0.343  1.00 10.82           C  
ANISOU 5180  CB  ASP B 263     1581   1364   1166    209   -145    -65       C  
ATOM   5181  CG  ASP B 263      26.300   4.227   1.408  1.00 11.09           C  
ANISOU 5181  CG  ASP B 263     1469   1523   1223    210    -28     77       C  
ATOM   5182  OD1 ASP B 263      26.170   4.878   2.479  1.00 12.76           O  
ANISOU 5182  OD1 ASP B 263     1515   2010   1321    237   -155    -90       O  
ATOM   5183  OD2 ASP B 263      27.232   3.441   1.188  1.00 14.06           O  
ANISOU 5183  OD2 ASP B 263     1796   2186   1358    631   -194   -126       O  
ATOM   5184  N   PHE B 264      22.824   3.486  -1.452  1.00  9.02           N  
ANISOU 5184  N   PHE B 264     1174   1186   1067    257    -86      9       N  
ATOM   5185  CA  PHE B 264      21.925   3.781  -2.567  1.00  9.23           C  
ANISOU 5185  CA  PHE B 264     1142   1165   1198    195   -107     45       C  
ATOM   5186  C   PHE B 264      21.352   2.496  -3.152  1.00  8.91           C  
ANISOU 5186  C   PHE B 264     1138   1229   1020    179    -99    -71       C  
ATOM   5187  O   PHE B 264      22.168   1.583  -3.469  1.00 11.41           O  
ANISOU 5187  O   PHE B 264     1398   1366   1571    349   -175    -99       O  
ATOM   5188  CB  PHE B 264      22.661   4.543  -3.699  1.00  9.73           C  
ANISOU 5188  CB  PHE B 264     1334   1278   1085    202     31     42       C  
ATOM   5189  CG  PHE B 264      23.297   5.833  -3.237  1.00  9.48           C  
ANISOU 5189  CG  PHE B 264     1300   1281   1022    156    -74    143       C  
ATOM   5190  CD1 PHE B 264      22.542   7.016  -3.163  1.00 10.45           C  
ANISOU 5190  CD1 PHE B 264     1473   1388   1111    168    -93    163       C  
ATOM   5191  CD2 PHE B 264      24.633   5.890  -2.816  1.00 10.16           C  
ANISOU 5191  CD2 PHE B 264     1304   1406   1149    145    -43    -12       C  
ATOM   5192  CE1 PHE B 264      23.097   8.168  -2.664  1.00 11.50           C  
ANISOU 5192  CE1 PHE B 264     1618   1429   1323     96    118    109       C  
ATOM   5193  CE2 PHE B 264      25.174   7.047  -2.257  1.00 11.88           C  
ANISOU 5193  CE2 PHE B 264     1608   1548   1358     41   -110     20       C  
ATOM   5194  CZ  PHE B 264      24.393   8.194  -2.205  1.00 11.94           C  
ANISOU 5194  CZ  PHE B 264     1685   1424   1429   -145     34     51       C  
ATOM   5195  N   SER B 265      20.059   2.414  -3.376  1.00  8.69           N  
ANISOU 5195  N   SER B 265     1144   1095   1064    186    -20     27       N  
ATOM   5196  CA  SER B 265      19.489   1.267  -4.107  1.00  8.67           C  
ANISOU 5196  CA  SER B 265     1148   1144   1003    192    -26      9       C  
ATOM   5197  C   SER B 265      18.606   1.786  -5.239  1.00  8.81           C  
ANISOU 5197  C   SER B 265     1274   1033   1042    326    111     82       C  
ATOM   5198  O   SER B 265      18.117   2.918  -5.244  1.00  9.33           O  
ANISOU 5198  O   SER B 265     1265   1148   1130    256     -3     17       O  
ATOM   5199  CB  SER B 265      18.685   0.359  -3.194  1.00  8.95           C  
ANISOU 5199  CB  SER B 265     1155   1046   1199    191    -50     95       C  
ATOM   5200  OG  SER B 265      17.533   1.054  -2.705  1.00 10.60           O  
ANISOU 5200  OG  SER B 265     1258   1289   1482    275    123    264       O  
ATOM   5201  N   PHE B 266      18.443   0.921  -6.269  1.00  8.59           N  
ANISOU 5201  N   PHE B 266     1108   1086   1070    248    -57     88       N  
ATOM   5202  CA  PHE B 266      17.742   1.251  -7.491  1.00  8.86           C  
ANISOU 5202  CA  PHE B 266     1090   1102   1173    175    -21    169       C  
ATOM   5203  C   PHE B 266      16.818   0.105  -7.893  1.00  8.91           C  
ANISOU 5203  C   PHE B 266     1205   1093   1088    141     91    105       C  
ATOM   5204  O   PHE B 266      17.307  -1.047  -8.000  1.00 10.10           O  
ANISOU 5204  O   PHE B 266     1271   1189   1378    185     29    -13       O  
ATOM   5205  CB  PHE B 266      18.730   1.503  -8.657  1.00  9.37           C  
ANISOU 5205  CB  PHE B 266     1228   1175   1158    161     15    -20       C  
ATOM   5206  CG  PHE B 266      19.728   2.606  -8.375  1.00  8.74           C  
ANISOU 5206  CG  PHE B 266     1052   1174   1097    229    109     -9       C  
ATOM   5207  CD1 PHE B 266      20.890   2.352  -7.654  1.00  9.30           C  
ANISOU 5207  CD1 PHE B 266     1038   1394   1102    103     62     69       C  
ATOM   5208  CD2 PHE B 266      19.464   3.922  -8.809  1.00  9.43           C  
ANISOU 5208  CD2 PHE B 266     1249   1295   1041     69     17     75       C  
ATOM   5209  CE1 PHE B 266      21.778   3.365  -7.370  1.00  9.75           C  
ANISOU 5209  CE1 PHE B 266     1144   1370   1191    178      3     95       C  
ATOM   5210  CE2 PHE B 266      20.351   4.928  -8.525  1.00 10.07           C  
ANISOU 5210  CE2 PHE B 266     1151   1378   1298     79     93    106       C  
ATOM   5211  CZ  PHE B 266      21.521   4.666  -7.797  1.00  9.87           C  
ANISOU 5211  CZ  PHE B 266     1328   1235   1188     91     11    -34       C  
ATOM   5212  N   GLU B 267      15.533   0.387  -8.123  1.00  8.82           N  
ANISOU 5212  N   GLU B 267     1104   1151   1098    125     21    -25       N  
ATOM   5213  CA  GLU B 267      14.619  -0.617  -8.671  1.00  9.16           C  
ANISOU 5213  CA  GLU B 267     1071   1324   1084     62    -24    108       C  
ATOM   5214  C   GLU B 267      14.559  -0.375 -10.176  1.00  8.66           C  
ANISOU 5214  C   GLU B 267     1116   1078   1096    163     72     75       C  
ATOM   5215  O   GLU B 267      14.135   0.703 -10.612  1.00  9.16           O  
ANISOU 5215  O   GLU B 267     1266   1126   1090    260     33    -22       O  
ATOM   5216  CB  GLU B 267      13.236  -0.611  -8.015  1.00  9.77           C  
ANISOU 5216  CB  GLU B 267     1285   1335   1094    125    100    115       C  
ATOM   5217  CG  GLU B 267      12.453  -1.880  -8.204  1.00 10.56           C  
ANISOU 5217  CG  GLU B 267     1342   1360   1310    105    115     34       C  
ATOM   5218  CD  GLU B 267      11.762  -2.124  -9.531  1.00 10.44           C  
ANISOU 5218  CD  GLU B 267     1177   1416   1372     31    153     10       C  
ATOM   5219  OE1 GLU B 267      11.907  -1.331 -10.461  1.00 11.40           O  
ANISOU 5219  OE1 GLU B 267     1372   1630   1328    -35     60     46       O  
ATOM   5220  OE2 GLU B 267      11.014  -3.154  -9.589  1.00 11.97           O  
ANISOU 5220  OE2 GLU B 267     1417   1497   1633    -77     60     45       O  
ATOM   5221  N   VAL B 268      15.043  -1.343 -10.970  1.00  8.78           N  
ANISOU 5221  N   VAL B 268     1189   1067   1081    164     45      0       N  
ATOM   5222  CA  VAL B 268      15.161  -1.204 -12.424  1.00  9.22           C  
ANISOU 5222  CA  VAL B 268     1128   1215   1159     46     73      1       C  
ATOM   5223  C   VAL B 268      14.526  -2.405 -13.133  1.00  9.95           C  
ANISOU 5223  C   VAL B 268     1259   1305   1216     89     14    -39       C  
ATOM   5224  O   VAL B 268      15.067  -2.975 -14.109  1.00 10.52           O  
ANISOU 5224  O   VAL B 268     1265   1503   1230     29     51   -107       O  
ATOM   5225  CB  VAL B 268      16.624  -0.938 -12.879  1.00  9.53           C  
ANISOU 5225  CB  VAL B 268     1208   1261   1150     59    132     22       C  
ATOM   5226  CG1 VAL B 268      16.618  -0.188 -14.205  1.00 10.28           C  
ANISOU 5226  CG1 VAL B 268     1187   1465   1254    127    253    106       C  
ATOM   5227  CG2 VAL B 268      17.451  -0.208 -11.834  1.00 10.73           C  
ANISOU 5227  CG2 VAL B 268     1494   1395   1189     81     29    -23       C  
ATOM   5228  N   ILE B 269      13.334  -2.802 -12.628  1.00  9.93           N  
ANISOU 5228  N   ILE B 269     1212   1401   1161     74     80   -101       N  
ATOM   5229  CA  ILE B 269      12.593  -3.984 -13.098  1.00 10.75           C  
ANISOU 5229  CA  ILE B 269     1479   1391   1216     64     90    -87       C  
ATOM   5230  C   ILE B 269      11.165  -3.597 -13.509  1.00 11.22           C  
ANISOU 5230  C   ILE B 269     1517   1545   1202     -8      0     39       C  
ATOM   5231  O   ILE B 269      10.808  -3.672 -14.688  1.00 12.01           O  
ANISOU 5231  O   ILE B 269     1612   1632   1319    -31    -91    -66       O  
ATOM   5232  CB  ILE B 269      12.559  -5.121 -12.035  1.00 10.80           C  
ANISOU 5232  CB  ILE B 269     1265   1481   1357      1     32     18       C  
ATOM   5233  CG1 ILE B 269      13.948  -5.531 -11.573  1.00 11.19           C  
ANISOU 5233  CG1 ILE B 269     1318   1440   1492    113     85     49       C  
ATOM   5234  CG2 ILE B 269      11.764  -6.302 -12.594  1.00 12.52           C  
ANISOU 5234  CG2 ILE B 269     1591   1442   1723    -20     48    -41       C  
ATOM   5235  CD1 ILE B 269      13.924  -6.254 -10.238  1.00 12.15           C  
ANISOU 5235  CD1 ILE B 269     1521   1610   1485     71    -54      3       C  
ATOM   5236  N   GLY B 270      10.400  -3.138 -12.499  1.00 11.74           N  
ANISOU 5236  N   GLY B 270     1372   1738   1352     92     29     51       N  
ATOM   5237  CA  GLY B 270       8.973  -2.852 -12.678  1.00 12.88           C  
ANISOU 5237  CA  GLY B 270     1345   2086   1463     79    -76     45       C  
ATOM   5238  C   GLY B 270       8.054  -3.749 -11.875  1.00 13.14           C  
ANISOU 5238  C   GLY B 270     1484   2124   1386    152     18    -34       C  
ATOM   5239  O   GLY B 270       7.019  -4.212 -12.417  1.00 16.75           O  
ANISOU 5239  O   GLY B 270     1725   2925   1714   -229   -116    149       O  
ATOM   5240  N   ARG B 271       8.379  -4.072 -10.627  1.00 11.84           N  
ANISOU 5240  N   ARG B 271     1344   1778   1377    -12     42    -41       N  
ATOM   5241  CA  ARG B 271       7.525  -4.892  -9.788  1.00 12.72           C  
ANISOU 5241  CA  ARG B 271     1561   1810   1463    -25    215    -80       C  
ATOM   5242  C   ARG B 271       7.298  -4.162  -8.458  1.00 12.10           C  
ANISOU 5242  C   ARG B 271     1373   1725   1500   -237    126    -33       C  
ATOM   5243  O   ARG B 271       8.228  -3.610  -7.865  1.00 11.91           O  
ANISOU 5243  O   ARG B 271     1459   1637   1428   -161     60    -62       O  
ATOM   5244  CB  ARG B 271       8.122  -6.282  -9.499  1.00 15.30           C  
ANISOU 5244  CB  ARG B 271     2072   1776   1967    106    147   -181       C  
ATOM   5245  CG AARG B 271       8.381  -7.189 -10.681  0.75 15.61           C  
ANISOU 5245  CG AARG B 271     2209   1801   1921    149    268   -171       C  
ATOM   5246  CD AARG B 271       9.084  -8.468 -10.205  0.75 17.53           C  
ANISOU 5246  CD AARG B 271     2507   1913   2241    324    183   -152       C  
ATOM   5247  NE AARG B 271       8.288  -9.206  -9.252  0.75 19.31           N  
ANISOU 5247  NE AARG B 271     2745   2090   2502    320    338    -80       N  
ATOM   5248  CZ AARG B 271       7.360 -10.102  -9.530  0.75 23.11           C  
ANISOU 5248  CZ AARG B 271     3084   2755   2940    -66    196    -68       C  
ATOM   5249  NH1AARG B 271       7.051 -10.428 -10.779  0.75 24.50           N  
ANISOU 5249  NH1AARG B 271     3241   3020   3047   -179    202   -293       N  
ATOM   5250  NH2AARG B 271       6.726 -10.668  -8.520  0.75 25.96           N  
ANISOU 5250  NH2AARG B 271     3536   3145   3183    -72    457     89       N  
ATOM   5251  CG BARG B 271       7.823  -7.183 -10.704  0.25 20.39           C  
ANISOU 5251  CG BARG B 271     2993   2463   2291   -249    -67   -302       C  
ATOM   5252  CD BARG B 271       8.877  -8.193 -11.080  0.25 26.04           C  
ANISOU 5252  CD BARG B 271     3315   3074   3506    158     30   -161       C  
ATOM   5253  NE BARG B 271       9.098  -8.283 -12.513  0.25 30.30           N  
ANISOU 5253  NE BARG B 271     4097   3786   3631    149    170    -39       N  
ATOM   5254  CZ BARG B 271       8.366  -8.642 -13.548  0.25 32.80           C  
ANISOU 5254  CZ BARG B 271     4346   4122   3993    127    -87    -74       C  
ATOM   5255  NH1BARG B 271       7.114  -9.050 -13.418  0.25 33.24           N  
ANISOU 5255  NH1BARG B 271     4413   4217   3999     68    -22    -53       N  
ATOM   5256  NH2BARG B 271       8.905  -8.598 -14.768  0.25 33.26           N  
ANISOU 5256  NH2BARG B 271     4461   4208   3967    137   -115    -11       N  
ATOM   5257  N   LEU B 272       6.053  -4.251  -7.957  1.00 12.36           N  
ANISOU 5257  N   LEU B 272     1443   1686   1569   -122    223    -42       N  
ATOM   5258  CA  LEU B 272       5.743  -3.615  -6.676  1.00 12.38           C  
ANISOU 5258  CA  LEU B 272     1366   1752   1585    -58    147    -90       C  
ATOM   5259  C   LEU B 272       6.598  -4.193  -5.547  1.00 12.26           C  
ANISOU 5259  C   LEU B 272     1546   1653   1460    -83    200    -28       C  
ATOM   5260  O   LEU B 272       7.105  -3.469  -4.679  1.00 14.28           O  
ANISOU 5260  O   LEU B 272     1958   1825   1645   -180     54    -67       O  
ATOM   5261  CB  LEU B 272       4.238  -3.752  -6.390  1.00 14.20           C  
ANISOU 5261  CB  LEU B 272     1475   2000   1923     21    280    -82       C  
ATOM   5262  CG  LEU B 272       3.299  -3.120  -7.420  1.00 15.88           C  
ANISOU 5262  CG  LEU B 272     1815   2299   1922    123    214     30       C  
ATOM   5263  CD1 LEU B 272       1.856  -3.422  -7.002  1.00 18.96           C  
ANISOU 5263  CD1 LEU B 272     1756   2970   2478    208    179    268       C  
ATOM   5264  CD2 LEU B 272       3.536  -1.633  -7.612  1.00 16.30           C  
ANISOU 5264  CD2 LEU B 272     1921   2325   1947    188    138     38       C  
ATOM   5265  N   ASP B 273       6.764  -5.528  -5.521  1.00 12.94           N  
ANISOU 5265  N   ASP B 273     1734   1711   1474   -196    181     34       N  
ATOM   5266  CA  ASP B 273       7.500  -6.167  -4.432  1.00 13.99           C  
ANISOU 5266  CA  ASP B 273     1853   1860   1604   -297     65    194       C  
ATOM   5267  C   ASP B 273       8.968  -5.760  -4.396  1.00 13.35           C  
ANISOU 5267  C   ASP B 273     1738   1793   1540   -202     30    123       C  
ATOM   5268  O   ASP B 273       9.497  -5.500  -3.288  1.00 14.66           O  
ANISOU 5268  O   ASP B 273     2080   2014   1475   -377     21    236       O  
ATOM   5269  CB  ASP B 273       7.345  -7.694  -4.408  1.00 16.17           C  
ANISOU 5269  CB  ASP B 273     2429   1882   1832   -204      9    137       C  
ATOM   5270  CG AASP B 273       7.721  -8.429  -5.662  0.50 17.34           C  
ANISOU 5270  CG AASP B 273     2581   2082   1925   -285   -175    -48       C  
ATOM   5271  OD1AASP B 273       8.153  -7.828  -6.671  0.50 17.36           O  
ANISOU 5271  OD1AASP B 273     2547   1958   2091   -394   -109    -36       O  
ATOM   5272  OD2AASP B 273       7.582  -9.686  -5.635  0.50 21.16           O  
ANISOU 5272  OD2AASP B 273     3244   2146   2649   -322   -214    120       O  
ATOM   5273  CG BASP B 273       7.986  -8.396  -5.581  0.50 15.21           C  
ANISOU 5273  CG BASP B 273     2257   1597   1926   -240    -78     79       C  
ATOM   5274  OD1BASP B 273       7.391  -8.456  -6.678  0.50 18.41           O  
ANISOU 5274  OD1BASP B 273     2741   2350   1905    -72   -143     40       O  
ATOM   5275  OD2BASP B 273       9.104  -8.944  -5.430  0.50 16.54           O  
ANISOU 5275  OD2BASP B 273     2247   2016   2023    -56    112     63       O  
ATOM   5276  N   THR B 274       9.627  -5.662  -5.549  1.00 12.00           N  
ANISOU 5276  N   THR B 274     1596   1560   1404   -129    -48     29       N  
ATOM   5277  CA  THR B 274      11.027  -5.246  -5.587  1.00 12.05           C  
ANISOU 5277  CA  THR B 274     1647   1416   1518    -42    -15    -11       C  
ATOM   5278  C   THR B 274      11.158  -3.753  -5.299  1.00 10.94           C  
ANISOU 5278  C   THR B 274     1481   1415   1262     59     40     38       C  
ATOM   5279  O   THR B 274      12.234  -3.371  -4.801  1.00 11.79           O  
ANISOU 5279  O   THR B 274     1437   1524   1518     95    -27    -34       O  
ATOM   5280  CB  THR B 274      11.697  -5.711  -6.888  1.00 12.86           C  
ANISOU 5280  CB  THR B 274     1847   1451   1588     23     84    -12       C  
ATOM   5281  OG1 THR B 274      10.880  -5.411  -8.017  1.00 12.90           O  
ANISOU 5281  OG1 THR B 274     1581   1713   1606     45     88   -186       O  
ATOM   5282  CG2 THR B 274      11.979  -7.213  -6.877  1.00 14.75           C  
ANISOU 5282  CG2 THR B 274     2197   1470   1937     36    344   -155       C  
ATOM   5283  N   MET B 275      10.141  -2.929  -5.558  1.00 10.57           N  
ANISOU 5283  N   MET B 275     1277   1469   1268     17     78     46       N  
ATOM   5284  CA  MET B 275      10.215  -1.538  -5.116  1.00 10.67           C  
ANISOU 5284  CA  MET B 275     1269   1503   1283    112    170    -18       C  
ATOM   5285  C   MET B 275      10.316  -1.452  -3.585  1.00 10.64           C  
ANISOU 5285  C   MET B 275     1261   1416   1367     17    165     23       C  
ATOM   5286  O   MET B 275      11.135  -0.688  -3.027  1.00 11.13           O  
ANISOU 5286  O   MET B 275     1383   1464   1382    -37    152     44       O  
ATOM   5287  CB  MET B 275       9.017  -0.736  -5.654  1.00 11.34           C  
ANISOU 5287  CB  MET B 275     1352   1542   1417     60    204     74       C  
ATOM   5288  CG  MET B 275       9.136  -0.592  -7.184  1.00 10.89           C  
ANISOU 5288  CG  MET B 275     1294   1488   1357    -38     49    -21       C  
ATOM   5289  SD  MET B 275       7.586   0.105  -7.889  1.00 12.17           S  
ANISOU 5289  SD  MET B 275     1413   1658   1552    121    -71     76       S  
ATOM   5290  CE  MET B 275       8.013  -0.175  -9.636  1.00 14.29           C  
ANISOU 5290  CE  MET B 275     1984   2002   1444   -200   -224     32       C  
ATOM   5291  N   VAL B 276       9.482  -2.203  -2.860  1.00 10.71           N  
ANISOU 5291  N   VAL B 276     1355   1486   1228     73    150     99       N  
ATOM   5292  CA  VAL B 276       9.536  -2.178  -1.383  1.00 12.07           C  
ANISOU 5292  CA  VAL B 276     1566   1785   1236    139    251     88       C  
ATOM   5293  C   VAL B 276      10.802  -2.845  -0.838  1.00 11.84           C  
ANISOU 5293  C   VAL B 276     1494   1658   1345    -69    144    146       C  
ATOM   5294  O   VAL B 276      11.432  -2.298   0.076  1.00 12.24           O  
ANISOU 5294  O   VAL B 276     1578   1730   1341     95     28    141       O  
ATOM   5295  CB  VAL B 276       8.257  -2.789  -0.784  1.00 14.25           C  
ANISOU 5295  CB  VAL B 276     1605   2351   1458     26    232    271       C  
ATOM   5296  CG1 VAL B 276       8.300  -2.758   0.748  1.00 17.85           C  
ANISOU 5296  CG1 VAL B 276     1927   3336   1520     -6    288    345       C  
ATOM   5297  CG2 VAL B 276       7.008  -2.072  -1.269  1.00 15.23           C  
ANISOU 5297  CG2 VAL B 276     1602   2608   1576     61     92     -6       C  
ATOM   5298  N   THR B 277      11.252  -3.952  -1.460  1.00 11.45           N  
ANISOU 5298  N   THR B 277     1491   1452   1406    -33     54    224       N  
ATOM   5299  CA  THR B 277      12.508  -4.597  -1.080  1.00 11.98           C  
ANISOU 5299  CA  THR B 277     1494   1431   1625   -108    -61     43       C  
ATOM   5300  C   THR B 277      13.689  -3.667  -1.242  1.00 10.27           C  
ANISOU 5300  C   THR B 277     1345   1154   1403    160     56      7       C  
ATOM   5301  O   THR B 277      14.603  -3.535  -0.393  1.00 10.62           O  
ANISOU 5301  O   THR B 277     1495   1162   1377    160     43     38       O  
ATOM   5302  CB  THR B 277      12.715  -5.891  -1.964  1.00 13.46           C  
ANISOU 5302  CB  THR B 277     1688   1219   2208     28    -33    -19       C  
ATOM   5303  OG1 THR B 277      11.721  -6.842  -1.510  1.00 17.14           O  
ANISOU 5303  OG1 THR B 277     2555   1725   2230   -258    320    120       O  
ATOM   5304  CG2 THR B 277      14.101  -6.485  -1.831  1.00 16.16           C  
ANISOU 5304  CG2 THR B 277     1982   1855   2304    248   -180   -102       C  
ATOM   5305  N   ALA B 278      13.747  -2.950  -2.401  1.00 10.03           N  
ANISOU 5305  N   ALA B 278     1250   1202   1360    105    105    124       N  
ATOM   5306  CA  ALA B 278      14.830  -2.026  -2.659  1.00  9.76           C  
ANISOU 5306  CA  ALA B 278     1305   1163   1239    102     59     14       C  
ATOM   5307  C   ALA B 278      14.853  -0.899  -1.620  1.00  9.35           C  
ANISOU 5307  C   ALA B 278     1171   1183   1199     60     96    122       C  
ATOM   5308  O   ALA B 278      15.927  -0.483  -1.164  1.00  9.82           O  
ANISOU 5308  O   ALA B 278     1309   1230   1193    116     39     37       O  
ATOM   5309  CB  ALA B 278      14.802  -1.485  -4.092  1.00 10.88           C  
ANISOU 5309  CB  ALA B 278     1387   1437   1309    151     79     55       C  
ATOM   5310  N   LEU B 279      13.692  -0.356  -1.258  1.00  9.44           N  
ANISOU 5310  N   LEU B 279     1367    987   1232    258     -6    110       N  
ATOM   5311  CA  LEU B 279      13.664   0.668  -0.200  1.00  9.81           C  
ANISOU 5311  CA  LEU B 279     1442   1029   1257    120     13     78       C  
ATOM   5312  C   LEU B 279      14.211   0.091   1.122  1.00  9.69           C  
ANISOU 5312  C   LEU B 279     1324   1195   1163     56     90     92       C  
ATOM   5313  O   LEU B 279      15.021   0.720   1.788  1.00 10.00           O  
ANISOU 5313  O   LEU B 279     1460   1128   1213    186     28     38       O  
ATOM   5314  CB  LEU B 279      12.237   1.192  -0.008  1.00 10.39           C  
ANISOU 5314  CB  LEU B 279     1493   1273   1181     91    122    138       C  
ATOM   5315  CG  LEU B 279      12.055   2.191   1.142  1.00 10.58           C  
ANISOU 5315  CG  LEU B 279     1543   1349   1129    293    116    279       C  
ATOM   5316  CD1 LEU B 279      12.823   3.491   0.895  1.00 10.56           C  
ANISOU 5316  CD1 LEU B 279     1393   1413   1206    281     62    207       C  
ATOM   5317  CD2 LEU B 279      10.578   2.484   1.346  1.00 12.26           C  
ANISOU 5317  CD2 LEU B 279     1578   1665   1414    372    122    109       C  
ATOM   5318  N   SER B 280      13.701  -1.091   1.486  1.00 10.47           N  
ANISOU 5318  N   SER B 280     1462   1239   1276     76     -5    201       N  
ATOM   5319  CA  SER B 280      14.066  -1.677   2.781  1.00 11.56           C  
ANISOU 5319  CA  SER B 280     1535   1521   1335    167     15    243       C  
ATOM   5320  C   SER B 280      15.556  -1.937   2.922  1.00 10.36           C  
ANISOU 5320  C   SER B 280     1491   1299   1147    141    -10    140       C  
ATOM   5321  O   SER B 280      16.086  -1.852   4.035  1.00 12.24           O  
ANISOU 5321  O   SER B 280     1676   1662   1314    295   -120     53       O  
ATOM   5322  CB ASER B 280      13.236  -2.957   2.976  0.59 11.57           C  
ANISOU 5322  CB ASER B 280     1627   1581   1187    153    114    520       C  
ATOM   5323  OG ASER B 280      11.834  -2.731   2.916  0.59 13.30           O  
ANISOU 5323  OG ASER B 280     1642   1666   1746    151    187     96       O  
ATOM   5324  CB BSER B 280      13.312  -3.005   2.968  0.41 13.71           C  
ANISOU 5324  CB BSER B 280     1794   1700   1713    -33    144    392       C  
ATOM   5325  OG BSER B 280      13.592  -3.495   4.270  0.41 15.63           O  
ANISOU 5325  OG BSER B 280     2406   1747   1786   -216     33    371       O  
ATOM   5326  N   CYS B 281      16.252  -2.318   1.839  1.00 10.47           N  
ANISOU 5326  N   CYS B 281     1437   1333   1208    308     23    101       N  
ATOM   5327  CA  CYS B 281      17.675  -2.684   1.924  1.00 10.05           C  
ANISOU 5327  CA  CYS B 281     1347   1191   1281    215    -51    108       C  
ATOM   5328  C   CYS B 281      18.621  -1.502   2.033  1.00 10.04           C  
ANISOU 5328  C   CYS B 281     1312   1254   1249    195    -40     20       C  
ATOM   5329  O   CYS B 281      19.822  -1.712   2.301  1.00 11.31           O  
ANISOU 5329  O   CYS B 281     1499   1293   1507    327   -125     65       O  
ATOM   5330  CB  CYS B 281      18.081  -3.579   0.745  1.00 11.80           C  
ANISOU 5330  CB  CYS B 281     1581   1214   1691    151     33   -127       C  
ATOM   5331  SG  CYS B 281      18.496  -2.738  -0.818  1.00 11.12           S  
ANISOU 5331  SG  CYS B 281     1504   1413   1310    309    -36   -132       S  
ATOM   5332  N   CYS B 282      18.125  -0.256   1.831  1.00 10.39           N  
ANISOU 5332  N   CYS B 282     1529   1108   1312    271   -119    -64       N  
ATOM   5333  C   CYS B 282      19.024   1.211   3.578  1.00  9.93           C  
ANISOU 5333  C   CYS B 282     1320   1092   1361    141     21     52       C  
ATOM   5334  O   CYS B 282      18.071   0.897   4.307  1.00 10.79           O  
ANISOU 5334  O   CYS B 282     1381   1256   1463    184     43    -90       O  
ATOM   5335  CA ACYS B 282      19.032   0.888   2.046  0.78 10.20           C  
ANISOU 5335  CA ACYS B 282     1524   1006   1347    204   -198    -17       C  
ATOM   5336  CB ACYS B 282      18.731   2.069   1.102  0.78 10.71           C  
ANISOU 5336  CB ACYS B 282     1417   1137   1514    381    -67     34       C  
ATOM   5337  SG ACYS B 282      17.271   3.137   1.481  0.78  9.30           S  
ANISOU 5337  SG ACYS B 282     1299   1124   1111    284    -50     96       S  
ATOM   5338  CA BCYS B 282      18.923   0.918   2.100  0.22 10.73           C  
ANISOU 5338  CA BCYS B 282     1479   1221   1376    118   -119     14       C  
ATOM   5339  CB BCYS B 282      18.152   2.206   1.714  0.22 10.55           C  
ANISOU 5339  CB BCYS B 282     1363   1311   1334    208    -36    -93       C  
ATOM   5340  SG BCYS B 282      18.056   2.140  -0.066  0.22 10.57           S  
ANISOU 5340  SG BCYS B 282     1549   1187   1279     56    -95    169       S  
ATOM   5341  N   GLN B 283      20.148   1.804   4.008  1.00  9.76           N  
ANISOU 5341  N   GLN B 283     1289   1179   1241    156    -11    -51       N  
ATOM   5342  CA  GLN B 283      20.364   2.053   5.459  1.00  9.66           C  
ANISOU 5342  CA  GLN B 283     1376   1095   1198    224     14    -30       C  
ATOM   5343  C   GLN B 283      19.230   2.903   6.020  1.00  8.74           C  
ANISOU 5343  C   GLN B 283     1227    992   1101    188      9    110       C  
ATOM   5344  O   GLN B 283      18.837   3.915   5.416  1.00  9.55           O  
ANISOU 5344  O   GLN B 283     1474   1105   1051    248    -96     80       O  
ATOM   5345  CB  GLN B 283      21.749   2.623   5.652  1.00 10.16           C  
ANISOU 5345  CB  GLN B 283     1339   1299   1223    218     67   -113       C  
ATOM   5346  CG  GLN B 283      22.356   2.437   7.057  1.00 10.83           C  
ANISOU 5346  CG  GLN B 283     1452   1370   1292    201      9     47       C  
ATOM   5347  CD  GLN B 283      21.699   3.309   8.099  1.00 10.49           C  
ANISOU 5347  CD  GLN B 283     1537   1145   1304    118    -39     92       C  
ATOM   5348  OE1 GLN B 283      21.307   4.441   7.797  1.00 10.80           O  
ANISOU 5348  OE1 GLN B 283     1528   1271   1304    282     38    -27       O  
ATOM   5349  NE2 GLN B 283      21.597   2.844   9.368  1.00 11.92           N  
ANISOU 5349  NE2 GLN B 283     1740   1401   1388    141    -31     30       N  
ATOM   5350  N   GLU B 284      18.710   2.532   7.204  1.00  8.86           N  
ANISOU 5350  N   GLU B 284     1289   1082    996    235    -44    189       N  
ATOM   5351  CA  GLU B 284      17.471   3.131   7.683  1.00  8.76           C  
ANISOU 5351  CA  GLU B 284     1128   1139   1061    126   -106     43       C  
ATOM   5352  C   GLU B 284      17.539   4.609   8.028  1.00  9.04           C  
ANISOU 5352  C   GLU B 284     1218   1244    972    131    -20     73       C  
ATOM   5353  O   GLU B 284      16.470   5.261   8.042  1.00  9.55           O  
ANISOU 5353  O   GLU B 284     1227   1255   1148    254    -44     60       O  
ATOM   5354  CB  GLU B 284      16.926   2.324   8.897  1.00  9.49           C  
ANISOU 5354  CB  GLU B 284     1325   1184   1097    160   -144    113       C  
ATOM   5355  CG  GLU B 284      17.838   2.402  10.101  1.00 10.25           C  
ANISOU 5355  CG  GLU B 284     1508   1296   1090     80    -88    160       C  
ATOM   5356  CD  GLU B 284      17.432   1.593  11.314  1.00 11.08           C  
ANISOU 5356  CD  GLU B 284     1662   1329   1221   -127   -144    126       C  
ATOM   5357  OE1 GLU B 284      16.341   0.973  11.311  1.00 15.71           O  
ANISOU 5357  OE1 GLU B 284     2087   2385   1497   -633   -243    336       O  
ATOM   5358  OE2 GLU B 284      18.217   1.575  12.284  1.00 11.77           O  
ANISOU 5358  OE2 GLU B 284     1913   1364   1197   -105    -29    246       O  
ATOM   5359  N   ALA B 285      18.715   5.125   8.371  1.00  8.93           N  
ANISOU 5359  N   ALA B 285     1257    989   1147     74     19     56       N  
ATOM   5360  CA  ALA B 285      18.867   6.513   8.789  1.00  9.01           C  
ANISOU 5360  CA  ALA B 285     1385    912   1128    164    -51     16       C  
ATOM   5361  C   ALA B 285      19.267   7.449   7.650  1.00  9.30           C  
ANISOU 5361  C   ALA B 285     1475   1006   1051    122    -33     35       C  
ATOM   5362  O   ALA B 285      18.886   8.638   7.725  1.00 10.84           O  
ANISOU 5362  O   ALA B 285     1857   1150   1113    279    119    106       O  
ATOM   5363  CB  ALA B 285      19.983   6.582   9.858  1.00  9.58           C  
ANISOU 5363  CB  ALA B 285     1492   1078   1070    129      5     26       C  
ATOM   5364  N   TYR B 286      19.994   6.983   6.633  1.00  9.36           N  
ANISOU 5364  N   TYR B 286     1545   1103    910    143      7     67       N  
ATOM   5365  CA  TYR B 286      20.528   7.880   5.608  1.00  9.79           C  
ANISOU 5365  CA  TYR B 286     1485   1272    963    157    143    105       C  
ATOM   5366  C   TYR B 286      20.504   7.277   4.199  1.00  9.55           C  
ANISOU 5366  C   TYR B 286     1404   1141   1082    112     39    199       C  
ATOM   5367  O   TYR B 286      20.987   7.951   3.253  1.00 10.82           O  
ANISOU 5367  O   TYR B 286     1697   1280   1134    154    130    187       O  
ATOM   5368  CB  TYR B 286      21.939   8.334   5.993  1.00 10.69           C  
ANISOU 5368  CB  TYR B 286     1673   1310   1079     88     94     39       C  
ATOM   5369  CG  TYR B 286      22.951   7.239   6.222  1.00 10.49           C  
ANISOU 5369  CG  TYR B 286     1529   1409   1047     85    -11    128       C  
ATOM   5370  CD1 TYR B 286      23.439   6.478   5.170  1.00 11.07           C  
ANISOU 5370  CD1 TYR B 286     1483   1669   1055     83     34     77       C  
ATOM   5371  CD2 TYR B 286      23.432   6.938   7.506  1.00 10.74           C  
ANISOU 5371  CD2 TYR B 286     1438   1550   1093     79    -28     36       C  
ATOM   5372  CE1 TYR B 286      24.349   5.444   5.360  1.00 12.38           C  
ANISOU 5372  CE1 TYR B 286     1685   1748   1271    226    -26      1       C  
ATOM   5373  CE2 TYR B 286      24.355   5.934   7.698  1.00 11.71           C  
ANISOU 5373  CE2 TYR B 286     1474   1703   1272    100    -74    121       C  
ATOM   5374  CZ  TYR B 286      24.815   5.193   6.645  1.00 11.71           C  
ANISOU 5374  CZ  TYR B 286     1513   1541   1394    131   -124     80       C  
ATOM   5375  OH  TYR B 286      25.728   4.165   6.889  1.00 16.24           O  
ANISOU 5375  OH  TYR B 286     1947   2493   1731    686   -103    154       O  
ATOM   5376  N   GLY B 287      19.943   6.094   4.026  1.00  9.15           N  
ANISOU 5376  N   GLY B 287     1367   1069   1041    206    -69    117       N  
ATOM   5377  CA  GLY B 287      19.871   5.477   2.703  1.00  9.85           C  
ANISOU 5377  CA  GLY B 287     1420   1278   1044    332    -72     81       C  
ATOM   5378  C   GLY B 287      18.930   6.219   1.749  1.00  8.83           C  
ANISOU 5378  C   GLY B 287     1170   1077   1107    243     47    118       C  
ATOM   5379  O   GLY B 287      17.993   6.913   2.158  1.00  9.78           O  
ANISOU 5379  O   GLY B 287     1356   1294   1065    343    -47    -10       O  
ATOM   5380  N   VAL B 288      19.175   6.024   0.451  1.00  8.99           N  
ANISOU 5380  N   VAL B 288     1227   1201    989    361    -25    144       N  
ATOM   5381  CA  VAL B 288      18.380   6.591  -0.642  1.00  9.22           C  
ANISOU 5381  CA  VAL B 288     1199   1230   1072    281     -3    126       C  
ATOM   5382  C   VAL B 288      17.992   5.458  -1.602  1.00  9.26           C  
ANISOU 5382  C   VAL B 288     1272   1271    977    247    -16     22       C  
ATOM   5383  O   VAL B 288      18.891   4.686  -2.019  1.00 10.89           O  
ANISOU 5383  O   VAL B 288     1408   1443   1285    285    -10   -227       O  
ATOM   5384  CB  VAL B 288      19.169   7.674  -1.388  1.00 10.52           C  
ANISOU 5384  CB  VAL B 288     1586   1283   1130    182    -65    151       C  
ATOM   5385  CG1 VAL B 288      18.412   8.199  -2.624  1.00 12.77           C  
ANISOU 5385  CG1 VAL B 288     2095   1535   1221    136   -155    264       C  
ATOM   5386  CG2 VAL B 288      19.501   8.863  -0.477  1.00 11.37           C  
ANISOU 5386  CG2 VAL B 288     1657   1327   1336     70    -60     53       C  
ATOM   5387  N   SER B 289      16.738   5.365  -1.981  1.00  8.89           N  
ANISOU 5387  N   SER B 289     1290   1127    962    274    -48     40       N  
ATOM   5388  CA  SER B 289      16.255   4.388  -2.958  1.00  8.59           C  
ANISOU 5388  CA  SER B 289     1232    977   1053    302    -40    147       C  
ATOM   5389  C   SER B 289      15.543   5.106  -4.107  1.00  8.48           C  
ANISOU 5389  C   SER B 289     1189    982   1050    292     37     74       C  
ATOM   5390  O   SER B 289      14.675   5.964  -3.866  1.00  9.94           O  
ANISOU 5390  O   SER B 289     1483   1237   1056    500     26     60       O  
ATOM   5391  CB  SER B 289      15.351   3.351  -2.311  1.00  9.62           C  
ANISOU 5391  CB  SER B 289     1272   1282   1100    238     -3    181       C  
ATOM   5392  OG  SER B 289      15.031   2.304  -3.231  1.00 10.31           O  
ANISOU 5392  OG  SER B 289     1436   1203   1280    196    -11     69       O  
ATOM   5393  N   VAL B 290      15.879   4.741  -5.342  1.00  8.37           N  
ANISOU 5393  N   VAL B 290     1129   1125    926    286    -69     69       N  
ATOM   5394  CA  VAL B 290      15.305   5.335  -6.552  1.00  8.76           C  
ANISOU 5394  CA  VAL B 290     1042   1209   1079    273    -13    182       C  
ATOM   5395  C   VAL B 290      14.525   4.290  -7.350  1.00  8.70           C  
ANISOU 5395  C   VAL B 290     1211   1092   1001    236      5     50       C  
ATOM   5396  O   VAL B 290      15.070   3.246  -7.744  1.00  9.91           O  
ANISOU 5396  O   VAL B 290     1349   1188   1228    258     29     15       O  
ATOM   5397  CB  VAL B 290      16.398   5.967  -7.453  1.00 10.11           C  
ANISOU 5397  CB  VAL B 290     1441   1298   1102    196    129    135       C  
ATOM   5398  CG1 VAL B 290      15.767   6.592  -8.720  1.00 11.59           C  
ANISOU 5398  CG1 VAL B 290     1845   1435   1125    103     97    240       C  
ATOM   5399  CG2 VAL B 290      17.207   7.021  -6.713  1.00 10.95           C  
ANISOU 5399  CG2 VAL B 290     1381   1454   1326    102     69    103       C  
ATOM   5400  N   ILE B 291      13.237   4.584  -7.630  1.00  9.03           N  
ANISOU 5400  N   ILE B 291     1175   1250   1007    189     74    -28       N  
ATOM   5401  CA  ILE B 291      12.410   3.766  -8.530  1.00  9.41           C  
ANISOU 5401  CA  ILE B 291     1225   1361    988    216     16     72       C  
ATOM   5402  C   ILE B 291      12.603   4.233  -9.972  1.00  8.81           C  
ANISOU 5402  C   ILE B 291     1195   1246    906    202    -57      1       C  
ATOM   5403  O   ILE B 291      12.356   5.407 -10.293  1.00 10.15           O  
ANISOU 5403  O   ILE B 291     1472   1335   1050    323    -23     12       O  
ATOM   5404  CB  ILE B 291      10.907   3.839  -8.151  1.00  9.93           C  
ANISOU 5404  CB  ILE B 291     1234   1489   1049    255      6    167       C  
ATOM   5405  CG1 ILE B 291      10.634   3.503  -6.682  1.00 10.24           C  
ANISOU 5405  CG1 ILE B 291     1332   1504   1056    180    121    113       C  
ATOM   5406  CG2 ILE B 291      10.120   2.940  -9.102  1.00 11.88           C  
ANISOU 5406  CG2 ILE B 291     1566   1665   1284     85     91     17       C  
ATOM   5407  CD1 ILE B 291       9.179   3.554  -6.274  1.00 12.06           C  
ANISOU 5407  CD1 ILE B 291     1471   1929   1181    226    150     26       C  
ATOM   5408  N   VAL B 292      13.021   3.289 -10.824  1.00  9.16           N  
ANISOU 5408  N   VAL B 292     1346   1164    971    182     52     33       N  
ATOM   5409  CA  VAL B 292      13.146   3.502 -12.260  1.00  9.50           C  
ANISOU 5409  CA  VAL B 292     1251   1417    941    129    114     32       C  
ATOM   5410  C   VAL B 292      12.162   2.605 -13.014  1.00  9.36           C  
ANISOU 5410  C   VAL B 292     1237   1327    994    245    110      3       C  
ATOM   5411  O   VAL B 292      11.623   3.014 -14.079  1.00 10.61           O  
ANISOU 5411  O   VAL B 292     1424   1540   1066    225     31     -5       O  
ATOM   5412  CB  VAL B 292      14.609   3.229 -12.743  1.00 10.22           C  
ANISOU 5412  CB  VAL B 292     1351   1388   1146     66    180     25       C  
ATOM   5413  CG1 VAL B 292      14.766   3.582 -14.224  1.00 11.44           C  
ANISOU 5413  CG1 VAL B 292     1527   1560   1260    234    235    134       C  
ATOM   5414  CG2 VAL B 292      15.625   3.981 -11.887  1.00 11.43           C  
ANISOU 5414  CG2 VAL B 292     1368   1592   1384    -19    159    -12       C  
ATOM   5415  N   GLY B 293      11.923   1.362 -12.574  1.00  9.93           N  
ANISOU 5415  N   GLY B 293     1274   1335   1165    169    -17    -21       N  
ATOM   5416  CA  GLY B 293      11.039   0.461 -13.295  1.00 10.25           C  
ANISOU 5416  CA  GLY B 293     1330   1507   1056    144   -155     70       C  
ATOM   5417  C   GLY B 293       9.580   0.940 -13.348  1.00 11.51           C  
ANISOU 5417  C   GLY B 293     1369   1840   1166    226    -35    -71       C  
ATOM   5418  O   GLY B 293       9.079   1.612 -12.434  1.00 12.51           O  
ANISOU 5418  O   GLY B 293     1436   2065   1252    212    157    -48       O  
ATOM   5419  N   VAL B 294       8.880   0.490 -14.399  1.00 11.94           N  
ANISOU 5419  N   VAL B 294     1344   1865   1327    318   -105   -150       N  
ATOM   5420  CA  VAL B 294       7.459   0.826 -14.617  1.00 13.14           C  
ANISOU 5420  CA  VAL B 294     1316   2208   1467    269   -149    -92       C  
ATOM   5421  C   VAL B 294       6.636  -0.450 -14.278  1.00 14.26           C  
ANISOU 5421  C   VAL B 294     1401   2467   1552     55   -143    112       C  
ATOM   5422  O   VAL B 294       6.705  -1.468 -14.842  1.00 16.84           O  
ANISOU 5422  O   VAL B 294     1779   2345   2275    -27    -17    152       O  
ATOM   5423  CB  VAL B 294       7.249   1.143 -16.120  1.00 12.84           C  
ANISOU 5423  CB  VAL B 294     1347   2119   1413    161   -109    -49       C  
ATOM   5424  CG1 VAL B 294       5.771   1.264 -16.480  1.00 15.39           C  
ANISOU 5424  CG1 VAL B 294     1519   2585   1743    266   -195     51       C  
ATOM   5425  CG2 VAL B 294       8.011   2.398 -16.501  1.00 16.43           C  
ANISOU 5425  CG2 VAL B 294     1551   2240   2450    157    -85    254       C  
ATOM   5426  N  APRO B 295       5.778  -0.296 -13.204  0.64 16.92           N  
ANISOU 5426  N  APRO B 295     1689   2766   1974     98     -1    145       N  
ATOM   5427  CA APRO B 295       4.942  -1.438 -12.809  0.64 17.46           C  
ANISOU 5427  CA APRO B 295     1765   2958   1910     67    108    229       C  
ATOM   5428  C  APRO B 295       3.575  -1.349 -13.491  0.64 18.10           C  
ANISOU 5428  C  APRO B 295     1716   3038   2122    114    121    198       C  
ATOM   5429  O  APRO B 295       3.264  -0.439 -14.268  0.64 17.52           O  
ANISOU 5429  O  APRO B 295     1503   3303   1852    206    152    129       O  
ATOM   5430  CB APRO B 295       4.769  -1.284 -11.291  0.64 16.48           C  
ANISOU 5430  CB APRO B 295     1988   2335   1938    185    223    114       C  
ATOM   5431  CG APRO B 295       4.549   0.232 -11.210  0.64 15.86           C  
ANISOU 5431  CG APRO B 295     1987   2249   1791     38    192    121       C  
ATOM   5432  CD APRO B 295       5.506   0.829 -12.216  0.64 16.56           C  
ANISOU 5432  CD APRO B 295     1621   2572   2099    332    257    162       C  
ATOM   5433  N  BPRO B 295       5.690  -0.015 -13.322  0.36 17.17           N  
ANISOU 5433  N  BPRO B 295     1683   2834   2005    205     22     80       N  
ATOM   5434  CA BPRO B 295       4.790  -1.052 -12.778  0.36 18.66           C  
ANISOU 5434  CA BPRO B 295     1959   3040   2093     84    108    219       C  
ATOM   5435  C  BPRO B 295       3.483  -1.281 -13.496  0.36 18.71           C  
ANISOU 5435  C  BPRO B 295     1880   3014   2215    138    138    200       C  
ATOM   5436  O  BPRO B 295       3.064  -0.358 -14.213  0.36 17.85           O  
ANISOU 5436  O  BPRO B 295     1667   3180   1935    197    187    143       O  
ATOM   5437  CB BPRO B 295       4.469  -0.558 -11.341  0.36 18.49           C  
ANISOU 5437  CB BPRO B 295     2132   2713   2180    146     29    100       C  
ATOM   5438  CG BPRO B 295       4.382   0.937 -11.520  0.36 15.98           C  
ANISOU 5438  CG BPRO B 295     1724   2673   1675    284    258    -93       C  
ATOM   5439  CD BPRO B 295       5.396   1.298 -12.573  0.36 16.88           C  
ANISOU 5439  CD BPRO B 295     1850   3060   1504    224    165     -3       C  
ATOM   5440  N   PRO B 296       2.814  -2.416 -13.316  1.00 20.12           N  
ANISOU 5440  N   PRO B 296     1988   3324   2332    -62    251    199       N  
ATOM   5441  CA  PRO B 296       1.530  -2.616 -13.964  1.00 19.47           C  
ANISOU 5441  CA  PRO B 296     1940   3234   2223    114    292    -58       C  
ATOM   5442  C   PRO B 296       0.577  -1.478 -13.609  1.00 17.30           C  
ANISOU 5442  C   PRO B 296     1660   3065   1849    -38     25   -230       C  
ATOM   5443  O   PRO B 296       0.438  -0.995 -12.470  1.00 18.84           O  
ANISOU 5443  O   PRO B 296     1735   3673   1750     86    175   -195       O  
ATOM   5444  CB  PRO B 296       1.021  -3.995 -13.519  1.00 22.35           C  
ANISOU 5444  CB  PRO B 296     2522   3271   2700    -82    168     38       C  
ATOM   5445  CG  PRO B 296       2.315  -4.702 -13.135  1.00 24.34           C  
ANISOU 5445  CG  PRO B 296     2790   3458   3000     46    142    213       C  
ATOM   5446  CD  PRO B 296       3.206  -3.589 -12.566  1.00 23.27           C  
ANISOU 5446  CD  PRO B 296     2456   3490   2895    -17    133    348       C  
ATOM   5447  N   ASP B 297      -0.175  -1.089 -14.656  1.00 17.78           N  
ANISOU 5447  N   ASP B 297     1749   3126   1881     22    110    -49       N  
ATOM   5448  CA  ASP B 297      -1.130  -0.016 -14.555  1.00 18.25           C  
ANISOU 5448  CA  ASP B 297     1956   2983   1996     61    -20   -157       C  
ATOM   5449  C   ASP B 297      -2.148  -0.156 -13.425  1.00 18.71           C  
ANISOU 5449  C   ASP B 297     2143   2982   1984      8     25    -94       C  
ATOM   5450  O   ASP B 297      -2.700  -1.232 -13.201  1.00 18.41           O  
ANISOU 5450  O   ASP B 297     1828   3279   1886   -187    -35   -146       O  
ATOM   5451  CB  ASP B 297      -1.943   0.009 -15.867  1.00 19.94           C  
ANISOU 5451  CB  ASP B 297     2131   3432   2012     -8    -10     45       C  
ATOM   5452  CG  ASP B 297      -2.904   1.174 -15.898  1.00 21.91           C  
ANISOU 5452  CG  ASP B 297     2602   3519   2204    176    -15     78       C  
ATOM   5453  OD1 ASP B 297      -2.428   2.301 -16.131  1.00 23.21           O  
ANISOU 5453  OD1 ASP B 297     2878   3392   2550    403    107    238       O  
ATOM   5454  OD2 ASP B 297      -4.119   1.022 -15.659  1.00 25.19           O  
ANISOU 5454  OD2 ASP B 297     2543   4407   2621    304    -43    286       O  
ATOM   5455  N   SER B 298      -2.378   0.937 -12.717  1.00 21.29           N  
ANISOU 5455  N   SER B 298     2538   3236   2317    313    -24   -208       N  
ATOM   5456  CA  SER B 298      -3.388   1.084 -11.665  1.00 25.19           C  
ANISOU 5456  CA  SER B 298     3007   3929   2634    519    307   -192       C  
ATOM   5457  C   SER B 298      -3.251   0.171 -10.472  1.00 27.34           C  
ANISOU 5457  C   SER B 298     3286   4060   3042    430    216    100       C  
ATOM   5458  O   SER B 298      -4.247  -0.120  -9.780  1.00 32.01           O  
ANISOU 5458  O   SER B 298     3489   4987   3687    496    484    350       O  
ATOM   5459  CB  SER B 298      -4.776   0.946 -12.311  1.00 26.84           C  
ANISOU 5459  CB  SER B 298     2941   4233   3026    411    421   -103       C  
ATOM   5460  OG  SER B 298      -5.001   1.965 -13.271  1.00 29.01           O  
ANISOU 5460  OG  SER B 298     3044   4677   3300    803    383    122       O  
ATOM   5461  N   GLN B 299      -2.064  -0.316 -10.152  1.00 22.59           N  
ANISOU 5461  N   GLN B 299     2863   3457   2262    -54    180   -139       N  
ATOM   5462  CA  GLN B 299      -1.856  -1.180  -8.996  1.00 22.32           C  
ANISOU 5462  CA  GLN B 299     2774   3381   2327   -125     17   -153       C  
ATOM   5463  C   GLN B 299      -1.067  -0.446  -7.921  1.00 21.29           C  
ANISOU 5463  C   GLN B 299     2621   3209   2258   -201    102    -83       C  
ATOM   5464  O   GLN B 299      -0.058   0.190  -8.198  1.00 22.63           O  
ANISOU 5464  O   GLN B 299     2553   3853   2192   -387     81   -278       O  
ATOM   5465  CB AGLN B 299      -1.098  -2.448  -9.398  0.62 24.14           C  
ANISOU 5465  CB AGLN B 299     3035   3370   2767    -44     76    -70       C  
ATOM   5466  CG AGLN B 299      -1.893  -3.289 -10.400  0.62 27.19           C  
ANISOU 5466  CG AGLN B 299     3413   3837   3080   -269    -84   -164       C  
ATOM   5467  CD AGLN B 299      -1.331  -4.677 -10.574  0.62 30.32           C  
ANISOU 5467  CD AGLN B 299     3792   3927   3801   -154    150     62       C  
ATOM   5468  OE1AGLN B 299      -1.418  -5.286 -11.644  0.62 32.73           O  
ANISOU 5468  OE1AGLN B 299     4164   4251   4022   -302    142   -148       O  
ATOM   5469  NE2AGLN B 299      -0.734  -5.181  -9.509  0.62 30.99           N  
ANISOU 5469  NE2AGLN B 299     3848   4016   3911   -184    -45    -19       N  
ATOM   5470  CB BGLN B 299      -1.093  -2.443  -9.409  0.38 23.17           C  
ANISOU 5470  CB BGLN B 299     2928   3274   2600    -99     44   -105       C  
ATOM   5471  CG BGLN B 299      -1.706  -3.133 -10.624  0.38 24.56           C  
ANISOU 5471  CG BGLN B 299     3247   3362   2724    -26    -18   -252       C  
ATOM   5472  CD BGLN B 299      -3.130  -3.590 -10.383  0.38 25.54           C  
ANISOU 5472  CD BGLN B 299     3333   3470   2900    -45    120   -182       C  
ATOM   5473  OE1BGLN B 299      -3.307  -4.502  -9.571  0.38 26.25           O  
ANISOU 5473  OE1BGLN B 299     3478   3545   2952    -55     69   -125       O  
ATOM   5474  NE2BGLN B 299      -4.125  -3.007 -11.029  0.38 26.27           N  
ANISOU 5474  NE2BGLN B 299     3388   3661   2932    -27     90   -123       N  
ATOM   5475  N   ASN B 300      -1.545  -0.524  -6.690  1.00 20.42           N  
ANISOU 5475  N   ASN B 300     2510   3151   2098   -258    -12   -244       N  
ATOM   5476  CA  ASN B 300      -0.900   0.108  -5.542  1.00 18.78           C  
ANISOU 5476  CA  ASN B 300     2258   2777   2102   -161     -5   -159       C  
ATOM   5477  C   ASN B 300      -0.004  -0.880  -4.813  1.00 18.72           C  
ANISOU 5477  C   ASN B 300     2352   2499   2264   -131     91   -187       C  
ATOM   5478  O   ASN B 300      -0.294  -2.080  -4.764  1.00 21.38           O  
ANISOU 5478  O   ASN B 300     2762   2561   2801   -229     -9   -206       O  
ATOM   5479  CB  ASN B 300      -1.955   0.624  -4.559  1.00 20.60           C  
ANISOU 5479  CB  ASN B 300     2476   3070   2281   -130    189   -159       C  
ATOM   5480  CG  ASN B 300      -2.590   1.953  -4.854  1.00 23.35           C  
ANISOU 5480  CG  ASN B 300     2727   3383   2762     11   -136    113       C  
ATOM   5481  OD1 ASN B 300      -3.214   2.571  -3.962  1.00 28.76           O  
ANISOU 5481  OD1 ASN B 300     3444   4089   3395    357     80   -185       O  
ATOM   5482  ND2 ASN B 300      -2.447   2.510  -6.031  1.00 20.29           N  
ANISOU 5482  ND2 ASN B 300     2168   2805   2735     76   -217     96       N  
ATOM   5483  N   LEU B 301       1.078  -0.374  -4.222  1.00 17.60           N  
ANISOU 5483  N   LEU B 301     2478   2250   1958   -133    -66    -91       N  
ATOM   5484  CA  LEU B 301       1.935  -1.147  -3.327  1.00 17.21           C  
ANISOU 5484  CA  LEU B 301     2485   2234   1818    -76    -52   -165       C  
ATOM   5485  C   LEU B 301       1.501  -0.882  -1.875  1.00 17.38           C  
ANISOU 5485  C   LEU B 301     2360   2376   1867     -7    -21    -90       C  
ATOM   5486  O   LEU B 301       0.796   0.081  -1.559  1.00 17.29           O  
ANISOU 5486  O   LEU B 301     2058   2593   1920    -23    154    -23       O  
ATOM   5487  CB  LEU B 301       3.422  -0.864  -3.495  1.00 16.87           C  
ANISOU 5487  CB  LEU B 301     2401   2282   1729    337     26    -37       C  
ATOM   5488  CG  LEU B 301       3.986   0.528  -3.292  1.00 16.43           C  
ANISOU 5488  CG  LEU B 301     2164   2379   1699    146     92     77       C  
ATOM   5489  CD1 LEU B 301       4.143   0.905  -1.813  1.00 15.59           C  
ANISOU 5489  CD1 LEU B 301     1888   2309   1726    103    264     22       C  
ATOM   5490  CD2 LEU B 301       5.341   0.701  -3.964  1.00 17.11           C  
ANISOU 5490  CD2 LEU B 301     2059   2595   1848    411     38    174       C  
ATOM   5491  N   SER B 302       1.903  -1.778  -0.981  1.00 18.90           N  
ANISOU 5491  N   SER B 302     3000   2291   1891    -22    -87   -139       N  
ATOM   5492  CA  SER B 302       1.670  -1.680   0.459  1.00 18.26           C  
ANISOU 5492  CA  SER B 302     2537   2483   1916    -97     81   -160       C  
ATOM   5493  C   SER B 302       3.027  -1.551   1.128  1.00 15.63           C  
ANISOU 5493  C   SER B 302     2343   1962   1633      5    223      9       C  
ATOM   5494  O   SER B 302       3.957  -2.333   0.863  1.00 17.12           O  
ANISOU 5494  O   SER B 302     2578   1979   1947     81    258   -193       O  
ATOM   5495  CB  SER B 302       0.965  -2.948   0.968  1.00 21.12           C  
ANISOU 5495  CB  SER B 302     2882   2824   2317   -396    130      4       C  
ATOM   5496  OG  SER B 302       0.918  -3.004   2.389  1.00 24.60           O  
ANISOU 5496  OG  SER B 302     3508   3330   2509   -691     89    -29       O  
ATOM   5497  N   MET B 303       3.210  -0.624   2.083  1.00 14.23           N  
ANISOU 5497  N   MET B 303     2010   1744   1652    -43    331    112       N  
ATOM   5498  CA  MET B 303       4.464  -0.462   2.790  1.00 13.77           C  
ANISOU 5498  CA  MET B 303     1958   1633   1640     23    300     44       C  
ATOM   5499  C   MET B 303       4.240   0.172   4.173  1.00 13.07           C  
ANISOU 5499  C   MET B 303     1850   1468   1650    -90    284     38       C  
ATOM   5500  O   MET B 303       3.229   0.848   4.400  1.00 14.35           O  
ANISOU 5500  O   MET B 303     1989   1862   1600     36    324    118       O  
ATOM   5501  CB  MET B 303       5.485   0.336   1.970  1.00 14.10           C  
ANISOU 5501  CB  MET B 303     1847   1841   1669     81    324    -76       C  
ATOM   5502  CG  MET B 303       5.119   1.761   1.633  1.00 14.30           C  
ANISOU 5502  CG  MET B 303     2056   1884   1496    136    274    -15       C  
ATOM   5503  SD  MET B 303       5.406   2.995   2.950  1.00 13.38           S  
ANISOU 5503  SD  MET B 303     1931   1433   1720     40    402    104       S  
ATOM   5504  CE  MET B 303       7.182   3.094   2.947  1.00 14.78           C  
ANISOU 5504  CE  MET B 303     2046   1765   1803    -44    333    -38       C  
ATOM   5505  N   ASN B 304       5.183  -0.064   5.074  1.00 13.47           N  
ANISOU 5505  N   ASN B 304     1903   1394   1820      4    255     19       N  
ATOM   5506  CA  ASN B 304       5.137   0.502   6.430  1.00 14.58           C  
ANISOU 5506  CA  ASN B 304     2233   1530   1777   -101    106     29       C  
ATOM   5507  C   ASN B 304       5.877   1.834   6.434  1.00 13.68           C  
ANISOU 5507  C   ASN B 304     1738   1604   1858      1    234     67       C  
ATOM   5508  O   ASN B 304       7.088   1.866   6.180  1.00 12.87           O  
ANISOU 5508  O   ASN B 304     1758   1523   1609     52    231    -28       O  
ATOM   5509  CB  ASN B 304       5.787  -0.497   7.410  1.00 16.15           C  
ANISOU 5509  CB  ASN B 304     2680   1634   1821   -162    117    158       C  
ATOM   5510  CG  ASN B 304       5.659  -0.070   8.868  1.00 17.60           C  
ANISOU 5510  CG  ASN B 304     2931   1934   1822   -197    177    120       C  
ATOM   5511  OD1 ASN B 304       5.637   1.113   9.193  1.00 17.82           O  
ANISOU 5511  OD1 ASN B 304     2938   2003   1830   -407    587     64       O  
ATOM   5512  ND2 ASN B 304       5.598  -1.031   9.800  1.00 20.40           N  
ANISOU 5512  ND2 ASN B 304     3313   2284   2153   -222     41    345       N  
ATOM   5513  N   PRO B 305       5.211   2.946   6.753  1.00 13.10           N  
ANISOU 5513  N   PRO B 305     1604   1503   1871    -50    452     72       N  
ATOM   5514  CA  PRO B 305       5.876   4.258   6.722  1.00 12.79           C  
ANISOU 5514  CA  PRO B 305     1732   1429   1698    -30    334    193       C  
ATOM   5515  C   PRO B 305       6.978   4.442   7.745  1.00 11.56           C  
ANISOU 5515  C   PRO B 305     1816   1026   1550      9    285    -55       C  
ATOM   5516  O   PRO B 305       7.778   5.387   7.621  1.00 11.95           O  
ANISOU 5516  O   PRO B 305     1572   1269   1699      7    330     37       O  
ATOM   5517  CB  PRO B 305       4.742   5.298   6.876  1.00 15.10           C  
ANISOU 5517  CB  PRO B 305     1915   1749   2074    232    295    122       C  
ATOM   5518  CG  PRO B 305       3.688   4.497   7.614  1.00 14.81           C  
ANISOU 5518  CG  PRO B 305     1859   1765   2004    145    251      9       C  
ATOM   5519  CD  PRO B 305       3.772   3.067   7.062  1.00 13.68           C  
ANISOU 5519  CD  PRO B 305     1523   1708   1965    -41    256     35       C  
ATOM   5520  N   MET B 306       7.127   3.552   8.751  1.00 12.94           N  
ANISOU 5520  N   MET B 306     1991   1442   1483      4    506     79       N  
ATOM   5521  CA  MET B 306       8.273   3.571   9.643  1.00 13.12           C  
ANISOU 5521  CA  MET B 306     2130   1427   1427    128    445     79       C  
ATOM   5522  C   MET B 306       9.583   3.389   8.860  1.00 11.50           C  
ANISOU 5522  C   MET B 306     1785   1212   1373     92    236    102       C  
ATOM   5523  O   MET B 306      10.632   3.861   9.307  1.00 12.15           O  
ANISOU 5523  O   MET B 306     1979   1402   1235    244     73    244       O  
ATOM   5524  CB  MET B 306       8.151   2.478  10.718  1.00 17.31           C  
ANISOU 5524  CB  MET B 306     2960   1850   1767   -248    436    332       C  
ATOM   5525  CG  MET B 306       7.228   2.776  11.870  1.00 24.15           C  
ANISOU 5525  CG  MET B 306     3515   3049   2613    212    849    284       C  
ATOM   5526  SD  MET B 306       7.642   4.321  12.726  1.00 30.00           S  
ANISOU 5526  SD  MET B 306     4504   3491   3405    510    544   -206       S  
ATOM   5527  CE  MET B 306       9.400   4.167  12.871  1.00 23.16           C  
ANISOU 5527  CE  MET B 306     4328   2617   1853    247    -94    525       C  
ATOM   5528  N   LEU B 307       9.555   2.773   7.643  1.00 10.95           N  
ANISOU 5528  N   LEU B 307     1705   1121   1334    176    248    130       N  
ATOM   5529  CA  LEU B 307      10.744   2.704   6.811  1.00 10.90           C  
ANISOU 5529  CA  LEU B 307     1539   1306   1298    189    182    153       C  
ATOM   5530  C   LEU B 307      11.287   4.097   6.471  1.00  9.41           C  
ANISOU 5530  C   LEU B 307     1319   1222   1034    189     80    140       C  
ATOM   5531  O   LEU B 307      12.502   4.291   6.311  1.00 10.11           O  
ANISOU 5531  O   LEU B 307     1415   1155   1271    184    -85     79       O  
ATOM   5532  CB  LEU B 307      10.460   1.955   5.488  1.00 10.74           C  
ANISOU 5532  CB  LEU B 307     1604   1116   1360    143    157    102       C  
ATOM   5533  CG  LEU B 307      10.232   0.444   5.627  1.00 12.47           C  
ANISOU 5533  CG  LEU B 307     1858   1221   1661    171    199     32       C  
ATOM   5534  CD1 LEU B 307       9.816  -0.147   4.286  1.00 14.87           C  
ANISOU 5534  CD1 LEU B 307     2343   1463   1842   -106     39   -146       C  
ATOM   5535  CD2 LEU B 307      11.476  -0.266   6.146  1.00 14.58           C  
ANISOU 5535  CD2 LEU B 307     2091   1305   2144    270     -8    126       C  
ATOM   5536  N   LEU B 308      10.365   5.082   6.297  1.00  9.49           N  
ANISOU 5536  N   LEU B 308     1274   1140   1194    157     13    151       N  
ATOM   5537  CA  LEU B 308      10.750   6.449   5.995  1.00  8.87           C  
ANISOU 5537  CA  LEU B 308     1313   1056   1003    233     28    102       C  
ATOM   5538  C   LEU B 308      11.016   7.279   7.250  1.00  7.83           C  
ANISOU 5538  C   LEU B 308     1037    960    980    177     -8    165       C  
ATOM   5539  O   LEU B 308      11.945   8.100   7.257  1.00  8.52           O  
ANISOU 5539  O   LEU B 308     1188   1089    962    131    -31     66       O  
ATOM   5540  CB  LEU B 308       9.655   7.143   5.149  1.00  9.19           C  
ANISOU 5540  CB  LEU B 308     1335   1182    977    247     30    133       C  
ATOM   5541  CG  LEU B 308       9.379   6.481   3.776  1.00 10.11           C  
ANISOU 5541  CG  LEU B 308     1511   1330   1003    285    -27     26       C  
ATOM   5542  CD1 LEU B 308       8.217   7.144   3.065  1.00 13.84           C  
ANISOU 5542  CD1 LEU B 308     1781   1950   1529    554   -355   -145       C  
ATOM   5543  CD2 LEU B 308      10.615   6.495   2.882  1.00 14.59           C  
ANISOU 5543  CD2 LEU B 308     1877   2531   1136    169     53     14       C  
ATOM   5544  N   LEU B 309      10.232   7.075   8.328  1.00  8.87           N  
ANISOU 5544  N   LEU B 309     1344   1176    851    208    122     20       N  
ATOM   5545  C   LEU B 309      11.784   7.850  10.134  1.00  8.03           C  
ANISOU 5545  C   LEU B 309     1272    920    857     90    101     77       C  
ATOM   5546  O   LEU B 309      12.272   8.836  10.699  1.00  9.46           O  
ANISOU 5546  O   LEU B 309     1444   1115   1036     89     45     44       O  
ATOM   5547  CA ALEU B 309      10.388   7.892   9.545  0.56  9.62           C  
ANISOU 5547  CA ALEU B 309     1368   1237   1050    138     36      4       C  
ATOM   5548  CB ALEU B 309       9.440   7.459  10.668  0.56 13.05           C  
ANISOU 5548  CB ALEU B 309     1897   1814   1249     39    217    130       C  
ATOM   5549  CG ALEU B 309       8.581   8.413  11.463  0.56 15.90           C  
ANISOU 5549  CG ALEU B 309     2485   1959   1596    172    581    181       C  
ATOM   5550  CD1ALEU B 309       8.407   8.052  12.934  0.56 16.06           C  
ANISOU 5550  CD1ALEU B 309     2287   2211   1605    208    534    296       C  
ATOM   5551  CD2ALEU B 309       8.639   9.893  11.188  0.56 16.55           C  
ANISOU 5551  CD2ALEU B 309     2054   1870   2365    278     58     74       C  
ATOM   5552  CA BLEU B 309      10.408   7.895   9.528  0.44  7.82           C  
ANISOU 5552  CA BLEU B 309     1185    948    839    181    177    117       C  
ATOM   5553  CB BLEU B 309       9.322   7.486  10.540  0.44  7.49           C  
ANISOU 5553  CB BLEU B 309     1232   1007    607    239    144    -61       C  
ATOM   5554  CG BLEU B 309       8.020   8.243  10.380  0.44  9.73           C  
ANISOU 5554  CG BLEU B 309     1284   1243   1169    271    -58   -199       C  
ATOM   5555  CD1BLEU B 309       6.928   7.429  11.051  0.44 13.29           C  
ANISOU 5555  CD1BLEU B 309     1653   1599   1797    -22    241   -180       C  
ATOM   5556  CD2BLEU B 309       8.049   9.614  11.059  0.44  5.70           C  
ANISOU 5556  CD2BLEU B 309      578    656    930    194    -75    194       C  
ATOM   5557  N   SER B 310      12.486   6.704  10.042  1.00  8.33           N  
ANISOU 5557  N   SER B 310     1233    979    955    163     -9    154       N  
ATOM   5558  CA  SER B 310      13.845   6.594  10.553  1.00  8.16           C  
ANISOU 5558  CA  SER B 310     1192    935    976     75    -12    130       C  
ATOM   5559  C   SER B 310      14.874   7.477   9.828  1.00  7.80           C  
ANISOU 5559  C   SER B 310     1102    926    934     36     23     19       C  
ATOM   5560  O   SER B 310      15.953   7.763  10.359  1.00  8.88           O  
ANISOU 5560  O   SER B 310     1224    996   1153     12    -75    106       O  
ATOM   5561  CB  SER B 310      14.311   5.129  10.541  1.00 10.17           C  
ANISOU 5561  CB  SER B 310     1416   1117   1330    206    -22    263       C  
ATOM   5562  OG  SER B 310      14.144   4.558   9.257  1.00 10.72           O  
ANISOU 5562  OG  SER B 310     1696    994   1383    255     38    120       O  
ATOM   5563  N   GLY B 311      14.564   7.861   8.550  1.00  8.47           N  
ANISOU 5563  N   GLY B 311     1309    977    931    112     43    108       N  
ATOM   5564  CA  GLY B 311      15.465   8.713   7.803  1.00  8.65           C  
ANISOU 5564  CA  GLY B 311     1207   1048   1031    100     33    137       C  
ATOM   5565  C   GLY B 311      15.637   8.385   6.350  1.00  9.02           C  
ANISOU 5565  C   GLY B 311     1170   1245   1014    120     68    179       C  
ATOM   5566  O   GLY B 311      16.291   9.186   5.640  1.00 11.43           O  
ANISOU 5566  O   GLY B 311     1828   1356   1158     30    274    108       O  
ATOM   5567  N   ARG B 312      15.139   7.286   5.825  1.00  8.69           N  
ANISOU 5567  N   ARG B 312     1243   1123    936    185     25    223       N  
ATOM   5568  CA  ARG B 312      15.307   6.964   4.409  1.00  8.58           C  
ANISOU 5568  CA  ARG B 312     1153   1169    939    231    -40     65       C  
ATOM   5569  C   ARG B 312      14.643   8.013   3.512  1.00  9.15           C  
ANISOU 5569  C   ARG B 312     1266   1264    947    326    -13     -7       C  
ATOM   5570  O   ARG B 312      13.656   8.674   3.857  1.00 10.62           O  
ANISOU 5570  O   ARG B 312     1467   1550   1019    497     12    114       O  
ATOM   5571  CB  ARG B 312      14.663   5.601   4.078  1.00  8.91           C  
ANISOU 5571  CB  ARG B 312     1200   1176   1010    214     -2    123       C  
ATOM   5572  CG  ARG B 312      15.351   4.372   4.717  1.00  9.42           C  
ANISOU 5572  CG  ARG B 312     1247   1191   1140    265    -36    160       C  
ATOM   5573  CD  ARG B 312      14.689   3.096   4.235  1.00  9.56           C  
ANISOU 5573  CD  ARG B 312     1400   1108   1123    229    -19    147       C  
ATOM   5574  NE  ARG B 312      15.283   1.856   4.751  1.00  9.66           N  
ANISOU 5574  NE  ARG B 312     1414   1197   1058    347    -45     30       N  
ATOM   5575  CZ  ARG B 312      14.994   1.362   5.952  1.00  9.40           C  
ANISOU 5575  CZ  ARG B 312     1350   1116   1107    212   -128     39       C  
ATOM   5576  NH1 ARG B 312      14.169   1.947   6.808  1.00 10.21           N  
ANISOU 5576  NH1 ARG B 312     1377   1350   1153    277      2    100       N  
ATOM   5577  NH2 ARG B 312      15.564   0.170   6.297  1.00 10.60           N  
ANISOU 5577  NH2 ARG B 312     1652   1134   1241    302    -77     64       N  
ATOM   5578  N   THR B 313      15.179   8.101   2.283  1.00  8.96           N  
ANISOU 5578  N   THR B 313     1274   1310    821    408    -80    110       N  
ATOM   5579  CA  THR B 313      14.670   8.918   1.184  1.00  9.13           C  
ANISOU 5579  CA  THR B 313     1338   1170    960    511    -67    108       C  
ATOM   5580  C   THR B 313      14.226   8.008   0.054  1.00 10.00           C  
ANISOU 5580  C   THR B 313     1469   1339    990    462    -84    -16       C  
ATOM   5581  O   THR B 313      15.040   7.139  -0.352  1.00 12.65           O  
ANISOU 5581  O   THR B 313     1922   1737   1147    813   -226   -114       O  
ATOM   5582  CB  THR B 313      15.758   9.884   0.671  1.00 10.79           C  
ANISOU 5582  CB  THR B 313     1631   1268   1203    308     56    284       C  
ATOM   5583  OG1 THR B 313      16.170  10.765   1.743  1.00 11.51           O  
ANISOU 5583  OG1 THR B 313     1709   1254   1410    319    180    221       O  
ATOM   5584  CG2 THR B 313      15.223  10.744  -0.471  1.00 13.15           C  
ANISOU 5584  CG2 THR B 313     1975   1771   1250    463     89    518       C  
ATOM   5585  N   TRP B 314      13.019   8.177  -0.472  1.00 10.12           N  
ANISOU 5585  N   TRP B 314     1427   1410   1006    481    -62     28       N  
ATOM   5586  CA  TRP B 314      12.492   7.383  -1.589  1.00 10.06           C  
ANISOU 5586  CA  TRP B 314     1451   1320   1051    436    -44     40       C  
ATOM   5587  C   TRP B 314      12.146   8.346  -2.708  1.00 10.79           C  
ANISOU 5587  C   TRP B 314     1672   1407   1019    594    -61     45       C  
ATOM   5588  O   TRP B 314      11.392   9.321  -2.490  1.00 13.39           O  
ANISOU 5588  O   TRP B 314     2176   1749   1161    968    -46    148       O  
ATOM   5589  CB  TRP B 314      11.251   6.631  -1.128  1.00 11.21           C  
ANISOU 5589  CB  TRP B 314     1459   1593   1206    403     -7    -41       C  
ATOM   5590  CG  TRP B 314      10.873   5.402  -1.861  1.00  9.97           C  
ANISOU 5590  CG  TRP B 314     1421   1348   1019    361    -48    148       C  
ATOM   5591  CD1 TRP B 314      11.624   4.673  -2.792  1.00 10.01           C  
ANISOU 5591  CD1 TRP B 314     1349   1422   1032    327    -12     35       C  
ATOM   5592  CD2 TRP B 314       9.701   4.606  -1.640  1.00 10.49           C  
ANISOU 5592  CD2 TRP B 314     1361   1492   1132    301    -27    105       C  
ATOM   5593  NE1 TRP B 314      10.970   3.518  -3.152  1.00 10.37           N  
ANISOU 5593  NE1 TRP B 314     1370   1459   1113    128    114     86       N  
ATOM   5594  CE2 TRP B 314       9.801   3.438  -2.425  1.00 10.77           C  
ANISOU 5594  CE2 TRP B 314     1370   1519   1201    204     91    159       C  
ATOM   5595  CE3 TRP B 314       8.565   4.803  -0.812  1.00 11.64           C  
ANISOU 5595  CE3 TRP B 314     1497   1637   1288    415    110    251       C  
ATOM   5596  CZ2 TRP B 314       8.801   2.476  -2.412  1.00 12.25           C  
ANISOU 5596  CZ2 TRP B 314     1532   1834   1287     18     34    173       C  
ATOM   5597  CZ3 TRP B 314       7.577   3.845  -0.812  1.00 13.03           C  
ANISOU 5597  CZ3 TRP B 314     1568   1964   1417    313    230    261       C  
ATOM   5598  CH2 TRP B 314       7.693   2.702  -1.608  1.00 14.13           C  
ANISOU 5598  CH2 TRP B 314     1804   1942   1624    -10    324    172       C  
ATOM   5599  N   LYS B 315      12.599   8.094  -3.917  1.00 10.26           N  
ANISOU 5599  N   LYS B 315     1656   1320    924    490    -46    166       N  
ATOM   5600  CA  LYS B 315      12.290   8.988  -5.036  1.00 10.65           C  
ANISOU 5600  CA  LYS B 315     1786   1275    986    249    -99    148       C  
ATOM   5601  C   LYS B 315      12.150   8.156  -6.292  1.00  9.70           C  
ANISOU 5601  C   LYS B 315     1425   1322    939    370    -24    105       C  
ATOM   5602  O   LYS B 315      12.545   6.980  -6.304  1.00 10.56           O  
ANISOU 5602  O   LYS B 315     1588   1408   1014    483    -33     89       O  
ATOM   5603  CB ALYS B 315      13.152  10.203  -4.999  0.58 11.20           C  
ANISOU 5603  CB ALYS B 315     1487   1419   1350    272    144    121       C  
ATOM   5604  CG ALYS B 315      14.535   9.691  -5.439  0.58 10.64           C  
ANISOU 5604  CG ALYS B 315     1301   1640   1101     20    282    138       C  
ATOM   5605  CD ALYS B 315      15.659  10.632  -5.051  0.58 13.88           C  
ANISOU 5605  CD ALYS B 315     1707   1941   1626    -59     44     49       C  
ATOM   5606  CE ALYS B 315      15.507  12.024  -5.596  0.58 15.17           C  
ANISOU 5606  CE ALYS B 315     2114   1920   1731    113    135    -66       C  
ATOM   5607  NZ ALYS B 315      16.712  12.860  -5.351  0.58 18.25           N  
ANISOU 5607  NZ ALYS B 315     2373   2102   2458   -122    135    -18       N  
ATOM   5608  CB BLYS B 315      13.626   9.721  -5.382  0.41 12.52           C  
ANISOU 5608  CB BLYS B 315     2005   1448   1303     59    -90    147       C  
ATOM   5609  CG BLYS B 315      14.348  10.677  -4.478  0.41 12.70           C  
ANISOU 5609  CG BLYS B 315     1852   1609   1364   -119    -83    234       C  
ATOM   5610  CD BLYS B 315      15.717  11.163  -4.920  0.41 13.82           C  
ANISOU 5610  CD BLYS B 315     2059   1641   1553    -90    180    281       C  
ATOM   5611  CE BLYS B 315      16.293  12.231  -4.007  0.41 16.48           C  
ANISOU 5611  CE BLYS B 315     2472   2218   1571     25    -40     32       C  
ATOM   5612  NZ BLYS B 315      17.679  12.566  -4.394  0.41 18.85           N  
ANISOU 5612  NZ BLYS B 315     2589   2797   1777    -51     96     15       N  
ATOM   5613  N   GLY B 316      11.558   8.749  -7.332  1.00 10.10           N  
ANISOU 5613  N   GLY B 316     1620   1386    832    490     38     75       N  
ATOM   5614  CA  GLY B 316      11.582   8.149  -8.654  1.00 10.09           C  
ANISOU 5614  CA  GLY B 316     1592   1303    938    364     67     17       C  
ATOM   5615  C   GLY B 316      11.934   9.196  -9.698  1.00  9.38           C  
ANISOU 5615  C   GLY B 316     1346   1287    931    402      5     50       C  
ATOM   5616  O   GLY B 316      12.041  10.378  -9.368  1.00 10.14           O  
ANISOU 5616  O   GLY B 316     1472   1428    954    259    -11     61       O  
ATOM   5617  N   ALA B 317      12.091   8.808 -10.966  1.00 10.04           N  
ANISOU 5617  N   ALA B 317     1439   1501    874    315    140    109       N  
ATOM   5618  CA  ALA B 317      12.324   9.777 -12.028  1.00 10.11           C  
ANISOU 5618  CA  ALA B 317     1450   1483    909    170     81    129       C  
ATOM   5619  C   ALA B 317      12.054   9.131 -13.394  1.00  9.95           C  
ANISOU 5619  C   ALA B 317     1371   1402   1009    140    114    127       C  
ATOM   5620  O   ALA B 317      12.142   7.916 -13.576  1.00 10.26           O  
ANISOU 5620  O   ALA B 317     1536   1424    937    212      3     70       O  
ATOM   5621  CB  ALA B 317      13.779  10.251 -12.019  1.00 11.77           C  
ANISOU 5621  CB  ALA B 317     1592   1890    992    -42     89    -72       C  
ATOM   5622  N   ILE B 318      11.758  10.029 -14.345  1.00 10.18           N  
ANISOU 5622  N   ILE B 318     1491   1498    878    216     63     87       N  
ATOM   5623  CA  ILE B 318      11.653   9.706 -15.767  1.00  9.87           C  
ANISOU 5623  CA  ILE B 318     1342   1587    819    149    129    167       C  
ATOM   5624  C   ILE B 318      12.922  10.189 -16.457  1.00  9.62           C  
ANISOU 5624  C   ILE B 318     1328   1413    914     67    -70    149       C  
ATOM   5625  O   ILE B 318      13.457  11.285 -16.204  1.00 10.04           O  
ANISOU 5625  O   ILE B 318     1428   1428    957    150     58     73       O  
ATOM   5626  CB  ILE B 318      10.415  10.426 -16.391  1.00 11.15           C  
ANISOU 5626  CB  ILE B 318     1320   1909   1006    235     53    120       C  
ATOM   5627  CG1 ILE B 318       9.111  10.060 -15.681  1.00 14.02           C  
ANISOU 5627  CG1 ILE B 318     1608   2537   1182    198    149    124       C  
ATOM   5628  CG2 ILE B 318      10.325  10.155 -17.887  1.00 13.09           C  
ANISOU 5628  CG2 ILE B 318     1496   2483    996    273     34    145       C  
ATOM   5629  CD1 ILE B 318       8.750   8.601 -15.683  1.00 17.01           C  
ANISOU 5629  CD1 ILE B 318     1987   2643   1833     78    -61    184       C  
ATOM   5630  N   PHE B 319      13.483   9.347 -17.362  1.00  9.92           N  
ANISOU 5630  N   PHE B 319     1346   1546    876    128    104    124       N  
ATOM   5631  CA  PHE B 319      14.615   9.728 -18.227  1.00  9.70           C  
ANISOU 5631  CA  PHE B 319     1263   1464    957     30     49    143       C  
ATOM   5632  C   PHE B 319      15.824  10.232 -17.426  1.00  9.66           C  
ANISOU 5632  C   PHE B 319     1262   1371   1037     66     27     69       C  
ATOM   5633  O   PHE B 319      16.542  11.163 -17.821  1.00 10.27           O  
ANISOU 5633  O   PHE B 319     1440   1489    975     93     99    108       O  
ATOM   5634  CB  PHE B 319      14.181  10.765 -19.306  1.00 10.59           C  
ANISOU 5634  CB  PHE B 319     1443   1539   1043    188    108    130       C  
ATOM   5635  CG  PHE B 319      15.141  10.917 -20.472  1.00  9.85           C  
ANISOU 5635  CG  PHE B 319     1290   1501    952    110     23     -8       C  
ATOM   5636  CD1 PHE B 319      15.480   9.845 -21.266  1.00  9.80           C  
ANISOU 5636  CD1 PHE B 319     1318   1519    887     28     76      8       C  
ATOM   5637  CD2 PHE B 319      15.700  12.163 -20.793  1.00 10.67           C  
ANISOU 5637  CD2 PHE B 319     1455   1534   1063     67     71     54       C  
ATOM   5638  CE1 PHE B 319      16.344   9.974 -22.357  1.00 10.62           C  
ANISOU 5638  CE1 PHE B 319     1457   1571   1006     92     89     77       C  
ATOM   5639  CE2 PHE B 319      16.558  12.280 -21.885  1.00 11.06           C  
ANISOU 5639  CE2 PHE B 319     1578   1542   1081     49     64    178       C  
ATOM   5640  CZ  PHE B 319      16.894  11.185 -22.666  1.00 11.38           C  
ANISOU 5640  CZ  PHE B 319     1568   1737   1020     15    145    109       C  
ATOM   5641  N   GLY B 320      16.092   9.568 -16.263  1.00  9.54           N  
ANISOU 5641  N   GLY B 320     1286   1331   1009     39     70    104       N  
ATOM   5642  CA  GLY B 320      17.303   9.883 -15.493  1.00 10.20           C  
ANISOU 5642  CA  GLY B 320     1386   1418   1070    113   -102     29       C  
ATOM   5643  C   GLY B 320      17.320  11.268 -14.877  1.00  9.80           C  
ANISOU 5643  C   GLY B 320     1302   1362   1061     64     35    127       C  
ATOM   5644  O   GLY B 320      18.401  11.738 -14.473  1.00 10.59           O  
ANISOU 5644  O   GLY B 320     1413   1554   1056     25      7     89       O  
ATOM   5645  N   GLY B 321      16.164  11.959 -14.850  1.00 10.23           N  
ANISOU 5645  N   GLY B 321     1480   1461    945    224     59     58       N  
ATOM   5646  CA  GLY B 321      16.137  13.335 -14.367  1.00 10.80           C  
ANISOU 5646  CA  GLY B 321     1606   1466   1030    146     -9    132       C  
ATOM   5647  C   GLY B 321      16.645  14.355 -15.360  1.00 10.81           C  
ANISOU 5647  C   GLY B 321     1676   1488    944    102    -61     53       C  
ATOM   5648  O   GLY B 321      16.639  15.558 -15.043  1.00 12.70           O  
ANISOU 5648  O   GLY B 321     2039   1572   1216     92     14     29       O  
ATOM   5649  N   PHE B 322      17.094  13.991 -16.560  1.00 10.27           N  
ANISOU 5649  N   PHE B 322     1513   1416    974    127     55    140       N  
ATOM   5650  CA  PHE B 322      17.662  14.928 -17.511  1.00 10.48           C  
ANISOU 5650  CA  PHE B 322     1555   1431    994     41     47    107       C  
ATOM   5651  C   PHE B 322      16.607  15.777 -18.202  1.00 10.77           C  
ANISOU 5651  C   PHE B 322     1602   1546    944     53    -32     50       C  
ATOM   5652  O   PHE B 322      15.625  15.276 -18.756  1.00 10.65           O  
ANISOU 5652  O   PHE B 322     1494   1514   1039     52     -1     95       O  
ATOM   5653  CB  PHE B 322      18.435  14.175 -18.603  1.00 10.95           C  
ANISOU 5653  CB  PHE B 322     1536   1554   1072     98    113    105       C  
ATOM   5654  CG  PHE B 322      19.757  13.591 -18.174  1.00 11.81           C  
ANISOU 5654  CG  PHE B 322     1531   1668   1288     50     67    141       C  
ATOM   5655  CD1 PHE B 322      20.792  14.419 -17.759  1.00 14.31           C  
ANISOU 5655  CD1 PHE B 322     1680   1702   2055     33    -41     35       C  
ATOM   5656  CD2 PHE B 322      19.980  12.214 -18.232  1.00 11.16           C  
ANISOU 5656  CD2 PHE B 322     1436   1662   1142     46    145    234       C  
ATOM   5657  CE1 PHE B 322      22.012  13.884 -17.403  1.00 15.66           C  
ANISOU 5657  CE1 PHE B 322     1685   1804   2462   -116   -162     99       C  
ATOM   5658  CE2 PHE B 322      21.226  11.687 -17.902  1.00 11.92           C  
ANISOU 5658  CE2 PHE B 322     1653   1762   1113    194    119    255       C  
ATOM   5659  CZ  PHE B 322      22.240  12.511 -17.463  1.00 14.54           C  
ANISOU 5659  CZ  PHE B 322     1817   1868   1838    168     33     80       C  
ATOM   5660  N   LYS B 323      16.828  17.112 -18.242  1.00 11.14           N  
ANISOU 5660  N   LYS B 323     1809   1468    955    139    -49     24       N  
ATOM   5661  CA  LYS B 323      16.057  18.010 -19.136  1.00 11.55           C  
ANISOU 5661  CA  LYS B 323     1922   1434   1032    175    -64     73       C  
ATOM   5662  C   LYS B 323      16.435  17.583 -20.571  1.00 11.46           C  
ANISOU 5662  C   LYS B 323     1722   1576   1055      6    -40    103       C  
ATOM   5663  O   LYS B 323      17.610  17.611 -20.940  1.00 12.80           O  
ANISOU 5663  O   LYS B 323     1813   1902   1147     96     35    109       O  
ATOM   5664  CB  LYS B 323      16.409  19.465 -18.859  1.00 11.74           C  
ANISOU 5664  CB  LYS B 323     1797   1526   1138     89     50     80       C  
ATOM   5665  CG  LYS B 323      15.893  19.944 -17.491  1.00 13.16           C  
ANISOU 5665  CG  LYS B 323     2163   1670   1166     73   -102    -40       C  
ATOM   5666  CD  LYS B 323      16.247  21.410 -17.229  1.00 14.91           C  
ANISOU 5666  CD  LYS B 323     2313   1794   1559    -12     92   -133       C  
ATOM   5667  CE  LYS B 323      15.783  21.970 -15.892  1.00 14.92           C  
ANISOU 5667  CE  LYS B 323     2268   1912   1488     99    -33   -104       C  
ATOM   5668  NZ  LYS B 323      14.319  22.188 -15.871  1.00 15.14           N  
ANISOU 5668  NZ  LYS B 323     2347   1879   1526    159    157   -195       N  
ATOM   5669  N   SER B 324      15.448  17.083 -21.292  1.00 11.25           N  
ANISOU 5669  N   SER B 324     1673   1526   1075    106     36     25       N  
ATOM   5670  CA  SER B 324      15.771  16.255 -22.457  1.00 11.83           C  
ANISOU 5670  CA  SER B 324     1779   1658   1056     87     87    -48       C  
ATOM   5671  C   SER B 324      16.477  16.924 -23.617  1.00 11.32           C  
ANISOU 5671  C   SER B 324     1606   1638   1058     73     12     72       C  
ATOM   5672  O   SER B 324      17.497  16.402 -24.133  1.00 12.24           O  
ANISOU 5672  O   SER B 324     1786   1764   1101    104     84     44       O  
ATOM   5673  CB  SER B 324      14.474  15.567 -22.907  1.00 12.04           C  
ANISOU 5673  CB  SER B 324     1720   1711   1143    130     77    -21       C  
ATOM   5674  OG  SER B 324      13.543  16.556 -23.284  1.00 12.27           O  
ANISOU 5674  OG  SER B 324     1842   1689   1133     95      4    111       O  
ATOM   5675  N   LYS B 325      15.963  18.087 -24.050  1.00 11.27           N  
ANISOU 5675  N   LYS B 325     1793   1608    882     89    134     66       N  
ATOM   5676  CA  LYS B 325      16.515  18.766 -25.236  1.00 11.73           C  
ANISOU 5676  CA  LYS B 325     1926   1564    966     16     13     47       C  
ATOM   5677  C   LYS B 325      17.867  19.393 -24.943  1.00 13.04           C  
ANISOU 5677  C   LYS B 325     1998   1734   1224    -91     59    153       C  
ATOM   5678  O   LYS B 325      18.758  19.409 -25.809  1.00 13.54           O  
ANISOU 5678  O   LYS B 325     2006   1727   1413    -46    114    261       O  
ATOM   5679  CB  LYS B 325      15.503  19.718 -25.851  1.00 12.40           C  
ANISOU 5679  CB  LYS B 325     1877   1658   1175    -43    -42    145       C  
ATOM   5680  CG  LYS B 325      15.889  20.248 -27.232  1.00 14.04           C  
ANISOU 5680  CG  LYS B 325     2218   1973   1145    161    -57    301       C  
ATOM   5681  CD  LYS B 325      14.676  20.726 -28.021  1.00 13.72           C  
ANISOU 5681  CD  LYS B 325     2052   2045   1117    113     85    167       C  
ATOM   5682  CE  LYS B 325      15.091  21.266 -29.389  1.00 13.74           C  
ANISOU 5682  CE  LYS B 325     2078   1994   1148     49     10    262       C  
ATOM   5683  NZ  LYS B 325      13.894  21.329 -30.301  1.00 14.66           N  
ANISOU 5683  NZ  LYS B 325     2220   2133   1215     77    -96    240       N  
ATOM   5684  N   ASP B 326      18.062  19.915 -23.702  1.00 12.60           N  
ANISOU 5684  N   ASP B 326     1837   1668   1282    -65     -7    104       N  
ATOM   5685  CA  ASP B 326      19.369  20.431 -23.346  1.00 13.80           C  
ANISOU 5685  CA  ASP B 326     1967   1743   1534   -105   -115    133       C  
ATOM   5686  C   ASP B 326      20.409  19.308 -23.232  1.00 12.87           C  
ANISOU 5686  C   ASP B 326     1767   1737   1385   -153    -98     37       C  
ATOM   5687  O   ASP B 326      21.587  19.444 -23.544  1.00 14.85           O  
ANISOU 5687  O   ASP B 326     1892   2129   1622   -179      6    271       O  
ATOM   5688  CB  ASP B 326      19.300  21.133 -21.975  1.00 16.82           C  
ANISOU 5688  CB  ASP B 326     2386   2111   1893   -120   -200   -251       C  
ATOM   5689  CG  ASP B 326      18.588  22.460 -21.936  1.00 19.37           C  
ANISOU 5689  CG  ASP B 326     2623   2336   2401    -10   -163   -329       C  
ATOM   5690  OD1 ASP B 326      18.445  23.104 -22.994  1.00 22.47           O  
ANISOU 5690  OD1 ASP B 326     3613   1973   2950    126   -198    -45       O  
ATOM   5691  OD2 ASP B 326      18.162  22.818 -20.805  1.00 22.46           O  
ANISOU 5691  OD2 ASP B 326     2953   2780   2800    -99    122   -794       O  
ATOM   5692  N   SER B 327      19.992  18.159 -22.652  1.00 12.26           N  
ANISOU 5692  N   SER B 327     1869   1650   1138     78    -22     76       N  
ATOM   5693  CA  SER B 327      20.923  17.105 -22.264  1.00 12.25           C  
ANISOU 5693  CA  SER B 327     1720   1740   1197     32    124     99       C  
ATOM   5694  C   SER B 327      21.356  16.143 -23.367  1.00 11.87           C  
ANISOU 5694  C   SER B 327     1633   1682   1195     10     65     76       C  
ATOM   5695  O   SER B 327      22.513  15.740 -23.415  1.00 13.15           O  
ANISOU 5695  O   SER B 327     1731   2082   1183     95     82     97       O  
ATOM   5696  CB  SER B 327      20.361  16.291 -21.092  1.00 12.82           C  
ANISOU 5696  CB  SER B 327     1911   1805   1153    101    193    103       C  
ATOM   5697  OG  SER B 327      20.057  17.095 -19.952  1.00 13.86           O  
ANISOU 5697  OG  SER B 327     2154   2001   1109    143     54     -5       O  
ATOM   5698  N   VAL B 328      20.397  15.746 -24.228  1.00 11.68           N  
ANISOU 5698  N   VAL B 328     1580   1699   1157     24    105     11       N  
ATOM   5699  CA  VAL B 328      20.717  14.760 -25.276  1.00 11.46           C  
ANISOU 5699  CA  VAL B 328     1485   1592   1276    120    141    -40       C  
ATOM   5700  C   VAL B 328      21.903  15.138 -26.156  1.00 11.76           C  
ANISOU 5700  C   VAL B 328     1582   1624   1262     -4     61    166       C  
ATOM   5701  O   VAL B 328      22.826  14.323 -26.334  1.00 12.08           O  
ANISOU 5701  O   VAL B 328     1511   1780   1297   -113     40    -10       O  
ATOM   5702  CB  VAL B 328      19.430  14.326 -26.017  1.00 10.81           C  
ANISOU 5702  CB  VAL B 328     1490   1533   1084     39    187    105       C  
ATOM   5703  CG1 VAL B 328      19.744  13.654 -27.364  1.00 12.70           C  
ANISOU 5703  CG1 VAL B 328     1898   1769   1160    -76    324      1       C  
ATOM   5704  CG2 VAL B 328      18.615  13.362 -25.119  1.00 12.21           C  
ANISOU 5704  CG2 VAL B 328     1608   1826   1204   -180    191    133       C  
ATOM   5705  N   PRO B 329      22.004  16.365 -26.644  1.00 11.98           N  
ANISOU 5705  N   PRO B 329     1653   1655   1243   -197    104     -5       N  
ATOM   5706  CA  PRO B 329      23.158  16.746 -27.488  1.00 13.12           C  
ANISOU 5706  CA  PRO B 329     1753   1892   1339   -233    126     49       C  
ATOM   5707  C   PRO B 329      24.477  16.677 -26.734  1.00 13.05           C  
ANISOU 5707  C   PRO B 329     1803   1749   1407   -187    121    132       C  
ATOM   5708  O   PRO B 329      25.516  16.293 -27.293  1.00 14.06           O  
ANISOU 5708  O   PRO B 329     1649   2204   1489   -344     46    115       O  
ATOM   5709  CB  PRO B 329      22.849  18.137 -28.051  1.00 14.39           C  
ANISOU 5709  CB  PRO B 329     1945   2047   1475   -202     42    248       C  
ATOM   5710  CG  PRO B 329      21.350  18.214 -27.953  1.00 14.02           C  
ANISOU 5710  CG  PRO B 329     2011   1904   1412    -61     46    224       C  
ATOM   5711  CD  PRO B 329      21.013  17.430 -26.678  1.00 13.22           C  
ANISOU 5711  CD  PRO B 329     2024   1900   1099     33      8    103       C  
ATOM   5712  N   LYS B 330      24.473  17.069 -25.447  1.00 13.89           N  
ANISOU 5712  N   LYS B 330     1763   2032   1482   -183    -51     16       N  
ATOM   5713  CA  LYS B 330      25.672  17.002 -24.611  1.00 14.35           C  
ANISOU 5713  CA  LYS B 330     1866   1984   1601   -201   -139    103       C  
ATOM   5714  C   LYS B 330      26.101  15.571 -24.324  1.00 12.80           C  
ANISOU 5714  C   LYS B 330     1553   1903   1407   -279   -111     92       C  
ATOM   5715  O   LYS B 330      27.308  15.259 -24.330  1.00 14.66           O  
ANISOU 5715  O   LYS B 330     1679   2210   1682   -194    -86      9       O  
ATOM   5716  CB ALYS B 330      25.439  17.816 -23.328  0.63 18.44           C  
ANISOU 5716  CB ALYS B 330     2414   2749   1844   -208   -218   -248       C  
ATOM   5717  CG ALYS B 330      25.166  19.286 -23.595  0.63 25.08           C  
ANISOU 5717  CG ALYS B 330     3482   2990   3057     84   -155    -84       C  
ATOM   5718  CD ALYS B 330      26.155  19.967 -24.522  0.63 29.85           C  
ANISOU 5718  CD ALYS B 330     3964   3656   3721   -134    233     16       C  
ATOM   5719  CE ALYS B 330      25.641  20.098 -25.949  0.63 32.04           C  
ANISOU 5719  CE ALYS B 330     4279   3967   3930    -95      0     37       C  
ATOM   5720  NZ ALYS B 330      26.646  19.705 -26.979  0.63 32.69           N  
ANISOU 5720  NZ ALYS B 330     4474   3844   4104   -130    176     21       N  
ATOM   5721  CB BLYS B 330      25.375  17.715 -23.272  0.37 15.35           C  
ANISOU 5721  CB BLYS B 330     2022   2240   1570   -226   -275     -4       C  
ATOM   5722  CG BLYS B 330      25.193  19.208 -23.414  0.37 18.25           C  
ANISOU 5722  CG BLYS B 330     2525   2342   2068   -106   -216     73       C  
ATOM   5723  CD BLYS B 330      24.787  19.909 -22.130  0.37 20.20           C  
ANISOU 5723  CD BLYS B 330     2779   2668   2230   -116   -142   -111       C  
ATOM   5724  CE BLYS B 330      24.754  21.417 -22.324  0.37 22.63           C  
ANISOU 5724  CE BLYS B 330     3097   2744   2758   -103   -169     44       C  
ATOM   5725  NZ BLYS B 330      24.011  22.122 -21.248  0.37 25.16           N  
ANISOU 5725  NZ BLYS B 330     3341   3286   2934   -125     45    -80       N  
ATOM   5726  N   LEU B 331      25.122  14.668 -24.090  1.00 12.87           N  
ANISOU 5726  N   LEU B 331     1565   1817   1508   -294     27     30       N  
ATOM   5727  CA  LEU B 331      25.445  13.250 -23.882  1.00 12.45           C  
ANISOU 5727  CA  LEU B 331     1427   1877   1425   -126     83    104       C  
ATOM   5728  C   LEU B 331      26.057  12.661 -25.163  1.00 12.24           C  
ANISOU 5728  C   LEU B 331     1459   1778   1415   -141     83     67       C  
ATOM   5729  O   LEU B 331      27.039  11.924 -25.094  1.00 13.01           O  
ANISOU 5729  O   LEU B 331     1476   2000   1469   -119    103    101       O  
ATOM   5730  CB  LEU B 331      24.178  12.506 -23.468  1.00 12.72           C  
ANISOU 5730  CB  LEU B 331     1467   2000   1367   -104    152     38       C  
ATOM   5731  CG  LEU B 331      23.728  12.801 -22.018  1.00 13.94           C  
ANISOU 5731  CG  LEU B 331     1861   2128   1309    -95    163     18       C  
ATOM   5732  CD1 LEU B 331      22.260  12.405 -21.812  1.00 15.36           C  
ANISOU 5732  CD1 LEU B 331     2113   2196   1526   -356    319    -79       C  
ATOM   5733  CD2 LEU B 331      24.607  12.079 -20.996  1.00 18.31           C  
ANISOU 5733  CD2 LEU B 331     2456   2865   1636    314     40    131       C  
ATOM   5734  N   VAL B 332      25.525  13.000 -26.344  1.00 12.79           N  
ANISOU 5734  N   VAL B 332     1515   1971   1373   -140    154    135       N  
ATOM   5735  CA  VAL B 332      26.156  12.558 -27.613  1.00 13.23           C  
ANISOU 5735  CA  VAL B 332     1626   2000   1403     -3    197    104       C  
ATOM   5736  C   VAL B 332      27.588  13.113 -27.716  1.00 13.62           C  
ANISOU 5736  C   VAL B 332     1720   1929   1526    -28    203    103       C  
ATOM   5737  O   VAL B 332      28.502  12.360 -28.081  1.00 14.09           O  
ANISOU 5737  O   VAL B 332     1718   2087   1549    -66    180    138       O  
ATOM   5738  CB  VAL B 332      25.318  12.915 -28.842  1.00 13.56           C  
ANISOU 5738  CB  VAL B 332     1723   2063   1366   -121    147     63       C  
ATOM   5739  CG1 VAL B 332      26.093  12.694 -30.135  1.00 14.14           C  
ANISOU 5739  CG1 VAL B 332     1745   2290   1339   -147    187    176       C  
ATOM   5740  CG2 VAL B 332      23.994  12.139 -28.875  1.00 13.14           C  
ANISOU 5740  CG2 VAL B 332     1731   1933   1328    -58    103     52       C  
ATOM   5741  N   ALA B 333      27.782  14.406 -27.407  1.00 13.97           N  
ANISOU 5741  N   ALA B 333     1723   1953   1632   -259    101    164       N  
ATOM   5742  CA  ALA B 333      29.147  14.970 -27.478  1.00 15.32           C  
ANISOU 5742  CA  ALA B 333     1732   2135   1953   -191    205    145       C  
ATOM   5743  C   ALA B 333      30.098  14.243 -26.531  1.00 15.38           C  
ANISOU 5743  C   ALA B 333     1806   2151   1886   -132    145     74       C  
ATOM   5744  O   ALA B 333      31.257  13.907 -26.868  1.00 16.60           O  
ANISOU 5744  O   ALA B 333     1768   2442   2098   -237     89    174       O  
ATOM   5745  CB  ALA B 333      29.149  16.471 -27.173  1.00 15.29           C  
ANISOU 5745  CB  ALA B 333     1901   2056   1852   -208     97    324       C  
ATOM   5746  N   ASP B 334      29.612  13.892 -25.326  1.00 15.37           N  
ANISOU 5746  N   ASP B 334     1721   2366   1753   -250    -73    -29       N  
ATOM   5747  CA  ASP B 334      30.416  13.166 -24.357  1.00 15.69           C  
ANISOU 5747  CA  ASP B 334     1822   2255   1883    -94    -21    -28       C  
ATOM   5748  C   ASP B 334      30.783  11.760 -24.851  1.00 15.54           C  
ANISOU 5748  C   ASP B 334     1744   2315   1845   -122   -113    -91       C  
ATOM   5749  O   ASP B 334      31.926  11.274 -24.639  1.00 16.10           O  
ANISOU 5749  O   ASP B 334     1662   2550   1904   -151     -9     11       O  
ATOM   5750  CB  ASP B 334      29.740  13.141 -22.987  1.00 18.19           C  
ANISOU 5750  CB  ASP B 334     2166   2818   1926    -35    -21   -138       C  
ATOM   5751  CG  ASP B 334      29.715  14.455 -22.237  1.00 22.08           C  
ANISOU 5751  CG  ASP B 334     3034   3073   2284    138   -154   -344       C  
ATOM   5752  OD1 ASP B 334      30.406  15.411 -22.622  1.00 24.35           O  
ANISOU 5752  OD1 ASP B 334     3504   3025   2723   -114   -424   -507       O  
ATOM   5753  OD2 ASP B 334      28.960  14.519 -21.232  1.00 25.88           O  
ANISOU 5753  OD2 ASP B 334     3877   3582   2374    472    107   -236       O  
ATOM   5754  N   PHE B 335      29.830  11.081 -25.509  1.00 14.87           N  
ANISOU 5754  N   PHE B 335     1589   2296   1766   -175    -31    -32       N  
ATOM   5755  CA  PHE B 335      30.113   9.806 -26.152  1.00 14.54           C  
ANISOU 5755  CA  PHE B 335     1486   2280   1757   -154    125     83       C  
ATOM   5756  C   PHE B 335      31.208   9.923 -27.226  1.00 15.13           C  
ANISOU 5756  C   PHE B 335     1583   2298   1868   -145    231    133       C  
ATOM   5757  O   PHE B 335      32.121   9.088 -27.290  1.00 16.58           O  
ANISOU 5757  O   PHE B 335     1702   2562   2035    -58    156    145       O  
ATOM   5758  CB  PHE B 335      28.817   9.232 -26.772  1.00 14.01           C  
ANISOU 5758  CB  PHE B 335     1459   2283   1580   -152    135     23       C  
ATOM   5759  CG  PHE B 335      29.041   7.962 -27.539  1.00 15.01           C  
ANISOU 5759  CG  PHE B 335     1531   2322   1850    -81    208    -12       C  
ATOM   5760  CD1 PHE B 335      29.400   6.776 -26.917  1.00 15.65           C  
ANISOU 5760  CD1 PHE B 335     1662   2283   2001     39    302    -37       C  
ATOM   5761  CD2 PHE B 335      29.003   7.980 -28.925  1.00 16.76           C  
ANISOU 5761  CD2 PHE B 335     1845   2660   1861    -21    108   -251       C  
ATOM   5762  CE1 PHE B 335      29.630   5.628 -27.645  1.00 16.58           C  
ANISOU 5762  CE1 PHE B 335     1938   2189   2171   -194    382    -72       C  
ATOM   5763  CE2 PHE B 335      29.237   6.858 -29.681  1.00 17.99           C  
ANISOU 5763  CE2 PHE B 335     2353   2509   1973    -65     72   -160       C  
ATOM   5764  CZ  PHE B 335      29.568   5.692 -29.039  1.00 16.84           C  
ANISOU 5764  CZ  PHE B 335     1884   2361   2154    183    276   -263       C  
ATOM   5765  N   MET B 336      31.110  10.957 -28.063  1.00 16.26           N  
ANISOU 5765  N   MET B 336     1752   2529   1896   -183    389    207       N  
ATOM   5766  CA  MET B 336      32.092  11.165 -29.132  1.00 17.03           C  
ANISOU 5766  CA  MET B 336     1811   2886   1775   -235    376    198       C  
ATOM   5767  C   MET B 336      33.466  11.455 -28.538  1.00 19.29           C  
ANISOU 5767  C   MET B 336     1951   3163   2214   -218    209    104       C  
ATOM   5768  O   MET B 336      34.482  11.148 -29.204  1.00 20.86           O  
ANISOU 5768  O   MET B 336     1951   3525   2451   -260    378    157       O  
ATOM   5769  CB AMET B 336      31.659  12.223 -30.140  0.51 18.82           C  
ANISOU 5769  CB AMET B 336     2178   2933   2041   -264    185    268       C  
ATOM   5770  CG AMET B 336      30.347  11.868 -30.813  0.51 19.57           C  
ANISOU 5770  CG AMET B 336     2211   3231   1994   -275    220    135       C  
ATOM   5771  SD AMET B 336      30.336  10.560 -32.017  0.51 21.31           S  
ANISOU 5771  SD AMET B 336     2597   3469   2029   -223    270     -5       S  
ATOM   5772  CE AMET B 336      31.137   9.147 -31.311  0.51 24.65           C  
ANISOU 5772  CE AMET B 336     3080   3594   2690    -73    144    130       C  
ATOM   5773  CB BMET B 336      31.667  12.316 -30.048  0.49 17.59           C  
ANISOU 5773  CB BMET B 336     1896   2826   1959   -370    162    221       C  
ATOM   5774  CG BMET B 336      30.384  12.102 -30.833  0.49 16.84           C  
ANISOU 5774  CG BMET B 336     1806   2883   1709   -328    310    124       C  
ATOM   5775  SD BMET B 336      30.400  10.609 -31.849  0.49 18.26           S  
ANISOU 5775  SD BMET B 336     1987   3147   1803   -218    186    -76       S  
ATOM   5776  CE BMET B 336      31.401  11.130 -33.230  0.49 18.25           C  
ANISOU 5776  CE BMET B 336     2192   3245   1497   -236    130   -136       C  
ATOM   5777  N   ALA B 337      33.531  12.013 -27.325  1.00 18.78           N  
ANISOU 5777  N   ALA B 337     1878   3131   2126   -428    268    178       N  
ATOM   5778  CA  ALA B 337      34.771  12.309 -26.617  1.00 20.29           C  
ANISOU 5778  CA  ALA B 337     2000   3213   2497   -284    112    115       C  
ATOM   5779  C   ALA B 337      35.204  11.196 -25.694  1.00 19.91           C  
ANISOU 5779  C   ALA B 337     2127   3103   2335   -383    190     88       C  
ATOM   5780  O   ALA B 337      36.198  11.250 -24.948  1.00 22.42           O  
ANISOU 5780  O   ALA B 337     2114   3479   2927   -476      6    238       O  
ATOM   5781  CB  ALA B 337      34.627  13.604 -25.841  1.00 20.35           C  
ANISOU 5781  CB  ALA B 337     2131   3223   2380   -395   -127    108       C  
ATOM   5782  N   LYS B 338      34.622   9.999 -25.859  1.00 19.95           N  
ANISOU 5782  N   LYS B 338     2203   2965   2411   -258    384     82       N  
ATOM   5783  CA  LYS B 338      34.962   8.767 -25.184  1.00 21.79           C  
ANISOU 5783  CA  LYS B 338     2515   3140   2623     23    104     98       C  
ATOM   5784  C   LYS B 338      34.806   8.836 -23.663  1.00 20.19           C  
ANISOU 5784  C   LYS B 338     2171   2962   2538     -8     -3     96       C  
ATOM   5785  O   LYS B 338      35.527   8.142 -22.916  1.00 21.53           O  
ANISOU 5785  O   LYS B 338     2281   3315   2585     53    114    355       O  
ATOM   5786  CB ALYS B 338      36.405   8.315 -25.497  0.54 26.31           C  
ANISOU 5786  CB ALYS B 338     2695   3743   3560    166    153     66       C  
ATOM   5787  CG ALYS B 338      36.855   8.383 -26.933  0.54 30.55           C  
ANISOU 5787  CG ALYS B 338     3649   4259   3701    233    307    175       C  
ATOM   5788  CD ALYS B 338      36.010   7.645 -27.941  0.54 34.11           C  
ANISOU 5788  CD ALYS B 338     3992   4603   4366    130    -71     55       C  
ATOM   5789  CE ALYS B 338      36.697   7.630 -29.309  0.54 36.99           C  
ANISOU 5789  CE ALYS B 338     4479   5067   4510    184    118    164       C  
ATOM   5790  NZ ALYS B 338      36.098   6.592 -30.196  0.54 38.60           N  
ANISOU 5790  NZ ALYS B 338     4722   5229   4716    132     61     55       N  
ATOM   5791  CB BLYS B 338      36.344   8.244 -25.628  0.46 24.59           C  
ANISOU 5791  CB BLYS B 338     2669   3535   3137     97    250     24       C  
ATOM   5792  CG BLYS B 338      36.462   8.155 -27.159  0.46 26.78           C  
ANISOU 5792  CG BLYS B 338     3095   3880   3201    255    175   -126       C  
ATOM   5793  CD BLYS B 338      37.384   9.254 -27.660  0.46 29.77           C  
ANISOU 5793  CD BLYS B 338     3529   4047   3735    -13    111    -44       C  
ATOM   5794  CE BLYS B 338      37.128   9.740 -29.066  0.46 30.80           C  
ANISOU 5794  CE BLYS B 338     3657   4266   3779     62     71    -20       C  
ATOM   5795  NZ BLYS B 338      37.358  11.213 -29.195  0.46 30.81           N  
ANISOU 5795  NZ BLYS B 338     3573   4299   3833     -2     78    -26       N  
ATOM   5796  N   LYS B 339      33.812   9.576 -23.163  1.00 18.04           N  
ANISOU 5796  N   LYS B 339     1835   2740   2278   -207   -133    119       N  
ATOM   5797  CA  LYS B 339      33.558   9.680 -21.733  1.00 18.89           C  
ANISOU 5797  CA  LYS B 339     2207   2704   2267   -302   -144     66       C  
ATOM   5798  C   LYS B 339      32.758   8.520 -21.141  1.00 18.55           C  
ANISOU 5798  C   LYS B 339     2181   2702   2163   -267     -5    -77       C  
ATOM   5799  O   LYS B 339      32.784   8.321 -19.921  1.00 19.47           O  
ANISOU 5799  O   LYS B 339     2248   3007   2142   -371    -30    -41       O  
ATOM   5800  CB  LYS B 339      32.940  11.037 -21.361  1.00 21.31           C  
ANISOU 5800  CB  LYS B 339     2741   2896   2459    -27   -158      2       C  
ATOM   5801  CG ALYS B 339      33.834  12.237 -21.650  0.56 24.31           C  
ANISOU 5801  CG ALYS B 339     3107   3148   2983   -249   -188     81       C  
ATOM   5802  CD ALYS B 339      33.211  13.538 -21.170  0.56 27.47           C  
ANISOU 5802  CD ALYS B 339     3474   3619   3345    101   -227   -154       C  
ATOM   5803  CE ALYS B 339      34.147  14.712 -21.432  0.56 30.44           C  
ANISOU 5803  CE ALYS B 339     3855   4003   3708   -180   -213    -12       C  
ATOM   5804  NZ ALYS B 339      33.442  16.014 -21.296  0.56 32.29           N  
ANISOU 5804  NZ ALYS B 339     4072   4178   4019    -11   -284   -112       N  
ATOM   5805  CG BLYS B 339      33.887  12.142 -21.835  0.44 24.18           C  
ANISOU 5805  CG BLYS B 339     3130   3193   2865   -218    -82    150       C  
ATOM   5806  CD BLYS B 339      33.503  13.557 -21.486  0.44 27.03           C  
ANISOU 5806  CD BLYS B 339     3645   3423   3203     27   -123    -28       C  
ATOM   5807  CE BLYS B 339      34.597  14.516 -21.971  0.44 29.44           C  
ANISOU 5807  CE BLYS B 339     3955   3721   3509   -123     70     28       C  
ATOM   5808  NZ BLYS B 339      35.908  14.211 -21.330  0.44 31.17           N  
ANISOU 5808  NZ BLYS B 339     4010   4032   3801    -46     23     13       N  
ATOM   5809  N   PHE B 340      32.067   7.766 -21.982  1.00 15.41           N  
ANISOU 5809  N   PHE B 340     1661   2370   1823    -35     90     39       N  
ATOM   5810  CA  PHE B 340      31.318   6.572 -21.594  1.00 15.38           C  
ANISOU 5810  CA  PHE B 340     1634   2350   1862    -32     -9     -2       C  
ATOM   5811  C   PHE B 340      31.210   5.673 -22.833  1.00 14.58           C  
ANISOU 5811  C   PHE B 340     1527   2263   1750   -177    156     10       C  
ATOM   5812  O   PHE B 340      31.456   6.130 -23.957  1.00 16.55           O  
ANISOU 5812  O   PHE B 340     1720   2702   1867    -39    264    144       O  
ATOM   5813  CB  PHE B 340      29.940   6.868 -21.003  1.00 14.58           C  
ANISOU 5813  CB  PHE B 340     1614   2250   1677   -101      8     62       C  
ATOM   5814  CG  PHE B 340      28.974   7.602 -21.890  1.00 14.01           C  
ANISOU 5814  CG  PHE B 340     1591   2069   1662     -7    107     71       C  
ATOM   5815  CD1 PHE B 340      28.203   6.943 -22.838  1.00 14.16           C  
ANISOU 5815  CD1 PHE B 340     1522   2226   1633    -75    117    184       C  
ATOM   5816  CD2 PHE B 340      28.813   8.977 -21.787  1.00 16.01           C  
ANISOU 5816  CD2 PHE B 340     2018   2127   1940    -45     68     77       C  
ATOM   5817  CE1 PHE B 340      27.282   7.620 -23.631  1.00 14.17           C  
ANISOU 5817  CE1 PHE B 340     1585   2167   1631     25    255    234       C  
ATOM   5818  CE2 PHE B 340      27.919   9.671 -22.571  1.00 15.10           C  
ANISOU 5818  CE2 PHE B 340     1798   2106   1834   -109    243    165       C  
ATOM   5819  CZ  PHE B 340      27.165   8.989 -23.513  1.00 14.06           C  
ANISOU 5819  CZ  PHE B 340     1641   2153   1549     21    210    240       C  
ATOM   5820  N   ALA B 341      30.884   4.416 -22.623  1.00 15.26           N  
ANISOU 5820  N   ALA B 341     1802   2195   1801      3    114     -5       N  
ATOM   5821  CA  ALA B 341      30.728   3.422 -23.678  1.00 15.13           C  
ANISOU 5821  CA  ALA B 341     1688   2184   1878    -21    103    -48       C  
ATOM   5822  C   ALA B 341      29.276   2.960 -23.809  1.00 14.57           C  
ANISOU 5822  C   ALA B 341     1540   2371   1625    108     85     14       C  
ATOM   5823  O   ALA B 341      28.521   2.882 -22.812  1.00 16.82           O  
ANISOU 5823  O   ALA B 341     2005   2794   1593   -127    114     -4       O  
ATOM   5824  CB  ALA B 341      31.569   2.175 -23.351  1.00 16.90           C  
ANISOU 5824  CB  ALA B 341     1976   2262   2185     79    -55    -94       C  
ATOM   5825  N   LEU B 342      28.886   2.659 -25.060  1.00 13.71           N  
ANISOU 5825  N   LEU B 342     1478   2111   1619    -33     90     -5       N  
ATOM   5826  CA  LEU B 342      27.551   2.149 -25.385  1.00 12.79           C  
ANISOU 5826  CA  LEU B 342     1539   1891   1429    -10    116     32       C  
ATOM   5827  C   LEU B 342      27.567   0.709 -25.874  1.00 12.79           C  
ANISOU 5827  C   LEU B 342     1459   1863   1538    103    151     90       C  
ATOM   5828  O   LEU B 342      26.613  -0.049 -25.684  1.00 13.68           O  
ANISOU 5828  O   LEU B 342     1435   2125   1636     52    127     -8       O  
ATOM   5829  CB  LEU B 342      26.808   3.008 -26.410  1.00 13.20           C  
ANISOU 5829  CB  LEU B 342     1575   2004   1437     73    126     12       C  
ATOM   5830  CG  LEU B 342      26.464   4.417 -25.893  1.00 12.71           C  
ANISOU 5830  CG  LEU B 342     1368   1934   1528     80    268     41       C  
ATOM   5831  CD1 LEU B 342      25.957   5.311 -27.021  1.00 13.56           C  
ANISOU 5831  CD1 LEU B 342     1464   1965   1725    -50    119    114       C  
ATOM   5832  CD2 LEU B 342      25.458   4.362 -24.741  1.00 13.84           C  
ANISOU 5832  CD2 LEU B 342     1542   2167   1550     36    326     23       C  
ATOM   5833  N   ASP B 343      28.696   0.264 -26.497  1.00 13.67           N  
ANISOU 5833  N   ASP B 343     1522   2092   1581     66    272    -81       N  
ATOM   5834  CA  ASP B 343      28.791  -1.099 -26.948  1.00 13.90           C  
ANISOU 5834  CA  ASP B 343     1488   2039   1752    -57    323     11       C  
ATOM   5835  C   ASP B 343      28.461  -2.196 -25.974  1.00 13.39           C  
ANISOU 5835  C   ASP B 343     1593   1869   1628    164    172     16       C  
ATOM   5836  O   ASP B 343      27.825  -3.191 -26.361  1.00 13.60           O  
ANISOU 5836  O   ASP B 343     1459   2061   1649    204    233    -79       O  
ATOM   5837  CB  ASP B 343      30.159  -1.395 -27.588  1.00 17.21           C  
ANISOU 5837  CB  ASP B 343     1733   2701   2105    190    440    -68       C  
ATOM   5838  CG  ASP B 343      30.366  -0.802 -28.959  1.00 21.12           C  
ANISOU 5838  CG  ASP B 343     2538   3353   2135    360    591    -14       C  
ATOM   5839  OD1 ASP B 343      29.427  -0.277 -29.577  1.00 22.09           O  
ANISOU 5839  OD1 ASP B 343     3001   3554   1837    515    671    187       O  
ATOM   5840  OD2 ASP B 343      31.523  -0.951 -29.457  1.00 24.08           O  
ANISOU 5840  OD2 ASP B 343     2614   3969   2566    141    853     60       O  
ATOM   5841  N   PRO B 344      28.773  -2.102 -24.673  1.00 13.79           N  
ANISOU 5841  N   PRO B 344     1578   2055   1605     61    155     61       N  
ATOM   5842  CA  PRO B 344      28.424  -3.156 -23.726  1.00 13.74           C  
ANISOU 5842  CA  PRO B 344     1674   2000   1546     25     59     52       C  
ATOM   5843  C   PRO B 344      26.937  -3.413 -23.622  1.00 13.15           C  
ANISOU 5843  C   PRO B 344     1677   1923   1397     43      5     40       C  
ATOM   5844  O   PRO B 344      26.528  -4.492 -23.189  1.00 14.53           O  
ANISOU 5844  O   PRO B 344     1796   1996   1730    160    -75    238       O  
ATOM   5845  CB  PRO B 344      29.018  -2.695 -22.376  1.00 14.50           C  
ANISOU 5845  CB  PRO B 344     1779   2018   1712     98    -18     23       C  
ATOM   5846  CG  PRO B 344      30.131  -1.768 -22.805  1.00 15.14           C  
ANISOU 5846  CG  PRO B 344     1838   2153   1761     57     -1    104       C  
ATOM   5847  CD  PRO B 344      29.601  -1.061 -24.053  1.00 14.60           C  
ANISOU 5847  CD  PRO B 344     1758   2138   1650     57     72     45       C  
ATOM   5848  N   LEU B 345      26.061  -2.463 -23.986  1.00 13.13           N  
ANISOU 5848  N   LEU B 345     1556   1968   1467     45    124     25       N  
ATOM   5849  CA  LEU B 345      24.619  -2.647 -23.917  1.00 12.45           C  
ANISOU 5849  CA  LEU B 345     1530   1849   1353    -12    198     22       C  
ATOM   5850  C   LEU B 345      24.066  -3.391 -25.121  1.00 12.79           C  
ANISOU 5850  C   LEU B 345     1568   1829   1464     52    167    -73       C  
ATOM   5851  O   LEU B 345      22.918  -3.863 -25.079  1.00 13.83           O  
ANISOU 5851  O   LEU B 345     1578   1992   1684    -87    228   -141       O  
ATOM   5852  CB  LEU B 345      23.914  -1.283 -23.837  1.00 13.35           C  
ANISOU 5852  CB  LEU B 345     1783   1856   1434    130    282   -163       C  
ATOM   5853  CG  LEU B 345      24.364  -0.366 -22.693  1.00 12.88           C  
ANISOU 5853  CG  LEU B 345     1541   2017   1335     73    276    -60       C  
ATOM   5854  CD1 LEU B 345      23.625   0.985 -22.757  1.00 15.19           C  
ANISOU 5854  CD1 LEU B 345     2074   2129   1570    279     75   -105       C  
ATOM   5855  CD2 LEU B 345      24.196  -0.965 -21.306  1.00 13.86           C  
ANISOU 5855  CD2 LEU B 345     1829   2010   1427    136    289     57       C  
ATOM   5856  N   ILE B 346      24.806  -3.452 -26.235  1.00 12.36           N  
ANISOU 5856  N   ILE B 346     1512   1729   1455    140    163   -247       N  
ATOM   5857  CA  ILE B 346      24.295  -3.972 -27.495  1.00 12.95           C  
ANISOU 5857  CA  ILE B 346     1556   1781   1583     18     94   -232       C  
ATOM   5858  C   ILE B 346      24.682  -5.426 -27.675  1.00 14.10           C  
ANISOU 5858  C   ILE B 346     1679   1865   1812    159    184   -364       C  
ATOM   5859  O   ILE B 346      25.887  -5.738 -27.822  1.00 16.69           O  
ANISOU 5859  O   ILE B 346     1674   2230   2436    244    135   -313       O  
ATOM   5860  CB  ILE B 346      24.821  -3.123 -28.684  1.00 14.43           C  
ANISOU 5860  CB  ILE B 346     1877   2137   1471     93     45   -215       C  
ATOM   5861  CG1 ILE B 346      24.393  -1.659 -28.524  1.00 14.12           C  
ANISOU 5861  CG1 ILE B 346     1829   2014   1522   -144     90   -127       C  
ATOM   5862  CG2 ILE B 346      24.332  -3.679 -30.017  1.00 15.96           C  
ANISOU 5862  CG2 ILE B 346     2050   2327   1689    105   -106   -394       C  
ATOM   5863  CD1 ILE B 346      25.060  -0.690 -29.502  1.00 16.73           C  
ANISOU 5863  CD1 ILE B 346     2251   2171   1933   -239    132    164       C  
ATOM   5864  N   THR B 347      23.695  -6.329 -27.643  1.00 13.69           N  
ANISOU 5864  N   THR B 347     1728   1732   1743    209    227   -154       N  
ATOM   5865  CA  THR B 347      23.976  -7.751 -27.839  1.00 14.72           C  
ANISOU 5865  CA  THR B 347     1864   1857   1874    312    145   -202       C  
ATOM   5866  C   THR B 347      23.602  -8.211 -29.252  1.00 15.15           C  
ANISOU 5866  C   THR B 347     1950   1959   1847    336    217   -353       C  
ATOM   5867  O   THR B 347      24.101  -9.289 -29.664  1.00 17.04           O  
ANISOU 5867  O   THR B 347     2041   2111   2324    289    304   -427       O  
ATOM   5868  CB  THR B 347      23.257  -8.608 -26.786  1.00 15.86           C  
ANISOU 5868  CB  THR B 347     1828   2044   2154    194    212   -110       C  
ATOM   5869  OG1 THR B 347      21.839  -8.279 -26.754  1.00 15.27           O  
ANISOU 5869  OG1 THR B 347     1777   1952   2072    162    389   -108       O  
ATOM   5870  CG2 THR B 347      23.797  -8.349 -25.387  1.00 17.30           C  
ANISOU 5870  CG2 THR B 347     2035   2453   2084    412    272     -1       C  
ATOM   5871  N   HIS B 348      22.717  -7.497 -29.951  1.00 14.60           N  
ANISOU 5871  N   HIS B 348     1626   2204   1717    170    175   -514       N  
ATOM   5872  CA  HIS B 348      22.180  -7.910 -31.248  1.00 15.92           C  
ANISOU 5872  CA  HIS B 348     1897   2332   1820    124    200   -693       C  
ATOM   5873  C   HIS B 348      21.887  -6.703 -32.145  1.00 16.44           C  
ANISOU 5873  C   HIS B 348     1955   2498   1794    126    212   -617       C  
ATOM   5874  O   HIS B 348      21.456  -5.665 -31.590  1.00 15.88           O  
ANISOU 5874  O   HIS B 348     1795   2520   1720    215    139   -648       O  
ATOM   5875  CB  HIS B 348      20.887  -8.711 -31.050  1.00 17.46           C  
ANISOU 5875  CB  HIS B 348     2043   2474   2118     35    252   -655       C  
ATOM   5876  CG  HIS B 348      20.956  -9.976 -30.281  1.00 19.38           C  
ANISOU 5876  CG  HIS B 348     2272   2336   2757    -72    150   -551       C  
ATOM   5877  ND1 HIS B 348      21.011 -10.023 -28.900  1.00 19.47           N  
ANISOU 5877  ND1 HIS B 348     2254   2322   2820    125    269   -368       N  
ATOM   5878  CD2 HIS B 348      21.080 -11.265 -30.716  1.00 20.24           C  
ANISOU 5878  CD2 HIS B 348     2311   2453   2925    149    163   -625       C  
ATOM   5879  CE1 HIS B 348      21.164 -11.283 -28.495  1.00 20.83           C  
ANISOU 5879  CE1 HIS B 348     2505   2396   3014     57    378   -249       C  
ATOM   5880  NE2 HIS B 348      21.155 -12.056 -29.596  1.00 21.74           N  
ANISOU 5880  NE2 HIS B 348     2512   2658   3091     99    262   -443       N  
ATOM   5881  N   VAL B 349      22.159  -6.848 -33.440  1.00 17.23           N  
ANISOU 5881  N   VAL B 349     1951   2843   1751    367    152   -697       N  
ATOM   5882  CA  VAL B 349      21.889  -5.776 -34.418  1.00 17.11           C  
ANISOU 5882  CA  VAL B 349     1996   2667   1837    297     43   -677       C  
ATOM   5883  C   VAL B 349      21.131  -6.448 -35.569  1.00 18.11           C  
ANISOU 5883  C   VAL B 349     2042   2956   1882    327    -37   -775       C  
ATOM   5884  O   VAL B 349      21.751  -7.290 -36.248  1.00 23.09           O  
ANISOU 5884  O   VAL B 349     2472   3844   2457    774   -196  -1291       O  
ATOM   5885  CB  VAL B 349      23.113  -4.992 -34.941  1.00 18.67           C  
ANISOU 5885  CB  VAL B 349     2105   3196   1793    269    153   -499       C  
ATOM   5886  CG1 VAL B 349      22.690  -3.911 -35.936  1.00 21.87           C  
ANISOU 5886  CG1 VAL B 349     2639   3314   2356    286     48   -242       C  
ATOM   5887  CG2 VAL B 349      23.851  -4.318 -33.783  1.00 19.32           C  
ANISOU 5887  CG2 VAL B 349     2280   3234   1828    126     29   -398       C  
ATOM   5888  N   LEU B 350      19.854  -6.155 -35.767  1.00 15.80           N  
ANISOU 5888  N   LEU B 350     1989   2454   1561    298     -7   -658       N  
ATOM   5889  CA  LEU B 350      18.997  -6.819 -36.762  1.00 15.41           C  
ANISOU 5889  CA  LEU B 350     2093   2099   1665    127    -73   -396       C  
ATOM   5890  C   LEU B 350      18.327  -5.828 -37.681  1.00 14.61           C  
ANISOU 5890  C   LEU B 350     1800   2107   1645     62    -30   -343       C  
ATOM   5891  O   LEU B 350      18.055  -4.702 -37.275  1.00 14.70           O  
ANISOU 5891  O   LEU B 350     1977   2025   1583    -22     87   -357       O  
ATOM   5892  CB  LEU B 350      17.848  -7.548 -36.014  1.00 15.59           C  
ANISOU 5892  CB  LEU B 350     2121   1989   1812    181   -139   -301       C  
ATOM   5893  CG  LEU B 350      18.288  -8.600 -34.981  1.00 18.13           C  
ANISOU 5893  CG  LEU B 350     2883   2180   1827    189     26   -102       C  
ATOM   5894  CD1 LEU B 350      17.048  -9.226 -34.346  1.00 18.70           C  
ANISOU 5894  CD1 LEU B 350     3016   2158   1930   -135   -157   -128       C  
ATOM   5895  CD2 LEU B 350      19.220  -9.645 -35.589  1.00 20.51           C  
ANISOU 5895  CD2 LEU B 350     3210   2550   2034    540     20     35       C  
ATOM   5896  N   PRO B 351      17.925  -6.230 -38.891  1.00 13.97           N  
ANISOU 5896  N   PRO B 351     2068   1849   1392    129    140   -364       N  
ATOM   5897  CA  PRO B 351      17.091  -5.353 -39.720  1.00 14.33           C  
ANISOU 5897  CA  PRO B 351     1891   2179   1373    236    135   -275       C  
ATOM   5898  C   PRO B 351      15.749  -5.133 -39.025  1.00 13.06           C  
ANISOU 5898  C   PRO B 351     1788   1801   1375    -13    136   -161       C  
ATOM   5899  O   PRO B 351      15.227  -6.014 -38.332  1.00 13.41           O  
ANISOU 5899  O   PRO B 351     1804   1805   1487    -47     25   -233       O  
ATOM   5900  CB  PRO B 351      16.900  -6.137 -41.040  1.00 14.99           C  
ANISOU 5900  CB  PRO B 351     2085   2138   1473    110    162   -343       C  
ATOM   5901  CG  PRO B 351      17.428  -7.488 -40.777  1.00 19.36           C  
ANISOU 5901  CG  PRO B 351     3056   2249   2052    125   -403   -325       C  
ATOM   5902  CD  PRO B 351      18.217  -7.548 -39.503  1.00 15.87           C  
ANISOU 5902  CD  PRO B 351     2342   1951   1738    258      4   -366       C  
ATOM   5903  N   PHE B 352      15.168  -3.963 -39.306  1.00 12.86           N  
ANISOU 5903  N   PHE B 352     1700   1757   1430    138    243   -275       N  
ATOM   5904  CA  PHE B 352      13.840  -3.605 -38.794  1.00 13.43           C  
ANISOU 5904  CA  PHE B 352     1635   1863   1605     64     89   -248       C  
ATOM   5905  C   PHE B 352      12.770  -4.647 -39.074  1.00 14.33           C  
ANISOU 5905  C   PHE B 352     1711   1937   1799    -21    123   -170       C  
ATOM   5906  O   PHE B 352      11.879  -4.850 -38.244  1.00 15.32           O  
ANISOU 5906  O   PHE B 352     1775   1880   2167   -110    344   -251       O  
ATOM   5907  CB  PHE B 352      13.420  -2.239 -39.375  1.00 13.92           C  
ANISOU 5907  CB  PHE B 352     1763   1907   1621     87    155    -98       C  
ATOM   5908  CG  PHE B 352      12.038  -1.794 -38.986  1.00 13.63           C  
ANISOU 5908  CG  PHE B 352     1711   1928   1539      3    142     -9       C  
ATOM   5909  CD1 PHE B 352      11.750  -1.467 -37.658  1.00 14.95           C  
ANISOU 5909  CD1 PHE B 352     1948   2096   1635    157    196    -59       C  
ATOM   5910  CD2 PHE B 352      11.000  -1.731 -39.887  1.00 15.56           C  
ANISOU 5910  CD2 PHE B 352     1881   2069   1963    -46    -96   -307       C  
ATOM   5911  CE1 PHE B 352      10.473  -1.079 -37.296  1.00 15.25           C  
ANISOU 5911  CE1 PHE B 352     1980   1961   1854     11    381    129       C  
ATOM   5912  CE2 PHE B 352       9.729  -1.317 -39.533  1.00 17.93           C  
ANISOU 5912  CE2 PHE B 352     2066   2434   2311     94   -100   -225       C  
ATOM   5913  CZ  PHE B 352       9.459  -1.023 -38.213  1.00 16.85           C  
ANISOU 5913  CZ  PHE B 352     1883   2174   2347   -107    229    103       C  
ATOM   5914  N   GLU B 353      12.842  -5.315 -40.238  1.00 14.68           N  
ANISOU 5914  N   GLU B 353     1930   1967   1681     22      7   -213       N  
ATOM   5915  CA  GLU B 353      11.888  -6.349 -40.638  1.00 16.43           C  
ANISOU 5915  CA  GLU B 353     2232   1973   2038    -18   -308     11       C  
ATOM   5916  C   GLU B 353      11.880  -7.503 -39.638  1.00 15.02           C  
ANISOU 5916  C   GLU B 353     2036   1860   1813    -60   -140   -134       C  
ATOM   5917  O   GLU B 353      10.936  -8.310 -39.668  1.00 18.05           O  
ANISOU 5917  O   GLU B 353     2204   2125   2529   -204   -318    -17       O  
ATOM   5918  CB AGLU B 353      12.241  -6.728 -42.092  0.68 16.40           C  
ANISOU 5918  CB AGLU B 353     2271   2125   1837    101   -204    304       C  
ATOM   5919  CG AGLU B 353      12.063  -5.695 -43.209  0.68 13.92           C  
ANISOU 5919  CG AGLU B 353     1779   1984   1525    -67    -82    223       C  
ATOM   5920  CD AGLU B 353      13.086  -4.586 -43.331  0.68 12.27           C  
ANISOU 5920  CD AGLU B 353     1842   1766   1053     46     92    145       C  
ATOM   5921  OE1AGLU B 353      14.212  -4.736 -42.769  0.68 13.23           O  
ANISOU 5921  OE1AGLU B 353     1773   1752   1504     18    -89    154       O  
ATOM   5922  OE2AGLU B 353      12.765  -3.540 -44.023  0.68 12.34           O  
ANISOU 5922  OE2AGLU B 353     1802   1770   1117    -17     33    213       O  
ATOM   5923  CB BGLU B 353      11.948  -6.909 -42.055  0.42 18.76           C  
ANISOU 5923  CB BGLU B 353     2589   2528   2012   -116     26     33       C  
ATOM   5924  CG BGLU B 353      11.481  -8.282 -42.419  0.42 20.83           C  
ANISOU 5924  CG BGLU B 353     2882   2624   2409   -196     81    -43       C  
ATOM   5925  CD BGLU B 353      10.095  -8.689 -42.822  0.42 21.05           C  
ANISOU 5925  CD BGLU B 353     2793   2875   2330   -275    282    255       C  
ATOM   5926  OE1BGLU B 353       9.747  -8.398 -44.006  0.42 21.87           O  
ANISOU 5926  OE1BGLU B 353     3144   2825   2342   -112     95     68       O  
ATOM   5927  OE2BGLU B 353       9.327  -9.304 -42.017  0.42 15.80           O  
ANISOU 5927  OE2BGLU B 353     2852   1749   1401   -112     -3    169       O  
ATOM   5928  N   LYS B 354      12.893  -7.664 -38.755  1.00 13.98           N  
ANISOU 5928  N   LYS B 354     2061   1653   1597     68    -55   -235       N  
ATOM   5929  CA  LYS B 354      12.993  -8.680 -37.730  1.00 13.99           C  
ANISOU 5929  CA  LYS B 354     1948   1981   1387     64    -17   -233       C  
ATOM   5930  C   LYS B 354      12.553  -8.147 -36.342  1.00 14.26           C  
ANISOU 5930  C   LYS B 354     1949   1839   1632    -92     97   -275       C  
ATOM   5931  O   LYS B 354      12.942  -8.736 -35.313  1.00 14.23           O  
ANISOU 5931  O   LYS B 354     1740   2117   1550    -68    290   -336       O  
ATOM   5932  CB  LYS B 354      14.393  -9.306 -37.657  1.00 14.94           C  
ANISOU 5932  CB  LYS B 354     2273   1983   1419    304     94    -64       C  
ATOM   5933  CG  LYS B 354      14.774 -10.122 -38.909  1.00 14.58           C  
ANISOU 5933  CG  LYS B 354     2311   2074   1153    280    176    160       C  
ATOM   5934  CD  LYS B 354      16.118 -10.812 -38.714  1.00 17.55           C  
ANISOU 5934  CD  LYS B 354     2516   2458   1693    488    116    -59       C  
ATOM   5935  CE  LYS B 354      16.745 -11.409 -39.961  1.00 18.55           C  
ANISOU 5935  CE  LYS B 354     2850   2231   1966    308    304   -165       C  
ATOM   5936  NZ  LYS B 354      15.817 -12.442 -40.509  1.00 17.98           N  
ANISOU 5936  NZ  LYS B 354     3047   2209   1575    133    243    -32       N  
ATOM   5937  N   ILE B 355      11.696  -7.121 -36.275  1.00 13.65           N  
ANISOU 5937  N   ILE B 355     1650   1986   1549   -117     33   -393       N  
ATOM   5938  CA  ILE B 355      11.253  -6.580 -34.974  1.00 14.15           C  
ANISOU 5938  CA  ILE B 355     1709   1984   1684   -111     38   -500       C  
ATOM   5939  C   ILE B 355      10.674  -7.671 -34.092  1.00 14.81           C  
ANISOU 5939  C   ILE B 355     2016   1847   1765   -135    -11   -531       C  
ATOM   5940  O   ILE B 355      10.982  -7.684 -32.877  1.00 14.56           O  
ANISOU 5940  O   ILE B 355     1900   2021   1613   -242    185   -310       O  
ATOM   5941  CB  ILE B 355      10.299  -5.395 -35.184  1.00 14.61           C  
ANISOU 5941  CB  ILE B 355     1728   2151   1674    -40      3   -450       C  
ATOM   5942  CG1 ILE B 355       9.867  -4.796 -33.829  1.00 14.48           C  
ANISOU 5942  CG1 ILE B 355     1552   2130   1819    143     74   -460       C  
ATOM   5943  CG2 ILE B 355       9.058  -5.764 -35.998  1.00 16.63           C  
ANISOU 5943  CG2 ILE B 355     1935   2423   1959     35   -194   -532       C  
ATOM   5944  CD1 ILE B 355       9.259  -3.408 -33.920  1.00 15.44           C  
ANISOU 5944  CD1 ILE B 355     2019   2069   1777    209     45   -401       C  
ATOM   5945  N   ASN B 356       9.782  -8.541 -34.575  1.00 15.13           N  
ANISOU 5945  N   ASN B 356     1947   2062   1742   -314    162   -504       N  
ATOM   5946  CA  ASN B 356       9.186  -9.544 -33.700  1.00 15.45           C  
ANISOU 5946  CA  ASN B 356     1890   2059   1920   -318    177   -477       C  
ATOM   5947  C   ASN B 356      10.205 -10.500 -33.090  1.00 15.43           C  
ANISOU 5947  C   ASN B 356     2125   1974   1763   -289    191   -350       C  
ATOM   5948  O   ASN B 356      10.162 -10.856 -31.880  1.00 15.97           O  
ANISOU 5948  O   ASN B 356     2047   2157   1865   -350    246   -347       O  
ATOM   5949  CB  ASN B 356       8.053 -10.302 -34.379  1.00 16.39           C  
ANISOU 5949  CB  ASN B 356     2003   2142   2084   -408    -17   -484       C  
ATOM   5950  CG  ASN B 356       6.810  -9.453 -34.570  1.00 17.15           C  
ANISOU 5950  CG  ASN B 356     2080   2291   2145   -258    176   -553       C  
ATOM   5951  OD1 ASN B 356       6.357  -8.810 -33.580  1.00 18.03           O  
ANISOU 5951  OD1 ASN B 356     1893   2678   2278   -301    185   -790       O  
ATOM   5952  ND2 ASN B 356       6.261  -9.362 -35.758  1.00 19.18           N  
ANISOU 5952  ND2 ASN B 356     2064   2915   2308   -275    115   -604       N  
ATOM   5953  N   GLU B 357      11.179 -10.955 -33.899  1.00 15.57           N  
ANISOU 5953  N   GLU B 357     2174   1876   1867   -205    211   -372       N  
ATOM   5954  CA  GLU B 357      12.280 -11.779 -33.412  1.00 16.06           C  
ANISOU 5954  CA  GLU B 357     2280   2071   1752   -110    134   -343       C  
ATOM   5955  C   GLU B 357      13.064 -11.055 -32.326  1.00 15.67           C  
ANISOU 5955  C   GLU B 357     2181   1976   1797    -64    144   -252       C  
ATOM   5956  O   GLU B 357      13.508 -11.649 -31.335  1.00 15.11           O  
ANISOU 5956  O   GLU B 357     2203   1773   1766    -78    141   -386       O  
ATOM   5957  CB AGLU B 357      13.181 -12.185 -34.594  0.72 16.00           C  
ANISOU 5957  CB AGLU B 357     2518   1927   1632    -47    169   -365       C  
ATOM   5958  CG AGLU B 357      12.535 -13.033 -35.687  0.72 15.81           C  
ANISOU 5958  CG AGLU B 357     2381   1872   1752    -64    164   -406       C  
ATOM   5959  CD AGLU B 357      11.787 -12.334 -36.783  0.72 16.64           C  
ANISOU 5959  CD AGLU B 357     2379   2126   1817    -87    219   -267       C  
ATOM   5960  OE1AGLU B 357      11.293 -11.204 -36.714  0.72 15.67           O  
ANISOU 5960  OE1AGLU B 357     2494   2057   1401    -57    274   -224       O  
ATOM   5961  OE2AGLU B 357      11.591 -12.978 -37.873  0.72 19.93           O  
ANISOU 5961  OE2AGLU B 357     3290   2198   2085    131    -98   -495       O  
ATOM   5962  CB BGLU B 357      13.268 -12.113 -34.540  0.28 17.00           C  
ANISOU 5962  CB BGLU B 357     2399   2208   1852    -43    175   -338       C  
ATOM   5963  CG BGLU B 357      14.530 -12.845 -34.114  0.28 19.48           C  
ANISOU 5963  CG BGLU B 357     2637   2443   2320     32    -94   -226       C  
ATOM   5964  CD BGLU B 357      15.454 -13.180 -35.267  0.28 21.45           C  
ANISOU 5964  CD BGLU B 357     2835   2735   2580    114     89   -187       C  
ATOM   5965  OE1BGLU B 357      14.925 -13.302 -36.391  0.28 23.28           O  
ANISOU 5965  OE1BGLU B 357     3237   3038   2569    182     19   -101       O  
ATOM   5966  OE2BGLU B 357      16.692 -13.328 -35.154  0.28 21.96           O  
ANISOU 5966  OE2BGLU B 357     2855   2792   2697    184     94   -152       O  
ATOM   5967  N   GLY B 358      13.272  -9.761 -32.498  1.00 14.53           N  
ANISOU 5967  N   GLY B 358     1906   1938   1678   -147    159   -374       N  
ATOM   5968  CA  GLY B 358      13.948  -8.938 -31.486  1.00 14.11           C  
ANISOU 5968  CA  GLY B 358     1692   1850   1819   -110     63   -330       C  
ATOM   5969  C   GLY B 358      13.204  -8.866 -30.153  1.00 14.43           C  
ANISOU 5969  C   GLY B 358     1910   1841   1732    -43    -84   -406       C  
ATOM   5970  O   GLY B 358      13.806  -8.924 -29.079  1.00 14.18           O  
ANISOU 5970  O   GLY B 358     1802   1893   1692    -63    102   -211       O  
ATOM   5971  N   PHE B 359      11.870  -8.738 -30.219  1.00 14.73           N  
ANISOU 5971  N   PHE B 359     1860   1952   1787    -75    151   -469       N  
ATOM   5972  CA  PHE B 359      11.066  -8.792 -28.983  1.00 14.99           C  
ANISOU 5972  CA  PHE B 359     1821   2147   1726     -1     73   -399       C  
ATOM   5973  C   PHE B 359      11.141 -10.167 -28.335  1.00 15.79           C  
ANISOU 5973  C   PHE B 359     1962   2231   1807    103     -8   -350       C  
ATOM   5974  O   PHE B 359      11.184 -10.275 -27.095  1.00 16.13           O  
ANISOU 5974  O   PHE B 359     1981   2294   1852     30    225   -167       O  
ATOM   5975  CB  PHE B 359       9.617  -8.326 -29.187  1.00 14.39           C  
ANISOU 5975  CB  PHE B 359     1699   2031   1736   -125    189   -425       C  
ATOM   5976  CG  PHE B 359       9.496  -6.810 -29.168  1.00 14.15           C  
ANISOU 5976  CG  PHE B 359     1739   1927   1710   -140    191   -294       C  
ATOM   5977  CD1 PHE B 359       9.832  -6.012 -30.242  1.00 14.51           C  
ANISOU 5977  CD1 PHE B 359     1747   2117   1647    -58    176   -274       C  
ATOM   5978  CD2 PHE B 359       9.006  -6.208 -27.995  1.00 15.20           C  
ANISOU 5978  CD2 PHE B 359     2030   2000   1744    -99    370   -183       C  
ATOM   5979  CE1 PHE B 359       9.723  -4.643 -30.176  1.00 15.04           C  
ANISOU 5979  CE1 PHE B 359     1990   2090   1632    -35    230   -332       C  
ATOM   5980  CE2 PHE B 359       8.908  -4.835 -27.960  1.00 15.31           C  
ANISOU 5980  CE2 PHE B 359     2034   1996   1786    -67    370   -293       C  
ATOM   5981  CZ  PHE B 359       9.238  -4.021 -29.023  1.00 15.22           C  
ANISOU 5981  CZ  PHE B 359     1876   2084   1824      6    422   -224       C  
ATOM   5982  N   ASP B 360      11.153 -11.233 -29.147  1.00 15.98           N  
ANISOU 5982  N   ASP B 360     2096   2075   1901   -142    192   -269       N  
ATOM   5983  CA  ASP B 360      11.268 -12.573 -28.541  1.00 17.31           C  
ANISOU 5983  CA  ASP B 360     2377   2204   1995   -156     71   -197       C  
ATOM   5984  C   ASP B 360      12.598 -12.755 -27.822  1.00 16.54           C  
ANISOU 5984  C   ASP B 360     2280   1938   2067   -128    188   -154       C  
ATOM   5985  O   ASP B 360      12.648 -13.399 -26.760  1.00 17.05           O  
ANISOU 5985  O   ASP B 360     2531   1866   2081    -86   -163   -240       O  
ATOM   5986  CB  ASP B 360      11.038 -13.667 -29.582  1.00 20.84           C  
ANISOU 5986  CB  ASP B 360     2951   2310   2656   -418    -50   -402       C  
ATOM   5987  CG  ASP B 360       9.586 -13.795 -30.036  1.00 24.94           C  
ANISOU 5987  CG  ASP B 360     3152   2927   3397   -388   -267     -2       C  
ATOM   5988  OD1 ASP B 360       8.648 -13.364 -29.362  1.00 25.83           O  
ANISOU 5988  OD1 ASP B 360     2881   2748   4186   -371   -292     85       O  
ATOM   5989  OD2 ASP B 360       9.430 -14.424 -31.107  1.00 29.04           O  
ANISOU 5989  OD2 ASP B 360     4104   3349   3583   -475   -734    -80       O  
ATOM   5990  N   LEU B 361      13.695 -12.179 -28.348  1.00 15.51           N  
ANISOU 5990  N   LEU B 361     2109   1911   1873    -70    249   -272       N  
ATOM   5991  CA  LEU B 361      14.988 -12.269 -27.676  1.00 16.06           C  
ANISOU 5991  CA  LEU B 361     2133   1955   2012     92    254   -191       C  
ATOM   5992  C   LEU B 361      14.913 -11.578 -26.318  1.00 15.90           C  
ANISOU 5992  C   LEU B 361     2083   1954   2003     98    141    -79       C  
ATOM   5993  O   LEU B 361      15.480 -12.039 -25.327  1.00 15.88           O  
ANISOU 5993  O   LEU B 361     2210   1710   2114     56     22   -161       O  
ATOM   5994  CB  LEU B 361      16.103 -11.608 -28.501  1.00 17.12           C  
ANISOU 5994  CB  LEU B 361     2196   2250   2060    -29    228   -257       C  
ATOM   5995  CG  LEU B 361      16.590 -12.339 -29.743  1.00 18.05           C  
ANISOU 5995  CG  LEU B 361     2376   2280   2202    136    248   -292       C  
ATOM   5996  CD1 LEU B 361      17.458 -11.439 -30.620  1.00 19.84           C  
ANISOU 5996  CD1 LEU B 361     2404   2672   2464    109    341    -94       C  
ATOM   5997  CD2 LEU B 361      17.399 -13.556 -29.314  1.00 20.17           C  
ANISOU 5997  CD2 LEU B 361     2790   2438   2437    323    226   -152       C  
ATOM   5998  N   LEU B 362      14.239 -10.415 -26.219  1.00 14.77           N  
ANISOU 5998  N   LEU B 362     1938   1879   1794     78    169   -303       N  
ATOM   5999  CA  LEU B 362      14.115  -9.725 -24.939  1.00 14.17           C  
ANISOU 5999  CA  LEU B 362     1833   1860   1693    -11    145   -137       C  
ATOM   6000  C   LEU B 362      13.298 -10.576 -23.960  1.00 14.56           C  
ANISOU 6000  C   LEU B 362     1845   1905   1782     42    161   -145       C  
ATOM   6001  O   LEU B 362      13.709 -10.784 -22.812  1.00 15.86           O  
ANISOU 6001  O   LEU B 362     2007   2063   1954    -91      8    -69       O  
ATOM   6002  CB  LEU B 362      13.426  -8.371 -25.138  1.00 14.11           C  
ANISOU 6002  CB  LEU B 362     1890   1900   1571     -6    160   -124       C  
ATOM   6003  CG  LEU B 362      13.244  -7.520 -23.864  1.00 14.88           C  
ANISOU 6003  CG  LEU B 362     2048   2097   1510    104    243    -75       C  
ATOM   6004  CD1 LEU B 362      14.552  -7.024 -23.299  1.00 16.20           C  
ANISOU 6004  CD1 LEU B 362     2273   1950   1932   -198    167    -85       C  
ATOM   6005  CD2 LEU B 362      12.275  -6.377 -24.137  1.00 17.39           C  
ANISOU 6005  CD2 LEU B 362     2487   2203   1918    280    437     -9       C  
ATOM   6006  N   ARG B 363      12.131 -11.052 -24.406  1.00 15.22           N  
ANISOU 6006  N   ARG B 363     1912   1941   1932    -88    193   -193       N  
ATOM   6007  CA  ARG B 363      11.256 -11.832 -23.523  1.00 16.63           C  
ANISOU 6007  CA  ARG B 363     2140   2103   2074   -135    209    -95       C  
ATOM   6008  C   ARG B 363      11.869 -13.126 -23.019  1.00 18.51           C  
ANISOU 6008  C   ARG B 363     2549   2197   2288    -76    202     64       C  
ATOM   6009  O   ARG B 363      11.538 -13.555 -21.897  1.00 19.90           O  
ANISOU 6009  O   ARG B 363     2943   2211   2406   -100    254    213       O  
ATOM   6010  CB  ARG B 363       9.923 -12.128 -24.237  1.00 17.64           C  
ANISOU 6010  CB  ARG B 363     2250   2233   2220   -258     94    -76       C  
ATOM   6011  CG  ARG B 363       9.102 -10.881 -24.563  1.00 18.52           C  
ANISOU 6011  CG  ARG B 363     2292   2251   2493   -190    101    -93       C  
ATOM   6012  CD  ARG B 363       8.031 -11.219 -25.616  1.00 21.74           C  
ANISOU 6012  CD  ARG B 363     2655   2524   3080   -141   -288    -86       C  
ATOM   6013  NE  ARG B 363       7.338 -10.013 -26.039  1.00 22.48           N  
ANISOU 6013  NE  ARG B 363     2853   2609   3079    -66   -281   -172       N  
ATOM   6014  CZ  ARG B 363       6.814  -9.757 -27.221  1.00 21.61           C  
ANISOU 6014  CZ  ARG B 363     2746   2758   2706   -118      4   -250       C  
ATOM   6015  NH1 ARG B 363       6.841 -10.662 -28.220  1.00 22.47           N  
ANISOU 6015  NH1 ARG B 363     2945   2687   2905   -232   -304   -368       N  
ATOM   6016  NH2 ARG B 363       6.218  -8.598 -27.437  1.00 20.63           N  
ANISOU 6016  NH2 ARG B 363     2821   2542   2475   -370     17   -225       N  
ATOM   6017  N   SER B 364      12.728 -13.756 -23.822  1.00 17.59           N  
ANISOU 6017  N   SER B 364     2539   1841   2303   -111     46    -98       N  
ATOM   6018  CA  SER B 364      13.360 -15.016 -23.411  1.00 19.00           C  
ANISOU 6018  CA  SER B 364     2601   2058   2561    -39   -156     39       C  
ATOM   6019  C   SER B 364      14.550 -14.829 -22.495  1.00 19.43           C  
ANISOU 6019  C   SER B 364     2651   2188   2544    -11   -178    -25       C  
ATOM   6020  O   SER B 364      15.081 -15.833 -21.993  1.00 21.82           O  
ANISOU 6020  O   SER B 364     3142   2048   3100   -135   -325      4       O  
ATOM   6021  CB  SER B 364      13.821 -15.794 -24.653  1.00 22.09           C  
ANISOU 6021  CB  SER B 364     3168   2319   2908     42    -11   -265       C  
ATOM   6022  OG  SER B 364      14.927 -15.117 -25.235  1.00 24.03           O  
ANISOU 6022  OG  SER B 364     3345   2645   3140    248    282   -100       O  
ATOM   6023  N   GLY B 365      14.988 -13.602 -22.217  1.00 18.66           N  
ANISOU 6023  N   GLY B 365     2488   2130   2471    -96    -37     59       N  
ATOM   6024  CA  GLY B 365      16.126 -13.353 -21.369  1.00 19.62           C  
ANISOU 6024  CA  GLY B 365     2742   2358   2355     48    -97     31       C  
ATOM   6025  C   GLY B 365      17.459 -13.367 -22.082  1.00 20.23           C  
ANISOU 6025  C   GLY B 365     2791   2377   2518   -108    -20    157       C  
ATOM   6026  O   GLY B 365      18.479 -13.170 -21.414  1.00 24.41           O  
ANISOU 6026  O   GLY B 365     2918   3491   2867   -145   -225    176       O  
ATOM   6027  N   GLU B 366      17.461 -13.512 -23.406  1.00 18.27           N  
ANISOU 6027  N   GLU B 366     2626   1815   2499    -50     94    -79       N  
ATOM   6028  CA  GLU B 366      18.703 -13.670 -24.159  1.00 21.64           C  
ANISOU 6028  CA  GLU B 366     2818   2339   3067     81    320   -129       C  
ATOM   6029  C   GLU B 366      19.387 -12.408 -24.636  1.00 21.42           C  
ANISOU 6029  C   GLU B 366     2748   2179   3211    282    259     26       C  
ATOM   6030  O   GLU B 366      20.518 -12.501 -25.185  1.00 25.96           O  
ANISOU 6030  O   GLU B 366     2820   2607   4436    305    500    106       O  
ATOM   6031  CB AGLU B 366      18.390 -14.589 -25.371  0.72 25.08           C  
ANISOU 6031  CB AGLU B 366     3236   3126   3166    125    150   -397       C  
ATOM   6032  CG AGLU B 366      18.054 -16.011 -24.958  0.72 30.07           C  
ANISOU 6032  CG AGLU B 366     4047   3402   3975    109    290    -77       C  
ATOM   6033  CD AGLU B 366      17.330 -16.905 -25.939  0.72 34.75           C  
ANISOU 6033  CD AGLU B 366     4606   4363   4234     38     40   -389       C  
ATOM   6034  OE1AGLU B 366      16.854 -16.499 -27.020  0.72 34.31           O  
ANISOU 6034  OE1AGLU B 366     5038   3917   4080    -66    -66   -699       O  
ATOM   6035  OE2AGLU B 366      17.178 -18.104 -25.585  0.72 37.28           O  
ANISOU 6035  OE2AGLU B 366     4938   4481   4747    -13     97   -267       O  
ATOM   6036  CB BGLU B 366      18.426 -14.542 -25.404  0.28 23.07           C  
ANISOU 6036  CB BGLU B 366     3200   2533   3034    -92     85    -41       C  
ATOM   6037  CG BGLU B 366      19.716 -15.221 -25.833  0.28 25.94           C  
ANISOU 6037  CG BGLU B 366     3320   3150   3387     88    139    -19       C  
ATOM   6038  CD BGLU B 366      19.787 -15.539 -27.309  0.28 27.18           C  
ANISOU 6038  CD BGLU B 366     3561   3371   3396    109     93    -36       C  
ATOM   6039  OE1BGLU B 366      18.858 -16.224 -27.780  0.28 27.79           O  
ANISOU 6039  OE1BGLU B 366     3605   3324   3630    107     49    -62       O  
ATOM   6040  OE2BGLU B 366      20.771 -15.101 -27.948  0.28 26.85           O  
ANISOU 6040  OE2BGLU B 366     3517   3219   3466    120     76    -56       O  
ATOM   6041  N   SER B 367      18.735 -11.258 -24.647  1.00 16.57           N  
ANISOU 6041  N   SER B 367     2364   1803   2130     49    216   -216       N  
ATOM   6042  CA  SER B 367      19.351 -10.018 -25.106  1.00 14.93           C  
ANISOU 6042  CA  SER B 367     1989   1869   1816     45    145   -281       C  
ATOM   6043  C   SER B 367      19.341  -8.965 -23.977  1.00 13.41           C  
ANISOU 6043  C   SER B 367     1799   1677   1619     69     76   -139       C  
ATOM   6044  O   SER B 367      18.622  -9.054 -22.979  1.00 13.94           O  
ANISOU 6044  O   SER B 367     1917   1758   1623     62    146   -157       O  
ATOM   6045  CB  SER B 367      18.575  -9.446 -26.295  1.00 15.21           C  
ANISOU 6045  CB  SER B 367     2024   1966   1788    201    200   -390       C  
ATOM   6046  OG  SER B 367      17.218  -9.291 -25.869  1.00 15.24           O  
ANISOU 6046  OG  SER B 367     1863   1924   2004     -7     70   -333       O  
ATOM   6047  N   ILE B 368      20.212  -7.985 -24.198  1.00 12.96           N  
ANISOU 6047  N   ILE B 368     1680   1574   1671    124    144   -109       N  
ATOM   6048  CA  ILE B 368      20.202  -6.711 -23.443  1.00 12.03           C  
ANISOU 6048  CA  ILE B 368     1462   1507   1602    223    134   -145       C  
ATOM   6049  C   ILE B 368      19.488  -5.768 -24.423  1.00 11.83           C  
ANISOU 6049  C   ILE B 368     1452   1607   1437    114    193   -164       C  
ATOM   6050  O   ILE B 368      18.241  -5.781 -24.441  1.00 12.61           O  
ANISOU 6050  O   ILE B 368     1489   1780   1522     75     69   -130       O  
ATOM   6051  CB  ILE B 368      21.577  -6.259 -22.992  1.00 11.97           C  
ANISOU 6051  CB  ILE B 368     1493   1560   1496    207    125   -158       C  
ATOM   6052  CG1 ILE B 368      22.217  -7.323 -22.072  1.00 14.12           C  
ANISOU 6052  CG1 ILE B 368     1748   1772   1845    191      0     -8       C  
ATOM   6053  CG2 ILE B 368      21.501  -4.889 -22.308  1.00 12.04           C  
ANISOU 6053  CG2 ILE B 368     1440   1726   1411    111    128   -222       C  
ATOM   6054  CD1 ILE B 368      21.491  -7.549 -20.773  1.00 16.66           C  
ANISOU 6054  CD1 ILE B 368     1915   2368   2047    -13     46    256       C  
ATOM   6055  N   ARG B 369      20.201  -5.040 -25.291  1.00 11.90           N  
ANISOU 6055  N   ARG B 369     1414   1574   1534    103    174    -40       N  
ATOM   6056  CA  ARG B 369      19.566  -4.263 -26.338  1.00 12.46           C  
ANISOU 6056  CA  ARG B 369     1586   1718   1433    150     79    -88       C  
ATOM   6057  C   ARG B 369      19.819  -4.888 -27.711  1.00 12.97           C  
ANISOU 6057  C   ARG B 369     1502   1861   1563    157    147   -179       C  
ATOM   6058  O   ARG B 369      20.981  -5.144 -28.116  1.00 13.94           O  
ANISOU 6058  O   ARG B 369     1545   2060   1692    165    218   -124       O  
ATOM   6059  CB  ARG B 369      20.045  -2.798 -26.339  1.00 12.03           C  
ANISOU 6059  CB  ARG B 369     1522   1761   1287     27     90   -157       C  
ATOM   6060  CG  ARG B 369      19.471  -1.962 -25.190  1.00 12.54           C  
ANISOU 6060  CG  ARG B 369     1521   1812   1431    241    155   -111       C  
ATOM   6061  CD  ARG B 369      17.978  -1.776 -25.378  1.00 12.39           C  
ANISOU 6061  CD  ARG B 369     1539   1764   1405    159     88    -68       C  
ATOM   6062  NE  ARG B 369      17.401  -0.619 -24.705  1.00 12.18           N  
ANISOU 6062  NE  ARG B 369     1507   1712   1408     57    277     28       N  
ATOM   6063  CZ  ARG B 369      16.732  -0.613 -23.544  1.00 11.71           C  
ANISOU 6063  CZ  ARG B 369     1508   1650   1291     39    113   -121       C  
ATOM   6064  NH1 ARG B 369      16.571  -1.698 -22.812  1.00 12.48           N  
ANISOU 6064  NH1 ARG B 369     1624   1793   1327    -25    132      0       N  
ATOM   6065  NH2 ARG B 369      16.203   0.544 -23.141  1.00 12.06           N  
ANISOU 6065  NH2 ARG B 369     1449   1791   1341     54    -42   -292       N  
ATOM   6066  N   THR B 370      18.724  -5.105 -28.433  1.00 12.18           N  
ANISOU 6066  N   THR B 370     1523   1685   1419     31    208   -124       N  
ATOM   6067  CA  THR B 370      18.720  -5.256 -29.883  1.00 12.30           C  
ANISOU 6067  CA  THR B 370     1545   1731   1398     96    258   -179       C  
ATOM   6068  C   THR B 370      18.523  -3.876 -30.512  1.00 12.81           C  
ANISOU 6068  C   THR B 370     1700   1672   1496     83    166   -241       C  
ATOM   6069  O   THR B 370      17.566  -3.166 -30.159  1.00 14.12           O  
ANISOU 6069  O   THR B 370     1844   1967   1552    261    203   -209       O  
ATOM   6070  CB  THR B 370      17.601  -6.196 -30.351  1.00 13.53           C  
ANISOU 6070  CB  THR B 370     1679   1862   1599    -60    257   -247       C  
ATOM   6071  OG1 THR B 370      17.881  -7.514 -29.880  1.00 15.25           O  
ANISOU 6071  OG1 THR B 370     1943   1839   2014     40    173   -400       O  
ATOM   6072  CG2 THR B 370      17.482  -6.216 -31.871  1.00 14.65           C  
ANISOU 6072  CG2 THR B 370     1913   2008   1646    -74    231   -488       C  
ATOM   6073  N   ILE B 371      19.419  -3.531 -31.447  1.00 12.86           N  
ANISOU 6073  N   ILE B 371     1520   2013   1352     99     98   -200       N  
ATOM   6074  CA  ILE B 371      19.246  -2.333 -32.266  1.00 12.81           C  
ANISOU 6074  CA  ILE B 371     1685   1883   1298     56    124   -302       C  
ATOM   6075  C   ILE B 371      18.676  -2.800 -33.622  1.00 12.52           C  
ANISOU 6075  C   ILE B 371     1702   1791   1266    120    111   -213       C  
ATOM   6076  O   ILE B 371      19.269  -3.679 -34.300  1.00 14.47           O  
ANISOU 6076  O   ILE B 371     1899   2199   1399    331     98   -403       O  
ATOM   6077  CB  ILE B 371      20.586  -1.592 -32.480  1.00 14.15           C  
ANISOU 6077  CB  ILE B 371     1654   2175   1547      3     42   -258       C  
ATOM   6078  CG1 ILE B 371      21.288  -1.313 -31.133  1.00 15.22           C  
ANISOU 6078  CG1 ILE B 371     1869   2200   1714     48   -154   -141       C  
ATOM   6079  CG2 ILE B 371      20.387  -0.358 -33.335  1.00 14.91           C  
ANISOU 6079  CG2 ILE B 371     1844   2118   1702    -67    127   -199       C  
ATOM   6080  CD1 ILE B 371      20.475  -0.487 -30.147  1.00 15.60           C  
ANISOU 6080  CD1 ILE B 371     1958   2434   1533    -49   -115   -245       C  
ATOM   6081  N   LEU B 372      17.551  -2.225 -34.018  1.00 12.74           N  
ANISOU 6081  N   LEU B 372     1621   1995   1225     61    114   -222       N  
ATOM   6082  CA  LEU B 372      16.958  -2.437 -35.331  1.00 12.40           C  
ANISOU 6082  CA  LEU B 372     1657   1776   1279    -31    -12   -255       C  
ATOM   6083  C   LEU B 372      17.389  -1.356 -36.306  1.00 12.85           C  
ANISOU 6083  C   LEU B 372     1680   1823   1381    -91    309   -274       C  
ATOM   6084  O   LEU B 372      17.329  -0.160 -35.996  1.00 13.58           O  
ANISOU 6084  O   LEU B 372     1996   1878   1286    -78    292   -271       O  
ATOM   6085  CB  LEU B 372      15.427  -2.384 -35.160  1.00 12.64           C  
ANISOU 6085  CB  LEU B 372     1680   1689   1435    -26     -3   -252       C  
ATOM   6086  CG  LEU B 372      14.782  -3.441 -34.248  1.00 13.14           C  
ANISOU 6086  CG  LEU B 372     1730   1817   1446     94     59   -101       C  
ATOM   6087  CD1 LEU B 372      13.296  -3.117 -34.100  1.00 14.17           C  
ANISOU 6087  CD1 LEU B 372     1741   1987   1656   -211    112   -125       C  
ATOM   6088  CD2 LEU B 372      14.988  -4.842 -34.780  1.00 14.72           C  
ANISOU 6088  CD2 LEU B 372     2038   1901   1653     16    182   -179       C  
ATOM   6089  N   THR B 373      17.859  -1.781 -37.492  1.00 13.29           N  
ANISOU 6089  N   THR B 373     1844   1950   1257    -85    223   -268       N  
ATOM   6090  CA  THR B 373      18.333  -0.842 -38.516  1.00 14.20           C  
ANISOU 6090  CA  THR B 373     1748   2129   1520    -66    240    -73       C  
ATOM   6091  C   THR B 373      17.362  -0.843 -39.700  1.00 14.21           C  
ANISOU 6091  C   THR B 373     1919   2073   1407    -30    231   -216       C  
ATOM   6092  O   THR B 373      16.967  -1.903 -40.200  1.00 15.01           O  
ANISOU 6092  O   THR B 373     1991   2087   1627    -15    233   -231       O  
ATOM   6093  CB  THR B 373      19.757  -1.156 -38.990  1.00 15.86           C  
ANISOU 6093  CB  THR B 373     1824   2476   1726   -158    321    -52       C  
ATOM   6094  OG1 THR B 373      19.833  -2.501 -39.457  1.00 18.73           O  
ANISOU 6094  OG1 THR B 373     2240   2653   2225    201    557   -214       O  
ATOM   6095  CG2 THR B 373      20.760  -1.068 -37.848  1.00 18.85           C  
ANISOU 6095  CG2 THR B 373     2015   3139   2007     78     98   -131       C  
ATOM   6096  N   PHE B 374      16.942   0.349 -40.126  1.00 15.19           N  
ANISOU 6096  N   PHE B 374     2206   2059   1507     29    288   -206       N  
ATOM   6097  CA  PHE B 374      16.039   0.482 -41.252  1.00 16.17           C  
ANISOU 6097  CA  PHE B 374     2234   2267   1642     91    210   -120       C  
ATOM   6098  C   PHE B 374      16.736   0.248 -42.610  1.00 16.42           C  
ANISOU 6098  C   PHE B 374     2323   2350   1565     82    203    -60       C  
ATOM   6099  O   PHE B 374      17.940   0.540 -42.704  1.00 18.25           O  
ANISOU 6099  O   PHE B 374     2585   2803   1546    -95    462   -362       O  
ATOM   6100  CB  PHE B 374      15.347   1.851 -41.188  1.00 16.41           C  
ANISOU 6100  CB  PHE B 374     2469   2106   1659     53    274    -86       C  
ATOM   6101  CG  PHE B 374      14.373   1.971 -40.031  1.00 17.71           C  
ANISOU 6101  CG  PHE B 374     2569   2238   1920    -13    468   -107       C  
ATOM   6102  CD1 PHE B 374      13.055   1.570 -40.172  1.00 17.83           C  
ANISOU 6102  CD1 PHE B 374     2520   2130   2125    167    413   -147       C  
ATOM   6103  CD2 PHE B 374      14.789   2.409 -38.772  1.00 19.11           C  
ANISOU 6103  CD2 PHE B 374     2792   2438   2032   -157    569   -336       C  
ATOM   6104  CE1 PHE B 374      12.171   1.654 -39.092  1.00 18.61           C  
ANISOU 6104  CE1 PHE B 374     2609   2195   2269   -166    521      1       C  
ATOM   6105  CE2 PHE B 374      13.906   2.475 -37.699  1.00 20.30           C  
ANISOU 6105  CE2 PHE B 374     2832   2734   2148   -192    572   -257       C  
ATOM   6106  CZ  PHE B 374      12.598   2.115 -37.867  1.00 19.92           C  
ANISOU 6106  CZ  PHE B 374     2827   2297   2446    -20    458   -242       C  
ATOM   6107  OXT PHE B 374      16.041  -0.252 -43.503  1.00 18.54           O  
ANISOU 6107  OXT PHE B 374     2411   3006   1625      6    172    -96       O  
TER    6108      PHE B 374                                                      
HETATM 6109 ZN    ZN A 400       7.624  14.247  21.319  1.00  8.87          ZN  
ANISOU 6109 ZN    ZN A 400     1159    934   1276   -172    187    143      ZN  
HETATM 6110 ZN    ZN A 401      25.622   6.279  17.430  1.00  7.81          ZN  
ANISOU 6110 ZN    ZN A 401      873   1058   1037    100     20    102      ZN  
HETATM 6111  PA  NAD A 402      -1.027  17.254  18.293  1.00  9.60           P  
ANISOU 6111  PA  NAD A 402     1178   1285   1187     87    219    382       P  
HETATM 6112  O1A NAD A 402      -0.885  18.416  19.202  1.00 12.15           O  
ANISOU 6112  O1A NAD A 402     1754   1505   1358    411    417    215       O  
HETATM 6113  O2A NAD A 402      -2.028  16.190  18.613  1.00 11.96           O  
ANISOU 6113  O2A NAD A 402     1155   1595   1792    -33     73    609       O  
HETATM 6114  O5B NAD A 402      -1.312  17.860  16.851  1.00 10.00           O  
ANISOU 6114  O5B NAD A 402     1193   1134   1471      2    -36    395       O  
HETATM 6115  C5B NAD A 402      -1.918  17.066  15.780  1.00 10.71           C  
ANISOU 6115  C5B NAD A 402     1268   1276   1525     47   -169    324       C  
HETATM 6116  C4B NAD A 402      -2.850  17.977  15.011  1.00  9.38           C  
ANISOU 6116  C4B NAD A 402     1156   1271   1137    206     67    234       C  
HETATM 6117  O4B NAD A 402      -3.420  17.151  13.920  1.00 10.03           O  
ANISOU 6117  O4B NAD A 402     1131   1417   1264     68     20    170       O  
HETATM 6118  C3B NAD A 402      -4.106  18.495  15.799  1.00 10.21           C  
ANISOU 6118  C3B NAD A 402     1158   1444   1279     88    149    179       C  
HETATM 6119  O3B NAD A 402      -4.125  19.953  15.817  1.00 10.69           O  
ANISOU 6119  O3B NAD A 402     1378   1459   1225    244     59     61       O  
HETATM 6120  C2B NAD A 402      -5.319  17.876  15.121  1.00 10.17           C  
ANISOU 6120  C2B NAD A 402     1028   1528   1309    109     72    229       C  
HETATM 6121  O2B NAD A 402      -6.505  18.600  15.120  1.00 11.35           O  
ANISOU 6121  O2B NAD A 402     1151   1759   1401    174    132    298       O  
HETATM 6122  C1B NAD A 402      -4.744  17.599  13.720  1.00  9.88           C  
ANISOU 6122  C1B NAD A 402     1051   1433   1269    125    -49    150       C  
HETATM 6123  O3  NAD A 402       0.373  16.508  18.142  1.00  8.17           O  
ANISOU 6123  O3  NAD A 402     1063    965   1077    -14    121    210       O  
HETATM 6124  PN  NAD A 402       1.935  17.001  18.240  1.00  7.92           P  
ANISOU 6124  PN  NAD A 402     1060    942   1007    -47    126    220       P  
HETATM 6125  O1N NAD A 402       2.383  16.899  19.643  1.00  9.02           O  
ANISOU 6125  O1N NAD A 402     1191   1201   1036    -12     72    179       O  
HETATM 6126  O2N NAD A 402       2.087  18.258  17.460  1.00  8.33           O  
ANISOU 6126  O2N NAD A 402     1117    983   1063    -10     94    239       O  
HETATM 6127  O5D NAD A 402       2.613  15.755  17.453  1.00  8.22           O  
ANISOU 6127  O5D NAD A 402     1176    971    974     17    145    255       O  
HETATM 6128  C5D NAD A 402       2.353  15.585  16.025  1.00  8.64           C  
ANISOU 6128  C5D NAD A 402     1298   1002    982    171    100    252       C  
HETATM 6129  C4D NAD A 402       2.795  14.245  15.581  1.00  8.80           C  
ANISOU 6129  C4D NAD A 402     1299    924   1122     36    200    255       C  
HETATM 6130  O4D NAD A 402       4.279  14.181  15.616  1.00  9.85           O  
ANISOU 6130  O4D NAD A 402     1359    963   1421     83    425    440       O  
HETATM 6131  C3D NAD A 402       2.317  13.064  16.506  1.00  8.47           C  
ANISOU 6131  C3D NAD A 402     1306    905   1006    -44     94    204       C  
HETATM 6132  O3D NAD A 402       1.993  11.909  15.715  1.00  8.73           O  
ANISOU 6132  O3D NAD A 402     1206    988   1122   -148    117    231       O  
HETATM 6133  C2D NAD A 402       3.580  12.729  17.329  1.00  8.25           C  
ANISOU 6133  C2D NAD A 402     1112    934   1088   -123    116    385       C  
HETATM 6134  O2D NAD A 402       3.564  11.408  17.795  1.00  8.61           O  
ANISOU 6134  O2D NAD A 402     1130    896   1246   -241    165    275       O  
HETATM 6135  C1D NAD A 402       4.699  12.961  16.248  1.00  8.46           C  
ANISOU 6135  C1D NAD A 402     1254    766   1193    -87    270    304       C  
HETATM 6136  N1N NAD A 402       6.079  13.142  16.789  1.00  9.00           N  
ANISOU 6136  N1N NAD A 402     1173    899   1346   -107    280     70       N  
HETATM 6137  C2N NAD A 402       7.134  12.746  15.918  1.00  8.10           C  
ANISOU 6137  C2N NAD A 402     1034    845   1201     33    297    187       C  
HETATM 6138  C3N NAD A 402       8.397  13.048  16.166  1.00  7.15           C  
ANISOU 6138  C3N NAD A 402     1019    686   1012     77     84    203       C  
HETATM 6139  C7N NAD A 402       9.498  12.592  15.241  1.00  7.22           C  
ANISOU 6139  C7N NAD A 402      871    775   1097   -120     89    261       C  
HETATM 6140  O7N NAD A 402      10.673  12.633  15.662  1.00  8.33           O  
ANISOU 6140  O7N NAD A 402     1058   1024   1084    -74    135    199       O  
HETATM 6141  N7N NAD A 402       9.190  12.197  14.000  1.00  8.40           N  
ANISOU 6141  N7N NAD A 402     1178   1041    972    -65     95    136       N  
HETATM 6142  C4N NAD A 402       8.787  13.879  17.365  1.00  9.12           C  
ANISOU 6142  C4N NAD A 402     1222   1133   1108     10     52    307       C  
HETATM 6143  C5N NAD A 402       7.629  14.757  17.730  1.00  9.33           C  
ANISOU 6143  C5N NAD A 402      889   1451   1207     93   -121    180       C  
HETATM 6144  C6N NAD A 402       6.352  14.155  17.730  1.00 10.84           C  
ANISOU 6144  C6N NAD A 402     1624    925   1571   -157    493      3       C  
HETATM 6145  N9AANAD A 402      -5.445  16.488  13.109  0.59 10.93           N  
ANISOU 6145  N9AANAD A 402     1204   1480   1470     69    -31    133       N  
HETATM 6146  C8AANAD A 402      -5.867  15.261  13.596  0.59 11.65           C  
ANISOU 6146  C8AANAD A 402     1306   1455   1666      5    -98     44       C  
HETATM 6147  N7AANAD A 402      -6.457  14.509  12.683  0.59 11.21           N  
ANISOU 6147  N7AANAD A 402     1303   1504   1452    -30   -163    212       N  
HETATM 6148  C5AANAD A 402      -6.446  15.199  11.531  0.59 11.07           C  
ANISOU 6148  C5AANAD A 402     1178   1501   1527     62     21    261       C  
HETATM 6149  C6AANAD A 402      -6.942  14.899  10.192  0.59 12.20           C  
ANISOU 6149  C6AANAD A 402     1355   1587   1695   -107    -59    201       C  
HETATM 6150  N6AANAD A 402      -7.547  13.768   9.887  0.59 13.77           N  
ANISOU 6150  N6AANAD A 402     1511   1679   2041   -277   -139    153       N  
HETATM 6151  N1AANAD A 402      -6.721  15.894   9.278  0.59 12.27           N  
ANISOU 6151  N1AANAD A 402     1237   1577   1849    -70   -209    298       N  
HETATM 6152  C2AANAD A 402      -6.126  17.057   9.532  0.59 11.07           C  
ANISOU 6152  C2AANAD A 402     1238   1575   1394     75    -61    100       C  
HETATM 6153  N3AANAD A 402      -5.665  17.410  10.790  0.59 10.49           N  
ANISOU 6153  N3AANAD A 402     1094   1576   1316    153     -5    117       N  
HETATM 6154  C4AANAD A 402      -5.830  16.441  11.762  0.59 11.06           C  
ANISOU 6154  C4AANAD A 402     1134   1526   1542     50     13    167       C  
HETATM 6155  N9ABNAD A 402      -5.433  16.683  12.881  0.41  9.18           N  
ANISOU 6155  N9ABNAD A 402      954   1414   1120    130     24    252       N  
HETATM 6156  C8ABNAD A 402      -6.072  15.502  13.174  0.41 10.89           C  
ANISOU 6156  C8ABNAD A 402     1323   1634   1182   -148    -30    200       C  
HETATM 6157  N7ABNAD A 402      -6.598  14.872  12.147  0.41 10.77           N  
ANISOU 6157  N7ABNAD A 402     1134   1616   1340   -184    -83    222       N  
HETATM 6158  C5ABNAD A 402      -6.331  15.630  11.087  0.41 10.26           C  
ANISOU 6158  C5ABNAD A 402     1178   1415   1304     97     52    229       C  
HETATM 6159  C6ABNAD A 402      -6.679  15.464   9.669  0.41 10.80           C  
ANISOU 6159  C6ABNAD A 402     1205   1514   1383     -7    -51    207       C  
HETATM 6160  N6ABNAD A 402      -7.350  14.450   9.194  0.41 12.81           N  
ANISOU 6160  N6ABNAD A 402     1697   1770   1398   -181   -169    114       N  
HETATM 6161  N1ABNAD A 402      -6.206  16.475   8.879  0.41 10.37           N  
ANISOU 6161  N1ABNAD A 402     1218   1459   1265     32    -92    169       N  
HETATM 6162  C2ABNAD A 402      -5.534  17.558   9.298  0.41 10.59           C  
ANISOU 6162  C2ABNAD A 402     1245   1387   1392    -19    135    109       C  
HETATM 6163  N3ABNAD A 402      -5.187  17.787  10.626  0.41 10.07           N  
ANISOU 6163  N3ABNAD A 402     1160   1298   1367     73     14    294       N  
HETATM 6164  C4ABNAD A 402      -5.615  16.787  11.480  0.41 10.11           C  
ANISOU 6164  C4ABNAD A 402     1172   1459   1212     44     26    255       C  
HETATM 6165  C1 AMRD A 403       9.116  10.358  20.165  0.50 18.17           C  
ANISOU 6165  C1 AMRD A 403     2244   1759   2902     53    141    309       C  
HETATM 6166  C2 AMRD A 403       8.684   9.353  19.071  0.50 18.84           C  
ANISOU 6166  C2 AMRD A 403     2141   2669   2346     15    208    135       C  
HETATM 6167  O2 AMRD A 403       7.243   9.144  19.048  0.50 17.52           O  
ANISOU 6167  O2 AMRD A 403     2171   2306   2180   -163     29     41       O  
HETATM 6168  CM AMRD A 403       9.137   9.844  17.673  0.50 18.73           C  
ANISOU 6168  CM AMRD A 403     2287   2491   2338   -178     71    212       C  
HETATM 6169  C3 AMRD A 403       9.344   8.030  19.361  0.50 19.48           C  
ANISOU 6169  C3 AMRD A 403     2331   2836   2233    222   -152     22       C  
HETATM 6170  C4 AMRD A 403       8.983   6.965  18.305  0.50 21.82           C  
ANISOU 6170  C4 AMRD A 403     2622   2894   2775    123   -298    -89       C  
HETATM 6171  O4 AMRD A 403       7.596   6.869  17.924  0.50 21.90           O  
ANISOU 6171  O4 AMRD A 403     2669   2878   2773    315   -446    -98       O  
HETATM 6172  C5 AMRD A 403       9.393   5.661  18.957  0.50 19.60           C  
ANISOU 6172  C5 AMRD A 403     2678   2848   1922     22   -327   -125       C  
HETATM 6173  C1 BMRD A 403       9.103  10.348  20.226  0.50 18.40           C  
ANISOU 6173  C1 BMRD A 403     2285   1867   2841    123    142    351       C  
HETATM 6174  C2 BMRD A 403       8.684   9.374  19.097  0.50 19.46           C  
ANISOU 6174  C2 BMRD A 403     2204   2768   2421     49    186    164       C  
HETATM 6175  O2 BMRD A 403       7.244   9.158  19.070  0.50 18.67           O  
ANISOU 6175  O2 BMRD A 403     2229   2522   2342   -109     55    112       O  
HETATM 6176  CM BMRD A 403       9.127   9.915  17.717  0.50 19.84           C  
ANISOU 6176  CM BMRD A 403     2427   2624   2488   -137     55    325       C  
HETATM 6177  C3 BMRD A 403       9.359   8.050  19.338  0.50 19.84           C  
ANISOU 6177  C3 BMRD A 403     2364   2873   2301    220   -149     20       C  
HETATM 6178  C4 BMRD A 403       8.984   6.988  18.286  0.50 21.95           C  
ANISOU 6178  C4 BMRD A 403     2624   2915   2800    137   -298    -74       C  
HETATM 6179  O4 BMRD A 403       7.599   6.903  17.897  0.50 22.09           O  
ANISOU 6179  O4 BMRD A 403     2678   2914   2801    377   -464   -121       O  
HETATM 6180  C5 BMRD A 403       9.345   5.679  18.971  0.50 19.47           C  
ANISOU 6180  C5 BMRD A 403     2617   2833   1948     44   -312   -156       C  
HETATM 6181 ZN    ZN B 400      12.688   3.008 -22.727  1.00 12.04          ZN  
ANISOU 6181 ZN    ZN B 400     1410   1684   1480    -38    142   -201      ZN  
HETATM 6182 ZN    ZN B 401       7.834  22.294 -20.366  1.00 12.50          ZN  
ANISOU 6182 ZN    ZN B 401     2129   1636    986    648   -212    -92      ZN  
HETATM 6183  PA  NAD B 402      14.847  -5.579 -19.150  1.00 11.73           P  
ANISOU 6183  PA  NAD B 402     1473   1475   1509     52    -36   -126       P  
HETATM 6184  O1A NAD B 402      13.655  -6.473 -19.295  1.00 14.26           O  
ANISOU 6184  O1A NAD B 402     1626   1589   2201    -39    -64    -29       O  
HETATM 6185  O2A NAD B 402      15.938  -5.629 -20.192  1.00 13.41           O  
ANISOU 6185  O2A NAD B 402     1714   1893   1488    268     41   -218       O  
HETATM 6186  O5B NAD B 402      15.546  -5.859 -17.751  1.00 12.17           O  
ANISOU 6186  O5B NAD B 402     1455   1575   1593    158     44    217       O  
HETATM 6187  C5B NAD B 402      14.805  -6.205 -16.531  1.00 12.94           C  
ANISOU 6187  C5B NAD B 402     1628   1631   1659    345    154    292       C  
HETATM 6188  C4B NAD B 402      15.684  -7.134 -15.746  1.00 12.10           C  
ANISOU 6188  C4B NAD B 402     1733   1424   1439    302     28     72       C  
HETATM 6189  O4B NAD B 402      14.911  -7.474 -14.519  1.00 12.39           O  
ANISOU 6189  O4B NAD B 402     1774   1322   1610    180    126   -110       O  
HETATM 6190  C3B NAD B 402      15.932  -8.545 -16.402  1.00 12.49           C  
ANISOU 6190  C3B NAD B 402     1656   1580   1511     84    -61    -45       C  
HETATM 6191  O3B NAD B 402      17.377  -8.809 -16.490  1.00 12.89           O  
ANISOU 6191  O3B NAD B 402     1740   1660   1496    213     98   -177       O  
HETATM 6192  C2B NAD B 402      15.202  -9.564 -15.529  1.00 12.12           C  
ANISOU 6192  C2B NAD B 402     1905   1238   1463     30    -59    -10       C  
HETATM 6193  O2B NAD B 402      15.774 -10.837 -15.456  1.00 13.02           O  
ANISOU 6193  O2B NAD B 402     1941   1393   1614    169    -84   -104       O  
HETATM 6194  C1B NAD B 402      15.183  -8.820 -14.188  1.00 11.52           C  
ANISOU 6194  C1B NAD B 402     1597   1243   1537     11     54      5       C  
HETATM 6195  O3  NAD B 402      14.265  -4.112 -18.996  1.00 10.92           O  
ANISOU 6195  O3  NAD B 402     1351   1433   1364    -52     94     56       O  
HETATM 6196  PN  NAD B 402      14.929  -2.647 -19.341  1.00 10.35           P  
ANISOU 6196  PN  NAD B 402     1219   1509   1204     51     93    -74       P  
HETATM 6197  O1N NAD B 402      14.721  -2.328 -20.783  1.00 11.04           O  
ANISOU 6197  O1N NAD B 402     1389   1580   1224     23    141    -37       O  
HETATM 6198  O2N NAD B 402      16.281  -2.592 -18.750  1.00 10.54           O  
ANISOU 6198  O2N NAD B 402     1315   1453   1236     -9     76   -152       O  
HETATM 6199  O5D NAD B 402      13.913  -1.726 -18.520  1.00 10.92           O  
ANISOU 6199  O5D NAD B 402     1445   1610   1094    160     92   -163       O  
HETATM 6200  C5D NAD B 402      13.882  -1.802 -17.069  1.00 11.31           C  
ANISOU 6200  C5D NAD B 402     1393   1711   1192    319     31   -103       C  
HETATM 6201  C4D NAD B 402      12.649  -1.134 -16.537  1.00 11.64           C  
ANISOU 6201  C4D NAD B 402     1269   1740   1413    212     26   -118       C  
HETATM 6202  O4D NAD B 402      12.828   0.348 -16.754  1.00 12.28           O  
ANISOU 6202  O4D NAD B 402     1336   1698   1631    178   -165   -399       O  
HETATM 6203  C3D NAD B 402      11.290  -1.470 -17.242  1.00 10.80           C  
ANISOU 6203  C3D NAD B 402     1215   1682   1207     83     55     69       C  
HETATM 6204  O3D NAD B 402      10.230  -1.559 -16.306  1.00 11.03           O  
ANISOU 6204  O3D NAD B 402     1360   1680   1150     46     87    -42       O  
HETATM 6205  C2D NAD B 402      11.046  -0.272 -18.191  1.00 10.72           C  
ANISOU 6205  C2D NAD B 402     1240   1438   1396    108      0     -9       C  
HETATM 6206  O2D NAD B 402       9.692  -0.158 -18.496  1.00 11.47           O  
ANISOU 6206  O2D NAD B 402     1168   1831   1358    -11    -32    -93       O  
HETATM 6207  C1D NAD B 402      11.602   0.872 -17.285  1.00 11.57           C  
ANISOU 6207  C1D NAD B 402     1235   1590   1570    130   -131   -170       C  
HETATM 6208  N1N NAD B 402      11.898   2.182 -17.990  1.00 11.36           N  
ANISOU 6208  N1N NAD B 402     1328   1644   1344    134    224   -192       N  
HETATM 6209  C2N NAD B 402      11.702   3.291 -17.242  1.00 10.21           C  
ANISOU 6209  C2N NAD B 402     1253   1385   1241     18    -48   -117       C  
HETATM 6210  C3N NAD B 402      12.194   4.483 -17.649  1.00 10.16           C  
ANISOU 6210  C3N NAD B 402     1304   1492   1064    159    -51    -15       C  
HETATM 6211  C7N NAD B 402      11.999   5.718 -16.853  1.00 10.78           C  
ANISOU 6211  C7N NAD B 402     1276   1528   1290    183      4     50       C  
HETATM 6212  O7N NAD B 402      12.138   6.850 -17.389  1.00 11.16           O  
ANISOU 6212  O7N NAD B 402     1475   1591   1174    108    -24     18       O  
HETATM 6213  N7N NAD B 402      11.714   5.651 -15.516  1.00 10.63           N  
ANISOU 6213  N7N NAD B 402     1395   1620   1023    156    111    -12       N  
HETATM 6214  C4N NAD B 402      12.982   4.641 -18.968  1.00 11.22           C  
ANISOU 6214  C4N NAD B 402     1489   1653   1119    297    105    -29       C  
HETATM 6215  C5N NAD B 402      13.596   3.329 -19.285  1.00 11.07           C  
ANISOU 6215  C5N NAD B 402     1574   1595   1037    106     75    169       C  
HETATM 6216  C6N NAD B 402      12.823   2.167 -19.056  1.00 13.27           C  
ANISOU 6216  C6N NAD B 402     1453   1819   1768     30    272   -152       C  
HETATM 6217  N9AANAD B 402      14.256  -9.286 -13.193  0.48 12.21           N  
ANISOU 6217  N9AANAD B 402     1657   1591   1390     76    -46     47       N  
HETATM 6218  C8AANAD B 402      12.971  -9.748 -13.293  0.48 13.77           C  
ANISOU 6218  C8AANAD B 402     1740   1682   1811     -5     46     77       C  
HETATM 6219  N7AANAD B 402      12.400 -10.089 -12.162  0.48 14.35           N  
ANISOU 6219  N7AANAD B 402     1902   1830   1719   -233   -106    107       N  
HETATM 6220  C5AANAD B 402      13.310  -9.857 -11.202  0.48 12.85           C  
ANISOU 6220  C5AANAD B 402     1612   1624   1648      5    -47     28       C  
HETATM 6221  C6AANAD B 402      13.234 -10.040  -9.743  0.48 13.31           C  
ANISOU 6221  C6AANAD B 402     1691   1672   1695      5     -9     22       C  
HETATM 6222  N6AANAD B 402      12.188 -10.510  -9.103  0.48 14.67           N  
ANISOU 6222  N6AANAD B 402     1811   1967   1796   -138    -51    144       N  
HETATM 6223  N1AANAD B 402      14.409  -9.681  -9.117  0.48 13.25           N  
ANISOU 6223  N1AANAD B 402     1660   1662   1712     59     25     56       N  
HETATM 6224  C2AANAD B 402      15.519  -9.221  -9.719  0.48 13.22           C  
ANISOU 6224  C2AANAD B 402     1707   1622   1694     37    125   -108       C  
HETATM 6225  N3AANAD B 402      15.631  -9.018 -11.090  0.48 12.81           N  
ANISOU 6225  N3AANAD B 402     1374   1789   1704    157    -45    -30       N  
HETATM 6226  C4AANAD B 402      14.483  -9.354 -11.796  0.48 11.86           C  
ANISOU 6226  C4AANAD B 402     1577   1499   1432     43    -78     21       C  
HETATM 6227  N9ABNAD B 402      14.020  -9.278 -13.434  0.52 12.82           N  
ANISOU 6227  N9ABNAD B 402     1587   1620   1664    -40     30     24       N  
HETATM 6228  C8ABNAD B 402      12.713  -9.563 -13.759  0.52 12.85           C  
ANISOU 6228  C8ABNAD B 402     1574   1592   1716     19     82     51       C  
HETATM 6229  N7ABNAD B 402      11.986  -9.940 -12.714  0.52 13.13           N  
ANISOU 6229  N7ABNAD B 402     1739   1733   1516   -119    -48     87       N  
HETATM 6230  C5ABNAD B 402      12.799  -9.931 -11.647  0.52 13.57           C  
ANISOU 6230  C5ABNAD B 402     1654   1758   1746    -45    -93     69       C  
HETATM 6231  C6ABNAD B 402      12.552 -10.252 -10.241  0.52 13.12           C  
ANISOU 6231  C6ABNAD B 402     1507   1700   1778     -4     56     13       C  
HETATM 6232  N6ABNAD B 402      11.402 -10.645  -9.755  0.52 14.77           N  
ANISOU 6232  N6ABNAD B 402     1676   2059   1875   -304    124    128       N  
HETATM 6233  N1ABNAD B 402      13.658 -10.108  -9.446  0.52 13.70           N  
ANISOU 6233  N1ABNAD B 402     1681   1610   1916   -225   -107     96       N  
HETATM 6234  C2ABNAD B 402      14.865  -9.722  -9.882  0.52 12.33           C  
ANISOU 6234  C2ABNAD B 402     1605   1509   1571    114      1     84       C  
HETATM 6235  N3ABNAD B 402      15.160  -9.408 -11.194  0.52 11.92           N  
ANISOU 6235  N3ABNAD B 402     1682   1309   1540     -9    -38    -14       N  
HETATM 6236  C4ABNAD B 402      14.079  -9.513 -12.051  0.52 12.30           C  
ANISOU 6236  C4ABNAD B 402     1605   1344   1725    -12    -63     34       C  
HETATM 6237  C1 AMRD B 403       9.144   5.153 -21.310  0.50 17.12           C  
ANISOU 6237  C1 AMRD B 403     1947   2012   2547    511     10   -180       C  
HETATM 6238  C2 AMRD B 403       8.131   5.012 -20.151  0.50 17.65           C  
ANISOU 6238  C2 AMRD B 403     2505   2276   1926    407    -35   -222       C  
HETATM 6239  O2 AMRD B 403       7.904   3.611 -19.886  0.50 16.52           O  
ANISOU 6239  O2 AMRD B 403     2209   2406   1662    136    176   -238       O  
HETATM 6240  CM AMRD B 403       8.731   5.735 -18.931  0.50 17.12           C  
ANISOU 6240  CM AMRD B 403     2497   2312   1695    409     41   -178       C  
HETATM 6241  C3 AMRD B 403       6.805   5.671 -20.511  0.50 15.91           C  
ANISOU 6241  C3 AMRD B 403     2514   2175   1355    394    -85   -121       C  
HETATM 6242  C4 AMRD B 403       5.808   5.689 -19.343  0.50 18.32           C  
ANISOU 6242  C4 AMRD B 403     2438   2445   2079    170    246     70       C  
HETATM 6243  O4 AMRD B 403       5.663   4.400 -18.696  0.50 16.52           O  
ANISOU 6243  O4 AMRD B 403     1978   2460   1838    543    368    209       O  
HETATM 6244  C5 AMRD B 403       4.473   6.168 -19.866  0.50 16.74           C  
ANISOU 6244  C5 AMRD B 403     2499   2321   1541    150    243    159       C  
HETATM 6245  C1 BMRD B 403       8.672   5.344 -21.345  0.50 26.20           C  
ANISOU 6245  C1 BMRD B 403     3397   3403   3153     14     76     32       C  
HETATM 6246  C2 BMRD B 403       8.061   5.065 -19.955  0.50 24.92           C  
ANISOU 6246  C2 BMRD B 403     3197   3205   3065    -87     -4    -62       C  
HETATM 6247  O2 BMRD B 403       7.585   3.711 -19.912  0.50 23.46           O  
ANISOU 6247  O2 BMRD B 403     2952   3163   2797    -69    110   -193       O  
HETATM 6248  CM BMRD B 403       9.225   5.205 -18.950  0.50 25.57           C  
ANISOU 6248  CM BMRD B 403     3239   3429   3048    -34    -53   -171       C  
HETATM 6249  C3 BMRD B 403       7.085   6.114 -19.483  0.50 26.86           C  
ANISOU 6249  C3 BMRD B 403     3406   3374   3425     49     94   -109       C  
HETATM 6250  C4 BMRD B 403       5.733   5.726 -18.898  0.50 27.70           C  
ANISOU 6250  C4 BMRD B 403     3502   3693   3331     10     98     40       C  
HETATM 6251  O4 BMRD B 403       5.382   6.650 -17.818  0.50 29.97           O  
ANISOU 6251  O4 BMRD B 403     3997   3988   3403     73    218      9       O  
HETATM 6252  C5 BMRD B 403       4.677   5.932 -19.999  0.50 26.73           C  
ANISOU 6252  C5 BMRD B 403     3460   3493   3201    147    166     59       C  
HETATM 6253  C1  MRD B 404      35.248  -7.693   0.322  1.00 25.20           C  
ANISOU 6253  C1  MRD B 404     3521   3390   2663    309    -75    320       C  
HETATM 6254  C2  MRD B 404      33.854  -7.193  -0.089  1.00 28.67           C  
ANISOU 6254  C2  MRD B 404     3750   3780   3364    558   -176    271       C  
HETATM 6255  O2  MRD B 404      32.959  -7.414   1.033  1.00 31.77           O  
ANISOU 6255  O2  MRD B 404     3868   4324   3876    427     85    270       O  
HETATM 6256  CM  MRD B 404      33.930  -5.671  -0.281  1.00 30.22           C  
ANISOU 6256  CM  MRD B 404     3995   3810   3677    439   -113    230       C  
HETATM 6257  C3  MRD B 404      33.331  -7.888  -1.335  1.00 29.25           C  
ANISOU 6257  C3  MRD B 404     3751   3708   3656    381   -126    103       C  
HETATM 6258  C4  MRD B 404      34.055  -7.582  -2.627  1.00 28.73           C  
ANISOU 6258  C4  MRD B 404     3880   3637   3400    415   -294    140       C  
HETATM 6259  O4  MRD B 404      33.760  -6.252  -3.163  1.00 30.01           O  
ANISOU 6259  O4  MRD B 404     4078   3418   3908    418   -394    -17       O  
HETATM 6260  C5  MRD B 404      33.686  -8.587  -3.720  1.00 28.88           C  
ANISOU 6260  C5  MRD B 404     3872   3520   3581    263   -431    198       C  
HETATM 6261  O   HOH A2001      27.814  13.844  47.950  1.00 61.04           O  
ANISOU 6261  O   HOH A2001     7527   7793   7873   -132     76   -176       O  
HETATM 6262  O   HOH A2002      23.776  14.952  47.203  1.00 50.12           O  
ANISOU 6262  O   HOH A2002     6733   6181   6130   -884    -81    405       O  
HETATM 6263  O   HOH A2003      20.812  15.701  50.204  1.00 45.49           O  
ANISOU 6263  O   HOH A2003     5987   5784   5512     11    457   -714       O  
HETATM 6264  O   HOH A2004      29.634  12.621  45.657  1.00 49.08           O  
ANISOU 6264  O   HOH A2004     5323   7298   6026   -234   -116     65       O  
HETATM 6265  O   HOH A2005      21.196  17.009  48.008  1.00 46.84           O  
ANISOU 6265  O   HOH A2005     5932   6441   5425   -423   -513      1       O  
HETATM 6266  O   HOH A2006      19.760  -0.825  46.707  1.00 65.47           O  
ANISOU 6266  O   HOH A2006     7953   8131   8793    339   -134    201       O  
HETATM 6267  O   HOH A2007      19.660  15.317  46.474  1.00 29.60           O  
ANISOU 6267  O   HOH A2007     3966   2978   4302    544    235    132       O  
HETATM 6268  O   HOH A2008      26.860   3.525  43.260  1.00 56.07           O  
ANISOU 6268  O   HOH A2008     6617   8323   6366    291     96    281       O  
HETATM 6269  O   HOH A2009      22.308   0.569  45.495  1.00 65.21           O  
ANISOU 6269  O   HOH A2009     8624   8261   7892    -27     54    293       O  
HETATM 6270  O   HOH A2010      18.878   9.275  51.741  1.00 35.73           O  
ANISOU 6270  O   HOH A2010     4944   5285   3348    359   -438   -548       O  
HETATM 6271  O   HOH A2011      14.802   7.596  51.485  1.00 41.29           O  
ANISOU 6271  O   HOH A2011     6136   6408   3144    -49    -67    468       O  
HETATM 6272  O   HOH A2012      18.833   1.218  49.639  1.00 42.07           O  
ANISOU 6272  O   HOH A2012     6375   5267   4343   -414   -108    922       O  
HETATM 6273  O   HOH A2013      16.422  11.179  49.037  1.00 22.85           O  
ANISOU 6273  O   HOH A2013     3088   3204   2389     46    -23   -401       O  
HETATM 6274  O   HOH A2014      25.980  10.370  49.721  1.00 39.24           O  
ANISOU 6274  O   HOH A2014     5267   6368   3273     26   -818   -943       O  
HETATM 6275  O   HOH A2015      15.636  13.204  47.338  1.00 25.40           O  
ANISOU 6275  O   HOH A2015     2777   3436   3438   -184   -245   -760       O  
HETATM 6276  O   HOH A2016     -10.291   9.551  35.265  1.00 55.98           O  
ANISOU 6276  O   HOH A2016     6662   7390   7216     29    460    357       O  
HETATM 6277  O   HOH A2017      -9.247   6.136  37.564  1.00 72.18           O  
ANISOU 6277  O   HOH A2017     9195   9611   8620   -181    440    343       O  
HETATM 6278  O   HOH A2018      -7.622  10.512  37.135  1.00 53.34           O  
ANISOU 6278  O   HOH A2018     6655   6861   6751    343    513   -103       O  
HETATM 6279  O   HOH A2019      26.172   3.126  45.830  1.00 39.50           O  
ANISOU 6279  O   HOH A2019     5002   5127   4880    972    456    245       O  
HETATM 6280  O   HOH A2020      22.481   2.406  47.192  1.00 47.37           O  
ANISOU 6280  O   HOH A2020     5676   6206   6116    136    341    525       O  
HETATM 6281  O   HOH A2021      19.258  -0.355  43.595  1.00 34.85           O  
ANISOU 6281  O   HOH A2021     5080   4508   3653    482   -479    844       O  
HETATM 6282  O   HOH A2022      20.849  10.875  52.896  1.00 67.13           O  
ANISOU 6282  O   HOH A2022     8553   8383   8569    105    215    -86       O  
HETATM 6283  O   HOH A2023      17.144   5.491  50.266  1.00 43.58           O  
ANISOU 6283  O   HOH A2023     7523   5202   3832   -254    551    342       O  
HETATM 6284  O   HOH A2024      20.379   3.409  49.293  1.00 28.03           O  
ANISOU 6284  O   HOH A2024     4602   3577   2473    334   -585   1255       O  
HETATM 6285  O   HOH A2025      18.433   9.240  49.092  1.00 23.13           O  
ANISOU 6285  O   HOH A2025     3605   2999   2183    329   -152   -304       O  
HETATM 6286  O   HOH A2026       1.250  -5.101  30.428  1.00 50.28           O  
ANISOU 6286  O   HOH A2026     6777   6144   6182     88   -158   -165       O  
HETATM 6287  O   HOH A2027      -2.241  -5.256  32.245  1.00 48.34           O  
ANISOU 6287  O   HOH A2027     6921   5219   6226     48     45   -287       O  
HETATM 6288  O   HOH A2028       2.281  -5.498  35.222  1.00 47.10           O  
ANISOU 6288  O   HOH A2028     5856   6034   6006    162    615    422       O  
HETATM 6289  O   HOH A2029      -9.643  -0.491  28.861  1.00 43.98           O  
ANISOU 6289  O   HOH A2029     5367   5600   5742   -959    334    290       O  
HETATM 6290  O   HOH A2030      14.067  25.211  39.407  1.00 40.18           O  
ANISOU 6290  O   HOH A2030     5592   5264   4410   -664   -183  -1180       O  
HETATM 6291  O   HOH A2031     -11.455   3.468  26.793  1.00 80.05           O  
ANISOU 6291  O   HOH A2031    10035  10672   9707    147    142    -67       O  
HETATM 6292  O   HOH A2032     -11.769   2.588  31.402  1.00 55.81           O  
ANISOU 6292  O   HOH A2032     6916   7835   6456     -5     99    223       O  
HETATM 6293  O   HOH A2033      -7.419   1.291  20.018  1.00 58.16           O  
ANISOU 6293  O   HOH A2033     7495   7950   6654   -253     15   -138       O  
HETATM 6294  O   HOH A2034     -10.878   7.851  33.487  1.00 65.41           O  
ANISOU 6294  O   HOH A2034     7272   9105   8475     99   -198     11       O  
HETATM 6295  O   HOH A2035      -9.361   8.789  20.825  1.00 52.12           O  
ANISOU 6295  O   HOH A2035     6173   6891   6740    -62   -105    219       O  
HETATM 6296  O   HOH A2036      -7.717   5.222  23.050  1.00 37.45           O  
ANISOU 6296  O   HOH A2036     3885   5350   4993    -74    180    272       O  
HETATM 6297  O   HOH A2037      10.381   0.797  52.023  1.00 53.74           O  
ANISOU 6297  O   HOH A2037     7373   6662   6383   -424     35    306       O  
HETATM 6298  O   HOH A2038      14.563   9.208  49.304  1.00 19.52           O  
ANISOU 6298  O   HOH A2038     2733   2810   1872    457   -517   -349       O  
HETATM 6299  O   HOH A2039      12.949  12.602  46.813  1.00 17.01           O  
ANISOU 6299  O   HOH A2039     2293   2008   2163    197    136    181       O  
HETATM 6300  O   HOH A2040      14.137   1.567  51.906  1.00 59.33           O  
ANISOU 6300  O   HOH A2040     7840   7283   7421    249      3    423       O  
HETATM 6301  O   HOH A2041      -7.446   3.805  36.669  1.00 57.16           O  
ANISOU 6301  O   HOH A2041     7579   7473   6668   -487    172    527       O  
HETATM 6302  O   HOH A2042      -7.152   8.724  38.660  1.00 46.06           O  
ANISOU 6302  O   HOH A2042     6197   6490   4813    410    108    376       O  
HETATM 6303  O   HOH A2043      -4.701   4.593  42.631  1.00 37.68           O  
ANISOU 6303  O   HOH A2043     5284   5313   3719   -708    109    309       O  
HETATM 6304  O   HOH A2044      -3.311   8.612  43.186  1.00 82.76           O  
ANISOU 6304  O   HOH A2044    10775  10813   9857    156    -10      1       O  
HETATM 6305  O   HOH A2045      -1.334   5.564  45.041  1.00 24.22           O  
ANISOU 6305  O   HOH A2045     3097   3661   2446     89    674    556       O  
HETATM 6306  O   HOH A2046      -3.520  11.870  41.354  1.00 34.04           O  
ANISOU 6306  O   HOH A2046     4862   4581   3491   -264    282   -389       O  
HETATM 6307  O   HOH A2047       1.815  13.727  44.976  1.00 30.62           O  
ANISOU 6307  O   HOH A2047     4354   3998   3283     59    388    563       O  
HETATM 6308  O   HOH A2048      18.400  27.629  -7.943  1.00 66.47           O  
ANISOU 6308  O   HOH A2048     8535   8639   8083    -34    163    -20       O  
HETATM 6309  O   HOH A2049       8.703   6.368  53.505  1.00 44.91           O  
ANISOU 6309  O   HOH A2049     7611   6669   2785   -493   -236    -64       O  
HETATM 6310  O   HOH A2050       9.625  -3.641  48.062  1.00 50.81           O  
ANISOU 6310  O   HOH A2050     6966   7438   4902     42    589    578       O  
HETATM 6311  O   HOH A2051       6.319  -0.181  48.457  1.00 35.47           O  
ANISOU 6311  O   HOH A2051     4982   4151   4342     91     25    685       O  
HETATM 6312  O   HOH A2052      17.310  -0.966  47.624  1.00 46.64           O  
ANISOU 6312  O   HOH A2052     6910   5794   5015    191    208    229       O  
HETATM 6313  O   HOH A2053      16.793   1.028  43.839  1.00 28.80           O  
ANISOU 6313  O   HOH A2053     4645   4014   2285    106   -259    456       O  
HETATM 6314  O   HOH A2054      38.112  12.357  28.466  1.00 43.72           O  
ANISOU 6314  O   HOH A2054     4178   6328   6105   -877    940    231       O  
HETATM 6315  O   HOH A2055      31.074  20.796  24.081  1.00 60.20           O  
ANISOU 6315  O   HOH A2055     7065   8278   7530    -71    535   -161       O  
HETATM 6316  O   HOH A2056       4.095   6.895  32.615  1.00 10.72           O  
ANISOU 6316  O   HOH A2056     1417   1335   1323   -142    249    379       O  
HETATM 6317  O   HOH A2057      20.929  -0.690  41.206  1.00 26.93           O  
ANISOU 6317  O   HOH A2057     3854   2946   3433    472   -921    316       O  
HETATM 6318  O   HOH A2058      25.073   0.730  41.763  1.00 51.10           O  
ANISOU 6318  O   HOH A2058     6205   6916   6296    445   -129    649       O  
HETATM 6319  O   HOH A2059      29.825   5.923  41.422  1.00 47.20           O  
ANISOU 6319  O   HOH A2059     7010   6327   4599     17   -414    187       O  
HETATM 6320  O   HOH A2060      26.573  28.608  37.148  1.00 54.01           O  
ANISOU 6320  O   HOH A2060     7440   6766   6316   -143   -250   -303       O  
HETATM 6321  O   HOH A2061      27.514  -2.100  35.741  1.00 58.43           O  
ANISOU 6321  O   HOH A2061     6911   7994   7295    299   -201    189       O  
HETATM 6322  O   HOH A2062      29.980  -0.680  32.363  1.00 52.79           O  
ANISOU 6322  O   HOH A2062     6461   6722   6876    -36    -34    142       O  
HETATM 6323  O   HOH A2063      -0.593  -3.528  31.240  1.00 40.23           O  
ANISOU 6323  O   HOH A2063     6502   3777   5006   -540   -667   -473       O  
HETATM 6324  O   HOH A2064       0.921  -3.455  34.823  1.00 32.84           O  
ANISOU 6324  O   HOH A2064     5571   3115   3791    222   -936    -64       O  
HETATM 6325  O   HOH A2065      -2.292   3.288  34.000  1.00 37.34           O  
ANISOU 6325  O   HOH A2065     2406   3022   8759   -148   1616   1054       O  
HETATM 6326  O   HOH A2066      29.435   6.900   1.439  1.00 41.12           O  
ANISOU 6326  O   HOH A2066     6085   5471   4066   -393   -685    160       O  
HETATM 6327  O   HOH A2067      29.848  17.460   0.713  1.00 49.61           O  
ANISOU 6327  O   HOH A2067     6155   6081   6614   -215    392    166       O  
HETATM 6328  O   HOH A2068      -6.665  -1.255  29.434  1.00 36.38           O  
ANISOU 6328  O   HOH A2068     4863   3680   5280  -1587    705    471       O  
HETATM 6329  O   HOH A2069      -8.765  -3.402  32.525  1.00 49.04           O  
ANISOU 6329  O   HOH A2069     6606   6910   5118   -505    685    864       O  
HETATM 6330  O   HOH A2070      18.753  20.822  42.964  1.00 77.54           O  
ANISOU 6330  O   HOH A2070     9646   9950   9866   -149     41    106       O  
HETATM 6331  O   HOH A2071      12.289  23.062  40.412  1.00 40.24           O  
ANISOU 6331  O   HOH A2071     5304   5653   4334   -333    -82   -273       O  
HETATM 6332  O   HOH A2072      20.360  -4.166  21.957  1.00 64.74           O  
ANISOU 6332  O   HOH A2072     8438   8345   7817     66    -48     57       O  
HETATM 6333  O   HOH A2073      15.447  -7.749  24.982  1.00 46.80           O  
ANISOU 6333  O   HOH A2073     6522   5724   5536    117     21   -385       O  
HETATM 6334  O   HOH A2074       0.600  -4.367  27.940  1.00 61.70           O  
ANISOU 6334  O   HOH A2074     8193   7786   7463    172    -13   -254       O  
HETATM 6335  O   HOH A2075       0.987  -1.049  24.159  1.00 19.88           O  
ANISOU 6335  O   HOH A2075     2745   1777   3032   -224   -333    115       O  
HETATM 6336  O   HOH A2076      -6.213  14.866  16.776  1.00 33.69           O  
ANISOU 6336  O   HOH A2076     5874   3860   3066   -381     -7    369       O  
HETATM 6337  O   HOH A2077      -8.458  10.893  23.126  1.00 40.77           O  
ANISOU 6337  O   HOH A2077     4983   5488   5018   -641    -11   -621       O  
HETATM 6338  O   HOH A2078      -7.427  12.730  18.884  1.00 41.54           O  
ANISOU 6338  O   HOH A2078     5341   4922   5520   -297    104     26       O  
HETATM 6339  O   HOH A2079      -4.300  10.599  14.701  1.00 68.95           O  
ANISOU 6339  O   HOH A2079     9426   8772   8001    -72    143    422       O  
HETATM 6340  O   HOH A2080      -4.384   9.245  18.707  1.00 27.31           O  
ANISOU 6340  O   HOH A2080     2903   5106   2366    221   -114     45       O  
HETATM 6341  O   HOH A2081      -6.985   7.618  21.505  1.00 57.09           O  
ANISOU 6341  O   HOH A2081     6756   7799   7137    169   -109   -118       O  
HETATM 6342  O   HOH A2082      -6.570   6.176  25.375  1.00 49.26           O  
ANISOU 6342  O   HOH A2082     6366   6940   5412     61   -204    175       O  
HETATM 6343  O   HOH A2083      -0.183  -3.332  40.139  1.00 44.90           O  
ANISOU 6343  O   HOH A2083     5751   6280   5029   -286   1029    -20       O  
HETATM 6344  O   HOH A2084     -10.107   2.068  29.406  1.00 38.76           O  
ANISOU 6344  O   HOH A2084     4450   6210   4065   -945    302   -627       O  
HETATM 6345  O   HOH A2085      -6.296  -1.589  25.172  1.00 54.03           O  
ANISOU 6345  O   HOH A2085     6815   6732   6982    161   -334   -337       O  
HETATM 6346  O   HOH A2086      -4.680  -0.137  21.491  1.00 63.04           O  
ANISOU 6346  O   HOH A2086     7990   8022   7941    -77     37     74       O  
HETATM 6347  O   HOH A2087      -9.858   5.275  31.307  1.00 54.25           O  
ANISOU 6347  O   HOH A2087     6307   7510   6796    -94   -110    -17       O  
HETATM 6348  O   HOH A2088      -3.843   8.605  30.483  1.00 23.43           O  
ANISOU 6348  O   HOH A2088     4765   2255   1881   -370   1141    171       O  
HETATM 6349  O   HOH A2089      -6.380   6.223  19.320  1.00 52.08           O  
ANISOU 6349  O   HOH A2089     6519   7567   5703    103   -540     -5       O  
HETATM 6350  O   HOH A2090      -1.898  -2.577  17.753  1.00 27.88           O  
ANISOU 6350  O   HOH A2090     4328   2629   3638   -411    370   -131       O  
HETATM 6351  O   HOH A2091      -5.780   3.792  15.474  1.00 35.79           O  
ANISOU 6351  O   HOH A2091     4891   4742   3966   -225   -371    -33       O  
HETATM 6352  O   HOH A2092      -5.238   6.552  15.074  1.00 30.42           O  
ANISOU 6352  O   HOH A2092     3907   4911   2740   -586    106    333       O  
HETATM 6353  O   HOH A2093      -4.796   4.885  36.880  1.00 40.95           O  
ANISOU 6353  O   HOH A2093     5446   5137   4976    347   1318   1241       O  
HETATM 6354  O   HOH A2094       8.127  -1.451  17.700  1.00 43.03           O  
ANISOU 6354  O   HOH A2094     5269   5856   5224   -535  -1323    611       O  
HETATM 6355  O   HOH A2095      -4.636   8.197  38.959  1.00 34.60           O  
ANISOU 6355  O   HOH A2095     3939   6113   3093   -101   1179    402       O  
HETATM 6356  O   HOH A2096      -3.492   3.000  39.616  1.00 55.67           O  
ANISOU 6356  O   HOH A2096     6810   7489   6852   -488    258    293       O  
HETATM 6357  O   HOH A2097      -2.404   6.315  42.536  1.00 31.41           O  
ANISOU 6357  O   HOH A2097     4258   4987   2689    945    124    132       O  
HETATM 6358  O   HOH A2098       4.758  -6.771  34.613  1.00 59.36           O  
ANISOU 6358  O   HOH A2098     8302   6704   7546     84    376    445       O  
HETATM 6359  O   HOH A2099       7.120  -6.484  33.931  1.00 48.04           O  
ANISOU 6359  O   HOH A2099     6589   5695   5969    177   -433   -257       O  
HETATM 6360  O   HOH A2100      -2.801   9.378  40.748  1.00 27.45           O  
ANISOU 6360  O   HOH A2100     2527   4003   3899   -194    746   -674       O  
HETATM 6361  O   HOH A2101       0.065   7.924  45.544  1.00 25.97           O  
ANISOU 6361  O   HOH A2101     3846   2995   3026    -11    691    -32       O  
HETATM 6362  O   HOH A2102       1.360  10.993  45.335  1.00 42.57           O  
ANISOU 6362  O   HOH A2102     5690   5366   5118   -210     97    619       O  
HETATM 6363  O   HOH A2103      17.099  26.411  -5.069  1.00 58.60           O  
ANISOU 6363  O   HOH A2103     7648   7774   6841     90    269    343       O  
HETATM 6364  O   HOH A2104       7.245  36.221  -3.071  1.00 66.67           O  
ANISOU 6364  O   HOH A2104     8912   8475   7943    158    100    232       O  
HETATM 6365  O   HOH A2105       3.954   3.477  45.155  1.00 16.56           O  
ANISOU 6365  O   HOH A2105     2576   2112   1604   -314    150    367       O  
HETATM 6366  O   HOH A2106       8.341   4.556  51.657  1.00 32.08           O  
ANISOU 6366  O   HOH A2106     4511   5853   1824   -391    -71    499       O  
HETATM 6367  O   HOH A2107       7.461   2.182  45.391  1.00 18.75           O  
ANISOU 6367  O   HOH A2107     3124   2133   1865    334    143    141       O  
HETATM 6368  O   HOH A2108       8.495   2.878  47.909  1.00 29.17           O  
ANISOU 6368  O   HOH A2108     5280   3214   2589   -190    -47    217       O  
HETATM 6369  O   HOH A2109       7.947   9.740  47.523  1.00 19.40           O  
ANISOU 6369  O   HOH A2109     2961   2538   1871     28    351   -212       O  
HETATM 6370  O   HOH A2110      19.784  18.770  41.799  1.00 40.25           O  
ANISOU 6370  O   HOH A2110     5207   4431   5656    167     63    897       O  
HETATM 6371  O   HOH A2111      21.000  17.324  43.620  1.00 73.29           O  
ANISOU 6371  O   HOH A2111     9421   9754   8673    267    -39    115       O  
HETATM 6372  O   HOH A2112      22.686  21.927  42.413  1.00 77.29           O  
ANISOU 6372  O   HOH A2112     9923  10226   9220    -33    145    -34       O  
HETATM 6373  O   HOH A2113      27.945  16.393  44.356  1.00 58.32           O  
ANISOU 6373  O   HOH A2113     7397   8261   6502    130   -388    -45       O  
HETATM 6374  O   HOH A2114      14.813   2.400  49.423  1.00 54.41           O  
ANISOU 6374  O   HOH A2114     6663   7671   6341    -10     74    340       O  
HETATM 6375  O   HOH A2115      11.741  -2.564  46.434  1.00 41.05           O  
ANISOU 6375  O   HOH A2115     6099   4957   4541    163    434    467       O  
HETATM 6376  O   HOH A2116       9.197   0.840  49.672  1.00 46.69           O  
ANISOU 6376  O   HOH A2116     6238   5721   5782    -18    -30    168       O  
HETATM 6377  O   HOH A2117       9.076  -0.958  47.850  1.00 43.15           O  
ANISOU 6377  O   HOH A2117     6945   5363   4089     84   -913    410       O  
HETATM 6378  O   HOH A2118       9.129  -0.095  45.052  1.00 20.82           O  
ANISOU 6378  O   HOH A2118     3164   2212   2536    -64   -166    233       O  
HETATM 6379  O   HOH A2119      15.416  -0.067  46.084  1.00 33.77           O  
ANISOU 6379  O   HOH A2119     5481   4125   3225   -632    187    678       O  
HETATM 6380  O   HOH A2120      32.532  11.758  40.275  1.00 48.08           O  
ANISOU 6380  O   HOH A2120     5822   6633   5811    485   -498    111       O  
HETATM 6381  O   HOH A2121      34.670  13.028  37.785  1.00 48.76           O  
ANISOU 6381  O   HOH A2121     6266   6815   5444    301   -345    -85       O  
HETATM 6382  O   HOH A2122      34.536   8.376  28.530  1.00 53.66           O  
ANISOU 6382  O   HOH A2122     6222   6721   7445    457    -31   -142       O  
HETATM 6383  O   HOH A2123      37.367   9.462  32.819  1.00 57.27           O  
ANISOU 6383  O   HOH A2123     6688   7870   7203    -34     37    146       O  
HETATM 6384  O   HOH A2124      32.446  19.154  29.793  1.00 67.46           O  
ANISOU 6384  O   HOH A2124     8620   8649   8360     35      1    260       O  
HETATM 6385  O   HOH A2125      31.818  10.425  26.087  1.00 43.94           O  
ANISOU 6385  O   HOH A2125     6814   6209   3672   -793   -304    288       O  
HETATM 6386  O   HOH A2126      32.905  12.455  24.974  1.00 51.77           O  
ANISOU 6386  O   HOH A2126     7160   7362   5150    234    290     94       O  
HETATM 6387  O   HOH A2127      36.722  14.381  27.996  1.00 48.20           O  
ANISOU 6387  O   HOH A2127     5240   6771   6301    -48    406    515       O  
HETATM 6388  O   HOH A2128      37.851  14.782  30.267  1.00 81.35           O  
ANISOU 6388  O   HOH A2128    10471  10661   9778     16    129     90       O  
HETATM 6389  O   HOH A2129      -9.966  34.093  14.925  1.00 63.28           O  
ANISOU 6389  O   HOH A2129     8158   8111   7775    130      4     61       O  
HETATM 6390  O   HOH A2130      30.890  17.507  25.747  1.00 40.06           O  
ANISOU 6390  O   HOH A2130     4764   5710   4748   1014    460    160       O  
HETATM 6391  O   HOH A2131      29.500  21.210  27.134  1.00 28.46           O  
ANISOU 6391  O   HOH A2131     2782   3783   4250   -572   -183    994       O  
HETATM 6392  O   HOH A2132      33.489  15.341  37.076  1.00 42.30           O  
ANISOU 6392  O   HOH A2132     4492   5741   5838    -80     10    281       O  
HETATM 6393  O   HOH A2133      -7.967  35.768  14.905  1.00 41.31           O  
ANISOU 6393  O   HOH A2133     4963   5043   5691   1106     64    185       O  
HETATM 6394  O   HOH A2134      -1.627  34.127  26.097  1.00 75.72           O  
ANISOU 6394  O   HOH A2134     9732   9858   9179    150     48    -56       O  
HETATM 6395  O   HOH A2135      30.124  25.263  36.404  1.00 64.79           O  
ANISOU 6395  O   HOH A2135     7653   8728   8237    118    -97     85       O  
HETATM 6396  O   HOH A2136      27.504  24.505  38.789  1.00 52.29           O  
ANISOU 6396  O   HOH A2136     6961   6623   6282    143   -455   -144       O  
HETATM 6397  O   HOH A2137      31.622  18.198  40.724  1.00 57.97           O  
ANISOU 6397  O   HOH A2137     6559   7882   7586    -19   -460   -203       O  
HETATM 6398  O   HOH A2138      29.760  18.185  43.046  1.00 57.76           O  
ANISOU 6398  O   HOH A2138     7087   7898   6961   -207   -696    -73       O  
HETATM 6399  O   HOH A2139       7.314  35.796  19.501  1.00 31.82           O  
ANISOU 6399  O   HOH A2139     5003   3652   3433    366   -184   -496       O  
HETATM 6400  O   HOH A2140       1.090  37.936  24.440  1.00 74.09           O  
ANISOU 6400  O   HOH A2140     9520   9609   9022     52    -45     42       O  
HETATM 6401  O   HOH A2141      22.663   1.362  40.835  1.00 26.27           O  
ANISOU 6401  O   HOH A2141     3703   2411   3866    670    511    764       O  
HETATM 6402  O   HOH A2142      20.867  26.170  38.714  1.00 40.25           O  
ANISOU 6402  O   HOH A2142     5435   5198   4659      4   -204    596       O  
HETATM 6403  O   HOH A2143      26.679  26.095  36.610  1.00 54.48           O  
ANISOU 6403  O   HOH A2143     7538   6468   6695    196   -154    167       O  
HETATM 6404  O   HOH A2144      28.373  25.986  32.892  1.00 41.61           O  
ANISOU 6404  O   HOH A2144     5467   4717   5628   -138     31    117       O  
HETATM 6405  O   HOH A2145      26.204   6.167  41.819  1.00 29.10           O  
ANISOU 6405  O   HOH A2145     3194   5017   2846    527   -493   -492       O  
HETATM 6406  O   HOH A2146      15.737  29.827  35.442  1.00 45.16           O  
ANISOU 6406  O   HOH A2146     7134   4861   5165   -743    322   -757       O  
HETATM 6407  O   HOH A2147      17.991  26.519  38.702  1.00 31.98           O  
ANISOU 6407  O   HOH A2147     4158   3914   4077   -345   -486   -144       O  
HETATM 6408  O   HOH A2148      15.717  30.124  38.085  1.00 47.14           O  
ANISOU 6408  O   HOH A2148     6428   6242   5241    205    428   -432       O  
HETATM 6409  O   HOH A2149      15.872  25.670  37.215  1.00 27.61           O  
ANISOU 6409  O   HOH A2149     4273   2856   3364     14   -653    131       O  
HETATM 6410  O   HOH A2150     -11.675  13.119   0.572  1.00 60.81           O  
ANISOU 6410  O   HOH A2150     7641   7970   7493    -61     32     60       O  
HETATM 6411  O   HOH A2151      -7.078   9.086  -4.995  1.00 56.01           O  
ANISOU 6411  O   HOH A2151     7108   7407   6767    163     29   -296       O  
HETATM 6412  O   HOH A2152      20.847  -3.811  37.709  1.00 39.17           O  
ANISOU 6412  O   HOH A2152     5029   6157   3696   -712   -525   1312       O  
HETATM 6413  O   HOH A2153      22.014  -3.213  40.467  1.00 40.96           O  
ANISOU 6413  O   HOH A2153     5276   4247   6038    401   -416    872       O  
HETATM 6414  O   HOH A2154      25.667  -3.729  36.782  1.00 47.25           O  
ANISOU 6414  O   HOH A2154     6424   5146   6381    929   -198    324       O  
HETATM 6415  O   HOH A2155      17.794   4.871  24.838  1.00 14.89           O  
ANISOU 6415  O   HOH A2155     2094   1496   2068   -117   -365    316       O  
HETATM 6416  O   HOH A2156      26.152   1.450  33.048  1.00 22.27           O  
ANISOU 6416  O   HOH A2156     2722   2920   2821    391     52      1       O  
HETATM 6417  O   HOH A2157      28.826   0.300  36.875  1.00 30.57           O  
ANISOU 6417  O   HOH A2157     3101   3523   4990    892   -253   1645       O  
HETATM 6418  O   HOH A2158      27.179   2.027  30.136  1.00 38.01           O  
ANISOU 6418  O   HOH A2158     4724   3616   6102    879   -387   -513       O  
HETATM 6419  O   HOH A2159      -2.115  20.370 -11.822  1.00 45.20           O  
ANISOU 6419  O   HOH A2159     5663   7146   4365     89    425     37       O  
HETATM 6420  O   HOH A2160      29.762   1.675  30.969  1.00 34.60           O  
ANISOU 6420  O   HOH A2160     4191   4031   4924    716    388   -255       O  
HETATM 6421  O   HOH A2161      35.530   5.691  31.239  1.00 51.76           O  
ANISOU 6421  O   HOH A2161     5861   7004   6802    -76    434   -206       O  
HETATM 6422  O   HOH A2162      28.409   4.359  23.489  1.00 33.74           O  
ANISOU 6422  O   HOH A2162     4569   4209   4041   1217    -67     65       O  
HETATM 6423  O   HOH A2163      29.779   8.983  25.713  1.00 26.39           O  
ANISOU 6423  O   HOH A2163     2908   3524   3594    145    -99    686       O  
HETATM 6424  O   HOH A2164      32.450  11.960  13.631  1.00 63.86           O  
ANISOU 6424  O   HOH A2164     7808   8685   7773   -172     53     -2       O  
HETATM 6425  O   HOH A2165      35.565   5.820  16.976  1.00 67.41           O  
ANISOU 6425  O   HOH A2165     8673   8888   8053    -58    123    124       O  
HETATM 6426  O   HOH A2166      -8.164   4.083   8.759  1.00 95.58           O  
ANISOU 6426  O   HOH A2166    12214  12516  11586     57    100     81       O  
HETATM 6427  O   HOH A2167      30.845   0.723  13.359  1.00 55.98           O  
ANISOU 6427  O   HOH A2167     6766   7108   7397    351     74    -44       O  
HETATM 6428  O   HOH A2168      29.268   5.618   5.856  1.00 48.83           O  
ANISOU 6428  O   HOH A2168     6343   7168   5040   -139   -202    144       O  
HETATM 6429  O   HOH A2169      -4.021  16.679 -14.778  1.00 91.05           O  
ANISOU 6429  O   HOH A2169    11648  11913  11035    133     75     67       O  
HETATM 6430  O   HOH A2170      30.260   7.098   3.651  1.00 57.47           O  
ANISOU 6430  O   HOH A2170     7705   7000   7130    220    -69    -59       O  
HETATM 6431  O   HOH A2171      32.050  13.989   6.952  1.00 57.66           O  
ANISOU 6431  O   HOH A2171     6788   7837   7284   -576    201    188       O  
HETATM 6432  O   HOH A2172      26.404  19.168  10.834  1.00 87.03           O  
ANISOU 6432  O   HOH A2172    11194  11365  10509    125    142     27       O  
HETATM 6433  O   HOH A2173      28.476  16.832  12.316  1.00 60.25           O  
ANISOU 6433  O   HOH A2173     7842   7874   7175   -148    378     64       O  
HETATM 6434  O   HOH A2174      25.796  13.574   1.393  1.00 56.44           O  
ANISOU 6434  O   HOH A2174     7499   6608   7338   -286     20   -192       O  
HETATM 6435  O   HOH A2175      29.281  15.875   3.067  1.00 47.42           O  
ANISOU 6435  O   HOH A2175     5892   6283   5841   -719    396    493       O  
HETATM 6436  O   HOH A2176      16.562  21.080  44.472  1.00 55.73           O  
ANISOU 6436  O   HOH A2176     7533   7411   6231     30    642    -74       O  
HETATM 6437  O   HOH A2177      17.891  19.079  45.440  1.00 36.55           O  
ANISOU 6437  O   HOH A2177     5769   3818   4299    337    148  -1187       O  
HETATM 6438  O   HOH A2178      10.892  17.412  43.265  1.00 24.79           O  
ANISOU 6438  O   HOH A2178     4517   3016   1886   -372    639   -191       O  
HETATM 6439  O   HOH A2179      12.815  20.605  40.529  1.00 31.96           O  
ANISOU 6439  O   HOH A2179     5614   3443   3084   -507    143   -142       O  
HETATM 6440  O   HOH A2180      19.592  -2.665  19.693  1.00 51.40           O  
ANISOU 6440  O   HOH A2180     7542   5769   6218   -268    263    150       O  
HETATM 6441  O   HOH A2181      27.360  29.785  21.766  1.00 59.19           O  
ANISOU 6441  O   HOH A2181     7178   8091   7222    -97    191     77       O  
HETATM 6442  O   HOH A2182      17.562  -4.108  18.566  1.00 59.22           O  
ANISOU 6442  O   HOH A2182     7922   7293   7286    -34    -51     20       O  
HETATM 6443  O   HOH A2183      10.522  -6.310  20.667  1.00 42.31           O  
ANISOU 6443  O   HOH A2183     5457   5466   5155   -195    309   -136       O  
HETATM 6444  O   HOH A2184      22.377  24.596  13.930  1.00 69.27           O  
ANISOU 6444  O   HOH A2184     9323   8829   8169    127    198    126       O  
HETATM 6445  O   HOH A2185       8.486  -6.705  24.402  1.00 23.91           O  
ANISOU 6445  O   HOH A2185     4024   1865   3194   -426   -425   -287       O  
HETATM 6446  O   HOH A2186       7.195  -3.702  22.664  1.00 35.28           O  
ANISOU 6446  O   HOH A2186     3225   5944   4236   -517   -621  -1913       O  
HETATM 6447  O   HOH A2187      11.338  -6.508  25.087  1.00 40.98           O  
ANISOU 6447  O   HOH A2187     5642   5011   4918   -510    -16  -1491       O  
HETATM 6448  O   HOH A2188      18.028  -7.433  24.517  1.00 55.43           O  
ANISOU 6448  O   HOH A2188     7059   7100   6903    343     80    -45       O  
HETATM 6449  O   HOH A2189      14.862  -6.427  27.227  1.00 37.61           O  
ANISOU 6449  O   HOH A2189     4428   5128   4734    419    344   -329       O  
HETATM 6450  O   HOH A2190      -3.669  31.905  33.192  1.00 60.99           O  
ANISOU 6450  O   HOH A2190     8053   8017   7102    284    -55   -175       O  
HETATM 6451  O   HOH A2191      -9.617  16.272  37.710  1.00 66.16           O  
ANISOU 6451  O   HOH A2191     8254   8927   7958   -118    167    -72       O  
HETATM 6452  O   HOH A2192       0.333  19.417  25.551  1.00  9.82           O  
ANISOU 6452  O   HOH A2192     1350   1196   1187    -19    152    188       O  
HETATM 6453  O   HOH A2193      17.048  -2.711  42.110  1.00 42.42           O  
ANISOU 6453  O   HOH A2193     6050   4993   5074    667      0   1432       O  
HETATM 6454  O   HOH A2194      18.111  -4.665  40.373  1.00 45.50           O  
ANISOU 6454  O   HOH A2194     6815   5408   5066   -122    399    412       O  
HETATM 6455  O   HOH A2195      15.689  -4.454  39.037  1.00 80.39           O  
ANISOU 6455  O   HOH A2195    10276  10266  10003     66    111    118       O  
HETATM 6456  O   HOH A2196      -6.587  17.052  18.739  1.00 23.04           O  
ANISOU 6456  O   HOH A2196     3235   3017   2501    534    152    621       O  
HETATM 6457  O   HOH A2197      -6.979  12.142  21.711  1.00 27.10           O  
ANISOU 6457  O   HOH A2197     2149   4768   3380   -556    419   -450       O  
HETATM 6458  O   HOH A2198      -4.677  12.082  17.898  1.00 45.25           O  
ANISOU 6458  O   HOH A2198     6467   5926   4799   -323   -417   -933       O  
HETATM 6459  O   HOH A2199       1.578  -5.101  44.443  1.00 28.52           O  
ANISOU 6459  O   HOH A2199     3824   4457   2556   -314    419     44       O  
HETATM 6460  O   HOH A2200      -1.975  -1.747  39.142  1.00 49.34           O  
ANISOU 6460  O   HOH A2200     6313   7054   5379   -586    482    588       O  
HETATM 6461  O   HOH A2201       4.686  -8.115  43.444  1.00 55.99           O  
ANISOU 6461  O   HOH A2201     7321   6670   7284    -85     -7    138       O  
HETATM 6462  O   HOH A2202      12.532  -7.903  40.615  1.00 67.66           O  
ANISOU 6462  O   HOH A2202     8716   8864   8129    213   -106    188       O  
HETATM 6463  O   HOH A2203      13.102  -5.366  32.373  1.00 61.46           O  
ANISOU 6463  O   HOH A2203     7930   7677   7744   -115   -244    598       O  
HETATM 6464  O   HOH A2204      11.613  -5.909  34.287  1.00 46.79           O  
ANISOU 6464  O   HOH A2204     6818   4961   5997    129     86   -475       O  
HETATM 6465  O   HOH A2205       7.405  -6.769  26.916  1.00 34.02           O  
ANISOU 6465  O   HOH A2205     6089   2446   4391   -851    245   -102       O  
HETATM 6466  O   HOH A2206      10.122  -7.901  30.774  1.00 43.91           O  
ANISOU 6466  O   HOH A2206     6992   3638   6053   -546    664    932       O  
HETATM 6467  O   HOH A2207       9.599  -7.287  33.590  1.00 49.89           O  
ANISOU 6467  O   HOH A2207     6290   5937   6727   -705    175   -299       O  
HETATM 6468  O   HOH A2208       7.307  14.369  27.280  1.00  8.85           O  
ANISOU 6468  O   HOH A2208     1243    995   1123    -74     98    183       O  
HETATM 6469  O   HOH A2209      -5.934   9.651  22.919  1.00 24.27           O  
ANISOU 6469  O   HOH A2209     2053   3848   3321   -741    162   -322       O  
HETATM 6470  O   HOH A2210      -5.136   8.056  24.936  1.00 31.90           O  
ANISOU 6470  O   HOH A2210     4261   3945   3914   -404    388   -538       O  
HETATM 6471  O   HOH A2211      -2.751   8.752  20.843  1.00 13.51           O  
ANISOU 6471  O   HOH A2211     1681   1965   1486   -331    112    405       O  
HETATM 6472  O   HOH A2212      31.173   5.345  27.217  1.00 44.36           O  
ANISOU 6472  O   HOH A2212     6228   5999   4626    757     54    -55       O  
HETATM 6473  O   HOH A2213      26.844   4.178  25.593  1.00 30.47           O  
ANISOU 6473  O   HOH A2213     4769   3456   3354   1016   -472     58       O  
HETATM 6474  O   HOH A2214      -5.583   3.498  19.814  1.00 48.75           O  
ANISOU 6474  O   HOH A2214     6651   6758   5113    288   -873   -479       O  
HETATM 6475  O   HOH A2215      -1.449  -1.420  20.207  1.00 31.86           O  
ANISOU 6475  O   HOH A2215     5967   2540   3600  -1625    375    284       O  
HETATM 6476  O   HOH A2216      -2.198   1.388  17.319  1.00 26.33           O  
ANISOU 6476  O   HOH A2216     4073   3213   2719   -484   -243   -528       O  
HETATM 6477  O   HOH A2217      28.026  21.094  23.376  1.00 25.46           O  
ANISOU 6477  O   HOH A2217     2778   2938   3958   -524    211   -254       O  
HETATM 6478  O   HOH A2218      27.379  25.914  28.577  1.00 48.74           O  
ANISOU 6478  O   HOH A2218     5442   7689   5387    141     80   -384       O  
HETATM 6479  O   HOH A2219      -4.321   2.987  17.400  1.00 47.60           O  
ANISOU 6479  O   HOH A2219     5871   6738   5477    260    426    -69       O  
HETATM 6480  O   HOH A2220      -3.228   7.426  16.829  1.00 20.55           O  
ANISOU 6480  O   HOH A2220     2723   2933   2151   -256     20    265       O  
HETATM 6481  O   HOH A2221      26.619  32.472  26.127  1.00 46.20           O  
ANISOU 6481  O   HOH A2221     5912   4714   6929   -449   -479   -326       O  
HETATM 6482  O   HOH A2222      27.569  29.888  31.880  1.00 48.83           O  
ANISOU 6482  O   HOH A2222     5760   5599   7194   -581   -163   -236       O  
HETATM 6483  O   HOH A2223      24.821  31.736  34.056  1.00 42.76           O  
ANISOU 6483  O   HOH A2223     6219   5372   4655   -162   -498     65       O  
HETATM 6484  O   HOH A2224      21.326  32.633  35.476  1.00 62.35           O  
ANISOU 6484  O   HOH A2224     8600   7753   7338   -126    -15   -118       O  
HETATM 6485  O   HOH A2225      23.710  29.350  37.848  1.00 57.70           O  
ANISOU 6485  O   HOH A2225     7893   7466   6564   -239     69   -135       O  
HETATM 6486  O   HOH A2226      15.968  34.007  30.290  1.00 50.23           O  
ANISOU 6486  O   HOH A2226     6050   6191   6843    367    -89     42       O  
HETATM 6487  O   HOH A2227       1.740   1.536  24.348  1.00 18.90           O  
ANISOU 6487  O   HOH A2227     3805   1363   2011   -266    879    402       O  
HETATM 6488  O   HOH A2228       7.128   1.023  18.920  1.00 27.62           O  
ANISOU 6488  O   HOH A2228     2458   5892   2144    -11   -136   1119       O  
HETATM 6489  O   HOH A2229       9.260  34.321  31.212  1.00 48.29           O  
ANISOU 6489  O   HOH A2229     6304   5224   6821    229    447   -531       O  
HETATM 6490  O   HOH A2230       5.257  29.545  33.610  1.00 39.72           O  
ANISOU 6490  O   HOH A2230     5157   4364   5573    429   -688   -306       O  
HETATM 6491  O   HOH A2231      10.428  26.081  36.813  1.00 45.00           O  
ANISOU 6491  O   HOH A2231     6100   5126   5871    168     93    153       O  
HETATM 6492  O   HOH A2232      11.719  30.706  37.027  1.00 52.82           O  
ANISOU 6492  O   HOH A2232     7552   6913   5603    -87    255   -747       O  
HETATM 6493  O   HOH A2233       3.066  -2.482  25.215  1.00 17.89           O  
ANISOU 6493  O   HOH A2233     2634   1642   2521   -349    119    -20       O  
HETATM 6494  O   HOH A2234       8.800   0.772  27.705  1.00 11.45           O  
ANISOU 6494  O   HOH A2234     1759   1253   1338   -383    204    128       O  
HETATM 6495  O   HOH A2235       3.339  30.743  29.735  1.00 54.78           O  
ANISOU 6495  O   HOH A2235     7480   6020   7313    152    173   -156       O  
HETATM 6496  O   HOH A2236       9.664  35.109  22.408  1.00 58.01           O  
ANISOU 6496  O   HOH A2236     8637   6786   6620     41    293     24       O  
HETATM 6497  O   HOH A2237      11.918  34.463  23.522  1.00 46.21           O  
ANISOU 6497  O   HOH A2237     6535   4630   6391    -70    901   -527       O  
HETATM 6498  O   HOH A2238       3.220  -4.082  27.492  1.00 23.17           O  
ANISOU 6498  O   HOH A2238     3533   2851   2419  -1051    356    -88       O  
HETATM 6499  O   HOH A2239       5.432  -6.351  32.006  1.00 30.34           O  
ANISOU 6499  O   HOH A2239     5007   2599   3922    380     88    496       O  
HETATM 6500  O   HOH A2240      19.857  30.903  13.824  1.00 57.48           O  
ANISOU 6500  O   HOH A2240     7281   7561   7000    -18    251   -303       O  
HETATM 6501  O   HOH A2241      17.502  27.560   5.479  1.00 54.47           O  
ANISOU 6501  O   HOH A2241     6335   7431   6929     41   -206    219       O  
HETATM 6502  O   HOH A2242      13.863  16.011  26.464  1.00  9.29           O  
ANISOU 6502  O   HOH A2242     1262   1141   1128   -115     96     58       O  
HETATM 6503  O   HOH A2243      18.353  23.739  -1.169  1.00 57.88           O  
ANISOU 6503  O   HOH A2243     6876   7912   7204    204     88    363       O  
HETATM 6504  O   HOH A2244      14.662  26.061  -6.178  1.00 44.00           O  
ANISOU 6504  O   HOH A2244     5264   6807   4646   -712    500    634       O  
HETATM 6505  O   HOH A2245      17.129  29.341  -3.354  1.00 60.15           O  
ANISOU 6505  O   HOH A2245     7209   8163   7483   -171    371    304       O  
HETATM 6506  O   HOH A2246       4.203  32.098  -4.761  1.00 35.45           O  
ANISOU 6506  O   HOH A2246     4928   4099   4443    983   -723   1225       O  
HETATM 6507  O   HOH A2247       5.759  34.618  -4.329  1.00 52.24           O  
ANISOU 6507  O   HOH A2247     7215   6243   6390    121     37    575       O  
HETATM 6508  O   HOH A2248      11.819  28.863  -6.828  1.00 53.79           O  
ANISOU 6508  O   HOH A2248     7673   7301   5465    271   -190   -105       O  
HETATM 6509  O   HOH A2249      22.181  19.464  42.108  1.00 46.00           O  
ANISOU 6509  O   HOH A2249     6417   6066   4994   -233   -888   -140       O  
HETATM 6510  O   HOH A2250      23.471  16.625  44.273  1.00 50.42           O  
ANISOU 6510  O   HOH A2250     6595   7169   5392    261   -184   -181       O  
HETATM 6511  O   HOH A2251      24.061  13.680  45.218  1.00 42.39           O  
ANISOU 6511  O   HOH A2251     5763   5857   4485   -519   -624     69       O  
HETATM 6512  O   HOH A2252      26.554  14.272  43.345  1.00 29.54           O  
ANISOU 6512  O   HOH A2252     3604   3952   3669    218   -636    245       O  
HETATM 6513  O   HOH A2253      25.157   8.691  42.763  1.00 17.84           O  
ANISOU 6513  O   HOH A2253     3102   2061   1616    459   -508    164       O  
HETATM 6514  O   HOH A2254      11.428  30.794  14.170  1.00 15.14           O  
ANISOU 6514  O   HOH A2254     2145   2066   1542   -178    -72    333       O  
HETATM 6515  O   HOH A2255      11.455  33.783  10.822  1.00 19.40           O  
ANISOU 6515  O   HOH A2255     3238   1850   2284   -741    419    500       O  
HETATM 6516  O   HOH A2256      28.151  12.606  41.524  1.00 18.34           O  
ANISOU 6516  O   HOH A2256     2026   3004   1939    -55   -570     26       O  
HETATM 6517  O   HOH A2257      31.024   9.555  40.096  1.00 47.46           O  
ANISOU 6517  O   HOH A2257     5460   6704   5869    357   -799    -90       O  
HETATM 6518  O   HOH A2258       6.677  36.511  15.221  1.00 37.42           O  
ANISOU 6518  O   HOH A2258     6705   3337   4175     87    155    162       O  
HETATM 6519  O   HOH A2259      12.447  36.099   7.441  1.00 85.79           O  
ANISOU 6519  O   HOH A2259    10935  11278  10382     24     11    116       O  
HETATM 6520  O   HOH A2260      14.106  33.427  11.554  1.00 19.84           O  
ANISOU 6520  O   HOH A2260     3125   2189   2226   -676    -47    250       O  
HETATM 6521  O   HOH A2261      32.483  10.133  38.166  1.00 47.38           O  
ANISOU 6521  O   HOH A2261     5801   5864   6337     85   -112     49       O  
HETATM 6522  O   HOH A2262      35.232   0.400  38.262  1.00 53.80           O  
ANISOU 6522  O   HOH A2262     7340   7124   5977    725   -760    299       O  
HETATM 6523  O   HOH A2263      28.745   4.646  39.193  1.00 22.02           O  
ANISOU 6523  O   HOH A2263     2921   2922   2522    331   -157    678       O  
HETATM 6524  O   HOH A2264       0.658  33.885  -6.807  1.00 46.18           O  
ANISOU 6524  O   HOH A2264     5191   6257   6097    666   -196    210       O  
HETATM 6525  O   HOH A2265      35.768   8.235  31.281  1.00 38.86           O  
ANISOU 6525  O   HOH A2265     4862   4964   4939   1364    521    113       O  
HETATM 6526  O   HOH A2266      35.199   8.202  37.462  1.00 51.52           O  
ANISOU 6526  O   HOH A2266     6373   7209   5994   -417   -557   -265       O  
HETATM 6527  O   HOH A2267      34.057  11.131  35.977  1.00 37.29           O  
ANISOU 6527  O   HOH A2267     4247   5235   4686   -155   -887    756       O  
HETATM 6528  O   HOH A2268     -10.419  17.707  17.344  1.00 61.10           O  
ANISOU 6528  O   HOH A2268     7107   8032   8077    -65     96    238       O  
HETATM 6529  O   HOH A2269      31.610  18.426  32.236  1.00 38.56           O  
ANISOU 6529  O   HOH A2269     4681   5198   4770   -827      0   -546       O  
HETATM 6530  O   HOH A2270      33.670  17.501  33.612  1.00 57.53           O  
ANISOU 6530  O   HOH A2270     6847   8304   6710   -319    298    151       O  
HETATM 6531  O   HOH A2271      32.489   9.946  28.866  1.00 23.04           O  
ANISOU 6531  O   HOH A2271     1720   3698   3334     87    153   -360       O  
HETATM 6532  O   HOH A2272      34.332  13.878  27.029  1.00 42.71           O  
ANISOU 6532  O   HOH A2272     4263   6959   5005   -284    620    417       O  
HETATM 6533  O   HOH A2273      35.498  16.321  31.522  1.00 42.55           O  
ANISOU 6533  O   HOH A2273     4136   6280   5749   -686   -226   -245       O  
HETATM 6534  O   HOH A2274      -9.624  31.908  13.439  1.00 35.18           O  
ANISOU 6534  O   HOH A2274     4586   4028   4752   1284    -44    503       O  
HETATM 6535  O   HOH A2275     -17.441  20.998  12.648  1.00 79.01           O  
ANISOU 6535  O   HOH A2275    10206  10416   9399    -90    206     89       O  
HETATM 6536  O   HOH A2276      -3.779  26.910  18.627  1.00 13.91           O  
ANISOU 6536  O   HOH A2276     1926   1865   1495    378     63     -3       O  
HETATM 6537  O   HOH A2277      -5.319  31.134  19.349  1.00 34.07           O  
ANISOU 6537  O   HOH A2277     5384   4425   3135    905     41  -1379       O  
HETATM 6538  O   HOH A2278      -9.882  33.200  17.377  1.00 63.53           O  
ANISOU 6538  O   HOH A2278     7626   8625   7890    290    202   -205       O  
HETATM 6539  O   HOH A2279      -7.867  32.627  18.949  1.00 46.80           O  
ANISOU 6539  O   HOH A2279     6569   6689   4525    518    348   -536       O  
HETATM 6540  O   HOH A2280      29.195  18.470  27.513  1.00 24.99           O  
ANISOU 6540  O   HOH A2280     2819   3804   2872   -250   -115    559       O  
HETATM 6541  O   HOH A2281      -6.550  34.875  12.902  1.00 30.36           O  
ANISOU 6541  O   HOH A2281     3478   3890   4165   1053   -177   1239       O  
HETATM 6542  O   HOH A2282      -1.917  36.623  12.653  1.00 35.79           O  
ANISOU 6542  O   HOH A2282     5212   3279   5108    433    301    198       O  
HETATM 6543  O   HOH A2283      -4.688  28.910  22.358  1.00 38.93           O  
ANISOU 6543  O   HOH A2283     4099   5344   5348    956    805   -626       O  
HETATM 6544  O   HOH A2284      -1.472  31.598  25.220  1.00 39.76           O  
ANISOU 6544  O   HOH A2284     5797   5459   3850    -39    331   -174       O  
HETATM 6545  O   HOH A2285      32.219  14.921  34.565  1.00 24.21           O  
ANISOU 6545  O   HOH A2285     2203   3433   3563   -209    -10   -142       O  
HETATM 6546  O   HOH A2286       0.281  36.748   6.213  1.00 64.40           O  
ANISOU 6546  O   HOH A2286     8279   7893   8297   -215     52    141       O  
HETATM 6547  O   HOH A2287      32.344  25.867  34.335  1.00 68.28           O  
ANISOU 6547  O   HOH A2287     8928   8919   8098      2    121    -52       O  
HETATM 6548  O   HOH A2288      29.804  23.145  34.819  1.00 43.79           O  
ANISOU 6548  O   HOH A2288     4255   5615   6770   -653    -15   -342       O  
HETATM 6549  O   HOH A2289       6.632  34.578  17.263  1.00 24.18           O  
ANISOU 6549  O   HOH A2289     3818   2233   3137    315    321    202       O  
HETATM 6550  O   HOH A2290      -0.102  36.098  22.990  1.00 85.91           O  
ANISOU 6550  O   HOH A2290    10925  11439  10279    117    -16      1       O  
HETATM 6551  O   HOH A2291       4.183  34.792  22.664  1.00 60.36           O  
ANISOU 6551  O   HOH A2291     7821   8071   7042    433     41   -164       O  
HETATM 6552  O   HOH A2292      -6.896  35.784  17.364  1.00 44.00           O  
ANISOU 6552  O   HOH A2292     5687   5451   5581   1539    554   -565       O  
HETATM 6553  O   HOH A2293       7.567  32.268  16.016  1.00 15.66           O  
ANISOU 6553  O   HOH A2293     2395   1648   1907   -258    -18    293       O  
HETATM 6554  O   HOH A2294      27.821  22.198  37.817  1.00 26.10           O  
ANISOU 6554  O   HOH A2294     3603   3400   2913  -1138  -1030     75       O  
HETATM 6555  O   HOH A2295      29.687  19.790  40.470  1.00 35.44           O  
ANISOU 6555  O   HOH A2295     4271   4846   4350    108  -1058   -181       O  
HETATM 6556  O   HOH A2296      25.413  20.368  42.791  1.00 71.72           O  
ANISOU 6556  O   HOH A2296     9410   9558   8284     81    -43     37       O  
HETATM 6557  O   HOH A2297      22.395  24.080  39.761  1.00 28.41           O  
ANISOU 6557  O   HOH A2297     4269   3089   3439    -18     91   -227       O  
HETATM 6558  O   HOH A2298      24.038  25.048  36.221  1.00 29.80           O  
ANISOU 6558  O   HOH A2298     5324   2325   3676   -318    922    146       O  
HETATM 6559  O   HOH A2299      26.652  24.521  34.546  1.00 21.25           O  
ANISOU 6559  O   HOH A2299     2665   2563   2846   -424   -775    -38       O  
HETATM 6560  O   HOH A2300      30.234  20.414  33.354  1.00 26.67           O  
ANISOU 6560  O   HOH A2300     2371   4525   3237   -279   -379    299       O  
HETATM 6561  O   HOH A2301     -11.152  15.275   7.046  1.00 41.87           O  
ANISOU 6561  O   HOH A2301     5410   5721   4780   -203    251   -315       O  
HETATM 6562  O   HOH A2302     -12.833  15.461   4.968  1.00 49.99           O  
ANISOU 6562  O   HOH A2302     6717   6168   6109   -180    259    330       O  
HETATM 6563  O   HOH A2303      18.290  30.535  35.038  1.00 72.61           O  
ANISOU 6563  O   HOH A2303     9154   9394   9041    266    240     87       O  
HETATM 6564  O   HOH A2304      17.783  28.637  37.270  1.00 40.99           O  
ANISOU 6564  O   HOH A2304     6207   5146   4222    543    948   -877       O  
HETATM 6565  O   HOH A2305     -20.022  16.022  -1.132  1.00 53.90           O  
ANISOU 6565  O   HOH A2305     7307   6671   6501   -384    166     -4       O  
HETATM 6566  O   HOH A2306     -11.491  15.133   2.667  1.00 44.40           O  
ANISOU 6566  O   HOH A2306     6286   4928   5655    102    183    655       O  
HETATM 6567  O   HOH A2307      -7.336  14.975   4.266  1.00 26.08           O  
ANISOU 6567  O   HOH A2307     4509   2841   2559    496   -479     39       O  
HETATM 6568  O   HOH A2308      -9.358  11.336   0.142  1.00 58.11           O  
ANISOU 6568  O   HOH A2308     7489   7684   6906    356    184    106       O  
HETATM 6569  O   HOH A2309      -7.894  10.285   1.994  1.00 38.46           O  
ANISOU 6569  O   HOH A2309     4215   5677   4722    569    288    487       O  
HETATM 6570  O   HOH A2310      -4.678  16.200  -7.027  1.00 33.78           O  
ANISOU 6570  O   HOH A2310     4267   4426   4144   1153     -5   -474       O  
HETATM 6571  O   HOH A2311      -4.984   8.705  -3.287  1.00 37.21           O  
ANISOU 6571  O   HOH A2311     5006   4860   4272    -91   -106   -575       O  
HETATM 6572  O   HOH A2312      -5.275  17.728  -9.201  1.00 35.06           O  
ANISOU 6572  O   HOH A2312     4450   4643   4229    192   -379   -139       O  
HETATM 6573  O   HOH A2313      -5.223  21.727 -10.413  1.00 49.02           O  
ANISOU 6573  O   HOH A2313     6588   7211   4828    225   -243     29       O  
HETATM 6574  O   HOH A2314      17.805   7.978  24.592  1.00 10.50           O  
ANISOU 6574  O   HOH A2314     1408   1147   1436    -65    -69    112       O  
HETATM 6575  O   HOH A2315      -9.297  24.639 -11.637  1.00 41.96           O  
ANISOU 6575  O   HOH A2315     5234   6265   4446    959   -257    117       O  
HETATM 6576  O   HOH A2316      -9.572  21.603 -11.796  1.00 59.35           O  
ANISOU 6576  O   HOH A2316     7391   7980   7178    116   -356    291       O  
HETATM 6577  O   HOH A2317      -2.924  25.177 -12.844  1.00 72.14           O  
ANISOU 6577  O   HOH A2317     9269   9439   8703    -95    -68     91       O  
HETATM 6578  O   HOH A2318       0.049  28.049 -14.223  1.00 55.05           O  
ANISOU 6578  O   HOH A2318     6495   7545   6875    537    294    -82       O  
HETATM 6579  O   HOH A2319       0.396  22.601 -13.593  1.00 41.85           O  
ANISOU 6579  O   HOH A2319     5144   6961   3795   1131    758     11       O  
HETATM 6580  O   HOH A2320      16.696  13.668  21.151  1.00 10.06           O  
ANISOU 6580  O   HOH A2320     1327   1149   1345    -63     69    301       O  
HETATM 6581  O   HOH A2321      -0.460  17.627 -11.267  1.00 42.00           O  
ANISOU 6581  O   HOH A2321     5272   6433   4252   -153    314   -199       O  
HETATM 6582  O   HOH A2322      28.473  11.232  22.835  1.00 26.79           O  
ANISOU 6582  O   HOH A2322     2497   4503   3177   -717   -395   -734       O  
HETATM 6583  O   HOH A2323      30.005   7.006  23.365  1.00 26.69           O  
ANISOU 6583  O   HOH A2323     2616   5132   2394    903     -9    559       O  
HETATM 6584  O   HOH A2324      31.132  10.640  21.879  1.00 52.39           O  
ANISOU 6584  O   HOH A2324     6410   7029   6467     39    125     -5       O  
HETATM 6585  O   HOH A2325      31.533  11.285  16.086  1.00 39.10           O  
ANISOU 6585  O   HOH A2325     3991   5533   5332   -138     45    217       O  
HETATM 6586  O   HOH A2326      -8.200   5.499  11.549  1.00 85.43           O  
ANISOU 6586  O   HOH A2326    10792  11176  10493    -49    118    228       O  
HETATM 6587  O   HOH A2327      -4.966   6.665   1.605  1.00 30.22           O  
ANISOU 6587  O   HOH A2327     4477   3947   3058   -607    -79   -436       O  
HETATM 6588  O   HOH A2328      33.937   4.273  15.881  1.00 47.86           O  
ANISOU 6588  O   HOH A2328     5067   6684   6434    530    179   -146       O  
HETATM 6589  O   HOH A2329      34.255   8.286  24.526  1.00 62.18           O  
ANISOU 6589  O   HOH A2329     7812   8229   7586     62   -104    -48       O  
HETATM 6590  O   HOH A2330      -8.458   5.338   4.788  1.00 61.82           O  
ANISOU 6590  O   HOH A2330     7666   8165   7656    196     27     90       O  
HETATM 6591  O   HOH A2331      -7.829   6.156   2.355  1.00 61.56           O  
ANISOU 6591  O   HOH A2331     8043   7717   7632   -138     31    155       O  
HETATM 6592  O   HOH A2332      -6.241   4.736   5.980  1.00 37.20           O  
ANISOU 6592  O   HOH A2332     4657   4872   4606    -54    -43   -378       O  
HETATM 6593  O   HOH A2333      30.631  -0.434   6.262  1.00 51.87           O  
ANISOU 6593  O   HOH A2333     6158   7425   6124    535    -87   -140       O  
HETATM 6594  O   HOH A2334      24.699   1.212   9.653  1.00 29.09           O  
ANISOU 6594  O   HOH A2334     3890   3708   3457    461   -172   -453       O  
HETATM 6595  O   HOH A2335      28.081   1.073  13.450  1.00 22.69           O  
ANISOU 6595  O   HOH A2335     3175   2396   3052    281    572   -322       O  
HETATM 6596  O   HOH A2336      26.586   0.723   3.026  1.00 21.24           O  
ANISOU 6596  O   HOH A2336     2913   2755   2404    161   -180    307       O  
HETATM 6597  O   HOH A2337      29.522   6.549   8.248  1.00 28.63           O  
ANISOU 6597  O   HOH A2337     3299   4474   3106    168   1349   -161       O  
HETATM 6598  O   HOH A2338      -2.285   8.230  -6.652  1.00 30.96           O  
ANISOU 6598  O   HOH A2338     3423   4150   4191    335   -380    185       O  
HETATM 6599  O   HOH A2339      -1.359  11.768 -10.177  1.00 40.28           O  
ANISOU 6599  O   HOH A2339     5469   4788   5048     33   -504     34       O  
HETATM 6600  O   HOH A2340      -1.877  15.363 -15.659  1.00 46.39           O  
ANISOU 6600  O   HOH A2340     5424   6617   5586    354    458    126       O  
HETATM 6601  O   HOH A2341      28.810  11.959  15.979  1.00 19.15           O  
ANISOU 6601  O   HOH A2341     2058   2570   2646    149    327   -450       O  
HETATM 6602  O   HOH A2342      30.286   8.426   6.673  1.00 55.18           O  
ANISOU 6602  O   HOH A2342     6683   7583   6699    428    469    134       O  
HETATM 6603  O   HOH A2343      30.991  13.052   9.090  1.00 55.65           O  
ANISOU 6603  O   HOH A2343     7285   6618   7241   -167     94    112       O  
HETATM 6604  O   HOH A2344      31.964   5.408   9.413  1.00 58.13           O  
ANISOU 6604  O   HOH A2344     6754   7749   7584   -100    191   -167       O  
HETATM 6605  O   HOH A2345      -0.630  -5.202  14.690  1.00 40.75           O  
ANISOU 6605  O   HOH A2345     5364   5962   4158   -392   -117     45       O  
HETATM 6606  O   HOH A2346       3.558  -7.243  12.339  1.00 40.95           O  
ANISOU 6606  O   HOH A2346     5833   5278   4449   -533    164   -423       O  
HETATM 6607  O   HOH A2347      27.076  17.130   9.163  1.00 61.60           O  
ANISOU 6607  O   HOH A2347     7952   7573   7881   -247   -111   -424       O  
HETATM 6608  O   HOH A2348      -2.610  -3.064   5.103  1.00 57.42           O  
ANISOU 6608  O   HOH A2348     7432   7437   6950   -493     69   -113       O  
HETATM 6609  O   HOH A2349      19.169  13.455   8.755  1.00 41.89           O  
ANISOU 6609  O   HOH A2349     5295   6121   4501     90    544   -357       O  
HETATM 6610  O   HOH A2350      26.747  15.543   3.056  1.00 44.39           O  
ANISOU 6610  O   HOH A2350     5826   6034   5007   -394     27    369       O  
HETATM 6611  O   HOH A2351      20.767  16.639   6.901  1.00 46.64           O  
ANISOU 6611  O   HOH A2351     6210   6046   5465    153    -37    169       O  
HETATM 6612  O   HOH A2352      22.351  18.723   6.645  1.00 41.91           O  
ANISOU 6612  O   HOH A2352     4951   5348   5624    315    -73    610       O  
HETATM 6613  O   HOH A2353      -6.160   3.319  -1.078  1.00 47.46           O  
ANISOU 6613  O   HOH A2353     5275   6473   6285     88   -228    -88       O  
HETATM 6614  O   HOH A2354       0.529   9.438 -10.439  1.00 34.28           O  
ANISOU 6614  O   HOH A2354     3794   5764   3469    -63   -453    -88       O  
HETATM 6615  O   HOH A2355      21.669  11.726  17.189  1.00 10.05           O  
ANISOU 6615  O   HOH A2355     1353   1106   1361   -101     79    202       O  
HETATM 6616  O   HOH A2356      15.968  10.495  11.339  1.00 10.16           O  
ANISOU 6616  O   HOH A2356     1206   1345   1309     99     93     62       O  
HETATM 6617  O   HOH A2357      17.145  12.227   9.311  1.00 28.23           O  
ANISOU 6617  O   HOH A2357     3991   2547   4189    513    776   -122       O  
HETATM 6618  O   HOH A2358      23.908  11.020  15.381  1.00 13.91           O  
ANISOU 6618  O   HOH A2358     1516   2063   1706    105     63    508       O  
HETATM 6619  O   HOH A2359      -2.893  17.382 -10.690  1.00 51.83           O  
ANISOU 6619  O   HOH A2359     6552   6845   6295    411     84   -228       O  
HETATM 6620  O   HOH A2360      19.645  -0.364  16.383  1.00 26.03           O  
ANISOU 6620  O   HOH A2360     4447   2773   2671   -269   -427    400       O  
HETATM 6621  O   HOH A2361      28.651  -1.972  21.012  1.00 73.62           O  
ANISOU 6621  O   HOH A2361     9225   9515   9233    183    -42    278       O  
HETATM 6622  O   HOH A2362      29.824   1.581  22.323  1.00 77.87           O  
ANISOU 6622  O   HOH A2362     9635  10348   9606    106    -20    130       O  
HETATM 6623  O   HOH A2363      24.942  -1.012  18.564  1.00 43.92           O  
ANISOU 6623  O   HOH A2363     5798   5028   5862    898    207   -683       O  
HETATM 6624  O   HOH A2364      18.807   0.837  23.504  1.00 24.98           O  
ANISOU 6624  O   HOH A2364     3308   2576   3608      4    351    939       O  
HETATM 6625  O   HOH A2365      27.293   0.524  17.827  1.00 38.73           O  
ANISOU 6625  O   HOH A2365     6879   3679   4159    810   -254    815       O  
HETATM 6626  O   HOH A2366      29.559   1.159  19.854  1.00 37.58           O  
ANISOU 6626  O   HOH A2366     3828   5166   5287    623   -119    752       O  
HETATM 6627  O   HOH A2367      19.854  -0.104  20.220  1.00 20.66           O  
ANISOU 6627  O   HOH A2367     2652   2029   3168     92    -40    278       O  
HETATM 6628  O   HOH A2368      29.414  16.382  23.791  1.00 54.04           O  
ANISOU 6628  O   HOH A2368     6138   7306   7087   -334    443    -35       O  
HETATM 6629  O   HOH A2369      29.727  14.552  12.709  1.00 80.87           O  
ANISOU 6629  O   HOH A2369    10312  10702   9713      3     28    191       O  
HETATM 6630  O   HOH A2370      17.020  -1.000  22.796  1.00 23.51           O  
ANISOU 6630  O   HOH A2370     2886   2128   3919     29    890    477       O  
HETATM 6631  O   HOH A2371      14.169   2.925  27.341  1.00 10.37           O  
ANISOU 6631  O   HOH A2371     1822    958   1159    -79     86    240       O  
HETATM 6632  O   HOH A2372      11.107   2.844  25.014  1.00 12.93           O  
ANISOU 6632  O   HOH A2372     1970   1155   1788   -263     90    106       O  
HETATM 6633  O   HOH A2373      16.434   5.877  22.604  1.00 10.88           O  
ANISOU 6633  O   HOH A2373     1557   1165   1411     22    -28     49       O  
HETATM 6634  O   HOH A2374      10.119   2.832  22.079  1.00 34.83           O  
ANISOU 6634  O   HOH A2374     5796   2969   4468   -648  -1315    404       O  
HETATM 6635  O   HOH A2375      26.484  27.607  20.446  1.00 49.94           O  
ANISOU 6635  O   HOH A2375     5233   7329   6413    103    480   -477       O  
HETATM 6636  O   HOH A2376       8.397   2.322  17.324  1.00 32.60           O  
ANISOU 6636  O   HOH A2376     5799   2839   3748    139   -792    -22       O  
HETATM 6637  O   HOH A2377       9.153   3.085  19.768  1.00 30.60           O  
ANISOU 6637  O   HOH A2377     3563   3477   4586    125   -317    -38       O  
HETATM 6638  O   HOH A2378      11.583   1.942  13.377  1.00 73.15           O  
ANISOU 6638  O   HOH A2378     9228   9916   8650      6     75    170       O  
HETATM 6639  O   HOH A2379       9.708   0.196  14.281  1.00 45.54           O  
ANISOU 6639  O   HOH A2379     5766   5315   6222   -507   -184    868       O  
HETATM 6640  O   HOH A2380      15.954  -0.123  18.907  1.00 24.71           O  
ANISOU 6640  O   HOH A2380     4760   1814   2814   -953   -275    -54       O  
HETATM 6641  O   HOH A2381      16.924  -2.711  14.706  1.00 47.28           O  
ANISOU 6641  O   HOH A2381     7171   4957   5836    175   -506   -142       O  
HETATM 6642  O   HOH A2382      17.559  -1.712  17.296  1.00 40.34           O  
ANISOU 6642  O   HOH A2382     5374   4348   5604     99    543  -1373       O  
HETATM 6643  O   HOH A2383      24.967  32.822  21.040  1.00 45.12           O  
ANISOU 6643  O   HOH A2383     5581   5968   5596   -529    635    -77       O  
HETATM 6644  O   HOH A2384      24.669  33.447  16.458  1.00 51.40           O  
ANISOU 6644  O   HOH A2384     6059   6881   6592   -133    531    -49       O  
HETATM 6645  O   HOH A2385      19.217  25.735  13.186  1.00 46.12           O  
ANISOU 6645  O   HOH A2385     5396   6546   5581     30     -6    858       O  
HETATM 6646  O   HOH A2386      15.781  -4.398  20.822  1.00 56.79           O  
ANISOU 6646  O   HOH A2386     7695   7414   6467     -8     48    243       O  
HETATM 6647  O   HOH A2387      13.207  -5.701  21.916  1.00 51.97           O  
ANISOU 6647  O   HOH A2387     6894   6040   6814   -292   -475   -356       O  
HETATM 6648  O   HOH A2388      16.632  -2.239  20.520  1.00 34.49           O  
ANISOU 6648  O   HOH A2388     6074   3515   3518    265    208   -428       O  
HETATM 6649  O   HOH A2389      21.976  38.781  19.492  1.00 39.15           O  
ANISOU 6649  O   HOH A2389     4276   6729   3869   -276   -846  -1188       O  
HETATM 6650  O   HOH A2390       9.565  36.900  20.129  1.00 65.40           O  
ANISOU 6650  O   HOH A2390     8145   8707   7998      8    104   -185       O  
HETATM 6651  O   HOH A2391      11.864  34.452  14.759  1.00 43.82           O  
ANISOU 6651  O   HOH A2391     6237   5666   4747    250   -841   1287       O  
HETATM 6652  O   HOH A2392      11.231  36.726  15.138  1.00 30.75           O  
ANISOU 6652  O   HOH A2392     5160   2219   4305   -209   -557    529       O  
HETATM 6653  O   HOH A2393      12.182  35.950  19.292  1.00 39.47           O  
ANISOU 6653  O   HOH A2393     5643   5083   4270   -682    168   -359       O  
HETATM 6654  O   HOH A2394      10.937  37.635  17.826  1.00 65.26           O  
ANISOU 6654  O   HOH A2394     7977   8866   7952   -106     93    -35       O  
HETATM 6655  O   HOH A2395       9.385  -4.836  22.580  1.00 34.34           O  
ANISOU 6655  O   HOH A2395     4795   3582   4671   -364    141     58       O  
HETATM 6656  O   HOH A2396      24.152  36.838  19.008  1.00 40.65           O  
ANISOU 6656  O   HOH A2396     5082   5209   5156    447    673    130       O  
HETATM 6657  O   HOH A2397      18.802  -6.498  26.628  1.00 39.66           O  
ANISOU 6657  O   HOH A2397     5833   4481   4754    613     76    599       O  
HETATM 6658  O   HOH A2398      22.221  -4.587  26.795  1.00 39.75           O  
ANISOU 6658  O   HOH A2398     5510   5258   4334    654   -737   -194       O  
HETATM 6659  O   HOH A2399      12.214  -5.467  27.471  1.00 20.04           O  
ANISOU 6659  O   HOH A2399     3195   1692   2729   -385    313    168       O  
HETATM 6660  O   HOH A2400       2.658  33.899  25.870  1.00 58.30           O  
ANISOU 6660  O   HOH A2400     7757   7822   6573    100    148   -114       O  
HETATM 6661  O   HOH A2401       6.639  34.837  21.699  1.00 39.74           O  
ANISOU 6661  O   HOH A2401     7638   2790   4672   -459     73    340       O  
HETATM 6662  O   HOH A2402       1.209  31.783  29.119  1.00 62.91           O  
ANISOU 6662  O   HOH A2402     8345   7711   7848    154   -366   -158       O  
HETATM 6663  O   HOH A2403      -6.494  28.327  30.430  1.00 38.62           O  
ANISOU 6663  O   HOH A2403     3529   5379   5764    842    755   -673       O  
HETATM 6664  O   HOH A2404      -3.700  31.429  30.353  1.00 44.30           O  
ANISOU 6664  O   HOH A2404     7402   3805   5626    128    402   -304       O  
HETATM 6665  O   HOH A2405      16.068  -0.335  26.149  1.00 43.01           O  
ANISOU 6665  O   HOH A2405     5424   4942   5975    139    334   -102       O  
HETATM 6666  O   HOH A2406      18.082   2.379  26.087  1.00 18.78           O  
ANISOU 6666  O   HOH A2406     2717   2133   2287    320    509    804       O  
HETATM 6667  O   HOH A2407      -1.865  30.029  33.813  1.00 35.37           O  
ANISOU 6667  O   HOH A2407     5171   4037   4230    588   -358   -680       O  
HETATM 6668  O   HOH A2408      24.967  -0.036  24.544  1.00 38.27           O  
ANISOU 6668  O   HOH A2408     4331   6451   3759   1605     23    -98       O  
HETATM 6669  O   HOH A2409      21.826  -0.209  22.369  1.00 20.76           O  
ANISOU 6669  O   HOH A2409     3205   2163   2522    271     16    144       O  
HETATM 6670  O   HOH A2410      -0.730  14.545  44.161  1.00 31.38           O  
ANISOU 6670  O   HOH A2410     5409   3479   3034   -284     77    171       O  
HETATM 6671  O   HOH A2411       4.478  23.056  42.036  1.00 18.16           O  
ANISOU 6671  O   HOH A2411     2305   2555   2039   -131   -133     10       O  
HETATM 6672  O   HOH A2412      -4.340  19.793  43.413  1.00 32.33           O  
ANISOU 6672  O   HOH A2412     4240   5006   3038    130   -163   -399       O  
HETATM 6673  O   HOH A2413      -7.112  12.612  38.625  1.00 52.26           O  
ANISOU 6673  O   HOH A2413     6618   6652   6589   -437   -400    302       O  
HETATM 6674  O   HOH A2414      21.013  -7.113  30.621  1.00 54.80           O  
ANISOU 6674  O   HOH A2414     7452   6662   6708     76    152    387       O  
HETATM 6675  O   HOH A2415      25.545   0.469  30.118  1.00 37.89           O  
ANISOU 6675  O   HOH A2415     4316   3855   6226   1039    465    294       O  
HETATM 6676  O   HOH A2416      25.869  -1.602  33.724  1.00 46.02           O  
ANISOU 6676  O   HOH A2416     5258   7395   4831    599   -302   -383       O  
HETATM 6677  O   HOH A2417      -7.616  25.794  31.531  1.00 51.08           O  
ANISOU 6677  O   HOH A2417     5812   7049   6546    494    100   -197       O  
HETATM 6678  O   HOH A2418      -7.639  14.802  36.932  1.00 37.63           O  
ANISOU 6678  O   HOH A2418     3689   6008   4599     71    465    524       O  
HETATM 6679  O   HOH A2419     -12.486  10.808  30.378  1.00 58.55           O  
ANISOU 6679  O   HOH A2419     6469   7948   7830    357    -80     -7       O  
HETATM 6680  O   HOH A2420      -8.162  11.334  34.969  1.00 38.03           O  
ANISOU 6680  O   HOH A2420     4308   4986   5156    -94    991    987       O  
HETATM 6681  O   HOH A2421      -8.939   9.466  31.174  1.00 53.01           O  
ANISOU 6681  O   HOH A2421     7133   6675   6334   -224   -113    188       O  
HETATM 6682  O   HOH A2422     -10.524  12.768  27.212  1.00 30.11           O  
ANISOU 6682  O   HOH A2422     3191   4500   3749   -515    445    121       O  
HETATM 6683  O   HOH A2423     -11.968  17.133  28.761  1.00 46.15           O  
ANISOU 6683  O   HOH A2423     5181   6587   5766    664    236    231       O  
HETATM 6684  O   HOH A2424     -11.931  14.854  24.910  1.00 54.49           O  
ANISOU 6684  O   HOH A2424     6580   7415   6711   -161   -125   -130       O  
HETATM 6685  O   HOH A2425      16.980  -6.708  28.910  1.00 30.33           O  
ANISOU 6685  O   HOH A2425     4416   2971   4138    -72   -400   -698       O  
HETATM 6686  O   HOH A2426     -10.438  11.486  24.750  1.00 38.89           O  
ANISOU 6686  O   HOH A2426     4229   5543   5003  -1214    372   -488       O  
HETATM 6687  O   HOH A2427      -8.035   7.329  27.140  1.00 76.88           O  
ANISOU 6687  O   HOH A2427     9783  10187   9241     56     -6    -15       O  
HETATM 6688  O   HOH A2428     -13.831  16.662  24.450  1.00 66.10           O  
ANISOU 6688  O   HOH A2428     7967   9146   8003     42   -123    160       O  
HETATM 6689  O   HOH A2429      -8.267  27.680  20.798  1.00 61.93           O  
ANISOU 6689  O   HOH A2429     8178   8122   7230    469   -241     21       O  
HETATM 6690  O   HOH A2430      16.482  -0.755  40.072  1.00 19.25           O  
ANISOU 6690  O   HOH A2430     3160   1996   2159    465    -68    528       O  
HETATM 6691  O   HOH A2431      18.453  -3.225  37.984  1.00 29.73           O  
ANISOU 6691  O   HOH A2431     5097   3183   3015    991    233    257       O  
HETATM 6692  O   HOH A2432      19.199  -0.565  39.089  1.00 18.73           O  
ANISOU 6692  O   HOH A2432     3516   1815   1784    451    -15    188       O  
HETATM 6693  O   HOH A2433       6.077  28.209  37.949  1.00 78.91           O  
ANISOU 6693  O   HOH A2433    10368  10198   9416     88    -73    124       O  
HETATM 6694  O   HOH A2434       3.598  27.770  37.220  1.00 39.77           O  
ANISOU 6694  O   HOH A2434     5455   5358   4299   -556    418   -747       O  
HETATM 6695  O   HOH A2435       7.545  25.595  40.665  1.00 34.20           O  
ANISOU 6695  O   HOH A2435     5458   3423   4115    -54   1532   -370       O  
HETATM 6696  O   HOH A2436      14.323  -2.081  38.503  1.00 22.01           O  
ANISOU 6696  O   HOH A2436     3232   2498   2633    807    533    876       O  
HETATM 6697  O   HOH A2437      10.373  25.202  39.355  1.00 46.22           O  
ANISOU 6697  O   HOH A2437     6984   4636   5942   -812    366   -381       O  
HETATM 6698  O   HOH A2438      15.044   0.926  41.736  1.00 16.59           O  
ANISOU 6698  O   HOH A2438     2440   1817   2046    107    216    556       O  
HETATM 6699  O   HOH A2439      15.225  -2.799  43.980  1.00 46.67           O  
ANISOU 6699  O   HOH A2439     6204   6355   5175   -443    672    581       O  
HETATM 6700  O   HOH A2440      14.201  -0.430  44.068  1.00 44.54           O  
ANISOU 6700  O   HOH A2440     5760   6504   4660    155    248    195       O  
HETATM 6701  O   HOH A2441      -0.653  -3.286  44.310  1.00 26.02           O  
ANISOU 6701  O   HOH A2441     4378   2688   2820   -366   -196    448       O  
HETATM 6702  O   HOH A2442      -3.744  -0.397  41.193  1.00 46.81           O  
ANISOU 6702  O   HOH A2442     5572   6640   5574   -642    -26    164       O  
HETATM 6703  O   HOH A2443       6.107  -6.506  44.656  1.00 41.96           O  
ANISOU 6703  O   HOH A2443     5378   5269   5298   -157    913    279       O  
HETATM 6704  O   HOH A2444       3.397  -4.615  46.467  1.00 17.30           O  
ANISOU 6704  O   HOH A2444     2524   2210   1841   -160    541    534       O  
HETATM 6705  O   HOH A2445      -3.904   1.923  41.840  1.00 31.29           O  
ANISOU 6705  O   HOH A2445     3797   4814   3278    -95    142    820       O  
HETATM 6706  O   HOH A2446      12.039  -5.414  42.025  1.00 42.92           O  
ANISOU 6706  O   HOH A2446     6123   4482   5702   -148    519    186       O  
HETATM 6707  O   HOH A2447       7.381  -8.429  43.193  1.00 94.22           O  
ANISOU 6707  O   HOH A2447    12101  12361  11337     40     21     20       O  
HETATM 6708  O   HOH A2448       8.316  -3.893  34.106  1.00 58.09           O  
ANISOU 6708  O   HOH A2448     7597   7753   6724     21     56     93       O  
HETATM 6709  O   HOH A2449       6.632  -5.223  36.584  1.00 31.48           O  
ANISOU 6709  O   HOH A2449     5344   3337   3278   -977      6    246       O  
HETATM 6710  O   HOH A2450      11.377  -3.540  33.712  1.00 36.52           O  
ANISOU 6710  O   HOH A2450     5492   4775   3609   -801   -429     50       O  
HETATM 6711  O   HOH A2451      10.185  -6.303  29.057  1.00 32.90           O  
ANISOU 6711  O   HOH A2451     4987   3918   3597    172    529    368       O  
HETATM 6712  O   HOH A2452       7.803  -6.786  30.880  1.00 32.27           O  
ANISOU 6712  O   HOH A2452     5182   2708   4373   -126    437    881       O  
HETATM 6713  O   HOH A2453     -10.339  12.945  14.535  1.00 55.11           O  
ANISOU 6713  O   HOH A2453     6774   7083   7084   -112    316    187       O  
HETATM 6714  O   HOH A2454      19.215   6.315  28.817  1.00 14.23           O  
ANISOU 6714  O   HOH A2454     1685   1778   1943    266   -377   -294       O  
HETATM 6715  O   HOH A2455      17.449   4.893  30.035  1.00 37.03           O  
ANISOU 6715  O   HOH A2455     4684   4678   4708    457    243    -24       O  
HETATM 6716  O   HOH A2456      10.420  13.966  46.439  1.00 19.58           O  
ANISOU 6716  O   HOH A2456     3212   2496   1731    470      5     75       O  
HETATM 6717  O   HOH A2457      11.962  16.929  40.694  1.00 12.16           O  
ANISOU 6717  O   HOH A2457     1987   1325   1309     62    118    156       O  
HETATM 6718  O   HOH A2458      18.556  16.547  44.278  1.00 24.91           O  
ANISOU 6718  O   HOH A2458     2993   3139   3333    -75   -459   -570       O  
HETATM 6719  O   HOH A2459      17.212  15.457  47.863  1.00 33.83           O  
ANISOU 6719  O   HOH A2459     3950   3982   4920    264    827   -478       O  
HETATM 6720  O   HOH A2460      14.497  16.799  45.917  1.00 30.14           O  
ANISOU 6720  O   HOH A2460     3986   4832   2635   -716    825  -1147       O  
HETATM 6721  O   HOH A2461      15.593   6.861  31.653  1.00 12.38           O  
ANISOU 6721  O   HOH A2461     1956   1288   1461   -320   -249    420       O  
HETATM 6722  O   HOH A2462      25.914   4.399  29.646  1.00 15.48           O  
ANISOU 6722  O   HOH A2462     2052   2114   1715    245    -38    201       O  
HETATM 6723  O   HOH A2463      23.176   1.400  31.035  1.00 13.90           O  
ANISOU 6723  O   HOH A2463     1883   1704   1693    159     17    174       O  
HETATM 6724  O   HOH A2464      29.268   7.342  27.852  1.00 19.60           O  
ANISOU 6724  O   HOH A2464     2091   2891   2466    352   -112    119       O  
HETATM 6725  O   HOH A2465      26.543   6.262  27.588  1.00 16.05           O  
ANISOU 6725  O   HOH A2465     2216   2139   1744    396     11    333       O  
HETATM 6726  O   HOH A2466      20.266   5.501  26.200  1.00 15.39           O  
ANISOU 6726  O   HOH A2466     1922   1881   2046    326   -277    -85       O  
HETATM 6727  O   HOH A2467      26.698  17.865  26.463  1.00 25.69           O  
ANISOU 6727  O   HOH A2467     2054   2900   4806   -446    858  -1039       O  
HETATM 6728  O   HOH A2468      30.555  24.986  32.581  1.00 51.27           O  
ANISOU 6728  O   HOH A2468     6343   6296   6842   -530   -366   -921       O  
HETATM 6729  O   HOH A2469      27.150  21.901  26.025  1.00 24.61           O  
ANISOU 6729  O   HOH A2469     2353   4123   2873   -506    -61    357       O  
HETATM 6730  O   HOH A2470      30.891  22.796  28.879  1.00 44.37           O  
ANISOU 6730  O   HOH A2470     4778   7034   5045   -975   -171   -164       O  
HETATM 6731  O   HOH A2471      26.194  24.443  26.849  1.00 41.76           O  
ANISOU 6731  O   HOH A2471     4707   5413   5749   -237     35   -106       O  
HETATM 6732  O   HOH A2472      24.395  24.105  33.023  1.00 17.83           O  
ANISOU 6732  O   HOH A2472     2498   2349   1928   -998   -356    366       O  
HETATM 6733  O   HOH A2473      27.073  28.391  27.971  1.00 47.27           O  
ANISOU 6733  O   HOH A2473     5859   6304   5799   -546    -35   -329       O  
HETATM 6734  O   HOH A2474      23.395  33.315  28.570  1.00 43.48           O  
ANISOU 6734  O   HOH A2474     5625   4727   6169     16   -215    543       O  
HETATM 6735  O   HOH A2475      25.262  28.247  25.575  1.00 33.43           O  
ANISOU 6735  O   HOH A2475     4993   4237   3471   -947    144   -230       O  
HETATM 6736  O   HOH A2476      24.207  30.597  25.408  1.00 30.94           O  
ANISOU 6736  O   HOH A2476     4353   3947   3456    260   -285    100       O  
HETATM 6737  O   HOH A2477      25.398  31.363  31.194  1.00 29.07           O  
ANISOU 6737  O   HOH A2477     3473   2732   4839   -762   -204   -248       O  
HETATM 6738  O   HOH A2478      26.757  27.531  30.918  1.00 27.21           O  
ANISOU 6738  O   HOH A2478     2525   4705   3107   -768    -20   -441       O  
HETATM 6739  O   HOH A2479      23.214  31.028  35.886  1.00 41.57           O  
ANISOU 6739  O   HOH A2479     6317   4574   4905   -521   -535   -300       O  
HETATM 6740  O   HOH A2480      22.527  27.050  36.774  1.00 25.18           O  
ANISOU 6740  O   HOH A2480     3489   3528   2551   -452   -482    459       O  
HETATM 6741  O   HOH A2481      18.300  33.678  31.679  1.00 48.96           O  
ANISOU 6741  O   HOH A2481     6647   5311   6646    329   -147    295       O  
HETATM 6742  O   HOH A2482      16.495  31.449  33.579  1.00 53.38           O  
ANISOU 6742  O   HOH A2482     7253   6039   6988     -3   -448   -392       O  
HETATM 6743  O   HOH A2483      15.054  27.322  35.093  1.00 18.29           O  
ANISOU 6743  O   HOH A2483     3203   2199   1549    -73   -132   -256       O  
HETATM 6744  O   HOH A2484       6.304  27.017  30.927  1.00 15.72           O  
ANISOU 6744  O   HOH A2484     2057   2039   1875    124    -66     61       O  
HETATM 6745  O   HOH A2485      11.419  32.508  32.286  1.00 39.80           O  
ANISOU 6745  O   HOH A2485     4567   3639   6917   -221     92   -171       O  
HETATM 6746  O   HOH A2486       7.909  31.297  32.976  1.00 39.27           O  
ANISOU 6746  O   HOH A2486     5047   3495   6380    944    284     50       O  
HETATM 6747  O   HOH A2487      12.324  26.934  35.551  1.00 42.76           O  
ANISOU 6747  O   HOH A2487     5347   6310   4590     37   -334     27       O  
HETATM 6748  O   HOH A2488      13.111  30.086  34.779  1.00 37.46           O  
ANISOU 6748  O   HOH A2488     5339   5863   3030   -596   -407  -1308       O  
HETATM 6749  O   HOH A2489       5.258  31.167  28.038  1.00 54.95           O  
ANISOU 6749  O   HOH A2489     8057   6538   6284   -378   -221    334       O  
HETATM 6750  O   HOH A2490       9.841  32.478  23.596  1.00 16.30           O  
ANISOU 6750  O   HOH A2490     2515   1422   2255   -207    199   -278       O  
HETATM 6751  O   HOH A2491       6.989  33.301  31.321  1.00 42.19           O  
ANISOU 6751  O   HOH A2491     5658   4965   5406    275    285   -318       O  
HETATM 6752  O   HOH A2492       5.804  29.637  30.472  1.00 26.05           O  
ANISOU 6752  O   HOH A2492     4835   2280   2783    718    101    251       O  
HETATM 6753  O   HOH A2493      15.341  14.653  23.475  1.00  8.69           O  
ANISOU 6753  O   HOH A2493     1189    979   1133     62    -60    146       O  
HETATM 6754  O   HOH A2494      17.939  29.266  14.831  1.00 41.14           O  
ANISOU 6754  O   HOH A2494     5033   5760   4839   -617     70   -456       O  
HETATM 6755  O   HOH A2495      18.564  24.576   4.881  1.00 56.27           O  
ANISOU 6755  O   HOH A2495     7342   7212   6825   -474    334    456       O  
HETATM 6756  O   HOH A2496      18.395  15.483   7.389  1.00 33.90           O  
ANISOU 6756  O   HOH A2496     3796   3429   5657    687    780    522       O  
HETATM 6757  O   HOH A2497      23.678  15.981  10.283  1.00 30.68           O  
ANISOU 6757  O   HOH A2497     3997   4673   2988    953    329   -106       O  
HETATM 6758  O   HOH A2498      14.944  18.128   0.132  1.00 28.88           O  
ANISOU 6758  O   HOH A2498     4060   3634   3278    420   -720   -763       O  
HETATM 6759  O   HOH A2499      16.149  22.154  -1.141  1.00 30.29           O  
ANISOU 6759  O   HOH A2499     5082   4397   2028   1655    983    617       O  
HETATM 6760  O   HOH A2500      17.936  25.257   1.053  1.00 54.54           O  
ANISOU 6760  O   HOH A2500     6665   7479   6579    133   -166    345       O  
HETATM 6761  O   HOH A2501      16.227  25.552   4.718  1.00 32.49           O  
ANISOU 6761  O   HOH A2501     4845   4429   3070   -273   -417    991       O  
HETATM 6762  O   HOH A2502      13.183  24.685  -4.330  1.00 21.99           O  
ANISOU 6762  O   HOH A2502     2501   3810   2044   -211    369   -231       O  
HETATM 6763  O   HOH A2503      10.759  27.420  -5.229  1.00 48.12           O  
ANISOU 6763  O   HOH A2503     6260   6283   5741    316   -131     86       O  
HETATM 6764  O   HOH A2504      19.630  33.157  -1.467  1.00 54.58           O  
ANISOU 6764  O   HOH A2504     6195   7084   7461  -1037    424    230       O  
HETATM 6765  O   HOH A2505      14.807  29.907  -4.143  1.00 42.40           O  
ANISOU 6765  O   HOH A2505     5248   6613   4248    339   1227    444       O  
HETATM 6766  O   HOH A2506      16.885  29.310  -0.719  1.00 31.51           O  
ANISOU 6766  O   HOH A2506     2531   4036   5406   -265    858    735       O  
HETATM 6767  O   HOH A2507       5.941  29.989  -4.136  1.00 20.39           O  
ANISOU 6767  O   HOH A2507     2835   2733   2179    299    105   1110       O  
HETATM 6768  O   HOH A2508       8.227  33.103  -5.037  1.00 37.16           O  
ANISOU 6768  O   HOH A2508     5463   4502   4156   -244   -374   2283       O  
HETATM 6769  O   HOH A2509       2.577  27.800  -5.315  1.00 26.56           O  
ANISOU 6769  O   HOH A2509     3921   3431   2741     15   -745    973       O  
HETATM 6770  O   HOH A2510       9.963  31.770  12.014  1.00 13.36           O  
ANISOU 6770  O   HOH A2510     2051   1444   1582   -212     74    328       O  
HETATM 6771  O   HOH A2511      10.225  36.154  11.571  1.00 45.48           O  
ANISOU 6771  O   HOH A2511     6716   4058   6505    921   -108   -105       O  
HETATM 6772  O   HOH A2512       8.647  36.031   5.807  1.00 46.88           O  
ANISOU 6772  O   HOH A2512     5887   5798   6129    167    480     30       O  
HETATM 6773  O   HOH A2513       4.577  35.407  11.702  1.00 38.69           O  
ANISOU 6773  O   HOH A2513     5418   4411   4871   -297    772   -530       O  
HETATM 6774  O   HOH A2514       7.653  38.771   8.999  1.00 51.20           O  
ANISOU 6774  O   HOH A2514     7353   5098   7002    396     79    153       O  
HETATM 6775  O   HOH A2515       3.804  35.824   9.403  1.00 43.78           O  
ANISOU 6775  O   HOH A2515     5704   4578   6354    176    107    211       O  
HETATM 6776  O   HOH A2516       7.394  35.224  12.927  1.00 25.21           O  
ANISOU 6776  O   HOH A2516     4645   1912   3023     52   -153    378       O  
HETATM 6777  O   HOH A2517      16.996  29.038   7.988  1.00 62.93           O  
ANISOU 6777  O   HOH A2517     8237   7620   8053     93    192    127       O  
HETATM 6778  O   HOH A2518      16.179  32.742   5.045  1.00 64.91           O  
ANISOU 6778  O   HOH A2518     8461   8621   7582   -155     31     91       O  
HETATM 6779  O   HOH A2519      14.129  34.694   5.571  1.00 50.84           O  
ANISOU 6779  O   HOH A2519     7284   5885   6145   -399   -304    -60       O  
HETATM 6780  O   HOH A2520      15.708  33.199   9.240  1.00 26.61           O  
ANISOU 6780  O   HOH A2520     3710   3719   2683  -1249    257     87       O  
HETATM 6781  O   HOH A2521      16.064  28.788   2.671  1.00 27.68           O  
ANISOU 6781  O   HOH A2521     4088   4015   2413    113    715    726       O  
HETATM 6782  O   HOH A2522       9.943  34.856   0.355  1.00 46.85           O  
ANISOU 6782  O   HOH A2522     6852   4735   6212    116    188    718       O  
HETATM 6783  O   HOH A2523       9.519  33.647   4.921  1.00 24.11           O  
ANISOU 6783  O   HOH A2523     4003   2618   2540     73   -243    519       O  
HETATM 6784  O   HOH A2524       1.692  31.582  -5.561  1.00 26.08           O  
ANISOU 6784  O   HOH A2524     4021   3358   2530    626    116    642       O  
HETATM 6785  O   HOH A2525     -13.164  22.714  13.004  1.00 20.93           O  
ANISOU 6785  O   HOH A2525     1584   3278   3091    169    -26     58       O  
HETATM 6786  O   HOH A2526     -12.307  18.921  14.720  1.00 55.85           O  
ANISOU 6786  O   HOH A2526     6950   6992   7277    205    442     94       O  
HETATM 6787  O   HOH A2527     -13.009  22.807  17.389  1.00 46.16           O  
ANISOU 6787  O   HOH A2527     4508   6599   6434    210    408   -253       O  
HETATM 6788  O   HOH A2528      -8.574  29.882  14.946  1.00 18.19           O  
ANISOU 6788  O   HOH A2528     2404   2127   2382    762    514    104       O  
HETATM 6789  O   HOH A2529     -10.925  29.595  12.772  1.00 43.51           O  
ANISOU 6789  O   HOH A2529     5440   5479   5614     24   -148    285       O  
HETATM 6790  O   HOH A2530     -15.310  23.496  11.443  1.00 36.60           O  
ANISOU 6790  O   HOH A2530     3228   5760   4917    862   -679      6       O  
HETATM 6791  O   HOH A2531      -5.194  29.051  17.493  1.00 14.02           O  
ANISOU 6791  O   HOH A2531     1910   1958   1459    406    105    131       O  
HETATM 6792  O   HOH A2532     -14.834  25.797  16.585  1.00 57.82           O  
ANISOU 6792  O   HOH A2532     7226   7857   6887   -167     15     84       O  
HETATM 6793  O   HOH A2533     -12.067  29.376  16.275  1.00 41.73           O  
ANISOU 6793  O   HOH A2533     4000   5175   6679    802    732    357       O  
HETATM 6794  O   HOH A2534      -9.389  30.427  17.511  1.00 33.23           O  
ANISOU 6794  O   HOH A2534     4828   4872   2926    646    826   -714       O  
HETATM 6795  O   HOH A2535     -10.351  23.365  19.951  1.00 26.33           O  
ANISOU 6795  O   HOH A2535     3756   3790   2457   1097    432    113       O  
HETATM 6796  O   HOH A2536      -4.985  24.979  20.369  1.00 18.33           O  
ANISOU 6796  O   HOH A2536     2273   2777   1913    419    212    186       O  
HETATM 6797  O   HOH A2537      -2.384  25.983  16.391  1.00 10.87           O  
ANISOU 6797  O   HOH A2537     1513   1407   1212    220     15    179       O  
HETATM 6798  O   HOH A2538      -2.978  20.385  18.387  1.00 16.26           O  
ANISOU 6798  O   HOH A2538     1965   2287   1926    221     16     80       O  
HETATM 6799  O   HOH A2539      -3.950  35.062  13.923  1.00 21.68           O  
ANISOU 6799  O   HOH A2539     3756   1747   2734    979   -102    165       O  
HETATM 6800  O   HOH A2540      -7.615  32.509  11.962  1.00 28.13           O  
ANISOU 6800  O   HOH A2540     3576   4053   3057   1063   -724    635       O  
HETATM 6801  O   HOH A2541      -2.596  28.454  20.590  1.00 17.24           O  
ANISOU 6801  O   HOH A2541     2621   2164   1765    192     43    245       O  
HETATM 6802  O   HOH A2542      -2.026  31.826  22.509  1.00 33.53           O  
ANISOU 6802  O   HOH A2542     5122   4044   3574    716    934   -954       O  
HETATM 6803  O   HOH A2543      -7.260  33.747   5.698  1.00 43.43           O  
ANISOU 6803  O   HOH A2543     5922   4708   5870    299    -24   -238       O  
HETATM 6804  O   HOH A2544      -7.852  30.875   8.743  1.00 41.34           O  
ANISOU 6804  O   HOH A2544     5456   4409   5841   1086    777   1180       O  
HETATM 6805  O   HOH A2545       0.935  34.986   8.964  1.00 31.41           O  
ANISOU 6805  O   HOH A2545     6047   2613   3275   -153    -24    190       O  
HETATM 6806  O   HOH A2546      -6.993  31.314   5.450  1.00 20.16           O  
ANISOU 6806  O   HOH A2546     2118   2151   3392    956   -583   -305       O  
HETATM 6807  O   HOH A2547      -3.693  32.995  18.529  1.00 57.57           O  
ANISOU 6807  O   HOH A2547     7664   6862   7349    438   -618   -327       O  
HETATM 6808  O   HOH A2548       4.066  34.870  17.769  1.00 40.25           O  
ANISOU 6808  O   HOH A2548     4504   4670   6120    381   -142   1294       O  
HETATM 6809  O   HOH A2549      -1.025  34.431  21.211  1.00 44.21           O  
ANISOU 6809  O   HOH A2549     7173   5035   4590    529    217   -303       O  
HETATM 6810  O   HOH A2550       1.843  33.541  22.027  1.00 43.81           O  
ANISOU 6810  O   HOH A2550     5475   4372   6801    636     -8    -86       O  
HETATM 6811  O   HOH A2551      -4.319  35.825  16.540  1.00 37.14           O  
ANISOU 6811  O   HOH A2551     5177   4454   4480    203    362  -1034       O  
HETATM 6812  O   HOH A2552       7.573  32.439  13.252  1.00 14.36           O  
ANISOU 6812  O   HOH A2552     2142   1481   1834   -135    -35    168       O  
HETATM 6813  O   HOH A2553       4.903  33.965   6.622  1.00 28.01           O  
ANISOU 6813  O   HOH A2553     4337   3158   3149  -1228    381   -148       O  
HETATM 6814  O   HOH A2554      -1.586  35.052   7.841  1.00 38.48           O  
ANISOU 6814  O   HOH A2554     6463   3755   4403   1014    309    448       O  
HETATM 6815  O   HOH A2555      -5.243  34.173   4.655  1.00 35.01           O  
ANISOU 6815  O   HOH A2555     4373   2748   6182   1919   1015    241       O  
HETATM 6816  O   HOH A2556      -1.427  36.033   4.558  1.00 45.47           O  
ANISOU 6816  O   HOH A2556     7143   3668   6467    307   -416    148       O  
HETATM 6817  O   HOH A2557      -7.627  29.668   1.276  1.00 29.71           O  
ANISOU 6817  O   HOH A2557     4065   4142   3083   1430    524    103       O  
HETATM 6818  O   HOH A2558     -12.618  14.823   9.203  1.00 43.94           O  
ANISOU 6818  O   HOH A2558     5837   5089   5768   -617   -407    756       O  
HETATM 6819  O   HOH A2559     -14.633  27.079   3.940  1.00 37.40           O  
ANISOU 6819  O   HOH A2559     4902   4639   4670   1262   -546    137       O  
HETATM 6820  O   HOH A2560     -18.564  22.995   6.502  1.00 45.33           O  
ANISOU 6820  O   HOH A2560     6142   5324   5757    334    114    191       O  
HETATM 6821  O   HOH A2561     -16.928  21.835   8.032  1.00 66.54           O  
ANISOU 6821  O   HOH A2561     8238   8525   8521    150    194     -9       O  
HETATM 6822  O   HOH A2562     -16.824  25.393   2.946  1.00 31.63           O  
ANISOU 6822  O   HOH A2562     3796   4301   3920    504   -184    136       O  
HETATM 6823  O   HOH A2563     -13.549  25.427   9.065  1.00 33.96           O  
ANISOU 6823  O   HOH A2563     4316   4862   3725   1134    463   -790       O  
HETATM 6824  O   HOH A2564     -11.293  25.815   5.112  1.00 21.73           O  
ANISOU 6824  O   HOH A2564     2222   2033   4001    655  -1037      5       O  
HETATM 6825  O   HOH A2565     -14.675  15.455   0.696  1.00 70.63           O  
ANISOU 6825  O   HOH A2565     9273   8907   8656    -37   -103    279       O  
HETATM 6826  O   HOH A2566     -11.553  27.265   3.023  1.00 36.68           O  
ANISOU 6826  O   HOH A2566     6524   3606   3807   1248   -972   -136       O  
HETATM 6827  O   HOH A2567     -14.935  16.832   3.336  1.00 35.99           O  
ANISOU 6827  O   HOH A2567     4658   4420   4596   -635    -62    777       O  
HETATM 6828  O   HOH A2568      -8.793  26.835  -0.647  1.00 34.95           O  
ANISOU 6828  O   HOH A2568     4009   4681   4589    174    109   1102       O  
HETATM 6829  O   HOH A2569     -17.632  15.159  -1.090  1.00 47.40           O  
ANISOU 6829  O   HOH A2569     6990   4485   6536   -272     60    -86       O  
HETATM 6830  O   HOH A2570     -23.128  18.027  -3.475  1.00 53.41           O  
ANISOU 6830  O   HOH A2570     5939   7533   6821    -76   -244    -25       O  
HETATM 6831  O   HOH A2571     -13.701  21.181  -2.956  1.00 26.98           O  
ANISOU 6831  O   HOH A2571     3940   2970   3339    186     65    478       O  
HETATM 6832  O   HOH A2572     -11.235  17.747   1.616  1.00 21.25           O  
ANISOU 6832  O   HOH A2572     2577   2623   2875    723   -442     59       O  
HETATM 6833  O   HOH A2573      -9.105  15.251   2.077  1.00 30.10           O  
ANISOU 6833  O   HOH A2573     4887   3958   2594  -1277  -1057    499       O  
HETATM 6834  O   HOH A2574      -7.367  12.935   0.377  1.00 46.31           O  
ANISOU 6834  O   HOH A2574     6361   6751   4484    706   -571   -626       O  
HETATM 6835  O   HOH A2575      -8.296  11.128  -2.105  1.00 57.94           O  
ANISOU 6835  O   HOH A2575     7524   7402   7088    265    357    230       O  
HETATM 6836  O   HOH A2576      -6.091  13.886  -7.036  1.00 41.94           O  
ANISOU 6836  O   HOH A2576     5244   5581   5110    344   -493   -164       O  
HETATM 6837  O   HOH A2577      -5.213  10.427  -1.272  1.00 36.87           O  
ANISOU 6837  O   HOH A2577     5422   4201   4384    103     20   -168       O  
HETATM 6838  O   HOH A2578     -12.687  15.427  -7.578  1.00 52.01           O  
ANISOU 6838  O   HOH A2578     5848   7826   6088   -473   -373   -353       O  
HETATM 6839  O   HOH A2579     -12.192  13.214  -6.288  1.00 66.58           O  
ANISOU 6839  O   HOH A2579     8450   8863   7986     24    -96   -248       O  
HETATM 6840  O   HOH A2580     -12.042  17.479 -10.634  1.00 57.48           O  
ANISOU 6840  O   HOH A2580     7465   7664   6711     80   -264   -262       O  
HETATM 6841  O   HOH A2581      -6.301  20.064  -8.743  1.00 37.22           O  
ANISOU 6841  O   HOH A2581     4522   5330   4290    543   -495   -212       O  
HETATM 6842  O   HOH A2582       0.133  17.895  -6.952  1.00 19.06           O  
ANISOU 6842  O   HOH A2582     2993   2589   1660   1159    148    368       O  
HETATM 6843  O   HOH A2583      -9.558  26.221  -9.733  1.00 69.16           O  
ANISOU 6843  O   HOH A2583     9231   8538   8507      0     30    145       O  
HETATM 6844  O   HOH A2584      -7.918  28.281  -9.941  1.00 46.84           O  
ANISOU 6844  O   HOH A2584     5137   5684   6976    613  -1081   -301       O  
HETATM 6845  O   HOH A2585      -8.861  20.108  -9.759  1.00 41.20           O  
ANISOU 6845  O   HOH A2585     4838   5922   4895      3   -227     36       O  
HETATM 6846  O   HOH A2586      -9.065  25.202  -4.617  1.00 38.89           O  
ANISOU 6846  O   HOH A2586     3492   6738   4548    982   -635    579       O  
HETATM 6847  O   HOH A2587      -4.832  26.213 -10.394  1.00 37.91           O  
ANISOU 6847  O   HOH A2587     5677   5661   3065   -167   -631    734       O  
HETATM 6848  O   HOH A2588     -11.375  24.446  -9.692  1.00 36.45           O  
ANISOU 6848  O   HOH A2588     4899   3750   5198   1059    -61    729       O  
HETATM 6849  O   HOH A2589     -10.780  26.482  -7.576  1.00 29.52           O  
ANISOU 6849  O   HOH A2589     3198   4804   3213    197   -266    703       O  
HETATM 6850  O   HOH A2590      -8.582  28.188  -4.988  1.00 23.71           O  
ANISOU 6850  O   HOH A2590     3688   2445   2875    333   -700    259       O  
HETATM 6851  O   HOH A2591      -6.891  29.559  -7.157  1.00 20.19           O  
ANISOU 6851  O   HOH A2591     2582   1889   3201    897    220    554       O  
HETATM 6852  O   HOH A2592      -2.977  31.845  -9.064  1.00 56.42           O  
ANISOU 6852  O   HOH A2592     7797   6462   7177    627     29    213       O  
HETATM 6853  O   HOH A2593      -0.842  31.847  -6.601  1.00 48.96           O  
ANISOU 6853  O   HOH A2593     6046   6648   5907    215   -157     93       O  
HETATM 6854  O   HOH A2594       1.863  27.188 -12.620  1.00 45.88           O  
ANISOU 6854  O   HOH A2594     5702   6382   5348    795    417     89       O  
HETATM 6855  O   HOH A2595       2.004  24.556 -13.571  1.00 39.23           O  
ANISOU 6855  O   HOH A2595     5575   5093   4239   1107    192   -810       O  
HETATM 6856  O   HOH A2596       1.618  29.433  -7.270  1.00 30.08           O  
ANISOU 6856  O   HOH A2596     5392   3343   2696   1247   -552    217       O  
HETATM 6857  O   HOH A2597       1.555  17.976  -9.373  1.00 17.77           O  
ANISOU 6857  O   HOH A2597     1937   2357   2458    643   -473    313       O  
HETATM 6858  O   HOH A2598       2.125  20.645 -12.053  1.00 19.99           O  
ANISOU 6858  O   HOH A2598     2853   3303   1439   1219    -70    -10       O  
HETATM 6859  O   HOH A2599       4.263  25.603  -5.593  1.00 20.82           O  
ANISOU 6859  O   HOH A2599     3001   2711   2200     98     -3    198       O  
HETATM 6860  O   HOH A2600      10.930  23.470  -5.405  1.00 14.70           O  
ANISOU 6860  O   HOH A2600     2220   2169   1195    164    189    316       O  
HETATM 6861  O   HOH A2601       6.639  27.959  -5.898  1.00 37.11           O  
ANISOU 6861  O   HOH A2601     6974   4337   2790   2005     24    820       O  
HETATM 6862  O   HOH A2602      -2.200  11.944  16.230  1.00 34.67           O  
ANISOU 6862  O   HOH A2602     4948   5468   2756   -210    -75   1045       O  
HETATM 6863  O   HOH A2603      -1.267   8.531  15.273  1.00 19.07           O  
ANISOU 6863  O   HOH A2603     2420   3082   1743   -753    -82    502       O  
HETATM 6864  O   HOH A2604      -4.139   7.164  12.589  1.00 22.25           O  
ANISOU 6864  O   HOH A2604     3325   2901   2227   -225      0    190       O  
HETATM 6865  O   HOH A2605     -10.367   7.714  11.965  1.00 81.66           O  
ANISOU 6865  O   HOH A2605    10476  10672   9878    -62     52    152       O  
HETATM 6866  O   HOH A2606      -4.040   5.893  10.177  1.00 15.06           O  
ANISOU 6866  O   HOH A2606     2058   1837   1827   -328    296    153       O  
HETATM 6867  O   HOH A2607      -2.852   4.971   3.079  1.00 37.54           O  
ANISOU 6867  O   HOH A2607     4950   5357   3957    234    315    385       O  
HETATM 6868  O   HOH A2608      -9.251   8.637   3.842  1.00 63.41           O  
ANISOU 6868  O   HOH A2608     7082   8712   8299     41    -71    -49       O  
HETATM 6869  O   HOH A2609      -8.321  12.457   7.284  1.00 28.12           O  
ANISOU 6869  O   HOH A2609     3430   4450   2805    143   -234   -417       O  
HETATM 6870  O   HOH A2610      -5.158   9.331   1.282  1.00 24.35           O  
ANISOU 6870  O   HOH A2610     2723   3834   2695   -588   -510   -475       O  
HETATM 6871  O   HOH A2611      -5.613   6.629   7.923  1.00 20.61           O  
ANISOU 6871  O   HOH A2611     2527   2995   2308   -378    -19    172       O  
HETATM 6872  O   HOH A2612       3.853  12.470   3.389  1.00 10.45           O  
ANISOU 6872  O   HOH A2612     1570   1232   1167    253      9     83       O  
HETATM 6873  O   HOH A2613      -6.253  12.469   3.724  1.00 21.37           O  
ANISOU 6873  O   HOH A2613     2434   3154   2531    227    120   -117       O  
HETATM 6874  O   HOH A2614      -3.006  11.273  -6.125  1.00 39.11           O  
ANISOU 6874  O   HOH A2614     4533   5065   5260   -155   -133   -793       O  
HETATM 6875  O   HOH A2615      -2.926   9.715  -4.378  1.00 47.83           O  
ANISOU 6875  O   HOH A2615     5741   5901   6531   -118   -339   -613       O  
HETATM 6876  O   HOH A2616      -2.840  16.177  -5.371  1.00 58.42           O  
ANISOU 6876  O   HOH A2616     7226   7428   7544   -165    136    200       O  
HETATM 6877  O   HOH A2617      -2.023  15.050  -7.290  1.00 45.56           O  
ANISOU 6877  O   HOH A2617     5284   6198   5829    499   -119     32       O  
HETATM 6878  O   HOH A2618      -2.447  12.725  -8.055  1.00 56.41           O  
ANISOU 6878  O   HOH A2618     6980   7094   7359    -10   -162    343       O  
HETATM 6879  O   HOH A2619       5.224  17.763 -13.991  1.00 15.43           O  
ANISOU 6879  O   HOH A2619     2200   2493   1170    344    136    149       O  
HETATM 6880  O   HOH A2620       1.993  15.413 -16.289  1.00 18.36           O  
ANISOU 6880  O   HOH A2620     2157   3475   1345     87    -26   -346       O  
HETATM 6881  O   HOH A2621      -0.448  14.500 -13.745  1.00 32.44           O  
ANISOU 6881  O   HOH A2621     3585   5864   2875   -390   -469   -174       O  
HETATM 6882  O   HOH A2622       0.914  18.394 -13.255  1.00 28.19           O  
ANISOU 6882  O   HOH A2622     3015   4456   3240    647    272   -426       O  
HETATM 6883  O   HOH A2623       2.075  11.909 -13.185  1.00 34.48           O  
ANISOU 6883  O   HOH A2623     4052   5651   3399    441    -23    766       O  
HETATM 6884  O   HOH A2624      11.253  15.983 -12.809  1.00 15.60           O  
ANISOU 6884  O   HOH A2624     2255   2264   1407    358    410   -172       O  
HETATM 6885  O   HOH A2625      13.160  16.527  -9.543  1.00 26.12           O  
ANISOU 6885  O   HOH A2625     3144   3654   3126   -101    471   -893       O  
HETATM 6886  O   HOH A2626       7.032  25.560  -7.669  1.00 28.06           O  
ANISOU 6886  O   HOH A2626     6281   2459   1921   1162   -864    149       O  
HETATM 6887  O   HOH A2627      10.682  21.004  -4.104  1.00 11.81           O  
ANISOU 6887  O   HOH A2627     1662   1718   1109    215    100    283       O  
HETATM 6888  O   HOH A2628       4.118   3.438  15.752  1.00 22.18           O  
ANISOU 6888  O   HOH A2628     3134   1787   3507   -576   -468   1012       O  
HETATM 6889  O   HOH A2629       4.742   1.578  17.755  1.00 13.86           O  
ANISOU 6889  O   HOH A2629     1950   1896   1420   -300    141    163       O  
HETATM 6890  O   HOH A2630       6.384  -2.114  15.503  1.00 23.00           O  
ANISOU 6890  O   HOH A2630     2769   2745   3223   -362    170    575       O  
HETATM 6891  O   HOH A2631       0.428  -3.665  17.107  1.00 23.60           O  
ANISOU 6891  O   HOH A2631     2750   1846   4372   -243   -493   1491       O  
HETATM 6892  O   HOH A2632      -2.029  -0.664  15.507  1.00 21.45           O  
ANISOU 6892  O   HOH A2632     2957   2494   2699   -797    148    -73       O  
HETATM 6893  O   HOH A2633       5.427  -5.100  13.336  1.00 31.90           O  
ANISOU 6893  O   HOH A2633     4084   4556   3480    243    -19    876       O  
HETATM 6894  O   HOH A2634       3.068  -5.008   9.926  1.00 44.82           O  
ANISOU 6894  O   HOH A2634     5714   5330   5986   -292     20  -1041       O  
HETATM 6895  O   HOH A2635       4.491   1.485  13.459  1.00 32.14           O  
ANISOU 6895  O   HOH A2635     4559   3858   3793   -839   1026    421       O  
HETATM 6896  O   HOH A2636       2.988   1.994  10.769  1.00 30.17           O  
ANISOU 6896  O   HOH A2636     6323   2887   2252  -1659    505   -305       O  
HETATM 6897  O   HOH A2637      -4.535   3.237  10.665  1.00 34.74           O  
ANISOU 6897  O   HOH A2637     6527   2836   3836  -1224    319     54       O  
HETATM 6898  O   HOH A2638      -5.498   2.195  13.258  1.00 43.10           O  
ANISOU 6898  O   HOH A2638     5669   5351   5355   -667    -94    531       O  
HETATM 6899  O   HOH A2639      -1.627  -4.414   9.965  1.00 55.67           O  
ANISOU 6899  O   HOH A2639     7365   7201   6587   -366    175   -227       O  
HETATM 6900  O   HOH A2640       4.980  -4.609   5.803  1.00 55.89           O  
ANISOU 6900  O   HOH A2640     6685   7562   6989    271    152    295       O  
HETATM 6901  O   HOH A2641      -3.609  -0.248   7.221  1.00 44.81           O  
ANISOU 6901  O   HOH A2641     5381   5872   5773   -741    517   -487       O  
HETATM 6902  O   HOH A2642      -1.823  -2.790   7.710  1.00 33.60           O  
ANISOU 6902  O   HOH A2642     4324   4782   3661  -2076   -105    326       O  
HETATM 6903  O   HOH A2643      -3.907   1.072   4.832  1.00 48.51           O  
ANISOU 6903  O   HOH A2643     5885   5833   6713   -184    -62   -286       O  
HETATM 6904  O   HOH A2644      -1.832  -2.199  -1.719  1.00 42.01           O  
ANISOU 6904  O   HOH A2644     4646   6801   4515   -333    -79   -287       O  
HETATM 6905  O   HOH A2645      -3.721   2.872   2.966  1.00 33.78           O  
ANISOU 6905  O   HOH A2645     4310   4649   3874    483    428    225       O  
HETATM 6906  O   HOH A2646      -4.196   5.157  -0.642  1.00 29.04           O  
ANISOU 6906  O   HOH A2646     3584   3639   3810    427   -563   -547       O  
HETATM 6907  O   HOH A2647      -1.763  -1.621   2.888  1.00 42.07           O  
ANISOU 6907  O   HOH A2647     5516   5659   4809   -200    -61    -94       O  
HETATM 6908  O   HOH A2648      -1.383   6.979 -11.724  1.00 61.34           O  
ANISOU 6908  O   HOH A2648     7794   8214   7297    183   -272    -47       O  
HETATM 6909  O   HOH A2649       0.259   2.573 -10.857  1.00 55.78           O  
ANISOU 6909  O   HOH A2649     8467   7404   5322   -244    -84   -293       O  
HETATM 6910  O   HOH A2650      -1.596   6.656  -4.245  1.00 21.28           O  
ANISOU 6910  O   HOH A2650     2687   2496   2903    153     -5     94       O  
HETATM 6911  O   HOH A2651      -0.753   7.860  -8.999  1.00 39.52           O  
ANISOU 6911  O   HOH A2651     4610   5910   4495    567    -73    -98       O  
HETATM 6912  O   HOH A2652       2.718  11.434 -10.531  1.00 22.37           O  
ANISOU 6912  O   HOH A2652     2929   3470   2102    430   -306   -544       O  
HETATM 6913  O   HOH A2653      11.577  15.721  -5.925  1.00 10.84           O  
ANISOU 6913  O   HOH A2653     1467   1510   1141    237     73    256       O  
HETATM 6914  O   HOH A2654       0.544  13.952 -10.017  1.00 26.77           O  
ANISOU 6914  O   HOH A2654     3306   4327   2539    -81   -880     26       O  
HETATM 6915  O   HOH A2655      -0.868  16.325  -9.198  1.00 50.17           O  
ANISOU 6915  O   HOH A2655     7063   5747   6253    547   -472    -28       O  
HETATM 6916  O   HOH A2656      15.067  15.549  -3.609  1.00 42.95           O  
ANISOU 6916  O   HOH A2656     4565   6463   5290   -338    151   -216       O  
HETATM 6917  O   HOH A2657      17.676  17.230   0.768  1.00 51.19           O  
ANISOU 6917  O   HOH A2657     6087   7691   5672     43     64     24       O  
HETATM 6918  O   HOH A2658      18.702  13.831   3.185  1.00 42.36           O  
ANISOU 6918  O   HOH A2658     6003   4730   5364    -50   -550    282       O  
HETATM 6919  O   HOH A2659      15.491  11.870   9.716  1.00 29.56           O  
ANISOU 6919  O   HOH A2659     3280   1862   6090    290   1897    530       O  
HETATM 6920  O   HOH A2660      11.522  14.857  12.275  1.00  9.32           O  
ANISOU 6920  O   HOH A2660     1217   1134   1192     51    -40    114       O  
HETATM 6921  O   HOH A2661      22.846  17.725  13.140  1.00 21.82           O  
ANISOU 6921  O   HOH A2661     2221   3183   2886   -718    -65   1724       O  
HETATM 6922  O   HOH A2662      27.199  18.554  23.438  1.00 20.35           O  
ANISOU 6922  O   HOH A2662     1859   2483   3389   -254   -434   -360       O  
HETATM 6923  O   HOH A2663      28.209  11.292  25.465  1.00 18.29           O  
ANISOU 6923  O   HOH A2663     2190   2437   2321    424     77    131       O  
HETATM 6924  O   HOH A2664      28.653  17.048  21.416  1.00 77.55           O  
ANISOU 6924  O   HOH A2664     9684  10110   9672    158    247    137       O  
HETATM 6925  O   HOH A2665      27.096  17.755  14.322  1.00 31.80           O  
ANISOU 6925  O   HOH A2665     5589   3384   3111  -1186    656     40       O  
HETATM 6926  O   HOH A2666      29.589  14.902  15.369  1.00 34.97           O  
ANISOU 6926  O   HOH A2666     3991   4028   5268    -33   1024   -530       O  
HETATM 6927  O   HOH A2667      27.120  21.747  20.794  1.00 33.10           O  
ANISOU 6927  O   HOH A2667     3996   4287   4295  -1588   -603   -202       O  
HETATM 6928  O   HOH A2668      29.314  19.802  19.658  1.00 46.86           O  
ANISOU 6928  O   HOH A2668     4119   7212   6474    -75   -160   -273       O  
HETATM 6929  O   HOH A2669      24.051  20.471  14.557  1.00 42.34           O  
ANISOU 6929  O   HOH A2669     6374   4562   5153   -801   1105    161       O  
HETATM 6930  O   HOH A2670      21.676  23.082  15.766  1.00 46.68           O  
ANISOU 6930  O   HOH A2670     5833   6203   5701   -150   -633   -137       O  
HETATM 6931  O   HOH A2671      23.573  25.758  25.653  1.00 15.36           O  
ANISOU 6931  O   HOH A2671     2111   2065   1661   -234   -166    -37       O  
HETATM 6932  O   HOH A2672      26.444  25.856  22.246  1.00 42.79           O  
ANISOU 6932  O   HOH A2672     5227   5035   5995   -524    -60   -391       O  
HETATM 6933  O   HOH A2673      23.430  32.556  23.350  1.00 19.31           O  
ANISOU 6933  O   HOH A2673     2602   1746   2987   -768   -383   -222       O  
HETATM 6934  O   HOH A2674      22.279  30.578  14.649  1.00 56.04           O  
ANISOU 6934  O   HOH A2674     7115   7374   6803    153    558    539       O  
HETATM 6935  O   HOH A2675      19.244  27.157  15.145  1.00 42.07           O  
ANISOU 6935  O   HOH A2675     5764   4626   5593  -1220    637     75       O  
HETATM 6936  O   HOH A2676      23.289  32.484  18.626  1.00 49.77           O  
ANISOU 6936  O   HOH A2676     6190   6554   6166   -138    343   -163       O  
HETATM 6937  O   HOH A2677      19.497  35.480  27.131  1.00 41.57           O  
ANISOU 6937  O   HOH A2677     8873   3389   3534    574    251    655       O  
HETATM 6938  O   HOH A2678      19.936  37.710  24.290  1.00 19.88           O  
ANISOU 6938  O   HOH A2678     3520   1457   2577   -188   -203    -65       O  
HETATM 6939  O   HOH A2679      19.766  38.064  17.983  1.00 16.67           O  
ANISOU 6939  O   HOH A2679     2749   1569   2015   -254     86    550       O  
HETATM 6940  O   HOH A2680      14.944  33.837  24.828  1.00 47.35           O  
ANISOU 6940  O   HOH A2680     5587   5935   6467    192   1066    115       O  
HETATM 6941  O   HOH A2681       9.538  38.642  21.985  1.00 51.87           O  
ANISOU 6941  O   HOH A2681     7482   5852   6376   -281    213    -75       O  
HETATM 6942  O   HOH A2682      13.481  33.740  27.856  1.00 64.58           O  
ANISOU 6942  O   HOH A2682     8544   8098   7895    275     34     16       O  
HETATM 6943  O   HOH A2683      12.413  35.142  17.014  1.00 41.32           O  
ANISOU 6943  O   HOH A2683     6237   4076   5385   -873    -44    134       O  
HETATM 6944  O   HOH A2684      16.183  33.662  27.747  1.00 55.85           O  
ANISOU 6944  O   HOH A2684     7285   7127   6810     63     92     -5       O  
HETATM 6945  O   HOH A2685      15.970  34.655  13.684  1.00 27.11           O  
ANISOU 6945  O   HOH A2685     5044   2709   2546   -763    492    507       O  
HETATM 6946  O   HOH A2686      14.128  31.319  13.455  1.00 14.60           O  
ANISOU 6946  O   HOH A2686     2299   1756   1492   -474    -30    340       O  
HETATM 6947  O   HOH A2687      23.856  37.370  16.040  1.00 43.81           O  
ANISOU 6947  O   HOH A2687     3789   6595   6262   -137    548    318       O  
HETATM 6948  O   HOH A2688      13.972  33.643  22.245  1.00 19.27           O  
ANISOU 6948  O   HOH A2688     3253   1850   2220   -847    522   -171       O  
HETATM 6949  O   HOH A2689      10.044  30.988  16.486  1.00 14.09           O  
ANISOU 6949  O   HOH A2689     2198   1689   1469   -131   -127    304       O  
HETATM 6950  O   HOH A2690       9.130  34.631  27.816  1.00 46.62           O  
ANISOU 6950  O   HOH A2690     6300   6677   4735    -69   -577   -608       O  
HETATM 6951  O   HOH A2691       1.025  31.021  23.520  1.00 25.64           O  
ANISOU 6951  O   HOH A2691     4261   2816   2665   1071   -363    -86       O  
HETATM 6952  O   HOH A2692       7.264  35.915  24.320  1.00 42.57           O  
ANISOU 6952  O   HOH A2692     6711   3953   5508   -660     -3   -257       O  
HETATM 6953  O   HOH A2693       4.742  35.674  25.193  1.00 53.15           O  
ANISOU 6953  O   HOH A2693     6996   6236   6962    556   -384    -62       O  
HETATM 6954  O   HOH A2694       3.172  31.290  26.810  1.00 35.18           O  
ANISOU 6954  O   HOH A2694     4642   3513   5210     48    378   -578       O  
HETATM 6955  O   HOH A2695       0.268  29.678  29.732  1.00 34.25           O  
ANISOU 6955  O   HOH A2695     4665   4305   4045    111    180   -156       O  
HETATM 6956  O   HOH A2696      -3.757  28.805  30.078  1.00 18.31           O  
ANISOU 6956  O   HOH A2696     2671   2498   1788    697    435    -48       O  
HETATM 6957  O   HOH A2697      -3.533  29.862  26.262  1.00 31.70           O  
ANISOU 6957  O   HOH A2697     4807   3679   3560   1789     13    832       O  
HETATM 6958  O   HOH A2698      -3.540  25.475  33.065  1.00 32.35           O  
ANISOU 6958  O   HOH A2698     3240   4813   4239    491    132    832       O  
HETATM 6959  O   HOH A2699      -2.413  27.715  32.268  1.00 18.08           O  
ANISOU 6959  O   HOH A2699     2579   2636   1653    730    334   -204       O  
HETATM 6960  O   HOH A2700      -1.824  26.519  36.515  1.00 25.54           O  
ANISOU 6960  O   HOH A2700     4479   3177   2050    102    804   -295       O  
HETATM 6961  O   HOH A2701       4.852  20.370  41.477  1.00 16.57           O  
ANISOU 6961  O   HOH A2701     2122   2473   1700     21    132   -172       O  
HETATM 6962  O   HOH A2702       4.010  14.485  43.780  1.00 23.18           O  
ANISOU 6962  O   HOH A2702     3609   2875   2323    425   -351    123       O  
HETATM 6963  O   HOH A2703       4.887  17.803  44.988  1.00 23.06           O  
ANISOU 6963  O   HOH A2703     4057   2759   1945   -386    -12    149       O  
HETATM 6964  O   HOH A2704      -3.224  14.270  37.716  1.00 15.52           O  
ANISOU 6964  O   HOH A2704     2134   2308   1454   -337    341    252       O  
HETATM 6965  O   HOH A2705      -1.634  13.744  41.647  1.00 28.43           O  
ANISOU 6965  O   HOH A2705     4438   3673   2690   -456    203    590       O  
HETATM 6966  O   HOH A2706      -6.487  22.374  43.034  1.00 29.47           O  
ANISOU 6966  O   HOH A2706     3385   5343   2471   -250    477   -492       O  
HETATM 6967  O   HOH A2707      -5.805  23.548  37.552  1.00 37.52           O  
ANISOU 6967  O   HOH A2707     4511   5988   3755    655    125   -880       O  
HETATM 6968  O   HOH A2708      -4.883  10.868  31.681  1.00 25.22           O  
ANISOU 6968  O   HOH A2708     4824   2626   2135    247   -477    234       O  
HETATM 6969  O   HOH A2709      -4.658  12.269  38.898  1.00 28.88           O  
ANISOU 6969  O   HOH A2709     4803   3345   2824   -903   1644    -87       O  
HETATM 6970  O   HOH A2710      -8.926  21.917  32.511  1.00 37.07           O  
ANISOU 6970  O   HOH A2710     5122   4960   4004    478    426    138       O  
HETATM 6971  O   HOH A2711      -8.360  19.299  31.679  1.00 36.16           O  
ANISOU 6971  O   HOH A2711     4517   4971   4250    250   1285    568       O  
HETATM 6972  O   HOH A2712      -5.160  16.031  37.076  1.00 19.38           O  
ANISOU 6972  O   HOH A2712     2544   3104   1716   -148    252      3       O  
HETATM 6973  O   HOH A2713      -6.066  24.228  33.177  1.00 43.56           O  
ANISOU 6973  O   HOH A2713     4919   6408   5224    430   -250    -27       O  
HETATM 6974  O   HOH A2714      -7.468  11.685  32.449  1.00 29.06           O  
ANISOU 6974  O   HOH A2714     4513   3085   3445    -68   -766    413       O  
HETATM 6975  O   HOH A2715      -8.689  13.918  34.788  1.00 32.79           O  
ANISOU 6975  O   HOH A2715     4842   4142   3475    -16     -8    592       O  
HETATM 6976  O   HOH A2716      -8.708  12.157  29.111  1.00 26.95           O  
ANISOU 6976  O   HOH A2716     2590   4824   2827    551    680    297       O  
HETATM 6977  O   HOH A2717     -10.448  15.431  27.159  1.00 23.90           O  
ANISOU 6977  O   HOH A2717     2091   3943   3045   -394    142    511       O  
HETATM 6978  O   HOH A2718     -11.680  13.088  32.097  1.00 55.39           O  
ANISOU 6978  O   HOH A2718     6929   7589   6527   -170    478     99       O  
HETATM 6979  O   HOH A2719      -9.724  17.680  33.318  1.00 26.39           O  
ANISOU 6979  O   HOH A2719     3028   3837   3162    -17    670    617       O  
HETATM 6980  O   HOH A2720      -7.093   7.794  30.054  1.00 38.26           O  
ANISOU 6980  O   HOH A2720     5137   4251   5149   -256    482    860       O  
HETATM 6981  O   HOH A2721      -7.392  15.063  20.381  1.00 21.63           O  
ANISOU 6981  O   HOH A2721     2020   4185   2015    202     60    407       O  
HETATM 6982  O   HOH A2722      -9.762  12.708  22.267  1.00 47.99           O  
ANISOU 6982  O   HOH A2722     6212   6658   5365      8   -336   -887       O  
HETATM 6983  O   HOH A2723     -11.514  21.868  21.752  1.00 48.95           O  
ANISOU 6983  O   HOH A2723     5978   5672   6948    657    116    323       O  
HETATM 6984  O   HOH A2724     -13.419  18.606  22.571  1.00 40.19           O  
ANISOU 6984  O   HOH A2724     3182   6753   5336   -101   -446    478       O  
HETATM 6985  O   HOH A2725      -7.682  24.805  19.946  1.00 24.84           O  
ANISOU 6985  O   HOH A2725     2932   3319   3186    710   -436    214       O  
HETATM 6986  O   HOH A2726      -4.571  26.181  22.807  1.00 35.29           O  
ANISOU 6986  O   HOH A2726     4410   4851   4147    141   -208    238       O  
HETATM 6987  O   HOH A2727      -9.935  19.503  29.376  1.00 40.68           O  
ANISOU 6987  O   HOH A2727     4380   5837   5237    549    506    613       O  
HETATM 6988  O   HOH A2728      -5.045  19.716  21.599  1.00 13.93           O  
ANISOU 6988  O   HOH A2728     1597   1879   1818   -116     38    331       O  
HETATM 6989  O   HOH A2729      -1.936  19.562  27.099  1.00 10.61           O  
ANISOU 6989  O   HOH A2729     1371   1385   1277     70     55    148       O  
HETATM 6990  O   HOH A2730       7.943  27.436  35.955  1.00 50.63           O  
ANISOU 6990  O   HOH A2730     7005   7118   5116     94    250     68       O  
HETATM 6991  O   HOH A2731       2.421  25.469  37.108  1.00 33.68           O  
ANISOU 6991  O   HOH A2731     5567   4029   3202   -758   -287   -641       O  
HETATM 6992  O   HOH A2732       4.492  24.709  39.824  1.00 26.92           O  
ANISOU 6992  O   HOH A2732     5314   2579   2334   -150    876     16       O  
HETATM 6993  O   HOH A2733       5.871  26.798  33.719  1.00 18.99           O  
ANISOU 6993  O   HOH A2733     2286   2751   2181     10     80    203       O  
HETATM 6994  O   HOH A2734       4.274  24.697  34.736  1.00 17.07           O  
ANISOU 6994  O   HOH A2734     2281   2098   2106    176    -63   -142       O  
HETATM 6995  O   HOH A2735      10.236  20.041  43.496  1.00 27.01           O  
ANISOU 6995  O   HOH A2735     3788   3375   3099     71   -575    150       O  
HETATM 6996  O   HOH A2736       6.677  17.257  41.781  1.00 15.42           O  
ANISOU 6996  O   HOH A2736     2106   1853   1900    326     50    346       O  
HETATM 6997  O   HOH A2737      10.122  22.776  38.951  1.00 25.26           O  
ANISOU 6997  O   HOH A2737     3411   3962   2223  -1389    896  -1258       O  
HETATM 6998  O   HOH A2738       7.458  23.279  42.513  1.00 25.96           O  
ANISOU 6998  O   HOH A2738     4418   3395   2050    191    453   -729       O  
HETATM 6999  O   HOH A2739       9.673  23.889  42.399  1.00 47.67           O  
ANISOU 6999  O   HOH A2739     8145   5981   3987    -95    -56   -580       O  
HETATM 7000  O  AHOH A2740       6.865  13.283  19.392  0.60  9.71           O  
ANISOU 7000  O  AHOH A2740     1483    969   1238   -120     20     84       O  
HETATM 7001  O  BHOH A2741       7.740  12.459  20.176  0.40  7.75           O  
ANISOU 7001  O  BHOH A2741     1117    855    972   -220    -73    310       O  
HETATM 7002  O   HOH A2742       0.750  19.886  20.799  1.00 13.01           O  
ANISOU 7002  O   HOH A2742     2012   1191   1741   -125    621     36       O  
HETATM 7003  O   HOH A2743      -8.135  15.298   6.743  1.00 32.22           O  
ANISOU 7003  O   HOH A2743     4589   5207   2448   1462   -470    107       O  
HETATM 7004  O   HOH A2744      -3.671  14.219  17.019  1.00 30.53           O  
ANISOU 7004  O   HOH A2744     4031   4622   2949  -1191    219    -94       O  
HETATM 7005  O   HOH A2745      -7.449  19.359  17.646  1.00 16.99           O  
ANISOU 7005  O   HOH A2745     2221   2509   1724    683    485    398       O  
HETATM 7006  O   HOH A2746      -8.662  16.543  15.785  1.00 57.87           O  
ANISOU 7006  O   HOH A2746     7370   7473   7143   -280     78   -238       O  
HETATM 7007  O   HOH A2747       1.296  19.019  14.893  1.00  8.93           O  
ANISOU 7007  O   HOH A2747     1176   1059   1159     41     97    257       O  
HETATM 7008  O   HOH A2748      -8.180  12.434  12.926  1.00 31.41           O  
ANISOU 7008  O   HOH A2748     3433   3709   4793   -475    296    152       O  
HETATM 7009  O   HOH A2749      -4.251  17.882  19.594  1.00 24.61           O  
ANISOU 7009  O   HOH A2749     3728   2764   2858   -766    972   -196       O  
HETATM 7010  O   HOH A2750      -5.887  16.591   5.911  1.00 29.87           O  
ANISOU 7010  O   HOH A2750     4179   4015   3157    847    211     70       O  
HETATM 7011  O   HOH A2751      -9.519  12.289  10.609  1.00 82.55           O  
ANISOU 7011  O   HOH A2751    10822  10616   9929    -94     99    -10       O  
HETATM 7012  O   HOH A2752       6.760   4.412  16.376  1.00 30.11           O  
ANISOU 7012  O   HOH A2752     3801   2566   5074    547   -473   -327       O  
HETATM 7013  O   HOH B2001      11.721  17.867 -52.114  1.00 59.08           O  
ANISOU 7013  O   HOH B2001     7583   7697   7170    131    332    197       O  
HETATM 7014  O   HOH B2002      13.303  10.709 -51.636  1.00 49.97           O  
ANISOU 7014  O   HOH B2002     6241   7447   5297     79    310   -626       O  
HETATM 7015  O   HOH B2003      15.231  13.716 -48.448  1.00 36.22           O  
ANISOU 7015  O   HOH B2003     5201   5566   2995   -111    537   -127       O  
HETATM 7016  O   HOH B2004       7.195  20.183 -54.480  1.00 64.46           O  
ANISOU 7016  O   HOH B2004     8615   8474   7405     21    -37    280       O  
HETATM 7017  O   HOH B2005      15.687  11.982 -52.049  1.00 71.31           O  
ANISOU 7017  O   HOH B2005     9284   9597   8212    161     56    174       O  
HETATM 7018  O   HOH B2006      17.190  13.249 -50.371  1.00 49.06           O  
ANISOU 7018  O   HOH B2006     6904   7140   4596     63    979   -382       O  
HETATM 7019  O   HOH B2007       9.023  22.870 -54.667  1.00 47.48           O  
ANISOU 7019  O   HOH B2007     6099   6452   5490   -251    465    621       O  
HETATM 7020  O   HOH B2008      -0.879  16.321 -47.483  1.00 56.83           O  
ANISOU 7020  O   HOH B2008     7236   7234   7122    -63   -407    -45       O  
HETATM 7021  O   HOH B2009       5.052   8.171 -55.175  1.00 57.95           O  
ANISOU 7021  O   HOH B2009     7813   7283   6921    193    248    -15       O  
HETATM 7022  O   HOH B2010      12.999  12.223 -49.227  1.00 30.98           O  
ANISOU 7022  O   HOH B2010     4412   4845   2513     -3    256    249       O  
HETATM 7023  O   HOH B2011      12.245  15.942 -50.297  1.00 36.34           O  
ANISOU 7023  O   HOH B2011     5053   5492   3263   -820   1358    435       O  
HETATM 7024  O   HOH B2012      -1.730  12.776 -51.146  1.00 50.68           O  
ANISOU 7024  O   HOH B2012     5958   7672   5627    -44   -682     63       O  
HETATM 7025  O   HOH B2013       1.674  13.889 -53.700  1.00 61.27           O  
ANISOU 7025  O   HOH B2013     7351   8493   7434     20   -274   -104       O  
HETATM 7026  O   HOH B2014      -0.544  16.329 -51.107  1.00 78.20           O  
ANISOU 7026  O   HOH B2014     9992  10194   9525     57     87    176       O  
HETATM 7027  O   HOH B2015       3.806   7.916 -52.613  1.00 49.73           O  
ANISOU 7027  O   HOH B2015     6698   6748   5448    185    -50    -36       O  
HETATM 7028  O   HOH B2016       5.451  18.957 -52.427  1.00 64.09           O  
ANISOU 7028  O   HOH B2016     8578   8575   7199    -64    119    251       O  
HETATM 7029  O   HOH B2017       5.674   6.373 -52.998  1.00 59.52           O  
ANISOU 7029  O   HOH B2017     7595   8017   7003    188   -353     29       O  
HETATM 7030  O   HOH B2018       1.631  20.059 -48.161  1.00 41.19           O  
ANISOU 7030  O   HOH B2018     5569   5251   4830    714   -218    280       O  
HETATM 7031  O   HOH B2019      -2.549  14.196 -44.900  1.00 39.98           O  
ANISOU 7031  O   HOH B2019     5459   5875   3856    -81   -890    197       O  
HETATM 7032  O   HOH B2020       7.401  17.173 -56.895  1.00 52.11           O  
ANISOU 7032  O   HOH B2020     6487   6761   6552   -554    142    483       O  
HETATM 7033  O   HOH B2021       2.301  10.317 -51.831  1.00 41.24           O  
ANISOU 7033  O   HOH B2021     4962   6649   4059    282   -677   -577       O  
HETATM 7034  O   HOH B2022       6.053  10.799 -50.992  1.00 32.01           O  
ANISOU 7034  O   HOH B2022     4409   5275   2477   -313    214     79       O  
HETATM 7035  O   HOH B2023       0.813  14.003 -51.113  1.00 30.21           O  
ANISOU 7035  O   HOH B2023     3703   4888   2888    -34  -1241    508       O  
HETATM 7036  O   HOH B2024      -2.543  -8.084 -35.363  1.00 35.89           O  
ANISOU 7036  O   HOH B2024     4645   3671   5320  -1782  -1674    150       O  
HETATM 7037  O   HOH B2025      -8.484  -0.662 -27.756  1.00 60.18           O  
ANISOU 7037  O   HOH B2025     7234   7702   7932   -246    -98     39       O  
HETATM 7038  O   HOH B2026      -8.740   0.190 -35.446  1.00 47.01           O  
ANISOU 7038  O   HOH B2026     4890   7255   5717   -975   -500   -500       O  
HETATM 7039  O   HOH B2027      -7.903  -6.704 -27.007  1.00 49.52           O  
ANISOU 7039  O   HOH B2027     5308   6775   6734   -283    -25    154       O  
HETATM 7040  O   HOH B2028      20.858  10.714 -46.357  1.00 65.37           O  
ANISOU 7040  O   HOH B2028     8101   8775   7960      3     67    -39       O  
HETATM 7041  O   HOH B2029      -7.288  11.656 -22.775  1.00 63.11           O  
ANISOU 7041  O   HOH B2029     7834   8336   7810     56    390     45       O  
HETATM 7042  O   HOH B2030       3.038  -8.951 -18.193  1.00 55.68           O  
ANISOU 7042  O   HOH B2030     7493   7786   5878   -115     45    382       O  
HETATM 7043  O   HOH B2031       1.413 -10.632 -21.737  1.00 39.56           O  
ANISOU 7043  O   HOH B2031     5553   4562   4916   -195     11   -132       O  
HETATM 7044  O   HOH B2032       4.933 -13.147 -20.460  1.00 59.61           O  
ANISOU 7044  O   HOH B2032     7633   7423   7594   -291    274    324       O  
HETATM 7045  O   HOH B2033       2.176 -11.770 -26.289  1.00 69.32           O  
ANISOU 7045  O   HOH B2033     9102   8654   8582    184   -118    137       O  
HETATM 7046  O   HOH B2034       6.377   3.254 -50.703  1.00 34.40           O  
ANISOU 7046  O   HOH B2034     4813   4612   3648    -10    652  -1235       O  
HETATM 7047  O   HOH B2035       5.714   7.862 -50.756  1.00 27.70           O  
ANISOU 7047  O   HOH B2035     4036   4167   2320    288    752    -67       O  
HETATM 7048  O   HOH B2036       8.906   5.738 -48.590  1.00 31.56           O  
ANISOU 7048  O   HOH B2036     3408   5202   3380   -132    522   -399       O  
HETATM 7049  O   HOH B2037       1.830   5.898 -53.856  1.00 38.70           O  
ANISOU 7049  O   HOH B2037     6847   5075   2780    599    147   -668       O  
HETATM 7050  O   HOH B2038      -1.379  -7.241 -48.112  1.00 71.43           O  
ANISOU 7050  O   HOH B2038     9192   9279   8669    162   -153     92       O  
HETATM 7051  O   HOH B2039       6.121  -4.499 -44.756  1.00 27.71           O  
ANISOU 7051  O   HOH B2039     3918   4134   2477    101    289     35       O  
HETATM 7052  O   HOH B2040       2.217  -3.735 -46.678  1.00 20.58           O  
ANISOU 7052  O   HOH B2040     2419   2965   2434   -391    299   -957       O  
HETATM 7053  O   HOH B2041      -1.533   2.656 -54.628  1.00 61.81           O  
ANISOU 7053  O   HOH B2041     7952   8038   7497    216    -43     32       O  
HETATM 7054  O   HOH B2042      -4.427  12.078 -48.072  1.00 57.95           O  
ANISOU 7054  O   HOH B2042     7283   7805   6931    -42   -121      9       O  
HETATM 7055  O   HOH B2043      -1.619  11.417 -44.911  1.00 31.09           O  
ANISOU 7055  O   HOH B2043     3973   5365   2477     71   -454    242       O  
HETATM 7056  O   HOH B2044      12.479  27.730 -45.337  1.00 76.45           O  
ANISOU 7056  O   HOH B2044    10147   9567   9334     15     53     63       O  
HETATM 7057  O   HOH B2045      15.128  24.418 -43.664  1.00 27.69           O  
ANISOU 7057  O   HOH B2045     3637   3925   2961    141    877    104       O  
HETATM 7058  O   HOH B2046      15.920  26.255 -28.183  1.00 51.26           O  
ANISOU 7058  O   HOH B2046     6580   7256   5640     92    -46     38       O  
HETATM 7059  O   HOH B2047       3.630  -0.491 -32.755  1.00 15.73           O  
ANISOU 7059  O   HOH B2047     1661   2383   1934    -78    -72   -702       O  
HETATM 7060  O   HOH B2048      -2.489  16.085 -42.650  1.00 28.52           O  
ANISOU 7060  O   HOH B2048     3280   4517   3041    636   -400    557       O  
HETATM 7061  O   HOH B2049       5.204  23.548 -44.807  1.00 56.84           O  
ANISOU 7061  O   HOH B2049     7428   8253   5917    147    -67      6       O  
HETATM 7062  O   HOH B2050      -0.175  22.546 -42.448  1.00 44.22           O  
ANISOU 7062  O   HOH B2050     5784   5382   5636    547   -395    365       O  
HETATM 7063  O   HOH B2051      -2.886  23.129 -38.188  1.00 70.78           O  
ANISOU 7063  O   HOH B2051     9334   9108   8449    166     33    397       O  
HETATM 7064  O   HOH B2052      -6.528  20.475 -35.958  1.00 76.60           O  
ANISOU 7064  O   HOH B2052     9558   9992   9555     68      3    172       O  
HETATM 7065  O   HOH B2053       0.908  21.912 -32.808  1.00 38.43           O  
ANISOU 7065  O   HOH B2053     6457   4336   3810   1246   -168   -372       O  
HETATM 7066  O   HOH B2054      -2.026  23.592 -40.857  1.00 61.71           O  
ANISOU 7066  O   HOH B2054     7930   8300   7217     76    -23    223       O  
HETATM 7067  O   HOH B2055      11.314  31.199 -13.523  1.00 61.85           O  
ANISOU 7067  O   HOH B2055     8771   7116   7614    164    142   -334       O  
HETATM 7068  O   HOH B2056      -7.426  -2.268 -33.657  1.00 41.51           O  
ANISOU 7068  O   HOH B2056     4104   6723   4947    258   -102    503       O  
HETATM 7069  O   HOH B2057      -7.190  -2.656 -30.163  1.00 44.82           O  
ANISOU 7069  O   HOH B2057     5381   6263   5386   -496   -267   -837       O  
HETATM 7070  O   HOH B2058      -0.973  -6.204 -34.038  1.00 21.03           O  
ANISOU 7070  O   HOH B2058     2483   2591   2917   -497   -526   -520       O  
HETATM 7071  O   HOH B2059      -0.575  21.460 -16.197  1.00 46.59           O  
ANISOU 7071  O   HOH B2059     5741   6913   5049    364    133   -258       O  
HETATM 7072  O   HOH B2060      -4.764  -8.915 -34.470  1.00 42.57           O  
ANISOU 7072  O   HOH B2060     5880   5417   4877  -1106   -482   -102       O  
HETATM 7073  O   HOH B2061      -8.562 -10.391 -32.727  1.00 46.15           O  
ANISOU 7073  O   HOH B2061     5892   5810   5834   -410     47   -126       O  
HETATM 7074  O   HOH B2062      -5.756  -9.322 -27.935  1.00 33.42           O  
ANISOU 7074  O   HOH B2062     2908   6046   3742  -1303    196   -154       O  
HETATM 7075  O   HOH B2063      16.693  10.918 -46.631  1.00 36.00           O  
ANISOU 7075  O   HOH B2063     4802   3891   4984    -67    518   1084       O  
HETATM 7076  O   HOH B2064      19.429   8.113 -44.939  1.00 63.92           O  
ANISOU 7076  O   HOH B2064     8133   8462   7693     52    -31   -225       O  
HETATM 7077  O   HOH B2065      17.767   5.508 -50.898  1.00 72.39           O  
ANISOU 7077  O   HOH B2065     9483   9210   8813    -10    175     15       O  
HETATM 7078  O   HOH B2066       3.568  25.542 -31.011  1.00 54.63           O  
ANISOU 7078  O   HOH B2066     6694   7414   6648    -69    255   -181       O  
HETATM 7079  O   HOH B2067      -8.264  13.680 -25.217  1.00 49.73           O  
ANISOU 7079  O   HOH B2067     5823   7160   5914    335    245    -33       O  
HETATM 7080  O   HOH B2068      -6.315  -4.547 -27.150  1.00 27.82           O  
ANISOU 7080  O   HOH B2068     2553   3382   4637    -78    669   -544       O  
HETATM 7081  O   HOH B2069      -5.756  -9.920 -21.098  1.00 40.00           O  
ANISOU 7081  O   HOH B2069     5557   4612   5029    170    434     28       O  
HETATM 7082  O   HOH B2070      -4.348  -6.344 -20.043  1.00 44.46           O  
ANISOU 7082  O   HOH B2070     5716   6224   4952   -555   -261   -407       O  
HETATM 7083  O   HOH B2071      -6.366  -3.148 -24.583  1.00 51.85           O  
ANISOU 7083  O   HOH B2071     7043   6009   6648   -191    352   -364       O  
HETATM 7084  O   HOH B2072      11.834 -10.315 -16.838  1.00 47.31           O  
ANISOU 7084  O   HOH B2072     5490   7403   5082    -88    377    202       O  
HETATM 7085  O   HOH B2073       9.253 -11.319 -17.893  1.00 56.48           O  
ANISOU 7085  O   HOH B2073     7074   7786   6600   -247     22    -73       O  
HETATM 7086  O   HOH B2074       4.038 -10.441 -20.769  1.00 46.42           O  
ANISOU 7086  O   HOH B2074     6015   5502   6122   -172    527     66       O  
HETATM 7087  O   HOH B2075       2.337 -10.302 -24.274  1.00 43.25           O  
ANISOU 7087  O   HOH B2075     5906   4835   5691   -165    223   -128       O  
HETATM 7088  O   HOH B2076      -1.685 -10.837 -18.454  1.00 51.85           O  
ANISOU 7088  O   HOH B2076     6165   7476   6060   -540    416    100       O  
HETATM 7089  O   HOH B2077      -3.695 -12.826 -27.804  1.00 32.28           O  
ANISOU 7089  O   HOH B2077     4487   3556   4223   -421    154     37       O  
HETATM 7090  O   HOH B2078       6.366  -7.699 -18.168  1.00 31.26           O  
ANISOU 7090  O   HOH B2078     4970   3821   3087    197    306     35       O  
HETATM 7091  O   HOH B2079       9.260   9.098 -53.311  1.00 45.93           O  
ANISOU 7091  O   HOH B2079     6878   6127   4446    147    331   -856       O  
HETATM 7092  O   HOH B2080       2.113  25.468 -33.740  1.00 46.92           O  
ANISOU 7092  O   HOH B2080     5809   5603   6415    325    307   -440       O  
HETATM 7093  O   HOH B2081      -3.254 -14.409 -29.976  1.00 31.36           O  
ANISOU 7093  O   HOH B2081     4366   3577   3972  -1066   -303   1063       O  
HETATM 7094  O   HOH B2082       4.382  -7.956 -30.021  1.00 31.01           O  
ANISOU 7094  O   HOH B2082     3291   5562   2929   -652    495  -1800       O  
HETATM 7095  O   HOH B2083      -7.552 -13.219 -30.552  1.00 47.66           O  
ANISOU 7095  O   HOH B2083     4944   6942   6222   -843    140    -26       O  
HETATM 7096  O   HOH B2084       3.232 -11.385 -28.664  1.00 44.02           O  
ANISOU 7096  O   HOH B2084     5410   5743   5573   -489   -501   -296       O  
HETATM 7097  O   HOH B2085       0.000  -9.559 -35.564  1.00 27.11           O  
ANISOU 7097  O   HOH B2085     3340   2729   4232   -189   -443   -718       O  
HETATM 7098  O   HOH B2086      -5.187   6.279 -19.804  1.00 55.61           O  
ANISOU 7098  O   HOH B2086     7510   7460   6158   -224    -50    158       O  
HETATM 7099  O   HOH B2087      22.617   0.141 -47.748  1.00 59.59           O  
ANISOU 7099  O   HOH B2087     8166   7966   6508   -115    -23     53       O  
HETATM 7100  O   HOH B2088       3.310  -9.875 -38.096  1.00 43.71           O  
ANISOU 7100  O   HOH B2088     6172   5774   4661     48   -301   -752       O  
HETATM 7101  O   HOH B2089      -7.020   2.408 -23.281  1.00 55.01           O  
ANISOU 7101  O   HOH B2089     6721   7756   6424    157   -125     13       O  
HETATM 7102  O   HOH B2090      -8.115   3.715 -25.518  1.00 58.39           O  
ANISOU 7102  O   HOH B2090     7042   8014   7131    -22     83    242       O  
HETATM 7103  O   HOH B2091      -7.827   6.606 -23.576  1.00 54.40           O  
ANISOU 7103  O   HOH B2091     6326   7710   6632     35    463    203       O  
HETATM 7104  O   HOH B2092      -8.254   3.253 -21.167  1.00 54.76           O  
ANISOU 7104  O   HOH B2092     6930   7317   6561    192    366    105       O  
HETATM 7105  O   HOH B2093       1.364  -8.324 -41.964  1.00 56.76           O  
ANISOU 7105  O   HOH B2093     7309   7971   6286   -139    409    368       O  
HETATM 7106  O   HOH B2094      -2.064  -7.899 -39.037  1.00 40.98           O  
ANISOU 7106  O   HOH B2094     4900   4631   6042   -519   -447   -369       O  
HETATM 7107  O   HOH B2095      -9.008   4.377 -33.388  1.00 67.34           O  
ANISOU 7107  O   HOH B2095     8397   8996   8194     91     45     32       O  
HETATM 7108  O   HOH B2096       5.238  -8.052 -43.181  1.00 53.15           O  
ANISOU 7108  O   HOH B2096     6737   7241   6215   -100   -441   -214       O  
HETATM 7109  O   HOH B2097       2.864  -6.151 -45.173  1.00 25.53           O  
ANISOU 7109  O   HOH B2097     4020   3526   2154   -206    334   -394       O  
HETATM 7110  O   HOH B2098       4.116  -8.512 -40.180  1.00 42.39           O  
ANISOU 7110  O   HOH B2098     5492   3949   6663   -100    327   -620       O  
HETATM 7111  O   HOH B2099      -1.049  -1.717 -44.876  1.00 22.02           O  
ANISOU 7111  O   HOH B2099     2177   3709   2480    -70   -288   -989       O  
HETATM 7112  O   HOH B2100      -1.217  -5.637 -45.063  1.00 59.71           O  
ANISOU 7112  O   HOH B2100     7700   7751   7237   -129   -128   -181       O  
HETATM 7113  O   HOH B2101      35.312  -0.615   0.155  1.00 53.33           O  
ANISOU 7113  O   HOH B2101     6264   7439   6558    599   -255    645       O  
HETATM 7114  O   HOH B2102       4.157   2.705 -52.186  1.00 41.74           O  
ANISOU 7114  O   HOH B2102     5739   5175   4944     52    235    -79       O  
HETATM 7115  O   HOH B2103       0.735   1.469 -52.118  1.00 27.46           O  
ANISOU 7115  O   HOH B2103     4683   3792   1960   -575    -99   -244       O  
HETATM 7116  O   HOH B2104       4.905   1.558 -48.983  1.00 28.66           O  
ANISOU 7116  O   HOH B2104     5171   2823   2896   1082    929    475       O  
HETATM 7117  O   HOH B2105       9.140  21.365 -46.598  1.00 34.50           O  
ANISOU 7117  O   HOH B2105     4289   5047   3773    275   -988   -337       O  
HETATM 7118  O   HOH B2106      -4.212   6.945 -49.888  1.00 60.54           O  
ANISOU 7118  O   HOH B2106     7752   8285   6965   -114   -312    226       O  
HETATM 7119  O   HOH B2107      -2.023   1.853 -45.406  1.00 25.15           O  
ANISOU 7119  O   HOH B2107     2521   4464   2571    651   -194   -651       O  
HETATM 7120  O   HOH B2108      -1.786   1.917 -47.966  1.00 70.62           O  
ANISOU 7120  O   HOH B2108     8822   9490   8521    322   -106    108       O  
HETATM 7121  O   HOH B2109      -4.491   4.020 -45.285  1.00 45.62           O  
ANISOU 7121  O   HOH B2109     7097   5478   4758    462    481    102       O  
HETATM 7122  O   HOH B2110      -1.314   8.755 -50.180  1.00 59.48           O  
ANISOU 7122  O   HOH B2110     8025   7612   6961   -171   -426   -419       O  
HETATM 7123  O   HOH B2111      -3.177  10.119 -46.902  1.00 34.73           O  
ANISOU 7123  O   HOH B2111     4216   5701   3279   -242   -709   -197       O  
HETATM 7124  O   HOH B2112       9.717  24.588 -46.698  1.00 61.56           O  
ANISOU 7124  O   HOH B2112     7799   8136   7457    -72    -72    115       O  
HETATM 7125  O   HOH B2113      11.094  25.336 -44.586  1.00 53.88           O  
ANISOU 7125  O   HOH B2113     7397   6555   6519    185    -74    117       O  
HETATM 7126  O   HOH B2114      12.921  23.556 -45.069  1.00 25.18           O  
ANISOU 7126  O   HOH B2114     4002   3285   2282      3    610    456       O  
HETATM 7127  O   HOH B2115      12.652  27.750 -42.785  1.00 67.52           O  
ANISOU 7127  O   HOH B2115     8665   8809   8179    204    238      5       O  
HETATM 7128  O   HOH B2116      13.412  30.727 -39.364  1.00 51.30           O  
ANISOU 7128  O   HOH B2116     6733   7430   5330   -287    -19   -433       O  
HETATM 7129  O   HOH B2117      15.826  31.043 -37.687  1.00 49.34           O  
ANISOU 7129  O   HOH B2117     6893   6285   5571    -96    -33   -319       O  
HETATM 7130  O   HOH B2118      30.349 -16.730 -16.530  1.00 50.59           O  
ANISOU 7130  O   HOH B2118     6702   5802   6717    740     80   -349       O  
HETATM 7131  O   HOH B2119      18.377  24.784 -30.121  1.00 38.51           O  
ANISOU 7131  O   HOH B2119     6032   4268   4333    272  -1080   -186       O  
HETATM 7132  O   HOH B2120      21.982  22.979 -32.060  1.00 26.71           O  
ANISOU 7132  O   HOH B2120     3384   3311   3452   -428   -235     38       O  
HETATM 7133  O   HOH B2121      15.201  26.402 -41.778  1.00 41.44           O  
ANISOU 7133  O   HOH B2121     5576   5147   5022   -178    496   -394       O  
HETATM 7134  O   HOH B2122      32.616 -14.902 -16.800  1.00 39.84           O  
ANISOU 7134  O   HOH B2122     5342   4465   5329   1134    136     -9       O  
HETATM 7135  O   HOH B2123      34.250  -0.238 -23.182  1.00 46.30           O  
ANISOU 7135  O   HOH B2123     5146   6709   5736    534    471    -67       O  
HETATM 7136  O   HOH B2124      -0.168  17.501 -42.760  1.00 28.63           O  
ANISOU 7136  O   HOH B2124     3256   4021   3602    595   -316      8       O  
HETATM 7137  O   HOH B2125       1.717  20.742 -43.513  1.00 54.14           O  
ANISOU 7137  O   HOH B2125     7565   7499   5506    410   -277      8       O  
HETATM 7138  O   HOH B2126       5.134  20.207 -44.596  1.00 31.72           O  
ANISOU 7138  O   HOH B2126     5156   4509   2387    189   -109    498       O  
HETATM 7139  O   HOH B2127      24.222   9.332 -42.388  1.00 32.00           O  
ANISOU 7139  O   HOH B2127     4457   4200   3502    251    213     84       O  
HETATM 7140  O   HOH B2128      27.830   7.080 -41.907  1.00 58.53           O  
ANISOU 7140  O   HOH B2128     7284   7927   7029    192    156   -258       O  
HETATM 7141  O   HOH B2129      27.780   7.133 -39.190  1.00 46.20           O  
ANISOU 7141  O   HOH B2129     5797   6714   5043   -290    819   -444       O  
HETATM 7142  O   HOH B2130       8.809  -7.912   5.640  1.00 45.41           O  
ANISOU 7142  O   HOH B2130     6003   5193   6056    161    288    489       O  
HETATM 7143  O   HOH B2131      -4.705  21.248 -38.599  1.00 56.59           O  
ANISOU 7143  O   HOH B2131     6615   7956   6931    333   -249    147       O  
HETATM 7144  O   HOH B2132      -5.252  17.004 -38.843  1.00 38.03           O  
ANISOU 7144  O   HOH B2132     5248   5605   3595   -130  -1036    318       O  
HETATM 7145  O   HOH B2133      -6.998  20.634 -40.521  1.00 78.16           O  
ANISOU 7145  O   HOH B2133    10007  10423   9268     25    -69     51       O  
HETATM 7146  O   HOH B2134      -4.789  17.604 -41.994  1.00 41.21           O  
ANISOU 7146  O   HOH B2134     4578   5106   5975    468   -462    697       O  
HETATM 7147  O   HOH B2135      23.246  -2.218  14.558  1.00 44.74           O  
ANISOU 7147  O   HOH B2135     6221   4864   5916     58    141    512       O  
HETATM 7148  O   HOH B2136       1.102  21.783 -35.523  1.00 30.03           O  
ANISOU 7148  O   HOH B2136     4189   4568   2654   -124     52    379       O  
HETATM 7149  O   HOH B2137       0.248  24.142 -39.856  1.00 34.04           O  
ANISOU 7149  O   HOH B2137     4068   3487   5381    666  -1300    587       O  
HETATM 7150  O   HOH B2138      14.533  25.073 -26.430  1.00 62.42           O  
ANISOU 7150  O   HOH B2138     8408   6705   8603    125    372    412       O  
HETATM 7151  O   HOH B2139      14.608  25.238 -23.282  1.00 37.78           O  
ANISOU 7151  O   HOH B2139     5636   5226   3491   -244     13    263       O  
HETATM 7152  O   HOH B2140       5.993  25.011 -26.642  1.00 45.56           O  
ANISOU 7152  O   HOH B2140     6493   5937   4879   1186     98   -173       O  
HETATM 7153  O   HOH B2141      10.183  25.095 -29.436  1.00 20.64           O  
ANISOU 7153  O   HOH B2141     2861   2645   2336    -20    -14    297       O  
HETATM 7154  O   HOH B2142      14.087  28.007 -24.443  1.00 37.65           O  
ANISOU 7154  O   HOH B2142     4984   4001   5321    321   -745    -97       O  
HETATM 7155  O   HOH B2143      15.086  28.772 -22.001  1.00 43.43           O  
ANISOU 7155  O   HOH B2143     6460   4804   5238    280    -48    446       O  
HETATM 7156  O   HOH B2144      14.629  28.435 -18.005  1.00 45.24           O  
ANISOU 7156  O   HOH B2144     6560   5764   4864   -641    403     50       O  
HETATM 7157  O   HOH B2145       1.307 -11.038 -14.523  1.00 57.75           O  
ANISOU 7157  O   HOH B2145     7386   6824   7731   -414   -198     29       O  
HETATM 7158  O   HOH B2146       8.877  29.242 -12.847  1.00 61.56           O  
ANISOU 7158  O   HOH B2146     7932   8231   7226    284     53     27       O  
HETATM 7159  O   HOH B2147       1.816  25.458 -18.207  1.00 58.04           O  
ANISOU 7159  O   HOH B2147     7311   7289   7454    110   -159    186       O  
HETATM 7160  O   HOH B2148       3.457  28.541 -16.187  1.00 49.92           O  
ANISOU 7160  O   HOH B2148     6323   6195   6448    362    456     80       O  
HETATM 7161  O   HOH B2149       3.135  29.428 -11.753  1.00 61.24           O  
ANISOU 7161  O   HOH B2149     8255   7711   7304    130    210    209       O  
HETATM 7162  O   HOH B2150      18.064  24.681 -16.966  1.00 62.83           O  
ANISOU 7162  O   HOH B2150     8515   7750   7608   -329    344   -165       O  
HETATM 7163  O   HOH B2151      21.485  21.395 -14.963  1.00 59.81           O  
ANISOU 7163  O   HOH B2151     7720   7920   7084   -203     14    -65       O  
HETATM 7164  O   HOH B2152      15.320  19.806  -2.127  1.00 41.82           O  
ANISOU 7164  O   HOH B2152     4163   7285   4441    315   -173    329       O  
HETATM 7165  O   HOH B2153      15.003  22.639  -3.527  1.00 31.05           O  
ANISOU 7165  O   HOH B2153     3801   4962   3036    -56     13    170       O  
HETATM 7166  O   HOH B2154      17.056  14.870 -10.402  1.00 38.83           O  
ANISOU 7166  O   HOH B2154     4483   4145   6123    665   -201   -148       O  
HETATM 7167  O   HOH B2155      -1.350  15.372 -18.447  1.00 40.81           O  
ANISOU 7167  O   HOH B2155     4596   6130   4780    805    533   -431       O  
HETATM 7168  O   HOH B2156      -0.621  19.029 -15.714  1.00 38.77           O  
ANISOU 7168  O   HOH B2156     4380   5935   4416    164    268   -119       O  
HETATM 7169  O   HOH B2157      17.307   3.683 -45.209  1.00 39.05           O  
ANISOU 7169  O   HOH B2157     5714   4990   4132   1280    215   -168       O  
HETATM 7170  O   HOH B2158      14.754   6.166 -48.927  1.00 40.53           O  
ANISOU 7170  O   HOH B2158     5722   7011   2666    -58    313  -1390       O  
HETATM 7171  O   HOH B2159      16.154   8.805 -48.410  1.00 32.50           O  
ANISOU 7171  O   HOH B2159     4848   4733   2769   1036    358   -258       O  
HETATM 7172  O   HOH B2160      15.360   3.844 -46.965  1.00 42.90           O  
ANISOU 7172  O   HOH B2160     5739   6234   4326    -45    499   -546       O  
HETATM 7173  O   HOH B2161      18.979   5.799 -44.243  1.00 48.36           O  
ANISOU 7173  O   HOH B2161     6324   7881   4171    161    856   -572       O  
HETATM 7174  O   HOH B2162       0.022  21.969 -20.881  1.00 79.11           O  
ANISOU 7174  O   HOH B2162    10157  10431   9469    188    142    139       O  
HETATM 7175  O   HOH B2163       2.543  22.955 -28.844  1.00 59.43           O  
ANISOU 7175  O   HOH B2163     7684   8163   6735    -71    -80    -94       O  
HETATM 7176  O   HOH B2164      -2.096  17.448 -21.234  1.00 61.79           O  
ANISOU 7176  O   HOH B2164     7352   8405   7720   -220   -161    -50       O  
HETATM 7177  O   HOH B2165       3.402   9.119 -15.633  1.00 72.11           O  
ANISOU 7177  O   HOH B2165     9113   9422   8864    -27    -87   -128       O  
HETATM 7178  O   HOH B2166       0.212   8.909 -13.153  1.00 50.67           O  
ANISOU 7178  O   HOH B2166     6091   6853   6308    615   -157    -10       O  
HETATM 7179  O   HOH B2167      24.836  15.920 -19.353  1.00 57.71           O  
ANISOU 7179  O   HOH B2167     7892   7251   6783   -105    649   -157       O  
HETATM 7180  O   HOH B2168      -7.518  12.554 -27.643  1.00 47.81           O  
ANISOU 7180  O   HOH B2168     6608   5957   5602    452    272   -193       O  
HETATM 7181  O   HOH B2169      31.277   3.803 -34.614  1.00 60.46           O  
ANISOU 7181  O   HOH B2169     7617   7912   7445    363    -74    107       O  
HETATM 7182  O   HOH B2170      -9.512  17.331 -33.497  1.00 64.06           O  
ANISOU 7182  O   HOH B2170     7817   8812   7710    193     97     11       O  
HETATM 7183  O   HOH B2171     -10.514  14.494 -30.989  1.00 74.31           O  
ANISOU 7183  O   HOH B2171     9243   9596   9397    117     42     46       O  
HETATM 7184  O   HOH B2172     -10.311  15.901 -28.791  1.00 79.79           O  
ANISOU 7184  O   HOH B2172    10282  10332   9701    134      2     48       O  
HETATM 7185  O   HOH B2173      -8.430  14.302 -35.750  1.00 48.34           O  
ANISOU 7185  O   HOH B2173     6162   6120   6083    347    197   -304       O  
HETATM 7186  O   HOH B2174      16.329  -5.320 -26.534  1.00 13.02           O  
ANISOU 7186  O   HOH B2174     1613   1608   1726    -37    183   -206       O  
HETATM 7187  O   HOH B2175      -5.007  12.533 -42.929  1.00 35.71           O  
ANISOU 7187  O   HOH B2175     4621   5211   3737    346   -641   -264       O  
HETATM 7188  O   HOH B2176      -6.481  14.219 -41.293  1.00 45.26           O  
ANISOU 7188  O   HOH B2176     5112   6418   5666    185   -402   -600       O  
HETATM 7189  O   HOH B2177      13.623 -11.180 -18.697  1.00 28.73           O  
ANISOU 7189  O   HOH B2177     3902   3260   3754    236   -461     18       O  
HETATM 7190  O   HOH B2178       8.470 -10.989 -21.031  1.00 31.56           O  
ANISOU 7190  O   HOH B2178     5244   3038   3711   -802    659     -4       O  
HETATM 7191  O   HOH B2179      -8.236  -3.549 -39.489  1.00 69.60           O  
ANISOU 7191  O   HOH B2179     8897   8962   8584     12    200    -72       O  
HETATM 7192  O   HOH B2180      -9.060   5.741 -26.975  1.00 50.91           O  
ANISOU 7192  O   HOH B2180     5778   6711   6853    -91     91    105       O  
HETATM 7193  O   HOH B2181      12.063   2.044 -28.546  1.00 12.50           O  
ANISOU 7193  O   HOH B2181     1383   1857   1510     10     62   -290       O  
HETATM 7194  O   HOH B2182       6.153  -9.727 -22.115  1.00 28.11           O  
ANISOU 7194  O   HOH B2182     3734   2898   4047   -885    695     91       O  
HETATM 7195  O   HOH B2183       4.470  -8.917 -24.239  1.00 37.10           O  
ANISOU 7195  O   HOH B2183     4548   4791   4756   -101   -156    211       O  
HETATM 7196  O   HOH B2184       5.877  -6.202 -20.408  1.00 16.52           O  
ANISOU 7196  O   HOH B2184     2052   2376   1850   -302    189   -129       O  
HETATM 7197  O   HOH B2185      11.393   8.765 -51.617  1.00 46.52           O  
ANISOU 7197  O   HOH B2185     6881   5532   5264    505    265   -294       O  
HETATM 7198  O   HOH B2186       2.564  23.126 -31.402  1.00 41.57           O  
ANISOU 7198  O   HOH B2186     4509   5259   6026    650    738    -97       O  
HETATM 7199  O   HOH B2187       6.108  26.419 -30.626  1.00 43.67           O  
ANISOU 7199  O   HOH B2187     5991   6248   4354    422     48   -190       O  
HETATM 7200  O   HOH B2188       4.981  23.113 -28.309  1.00 35.18           O  
ANISOU 7200  O   HOH B2188     4300   5501   3567   1188    261    -45       O  
HETATM 7201  O   HOH B2189      -1.227  -4.256 -16.302  1.00 38.43           O  
ANISOU 7201  O   HOH B2189     4532   5693   4375   -357    876     87       O  
HETATM 7202  O   HOH B2190      -4.022  -3.409 -19.312  1.00 40.35           O  
ANISOU 7202  O   HOH B2190     3630   5796   5905   -586    399    -73       O  
HETATM 7203  O   HOH B2191      25.795  19.936 -33.732  1.00 56.38           O  
ANISOU 7203  O   HOH B2191     7533   6932   6956    -12    281    139       O  
HETATM 7204  O   HOH B2192      27.984  18.061 -30.499  1.00 44.34           O  
ANISOU 7204  O   HOH B2192     6128   5867   4853  -1027    442    335       O  
HETATM 7205  O   HOH B2193      22.127  21.712 -28.063  1.00 29.15           O  
ANISOU 7205  O   HOH B2193     4871   3187   3019   -783    249     85       O  
HETATM 7206  O   HOH B2194       4.911  -6.094 -16.300  1.00 23.79           O  
ANISOU 7206  O   HOH B2194     3369   3323   2350   -123     12   -201       O  
HETATM 7207  O   HOH B2195      34.219  12.791 -34.659  1.00 62.89           O  
ANISOU 7207  O   HOH B2195     7714   8452   7729     10    272     12       O  
HETATM 7208  O   HOH B2196      34.917  14.070 -32.330  1.00 77.00           O  
ANISOU 7208  O   HOH B2196     9839  10264   9156    -99     81     52       O  
HETATM 7209  O   HOH B2197      30.906  16.210 -39.243  1.00 39.66           O  
ANISOU 7209  O   HOH B2197     5306   5561   4202    175    671   1344       O  
HETATM 7210  O   HOH B2198      23.884  12.078 -42.339  1.00 32.58           O  
ANISOU 7210  O   HOH B2198     5276   3306   3799    -57   -450    887       O  
HETATM 7211  O   HOH B2199      -1.303  -1.643 -23.578  1.00 24.27           O  
ANISOU 7211  O   HOH B2199     2189   4243   2790    133    -73  -1087       O  
HETATM 7212  O   HOH B2200      -3.142   5.181 -18.851  1.00 47.18           O  
ANISOU 7212  O   HOH B2200     6293   5731   5902    245    393    623       O  
HETATM 7213  O   HOH B2201      -0.428   4.859 -18.976  1.00 34.87           O  
ANISOU 7213  O   HOH B2201     5897   4097   3254   -118   -907    -81       O  
HETATM 7214  O   HOH B2202      23.356   7.400 -40.565  1.00 30.66           O  
ANISOU 7214  O   HOH B2202     3560   4402   3687     61    346    329       O  
HETATM 7215  O   HOH B2203      22.934   5.196 -42.227  1.00 45.34           O  
ANISOU 7215  O   HOH B2203     5914   6294   5019  -1054    846    -32       O  
HETATM 7216  O   HOH B2204      21.916   2.159 -44.976  1.00 53.07           O  
ANISOU 7216  O   HOH B2204     6833   6965   6365    112    487   -271       O  
HETATM 7217  O   HOH B2205      -5.505   0.820 -24.373  1.00 44.92           O  
ANISOU 7217  O   HOH B2205     5456   6581   5029    168   -212    199       O  
HETATM 7218  O   HOH B2206      -1.090   5.571 -27.869  1.00 15.68           O  
ANISOU 7218  O   HOH B2206     1716   2410   1831    -68    211   -399       O  
HETATM 7219  O   HOH B2207      -3.291  -0.027 -24.106  1.00 27.05           O  
ANISOU 7219  O   HOH B2207     2819   4025   3432    -17   -128   -449       O  
HETATM 7220  O   HOH B2208       1.616   6.224 -23.448  1.00 37.22           O  
ANISOU 7220  O   HOH B2208     4277   4871   4995     11   -113    425       O  
HETATM 7221  O   HOH B2209      -6.055   4.610 -23.387  1.00 47.89           O  
ANISOU 7221  O   HOH B2209     5644   6884   5670    174      9    626       O  
HETATM 7222  O   HOH B2210      -9.177   2.794 -31.273  1.00 47.85           O  
ANISOU 7222  O   HOH B2210     5505   7470   5206    449    167    -38       O  
HETATM 7223  O   HOH B2211      -9.012   0.086 -30.818  1.00 70.89           O  
ANISOU 7223  O   HOH B2211     8675   9656   8603   -120    100    102       O  
HETATM 7224  O   HOH B2212      -7.010   1.392 -26.609  1.00 31.70           O  
ANISOU 7224  O   HOH B2212     3232   4954   3859   -803    980   -317       O  
HETATM 7225  O   HOH B2213      30.781  12.540 -14.340  1.00 72.58           O  
ANISOU 7225  O   HOH B2213     9241   9462   8875   -117     30    187       O  
HETATM 7226  O   HOH B2214      24.452  16.349 -12.482  1.00 82.82           O  
ANISOU 7226  O   HOH B2214    10633  10880   9957     21    -98    163       O  
HETATM 7227  O   HOH B2215      14.685   8.284 -28.779  1.00 11.56           O  
ANISOU 7227  O   HOH B2215     1560   1739   1094     58    192    -30       O  
HETATM 7228  O   HOH B2216      20.045  20.533 -16.822  1.00 50.99           O  
ANISOU 7228  O   HOH B2216     5687   6290   7396    149   -224    320       O  
HETATM 7229  O   HOH B2217      20.661  12.074  -0.614  1.00 44.93           O  
ANISOU 7229  O   HOH B2217     6671   4563   5838    175   -638    923       O  
HETATM 7230  O   HOH B2218      24.973  11.532  -0.074  1.00 29.40           O  
ANISOU 7230  O   HOH B2218     3988   3815   3369    328    369    -65       O  
HETATM 7231  O   HOH B2219      29.272  11.831  -9.913  1.00 52.38           O  
ANISOU 7231  O   HOH B2219     6844   6395   6663     93    204    475       O  
HETATM 7232  O   HOH B2220      27.991  11.189   2.428  1.00 36.59           O  
ANISOU 7232  O   HOH B2220     5809   4273   3819  -1317    -72   -382       O  
HETATM 7233  O   HOH B2221      29.547  13.796  -1.282  1.00 39.08           O  
ANISOU 7233  O   HOH B2221     5648   4215   4987  -1061   -113     37       O  
HETATM 7234  O   HOH B2222      32.872  -0.355   1.524  1.00 32.81           O  
ANISOU 7234  O   HOH B2222     3580   4172   4715    401   -784    994       O  
HETATM 7235  O   HOH B2223      15.945  13.641 -45.840  1.00 29.63           O  
ANISOU 7235  O   HOH B2223     3658   4380   3220    520    416    201       O  
HETATM 7236  O   HOH B2224      12.885  19.261 -46.812  1.00 24.32           O  
ANISOU 7236  O   HOH B2224     3692   3249   2298   -190     61     46       O  
HETATM 7237  O   HOH B2225      14.505  16.167 -47.797  1.00 34.51           O  
ANISOU 7237  O   HOH B2225     5051   5563   2500    851   1546    789       O  
HETATM 7238  O   HOH B2226       7.164  18.523 -45.670  1.00 22.24           O  
ANISOU 7238  O   HOH B2226     2621   4220   1610     99    -90    440       O  
HETATM 7239  O   HOH B2227      30.516   5.038 -17.859  1.00 18.17           O  
ANISOU 7239  O   HOH B2227     2099   2853   1950    109    172    124       O  
HETATM 7240  O   HOH B2228      33.802   4.792 -14.845  1.00 21.09           O  
ANISOU 7240  O   HOH B2228     1968   3815   2231   -311   -125    -20       O  
HETATM 7241  O   HOH B2229       7.373  21.195 -44.956  1.00 40.77           O  
ANISOU 7241  O   HOH B2229     5890   5985   3618   -331   -444    315       O  
HETATM 7242  O   HOH B2230      11.533  21.117 -45.126  1.00 18.32           O  
ANISOU 7242  O   HOH B2230     2794   2790   1379    -59     84    387       O  
HETATM 7243  O   HOH B2231       8.197  24.202 -44.317  1.00 50.90           O  
ANISOU 7243  O   HOH B2231     6655   6904   5780    729    456    490       O  
HETATM 7244  O   HOH B2232      38.188   2.983 -13.388  1.00 70.33           O  
ANISOU 7244  O   HOH B2232     8816   9278   8627    -44    101     55       O  
HETATM 7245  O   HOH B2233      33.785   7.455 -15.828  1.00 23.33           O  
ANISOU 7245  O   HOH B2233     2654   3836   2374   -233    375    250       O  
HETATM 7246  O   HOH B2234      10.211  25.967 -42.252  1.00 54.85           O  
ANISOU 7246  O   HOH B2234     6948   6932   6962     38   -128    204       O  
HETATM 7247  O   HOH B2235       4.032  23.429 -42.150  1.00 34.24           O  
ANISOU 7247  O   HOH B2235     4250   5649   3113    326   -544   -166       O  
HETATM 7248  O   HOH B2236       1.773  26.241 -41.739  1.00 52.63           O  
ANISOU 7248  O   HOH B2236     6455   7384   6156    -28   -572    315       O  
HETATM 7249  O   HOH B2237       0.304  27.058 -39.671  1.00 53.83           O  
ANISOU 7249  O   HOH B2237     7050   6562   6843    383   -379    577       O  
HETATM 7250  O   HOH B2238      34.332  -3.586   3.741  1.00 48.21           O  
ANISOU 7250  O   HOH B2238     6141   5911   6265    474    142    104       O  
HETATM 7251  O   HOH B2239       9.071  28.968 -40.966  1.00 40.02           O  
ANISOU 7251  O   HOH B2239     5326   4752   5129   -842    115     57       O  
HETATM 7252  O   HOH B2240       8.981  29.904 -34.258  1.00 38.31           O  
ANISOU 7252  O   HOH B2240     6447   4274   3834    -10   -130   -672       O  
HETATM 7253  O   HOH B2241      10.216  30.955 -36.784  1.00 41.54           O  
ANISOU 7253  O   HOH B2241     5764   3898   6119    251   -371   -173       O  
HETATM 7254  O   HOH B2242      11.275  29.224 -39.148  1.00 39.05           O  
ANISOU 7254  O   HOH B2242     5312   4972   4554   -409   -468    661       O  
HETATM 7255  O   HOH B2243      17.162  28.621 -37.045  1.00 41.17           O  
ANISOU 7255  O   HOH B2243     5883   5081   4678   -123   1021    244       O  
HETATM 7256  O   HOH B2244      14.434  28.054 -31.074  1.00 30.78           O  
ANISOU 7256  O   HOH B2244     6124   2229   3342     49   -982    225       O  
HETATM 7257  O   HOH B2245      28.683 -15.665 -14.726  1.00 38.55           O  
ANISOU 7257  O   HOH B2245     4167   4497   5984   1286   -412     36       O  
HETATM 7258  O   HOH B2246      28.940 -14.705 -20.481  1.00 63.30           O  
ANISOU 7258  O   HOH B2246     8472   8356   7222     10    253   -384       O  
HETATM 7259  O   HOH B2247      24.022  -9.892 -20.067  1.00 17.79           O  
ANISOU 7259  O   HOH B2247     2488   2280   1992    396    100    -35       O  
HETATM 7260  O   HOH B2248      27.912 -12.024 -21.055  1.00 36.81           O  
ANISOU 7260  O   HOH B2248     4819   5644   3524   1274   1069   -853       O  
HETATM 7261  O   HOH B2249      19.068  22.880 -32.004  1.00 22.13           O  
ANISOU 7261  O   HOH B2249     3553   2544   2312   -339   -377    366       O  
HETATM 7262  O   HOH B2250      32.149 -13.103 -14.890  1.00 30.45           O  
ANISOU 7262  O   HOH B2250     4069   3598   3903    816  -1072    199       O  
HETATM 7263  O   HOH B2251      25.662 -11.269 -23.880  1.00 45.55           O  
ANISOU 7263  O   HOH B2251     7025   4568   5713    370    479    -76       O  
HETATM 7264  O   HOH B2252      15.131  25.537 -38.966  1.00 27.17           O  
ANISOU 7264  O   HOH B2252     4159   3209   2955   -563    311    286       O  
HETATM 7265  O   HOH B2253      24.045  26.435 -40.084  1.00 54.78           O  
ANISOU 7265  O   HOH B2253     6491   7470   6853    352    391   -224       O  
HETATM 7266  O   HOH B2254      19.665  29.366 -36.699  1.00 48.72           O  
ANISOU 7266  O   HOH B2254     5638   6186   6689    -30    350   -261       O  
HETATM 7267  O   HOH B2255      21.394  25.744 -43.465  1.00 21.81           O  
ANISOU 7267  O   HOH B2255     3058   3115   2114   -111    730    -65       O  
HETATM 7268  O   HOH B2256      18.792  24.683 -37.097  1.00 46.29           O  
ANISOU 7268  O   HOH B2256     5992   5934   5662   -378    381    139       O  
HETATM 7269  O   HOH B2257      23.570  19.817 -43.406  1.00 24.79           O  
ANISOU 7269  O   HOH B2257     3467   3416   2537    181     94    340       O  
HETATM 7270  O   HOH B2258      32.518 -13.802 -19.339  1.00 55.82           O  
ANISOU 7270  O   HOH B2258     7244   7536   6430    339      5   -385       O  
HETATM 7271  O   HOH B2259      35.193 -10.554 -12.858  1.00 56.67           O  
ANISOU 7271  O   HOH B2259     6629   8103   6801     45    -54   -108       O  
HETATM 7272  O   HOH B2260      32.039  -3.538 -25.567  1.00 62.51           O  
ANISOU 7272  O   HOH B2260     8196   8460   7096    394    -41    111       O  
HETATM 7273  O   HOH B2261      33.205  -0.447 -20.823  1.00 28.75           O  
ANISOU 7273  O   HOH B2261     2577   4529   3817    426    431   -424       O  
HETATM 7274  O   HOH B2262      36.628  -2.851 -19.222  1.00 61.90           O  
ANISOU 7274  O   HOH B2262     7896   7920   7702    209    109    142       O  
HETATM 7275  O   HOH B2263      31.182   0.835 -19.419  1.00 18.16           O  
ANISOU 7275  O   HOH B2263     1994   2535   2372    184    236    243       O  
HETATM 7276  O   HOH B2264      19.037  21.878 -44.789  1.00 17.96           O  
ANISOU 7276  O   HOH B2264     2923   2187   1712   -139    268    305       O  
HETATM 7277  O   HOH B2265      21.467  19.367 -42.345  1.00 26.31           O  
ANISOU 7277  O   HOH B2265     3399   4273   2326   -345     97    761       O  
HETATM 7278  O   HOH B2266      24.121  16.018 -41.628  1.00 39.27           O  
ANISOU 7278  O   HOH B2266     3715   4986   6220    623   -595      6       O  
HETATM 7279  O   HOH B2267      23.900  18.897 -39.202  1.00 22.04           O  
ANISOU 7279  O   HOH B2267     2831   3366   2175   -408    257    611       O  
HETATM 7280  O   HOH B2268      20.455  22.899 -37.975  1.00 28.81           O  
ANISOU 7280  O   HOH B2268     4778   3141   3027   -651   -351    186       O  
HETATM 7281  O   HOH B2269      13.167 -13.955  -2.182  1.00 46.52           O  
ANISOU 7281  O   HOH B2269     5127   6422   6128     43   -151    298       O  
HETATM 7282  O   HOH B2270      12.960 -15.565  -4.258  1.00 56.17           O  
ANISOU 7282  O   HOH B2270     6809   7487   7047     83    -26    264       O  
HETATM 7283  O   HOH B2271      23.411  16.742 -37.455  1.00 19.99           O  
ANISOU 7283  O   HOH B2271     2596   3238   1760  -1004    -76    354       O  
HETATM 7284  O   HOH B2272      26.529   9.167 -41.147  1.00 39.54           O  
ANISOU 7284  O   HOH B2272     5618   5364   4041    654    553   -969       O  
HETATM 7285  O   HOH B2273      11.307 -13.032  -0.644  1.00 65.99           O  
ANISOU 7285  O   HOH B2273     8391   8284   8399    -60     36   -192       O  
HETATM 7286  O   HOH B2274      13.415 -10.042  -4.227  1.00 28.24           O  
ANISOU 7286  O   HOH B2274     3385   4640   2706    922    284    291       O  
HETATM 7287  O   HOH B2275      17.911  -7.014   8.432  1.00 35.95           O  
ANISOU 7287  O   HOH B2275     4388   4292   4981   -129    399     24       O  
HETATM 7288  O   HOH B2276       9.847 -11.336   0.701  1.00 46.71           O  
ANISOU 7288  O   HOH B2276     5691   6497   5560    332   -372   -249       O  
HETATM 7289  O   HOH B2277      10.303  -9.938   4.663  1.00 44.64           O  
ANISOU 7289  O   HOH B2277     5107   5156   6696    269    526    301       O  
HETATM 7290  O   HOH B2278       8.514  -5.995   3.672  1.00 33.14           O  
ANISOU 7290  O   HOH B2278     4295   3865   4432    -20    337   -144       O  
HETATM 7291  O   HOH B2279       9.044  -9.582  -1.458  1.00 35.97           O  
ANISOU 7291  O   HOH B2279     4903   4114   4651    110   -700    626       O  
HETATM 7292  O   HOH B2280       9.646 -12.164   5.660  1.00 61.26           O  
ANISOU 7292  O   HOH B2280     7951   7695   7633    -29    116     94       O  
HETATM 7293  O   HOH B2281      13.817 -16.525   6.869  1.00 80.85           O  
ANISOU 7293  O   HOH B2281    10302  10524   9895     -9    150    107       O  
HETATM 7294  O   HOH B2282      23.744  -9.122  10.387  1.00 84.49           O  
ANISOU 7294  O   HOH B2282    10738  11086  10278    117    -13     64       O  
HETATM 7295  O   HOH B2283      29.644  -2.846  11.769  1.00 50.00           O  
ANISOU 7295  O   HOH B2283     6497   6087   6415    451     66   -327       O  
HETATM 7296  O   HOH B2284      23.863  -1.769  11.747  1.00 35.53           O  
ANISOU 7296  O   HOH B2284     5743   4295   3462   1118   -725   -396       O  
HETATM 7297  O   HOH B2285      13.383  12.015 -23.650  1.00 12.66           O  
ANISOU 7297  O   HOH B2285     1695   1975   1141    222    -11      9       O  
HETATM 7298  O   HOH B2286      21.147  -4.128  10.457  1.00 44.01           O  
ANISOU 7298  O   HOH B2286     6706   5670   4345   -248     59      3       O  
HETATM 7299  O   HOH B2287      24.014  -4.422  11.406  1.00 49.68           O  
ANISOU 7299  O   HOH B2287     7458   6176   5240    -17     84    422       O  
HETATM 7300  O   HOH B2288      18.624  -2.015   9.945  1.00 39.71           O  
ANISOU 7300  O   HOH B2288     6080   5495   3511    -72    263   -215       O  
HETATM 7301  O   HOH B2289      12.570  23.662 -26.531  1.00 30.88           O  
ANISOU 7301  O   HOH B2289     5319   4184   2230   -198    814    566       O  
HETATM 7302  O   HOH B2290      14.694  23.173 -24.853  1.00 50.31           O  
ANISOU 7302  O   HOH B2290     7807   6598   4709    -89     43    191       O  
HETATM 7303  O   HOH B2291      11.475  27.900 -25.039  1.00 38.42           O  
ANISOU 7303  O   HOH B2291     5863   4372   4364   -249   -121    459       O  
HETATM 7304  O   HOH B2292       8.807  25.862 -27.047  1.00 25.42           O  
ANISOU 7304  O   HOH B2292     4431   3167   2062    104   -435    284       O  
HETATM 7305  O   HOH B2293      13.605  27.472 -20.254  1.00 46.64           O  
ANISOU 7305  O   HOH B2293     6669   5113   5940    503    -35    266       O  
HETATM 7306  O   HOH B2294       1.133  -7.974 -14.178  1.00 46.55           O  
ANISOU 7306  O   HOH B2294     5936   6239   5512   -184    -87    -57       O  
HETATM 7307  O   HOH B2295       8.241  28.229 -27.993  1.00 56.00           O  
ANISOU 7307  O   HOH B2295     7453   7121   6702    248    -73    103       O  
HETATM 7308  O   HOH B2296       6.692  31.171 -20.026  1.00 56.20           O  
ANISOU 7308  O   HOH B2296     7870   6784   6697    193    273   -142       O  
HETATM 7309  O   HOH B2297       5.878  -6.092  -0.960  1.00 29.00           O  
ANISOU 7309  O   HOH B2297     3014   4836   3167   -186    442    144       O  
HETATM 7310  O   HOH B2298       3.233  -7.665  -5.113  1.00 44.32           O  
ANISOU 7310  O   HOH B2298     5907   5899   5034   -303    285   -301       O  
HETATM 7311  O   HOH B2299       6.517 -10.655  -1.789  1.00 57.28           O  
ANISOU 7311  O   HOH B2299     7334   6874   7556   -227    118    254       O  
HETATM 7312  O   HOH B2300       3.440  25.912 -16.173  1.00 30.95           O  
ANISOU 7312  O   HOH B2300     3266   4321   4174   1037    136   -930       O  
HETATM 7313  O   HOH B2301       3.472  29.245  -9.208  1.00 68.74           O  
ANISOU 7313  O   HOH B2301     8754   9225   8140     47     73    290       O  
HETATM 7314  O   HOH B2302       9.779  27.041 -11.867  1.00 28.65           O  
ANISOU 7314  O   HOH B2302     4898   3191   2796    -47    -11   -832       O  
HETATM 7315  O   HOH B2303      12.904  -1.865   9.839  1.00 43.48           O  
ANISOU 7315  O   HOH B2303     5469   5862   5188   -383    544    293       O  
HETATM 7316  O   HOH B2304       8.841  -2.793   6.826  1.00 30.86           O  
ANISOU 7316  O   HOH B2304     4249   3132   4345    128    178    415       O  
HETATM 7317  O   HOH B2305      20.614  -1.988  14.316  1.00 36.43           O  
ANISOU 7317  O   HOH B2305     6723   3222   3895     13    210    236       O  
HETATM 7318  O   HOH B2306      19.849  11.408   4.141  1.00 24.00           O  
ANISOU 7318  O   HOH B2306     3284   3235   2598   -508    -65    -12       O  
HETATM 7319  O   HOH B2307      17.277  13.218   6.832  1.00 42.34           O  
ANISOU 7319  O   HOH B2307     3962   5341   6783   -367    487  -1652       O  
HETATM 7320  O   HOH B2308      22.924  10.346   0.553  1.00 28.84           O  
ANISOU 7320  O   HOH B2308     5871   2380   2706   -636   -674    366       O  
HETATM 7321  O   HOH B2309      14.068  24.737 -19.872  1.00 19.94           O  
ANISOU 7321  O   HOH B2309     3593   1900   2083    124    355      7       O  
HETATM 7322  O   HOH B2310      16.312  25.995 -15.418  1.00 67.77           O  
ANISOU 7322  O   HOH B2310     8515   8866   8367     46    267     95       O  
HETATM 7323  O   HOH B2311      -7.298  -0.183 -18.720  1.00 58.79           O  
ANISOU 7323  O   HOH B2311     6244   8349   7744   -301     27     35       O  
HETATM 7324  O   HOH B2312      -8.315  -0.193 -14.296  1.00 70.14           O  
ANISOU 7324  O   HOH B2312     8619   9547   8482    -78     68    112       O  
HETATM 7325  O   HOH B2313      19.408  23.243 -13.888  1.00 50.89           O  
ANISOU 7325  O   HOH B2313     6158   7042   6134   -271    423     68       O  
HETATM 7326  O   HOH B2314      -4.291   6.296  -7.380  1.00 50.18           O  
ANISOU 7326  O   HOH B2314     5821   7114   6133   -290   -615     49       O  
HETATM 7327  O   HOH B2315      -4.060   6.220  -3.094  1.00 36.86           O  
ANISOU 7327  O   HOH B2315     3597   5814   4596    382    650     67       O  
HETATM 7328  O   HOH B2316      13.757  17.146  -6.998  1.00 27.99           O  
ANISOU 7328  O   HOH B2316     3761   4230   2644   -526    452    450       O  
HETATM 7329  O   HOH B2317      13.513  20.669  -3.762  1.00 26.79           O  
ANISOU 7329  O   HOH B2317     2366   5085   2727    363    256    530       O  
HETATM 7330  O   HOH B2318      14.896  15.741 -11.883  1.00 42.86           O  
ANISOU 7330  O   HOH B2318     5694   5771   4820    -87   -285   -178       O  
HETATM 7331  O   HOH B2319      18.533  17.039 -10.417  1.00 55.75           O  
ANISOU 7331  O   HOH B2319     7148   7555   6479    200    132    261       O  
HETATM 7332  O   HOH B2320      17.634  19.414  -4.015  1.00 59.95           O  
ANISOU 7332  O   HOH B2320     7592   8232   6953    190     59    -27       O  
HETATM 7333  O   HOH B2321       5.997  -4.719   3.552  1.00 37.61           O  
ANISOU 7333  O   HOH B2321     5730   3827   4733    -10    282   -171       O  
HETATM 7334  O   HOH B2322       6.888  -4.479   7.643  1.00 56.53           O  
ANISOU 7334  O   HOH B2322     6583   7469   7427    -45    102    348       O  
HETATM 7335  O   HOH B2323      10.885   0.105   9.936  1.00 40.16           O  
ANISOU 7335  O   HOH B2323     6487   5031   3743   -391    273    557       O  
HETATM 7336  O   HOH B2324      11.326  12.801 -13.570  1.00 12.56           O  
ANISOU 7336  O   HOH B2324     1796   1713   1264    399    219     23       O  
HETATM 7337  O   HOH B2325      12.410  20.113 -18.586  1.00 16.09           O  
ANISOU 7337  O   HOH B2325     2545   1906   1661    342   -280    205       O  
HETATM 7338  O   HOH B2326      13.352  13.791 -11.810  1.00 27.55           O  
ANISOU 7338  O   HOH B2326     3476   3390   3601    684    200   -380       O  
HETATM 7339  O   HOH B2327      12.633  17.631 -20.196  1.00 13.06           O  
ANISOU 7339  O   HOH B2327     1931   1933   1099    219    122     72       O  
HETATM 7340  O   HOH B2328      18.321  -4.464   9.947  1.00 51.49           O  
ANISOU 7340  O   HOH B2328     6837   6753   5975     53    540    364       O  
HETATM 7341  O   HOH B2329      15.513  13.896  -8.699  1.00 34.74           O  
ANISOU 7341  O   HOH B2329     4490   3351   5360   -178    340      9       O  
HETATM 7342  O   HOH B2330       0.552  17.382 -17.867  1.00 33.41           O  
ANISOU 7342  O   HOH B2330     3527   6012   3157    882   -157     35       O  
HETATM 7343  O   HOH B2331       0.707  21.712 -26.746  1.00 42.99           O  
ANISOU 7343  O   HOH B2331     6290   5373   4670    781   -144     93       O  
HETATM 7344  O   HOH B2332       3.316  26.817 -22.963  1.00 45.97           O  
ANISOU 7344  O   HOH B2332     6083   5282   6102    653   -477     20       O  
HETATM 7345  O   HOH B2333       2.859  26.102 -20.480  1.00 63.83           O  
ANISOU 7345  O   HOH B2333     7843   8752   7658    500   -176    110       O  
HETATM 7346  O   HOH B2334       0.721  15.758 -24.868  1.00 32.61           O  
ANISOU 7346  O   HOH B2334     3973   3601   4814    367   -864    239       O  
HETATM 7347  O   HOH B2335       1.775  23.711 -19.991  1.00 44.57           O  
ANISOU 7347  O   HOH B2335     5378   6612   4945    448   -723   -185       O  
HETATM 7348  O   HOH B2336       0.354  17.252 -21.706  1.00 25.81           O  
ANISOU 7348  O   HOH B2336     3010   3865   2933    886   -207   -223       O  
HETATM 7349  O   HOH B2337      -0.080  13.537 -20.033  1.00 26.05           O  
ANISOU 7349  O   HOH B2337     2388   4444   3066    224    524   -325       O  
HETATM 7350  O   HOH B2338      18.174  23.814 -27.427  1.00 48.55           O  
ANISOU 7350  O   HOH B2338     7289   5200   5958    159    412     15       O  
HETATM 7351  O   HOH B2339      17.528  27.216 -21.516  1.00 46.29           O  
ANISOU 7351  O   HOH B2339     6301   5200   6086    129    304     50       O  
HETATM 7352  O   HOH B2340       1.463   7.787 -25.749  1.00 18.31           O  
ANISOU 7352  O   HOH B2340     1682   3405   1868    148    404   -175       O  
HETATM 7353  O   HOH B2341       1.737  10.584 -28.433  1.00 14.70           O  
ANISOU 7353  O   HOH B2341     1490   2618   1476    183   -129   -271       O  
HETATM 7354  O   HOH B2342      -1.205  14.459 -23.791  1.00 29.11           O  
ANISOU 7354  O   HOH B2342     2783   3790   4487    401   -244  -1088       O  
HETATM 7355  O   HOH B2343       5.485  12.773 -24.264  1.00 15.41           O  
ANISOU 7355  O   HOH B2343     1867   2652   1335    523    127    -13       O  
HETATM 7356  O   HOH B2344      22.692  17.674 -16.245  1.00 54.97           O  
ANISOU 7356  O   HOH B2344     7344   6741   6802   -242   -356   -101       O  
HETATM 7357  O   HOH B2345       1.639   6.492 -20.484  1.00 45.70           O  
ANISOU 7357  O   HOH B2345     6563   5375   5427    241    371    317       O  
HETATM 7358  O   HOH B2346       1.366   6.271 -17.728  1.00 39.47           O  
ANISOU 7358  O   HOH B2346     4362   5825   4809     61     33    592       O  
HETATM 7359  O   HOH B2347      -2.770   6.896 -17.148  1.00 65.98           O  
ANISOU 7359  O   HOH B2347     8561   8772   7736    119     54    441       O  
HETATM 7360  O   HOH B2348       0.663   7.226 -15.439  1.00 67.46           O  
ANISOU 7360  O   HOH B2348     8280   9068   8285    -41    -85    286       O  
HETATM 7361  O   HOH B2349      34.796  14.878 -29.821  1.00 49.08           O  
ANISOU 7361  O   HOH B2349     6160   6540   5948     54    908     30       O  
HETATM 7362  O   HOH B2350      26.276  13.753 -17.219  1.00 56.76           O  
ANISOU 7362  O   HOH B2350     7453   7306   6805   -126   -299    319       O  
HETATM 7363  O   HOH B2351      -2.554  14.157 -21.411  1.00 61.16           O  
ANISOU 7363  O   HOH B2351     8174   8209   6856     26    143    -92       O  
HETATM 7364  O   HOH B2352      -4.438   5.863 -22.097  1.00 37.94           O  
ANISOU 7364  O   HOH B2352     4839   5615   3961    301   1122   -232       O  
HETATM 7365  O   HOH B2353      33.679   4.645 -27.989  1.00 51.72           O  
ANISOU 7365  O   HOH B2353     6308   6617   6728    192    335   -165       O  
HETATM 7366  O   HOH B2354      -4.576  19.689 -28.098  1.00 42.70           O  
ANISOU 7366  O   HOH B2354     5817   6227   4179    773    684   -224       O  
HETATM 7367  O   HOH B2355      -6.810   9.840 -27.588  1.00 27.58           O  
ANISOU 7367  O   HOH B2355     1878   4737   3862    168    226   -508       O  
HETATM 7368  O   HOH B2356      33.348   1.461 -26.257  1.00 45.47           O  
ANISOU 7368  O   HOH B2356     4610   6741   5926    555    136   -555       O  
HETATM 7369  O   HOH B2357      31.472   4.099 -32.112  1.00 61.36           O  
ANISOU 7369  O   HOH B2357     7453   8582   7279    161    160    -72       O  
HETATM 7370  O   HOH B2358      32.867  -1.120 -25.178  1.00 42.30           O  
ANISOU 7370  O   HOH B2358     3905   7222   4944    354    717    131       O  
HETATM 7371  O   HOH B2359      28.247  -7.216 -32.689  1.00 51.85           O  
ANISOU 7371  O   HOH B2359     6077   7287   6337    -77    265   -498       O  
HETATM 7372  O   HOH B2360      23.659 -13.158 -32.950  1.00 76.96           O  
ANISOU 7372  O   HOH B2360     9832   9754   9657    118    110     12       O  
HETATM 7373  O   HOH B2361      27.126 -11.192 -32.501  1.00 50.75           O  
ANISOU 7373  O   HOH B2361     6046   7309   5928    496    371      1       O  
HETATM 7374  O   HOH B2362      -1.127  12.961 -27.129  1.00 36.13           O  
ANISOU 7374  O   HOH B2362     4253   5467   4006    363   -244   -414       O  
HETATM 7375  O   HOH B2363       1.927  14.609 -27.626  1.00 24.28           O  
ANISOU 7375  O   HOH B2363     2928   3086   3210    416   -497   -431       O  
HETATM 7376  O   HOH B2364      21.799 -12.175 -34.496  1.00 49.99           O  
ANISOU 7376  O   HOH B2364     6413   6696   5887    634    118    162       O  
HETATM 7377  O   HOH B2365      19.953 -10.930 -38.800  1.00 28.20           O  
ANISOU 7377  O   HOH B2365     4904   3498   2313     51    313   -739       O  
HETATM 7378  O   HOH B2366      22.161  -7.162 -40.175  1.00 42.33           O  
ANISOU 7378  O   HOH B2366     5565   5470   5048     61   -107    -55       O  
HETATM 7379  O   HOH B2367       0.170  18.954 -24.098  1.00 25.18           O  
ANISOU 7379  O   HOH B2367     3006   4000   2562   1088    -31    -85       O  
HETATM 7380  O   HOH B2368      -7.662  18.436 -32.111  1.00 56.78           O  
ANISOU 7380  O   HOH B2368     6717   7769   7086    240    -95      1       O  
HETATM 7381  O   HOH B2369      -1.783  22.075 -35.822  1.00 41.29           O  
ANISOU 7381  O   HOH B2369     6311   5237   4141   -109   -102    223       O  
HETATM 7382  O   HOH B2370      -6.157  20.804 -33.323  1.00 53.16           O  
ANISOU 7382  O   HOH B2370     6399   6639   7160    740     81    299       O  
HETATM 7383  O   HOH B2371      20.665 -12.875 -37.104  1.00 44.35           O  
ANISOU 7383  O   HOH B2371     6445   5817   4589    481    367    276       O  
HETATM 7384  O   HOH B2372       6.961 -17.170 -28.276  1.00 49.71           O  
ANISOU 7384  O   HOH B2372     6856   5301   6732   -570    289      9       O  
HETATM 7385  O   HOH B2373       6.179 -14.300 -24.519  1.00 65.50           O  
ANISOU 7385  O   HOH B2373     8181   8583   8122    -90    254     20       O  
HETATM 7386  O   HOH B2374       5.791 -13.420 -34.175  1.00 45.37           O  
ANISOU 7386  O   HOH B2374     5024   5991   6225   -472    325    -13       O  
HETATM 7387  O   HOH B2375      12.155 -17.280 -28.179  1.00 44.06           O  
ANISOU 7387  O   HOH B2375     6079   5939   4721   -123    -56    297       O  
HETATM 7388  O   HOH B2376       9.853 -16.323 -23.731  1.00 61.99           O  
ANISOU 7388  O   HOH B2376     8286   8190   7077   -259    134    206       O  
HETATM 7389  O   HOH B2377      11.360 -17.211 -34.512  1.00 43.37           O  
ANISOU 7389  O   HOH B2377     6065   5806   4610   -101    401   -468       O  
HETATM 7390  O   HOH B2378      10.438 -17.854 -30.030  1.00 60.52           O  
ANISOU 7390  O   HOH B2378     7613   7890   7492   -186     97     53       O  
HETATM 7391  O   HOH B2379      -7.675  14.520 -29.488  1.00 35.92           O  
ANISOU 7391  O   HOH B2379     3854   5567   4229    342    780     -5       O  
HETATM 7392  O   HOH B2380      -8.495  14.970 -33.139  1.00 55.20           O  
ANISOU 7392  O   HOH B2380     6689   8014   6271   -166   -321    -37       O  
HETATM 7393  O   HOH B2381      -4.886  14.574 -38.970  1.00 32.58           O  
ANISOU 7393  O   HOH B2381     3567   5631   3181   1075   -358   -406       O  
HETATM 7394  O   HOH B2382      -6.015  12.622 -36.829  1.00 36.49           O  
ANISOU 7394  O   HOH B2382     3071   5618   5178   -347  -1572   -210       O  
HETATM 7395  O   HOH B2383      -3.079  11.844 -41.015  1.00 24.14           O  
ANISOU 7395  O   HOH B2383     2595   3544   3035    185   -253   -474       O  
HETATM 7396  O   HOH B2384      -2.386  14.604 -40.419  1.00 21.69           O  
ANISOU 7396  O   HOH B2384     2388   3503   2349    501   -271   -241       O  
HETATM 7397  O   HOH B2385      20.790  -5.417 -42.312  1.00 40.21           O  
ANISOU 7397  O   HOH B2385     4578   5530   5170    149    432    -96       O  
HETATM 7398  O   HOH B2386      -4.395  10.196 -38.999  1.00 24.22           O  
ANISOU 7398  O   HOH B2386     2361   3753   3090    298   -535   -253       O  
HETATM 7399  O   HOH B2387      -1.693   9.954 -42.629  1.00 20.83           O  
ANISOU 7399  O   HOH B2387     2127   3298   2489    180   -424   -375       O  
HETATM 7400  O   HOH B2388      -4.436   8.552 -45.277  1.00 79.28           O  
ANISOU 7400  O   HOH B2388    10082  10528   9512    -43    -17     92       O  
HETATM 7401  O   HOH B2389      -5.712  10.459 -44.317  1.00 57.40           O  
ANISOU 7401  O   HOH B2389     7095   7631   7084    -78   -353     13       O  
HETATM 7402  O   HOH B2390      -5.347  -8.032 -39.647  1.00 58.39           O  
ANISOU 7402  O   HOH B2390     6900   7972   7313   -433     50    348       O  
HETATM 7403  O   HOH B2391      -3.656  -8.830 -41.919  1.00 59.93           O  
ANISOU 7403  O   HOH B2391     7989   7427   7356    -27    -79   -152       O  
HETATM 7404  O   HOH B2392      -0.958  -7.558 -43.211  1.00 93.14           O  
ANISOU 7404  O   HOH B2392    11984  12213  11191     89     67     29       O  
HETATM 7405  O   HOH B2393      -6.862  -5.506 -38.434  1.00 44.68           O  
ANISOU 7405  O   HOH B2393     5226   6300   5451  -1059    431   -246       O  
HETATM 7406  O   HOH B2394      -8.119  -5.054 -43.833  1.00 60.54           O  
ANISOU 7406  O   HOH B2394     7359   7589   8055   -615   -125    101       O  
HETATM 7407  O   HOH B2395     -11.567   4.996 -40.606  1.00 75.86           O  
ANISOU 7407  O   HOH B2395     9678   9977   9168    143    106     28       O  
HETATM 7408  O   HOH B2396      -8.547   7.631 -41.649  1.00 55.65           O  
ANISOU 7408  O   HOH B2396     6400   7878   6865     15   -200     52       O  
HETATM 7409  O   HOH B2397      -8.374   3.547 -35.715  1.00 36.27           O  
ANISOU 7409  O   HOH B2397     3089   6125   4567   -568    -38    223       O  
HETATM 7410  O   HOH B2398      -8.146   7.828 -28.993  1.00 45.75           O  
ANISOU 7410  O   HOH B2398     4801   6581   6002    409    -74   -242       O  
HETATM 7411  O   HOH B2399      12.795 -14.085  -6.506  1.00 46.83           O  
ANISOU 7411  O   HOH B2399     6288   6022   5485     14    434    102       O  
HETATM 7412  O   HOH B2400       4.409  14.017 -26.545  1.00 19.71           O  
ANISOU 7412  O   HOH B2400     2257   3098   2134    386    -73    144       O  
HETATM 7413  O   HOH B2401       5.697  14.767 -30.790  1.00 16.88           O  
ANISOU 7413  O   HOH B2401     2615   2251   1546    480    540    269       O  
HETATM 7414  O   HOH B2402       3.768  13.110 -31.724  1.00 31.06           O  
ANISOU 7414  O   HOH B2402     4076   4728   2998    136   -233   -177       O  
HETATM 7415  O   HOH B2403      10.304   3.915 -47.577  1.00 30.43           O  
ANISOU 7415  O   HOH B2403     4379   4098   3087    122    355    310       O  
HETATM 7416  O   HOH B2404      13.919  10.737 -47.045  1.00 28.64           O  
ANISOU 7416  O   HOH B2404     4283   3690   2908   -554    741    457       O  
HETATM 7417  O   HOH B2405      10.295   7.810 -49.193  1.00 36.88           O  
ANISOU 7417  O   HOH B2405     4232   6844   2938    286    127   -146       O  
HETATM 7418  O   HOH B2406       5.333  10.874 -33.205  1.00 15.71           O  
ANISOU 7418  O   HOH B2406     1741   2878   1352   -125    -98    299       O  
HETATM 7419  O   HOH B2407       1.045  19.181 -33.090  1.00 18.81           O  
ANISOU 7419  O   HOH B2407     2630   2959   1558    556    -97   -151       O  
HETATM 7420  O   HOH B2408       4.576  21.479 -32.250  1.00 18.47           O  
ANISOU 7420  O   HOH B2408     2895   2483   1640    452   -347     15       O  
HETATM 7421  O   HOH B2409      10.712  27.341 -33.464  1.00 19.92           O  
ANISOU 7421  O   HOH B2409     2663   2637   2268   -453    250   -113       O  
HETATM 7422  O   HOH B2410       8.101  24.617 -31.308  1.00 19.78           O  
ANISOU 7422  O   HOH B2410     2849   2761   1905    116    -66    170       O  
HETATM 7423  O   HOH B2411       6.723  22.077 -30.546  1.00 17.45           O  
ANISOU 7423  O   HOH B2411     2528   2742   1360    300   -228     99       O  
HETATM 7424  O   HOH B2412       5.211  16.209 -28.226  1.00 18.32           O  
ANISOU 7424  O   HOH B2412     2675   2555   1732    593    408    451       O  
HETATM 7425  O   HOH B2413       7.513  13.579 -26.604  1.00 13.42           O  
ANISOU 7425  O   HOH B2413     1736   1941   1421     66    159     91       O  
HETATM 7426  O   HOH B2414      22.447  20.530 -30.631  1.00 24.36           O  
ANISOU 7426  O   HOH B2414     4151   2887   2218   -380   -221    393       O  
HETATM 7427  O   HOH B2415      23.883  25.232 -37.313  1.00 53.63           O  
ANISOU 7427  O   HOH B2415     6911   7071   6395    126    612    691       O  
HETATM 7428  O   HOH B2416      18.387  20.598 -30.435  1.00 20.46           O  
ANISOU 7428  O   HOH B2416     2849   2188   2738   -346    695   -192       O  
HETATM 7429  O   HOH B2417      24.718  22.005 -38.575  1.00 40.42           O  
ANISOU 7429  O   HOH B2417     5623   5739   3995    -40   1050    388       O  
HETATM 7430  O   HOH B2418      24.161  23.019 -34.170  1.00 36.12           O  
ANISOU 7430  O   HOH B2418     5192   4959   3574  -1416    202     61       O  
HETATM 7431  O   HOH B2419      24.689  19.206 -31.515  1.00 43.09           O  
ANISOU 7431  O   HOH B2419     5468   5110   5793   -176    492    359       O  
HETATM 7432  O   HOH B2420      31.128  16.664 -36.216  1.00 41.25           O  
ANISOU 7432  O   HOH B2420     4796   5413   5463   -942    888    209       O  
HETATM 7433  O   HOH B2421      32.738  14.892 -33.377  1.00 43.03           O  
ANISOU 7433  O   HOH B2421     3959   6436   5953   -174    704    113       O  
HETATM 7434  O   HOH B2422      30.469  16.294 -30.396  1.00 32.31           O  
ANISOU 7434  O   HOH B2422     4274   4751   3250    117     48   -326       O  
HETATM 7435  O   HOH B2423      25.743  13.770 -41.252  1.00 29.03           O  
ANISOU 7435  O   HOH B2423     4397   3514   3120    166   -154    200       O  
HETATM 7436  O   HOH B2424      30.053  14.176 -40.287  1.00 48.05           O  
ANISOU 7436  O   HOH B2424     5874   7138   5245     97    340    291       O  
HETATM 7437  O   HOH B2425      29.045  11.096 -40.515  1.00 49.40           O  
ANISOU 7437  O   HOH B2425     7099   6107   5565    478    450   -312       O  
HETATM 7438  O   HOH B2426      27.344  18.738 -36.081  1.00 31.24           O  
ANISOU 7438  O   HOH B2426     5124   3689   3056   -824    382   -435       O  
HETATM 7439  O   HOH B2427      25.169   6.794 -38.561  1.00 24.13           O  
ANISOU 7439  O   HOH B2427     3014   4445   1709    -22    706     63       O  
HETATM 7440  O   HOH B2428      28.280  -0.342 -36.099  1.00 51.15           O  
ANISOU 7440  O   HOH B2428     6309   6612   6513    -45      1   -134       O  
HETATM 7441  O   HOH B2429      21.923   2.752 -42.060  1.00 43.03           O  
ANISOU 7441  O   HOH B2429     4742   5983   5624    -14   1250  -1102       O  
HETATM 7442  O   HOH B2430      27.029   4.719 -38.519  1.00 40.73           O  
ANISOU 7442  O   HOH B2430     5760   5681   4036    -63   1178     -1       O  
HETATM 7443  O   HOH B2431      24.471  -1.106 -33.304  1.00 33.90           O  
ANISOU 7443  O   HOH B2431     6083   3800   2999    975    726    -21       O  
HETATM 7444  O   HOH B2432      26.669  -2.213 -32.861  1.00 47.92           O  
ANISOU 7444  O   HOH B2432     6150   7207   4850    266    195   -524       O  
HETATM 7445  O   HOH B2433      30.472  -1.626 -34.079  1.00 53.11           O  
ANISOU 7445  O   HOH B2433     6797   6849   6535    445    775   -623       O  
HETATM 7446  O   HOH B2434      28.612  -3.226 -31.032  1.00 56.48           O  
ANISOU 7446  O   HOH B2434     7034   7685   6742     93    113   -156       O  
HETATM 7447  O   HOH B2435      13.914  10.270 -25.875  1.00 11.43           O  
ANISOU 7447  O   HOH B2435     1552   1701   1089    190    136     60       O  
HETATM 7448  O   HOH B2436      29.606  11.710 -16.601  1.00 49.72           O  
ANISOU 7448  O   HOH B2436     6096   6669   6126    -89   -319    -59       O  
HETATM 7449  O   HOH B2437      29.797  11.396 -18.987  1.00 41.05           O  
ANISOU 7449  O   HOH B2437     5302   5298   4999   -317    383    -24       O  
HETATM 7450  O   HOH B2438      24.668  15.464  -9.983  1.00 55.54           O  
ANISOU 7450  O   HOH B2438     7261   7259   6583   -575     -3   -140       O  
HETATM 7451  O   HOH B2439      26.142  13.799  -8.706  1.00 52.61           O  
ANISOU 7451  O   HOH B2439     6995   6673   6323   -463   -191     69       O  
HETATM 7452  O   HOH B2440      17.906  19.561 -14.085  1.00 30.72           O  
ANISOU 7452  O   HOH B2440     4928   4113   2631    887   -328   -191       O  
HETATM 7453  O   HOH B2441      21.049  18.090 -10.763  1.00 58.15           O  
ANISOU 7453  O   HOH B2441     7870   7298   6926    -50   -152    249       O  
HETATM 7454  O   HOH B2442      20.045  11.741  -3.158  1.00 31.01           O  
ANISOU 7454  O   HOH B2442     4339   4208   3236    808   1334    758       O  
HETATM 7455  O   HOH B2443      27.200  13.325  -5.051  1.00 49.19           O  
ANISOU 7455  O   HOH B2443     6280   6385   6024     52   -745    234       O  
HETATM 7456  O   HOH B2444      24.277  12.422  -2.491  1.00 31.41           O  
ANISOU 7456  O   HOH B2444     4486   4821   2626   1519   -804  -1125       O  
HETATM 7457  O   HOH B2445      26.978  11.462  -8.659  1.00 35.30           O  
ANISOU 7457  O   HOH B2445     4832   5317   3261     73   -879    441       O  
HETATM 7458  O   HOH B2446      26.779   9.422   0.764  1.00 21.36           O  
ANISOU 7458  O   HOH B2446     3581   2311   2224   -530    273   -193       O  
HETATM 7459  O   HOH B2447      33.658  12.607  -2.159  1.00 44.78           O  
ANISOU 7459  O   HOH B2447     5369   4534   7111   -560   -185      9       O  
HETATM 7460  O   HOH B2448      36.739   5.476  -2.578  1.00 71.44           O  
ANISOU 7460  O   HOH B2448     8789   9943   8412    180    169     34       O  
HETATM 7461  O   HOH B2449      35.798   4.072  -4.551  1.00 47.92           O  
ANISOU 7461  O   HOH B2449     5269   6330   6609     97   -308    454       O  
HETATM 7462  O   HOH B2450      31.237  12.007  -3.473  1.00 29.74           O  
ANISOU 7462  O   HOH B2450     3302   2382   5615   -340     93    129       O  
HETATM 7463  O   HOH B2451      32.076  10.431  -0.279  1.00 38.05           O  
ANISOU 7463  O   HOH B2451     5369   4630   4459     12   -601  -1195       O  
HETATM 7464  O   HOH B2452      34.496   3.379   1.168  1.00 33.06           O  
ANISOU 7464  O   HOH B2452     3354   4978   4231   -368  -1326    487       O  
HETATM 7465  O   HOH B2453      30.975   1.549   0.940  1.00 20.30           O  
ANISOU 7465  O   HOH B2453     2460   2736   2517   -106   -699    572       O  
HETATM 7466  O   HOH B2454      28.466  -1.318   2.675  1.00 25.24           O  
ANISOU 7466  O   HOH B2454     2957   3995   2637    226   -404    852       O  
HETATM 7467  O   HOH B2455      31.433   3.647 -15.695  1.00 14.56           O  
ANISOU 7467  O   HOH B2455     1660   2177   1697     38    165     86       O  
HETATM 7468  O   HOH B2456      34.069   3.584  -8.850  1.00 25.17           O  
ANISOU 7468  O   HOH B2456     2949   3966   2649    182    186    218       O  
HETATM 7469  O   HOH B2457      36.072   5.635 -12.005  1.00 73.74           O  
ANISOU 7469  O   HOH B2457     9295   9901   8821    234     68     99       O  
HETATM 7470  O   HOH B2458      35.369  -3.721 -10.299  1.00 69.90           O  
ANISOU 7470  O   HOH B2458     8976   9264   8319    -25    316     75       O  
HETATM 7471  O   HOH B2459      36.085   2.295  -9.528  1.00 60.28           O  
ANISOU 7471  O   HOH B2459     7279   7887   7736     46     36    115       O  
HETATM 7472  O   HOH B2460      35.696   2.900 -15.896  1.00 43.70           O  
ANISOU 7472  O   HOH B2460     4181   6288   6133    511    -75     75       O  
HETATM 7473  O   HOH B2461      34.236  -2.170 -14.995  1.00 45.07           O  
ANISOU 7473  O   HOH B2461     4657   6033   6435    366    499   -280       O  
HETATM 7474  O   HOH B2462      34.320   0.330 -16.640  1.00 28.40           O  
ANISOU 7474  O   HOH B2462     2840   4502   3449    714   -202   -321       O  
HETATM 7475  O   HOH B2463      38.351   0.175 -13.718  1.00 51.45           O  
ANISOU 7475  O   HOH B2463     4839   7232   7479    297     90     -4       O  
HETATM 7476  O   HOH B2464      34.856  -2.705 -12.614  1.00 42.55           O  
ANISOU 7476  O   HOH B2464     4439   5945   5783    445     -7    103       O  
HETATM 7477  O   HOH B2465      30.079  10.982 -12.412  1.00 50.85           O  
ANISOU 7477  O   HOH B2465     6417   6398   6505     82    292    227       O  
HETATM 7478  O   HOH B2466      34.743  10.019  -9.291  1.00 70.24           O  
ANISOU 7478  O   HOH B2466     9040   9167   8481   -278    283    118       O  
HETATM 7479  O   HOH B2467      33.961   9.345 -13.786  1.00 29.46           O  
ANISOU 7479  O   HOH B2467     3863   4674   2655  -1065    380    124       O  
HETATM 7480  O   HOH B2468      30.428  11.035  -6.806  1.00 26.74           O  
ANISOU 7480  O   HOH B2468     3604   3374   3181   -333   -474     38       O  
HETATM 7481  O   HOH B2469      33.362  -0.118  -7.755  1.00 56.65           O  
ANISOU 7481  O   HOH B2469     7604   6756   7164    407    -32     -6       O  
HETATM 7482  O   HOH B2470      35.566  -0.892  -6.342  1.00 51.11           O  
ANISOU 7482  O   HOH B2470     6370   6298   6750    325    731    319       O  
HETATM 7483  O   HOH B2471      32.196  -2.711   2.614  1.00 25.37           O  
ANISOU 7483  O   HOH B2471     3497   3605   2538    415   -200    190       O  
HETATM 7484  O   HOH B2472      19.121 -17.767 -13.046  1.00 23.02           O  
ANISOU 7484  O   HOH B2472     3127   2101   3517    -23    142    121       O  
HETATM 7485  O   HOH B2473      14.982 -17.127 -13.443  1.00 51.09           O  
ANISOU 7485  O   HOH B2473     6447   6598   6367    -63   -172   -569       O  
HETATM 7486  O   HOH B2474      19.125 -18.173 -16.795  1.00 49.36           O  
ANISOU 7486  O   HOH B2474     6327   5172   7256    352     13    -85       O  
HETATM 7487  O   HOH B2475      25.714 -18.078 -18.046  1.00 66.04           O  
ANISOU 7487  O   HOH B2475     8317   8211   8566    350     84   -256       O  
HETATM 7488  O   HOH B2476      21.189 -20.212 -16.346  1.00 66.59           O  
ANISOU 7488  O   HOH B2476     8713   8487   8100     30     -8    -22       O  
HETATM 7489  O   HOH B2477      26.645 -14.575 -16.198  1.00 21.76           O  
ANISOU 7489  O   HOH B2477     2809   2214   3243    796    -60   -551       O  
HETATM 7490  O   HOH B2478      21.586 -20.056 -20.651  1.00 78.75           O  
ANISOU 7490  O   HOH B2478    10160  10121   9640    -36    -74    -61       O  
HETATM 7491  O   HOH B2479      24.205 -14.602 -21.608  1.00 65.68           O  
ANISOU 7491  O   HOH B2479     8776   8244   7936    249     93     52       O  
HETATM 7492  O   HOH B2480      26.108 -11.425 -19.017  1.00 17.08           O  
ANISOU 7492  O   HOH B2480     2629   2021   1840    578    -19   -232       O  
HETATM 7493  O   HOH B2481      19.165 -15.921 -20.215  1.00 31.77           O  
ANISOU 7493  O   HOH B2481     5013   3912   3145    686    -75   -366       O  
HETATM 7494  O   HOH B2482      26.877 -15.618 -18.751  1.00 35.97           O  
ANISOU 7494  O   HOH B2482     5094   4264   4309    -42    433  -1099       O  
HETATM 7495  O   HOH B2483      21.768 -10.912 -21.573  1.00 34.05           O  
ANISOU 7495  O   HOH B2483     4452   3835   4652    119    -85     47       O  
HETATM 7496  O   HOH B2484      23.535  -8.073 -17.962  1.00 15.28           O  
ANISOU 7496  O   HOH B2484     2041   1986   1780    316     11    -52       O  
HETATM 7497  O   HOH B2485      32.551 -10.666 -16.253  1.00 22.61           O  
ANISOU 7497  O   HOH B2485     2184   3196   3210    915    -11   -428       O  
HETATM 7498  O   HOH B2486      29.834 -13.624 -13.596  1.00 30.97           O  
ANISOU 7498  O   HOH B2486     4614   3569   3586   1147   -453    299       O  
HETATM 7499  O   HOH B2487      25.420  -9.048 -22.368  1.00 22.58           O  
ANISOU 7499  O   HOH B2487     3413   3010   2158    374    183   -137       O  
HETATM 7500  O   HOH B2488      28.558  -9.117 -24.650  1.00 45.20           O  
ANISOU 7500  O   HOH B2488     5834   6468   4873    452   1364   -678       O  
HETATM 7501  O   HOH B2489      35.143  -6.771 -13.634  1.00 57.92           O  
ANISOU 7501  O   HOH B2489     6624   7958   7424    183    -95   -213       O  
HETATM 7502  O   HOH B2490      35.761  -4.683 -17.551  1.00 57.92           O  
ANISOU 7502  O   HOH B2490     6910   7855   7243     94    301     30       O  
HETATM 7503  O   HOH B2491      31.758  -8.239 -23.840  1.00 48.79           O  
ANISOU 7503  O   HOH B2491     6776   6179   5583    532     59   -225       O  
HETATM 7504  O   HOH B2492      33.189  -3.135 -20.919  1.00 49.48           O  
ANISOU 7504  O   HOH B2492     5643   6523   6633    138   -765    162       O  
HETATM 7505  O   HOH B2493      29.935 -10.314 -20.902  1.00 50.46           O  
ANISOU 7505  O   HOH B2493     6435   6374   6364    880    885    712       O  
HETATM 7506  O   HOH B2494      30.949  -5.609 -24.547  1.00 39.58           O  
ANISOU 7506  O   HOH B2494     4843   5383   4814   1375    642    161       O  
HETATM 7507  O   HOH B2495      34.496  -8.752 -15.533  1.00 35.94           O  
ANISOU 7507  O   HOH B2495     3723   4730   5202    385      4    154       O  
HETATM 7508  O   HOH B2496      33.088 -11.393 -18.813  1.00 36.51           O  
ANISOU 7508  O   HOH B2496     5187   4772   3912    583   1255   -890       O  
HETATM 7509  O   HOH B2497      31.593   1.032 -16.706  1.00 16.98           O  
ANISOU 7509  O   HOH B2497     2058   2578   1815    156     97    104       O  
HETATM 7510  O   HOH B2498      33.473  -1.101  -9.997  1.00 29.08           O  
ANISOU 7510  O   HOH B2498     3140   4583   3327   -864    325   -583       O  
HETATM 7511  O   HOH B2499      33.494  -7.857 -10.489  1.00 40.18           O  
ANISOU 7511  O   HOH B2499     4516   6303   4450    618   -204   -466       O  
HETATM 7512  O   HOH B2500      33.668  -5.439 -11.920  1.00 40.38           O  
ANISOU 7512  O   HOH B2500     4647   6584   4111    206    134   -183       O  
HETATM 7513  O   HOH B2501      32.437 -10.984  -6.360  1.00 35.81           O  
ANISOU 7513  O   HOH B2501     3416   3724   6465   1882   -412   -195       O  
HETATM 7514  O   HOH B2502      31.516 -11.887  -3.909  1.00 31.53           O  
ANISOU 7514  O   HOH B2502     2696   2278   7004    911   -143    643       O  
HETATM 7515  O   HOH B2503      28.113 -12.213  -2.708  1.00 29.41           O  
ANISOU 7515  O   HOH B2503     4395   3465   3312   1488   -631   -673       O  
HETATM 7516  O   HOH B2504      19.713 -19.733 -11.419  1.00 41.92           O  
ANISOU 7516  O   HOH B2504     6106   4488   5333    737     89    632       O  
HETATM 7517  O   HOH B2505      15.788 -14.073  -1.476  1.00 21.90           O  
ANISOU 7517  O   HOH B2505     3097   2560   2664    755    103    342       O  
HETATM 7518  O   HOH B2506      12.546 -17.404 -12.761  1.00 54.74           O  
ANISOU 7518  O   HOH B2506     7244   6310   7246   -369   -274    -88       O  
HETATM 7519  O   HOH B2507      22.298 -18.055  -9.415  1.00 33.11           O  
ANISOU 7519  O   HOH B2507     4654   4125   3800    710    631   -122       O  
HETATM 7520  O   HOH B2508      19.465 -22.691  -6.218  1.00 62.96           O  
ANISOU 7520  O   HOH B2508     8215   8528   7177     -8    -50    200       O  
HETATM 7521  O   HOH B2509      23.403 -15.617  -5.814  1.00 21.22           O  
ANISOU 7521  O   HOH B2509     2357   2111   3593    701    418    990       O  
HETATM 7522  O   HOH B2510      14.250 -17.746  -2.491  1.00 41.76           O  
ANISOU 7522  O   HOH B2510     4795   5773   5298     60   -714    616       O  
HETATM 7523  O   HOH B2511      24.915 -16.067  -3.787  1.00 30.51           O  
ANISOU 7523  O   HOH B2511     3962   4851   2781    947    122    498       O  
HETATM 7524  O   HOH B2512      25.275 -12.868  -0.157  1.00 43.40           O  
ANISOU 7524  O   HOH B2512     4256   6635   5600   -391   -628   -682       O  
HETATM 7525  O   HOH B2513      16.026 -25.722   4.991  1.00 40.78           O  
ANISOU 7525  O   HOH B2513     5127   4865   5501   -960    415   1369       O  
HETATM 7526  O   HOH B2514      13.677 -11.680  -1.828  1.00 30.36           O  
ANISOU 7526  O   HOH B2514     3472   5316   2746   -978   -481    672       O  
HETATM 7527  O   HOH B2515      11.505 -10.066  -0.527  1.00 63.87           O  
ANISOU 7527  O   HOH B2515     8074   8789   7405    198     73    -15       O  
HETATM 7528  O   HOH B2516       9.698  -6.729   1.461  1.00 34.10           O  
ANISOU 7528  O   HOH B2516     4308   4933   3716   -226   -221    366       O  
HETATM 7529  O   HOH B2517      10.451  -9.427   2.203  1.00 43.46           O  
ANISOU 7529  O   HOH B2517     6244   5277   4992    429   -440   -131       O  
HETATM 7530  O   HOH B2518      13.627  -7.595   6.881  1.00 39.72           O  
ANISOU 7530  O   HOH B2518     5507   4682   4901    661    756    108       O  
HETATM 7531  O   HOH B2519      16.191  -6.425   6.336  1.00 35.24           O  
ANISOU 7531  O   HOH B2519     5288   4056   4045    941     -4   -805       O  
HETATM 7532  O   HOH B2520      14.248 -14.191   8.001  1.00 50.00           O  
ANISOU 7532  O   HOH B2520     7470   6150   5377   -895    466    497       O  
HETATM 7533  O   HOH B2521      12.005 -13.239   7.267  1.00 76.76           O  
ANISOU 7533  O   HOH B2521     9914  10261   8992     41    199    155       O  
HETATM 7534  O   HOH B2522      19.927  -8.485   7.961  1.00 37.16           O  
ANISOU 7534  O   HOH B2522     4997   5193   3928    205   -160    952       O  
HETATM 7535  O   HOH B2523      18.608  -1.987   5.657  1.00 18.21           O  
ANISOU 7535  O   HOH B2523     2743   2028   2148    813   -361     39       O  
HETATM 7536  O   HOH B2524      27.327 -12.275   3.639  1.00 24.77           O  
ANISOU 7536  O   HOH B2524     2720   3758   2933    939   -341    681       O  
HETATM 7537  O   HOH B2525      23.773 -14.094   8.964  1.00 39.43           O  
ANISOU 7537  O   HOH B2525     4218   5104   5658   1648   -599    317       O  
HETATM 7538  O   HOH B2526      24.560 -11.844  10.562  1.00 42.84           O  
ANISOU 7538  O   HOH B2526     6397   5504   4377    240    236    693       O  
HETATM 7539  O   HOH B2527      25.837 -13.906   6.526  1.00 27.91           O  
ANISOU 7539  O   HOH B2527     3518   3043   4043     88   -569    168       O  
HETATM 7540  O   HOH B2528      26.490  -7.798   8.738  1.00 35.25           O  
ANISOU 7540  O   HOH B2528     4615   5436   3345   -270   -691    187       O  
HETATM 7541  O   HOH B2529      29.545  -8.837   2.332  1.00 32.54           O  
ANISOU 7541  O   HOH B2529     2770   2562   7030   1154    921   1389       O  
HETATM 7542  O   HOH B2530      32.211  -5.006   4.073  1.00 53.52           O  
ANISOU 7542  O   HOH B2530     7099   6931   6305     63    164     11       O  
HETATM 7543  O   HOH B2531      28.774  -0.991   9.948  1.00 41.53           O  
ANISOU 7543  O   HOH B2531     5672   4975   5131   1144   -152   -169       O  
HETATM 7544  O   HOH B2532      32.287  -6.912   6.852  1.00 47.84           O  
ANISOU 7544  O   HOH B2532     6186   6456   5536   1049   -214     -1       O  
HETATM 7545  O   HOH B2533      26.328  -0.388  11.173  1.00 38.92           O  
ANISOU 7545  O   HOH B2533     6351   4879   3557    847    614   -536       O  
HETATM 7546  O   HOH B2534      30.245  -2.291   4.590  1.00 29.21           O  
ANISOU 7546  O   HOH B2534     3681   4812   2604   1364   -127    517       O  
HETATM 7547  O   HOH B2535      29.742  -5.307  10.647  1.00 42.76           O  
ANISOU 7547  O   HOH B2535     7586   4387   4273   1197   -141    934       O  
HETATM 7548  O   HOH B2536      19.200  -0.345   7.880  1.00 16.14           O  
ANISOU 7548  O   HOH B2536     1983   1690   2461    422     30    587       O  
HETATM 7549  O   HOH B2537      22.221   0.026  10.129  1.00 16.23           O  
ANISOU 7549  O   HOH B2537     2692   1809   1668    578   -311   -126       O  
HETATM 7550  O   HOH B2538      23.590  -5.991   9.454  1.00 48.45           O  
ANISOU 7550  O   HOH B2538     8045   5714   4651    -46   -176    339       O  
HETATM 7551  O   HOH B2539      25.362   7.507   2.235  1.00 13.88           O  
ANISOU 7551  O   HOH B2539     1911   1984   1379   -219    -99    -49       O  
HETATM 7552  O   HOH B2540      29.196   2.538   2.788  1.00 38.86           O  
ANISOU 7552  O   HOH B2540     5002   6430   3333   1492  -1220   -537       O  
HETATM 7553  O   HOH B2541       9.793  -5.692 -16.354  1.00 44.69           O  
ANISOU 7553  O   HOH B2541     6974   5779   4229   -301   -523   -235       O  
HETATM 7554  O   HOH B2542       6.438  -4.182 -15.082  1.00 21.75           O  
ANISOU 7554  O   HOH B2542     3024   3092   2147   -711   -218     -7       O  
HETATM 7555  O   HOH B2543       5.072  -6.560 -12.026  1.00 27.40           O  
ANISOU 7555  O   HOH B2543     3187   4393   2829    -81    451   -217       O  
HETATM 7556  O   HOH B2544       9.335  -8.247 -17.564  1.00 47.42           O  
ANISOU 7556  O   HOH B2544     5490   6779   5746   -193    984    103       O  
HETATM 7557  O   HOH B2545       3.933  -7.792 -14.136  1.00 31.16           O  
ANISOU 7557  O   HOH B2545     4891   3860   3090   -619    266   -163       O  
HETATM 7558  O   HOH B2546       4.126  -5.999  -9.440  1.00 17.08           O  
ANISOU 7558  O   HOH B2546     2050   2335   2105   -287    166   -261       O  
HETATM 7559  O   HOH B2547       6.035 -11.041  -4.222  1.00 65.08           O  
ANISOU 7559  O   HOH B2547     8561   7710   8457    -28     27    213       O  
HETATM 7560  O   HOH B2548       4.937  -7.417  -7.136  1.00 21.57           O  
ANISOU 7560  O   HOH B2548     2727   2754   2714   -462    -35    -23       O  
HETATM 7561  O   HOH B2549      10.292 -10.984  -6.846  1.00 31.39           O  
ANISOU 7561  O   HOH B2549     5545   3346   3036    497    505   -178       O  
HETATM 7562  O   HOH B2550       8.526  -6.811  -0.913  1.00 23.57           O  
ANISOU 7562  O   HOH B2550     3259   3254   2441   -198    333     85       O  
HETATM 7563  O   HOH B2551      12.528   1.411  -4.453  1.00 11.23           O  
ANISOU 7563  O   HOH B2551     1484   1415   1368    297    130     61       O  
HETATM 7564  O   HOH B2552      11.172  -8.562  -3.547  1.00 22.22           O  
ANISOU 7564  O   HOH B2552     3289   2451   2702     40   -177   -565       O  
HETATM 7565  O   HOH B2553      10.317  -3.960   4.860  1.00 37.65           O  
ANISOU 7565  O   HOH B2553     6131   3598   4576   -592   2129    112       O  
HETATM 7566  O   HOH B2554      15.672  -3.626   6.390  1.00 45.24           O  
ANISOU 7566  O   HOH B2554     6463   5157   5571    151    -14    558       O  
HETATM 7567  O   HOH B2555      13.121  -3.599   7.351  1.00 44.86           O  
ANISOU 7567  O   HOH B2555     5587   5339   6118   -224   -326     64       O  
HETATM 7568  O   HOH B2556      17.578   1.167  14.886  1.00 14.75           O  
ANISOU 7568  O   HOH B2556     2580   1651   1376   -313    229    102       O  
HETATM 7569  O   HOH B2557      13.663   1.538  12.095  1.00 28.12           O  
ANISOU 7569  O   HOH B2557     4322   3117   3244   -302   -219    -67       O  
HETATM 7570  O   HOH B2558      15.777  -1.255  12.815  1.00 29.99           O  
ANISOU 7570  O   HOH B2558     5164   3318   2911  -1381     52    194       O  
HETATM 7571  O   HOH B2559      20.040   3.754  11.985  1.00 11.88           O  
ANISOU 7571  O   HOH B2559     1694   1483   1337     -7      0     87       O  
HETATM 7572  O   HOH B2560      19.894  -0.675  11.688  1.00 23.65           O  
ANISOU 7572  O   HOH B2560     3510   2449   3027    335    230   -277       O  
HETATM 7573  O   HOH B2561      18.986   9.809  10.271  1.00 12.66           O  
ANISOU 7573  O   HOH B2561     1776   1603   1429     67    133   -212       O  
HETATM 7574  O   HOH B2562      19.513  11.262   6.750  1.00 21.36           O  
ANISOU 7574  O   HOH B2562     3381   2232   2505   -351    627     -5       O  
HETATM 7575  O   HOH B2563      22.317  11.217   3.084  1.00 31.79           O  
ANISOU 7575  O   HOH B2563     4804   4654   2620    732    -71    318       O  
HETATM 7576  O   HOH B2564      22.776   7.564   1.205  1.00 11.56           O  
ANISOU 7576  O   HOH B2564     1638   1406   1348     -2     79     92       O  
HETATM 7577  O   HOH B2565       2.122   1.403 -16.209  1.00 28.90           O  
ANISOU 7577  O   HOH B2565     2431   4022   4527   -134   -912    870       O  
HETATM 7578  O   HOH B2566      -2.784  -3.736 -14.236  1.00 35.01           O  
ANISOU 7578  O   HOH B2566     3939   5362   4001   -683     57   -308       O  
HETATM 7579  O   HOH B2567      -6.621   1.928 -17.290  1.00 55.71           O  
ANISOU 7579  O   HOH B2567     7021   7531   6617    164    630   -185       O  
HETATM 7580  O   HOH B2568      -3.309   4.940 -15.480  1.00 72.84           O  
ANISOU 7580  O   HOH B2568     9469   9297   8909    110    329    201       O  
HETATM 7581  O   HOH B2569      -4.761   3.577 -17.159  1.00 45.70           O  
ANISOU 7581  O   HOH B2569     5427   6022   5915    633    768     46       O  
HETATM 7582  O   HOH B2570      -5.604  -1.006 -16.024  1.00 43.84           O  
ANISOU 7582  O   HOH B2570     4561   6677   5418   -770   -163    418       O  
HETATM 7583  O   HOH B2571      -0.119   2.458 -17.628  1.00 20.91           O  
ANISOU 7583  O   HOH B2571     2764   3128   2052    554   -191   -279       O  
HETATM 7584  O   HOH B2572      -1.374   3.417 -12.566  1.00 42.98           O  
ANISOU 7584  O   HOH B2572     6108   6214   4010   -124    202    -38       O  
HETATM 7585  O   HOH B2573      -0.043  -7.500 -11.607  1.00 45.40           O  
ANISOU 7585  O   HOH B2573     5450   5897   5904   -354    106   -218       O  
HETATM 7586  O   HOH B2574       1.442  -6.102  -9.623  1.00 37.71           O  
ANISOU 7586  O   HOH B2574     3427   6822   4080   -539    209   -432       O  
HETATM 7587  O   HOH B2575       1.412   0.533 -10.370  1.00 32.45           O  
ANISOU 7587  O   HOH B2575     3117   6415   2796  -1281    633   -722       O  
HETATM 7588  O   HOH B2576      -3.926   3.596  -7.918  1.00 49.18           O  
ANISOU 7588  O   HOH B2576     5310   7495   5880    -72   -186    363       O  
HETATM 7589  O   HOH B2577       0.176  -4.676  -3.818  1.00 58.34           O  
ANISOU 7589  O   HOH B2577     7457   7396   7314    -83    314    314       O  
HETATM 7590  O   HOH B2578      -4.007  -2.057  -6.113  1.00 37.45           O  
ANISOU 7590  O   HOH B2578     4464   6015   3748  -1187    153   -361       O  
HETATM 7591  O   HOH B2579      -4.800   4.818  -4.945  1.00 50.45           O  
ANISOU 7591  O   HOH B2579     6390   6390   6390      0      0      0       O  
HETATM 7592  O   HOH B2580      -1.540  -4.381  -5.698  1.00 48.59           O  
ANISOU 7592  O   HOH B2580     6547   6301   5612  -1038    761    -35       O  
HETATM 7593  O   HOH B2581       3.601  -4.127  -2.261  1.00 40.57           O  
ANISOU 7593  O   HOH B2581     7800   4087   3529    581   -597   -402       O  
HETATM 7594  O   HOH B2582       4.679  -4.999   1.264  1.00 31.63           O  
ANISOU 7594  O   HOH B2582     4197   3698   4123   1251    996    624       O  
HETATM 7595  O   HOH B2583       9.052  -1.020   9.005  1.00 35.96           O  
ANISOU 7595  O   HOH B2583     4818   4854   3989    683    325    827       O  
HETATM 7596  O   HOH B2584       8.571  -1.288  11.808  1.00 40.25           O  
ANISOU 7596  O   HOH B2584     5450   5748   4096    591    432    601       O  
HETATM 7597  O   HOH B2585       4.846  -3.619   8.935  1.00 45.42           O  
ANISOU 7597  O   HOH B2585     7726   3888   5644   -665    385    274       O  
HETATM 7598  O   HOH B2586       5.771  -0.514  12.771  1.00 37.27           O  
ANISOU 7598  O   HOH B2586     6055   4666   3441   -547   -342   -228       O  
HETATM 7599  O   HOH B2587       6.970  -2.265   4.463  1.00 20.48           O  
ANISOU 7599  O   HOH B2587     2416   2430   2936    459    329    -77       O  
HETATM 7600  O   HOH B2588      12.945   1.964   9.536  1.00 22.37           O  
ANISOU 7600  O   HOH B2588     4005   2454   2040    165    531    334       O  
HETATM 7601  O   HOH B2589      17.952   9.438   3.445  1.00 10.57           O  
ANISOU 7601  O   HOH B2589     1422   1298   1295    118    -18    188       O  
HETATM 7602  O   HOH B2590      15.114  -0.675   9.077  1.00 23.18           O  
ANISOU 7602  O   HOH B2590     3511   3130   2167   -227     62    646       O  
HETATM 7603  O   HOH B2591      17.210  -2.394   8.081  1.00 39.98           O  
ANISOU 7603  O   HOH B2591     5214   5259   4716    901    161    678       O  
HETATM 7604  O   HOH B2592      17.744  12.574   0.773  1.00 39.32           O  
ANISOU 7604  O   HOH B2592     5085   5076   4779   -465    763     18       O  
HETATM 7605  O   HOH B2593      19.446  14.721  -3.954  1.00 48.68           O  
ANISOU 7605  O   HOH B2593     6593   5936   5966   -493    314     50       O  
HETATM 7606  O   HOH B2594      15.997  15.763  -6.342  1.00 48.03           O  
ANISOU 7606  O   HOH B2594     5953   6757   5540   -485   -141    501       O  
HETATM 7607  O   HOH B2595      13.273  12.475  -8.035  1.00 24.88           O  
ANISOU 7607  O   HOH B2595     1962   2559   4932    485    -57   -913       O  
HETATM 7608  O   HOH B2596      14.882   7.687 -14.399  1.00 11.85           O  
ANISOU 7608  O   HOH B2596     1659   1631   1212    357    162    188       O  
HETATM 7609  O   HOH B2597      19.070  18.317 -16.783  1.00 25.11           O  
ANISOU 7609  O   HOH B2597     3594   2953   2993   -490  -1359    643       O  
HETATM 7610  O   HOH B2598      19.358  21.334 -27.815  1.00 21.01           O  
ANISOU 7610  O   HOH B2598     3341   2257   2384     42    621    554       O  
HETATM 7611  O   HOH B2599      12.110  23.105 -29.114  1.00 18.14           O  
ANISOU 7611  O   HOH B2599     2805   2432   1655    352    384    204       O  
HETATM 7612  O   HOH B2600      17.574  25.516 -23.325  1.00 45.12           O  
ANISOU 7612  O   HOH B2600     6288   4101   6753    320    170    448       O  
HETATM 7613  O   HOH B2601      16.960  25.069 -19.880  1.00 30.96           O  
ANISOU 7613  O   HOH B2601     3996   3456   4311   -152    680   -522       O  
HETATM 7614  O   HOH B2602      19.713  22.219 -18.680  1.00 37.35           O  
ANISOU 7614  O   HOH B2602     4660   6894   2638   -531    213   -729       O  
HETATM 7615  O   HOH B2603      22.832  21.078 -25.434  1.00 32.64           O  
ANISOU 7615  O   HOH B2603     4717   4428   3257  -1147    137    718       O  
HETATM 7616  O   HOH B2604      21.718  19.142 -19.004  1.00 50.91           O  
ANISOU 7616  O   HOH B2604     5974   7109   6258   -453   -253   -837       O  
HETATM 7617  O   HOH B2605      25.735  16.418 -30.192  1.00 18.41           O  
ANISOU 7617  O   HOH B2605     2758   2731   1505   -241    285    130       O  
HETATM 7618  O   HOH B2606      21.775  24.144 -19.863  1.00 59.75           O  
ANISOU 7618  O   HOH B2606     7134   8074   7495   -315   -261   -187       O  
HETATM 7619  O   HOH B2607      28.947  19.677 -25.632  1.00 58.16           O  
ANISOU 7619  O   HOH B2607     8367   6746   6985   -138   -336   -344       O  
HETATM 7620  O   HOH B2608      32.576  15.677 -28.629  1.00 25.09           O  
ANISOU 7620  O   HOH B2608     2999   3185   3349   -692    661     95       O  
HETATM 7621  O   HOH B2609      32.643  16.023 -24.116  1.00 51.56           O  
ANISOU 7621  O   HOH B2609     6399   7006   6184   -459    -55   -444       O  
HETATM 7622  O   HOH B2610      27.910  12.974 -18.934  1.00 54.61           O  
ANISOU 7622  O   HOH B2610     6491   6885   7374   -369    -20    167       O  
HETATM 7623  O   HOH B2611      28.812  17.986 -23.224  1.00 60.02           O  
ANISOU 7623  O   HOH B2611     7742   7727   7336   -283     62    206       O  
HETATM 7624  O   HOH B2612      34.814  11.381 -32.083  1.00 63.51           O  
ANISOU 7624  O   HOH B2612     7638   8883   7610     97    195    -23       O  
HETATM 7625  O   HOH B2613      33.888   6.997 -31.518  1.00 69.34           O  
ANISOU 7625  O   HOH B2613     9153   8964   8230     34    106    -44       O  
HETATM 7626  O   HOH B2614      35.083   4.641 -23.569  1.00 47.93           O  
ANISOU 7626  O   HOH B2614     5735   5704   6773   -160    312   -193       O  
HETATM 7627  O   HOH B2615      37.034  14.718 -28.710  1.00 73.42           O  
ANISOU 7627  O   HOH B2615     9104   9810   8983    -55    206    115       O  
HETATM 7628  O   HOH B2616      31.224  16.167 -19.831  1.00 52.29           O  
ANISOU 7628  O   HOH B2616     6840   6794   6234   -182   -263   -436       O  
HETATM 7629  O   HOH B2617      36.751  17.608 -20.882  1.00 70.01           O  
ANISOU 7629  O   HOH B2617     8781   9179   8641    -89      6   -163       O  
HETATM 7630  O   HOH B2618      31.490   7.597 -17.566  1.00 19.19           O  
ANISOU 7630  O   HOH B2618     2346   2906   2038   -447    -83    156       O  
HETATM 7631  O   HOH B2619      34.999   9.267 -18.367  1.00 44.33           O  
ANISOU 7631  O   HOH B2619     6140   6447   4256   -603   -548   -383       O  
HETATM 7632  O   HOH B2620      32.057  19.120 -20.618  1.00 52.10           O  
ANISOU 7632  O   HOH B2620     6039   6848   6910   -382   -158    -10       O  
HETATM 7633  O   HOH B2621      32.835   6.461 -26.409  1.00 22.08           O  
ANISOU 7633  O   HOH B2621     2363   3583   2444   -190    526   -141       O  
HETATM 7634  O   HOH B2622      30.189   3.395 -20.016  1.00 16.37           O  
ANISOU 7634  O   HOH B2622     2206   2341   1672     54    -86    237       O  
HETATM 7635  O   HOH B2623      30.873   2.145 -27.121  1.00 19.52           O  
ANISOU 7635  O   HOH B2623     2093   2926   2399    -91    757   -436       O  
HETATM 7636  O   HOH B2624      33.395  -2.451 -28.087  1.00 57.85           O  
ANISOU 7636  O   HOH B2624     6456   8352   7174    398    355    214       O  
HETATM 7637  O   HOH B2625      31.683  -0.855 -31.996  1.00 57.69           O  
ANISOU 7637  O   HOH B2625     6926   8154   6838     97    570    188       O  
HETATM 7638  O   HOH B2626      30.946   2.417 -29.811  1.00 41.29           O  
ANISOU 7638  O   HOH B2626     7637   5184   2868    929    590     81       O  
HETATM 7639  O   HOH B2627      33.153   0.928 -30.748  1.00 68.97           O  
ANISOU 7639  O   HOH B2627     8805   8910   8490    299    215    -41       O  
HETATM 7640  O   HOH B2628      28.458  -4.772 -29.174  1.00 60.86           O  
ANISOU 7640  O   HOH B2628     8105   7475   7545   -268    -40   -146       O  
HETATM 7641  O   HOH B2629      28.182  -6.253 -25.925  1.00 32.02           O  
ANISOU 7641  O   HOH B2629     4136   4788   3243   1288   -146   -169       O  
HETATM 7642  O   HOH B2630      24.554 -10.912 -31.933  1.00 28.73           O  
ANISOU 7642  O   HOH B2630     3535   3686   3695    971    108  -1589       O  
HETATM 7643  O   HOH B2631      26.064  -7.321 -31.687  1.00 44.78           O  
ANISOU 7643  O   HOH B2631     5500   5692   5821    336    526    -81       O  
HETATM 7644  O   HOH B2632      25.974 -10.716 -28.263  1.00 36.43           O  
ANISOU 7644  O   HOH B2632     4465   4660   4716   1529   -194   -518       O  
HETATM 7645  O   HOH B2633      21.764  -8.913 -38.479  1.00 29.41           O  
ANISOU 7645  O   HOH B2633     3492   4297   3384    841    115  -1437       O  
HETATM 7646  O   HOH B2634      23.306  -9.519 -34.085  1.00 32.49           O  
ANISOU 7646  O   HOH B2634     4462   4435   3446   1302    166  -1507       O  
HETATM 7647  O   HOH B2635      15.526  -6.838 -44.353  1.00 19.67           O  
ANISOU 7647  O   HOH B2635     2685   2713   2076    267   -146   -328       O  
HETATM 7648  O   HOH B2636      11.309 -11.112 -40.180  1.00 22.68           O  
ANISOU 7648  O   HOH B2636     3674   3187   1756   -311    323    -92       O  
HETATM 7649  O   HOH B2637       6.546  -9.642 -41.976  1.00 47.37           O  
ANISOU 7649  O   HOH B2637     5832   5739   6428     87   -262   -504       O  
HETATM 7650  O   HOH B2638      16.460  -3.157 -43.317  1.00 27.39           O  
ANISOU 7650  O   HOH B2638     3028   3292   4086   -287    357    512       O  
HETATM 7651  O   HOH B2639      13.521 -11.382 -41.870  1.00 19.09           O  
ANISOU 7651  O   HOH B2639     3036   2530   1686     49    195    -23       O  
HETATM 7652  O   HOH B2640       6.341  -9.968 -31.027  1.00 34.46           O  
ANISOU 7652  O   HOH B2640     3827   6188   3076    -51    392   -215       O  
HETATM 7653  O   HOH B2641       7.233 -10.977 -38.073  1.00 32.27           O  
ANISOU 7653  O   HOH B2641     3523   5376   3363   -462    479  -1250       O  
HETATM 7654  O   HOH B2642      18.813 -14.371 -36.401  1.00 71.93           O  
ANISOU 7654  O   HOH B2642     8842   9675   8812     61   -180    -84       O  
HETATM 7655  O   HOH B2643      15.324 -14.334 -38.473  1.00 26.49           O  
ANISOU 7655  O   HOH B2643     4442   3283   2341   -443    277    386       O  
HETATM 7656  O   HOH B2644       9.395  -9.414 -37.470  1.00 18.94           O  
ANISOU 7656  O   HOH B2644     2451   2471   2274   -283    -99   -380       O  
HETATM 7657  O   HOH B2645      16.275 -15.100 -32.814  1.00 78.65           O  
ANISOU 7657  O   HOH B2645     9883  10269   9733     27     92    -57       O  
HETATM 7658  O   HOH B2646       8.942 -12.988 -39.304  1.00 41.45           O  
ANISOU 7658  O   HOH B2646     6003   5212   4532    306    967    445       O  
HETATM 7659  O   HOH B2647      12.847 -15.188 -38.656  1.00 25.89           O  
ANISOU 7659  O   HOH B2647     4031   3291   2514    556   -605   -721       O  
HETATM 7660  O   HOH B2648      14.093 -14.442 -31.548  1.00 29.95           O  
ANISOU 7660  O   HOH B2648     4578   3190   3610    -24    505   -724       O  
HETATM 7661  O   HOH B2649      15.965  -7.722 -27.820  1.00 14.11           O  
ANISOU 7661  O   HOH B2649     1783   1847   1732      8    228    -30       O  
HETATM 7662  O   HOH B2650       7.494 -16.457 -30.645  1.00 42.15           O  
ANISOU 7662  O   HOH B2650     6043   5044   4928   -593   -340   -279       O  
HETATM 7663  O   HOH B2651       9.076 -14.006 -33.627  1.00 71.38           O  
ANISOU 7663  O   HOH B2651     9446   9027   8650   -212    194   -165       O  
HETATM 7664  O   HOH B2652      11.863 -15.588 -32.526  1.00 33.27           O  
ANISOU 7664  O   HOH B2652     5728   3468   3443  -1173   -237   -716       O  
HETATM 7665  O   HOH B2653      10.484 -15.397 -26.188  1.00 35.40           O  
ANISOU 7665  O   HOH B2653     5428   4206   3816     -2    123    299       O  
HETATM 7666  O   HOH B2654       6.486 -12.658 -31.584  1.00 38.22           O  
ANISOU 7666  O   HOH B2654     4602   5165   4757   -295    441    -25       O  
HETATM 7667  O   HOH B2655       8.217 -14.511 -26.712  1.00 42.97           O  
ANISOU 7667  O   HOH B2655     4798   6068   5459   -147    183   -801       O  
HETATM 7668  O   HOH B2656      11.205 -11.669 -19.999  1.00 32.77           O  
ANISOU 7668  O   HOH B2656     6793   3090   2568   -410    173   -204       O  
HETATM 7669  O   HOH B2657      13.515 -18.218 -21.369  1.00 64.47           O  
ANISOU 7669  O   HOH B2657     8317   8124   8055     51   -102    411       O  
HETATM 7670  O   HOH B2658      21.055 -13.574 -20.634  1.00 35.23           O  
ANISOU 7670  O   HOH B2658     4645   4389   4350    762     73    181       O  
HETATM 7671  O   HOH B2659      21.050 -14.933 -30.291  1.00 45.90           O  
ANISOU 7671  O   HOH B2659     5261   5015   7163    974    615   -267       O  
HETATM 7672  O   HOH B2660      22.558 -14.414 -26.354  1.00 49.32           O  
ANISOU 7672  O   HOH B2660     7080   5999   5659    391    268   -490       O  
HETATM 7673  O   HOH B2661      19.086 -16.742 -30.286  1.00 61.83           O  
ANISOU 7673  O   HOH B2661     7826   7447   8218    311    198    -88       O  
HETATM 7674  O   HOH B2662      16.723 -17.737 -29.458  1.00 68.12           O  
ANISOU 7674  O   HOH B2662     8722   8740   8420     41   -107    -12       O  
HETATM 7675  O   HOH B2663      22.574 -11.158 -24.008  1.00 56.33           O  
ANISOU 7675  O   HOH B2663     7182   6985   7237   -244    -84    467       O  
HETATM 7676  O   HOH B2664      14.169 -15.830 -29.120  1.00 39.57           O  
ANISOU 7676  O   HOH B2664     5381   4300   5353    221   -202    285       O  
HETATM 7677  O   HOH B2665      16.378 -10.274 -21.975  1.00 18.87           O  
ANISOU 7677  O   HOH B2665     2738   2133   2299    -75   -139    110       O  
HETATM 7678  O   HOH B2666      21.548  -4.739 -39.418  1.00 40.60           O  
ANISOU 7678  O   HOH B2666     5256   5506   4663   1101      7  -1272       O  
HETATM 7679  O   HOH B2667      19.087  -3.192 -42.092  1.00 27.47           O  
ANISOU 7679  O   HOH B2667     3834   4108   2494    613    757   -361       O  
HETATM 7680  O   HOH B2668      15.539  -1.093 -46.877  1.00 47.20           O  
ANISOU 7680  O   HOH B2668     5715   5831   6388   -506    586     80       O  
HETATM 7681  O   HOH B2669      13.316  -0.833 -43.237  1.00 18.91           O  
ANISOU 7681  O   HOH B2669     2389   2729   2068    418     54    101       O  
HETATM 7682  O   HOH B2670      19.547   2.232 -41.227  1.00 21.92           O  
ANISOU 7682  O   HOH B2670     3297   2969   2062   -877   1250   -628       O  
HETATM 7683  O   HOH B2671      20.009  -0.956 -43.676  1.00 49.36           O  
ANISOU 7683  O   HOH B2671     5696   6485   6573     61     70   -560       O  
HETATM 7684  O  BHOH B2672      11.124   3.596 -21.430  0.40 10.50           O  
ANISOU 7684  O  BHOH B2672     1371   1349   1268    119     79    255       O  
HETATM 7685  O  AHOH B2673      11.751   2.604 -20.645  0.60 12.55           O  
ANISOU 7685  O  AHOH B2673     1613   1970   1185     96     48   -146       O  
HETATM 7686  O   HOH B2674       9.835 -12.642  -9.362  1.00 65.75           O  
ANISOU 7686  O   HOH B2674     8179   8811   7990    290     18    -36       O  
HETATM 7687  O   HOH B2675      17.372  -4.365 -22.161  1.00 14.28           O  
ANISOU 7687  O   HOH B2675     1645   1907   1872     11     77   -457       O  
HETATM 7688  O   HOH B2676       9.743 -11.311 -12.405  1.00 33.38           O  
ANISOU 7688  O   HOH B2676     3594   4254   4834   -630    367    -41       O  
HETATM 7689  O   HOH B2677      11.702  -7.831 -16.931  1.00 38.20           O  
ANISOU 7689  O   HOH B2677     4270   6263   3979   -972   -357    -25       O  
HETATM 7690  O   HOH B2678      13.037 -11.193  -6.623  1.00 34.37           O  
ANISOU 7690  O   HOH B2678     5613   4807   2638   1467   -654   -208       O  
HETATM 7691  O   HOH B2679      17.749  -7.555 -20.740  1.00 19.98           O  
ANISOU 7691  O   HOH B2679     3063   2555   1974    816    312      3       O  
HETATM 7692  O   HOH B2680      17.283  -3.248 -16.203  1.00 11.55           O  
ANISOU 7692  O   HOH B2680     1413   1618   1358     95    111    -83       O  
HETATM 7693  O   HOH B2681      15.034  -9.006  -6.195  1.00 30.20           O  
ANISOU 7693  O   HOH B2681     4170   3815   3489    517   -192   -133       O  
HETATM 7694  O   HOH B2682      14.930  -9.206 -19.864  1.00 27.27           O  
ANISOU 7694  O   HOH B2682     3175   4871   2315   -886   -433    123       O  
HETATM 7695  O   HOH B2683      16.209 -12.007 -17.965  1.00 21.44           O  
ANISOU 7695  O   HOH B2683     3153   2925   2068    827   -460   -658       O  
HETATM 7696  O   HOH B2684       3.234   4.054 -16.959  1.00 36.89           O  
ANISOU 7696  O   HOH B2684     3824   5264   4929    778    613    784       O  
CONECT  391 6109                                                                
CONECT  547 6109                                                                
CONECT  772 6110                                                                
CONECT  796 6110                                                                
CONECT  827 6110                                                                
CONECT  899 6110                                                                
CONECT 1416 6109                                                                
CONECT 3434 6181                                                                
CONECT 3595 6181                                                                
CONECT 3823 6182                                                                
CONECT 3847 6182                                                                
CONECT 3878 6182                                                                
CONECT 3954 6182                                                                
CONECT 4482 6181                                                                
CONECT 6109  391  547 1416 7000                                                 
CONECT 6109 7001                                                                
CONECT 6110  772  796  827  899                                                 
CONECT 6111 6112 6113 6114 6123                                                 
CONECT 6112 6111                                                                
CONECT 6113 6111                                                                
CONECT 6114 6111 6115                                                           
CONECT 6115 6114 6116                                                           
CONECT 6116 6115 6117 6118                                                      
CONECT 6117 6116 6122                                                           
CONECT 6118 6116 6119 6120                                                      
CONECT 6119 6118                                                                
CONECT 6120 6118 6121 6122                                                      
CONECT 6121 6120                                                                
CONECT 6122 6117 6120 6145 6155                                                 
CONECT 6123 6111 6124                                                           
CONECT 6124 6123 6125 6126 6127                                                 
CONECT 6125 6124                                                                
CONECT 6126 6124                                                                
CONECT 6127 6124 6128                                                           
CONECT 6128 6127 6129                                                           
CONECT 6129 6128 6130 6131                                                      
CONECT 6130 6129 6135                                                           
CONECT 6131 6129 6132 6133                                                      
CONECT 6132 6131                                                                
CONECT 6133 6131 6134 6135                                                      
CONECT 6134 6133                                                                
CONECT 6135 6130 6133 6136                                                      
CONECT 6136 6135 6137 6144                                                      
CONECT 6137 6136 6138                                                           
CONECT 6138 6137 6139 6142                                                      
CONECT 6139 6138 6140 6141                                                      
CONECT 6140 6139                                                                
CONECT 6141 6139                                                                
CONECT 6142 6138 6143                                                           
CONECT 6143 6142 6144                                                           
CONECT 6144 6136 6143                                                           
CONECT 6145 6122 6146 6154                                                      
CONECT 6146 6145 6147                                                           
CONECT 6147 6146 6148                                                           
CONECT 6148 6147 6149 6154                                                      
CONECT 6149 6148 6150 6151                                                      
CONECT 6150 6149                                                                
CONECT 6151 6149 6152                                                           
CONECT 6152 6151 6153                                                           
CONECT 6153 6152 6154                                                           
CONECT 6154 6145 6148 6153                                                      
CONECT 6155 6122 6156 6164                                                      
CONECT 6156 6155 6157                                                           
CONECT 6157 6156 6158                                                           
CONECT 6158 6157 6159 6164                                                      
CONECT 6159 6158 6160 6161                                                      
CONECT 6160 6159                                                                
CONECT 6161 6159 6162                                                           
CONECT 6162 6161 6163                                                           
CONECT 6163 6162 6164                                                           
CONECT 6164 6155 6158 6163                                                      
CONECT 6165 6166                                                                
CONECT 6166 6165 6167 6168 6169                                                 
CONECT 6167 6166                                                                
CONECT 6168 6166                                                                
CONECT 6169 6166 6170                                                           
CONECT 6170 6169 6171 6172                                                      
CONECT 6171 6170                                                                
CONECT 6172 6170                                                                
CONECT 6173 6174                                                                
CONECT 6174 6173 6175 6176 6177                                                 
CONECT 6175 6174                                                                
CONECT 6176 6174                                                                
CONECT 6177 6174 6178                                                           
CONECT 6178 6177 6179 6180                                                      
CONECT 6179 6178                                                                
CONECT 6180 6178                                                                
CONECT 6181 3434 3595 4482 7684                                                 
CONECT 6181 7685                                                                
CONECT 6182 3823 3847 3878 3954                                                 
CONECT 6183 6184 6185 6186 6195                                                 
CONECT 6184 6183                                                                
CONECT 6185 6183                                                                
CONECT 6186 6183 6187                                                           
CONECT 6187 6186 6188                                                           
CONECT 6188 6187 6189 6190                                                      
CONECT 6189 6188 6194                                                           
CONECT 6190 6188 6191 6192                                                      
CONECT 6191 6190                                                                
CONECT 6192 6190 6193 6194                                                      
CONECT 6193 6192                                                                
CONECT 6194 6189 6192 6217 6227                                                 
CONECT 6195 6183 6196                                                           
CONECT 6196 6195 6197 6198 6199                                                 
CONECT 6197 6196                                                                
CONECT 6198 6196                                                                
CONECT 6199 6196 6200                                                           
CONECT 6200 6199 6201                                                           
CONECT 6201 6200 6202 6203                                                      
CONECT 6202 6201 6207                                                           
CONECT 6203 6201 6204 6205                                                      
CONECT 6204 6203                                                                
CONECT 6205 6203 6206 6207                                                      
CONECT 6206 6205                                                                
CONECT 6207 6202 6205 6208                                                      
CONECT 6208 6207 6209 6216                                                      
CONECT 6209 6208 6210                                                           
CONECT 6210 6209 6211 6214                                                      
CONECT 6211 6210 6212 6213                                                      
CONECT 6212 6211                                                                
CONECT 6213 6211                                                                
CONECT 6214 6210 6215                                                           
CONECT 6215 6214 6216                                                           
CONECT 6216 6208 6215                                                           
CONECT 6217 6194 6218 6226                                                      
CONECT 6218 6217 6219                                                           
CONECT 6219 6218 6220                                                           
CONECT 6220 6219 6221 6226                                                      
CONECT 6221 6220 6222 6223                                                      
CONECT 6222 6221                                                                
CONECT 6223 6221 6224                                                           
CONECT 6224 6223 6225                                                           
CONECT 6225 6224 6226                                                           
CONECT 6226 6217 6220 6225                                                      
CONECT 6227 6194 6228 6236                                                      
CONECT 6228 6227 6229                                                           
CONECT 6229 6228 6230                                                           
CONECT 6230 6229 6231 6236                                                      
CONECT 6231 6230 6232 6233                                                      
CONECT 6232 6231                                                                
CONECT 6233 6231 6234                                                           
CONECT 6234 6233 6235                                                           
CONECT 6235 6234 6236                                                           
CONECT 6236 6227 6230 6235                                                      
CONECT 6237 6238                                                                
CONECT 6238 6237 6239 6240 6241                                                 
CONECT 6239 6238                                                                
CONECT 6240 6238                                                                
CONECT 6241 6238 6242                                                           
CONECT 6242 6241 6243 6244                                                      
CONECT 6243 6242                                                                
CONECT 6244 6242                                                                
CONECT 6245 6246                                                                
CONECT 6246 6245 6247 6248 6249                                                 
CONECT 6247 6246                                                                
CONECT 6248 6246                                                                
CONECT 6249 6246 6250                                                           
CONECT 6250 6249 6251 6252                                                      
CONECT 6251 6250                                                                
CONECT 6252 6250                                                                
CONECT 6253 6254                                                                
CONECT 6254 6253 6255 6256 6257                                                 
CONECT 6255 6254                                                                
CONECT 6256 6254                                                                
CONECT 6257 6254 6258                                                           
CONECT 6258 6257 6259 6260                                                      
CONECT 6259 6258                                                                
CONECT 6260 6258                                                                
CONECT 7000 6109                                                                
CONECT 7001 6109                                                                
CONECT 7684 6181                                                                
CONECT 7685 6181                                                                
MASTER      497    0    9   20   42    0   30    9 7694    2  172   58          
END