path: root/plip/test/pdb/2pvb.pdb

HEADER    METAL BINDING PROTEIN                   02-OCT-98   2PVB              
TITLE     PIKE PARVALBUMIN (PI 4.10) AT LOW TEMPERATURE (100K) AND              
TITLE    2 ATOMIC RESOLUTION (0.91 A).                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (PARVALBUMIN);                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 OTHER_DETAILS: (PIKE PI 4.10)                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESOX LUCIUS;                                    
SOURCE   3 ORGANISM_COMMON: NORTHERN PIKE;                                      
SOURCE   4 ORGANISM_TAXID: 8010;                                                
SOURCE   5 TISSUE: MUSCLE                                                       
KEYWDS    CALCIUM BINDING PROTEIN, METAL BINDING PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.DECLERCQ,C.EVRARD                                                 
REVDAT   4   24-FEB-09 2PVB    1       VERSN                                    
REVDAT   3   05-MAY-00 2PVB    1       JRNL                                     
REVDAT   2   22-DEC-99 2PVB    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   07-OCT-98 2PVB    0                                                
JRNL        AUTH   J.P.DECLERCQ,C.EVRARD,V.LAMZIN,J.PARELLO                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE EF-HAND PARVALBUMIN AT              
JRNL        TITL 2 ATOMIC RESOLUTION (0.91 A) AND AT LOW TEMPERATURE            
JRNL        TITL 3 (100 K). EVIDENCE FOR CONFORMATIONAL MULTISTATES             
JRNL        TITL 4 WITHIN THE HYDROPHOBIC CORE.                                 
JRNL        REF    PROTEIN SCI.                  V.   8  2194 1999              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   10548066                                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.P.DECLERCQ,C.EVRARD,D.C.CARTER,B.S.WRIGHT,                 
REMARK   1  AUTH 2 G.ETIENNE,J.PARELLO                                          
REMARK   1  TITL   A CRYSTAL OF A TYPICAL EF-HAND PROTEIN GROWN UNDER           
REMARK   1  TITL 2 MICROGRAVITY DIFFRACTS X- RAYS BEYOND 0.9 A                  
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    J.CRYST.GROWTH                V. 196   595 1999              
REMARK   1  REFN                   ISSN 0022-0248                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.P.DECLERCQ,B.TINANT,J.PARELLO                              
REMARK   1  TITL   X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10           
REMARK   1  TITL 2 BETA PARVALBUMIN                                             
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  52   165 1996              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.P.DECLERCQ,B.TINANT,J.PARELLO,J.RAMBAUD                    
REMARK   1  TITL   IONIC INTERACTIONS WITH PARVALBUMINS. CRYSTAL                
REMARK   1  TITL 2 STRUCTURE DETERMINATION OF PIKE 4.10 PARVALBUMIN             
REMARK   1  TITL 3 IN FOUR DIFFERENT IONIC ENVIRONMENTS                         
REMARK   1  REF    J.MOL.BIOL.                   V. 220  1017 1991              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.P.DECLERCQ,B.TINANT,J.PARELLO,G.ETIENNE,R.HUBER            
REMARK   1  TITL   CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT OF            
REMARK   1  TITL 2 PIKE 4.10 PARVALBUMIN (MINOR COMPONENT FROM ESOX             
REMARK   1  TITL 3 LUCIUS)                                                      
REMARK   1  REF    J.MOL.BIOL.                   V. 202   349 1988              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM, 5%                     
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.110                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.110                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.132                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 3187                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 63698                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.109                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.109                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.131                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 3103                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 62168                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 873                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 6                                             
REMARK   3   SOLVENT ATOMS      : 217                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1025.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 784.00                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 16                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 9883                    
REMARK   3   NUMBER OF RESTRAINTS                     : 12405                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.015                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.032                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.335                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.093                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.102                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.061                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.007                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.037                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.100                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER                                    
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PVB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008041.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
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                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9096                             
REMARK 200  MONOCHROMATOR                  : BENT SINGLE-CRYSTAL GERMANIUM      
REMARK 200                                   TRIANGULAR MONOCHROMATOR           
REMARK 200  OPTICS                         : SEGMENTED MIRROR                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63698                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.910                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 3.60000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.91                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 12.40000                           
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1PVB                                       
REMARK 200                                                                      
REMARK 200 REMARK: STRUCTURE PREVIOUSLY SOLVED AT 1.75 A                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP, MICROGRAVITY               
REMARK 280  CONDITIONS PROTEIN SOLUTION : 27 MG/ML, 0.02% (W/V) NAN3            
REMARK 280  RESERVOIR : 2.4M AMMONIUM SULFATE 0.03%(W/V) EDTA, 0.02% (W/V)      
REMARK 280  NAN3 TRIS BUFFER (PH 8.0) DROP : 10 MICROL. PROTEIN SOLUTION +      
REMARK 280  10 MICROL. RESERVOIR, VAPOR DIFFUSION - SITTING DROP IN             
REMARK 280  MICROGRAVITY                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000       25.51500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       17.28500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.90500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       17.28500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.51500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.90500            
REMARK 290   SMTRY3   4  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 350                                                                      
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 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    VAL A  33   CB  -  CA  -  C   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ASP A 100   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    MET A 105   N   -  CA  -  CB  ANGL. DEV. =  10.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 ACETYL IS COVALENTLY ATTACHED TO THE                                 
REMARK 600 N-TERMINAL SERINE BY AN AMIDE LINKAGE                                
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                              CA A 110  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  51   OD1                                                    
REMARK 620 2 ASP A  53   OD1  82.6                                              
REMARK 620 3 SER A  55   OG   87.8  78.2                                        
REMARK 620 4 PHE A  57   O    82.9 150.3  75.3                                  
REMARK 620 5 GLU A  59   OE1 168.8 103.5  84.3  87.3                            
REMARK 620 6 GLU A  62   OE1 103.6 128.4 151.7  80.4  80.1                      
REMARK 620 7 GLU A  62   OE2 100.2  75.4 151.2 132.9  90.5  52.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 111  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  90   OD1                                                    
REMARK 620 2 ASP A  92   OD1  84.8                                              
REMARK 620 3 ASP A  94   OD1  86.0  82.5                                        
REMARK 620 4 MET A  96   O    83.7 158.6  78.8                                  
REMARK 620 5 GLU A 101   OE1 116.3 117.9 149.8  83.5                            
REMARK 620 6 GLU A 101   OE2  86.9  74.2 156.1 123.0  51.8                      
REMARK 620 7 HOH A 201   O   161.9  97.1  76.5  88.5  78.8 111.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CD                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATION BINDING SITE OCCUPIED BY CA2+ CA 110 A      
REMARK 800 SITE_IDENTIFIER: EF                                                  
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATION BINDING SITE OCCUPIED BY CA2+ CA 111 A      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 110                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 111                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 A 200                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 150                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 151                 
DBREF  2PVB A    1   107  UNP    P02619   PRVB_ESOLU       1    107             
SEQRES   1 A  108  ACE SER PHE ALA GLY LEU LYS ASP ALA ASP VAL ALA ALA          
SEQRES   2 A  108  ALA LEU ALA ALA CYS SER ALA ALA ASP SER PHE LYS HIS          
SEQRES   3 A  108  LYS GLU PHE PHE ALA LYS VAL GLY LEU ALA SER LYS SER          
SEQRES   4 A  108  LEU ASP ASP VAL LYS LYS ALA PHE TYR VAL ILE ASP GLN          
SEQRES   5 A  108  ASP LYS SER GLY PHE ILE GLU GLU ASP GLU LEU LYS LEU          
SEQRES   6 A  108  PHE LEU GLN ASN PHE SER PRO SER ALA ARG ALA LEU THR          
SEQRES   7 A  108  ASP ALA GLU THR LYS ALA PHE LEU ALA ASP GLY ASP LYS          
SEQRES   8 A  108  ASP GLY ASP GLY MET ILE GLY VAL ASP GLU PHE ALA ALA          
SEQRES   9 A  108  MET ILE LYS ALA                                              
HET    ACE  A   0       3                                                       
HET     CA  A 110       1                                                       
HET     CA  A 111       1                                                       
HET    NH4  A 200       1                                                       
HET    FMT  A 150       3                                                       
HET    FMT  A 151       3                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      CA CALCIUM ION                                                      
HETNAM     NH4 AMMONIUM ION                                                     
HETNAM     FMT FORMIC ACID                                                      
FORMUL   1  ACE    C2 H4 O                                                      
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  NH4    H4 N 1+                                                      
FORMUL   5  FMT    2(C H2 O2)                                                   
FORMUL   7  HOH   *211(H2 O)                                                    
HELIX    1   1 ASP A    8  CYS A   18  1                                  11    
HELIX    2   2 HIS A   26  VAL A   33  1                                   8    
HELIX    3   3 LEU A   35  SER A   37  5                                   3    
HELIX    4   4 LEU A   40  ILE A   50  1                                  11    
HELIX    5   5 GLU A   60  LYS A   64  1                                   5    
HELIX    6   6 PHE A   66  ASN A   69  5                                   4    
HELIX    7   7 ASP A   79  GLY A   89  1                                  11    
HELIX    8   8 VAL A   99  ILE A  106  1                                   8    
LINK         OD1 ASP A  51                CA    CA A 110     1555   1555  2.27  
LINK         OD1 ASP A  53                CA    CA A 110     1555   1555  2.30  
LINK         OG  SER A  55                CA    CA A 110     1555   1555  2.51  
LINK         O   PHE A  57                CA    CA A 110     1555   1555  2.32  
LINK         OE1 GLU A  59                CA    CA A 110     1555   1555  2.33  
LINK         OE1 GLU A  62                CA    CA A 110     1555   1555  2.44  
LINK         OE2 GLU A  62                CA    CA A 110     1555   1555  2.51  
LINK         OD1 ASP A  90                CA    CA A 111     1555   1555  2.31  
LINK         OD1 ASP A  92                CA    CA A 111     1555   1555  2.35  
LINK         OD1 ASP A  94                CA    CA A 111     1555   1555  2.36  
LINK         O   MET A  96                CA    CA A 111     1555   1555  2.37  
LINK         OE1 GLU A 101                CA    CA A 111     1555   1555  2.43  
LINK         OE2 GLU A 101                CA    CA A 111     1555   1555  2.54  
LINK        CA    CA A 111                 O   HOH A 201     1555   1555  2.37  
LINK         C   ACE A   0                 N   SER A   1     1555   1555  1.33  
SITE     1  CD  6 ASP A  51  ASP A  53  SER A  55  PHE A  57                    
SITE     2  CD  6 GLU A  59  GLU A  62                                          
SITE     1  EF  6 ASP A  90  ASP A  92  ASP A  94  MET A  96                    
SITE     2  EF  6 HOH A 201  GLU A 101                                          
SITE     1 AC1  6 ASP A  51  ASP A  53  SER A  55  PHE A  57                    
SITE     2 AC1  6 GLU A  59  GLU A  62                                          
SITE     1 AC2  6 ASP A  90  ASP A  92  ASP A  94  MET A  96                    
SITE     2 AC2  6 GLU A 101  HOH A 201                                          
SITE     1 AC3  6 ASP A  53  GLU A  59  ASP A  61  HOH A 212                    
SITE     2 AC3  6 HOH A 293  HOH A 308                                          
SITE     1 AC4  6 LYS A 107  FMT A 151  HOH A 223  HOH A 226                    
SITE     2 AC4  6 HOH A 277  HOH A 353                                          
SITE     1 AC5  7 THR A  78  ASP A  79  ALA A  80  LYS A 107                    
SITE     2 AC5  7 FMT A 150  HOH A 306  HOH A 323                               
CRYST1   51.030   49.810   34.570  90.00  90.00  90.00 P 21 21 21    4          
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      0.019596  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020076  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.028927        0.00000                         
HETATM    1  C   ACE A   0       3.753  17.697  16.468  1.00  6.24           C  
ANISOU    1  C   ACE A   0      963    734    674   -159    -23     47       C  
HETATM    2  O   ACE A   0       3.169  17.058  17.352  1.00  7.96           O  
ANISOU    2  O   ACE A   0     1254   1133    640   -467    -26     59       O  
HETATM    3  CH3 ACE A   0       3.163  17.765  15.090  1.00  8.20           C  
ANISOU    3  CH3 ACE A   0     1510    876    729   -348   -241    152       C  
ATOM      4  N   SER A   1       4.877  18.359  16.704  1.00  6.66           N  
ANISOU    4  N   SER A   1     1067    743    720   -217    -87    188       N  
ATOM      5  CA ASER A   1       5.448  18.370  18.030  0.46  8.09           C  
ANISOU    5  CA ASER A   1     1071   1007    996   -402   -338    324       C  
ATOM      6  CA BSER A   1       5.579  18.279  17.960  0.54  7.39           C  
ANISOU    6  CA BSER A   1      953   1000    855   -305   -178    157       C  
ATOM      7  C   SER A   1       6.405  19.560  18.155  1.00  7.49           C  
ANISOU    7  C   SER A   1      985   1023    839   -300   -118    208       C  
ATOM      8  O   SER A   1       6.998  20.038  17.208  1.00 10.46           O  
ANISOU    8  O   SER A   1     1549   1555    870   -863   -268    347       O  
ATOM      9  CB ASER A   1       6.225  17.109  18.342  0.46 10.67           C  
ANISOU    9  CB ASER A   1     1326   1174   1553   -402   -441    752       C  
ATOM     10  CB BSER A   1       6.500  17.057  17.937  0.54 11.64           C  
ANISOU   10  CB BSER A   1     1895    976   1553    -15   -734    408       C  
ATOM     11  OG ASER A   1       7.464  17.138  17.697  0.46 14.45           O  
ANISOU   11  OG ASER A   1     1731   1696   2063    303    148    645       O  
ATOM     12  OG BSER A   1       7.078  16.800  19.210  0.54 12.01           O  
ANISOU   12  OG BSER A   1     2237   1064   1261    -17   -881    247       O  
ATOM     13  N   PHE A   2       6.458  20.045  19.377  1.00  6.93           N  
ANISOU   13  N   PHE A   2      865    844    924   -140   -178    152       N  
ATOM     14  CA  PHE A   2       7.323  21.172  19.687  1.00  6.96           C  
ANISOU   14  CA  PHE A   2      710    860   1076   -165    -66    114       C  
ATOM     15  C   PHE A   2       7.584  21.108  21.189  1.00  7.00           C  
ANISOU   15  C   PHE A   2      801    860   1000    -45    -96    102       C  
ATOM     16  O   PHE A   2       6.651  21.017  21.981  1.00  7.13           O  
ANISOU   16  O   PHE A   2      807    977    924    -36    -62   -161       O  
ATOM     17  CB  PHE A   2       6.627  22.488  19.323  1.00  7.51           C  
ANISOU   17  CB  PHE A   2      806    961   1088   -128   -140    233       C  
ATOM     18  CG  PHE A   2       7.511  23.700  19.330  1.00  6.69           C  
ANISOU   18  CG  PHE A   2      773    850    920    -75    -66    100       C  
ATOM     19  CD1 PHE A   2       7.731  24.401  20.482  1.00  8.50           C  
ANISOU   19  CD1 PHE A   2     1233   1127    870   -255     12     79       C  
ATOM     20  CD2 PHE A   2       8.074  24.175  18.171  1.00  6.75           C  
ANISOU   20  CD2 PHE A   2      928    812    823     -7     27      7       C  
ATOM     21  CE1 PHE A   2       8.508  25.556  20.476  1.00  8.94           C  
ANISOU   21  CE1 PHE A   2     1540   1040    815   -324     30   -109       C  
ATOM     22  CE2 PHE A   2       8.856  25.316  18.156  1.00  7.63           C  
ANISOU   22  CE2 PHE A   2     1024    968    909   -110     91     76       C  
ATOM     23  CZ  PHE A   2       9.057  26.019  19.315  1.00  8.66           C  
ANISOU   23  CZ  PHE A   2     1275    907   1109   -260    194    -78       C  
ATOM     24  N   ALA A   3       8.853  21.016  21.564  1.00  9.04           N  
ANISOU   24  N   ALA A   3      808   1355   1272    -33   -162    197       N  
ATOM     25  CA  ALA A   3       9.159  20.776  22.973  1.00  8.94           C  
ANISOU   25  CA  ALA A   3      870   1262   1265     64   -191     83       C  
ATOM     26  C   ALA A   3       8.445  21.762  23.869  1.00  9.21           C  
ANISOU   26  C   ALA A   3     1206   1137   1158     -8   -597    -60       C  
ATOM     27  O   ALA A   3       8.354  22.963  23.660  1.00 10.42           O  
ANISOU   27  O   ALA A   3     1400   1139   1419    -38   -501   -199       O  
ATOM     28  CB  ALA A   3      10.672  20.869  23.156  1.00 12.56           C  
ANISOU   28  CB  ALA A   3     1155   2250   1368     68   -395    259       C  
ATOM     29  N   GLY A   4       7.866  21.283  24.962  1.00  9.48           N  
ANISOU   29  N   GLY A   4     1128   1405   1069    303   -394    -17       N  
ATOM     30  CA  GLY A   4       7.151  22.063  25.901  1.00  9.59           C  
ANISOU   30  CA  GLY A   4     1287   1137   1220    373   -651    -64       C  
ATOM     31  C   GLY A   4       5.633  22.165  25.670  1.00  7.79           C  
ANISOU   31  C   GLY A   4     1253    845    861    241   -389     -7       C  
ATOM     32  O   GLY A   4       4.876  22.506  26.580  1.00  8.87           O  
ANISOU   32  O   GLY A   4     1309   1225    834    306   -359   -219       O  
ATOM     33  N   LEU A   6       5.204  21.859  24.449  1.00  7.05           N  
ANISOU   33  N   LEU A   6     1101    814    761    237   -376   -126       N  
ATOM     34  CA  LEU A   6       3.808  21.906  24.058  1.00  6.47           C  
ANISOU   34  CA  LEU A   6     1027    783    647    226   -179    -86       C  
ATOM     35  C   LEU A   6       3.301  20.505  23.930  1.00  6.36           C  
ANISOU   35  C   LEU A   6      965    808    645    177   -111     -7       C  
ATOM     36  O   LEU A   6       4.070  19.533  23.765  1.00  7.42           O  
ANISOU   36  O   LEU A   6     1054    790    974    229    -99     13       O  
ATOM     37  CB  LEU A   6       3.647  22.661  22.709  1.00  5.79           C  
ANISOU   37  CB  LEU A   6      832    713    653    127   -219    -67       C  
ATOM     38  CG  LEU A   6       4.234  24.076  22.716  1.00  6.77           C  
ANISOU   38  CG  LEU A   6     1068    667    839    131   -227    -93       C  
ATOM     39  CD1 LEU A   6       4.050  24.736  21.363  1.00  7.11           C  
ANISOU   39  CD1 LEU A   6      963    782    957    150   -180     33       C  
ATOM     40  CD2 LEU A   6       3.604  24.952  23.804  1.00  7.91           C  
ANISOU   40  CD2 LEU A   6     1310    746    950    158   -178   -128       C  
ATOM     41  N   LYS A   7       1.980  20.360  23.980  1.00  6.80           N  
ANISOU   41  N   LYS A   7     1043    852    691    173    -99    -43       N  
ATOM     42  CA  LYS A   7       1.357  19.030  23.804  1.00  6.82           C  
ANISOU   42  CA  LYS A   7     1118    821    653     58     72    152       C  
ATOM     43  C   LYS A   7       1.238  18.704  22.329  1.00  5.99           C  
ANISOU   43  C   LYS A   7      860    659    754    -67    -10     82       C  
ATOM     44  O   LYS A   7       0.736  19.508  21.537  1.00  6.37           O  
ANISOU   44  O   LYS A   7     1047    692    680    -92   -105     96       O  
ATOM     45  CB  LYS A   7      -0.003  19.111  24.459  1.00  9.00           C  
ANISOU   45  CB  LYS A   7     1189   1331    899    205    141    132       C  
ATOM     46  CG  LYS A   7      -0.708  17.838  24.547  1.00 11.73           C  
ANISOU   46  CG  LYS A   7     1258   1405   1792     14    140   -130       C  
ATOM     47  CD  LYS A   7      -1.908  18.019  25.507  1.00 25.13           C  
ANISOU   47  CD  LYS A   7     1333   3988   4225    347   1221   1436       C  
ATOM     48  CE  LYS A   7      -2.950  16.930  25.153  1.00 25.31           C  
ANISOU   48  CE  LYS A   7     1355   5163   3099    -78    385   1840       C  
ATOM     49  NZ  LYS A   7      -4.160  17.514  25.846  1.00 28.34           N  
ANISOU   49  NZ  LYS A   7     1560   6050   3159   -282    717   1506       N  
ATOM     50  N   ASP A   8       1.666  17.496  21.951  1.00  6.48           N  
ANISOU   50  N   ASP A   8     1087    683    694    -95    -19    111       N  
ATOM     51  CA  ASP A   8       1.608  17.088  20.572  1.00  6.24           C  
ANISOU   51  CA  ASP A   8     1002    661    709   -117     -6     69       C  
ATOM     52  C   ASP A   8       0.204  17.261  19.965  1.00  6.28           C  
ANISOU   52  C   ASP A   8     1071    589    726   -119    -32     54       C  
ATOM     53  O   ASP A   8       0.040  17.711  18.866  1.00  6.70           O  
ANISOU   53  O   ASP A   8     1081    696    770    -75   -106    126       O  
ATOM     54  CB  ASP A   8       2.056  15.655  20.373  1.00  7.13           C  
ANISOU   54  CB  ASP A   8     1132    688    891    -72    -82     27       C  
ATOM     55  CG  ASP A   8       3.532  15.407  20.614  1.00  8.85           C  
ANISOU   55  CG  ASP A   8     1040    967   1353    103    -97   -160       C  
ATOM     56  OD1 ASP A   8       4.304  16.297  20.933  1.00  9.30           O  
ANISOU   56  OD1 ASP A   8     1087   1156   1291    -51   -129   -144       O  
ATOM     57  OD2 ASP A   8       3.930  14.248  20.404  1.00 18.32           O  
ANISOU   57  OD2 ASP A   8     1228   1037   4695    170   -740   -726       O  
ATOM     58  N   ALA A   9      -0.846  16.877  20.748  1.00  6.88           N  
ANISOU   58  N   ALA A   9     1086    745    785   -164    -42    180       N  
ATOM     59  CA  ALA A   9      -2.166  16.932  20.185  1.00  7.78           C  
ANISOU   59  CA  ALA A   9     1010    842   1103   -212     15    158       C  
ATOM     60  C   ALA A   9      -2.551  18.390  19.874  1.00  7.07           C  
ANISOU   60  C   ALA A   9      926    811    950   -198     56    202       C  
ATOM     61  O   ALA A   9      -3.329  18.655  18.934  1.00  7.96           O  
ANISOU   61  O   ALA A   9     1053    834   1135   -196    -65    179       O  
ATOM     62  CB  ALA A   9      -3.195  16.352  21.115  1.00 10.73           C  
ANISOU   62  CB  ALA A   9     1117   1027   1932   -305     48    594       C  
ATOM     63  N   ASP A  10      -2.107  19.338  20.693  1.00  6.58           N  
ANISOU   63  N   ASP A  10      870    758    873   -111      3    153       N  
ATOM     64  CA  ASP A  10      -2.413  20.756  20.440  1.00  6.59           C  
ANISOU   64  CA  ASP A  10      975    811    719    -77     63    161       C  
ATOM     65  C   ASP A  10      -1.681  21.227  19.174  1.00  5.73           C  
ANISOU   65  C   ASP A  10      852    696    632   -125    -10      4       C  
ATOM     66  O   ASP A  10      -2.228  21.999  18.369  1.00  6.13           O  
ANISOU   66  O   ASP A  10      913    765    651     15    -29     99       O  
ATOM     67  CB  ASP A  10      -2.020  21.641  21.615  1.00  7.01           C  
ANISOU   67  CB  ASP A  10     1106    874    683    105    155     77       C  
ATOM     68  CG  ASP A  10      -2.842  21.430  22.877  1.00  8.41           C  
ANISOU   68  CG  ASP A  10     1156   1229    811    246    203    205       C  
ATOM     69  OD1 ASP A  10      -3.982  20.984  22.793  1.00 12.60           O  
ANISOU   69  OD1 ASP A  10     1029   2681   1078     27    249    253       O  
ATOM     70  OD2 ASP A  10      -2.314  21.782  23.941  1.00  9.54           O  
ANISOU   70  OD2 ASP A  10     1547   1374    704    223    227    119       O  
ATOM     71  N   VAL A  11      -0.424  20.824  19.029  1.00  5.52           N  
ANISOU   71  N   VAL A  11      835    663    601   -138    -18    -33       N  
ATOM     72  CA  VAL A  11       0.327  21.195  17.840  1.00  5.47           C  
ANISOU   72  CA  VAL A  11      857    651    571   -162    -56     11       C  
ATOM     73  C   VAL A  11      -0.357  20.634  16.582  1.00  5.19           C  
ANISOU   73  C   VAL A  11      688    673    609   -113    -41      8       C  
ATOM     74  O   VAL A  11      -0.547  21.331  15.585  1.00  5.39           O  
ANISOU   74  O   VAL A  11      861    639    546    -63    -65     18       O  
ATOM     75  CB  VAL A  11       1.801  20.743  17.938  1.00  5.64           C  
ANISOU   75  CB  VAL A  11      859    708    575   -204    -71     73       C  
ATOM     76  CG1 VAL A  11       2.536  21.077  16.653  1.00  6.16           C  
ANISOU   76  CG1 VAL A  11      914    790    635    -62     17     10       C  
ATOM     77  CG2 VAL A  11       2.449  21.442  19.165  1.00  7.18           C  
ANISOU   77  CG2 VAL A  11      958   1126    644   -322   -123      9       C  
ATOM     78  N   ALA A  12      -0.710  19.338  16.660  1.00  5.72           N  
ANISOU   78  N   ALA A  12      936    607    630   -170   -117     -2       N  
ATOM     79  CA  ALA A  12      -1.346  18.721  15.505  1.00  6.27           C  
ANISOU   79  CA  ALA A  12     1008    633    742    -87   -228    -44       C  
ATOM     80  C   ALA A  12      -2.685  19.388  15.177  1.00  6.35           C  
ANISOU   80  C   ALA A  12      969    627    818   -192   -234     50       C  
ATOM     81  O   ALA A  12      -3.038  19.569  13.992  1.00  7.30           O  
ANISOU   81  O   ALA A  12     1124    756    894   -218   -371     26       O  
ATOM     82  CB  ALA A  12      -1.546  17.240  15.808  1.00  8.71           C  
ANISOU   82  CB  ALA A  12     1458    582   1271   -215   -423    -66       C  
ATOM     83  N   ALA A  13      -3.445  19.776  16.213  1.00  6.95           N  
ANISOU   83  N   ALA A  13      838    900    904   -128   -115    138       N  
ATOM     84  CA  ALA A  13      -4.722  20.457  15.968  1.00  7.47           C  
ANISOU   84  CA  ALA A  13      850   1019    968   -205   -152    317       C  
ATOM     85  C   ALA A  13      -4.491  21.828  15.360  1.00  7.07           C  
ANISOU   85  C   ALA A  13      785    933    967    -42      4    204       C  
ATOM     86  O   ALA A  13      -5.262  22.245  14.495  1.00  7.79           O  
ANISOU   86  O   ALA A  13      882   1063   1014    -23   -211    137       O  
ATOM     87  CB  ALA A  13      -5.507  20.532  17.258  1.00  9.57           C  
ANISOU   87  CB  ALA A  13      942   1174   1520    -42    226    399       C  
ATOM     88  N   ALA A  14      -3.497  22.565  15.818  1.00  6.42           N  
ANISOU   88  N   ALA A  14      828    821    790     17     -5     59       N  
ATOM     89  CA  ALA A  14      -3.219  23.859  15.283  1.00  6.38           C  
ANISOU   89  CA  ALA A  14      871    709    845     90     59     76       C  
ATOM     90  C   ALA A  14      -2.826  23.786  13.813  1.00  5.96           C  
ANISOU   90  C   ALA A  14      827    620    817     97     61     41       C  
ATOM     91  O   ALA A  14      -3.216  24.630  13.008  1.00  6.87           O  
ANISOU   91  O   ALA A  14      966    769    875    200     47    108       O  
ATOM     92  CB  ALA A  14      -2.141  24.560  16.081  1.00  6.45           C  
ANISOU   92  CB  ALA A  14      950    674    828     45     24    -11       C  
ATOM     93  N   LEU A  15      -2.019  22.757  13.476  1.00  5.51           N  
ANISOU   93  N   LEU A  15      794    638    660     16    -79     -3       N  
ATOM     94  CA  LEU A  15      -1.640  22.566  12.085  1.00  5.48           C  
ANISOU   94  CA  LEU A  15      848    593    640     -7    -28    -64       C  
ATOM     95  C   LEU A  15      -2.852  22.208  11.240  1.00  5.95           C  
ANISOU   95  C   LEU A  15      859    587    817    -19    -84    -22       C  
ATOM     96  O   LEU A  15      -2.996  22.669  10.094  1.00  6.68           O  
ANISOU   96  O   LEU A  15      896    899    743     16   -130     87       O  
ATOM     97  CB  LEU A  15      -0.551  21.490  11.986  1.00  5.47           C  
ANISOU   97  CB  LEU A  15      851    550    679    -30    -85    -36       C  
ATOM     98  CG  LEU A  15       0.815  21.920  12.513  1.00  5.23           C  
ANISOU   98  CG  LEU A  15      757    577    653     15    -17    -46       C  
ATOM     99  CD1 LEU A  15       1.713  20.701  12.667  1.00  6.48           C  
ANISOU   99  CD1 LEU A  15      913    646    904     94    -76    -20       C  
ATOM    100  CD2 LEU A  15       1.442  22.968  11.607  1.00  6.54           C  
ANISOU  100  CD2 LEU A  15      804    701    979    -41    -66    153       C  
ATOM    101  N   ALA A  16      -3.741  21.356  11.734  1.00  6.65           N  
ANISOU  101  N   ALA A  16      947    694    887   -120   -268     85       N  
ATOM    102  CA  ALA A  16      -4.951  21.037  10.980  1.00  7.00           C  
ANISOU  102  CA  ALA A  16     1064    754    841   -126   -339    -44       C  
ATOM    103  C   ALA A  16      -5.813  22.306  10.770  1.00  6.80           C  
ANISOU  103  C   ALA A  16      882    785    915   -187   -265     77       C  
ATOM    104  O   ALA A  16      -6.416  22.460   9.715  1.00  7.34           O  
ANISOU  104  O   ALA A  16      956    893    941   -160   -285    104       O  
ATOM    105  CB  ALA A  16      -5.700  19.928  11.650  1.00  8.96           C  
ANISOU  105  CB  ALA A  16     1124    975   1305   -389   -494    265       C  
ATOM    106  N   ALA A  17      -5.859  23.180  11.764  1.00  6.96           N  
ANISOU  106  N   ALA A  17      859    846    940    -84   -172     39       N  
ATOM    107  CA  ALA A  17      -6.726  24.348  11.684  1.00  7.26           C  
ANISOU  107  CA  ALA A  17      764    956   1038    -29    -53    -42       C  
ATOM    108  C   ALA A  17      -6.274  25.341  10.626  1.00  7.03           C  
ANISOU  108  C   ALA A  17      814    831   1028     47   -196    -17       C  
ATOM    109  O   ALA A  17      -7.081  26.154  10.152  1.00  8.92           O  
ANISOU  109  O   ALA A  17      849   1121   1418     93   -138    258       O  
ATOM    110  CB  ALA A  17      -6.759  25.047  13.039  1.00  8.67           C  
ANISOU  110  CB  ALA A  17     1056   1204   1036     22    -15   -152       C  
ATOM    111  N   CYS A  18      -5.011  25.281  10.224  1.00  6.50           N  
ANISOU  111  N   CYS A  18      824    688    958     49   -142    121       N  
ATOM    112  CA  CYS A  18      -4.503  26.160   9.139  1.00  6.20           C  
ANISOU  112  CA  CYS A  18      903    646    808     28   -104     85       C  
ATOM    113  C   CYS A  18      -4.111  25.393   7.907  1.00  5.90           C  
ANISOU  113  C   CYS A  18      730    602    909    -44   -202     49       C  
ATOM    114  O   CYS A  18      -3.306  25.878   7.111  1.00  6.37           O  
ANISOU  114  O   CYS A  18      841    673    906    -48    -55     44       O  
ATOM    115  CB  CYS A  18      -3.396  27.073   9.644  1.00  6.69           C  
ANISOU  115  CB  CYS A  18     1149    572    820    -76   -175     88       C  
ATOM    116  SG  CYS A  18      -1.881  26.275  10.194  1.00  7.04           S  
ANISOU  116  SG  CYS A  18      914    818    944   -164   -186     71       S  
ATOM    117  N   SER A  19      -4.723  24.223   7.681  1.00  6.07           N  
ANISOU  117  N   SER A  19      809    585    913    -38   -100     15       N  
ATOM    118  CA  SER A  19      -4.374  23.412   6.552  1.00  6.13           C  
ANISOU  118  CA  SER A  19      784    607    938    -31    -87     32       C  
ATOM    119  C   SER A  19      -4.628  24.087   5.205  1.00  6.27           C  
ANISOU  119  C   SER A  19      842    626    912    -18    -88    -92       C  
ATOM    120  O   SER A  19      -3.851  23.865   4.293  1.00  7.64           O  
ANISOU  120  O   SER A  19     1172    773    959     82     84     20       O  
ATOM    121  CB  SER A  19      -5.130  22.067   6.615  1.00  6.54           C  
ANISOU  121  CB  SER A  19      850    548   1088    -31   -172     -9       C  
ATOM    122  OG  SER A  19      -6.535  22.247   6.641  1.00  6.57           O  
ANISOU  122  OG  SER A  19      835    747    915   -102    -36    -82       O  
ATOM    123  N   ALA A  20      -5.671  24.896   5.083  1.00  6.55           N  
ANISOU  123  N   ALA A  20      941    709    838    -37   -111     14       N  
ATOM    124  CA  ALA A  20      -5.968  25.588   3.847  1.00  6.51           C  
ANISOU  124  CA  ALA A  20      979    743    750    -39   -112    -27       C  
ATOM    125  C   ALA A  20      -5.067  26.798   3.677  1.00  6.70           C  
ANISOU  125  C   ALA A  20      952    751    843     20   -186    -36       C  
ATOM    126  O   ALA A  20      -4.868  27.585   4.589  1.00  6.49           O  
ANISOU  126  O   ALA A  20      893    739    834   -116    -97    -49       O  
ATOM    127  CB  ALA A  20      -7.413  26.076   3.802  1.00  7.10           C  
ANISOU  127  CB  ALA A  20      996    815    887   -109   -264    -35       C  
ATOM    128  N   ALA A  21      -4.547  26.985   2.456  1.00  8.00           N  
ANISOU  128  N   ALA A  21     1335    754    949   -223    197   -179       N  
ATOM    129  CA  ALA A  21      -3.758  28.172   2.158  1.00  8.04           C  
ANISOU  129  CA  ALA A  21     1199    784   1073   -157    106   -106       C  
ATOM    130  C   ALA A  21      -4.609  29.406   2.444  1.00  6.50           C  
ANISOU  130  C   ALA A  21      915    855    702   -106   -112     24       C  
ATOM    131  O   ALA A  21      -5.804  29.461   2.151  1.00  8.66           O  
ANISOU  131  O   ALA A  21     1100   1264    927   -121   -202    111       O  
ATOM    132  CB  ALA A  21      -3.329  28.172   0.697  1.00 12.03           C  
ANISOU  132  CB  ALA A  21     2371    997   1201   -576    637   -307       C  
ATOM    133  N   ASP A  22      -3.979  30.407   3.068  1.00  6.50           N  
ANISOU  133  N   ASP A  22     1029    697    742    -24   -137     58       N  
ATOM    134  CA  ASP A  22      -4.531  31.687   3.446  1.00  7.42           C  
ANISOU  134  CA  ASP A  22     1134    783    901     78   -161     60       C  
ATOM    135  C   ASP A  22      -5.452  31.612   4.652  1.00  7.18           C  
ANISOU  135  C   ASP A  22     1059    745    924    122   -114    113       C  
ATOM    136  O   ASP A  22      -5.974  32.646   5.027  1.00  9.99           O  
ANISOU  136  O   ASP A  22     1596   1033   1167    427    209    134       O  
ATOM    137  CB  ASP A  22      -5.101  32.467   2.266  1.00  8.80           C  
ANISOU  137  CB  ASP A  22     1209   1100   1034    183   -181    284       C  
ATOM    138  CG  ASP A  22      -3.937  32.917   1.392  1.00 10.71           C  
ANISOU  138  CG  ASP A  22     1387   1575   1107   -129   -290    508       C  
ATOM    139  OD1 ASP A  22      -2.951  33.459   1.892  1.00 10.29           O  
ANISOU  139  OD1 ASP A  22     1119   1178   1612    107   -161     31       O  
ATOM    140  OD2 ASP A  22      -3.996  32.728   0.172  1.00 24.02           O  
ANISOU  140  OD2 ASP A  22     2299   5834    994  -1344   -354    588       O  
ATOM    141  N   SER A  23      -5.511  30.457   5.328  1.00  6.48           N  
ANISOU  141  N   SER A  23      909    758    794    -30   -156     -1       N  
ATOM    142  CA  SER A  23      -6.247  30.345   6.587  1.00  6.38           C  
ANISOU  142  CA  SER A  23      757    783    884     -4   -199     27       C  
ATOM    143  C   SER A  23      -5.394  30.534   7.829  1.00  6.07           C  
ANISOU  143  C   SER A  23      892    674    739    -37    -81    -65       C  
ATOM    144  O   SER A  23      -5.950  30.559   8.932  1.00  7.23           O  
ANISOU  144  O   SER A  23      894   1082    772    -59    -34    -75       O  
ATOM    145  CB  SER A  23      -6.948  28.985   6.667  1.00  7.08           C  
ANISOU  145  CB  SER A  23      881    934    875    -60   -162     90       C  
ATOM    146  OG  SER A  23      -6.057  27.933   6.970  1.00  7.31           O  
ANISOU  146  OG  SER A  23     1136    740    900    -48   -120     65       O  
ATOM    147  N   PHE A  24      -4.076  30.637   7.695  1.00  6.14           N  
ANISOU  147  N   PHE A  24      727    777    828     95    -33    -78       N  
ATOM    148  CA  PHE A  24      -3.237  30.799   8.875  1.00  5.84           C  
ANISOU  148  CA  PHE A  24      762    683    775     55    -49    -12       C  
ATOM    149  C   PHE A  24      -3.491  32.146   9.474  1.00  5.58           C  
ANISOU  149  C   PHE A  24      702    664    756    -17    -37     40       C  
ATOM    150  O   PHE A  24      -3.536  33.172   8.770  1.00  6.81           O  
ANISOU  150  O   PHE A  24      962    719    907      9    -98    177       O  
ATOM    151  CB  PHE A  24      -1.783  30.646   8.502  1.00  6.61           C  
ANISOU  151  CB  PHE A  24      840    924    747     54     11   -145       C  
ATOM    152  CG  PHE A  24      -0.795  30.904   9.617  1.00  5.70           C  
ANISOU  152  CG  PHE A  24      702    772    692    132     17    -37       C  
ATOM    153  CD1 PHE A  24      -0.527  29.966  10.589  1.00  5.94           C  
ANISOU  153  CD1 PHE A  24      748    680    830     14     78    -26       C  
ATOM    154  CD2 PHE A  24      -0.109  32.091   9.662  1.00  6.02           C  
ANISOU  154  CD2 PHE A  24      786    779    722     67     63    117       C  
ATOM    155  CE1 PHE A  24       0.428  30.203  11.560  1.00  5.77           C  
ANISOU  155  CE1 PHE A  24      772    772    650    181     14     19       C  
ATOM    156  CE2 PHE A  24       0.837  32.343  10.650  1.00  6.20           C  
ANISOU  156  CE2 PHE A  24      726    734    895     21    100      5       C  
ATOM    157  CZ  PHE A  24       1.112  31.389  11.584  1.00  5.96           C  
ANISOU  157  CZ  PHE A  24      673    852    740    114    -15   -133       C  
ATOM    158  N   LYS A  25      -3.621  32.176  10.801  1.00  5.57           N  
ANISOU  158  N   LYS A  25      695    643    778     48    -59     25       N  
ATOM    159  CA  LYS A  25      -3.748  33.411  11.603  1.00  6.22           C  
ANISOU  159  CA  LYS A  25      883    636    842     71   -115    -15       C  
ATOM    160  C   LYS A  25      -2.780  33.210  12.749  1.00  5.98           C  
ANISOU  160  C   LYS A  25      752    630    890     82   -134    -26       C  
ATOM    161  O   LYS A  25      -3.054  32.393  13.651  1.00  6.19           O  
ANISOU  161  O   LYS A  25      830    744    776      3    -57      5       O  
ATOM    162  CB  LYS A  25      -5.194  33.585  12.054  1.00  8.06           C  
ANISOU  162  CB  LYS A  25      960   1142    959    349   -107   -206       C  
ATOM    163  CG  LYS A  25      -6.140  33.787  10.880  1.00  8.28           C  
ANISOU  163  CG  LYS A  25      866   1234   1046    401   -122   -244       C  
ATOM    164  CD  LYS A  25      -7.594  33.826  11.319  1.00 11.31           C  
ANISOU  164  CD  LYS A  25      919   2246   1131    498     26   -308       C  
ATOM    165  CE  LYS A  25      -8.593  34.114  10.236  1.00 13.25           C  
ANISOU  165  CE  LYS A  25     1136   2770   1127    556   -118   -363       C  
ATOM    166  NZ  LYS A  25      -8.548  33.128   9.154  1.00 14.71           N  
ANISOU  166  NZ  LYS A  25     1222   2891   1477    253    -51   -665       N  
ATOM    167  N   HIS A  26      -1.632  33.889  12.743  1.00  6.21           N  
ANISOU  167  N   HIS A  26      832    720    808     14    -30    102       N  
ATOM    168  CA  HIS A  26      -0.600  33.599  13.734  1.00  5.75           C  
ANISOU  168  CA  HIS A  26      693    629    865     40    -33     34       C  
ATOM    169  C   HIS A  26      -1.099  33.688  15.148  1.00  5.57           C  
ANISOU  169  C   HIS A  26      646    643    828     -3    -26    -87       C  
ATOM    170  O   HIS A  26      -0.732  32.849  15.965  1.00  5.84           O  
ANISOU  170  O   HIS A  26      721    684    813    -18     20    -34       O  
ATOM    171  CB  HIS A  26       0.643  34.443  13.505  1.00  6.66           C  
ANISOU  171  CB  HIS A  26      767    826    937    -31     13    -15       C  
ATOM    172  CG  HIS A  26       0.378  35.905  13.375  1.00 10.41           C  
ANISOU  172  CG  HIS A  26      670    797   2489   -110    223    -50       C  
ATOM    173  ND1 HIS A  26      -0.083  36.435  12.220  1.00 16.77           N  
ANISOU  173  ND1 HIS A  26     1121   1173   4079    -55   -330   1196       N  
ATOM    174  CD2 HIS A  26       0.565  36.872  14.312  1.00 17.31           C  
ANISOU  174  CD2 HIS A  26     1783   1051   3745   -440   1587  -1005       C  
ATOM    175  CE1 HIS A  26      -0.212  37.736  12.449  1.00 24.01           C  
ANISOU  175  CE1 HIS A  26     1577   1131   6415    303   1457   1474       C  
ATOM    176  NE2 HIS A  26       0.173  38.006  13.693  1.00 25.02           N  
ANISOU  176  NE2 HIS A  26     2309    789   6408   -154   2696   -264       N  
ATOM    177  N   LYS A  27      -1.935  34.678  15.488  1.00  6.25           N  
ANISOU  177  N   LYS A  27      790    610    975     83     -1   -108       N  
ATOM    178  CA  LYS A  27      -2.373  34.783  16.869  1.00  7.24           C  
ANISOU  178  CA  LYS A  27      912    835   1004      8    172   -259       C  
ATOM    179  C   LYS A  27      -3.300  33.609  17.242  1.00  6.26           C  
ANISOU  179  C   LYS A  27      739    778    862    115     30   -163       C  
ATOM    180  O   LYS A  27      -3.301  33.157  18.387  1.00  7.19           O  
ANISOU  180  O   LYS A  27      775   1012    944    -25     88   -206       O  
ATOM    181  CB  LYS A  27      -2.985  36.136  17.173  1.00 11.34           C  
ANISOU  181  CB  LYS A  27     1700    741   1867     10    838   -370       C  
ATOM    182  CG  LYS A  27      -1.804  37.171  17.273  1.00 17.41           C  
ANISOU  182  CG  LYS A  27     1821   1317   3475   -390   1465   -350       C  
ATOM    183  CD  LYS A  27      -2.224  38.580  17.469  1.00 17.34           C  
ANISOU  183  CD  LYS A  27     2485   1255   2849   -605   1381   -567       C  
ATOM    184  CE ALYS A  27      -1.005  39.463  17.746  0.48 13.04           C  
ANISOU  184  CE ALYS A  27     1734   1150   2071    312   -330    193       C  
ATOM    185  CE BLYS A  27      -1.024  39.493  17.619  0.52 13.39           C  
ANISOU  185  CE BLYS A  27     1527   1374   2187   -112   1261   -262       C  
ATOM    186  NZ ALYS A  27      -1.370  40.910  17.483  0.48  9.47           N  
ANISOU  186  NZ ALYS A  27      948    999   1654     28    182     18       N  
ATOM    187  NZ BLYS A  27      -0.739  39.951  18.999  0.52 13.21           N  
ANISOU  187  NZ BLYS A  27      818   2366   1835    505    170    645       N  
ATOM    188  N   GLU A  28      -4.094  33.127  16.291  1.00  6.28           N  
ANISOU  188  N   GLU A  28      640    756    988     84    -44    -69       N  
ATOM    189  CA  GLU A  28      -4.906  31.951  16.556  1.00  6.43           C  
ANISOU  189  CA  GLU A  28      573    887    984    109     -8     -3       C  
ATOM    190  C   GLU A  28      -4.016  30.696  16.743  1.00  5.62           C  
ANISOU  190  C   GLU A  28      557    785    795     17      4    -11       C  
ATOM    191  O   GLU A  28      -4.285  29.884  17.619  1.00  6.56           O  
ANISOU  191  O   GLU A  28      635    939    920     57    150     74       O  
ATOM    192  CB  GLU A  28      -5.954  31.706  15.463  1.00  6.75           C  
ANISOU  192  CB  GLU A  28      571    895   1099     67    -69    -29       C  
ATOM    193  CG  GLU A  28      -6.989  32.793  15.438  1.00  7.34           C  
ANISOU  193  CG  GLU A  28      722   1008   1059    180   -116    -82       C  
ATOM    194  CD  GLU A  28      -8.207  32.465  14.586  1.00  8.02           C  
ANISOU  194  CD  GLU A  28      665   1023   1361    143   -170   -155       C  
ATOM    195  OE1 GLU A  28      -8.245  31.364  13.987  1.00 10.29           O  
ANISOU  195  OE1 GLU A  28      866   1324   1718    230   -318   -519       O  
ATOM    196  OE2 GLU A  28      -9.155  33.250  14.554  1.00  9.37           O  
ANISOU  196  OE2 GLU A  28      763   1293   1503    323   -238   -325       O  
ATOM    197  N   PHE A  29      -2.999  30.574  15.889  1.00  5.30           N  
ANISOU  197  N   PHE A  29      567    762    685      4     22    -46       N  
ATOM    198  CA  PHE A  29      -2.081  29.450  16.018  1.00  4.91           C  
ANISOU  198  CA  PHE A  29      582    615    667     -3     26    -62       C  
ATOM    199  C   PHE A  29      -1.404  29.475  17.390  1.00  4.78           C  
ANISOU  199  C   PHE A  29      524    639    653    -24     55    -30       C  
ATOM    200  O   PHE A  29      -1.283  28.445  18.065  1.00  5.12           O  
ANISOU  200  O   PHE A  29      620    687    638      3      1    -14       O  
ATOM    201  CB  PHE A  29      -1.049  29.524  14.868  1.00  4.98           C  
ANISOU  201  CB  PHE A  29      589    698    606     30    -14     18       C  
ATOM    202  CG  PHE A  29      -0.112  28.345  14.851  1.00  5.59           C  
ANISOU  202  CG  PHE A  29      705    806    614    122    139    137       C  
ATOM    203  CD1 PHE A  29       1.033  28.305  15.587  1.00  7.97           C  
ANISOU  203  CD1 PHE A  29      586   1359   1084    141    122    525       C  
ATOM    204  CD2 PHE A  29      -0.400  27.260  14.055  1.00  7.37           C  
ANISOU  204  CD2 PHE A  29     1137    760    902    122    302     20       C  
ATOM    205  CE1 PHE A  29       1.884  27.212  15.557  1.00 11.56           C  
ANISOU  205  CE1 PHE A  29      783   1952   1657    499    376   1000       C  
ATOM    206  CE2 PHE A  29       0.440  26.156  14.046  1.00 10.74           C  
ANISOU  206  CE2 PHE A  29     1811    891   1378    508    863    356       C  
ATOM    207  CZ  PHE A  29       1.582  26.128  14.775  1.00 12.72           C  
ANISOU  207  CZ  PHE A  29     1643   1429   1763    889    895    933       C  
ATOM    208  N   PHE A  30      -0.919  30.648  17.811  1.00  5.33           N  
ANISOU  208  N   PHE A  30      701    709    616    -40     -1    -45       N  
ATOM    209  CA APHE A  30      -0.253  30.781  19.092  0.41  5.91           C  
ANISOU  209  CA APHE A  30      748    907    589   -100      0   -123       C  
ATOM    210  CA BPHE A  30      -0.199  30.689  19.092  0.59  5.68           C  
ANISOU  210  CA BPHE A  30      781    757    622   -116    -43    -17       C  
ATOM    211  C   PHE A  30      -1.135  30.286  20.241  1.00  5.62           C  
ANISOU  211  C   PHE A  30      858    671    605    -16    -10   -106       C  
ATOM    212  O   PHE A  30      -0.631  29.652  21.178  1.00  6.45           O  
ANISOU  212  O   PHE A  30      922    879    650     59     38      8       O  
ATOM    213  CB APHE A  30       0.054  32.250  19.451  0.41  6.28           C  
ANISOU  213  CB APHE A  30      841    896    650    -79    -50   -136       C  
ATOM    214  CB BPHE A  30       0.370  32.114  19.277  0.59  6.84           C  
ANISOU  214  CB BPHE A  30     1000    889    711   -203     -8   -106       C  
ATOM    215  CG APHE A  30       0.948  32.981  18.508  0.41  6.50           C  
ANISOU  215  CG APHE A  30      719    876    876   -174    -66   -219       C  
ATOM    216  CG BPHE A  30       1.583  32.458  18.472  0.59  7.42           C  
ANISOU  216  CG BPHE A  30     1019   1141    661   -401     28   -198       C  
ATOM    217  CD1APHE A  30       1.893  32.342  17.752  0.41  8.04           C  
ANISOU  217  CD1APHE A  30      568   1140   1348   -160    105   -248       C  
ATOM    218  CD1BPHE A  30       2.667  31.620  18.314  0.59  8.37           C  
ANISOU  218  CD1BPHE A  30     1032   1313    838   -334    213   -442       C  
ATOM    219  CD2APHE A  30       0.834  34.371  18.371  0.41  6.74           C  
ANISOU  219  CD2APHE A  30      797    984    782    -32    -54     43       C  
ATOM    220  CD2BPHE A  30       1.662  33.713  17.869  0.59  8.95           C  
ANISOU  220  CD2BPHE A  30     1073   1508    821   -546   -398    312       C  
ATOM    221  CE1APHE A  30       2.692  33.046  16.880  0.41  9.56           C  
ANISOU  221  CE1APHE A  30     1012   1535   1085   -319    172   -274       C  
ATOM    222  CE1BPHE A  30       3.803  32.019  17.601  0.59 10.36           C  
ANISOU  222  CE1BPHE A  30     1105   1883    951   -583    156   -512       C  
ATOM    223  CE2APHE A  30       1.629  35.078  17.503  0.41  8.53           C  
ANISOU  223  CE2APHE A  30      985   1225   1033   -528     63   -111       C  
ATOM    224  CE2BPHE A  30       2.759  34.148  17.150  0.59 10.38           C  
ANISOU  224  CE2BPHE A  30     1388   1904    652   -907   -493    422       C  
ATOM    225  CZ APHE A  30       2.570  34.414  16.743  0.41  9.60           C  
ANISOU  225  CZ APHE A  30     1221   1498    930   -484    238   -102       C  
ATOM    226  CZ BPHE A  30       3.858  33.294  17.027  0.59 11.42           C  
ANISOU  226  CZ BPHE A  30     1130   2572    638   -884   -171     92       C  
ATOM    227  N   ALA A  31      -2.412  30.620  20.185  1.00  5.82           N  
ANISOU  227  N   ALA A  31      870    673    669     -4    105     20       N  
ATOM    228  CA  ALA A  31      -3.342  30.170  21.221  1.00  6.70           C  
ANISOU  228  CA  ALA A  31      981    748    815     33    213   -106       C  
ATOM    229  C   ALA A  31      -3.538  28.670  21.139  1.00  6.38           C  
ANISOU  229  C   ALA A  31      841    725    859     65    231     15       C  
ATOM    230  O   ALA A  31      -3.453  27.973  22.146  1.00  6.62           O  
ANISOU  230  O   ALA A  31      928    816    772     67     83     59       O  
ATOM    231  CB  ALA A  31      -4.646  30.928  21.077  1.00  8.74           C  
ANISOU  231  CB  ALA A  31     1087   1033   1200    273    461      5       C  
ATOM    232  N   LYS A  32      -3.855  28.160  19.950  1.00  6.03           N  
ANISOU  232  N   LYS A  32      858    679    755     15    174     52       N  
ATOM    233  CA  LYS A  32      -4.215  26.743  19.808  1.00  6.56           C  
ANISOU  233  CA  LYS A  32      795    743    954     -9    143     18       C  
ATOM    234  C   LYS A  32      -3.079  25.840  20.183  1.00  6.30           C  
ANISOU  234  C   LYS A  32      756    674    962    -78     46      3       C  
ATOM    235  O   LYS A  32      -3.292  24.777  20.752  1.00  7.67           O  
ANISOU  235  O   LYS A  32      749    754   1410    -30    162    149       O  
ATOM    236  CB  LYS A  32      -4.712  26.504  18.396  1.00  7.55           C  
ANISOU  236  CB  LYS A  32     1149    847    874     35     63    -75       C  
ATOM    237  CG  LYS A  32      -5.309  25.137  18.183  1.00  9.08           C  
ANISOU  237  CG  LYS A  32     1143   1144   1161     24     69   -277       C  
ATOM    238  CD  LYS A  32      -6.540  24.871  19.016  1.00 16.22           C  
ANISOU  238  CD  LYS A  32     1316   1858   2990   -681    631  -1063       C  
ATOM    239  CE  LYS A  32      -7.083  23.453  18.801  1.00 24.33           C  
ANISOU  239  CE  LYS A  32     1691   1842   5711   -771    727  -1142       C  
ATOM    240  NZ  LYS A  32      -8.125  23.161  19.823  1.00 34.66           N  
ANISOU  240  NZ  LYS A  32     3072   2146   7952  -1421   2220   -897       N  
ATOM    241  N   VAL A  33      -1.843  26.214  19.825  1.00  6.28           N  
ANISOU  241  N   VAL A  33      765    689    932    -42    188   -156       N  
ATOM    242  CA AVAL A  33      -0.756  25.292  20.149  0.58  7.87           C  
ANISOU  242  CA AVAL A  33      776    862   1353    -16    100   -341       C  
ATOM    243  CA BVAL A  33      -0.662  25.399  20.085  0.42  6.75           C  
ANISOU  243  CA BVAL A  33      748    467   1349    -89    180   -335       C  
ATOM    244  C   VAL A  33      -0.301  25.373  21.591  1.00  6.98           C  
ANISOU  244  C   VAL A  33      653    662   1338    -19    141    -64       C  
ATOM    245  O   VAL A  33       0.458  24.517  22.012  1.00  9.20           O  
ANISOU  245  O   VAL A  33      861    791   1845    159     63     53       O  
ATOM    246  CB AVAL A  33       0.637  25.454  19.498  0.58  6.28           C  
ANISOU  246  CB AVAL A  33      801    693    891    140    -94    -28       C  
ATOM    247  CB BVAL A  33       0.369  25.907  19.038  0.42  5.69           C  
ANISOU  247  CB BVAL A  33      557    693    912     57    -57   -304       C  
ATOM    248  CG1AVAL A  33       0.381  25.228  18.025  0.58  6.46           C  
ANISOU  248  CG1AVAL A  33     1024    582    851    102   -157    -57       C  
ATOM    249  CG1BVAL A  33       1.270  27.020  19.608  0.42  8.25           C  
ANISOU  249  CG1BVAL A  33      752    912   1471   -367    358   -707       C  
ATOM    250  CG2AVAL A  33       1.220  26.838  19.650  0.58  6.02           C  
ANISOU  250  CG2AVAL A  33      683   1037    568    -47     47   -134       C  
ATOM    251  CG2BVAL A  33       1.293  24.796  18.573  0.42  4.81           C  
ANISOU  251  CG2BVAL A  33      702    551    573    140    -47    -68       C  
ATOM    252  N   GLY A  34      -0.780  26.382  22.320  1.00  6.81           N  
ANISOU  252  N   GLY A  34      823    768    996     65    -41     19       N  
ATOM    253  CA  GLY A  34      -0.499  26.533  23.746  1.00  7.62           C  
ANISOU  253  CA  GLY A  34      976    886   1032      0      6     80       C  
ATOM    254  C   GLY A  34       0.534  27.565  24.071  1.00  6.86           C  
ANISOU  254  C   GLY A  34      762    932    914     84    -78     -9       C  
ATOM    255  O   GLY A  34       0.817  27.766  25.270  1.00  8.26           O  
ANISOU  255  O   GLY A  34     1061   1153    924    -43    -36     38       O  
ATOM    256  N   LEU A  35       1.143  28.233  23.118  1.00  6.40           N  
ANISOU  256  N   LEU A  35      749    861    820     78    -17    -52       N  
ATOM    257  CA  LEU A  35       2.189  29.217  23.396  1.00  6.60           C  
ANISOU  257  CA  LEU A  35      749    952    808     50     13   -166       C  
ATOM    258  C   LEU A  35       1.642  30.467  24.112  1.00  6.49           C  
ANISOU  258  C   LEU A  35      785    852    830   -124    108    -53       C  
ATOM    259  O   LEU A  35       2.332  31.022  24.941  1.00  7.22           O  
ANISOU  259  O   LEU A  35      873   1076    795   -137     29   -152       O  
ATOM    260  CB ALEU A  35       2.948  29.653  22.143  0.77  7.74           C  
ANISOU  260  CB ALEU A  35      726   1204   1011     93    163    -51       C  
ATOM    261  CB BLEU A  35       2.918  29.669  22.132  0.23  6.73           C  
ANISOU  261  CB BLEU A  35     1109    592    856   -112     40   -215       C  
ATOM    262  CG ALEU A  35       4.043  28.693  21.737  0.77  7.64           C  
ANISOU  262  CG ALEU A  35      782    818   1301    -63    243   -224       C  
ATOM    263  CG BLEU A  35       4.403  30.017  22.297  0.23 13.64           C  
ANISOU  263  CG BLEU A  35     1006   1636   2540   -154    303    158       C  
ATOM    264  CD1ALEU A  35       4.503  29.017  20.310  0.77  9.81           C  
ANISOU  264  CD1ALEU A  35     1073   1288   1366   -309    584   -464       C  
ATOM    265  CD1BLEU A  35       5.096  29.032  23.231  0.23 16.36           C  
ANISOU  265  CD1BLEU A  35      494   2570   3153    301    250    429       C  
ATOM    266  CD2ALEU A  35       5.236  28.723  22.679  0.77 10.96           C  
ANISOU  266  CD2ALEU A  35      632   1721   1812    169    123    152       C  
ATOM    267  CD2BLEU A  35       5.095  30.057  20.954  0.23 11.42           C  
ANISOU  267  CD2BLEU A  35      697   1084   2557    115    248   -540       C  
ATOM    268  N   ALA A  36       0.431  30.880  23.772  1.00  7.22           N  
ANISOU  268  N   ALA A  36      875    872    996     23     -5   -120       N  
ATOM    269  CA  ALA A  36      -0.136  32.049  24.442  1.00  8.16           C  
ANISOU  269  CA  ALA A  36     1122    848   1129     21    103   -262       C  
ATOM    270  C   ALA A  36      -0.311  31.824  25.965  1.00  8.60           C  
ANISOU  270  C   ALA A  36     1011   1221   1034    214     27   -330       C  
ATOM    271  O   ALA A  36      -0.332  32.824  26.672  1.00 12.06           O  
ANISOU  271  O   ALA A  36     1712   1415   1455    192    -55   -650       O  
ATOM    272  CB  ALA A  36      -1.427  32.468  23.803  1.00  9.07           C  
ANISOU  272  CB  ALA A  36     1228    912   1308    123    -98   -141       C  
ATOM    273  N   SER A  37      -0.393  30.587  26.414  1.00  8.48           N  
ANISOU  273  N   SER A  37      932   1297    992    -47    133   -168       N  
ATOM    274  CA ASER A  37      -0.559  30.202  27.813  0.61  9.54           C  
ANISOU  274  CA ASER A  37     1028   1534   1061    153    211   -191       C  
ATOM    275  CA BSER A  37      -0.545  30.349  27.852  0.40 10.01           C  
ANISOU  275  CA BSER A  37      897   1832   1076   -204    160   -119       C  
ATOM    276  C   SER A  37       0.759  29.925  28.492  1.00  8.82           C  
ANISOU  276  C   SER A  37     1176   1300    875    -13    157   -155       C  
ATOM    277  O   SER A  37       0.746  29.619  29.681  1.00 11.82           O  
ANISOU  277  O   SER A  37     1516   2064    912     -6    173     11       O  
ATOM    278  CB ASER A  37      -1.445  28.942  27.877  0.61 11.52           C  
ANISOU  278  CB ASER A  37     1196   2326    855   -445    411     49       C  
ATOM    279  CB BSER A  37      -1.602  29.277  28.095  0.40 13.55           C  
ANISOU  279  CB BSER A  37     1469   2582   1097   -819    340   -130       C  
ATOM    280  OG ASER A  37      -2.763  29.307  27.447  0.61 14.79           O  
ANISOU  280  OG ASER A  37     1236   2995   1389   -476     68    396       O  
ATOM    281  OG BSER A  37      -1.239  28.071  27.460  0.40 25.02           O  
ANISOU  281  OG BSER A  37     3512   2594   3400  -1161   -441  -1395       O  
ATOM    282  N   LYS A  38       1.889  29.926  27.754  1.00  8.38           N  
ANISOU  282  N   LYS A  38      988   1305    892    173     56     40       N  
ATOM    283  CA  LYS A  38       3.203  29.712  28.341  1.00  8.90           C  
ANISOU  283  CA  LYS A  38     1180   1209    993    238     -2     44       C  
ATOM    284  C   LYS A  38       3.724  30.949  29.026  1.00  8.29           C  
ANISOU  284  C   LYS A  38     1051   1289    810    161     55    112       C  
ATOM    285  O   LYS A  38       3.417  32.080  28.652  1.00  9.08           O  
ANISOU  285  O   LYS A  38     1314   1339    797    394    -51   -162       O  
ATOM    286  CB  LYS A  38       4.197  29.256  27.257  1.00  9.06           C  
ANISOU  286  CB  LYS A  38     1120   1356    967    166    -34    -33       C  
ATOM    287  CG  LYS A  38       4.023  27.826  26.792  1.00  9.89           C  
ANISOU  287  CG  LYS A  38     1317   1467    974    330     45    -82       C  
ATOM    288  CD  LYS A  38       4.591  26.859  27.882  1.00 12.30           C  
ANISOU  288  CD  LYS A  38     1938   1616   1120    749     -1    -21       C  
ATOM    289  CE  LYS A  38       4.660  25.452  27.379  1.00 12.97           C  
ANISOU  289  CE  LYS A  38     1614   1637   1678    655   -571   -417       C  
ATOM    290  NZ  LYS A  38       5.433  24.593  28.353  1.00 13.46           N  
ANISOU  290  NZ  LYS A  38     2365   1359   1389    728   -560   -493       N  
ATOM    291  N   SER A  39       4.621  30.733  30.005  1.00  8.81           N  
ANISOU  291  N   SER A  39     1290   1334    724    224     33     20       N  
ATOM    292  CA  SER A  39       5.347  31.791  30.636  1.00  8.88           C  
ANISOU  292  CA  SER A  39     1304   1330    741    313     23    -64       C  
ATOM    293  C   SER A  39       6.199  32.560  29.614  1.00  7.78           C  
ANISOU  293  C   SER A  39      906   1294    755    248   -144   -188       C  
ATOM    294  O   SER A  39       6.647  32.017  28.613  1.00  8.07           O  
ANISOU  294  O   SER A  39      937   1396    732    275     -9   -346       O  
ATOM    295  CB  SER A  39       6.283  31.304  31.744  1.00 11.37           C  
ANISOU  295  CB  SER A  39     2000   1555    766    167   -204   -129       C  
ATOM    296  OG  SER A  39       7.271  30.526  31.275  1.00 15.52           O  
ANISOU  296  OG  SER A  39     2377   1869   1649    786  -1055   -524       O  
ATOM    297  N   LEU A  40       6.558  33.777  29.982  1.00  8.20           N  
ANISOU  297  N   LEU A  40     1100   1411    603    179     -3   -173       N  
ATOM    298  CA  LEU A  40       7.496  34.538  29.147  1.00  8.02           C  
ANISOU  298  CA  LEU A  40     1142   1236    668    275     76   -151       C  
ATOM    299  C   LEU A  40       8.800  33.785  28.937  1.00  7.90           C  
ANISOU  299  C   LEU A  40     1108   1185    708    170    -20   -282       C  
ATOM    300  O   LEU A  40       9.315  33.755  27.794  1.00  7.81           O  
ANISOU  300  O   LEU A  40     1086   1020    862    131     72   -310       O  
ATOM    301  CB  LEU A  40       7.762  35.925  29.783  1.00  9.19           C  
ANISOU  301  CB  LEU A  40     1519   1258    715    324     93   -228       C  
ATOM    302  CG  LEU A  40       8.758  36.769  29.022  1.00 10.07           C  
ANISOU  302  CG  LEU A  40     1620   1125   1082    224     21   -237       C  
ATOM    303  CD1 LEU A  40       8.283  37.027  27.612  1.00 10.31           C  
ANISOU  303  CD1 LEU A  40     1444   1346   1128    280     68     41       C  
ATOM    304  CD2 LEU A  40       8.982  38.057  29.799  1.00 14.07           C  
ANISOU  304  CD2 LEU A  40     2534   1245   1567     91    -34   -406       C  
ATOM    305  N   ASP A  41       9.339  33.170  29.967  1.00  9.38           N  
ANISOU  305  N   ASP A  41     1164   1602    798    314   -233   -321       N  
ATOM    306  CA  ASP A  41      10.565  32.384  29.799  1.00 10.82           C  
ANISOU  306  CA  ASP A  41     1119   1638   1353    284   -508   -406       C  
ATOM    307  C   ASP A  41      10.437  31.347  28.694  1.00  8.50           C  
ANISOU  307  C   ASP A  41      972   1289    967    359   -171   -134       C  
ATOM    308  O   ASP A  41      11.310  31.161  27.852  1.00  9.41           O  
ANISOU  308  O   ASP A  41      789   1341   1447    308    -95   -200       O  
ATOM    309  CB  ASP A  41      11.007  31.698  31.101  1.00 14.05           C  
ANISOU  309  CB  ASP A  41     1751   2314   1275    658   -893   -582       C  
ATOM    310  CG  ASP A  41      12.169  30.719  31.027  1.00 24.28           C  
ANISOU  310  CG  ASP A  41     3083   3075   3066   1654   -772    150       C  
ATOM    311  OD1 ASP A  41      13.274  30.989  30.462  1.00 25.64           O  
ANISOU  311  OD1 ASP A  41     2595   3899   3247   1994   -724  -1125       O  
ATOM    312  OD2 ASP A  41      12.055  29.602  31.643  1.00 34.84           O  
ANISOU  312  OD2 ASP A  41     6248   3192   3796   1950  -1193    656       O  
ATOM    313  N   ASP A  42       9.343  30.619  28.728  1.00  7.94           N  
ANISOU  313  N   ASP A  42      979   1278    758    264    -37    -38       N  
ATOM    314  CA  ASP A  42       9.109  29.568  27.772  1.00  7.35           C  
ANISOU  314  CA  ASP A  42      946   1079    767    336    -53    -20       C  
ATOM    315  C   ASP A  42       8.842  30.112  26.383  1.00  6.58           C  
ANISOU  315  C   ASP A  42      792    914    795    149    -59    -95       C  
ATOM    316  O   ASP A  42       9.266  29.523  25.358  1.00  6.72           O  
ANISOU  316  O   ASP A  42      884    809    862    175    106   -118       O  
ATOM    317  CB  ASP A  42       7.972  28.656  28.244  1.00  8.30           C  
ANISOU  317  CB  ASP A  42     1126   1125    902    279    132     58       C  
ATOM    318  CG  ASP A  42       8.364  27.792  29.427  1.00 10.00           C  
ANISOU  318  CG  ASP A  42     1403   1378   1018    388    203    187       C  
ATOM    319  OD1 ASP A  42       9.515  27.668  29.789  1.00 13.13           O  
ANISOU  319  OD1 ASP A  42     1610   1959   1420    348   -309    433       O  
ATOM    320  OD2 ASP A  42       7.451  27.194  30.010  1.00 17.33           O  
ANISOU  320  OD2 ASP A  42     1640   2819   2126    610    515   1480       O  
ATOM    321  N   VAL A  43       8.178  31.262  26.283  1.00  5.96           N  
ANISOU  321  N   VAL A  43      749    912    605    222     15   -124       N  
ATOM    322  CA  VAL A  43       7.977  31.877  24.986  1.00  6.18           C  
ANISOU  322  CA  VAL A  43      781    938    629    264    -61   -161       C  
ATOM    323  C   VAL A  43       9.316  32.292  24.369  1.00  5.96           C  
ANISOU  323  C   VAL A  43      776    831    656    260    -39   -159       C  
ATOM    324  O   VAL A  43       9.562  32.142  23.164  1.00  6.54           O  
ANISOU  324  O   VAL A  43      862    977    646    274    -29   -146       O  
ATOM    325  CB  VAL A  43       7.003  33.075  25.101  1.00  6.64           C  
ANISOU  325  CB  VAL A  43      742   1011    770    288     -7   -126       C  
ATOM    326  CG1 VAL A  43       6.943  33.871  23.850  1.00  8.11           C  
ANISOU  326  CG1 VAL A  43      916   1096   1068    346     28     89       C  
ATOM    327  CG2 VAL A  43       5.611  32.545  25.437  1.00  7.48           C  
ANISOU  327  CG2 VAL A  43      684   1225    934    311     -1     23       C  
ATOM    328  N   LYS A  44      10.234  32.840  25.181  1.00  5.81           N  
ANISOU  328  N   LYS A  44      777    803    625    204    -55   -130       N  
ATOM    329  CA  LYS A  44      11.550  33.168  24.719  1.00  6.25           C  
ANISOU  329  CA  LYS A  44      841    733    801    141    -76    -72       C  
ATOM    330  C   LYS A  44      12.255  31.928  24.178  1.00  5.71           C  
ANISOU  330  C   LYS A  44      700    741    728     98    -37    -49       C  
ATOM    331  O   LYS A  44      12.951  32.006  23.147  1.00  6.38           O  
ANISOU  331  O   LYS A  44      801    813    809    137     21     30       O  
ATOM    332  CB  LYS A  44      12.389  33.801  25.832  1.00  7.09           C  
ANISOU  332  CB  LYS A  44      854    873    965     57    -91   -127       C  
ATOM    333  CG  LYS A  44      11.921  35.191  26.217  1.00  8.04           C  
ANISOU  333  CG  LYS A  44     1257    864    933     98     -5   -167       C  
ATOM    334  CD  LYS A  44      12.730  35.765  27.336  1.00 11.92           C  
ANISOU  334  CD  LYS A  44     1988   1249   1292    322   -449   -479       C  
ATOM    335  CE  LYS A  44      12.388  37.180  27.704  1.00 12.69           C  
ANISOU  335  CE  LYS A  44     1986   1233   1602   -176   -110   -559       C  
ATOM    336  NZ  LYS A  44      13.226  37.553  28.904  1.00 21.77           N  
ANISOU  336  NZ  LYS A  44     3351   2486   2433    166  -1008  -1569       N  
ATOM    337  N   LYS A  45      12.151  30.776  24.846  1.00  5.78           N  
ANISOU  337  N   LYS A  45      799    767    632    148     28    -13       N  
ATOM    338  CA  LYS A  45      12.787  29.587  24.322  1.00  5.73           C  
ANISOU  338  CA  LYS A  45      674    774    729    135     37    -20       C  
ATOM    339  C   LYS A  45      12.286  29.265  22.928  1.00  5.80           C  
ANISOU  339  C   LYS A  45      672    742    790    147      0    -34       C  
ATOM    340  O   LYS A  45      13.067  28.886  22.013  1.00  6.08           O  
ANISOU  340  O   LYS A  45      748    879    685    249     63     -3       O  
ATOM    341  CB  LYS A  45      12.507  28.374  25.218  1.00  6.47           C  
ANISOU  341  CB  LYS A  45      816    715    925     89     62     75       C  
ATOM    342  CG  LYS A  45      13.066  28.492  26.632  1.00  6.67           C  
ANISOU  342  CG  LYS A  45     1000    826    707    125    165    -18       C  
ATOM    343  CD  LYS A  45      12.555  27.351  27.453  1.00  9.07           C  
ANISOU  343  CD  LYS A  45     1341   1191    913    173    372    218       C  
ATOM    344  CE  LYS A  45      12.805  27.573  28.954  1.00 11.81           C  
ANISOU  344  CE  LYS A  45     1782   1565   1140    -10   -237    467       C  
ATOM    345  NZ  LYS A  45      12.017  26.590  29.703  1.00 13.78           N  
ANISOU  345  NZ  LYS A  45     2388   1639   1210    345    838    347       N  
ATOM    346  N   ALA A  46      10.989  29.410  22.705  1.00  5.77           N  
ANISOU  346  N   ALA A  46      602    779    813    114     58   -125       N  
ATOM    347  CA  ALA A  46      10.426  29.120  21.397  1.00  5.90           C  
ANISOU  347  CA  ALA A  46      650    789    804     52     23   -152       C  
ATOM    348  C   ALA A  46      10.979  30.035  20.321  1.00  5.70           C  
ANISOU  348  C   ALA A  46      562    828    777    145    -36   -107       C  
ATOM    349  O   ALA A  46      11.232  29.600  19.200  1.00  6.14           O  
ANISOU  349  O   ALA A  46      716    899    717    133     14   -145       O  
ATOM    350  CB  ALA A  46       8.902  29.221  21.463  1.00  6.82           C  
ANISOU  350  CB  ALA A  46      639   1027    926    114     -9   -236       C  
ATOM    351  N   PHE A  47      11.187  31.312  20.652  1.00  5.83           N  
ANISOU  351  N   PHE A  47      683    829    701    152      0   -134       N  
ATOM    352  CA  PHE A  47      11.754  32.236  19.671  1.00  5.94           C  
ANISOU  352  CA  PHE A  47      735    813    707    139    -13    -20       C  
ATOM    353  C   PHE A  47      13.050  31.724  19.080  1.00  5.68           C  
ANISOU  353  C   PHE A  47      664    821    673    139      1     48       C  
ATOM    354  O   PHE A  47      13.289  31.773  17.889  1.00  6.22           O  
ANISOU  354  O   PHE A  47      888    815    659    251     67     35       O  
ATOM    355  CB  PHE A  47      12.045  33.595  20.368  1.00  6.06           C  
ANISOU  355  CB  PHE A  47      787    789    726    140    -60     21       C  
ATOM    356  CG  PHE A  47      12.817  34.542  19.487  1.00  5.99           C  
ANISOU  356  CG  PHE A  47      821    887    568    177     -4      5       C  
ATOM    357  CD1 PHE A  47      12.179  35.256  18.483  1.00  6.19           C  
ANISOU  357  CD1 PHE A  47      922    710    718    217    -67    -71       C  
ATOM    358  CD2 PHE A  47      14.180  34.709  19.657  1.00  6.72           C  
ANISOU  358  CD2 PHE A  47      879    979    694    -15   -110     73       C  
ATOM    359  CE1 PHE A  47      12.850  36.099  17.678  1.00  6.69           C  
ANISOU  359  CE1 PHE A  47     1192    783    567    189    -87    -17       C  
ATOM    360  CE2 PHE A  47      14.902  35.528  18.807  1.00  7.58           C  
ANISOU  360  CE2 PHE A  47      839   1166    874   -100   -102    170       C  
ATOM    361  CZ  PHE A  47      14.218  36.200  17.809  1.00  7.41           C  
ANISOU  361  CZ  PHE A  47     1156   1000    661    -31    -61     96       C  
ATOM    362  N   TYR A  48      13.969  31.294  19.999  1.00  6.14           N  
ANISOU  362  N   TYR A  48      669    989    675    212     58    156       N  
ATOM    363  CA  TYR A  48      15.304  30.930  19.547  1.00  6.63           C  
ANISOU  363  CA  TYR A  48      754    908    857    224     88    211       C  
ATOM    364  C   TYR A  48      15.270  29.692  18.696  1.00  7.10           C  
ANISOU  364  C   TYR A  48      833   1058    806    266    158    259       C  
ATOM    365  O   TYR A  48      16.182  29.532  17.858  1.00  8.66           O  
ANISOU  365  O   TYR A  48     1044   1060   1185    243    361     86       O  
ATOM    366  CB  TYR A  48      16.299  30.905  20.735  1.00  7.32           C  
ANISOU  366  CB  TYR A  48      610   1287    883    245     77    326       C  
ATOM    367  CG  TYR A  48      16.528  32.251  21.345  1.00  7.58           C  
ANISOU  367  CG  TYR A  48      778   1291    810    123    -18    120       C  
ATOM    368  CD1 TYR A  48      17.316  33.198  20.701  1.00  7.96           C  
ANISOU  368  CD1 TYR A  48      815   1351    858    117     -8    230       C  
ATOM    369  CD2 TYR A  48      15.913  32.636  22.546  1.00  7.65           C  
ANISOU  369  CD2 TYR A  48      760   1391    756    247    -24    331       C  
ATOM    370  CE1 TYR A  48      17.500  34.454  21.245  1.00  8.92           C  
ANISOU  370  CE1 TYR A  48      905   1480   1006   -126    -75    -85       C  
ATOM    371  CE2 TYR A  48      16.065  33.873  23.093  1.00  8.27           C  
ANISOU  371  CE2 TYR A  48      923   1343    877    350     22    101       C  
ATOM    372  CZ  TYR A  48      16.857  34.787  22.463  1.00  8.20           C  
ANISOU  372  CZ  TYR A  48      851   1430    833    174   -198    193       C  
ATOM    373  OH  TYR A  48      17.052  36.072  22.941  1.00 10.96           O  
ANISOU  373  OH  TYR A  48     1671   1390   1103     69   -148   -212       O  
ATOM    374  N   VAL A  49      14.299  28.805  18.887  1.00  7.51           N  
ANISOU  374  N   VAL A  49     1072    838    942    279    267     80       N  
ATOM    375  CA  VAL A  49      14.117  27.686  18.016  1.00  8.24           C  
ANISOU  375  CA  VAL A  49     1101    855   1173    272    148     73       C  
ATOM    376  C   VAL A  49      13.676  28.129  16.612  1.00  7.74           C  
ANISOU  376  C   VAL A  49     1053    780   1108    119    215    -96       C  
ATOM    377  O   VAL A  49      14.156  27.688  15.531  1.00  9.63           O  
ANISOU  377  O   VAL A  49     1325   1015   1320    278    551    -11       O  
ATOM    378  CB  VAL A  49      13.075  26.717  18.587  1.00  8.90           C  
ANISOU  378  CB  VAL A  49     1415    790   1177    326    317     98       C  
ATOM    379  CG1 VAL A  49      12.703  25.642  17.603  1.00  9.63           C  
ANISOU  379  CG1 VAL A  49     1299   1029   1330    101     40     99       C  
ATOM    380  CG2 VAL A  49      13.622  26.081  19.879  1.00 10.27           C  
ANISOU  380  CG2 VAL A  49     1925    892   1085     45    216     99       C  
ATOM    381  N   ILE A  50      12.700  29.040  16.529  1.00  6.50           N  
ANISOU  381  N   ILE A  50      780    677   1014      0    236    -12       N  
ATOM    382  CA AILE A  50      12.087  29.545  15.259  0.50  7.48           C  
ANISOU  382  CA AILE A  50      647    915   1280    -43    175     90       C  
ATOM    383  CA BILE A  50      12.152  29.439  15.218  0.50  6.03           C  
ANISOU  383  CA BILE A  50      712    635    942    -41    235   -359       C  
ATOM    384  C   ILE A  50      13.167  30.287  14.463  1.00  5.63           C  
ANISOU  384  C   ILE A  50      695    692    754     40     25    -47       C  
ATOM    385  O   ILE A  50      13.134  30.314  13.220  1.00  6.27           O  
ANISOU  385  O   ILE A  50      708    776    897    -11    -32    -41       O  
ATOM    386  CB AILE A  50      10.861  30.508  15.329  0.50  6.93           C  
ANISOU  386  CB AILE A  50      469    790   1372   -150     53    -90       C  
ATOM    387  CB BILE A  50      10.785  30.057  15.614  0.50  5.70           C  
ANISOU  387  CB BILE A  50      552    802    810   -127     59   -326       C  
ATOM    388  CG1AILE A  50       9.748  29.929  16.161  0.50  6.60           C  
ANISOU  388  CG1AILE A  50      653    757   1096     33     79      7       C  
ATOM    389  CG1BILE A  50       9.906  28.964  16.175  0.50  5.49           C  
ANISOU  389  CG1BILE A  50      557    768    762    -73     66   -226       C  
ATOM    390  CG2AILE A  50      10.340  30.914  13.953  0.50  6.53           C  
ANISOU  390  CG2AILE A  50      450    865   1167    -17    248   -124       C  
ATOM    391  CG2BILE A  50      10.140  30.783  14.473  0.50  6.07           C  
ANISOU  391  CG2BILE A  50      530    977    799   -147    134   -227       C  
ATOM    392  CD1AILE A  50       9.177  28.610  15.711  0.50  6.82           C  
ANISOU  392  CD1AILE A  50      714    712   1166   -112    312    -28       C  
ATOM    393  CD1BILE A  50       8.673  29.502  16.923  0.50  6.89           C  
ANISOU  393  CD1BILE A  50      554   1256    806     88     29     -8       C  
ATOM    394  N   ASP A  51      14.088  30.940  15.164  1.00  5.40           N  
ANISOU  394  N   ASP A  51      516    819    718    -47     65    -69       N  
ATOM    395  CA  ASP A  51      15.272  31.557  14.554  1.00  5.48           C  
ANISOU  395  CA  ASP A  51      601    816    664    -31      6      3       C  
ATOM    396  C   ASP A  51      16.254  30.461  14.132  1.00  5.80           C  
ANISOU  396  C   ASP A  51      671    878    653    -74    114     35       C  
ATOM    397  O   ASP A  51      17.243  30.174  14.803  1.00  6.51           O  
ANISOU  397  O   ASP A  51      694   1003    779     85     24     43       O  
ATOM    398  CB  ASP A  51      15.892  32.484  15.596  1.00  6.08           C  
ANISOU  398  CB  ASP A  51      676    893    742    -79     92    -89       C  
ATOM    399  CG  ASP A  51      17.231  33.029  15.135  1.00  5.94           C  
ANISOU  399  CG  ASP A  51      637    880    741    -34      9      0       C  
ATOM    400  OD1 ASP A  51      17.484  33.086  13.930  1.00  6.26           O  
ANISOU  400  OD1 ASP A  51      631    957    789    -80     13     67       O  
ATOM    401  OD2 ASP A  51      18.025  33.412  16.064  1.00  7.31           O  
ANISOU  401  OD2 ASP A  51      704   1165    908   -198    -68    -28       O  
ATOM    402  N   GLN A  52      15.958  29.849  13.008  1.00  5.82           N  
ANISOU  402  N   GLN A  52      795    771    647     70     69    110       N  
ATOM    403  CA  GLN A  52      16.651  28.612  12.593  1.00  6.39           C  
ANISOU  403  CA  GLN A  52      955    801    671    114     85     53       C  
ATOM    404  C   GLN A  52      18.122  28.819  12.271  1.00  7.21           C  
ANISOU  404  C   GLN A  52      924   1079    735    215    183    114       C  
ATOM    405  O   GLN A  52      18.892  27.891  12.414  1.00  8.34           O  
ANISOU  405  O   GLN A  52     1110   1079    979    393    186    174       O  
ATOM    406  CB  GLN A  52      15.957  27.959  11.440  1.00  7.44           C  
ANISOU  406  CB  GLN A  52     1118    855    854     61    128    -14       C  
ATOM    407  CG  GLN A  52      14.542  27.416  11.786  1.00  8.25           C  
ANISOU  407  CG  GLN A  52     1212    910   1012   -103     37     50       C  
ATOM    408  CD  GLN A  52      14.098  26.497  10.693  1.00 10.85           C  
ANISOU  408  CD  GLN A  52     1475   1020   1627    -33   -471    -77       C  
ATOM    409  OE1 GLN A  52      14.665  25.450  10.461  1.00 16.50           O  
ANISOU  409  OE1 GLN A  52     2113   1361   2793    380   -966   -931       O  
ATOM    410  NE2 GLN A  52      13.089  26.946   9.965  1.00  9.79           N  
ANISOU  410  NE2 GLN A  52     1253   1170   1297   -122    -89     47       N  
ATOM    411  N   ASP A  53      18.468  30.001  11.740  1.00  7.02           N  
ANISOU  411  N   ASP A  53      805   1081    783    272    199    122       N  
ATOM    412  CA  ASP A  53      19.883  30.273  11.443  1.00  8.12           C  
ANISOU  412  CA  ASP A  53      806   1254   1026    322    375    324       C  
ATOM    413  C   ASP A  53      20.650  30.921  12.581  1.00  8.74           C  
ANISOU  413  C   ASP A  53      702   1374   1246    228    193    306       C  
ATOM    414  O   ASP A  53      21.833  31.253  12.409  1.00 10.98           O  
ANISOU  414  O   ASP A  53      638   1691   1844    190    319    658       O  
ATOM    415  CB  ASP A  53      20.023  31.087  10.133  1.00  8.72           C  
ANISOU  415  CB  ASP A  53     1006   1182   1124    324    512    311       C  
ATOM    416  CG  ASP A  53      19.575  32.495  10.278  1.00  8.46           C  
ANISOU  416  CG  ASP A  53      806   1225   1183    260    386    378       C  
ATOM    417  OD1 ASP A  53      19.106  32.900  11.388  1.00  8.11           O  
ANISOU  417  OD1 ASP A  53      706   1245   1129    197    284    191       O  
ATOM    418  OD2 ASP A  53      19.635  33.251   9.270  1.00 11.40           O  
ANISOU  418  OD2 ASP A  53     1654   1413   1263    461    622    518       O  
ATOM    419  N   LYS A  54      20.040  31.090  13.735  1.00  8.10           N  
ANISOU  419  N   LYS A  54      630   1426   1022     88     68    362       N  
ATOM    420  CA  LYS A  54      20.738  31.618  14.921  1.00  9.06           C  
ANISOU  420  CA  LYS A  54      654   1593   1195     68   -126    243       C  
ATOM    421  C   LYS A  54      21.260  33.008  14.674  1.00  9.96           C  
ANISOU  421  C   LYS A  54      586   1666   1533     12   -128    378       C  
ATOM    422  O   LYS A  54      22.288  33.400  15.252  1.00 12.81           O  
ANISOU  422  O   LYS A  54      833   2079   1954   -209   -549    495       O  
ATOM    423  CB  LYS A  54      21.824  30.695  15.435  1.00 12.25           C  
ANISOU  423  CB  LYS A  54     1097   1960   1597    117   -316    758       C  
ATOM    424  CG  LYS A  54      21.332  29.263  15.536  1.00 12.47           C  
ANISOU  424  CG  LYS A  54     1299   1764   1675    438     75    543       C  
ATOM    425  CD  LYS A  54      20.059  29.030  16.320  1.00 10.47           C  
ANISOU  425  CD  LYS A  54     1163   1665   1149    231   -191    266       C  
ATOM    426  CE  LYS A  54      19.292  27.804  15.955  1.00  9.71           C  
ANISOU  426  CE  LYS A  54     1389   1341    959    471     36     83       C  
ATOM    427  NZ  LYS A  54      18.019  27.706  16.673  1.00  9.53           N  
ANISOU  427  NZ  LYS A  54     1174   1176   1273    357      6    -21       N  
ATOM    428  N   SER A  55      20.539  33.800  13.903  1.00  8.65           N  
ANISOU  428  N   SER A  55      575   1435   1276   -149   -138    151       N  
ATOM    429  CA  SER A  55      20.947  35.132  13.627  1.00  9.42           C  
ANISOU  429  CA  SER A  55      735   1597   1249   -263   -190    293       C  
ATOM    430  C   SER A  55      20.511  36.121  14.717  1.00  9.33           C  
ANISOU  430  C   SER A  55      905   1472   1167   -357   -410    268       C  
ATOM    431  O   SER A  55      20.962  37.245  14.696  1.00 12.53           O  
ANISOU  431  O   SER A  55     1722   1632   1406   -895   -537    328       O  
ATOM    432  CB  SER A  55      20.314  35.633  12.344  1.00  8.90           C  
ANISOU  432  CB  SER A  55      722   1572   1090   -280      9    214       C  
ATOM    433  OG  SER A  55      18.888  35.730  12.484  1.00  7.45           O  
ANISOU  433  OG  SER A  55      673   1187    970   -157    -98     98       O  
ATOM    434  N   GLY A  56      19.631  35.693  15.626  1.00  8.51           N  
ANISOU  434  N   GLY A  56      812   1245   1175   -289   -368    199       N  
ATOM    435  CA  GLY A  56      19.073  36.549  16.613  1.00  9.48           C  
ANISOU  435  CA  GLY A  56     1244   1236   1122   -366   -579     52       C  
ATOM    436  C   GLY A  56      17.755  37.196  16.245  1.00  7.63           C  
ANISOU  436  C   GLY A  56     1133    990    778   -345   -197    -86       C  
ATOM    437  O   GLY A  56      17.136  37.884  17.064  1.00  9.61           O  
ANISOU  437  O   GLY A  56     1571   1278    802   -388   -118   -209       O  
ATOM    438  N   PHE A  57      17.313  36.985  15.009  1.00  6.28           N  
ANISOU  438  N   PHE A  57      802    840    743    -54   -142    -42       N  
ATOM    439  CA  PHE A  57      16.042  37.523  14.522  1.00  6.07           C  
ANISOU  439  CA  PHE A  57      756    802    749    -42    -75    -82       C  
ATOM    440  C   PHE A  57      15.337  36.447  13.734  1.00  5.64           C  
ANISOU  440  C   PHE A  57      656    802    684    -49     -3   -116       C  
ATOM    441  O   PHE A  57      15.999  35.609  13.105  1.00  6.73           O  
ANISOU  441  O   PHE A  57      608    978    969    -33    -53   -279       O  
ATOM    442  CB  PHE A  57      16.242  38.735  13.610  1.00  6.62           C  
ANISOU  442  CB  PHE A  57      869    890    757   -111   -119    -46       C  
ATOM    443  CG  PHE A  57      16.849  39.915  14.266  1.00  6.68           C  
ANISOU  443  CG  PHE A  57      734    861    942    -72   -113     13       C  
ATOM    444  CD1 PHE A  57      18.260  40.066  14.318  1.00  7.16           C  
ANISOU  444  CD1 PHE A  57      760    813   1149    -83   -128     68       C  
ATOM    445  CD2 PHE A  57      16.079  40.877  14.876  1.00  6.97           C  
ANISOU  445  CD2 PHE A  57      764    823   1062    -10   -264    -80       C  
ATOM    446  CE1 PHE A  57      18.812  41.188  14.933  1.00  8.02           C  
ANISOU  446  CE1 PHE A  57      791    940   1317   -147   -226     -7       C  
ATOM    447  CE2 PHE A  57      16.628  41.980  15.473  1.00  8.41           C  
ANISOU  447  CE2 PHE A  57      879    847   1470     12   -468   -138       C  
ATOM    448  CZ  PHE A  57      17.996  42.135  15.482  1.00  9.20           C  
ANISOU  448  CZ  PHE A  57      985    752   1759     22   -622    -88       C  
ATOM    449  N   ILE A  58      14.009  36.502  13.731  1.00  5.48           N  
ANISOU  449  N   ILE A  58      660    741    683     20     32   -111       N  
ATOM    450  CA  ILE A  58      13.237  35.733  12.780  1.00  4.99           C  
ANISOU  450  CA  ILE A  58      589    640    667      8     13    -55       C  
ATOM    451  C   ILE A  58      13.059  36.606  11.552  1.00  5.47           C  
ANISOU  451  C   ILE A  58      727    657    694    -70     22   -109       C  
ATOM    452  O   ILE A  58      12.401  37.642  11.593  1.00  6.89           O  
ANISOU  452  O   ILE A  58     1005    834    778    162     90     70       O  
ATOM    453  CB  ILE A  58      11.883  35.291  13.357  1.00  5.60           C  
ANISOU  453  CB  ILE A  58      608    786    732     66     40    -22       C  
ATOM    454  CG1 ILE A  58      12.084  34.420  14.594  1.00  5.71           C  
ANISOU  454  CG1 ILE A  58      734    749    688    -21      3    -60       C  
ATOM    455  CG2 ILE A  58      11.094  34.555  12.304  1.00  7.93           C  
ANISOU  455  CG2 ILE A  58      739   1431    842   -315   -179    246       C  
ATOM    456  CD1 ILE A  58      10.826  34.217  15.420  1.00  7.50           C  
ANISOU  456  CD1 ILE A  58      983   1057    809   -206    109   -152       C  
ATOM    457  N   GLU A  59      13.745  36.219  10.467  1.00  5.68           N  
ANISOU  457  N   GLU A  59      846    648    662    -27     27     -3       N  
ATOM    458  CA  GLU A  59      13.636  36.908   9.182  1.00  6.15           C  
ANISOU  458  CA  GLU A  59      976    671    689    -91     71     96       C  
ATOM    459  C   GLU A  59      12.418  36.376   8.422  1.00  5.83           C  
ANISOU  459  C   GLU A  59      843    633    738      7     86     62       C  
ATOM    460  O   GLU A  59      11.816  35.371   8.775  1.00  5.99           O  
ANISOU  460  O   GLU A  59      892    644    741    -73    -45    123       O  
ATOM    461  CB  GLU A  59      14.909  36.770   8.371  1.00  6.49           C  
ANISOU  461  CB  GLU A  59      915    813    739   -100     15    103       C  
ATOM    462  CG  GLU A  59      16.158  37.414   8.950  1.00  7.81           C  
ANISOU  462  CG  GLU A  59     1029    915   1023   -275    -53    254       C  
ATOM    463  CD  GLU A  59      16.958  36.597   9.981  1.00  7.48           C  
ANISOU  463  CD  GLU A  59      816   1026   1000   -149    -16     84       C  
ATOM    464  OE1 GLU A  59      16.807  35.362  10.006  1.00  7.31           O  
ANISOU  464  OE1 GLU A  59      959    968    850    -22    -37    195       O  
ATOM    465  OE2 GLU A  59      17.745  37.239  10.706  1.00  9.79           O  
ANISOU  465  OE2 GLU A  59     1402   1102   1216   -321   -388    251       O  
ATOM    466  N   GLU A  60      12.104  37.050   7.314  1.00  6.66           N  
ANISOU  466  N   GLU A  60      836    755    940     13      8    289       N  
ATOM    467  CA AGLU A  60      10.909  36.685   6.575  0.63  7.04           C  
ANISOU  467  CA AGLU A  60      832    895    945      7     -3    431       C  
ATOM    468  CA BGLU A  60      10.902  36.688   6.568  0.37  7.37           C  
ANISOU  468  CA BGLU A  60      940    923    938     39    -75    351       C  
ATOM    469  C   GLU A  60      10.938  35.257   6.092  1.00  6.97           C  
ANISOU  469  C   GLU A  60      928    916    805    -78   -174    363       C  
ATOM    470  O   GLU A  60       9.897  34.586   6.096  1.00  7.98           O  
ANISOU  470  O   GLU A  60      825   1103   1104   -112   -227    465       O  
ATOM    471  CB AGLU A  60      10.811  37.729   5.450  0.63  9.85           C  
ANISOU  471  CB AGLU A  60     1001   1233   1507    281     26    847       C  
ATOM    472  CB BGLU A  60      10.628  37.461   5.266  0.37  7.67           C  
ANISOU  472  CB BGLU A  60     1081    937    897    -87    -68    378       C  
ATOM    473  CG AGLU A  60       9.440  37.905   4.937  0.63 11.62           C  
ANISOU  473  CG AGLU A  60     1476   1606   1334   -102   -717    516       C  
ATOM    474  CG BGLU A  60      10.083  38.824   5.545  0.37  7.76           C  
ANISOU  474  CG BGLU A  60     1356    674    919   -221   -459    229       C  
ATOM    475  CD AGLU A  60       9.274  38.996   3.900  0.63 15.89           C  
ANISOU  475  CD AGLU A  60     1745   2628   1667     85   -744   1245       C  
ATOM    476  CD BGLU A  60       9.750  39.657   4.308  0.37  8.41           C  
ANISOU  476  CD BGLU A  60     1434   1112    649    260     12    267       C  
ATOM    477  OE1AGLU A  60      10.030  39.988   3.902  0.63 28.10           O  
ANISOU  477  OE1AGLU A  60     2023   4676   3979  -1344  -1481   3731       O  
ATOM    478  OE1BGLU A  60       9.165  39.062   3.353  0.37 17.86           O  
ANISOU  478  OE1BGLU A  60     3229   1510   2048    -38  -2208    886       O  
ATOM    479  OE2AGLU A  60       8.356  38.855   3.097  0.63 21.02           O  
ANISOU  479  OE2AGLU A  60     3464   2176   2347    572  -1863    604       O  
ATOM    480  OE2BGLU A  60      10.007  40.857   4.154  0.37 12.17           O  
ANISOU  480  OE2BGLU A  60     2676    899   1050    518    216    377       O  
ATOM    481  N   ASP A  61      12.100  34.740   5.654  1.00  7.00           N  
ANISOU  481  N   ASP A  61      978    981    700    -90     -1    186       N  
ATOM    482  CA  ASP A  61      12.138  33.360   5.190  1.00  7.94           C  
ANISOU  482  CA  ASP A  61     1210   1098    708    -32   -222    -28       C  
ATOM    483  C   ASP A  61      11.811  32.338   6.299  1.00  7.27           C  
ANISOU  483  C   ASP A  61     1142    856    764    109   -241     33       C  
ATOM    484  O   ASP A  61      11.208  31.290   6.056  1.00  9.17           O  
ANISOU  484  O   ASP A  61     1728    883    872     -7   -599    -64       O  
ATOM    485  CB  ASP A  61      13.454  33.019   4.516  1.00 10.20           C  
ANISOU  485  CB  ASP A  61     1410   1505    960    141      9    -62       C  
ATOM    486  CG  ASP A  61      14.753  33.158   5.257  1.00 11.04           C  
ANISOU  486  CG  ASP A  61     1262   1742   1193    103    162   -271       C  
ATOM    487  OD1 ASP A  61      14.746  33.713   6.352  1.00  9.80           O  
ANISOU  487  OD1 ASP A  61     1069   1523   1133    200    -49     59       O  
ATOM    488  OD2 ASP A  61      15.786  32.705   4.678  1.00 18.93           O  
ANISOU  488  OD2 ASP A  61     1204   4085   1902     -6    282  -1253       O  
ATOM    489  N   GLU A  62      12.191  32.693   7.552  1.00  6.93           N  
ANISOU  489  N   GLU A  62     1121    790    721   -120   -282     97       N  
ATOM    490  CA  GLU A  62      11.865  31.869   8.730  1.00  7.06           C  
ANISOU  490  CA  GLU A  62     1158    629    894    -95   -389    163       C  
ATOM    491  C   GLU A  62      10.403  32.003   9.134  1.00  6.61           C  
ANISOU  491  C   GLU A  62     1105    610    797   -154   -376    132       C  
ATOM    492  O   GLU A  62       9.871  31.062   9.719  1.00  8.57           O  
ANISOU  492  O   GLU A  62      970    742   1545   -238   -556    488       O  
ATOM    493  CB  GLU A  62      12.802  32.249   9.864  1.00  6.08           C  
ANISOU  493  CB  GLU A  62      972    601    736    -58   -259    132       C  
ATOM    494  CG  GLU A  62      14.240  31.824   9.612  1.00  6.78           C  
ANISOU  494  CG  GLU A  62     1027    712    838     86   -309    -70       C  
ATOM    495  CD  GLU A  62      15.237  32.417  10.590  1.00  5.70           C  
ANISOU  495  CD  GLU A  62      814    733    618     51    -57    -64       C  
ATOM    496  OE1 GLU A  62      14.869  33.378  11.324  1.00  6.19           O  
ANISOU  496  OE1 GLU A  62      682    823    845     -2    -26   -204       O  
ATOM    497  OE2 GLU A  62      16.419  31.995  10.591  1.00  6.59           O  
ANISOU  497  OE2 GLU A  62      838    873    793    130    -31   -121       O  
ATOM    498  N   LEU A  63       9.760  33.139   8.854  1.00  6.70           N  
ANISOU  498  N   LEU A  63     1267    648    629    -66   -200    171       N  
ATOM    499  CA  LEU A  63       8.320  33.250   8.990  1.00  6.67           C  
ANISOU  499  CA  LEU A  63     1238    665    633    125     20    134       C  
ATOM    500  C   LEU A  63       7.622  32.396   7.947  1.00  6.02           C  
ANISOU  500  C   LEU A  63      943    566    777    162    119    153       C  
ATOM    501  O   LEU A  63       6.679  31.680   8.263  1.00  6.69           O  
ANISOU  501  O   LEU A  63      909    708    925    206    204    155       O  
ATOM    502  CB  LEU A  63       7.837  34.701   8.886  1.00  7.36           C  
ANISOU  502  CB  LEU A  63     1334    630    831    103    213     35       C  
ATOM    503  CG  LEU A  63       8.273  35.634  10.004  1.00  6.89           C  
ANISOU  503  CG  LEU A  63      939    733    945     39    -38    -12       C  
ATOM    504  CD1 LEU A  63       7.846  37.057   9.643  1.00  9.06           C  
ANISOU  504  CD1 LEU A  63     1405    796   1240    288    -29   -125       C  
ATOM    505  CD2 LEU A  63       7.670  35.205  11.343  1.00  7.17           C  
ANISOU  505  CD2 LEU A  63      833   1080    813    275     57    -79       C  
ATOM    506  N   LYS A  64       8.117  32.461   6.702  1.00  5.69           N  
ANISOU  506  N   LYS A  64      864    636    661      0     62     81       N  
ATOM    507  CA  LYS A  64       7.453  31.667   5.678  1.00  5.79           C  
ANISOU  507  CA  LYS A  64      726    709    765     73    -61    157       C  
ATOM    508  C   LYS A  64       7.451  30.183   6.038  1.00  5.47           C  
ANISOU  508  C   LYS A  64      837    594    646      4     56    112       C  
ATOM    509  O   LYS A  64       6.476  29.458   5.775  1.00  5.85           O  
ANISOU  509  O   LYS A  64      792    740    693     36    -56    110       O  
ATOM    510  CB  LYS A  64       8.165  31.896   4.323  1.00  6.81           C  
ANISOU  510  CB  LYS A  64     1183    764    641    -72   -100    265       C  
ATOM    511  CG ALYS A  64       7.430  31.114   3.245  0.54 10.08           C  
ANISOU  511  CG ALYS A  64     1407   1795    628   -480   -209    346       C  
ATOM    512  CG BLYS A  64       7.628  31.116   3.148  0.46  9.12           C  
ANISOU  512  CG BLYS A  64     1746    913    806   -544      3    130       C  
ATOM    513  CD ALYS A  64       7.842  31.696   1.895  0.54  9.28           C  
ANISOU  513  CD ALYS A  64     1698   1199    631   -375   -156    240       C  
ATOM    514  CD BLYS A  64       8.476  31.167   1.885  0.46  8.58           C  
ANISOU  514  CD BLYS A  64     1428    967    864    245    -31    147       C  
ATOM    515  CE ALYS A  64       7.057  31.047   0.765  0.54  8.29           C  
ANISOU  515  CE ALYS A  64     1370   1084    696     24    -54    -55       C  
ATOM    516  CE BLYS A  64       8.023  30.295   0.741  0.46  9.02           C  
ANISOU  516  CE BLYS A  64     1271   1372    784    152   -122    132       C  
ATOM    517  NZ ALYS A  64       5.677  31.556   0.572  0.54  8.40           N  
ANISOU  517  NZ ALYS A  64     1265   1265    661    107    204    379       N  
ATOM    518  NZ BLYS A  64       8.950  30.387  -0.423  0.46 18.04           N  
ANISOU  518  NZ BLYS A  64     3789   1643   1424    459   1275     15       N  
ATOM    519  N   LEU A  65       8.535  29.706   6.626  1.00  4.93           N  
ANISOU  519  N   LEU A  65      741    586    546     30      5     66       N  
ATOM    520  CA  LEU A  65       8.675  28.305   7.007  1.00  4.84           C  
ANISOU  520  CA  LEU A  65      634    620    584     92     42     79       C  
ATOM    521  C   LEU A  65       8.413  28.053   8.479  1.00  4.78           C  
ANISOU  521  C   LEU A  65      688    549    578      5     33     19       C  
ATOM    522  O   LEU A  65       8.785  27.012   9.034  1.00  5.51           O  
ANISOU  522  O   LEU A  65      790    614    688     98     20    100       O  
ATOM    523  CB  LEU A  65      10.051  27.777   6.548  1.00  5.55           C  
ANISOU  523  CB  LEU A  65      663    657    788     63    127     44       C  
ATOM    524  CG  LEU A  65      10.235  27.839   5.033  1.00  6.51           C  
ANISOU  524  CG  LEU A  65      867    747    858    100    229    116       C  
ATOM    525  CD1 LEU A  65      11.585  27.283   4.661  1.00  8.47           C  
ANISOU  525  CD1 LEU A  65      995   1064   1157     28    454    -22       C  
ATOM    526  CD2 LEU A  65       9.144  27.056   4.304  1.00  9.13           C  
ANISOU  526  CD2 LEU A  65     1051   1577    840    -36     62   -218       C  
ATOM    527  N   PHE A  66       7.676  28.978   9.118  1.00  4.79           N  
ANISOU  527  N   PHE A  66      737    550    534     20      9     37       N  
ATOM    528  CA  PHE A  66       7.347  28.900  10.525  1.00  4.79           C  
ANISOU  528  CA  PHE A  66      760    556    504     28      1     32       C  
ATOM    529  C   PHE A  66       6.778  27.539  10.924  1.00  4.68           C  
ANISOU  529  C   PHE A  66      680    573    525    124     10    -14       C  
ATOM    530  O   PHE A  66       7.130  26.988  11.985  1.00  4.93           O  
ANISOU  530  O   PHE A  66      794    551    529      0     26     50       O  
ATOM    531  CB  PHE A  66       6.334  30.027  10.832  1.00  5.32           C  
ANISOU  531  CB  PHE A  66      839    518    663     78      2     44       C  
ATOM    532  CG  PHE A  66       5.732  30.008  12.202  1.00  5.04           C  
ANISOU  532  CG  PHE A  66      729    502    683     99      6     69       C  
ATOM    533  CD1 PHE A  66       6.406  30.464  13.307  1.00  6.54           C  
ANISOU  533  CD1 PHE A  66      827    865    793     55    -68   -136       C  
ATOM    534  CD2 PHE A  66       4.422  29.535  12.381  1.00  5.58           C  
ANISOU  534  CD2 PHE A  66      747    597    775     75    -45    128       C  
ATOM    535  CE1 PHE A  66       5.751  30.470  14.568  1.00  7.33           C  
ANISOU  535  CE1 PHE A  66     1129    972    685     95   -108   -160       C  
ATOM    536  CE2 PHE A  66       3.819  29.525  13.605  1.00  6.65           C  
ANISOU  536  CE2 PHE A  66      856    835    835    130    122     78       C  
ATOM    537  CZ  PHE A  66       4.486  29.990  14.672  1.00  7.10           C  
ANISOU  537  CZ  PHE A  66     1037    834    829    279    150    -39       C  
ATOM    538  N   LEU A  67       5.831  27.030  10.128  1.00  4.56           N  
ANISOU  538  N   LEU A  67      730    484    519    109     23     19       N  
ATOM    539  CA  LEU A  67       5.154  25.796  10.512  1.00  4.63           C  
ANISOU  539  CA  LEU A  67      691    539    530     58    107     14       C  
ATOM    540  C   LEU A  67       6.098  24.580  10.517  1.00  4.48           C  
ANISOU  540  C   LEU A  67      693    506    502     42    -40    -36       C  
ATOM    541  O   LEU A  67       5.796  23.600  11.195  1.00  4.80           O  
ANISOU  541  O   LEU A  67      808    479    538     50     13     26       O  
ATOM    542  CB  LEU A  67       3.948  25.492   9.613  1.00  4.73           C  
ANISOU  542  CB  LEU A  67      706    548    545     39     58     62       C  
ATOM    543  CG  LEU A  67       2.854  26.583   9.622  1.00  5.38           C  
ANISOU  543  CG  LEU A  67      715    601    730     58     13      2       C  
ATOM    544  CD1 LEU A  67       1.782  26.188   8.607  1.00  6.58           C  
ANISOU  544  CD1 LEU A  67      762    864    874    156    -95     30       C  
ATOM    545  CD2 LEU A  67       2.259  26.772  10.990  1.00  5.78           C  
ANISOU  545  CD2 LEU A  67      689    620    888     50    147    -70       C  
ATOM    546  N   GLN A  68       7.194  24.645   9.784  1.00  4.46           N  
ANISOU  546  N   GLN A  68      757    511    428     83     91     22       N  
ATOM    547  CA  GLN A  68       8.123  23.515   9.744  1.00  5.08           C  
ANISOU  547  CA  GLN A  68      923    524    484    138     92     58       C  
ATOM    548  C   GLN A  68       8.769  23.256  11.091  1.00  5.16           C  
ANISOU  548  C   GLN A  68      749    639    572    121    100     41       C  
ATOM    549  O   GLN A  68       9.288  22.146  11.319  1.00  6.55           O  
ANISOU  549  O   GLN A  68      998    737    755    238    105    136       O  
ATOM    550  CB  GLN A  68       9.193  23.682   8.675  1.00  5.45           C  
ANISOU  550  CB  GLN A  68      900    563    608    181    161     24       C  
ATOM    551  CG  GLN A  68       8.664  23.583   7.233  1.00  5.91           C  
ANISOU  551  CG  GLN A  68     1051    619    575    147    129    -33       C  
ATOM    552  CD  GLN A  68       9.838  23.354   6.325  1.00  6.24           C  
ANISOU  552  CD  GLN A  68     1117    604    648     14    170    -24       C  
ATOM    553  OE1 GLN A  68      10.632  24.213   6.092  1.00 10.26           O  
ANISOU  553  OE1 GLN A  68     1831    800   1269   -391    793   -326       O  
ATOM    554  NE2 GLN A  68       9.954  22.128   5.821  1.00  5.59           N  
ANISOU  554  NE2 GLN A  68      791    704    629     39     88   -123       N  
ATOM    555  N   ASN A  69       8.784  24.235  11.982  1.00  5.13           N  
ANISOU  555  N   ASN A  69      719    655    573     62     21    103       N  
ATOM    556  CA  ASN A  69       9.307  24.022  13.341  1.00  5.11           C  
ANISOU  556  CA  ASN A  69      689    698    554    -13     -9    118       C  
ATOM    557  C   ASN A  69       8.388  23.123  14.157  1.00  5.28           C  
ANISOU  557  C   ASN A  69      840    633    533    -19    -19     87       C  
ATOM    558  O   ASN A  69       8.799  22.592  15.200  1.00  7.03           O  
ANISOU  558  O   ASN A  69     1026    918    728    -78   -137    280       O  
ATOM    559  CB  ASN A  69       9.484  25.358  14.036  1.00  6.71           C  
ANISOU  559  CB  ASN A  69     1071    834    647   -220   -188    177       C  
ATOM    560  CG  ASN A  69      10.475  26.244  13.320  1.00  8.40           C  
ANISOU  560  CG  ASN A  69      973   1130   1087   -418   -466    446       C  
ATOM    561  OD1 ASN A  69      11.674  26.019  13.440  1.00 15.12           O  
ANISOU  561  OD1 ASN A  69     1025   2293   2429   -578   -664   1700       O  
ATOM    562  ND2 ASN A  69      10.002  27.222  12.614  1.00  7.07           N  
ANISOU  562  ND2 ASN A  69      991    819    878   -274   -227    258       N  
ATOM    563  N   PHE A  70       7.136  22.986  13.733  1.00  4.87           N  
ANISOU  563  N   PHE A  70      784    579    488     14     53     99       N  
ATOM    564  CA  PHE A  70       6.128  22.181  14.398  1.00  5.18           C  
ANISOU  564  CA  PHE A  70      777    633    559    -49     89     36       C  
ATOM    565  C   PHE A  70       5.932  20.848  13.711  1.00  5.62           C  
ANISOU  565  C   PHE A  70      803    734    597   -102     27     74       C  
ATOM    566  O   PHE A  70       5.636  19.848  14.365  1.00  8.34           O  
ANISOU  566  O   PHE A  70     1808    738    624   -402      2    112       O  
ATOM    567  CB  PHE A  70       4.804  22.992  14.443  1.00  5.54           C  
ANISOU  567  CB  PHE A  70      699    813    593    -79     21     61       C  
ATOM    568  CG  PHE A  70       4.971  24.281  15.245  1.00  5.17           C  
ANISOU  568  CG  PHE A  70      650    723    590      9     42     51       C  
ATOM    569  CD1 PHE A  70       5.427  25.432  14.635  1.00  5.86           C  
ANISOU  569  CD1 PHE A  70      792    774    661     98    137     79       C  
ATOM    570  CD2 PHE A  70       4.742  24.310  16.605  1.00  5.67           C  
ANISOU  570  CD2 PHE A  70      786    808    560     18     30     95       C  
ATOM    571  CE1 PHE A  70       5.651  26.577  15.336  1.00  6.36           C  
ANISOU  571  CE1 PHE A  70      761    734    920     80     58    166       C  
ATOM    572  CE2 PHE A  70       4.955  25.461  17.332  1.00  5.92           C  
ANISOU  572  CE2 PHE A  70      830    855    563    134    -38    -23       C  
ATOM    573  CZ  PHE A  70       5.427  26.611  16.699  1.00  6.37           C  
ANISOU  573  CZ  PHE A  70      797    751    873     65     79    -69       C  
ATOM    574  N   SER A  71       6.109  20.766  12.404  1.00  5.37           N  
ANISOU  574  N   SER A  71      901    540    597      3     72     31       N  
ATOM    575  CA  SER A  71       6.159  19.522  11.676  1.00  5.87           C  
ANISOU  575  CA  SER A  71      981    614    635     26     95    -41       C  
ATOM    576  C   SER A  71       6.977  19.747  10.421  1.00  5.77           C  
ANISOU  576  C   SER A  71      896    557    737     53    118    -16       C  
ATOM    577  O   SER A  71       6.622  20.646   9.669  1.00  6.04           O  
ANISOU  577  O   SER A  71     1047    559    690     48    157    -43       O  
ATOM    578  CB  SER A  71       4.769  19.027  11.291  1.00  6.84           C  
ANISOU  578  CB  SER A  71     1024    755    819   -115    150    -66       C  
ATOM    579  OG  SER A  71       4.893  17.887  10.476  1.00  9.70           O  
ANISOU  579  OG  SER A  71     1491    854   1340   -118   -138   -304       O  
ATOM    580  N   PRO A  72       7.996  18.948  10.140  1.00  5.99           N  
ANISOU  580  N   PRO A  72      959    629    686     59    163     21       N  
ATOM    581  CA  PRO A  72       8.796  19.255   8.932  1.00  6.36           C  
ANISOU  581  CA  PRO A  72      915    661    839     38    125   -101       C  
ATOM    582  C   PRO A  72       8.013  19.226   7.643  1.00  5.83           C  
ANISOU  582  C   PRO A  72      964    537    714     52    162    -73       C  
ATOM    583  O   PRO A  72       8.388  19.894   6.694  1.00  6.51           O  
ANISOU  583  O   PRO A  72      996    631    847     40    248    -26       O  
ATOM    584  CB APRO A  72       9.880  18.197   8.981  0.56  6.82           C  
ANISOU  584  CB APRO A  72      834    893    866     60     90    -95       C  
ATOM    585  CB BPRO A  72       9.920  18.217   8.979  0.44  7.17           C  
ANISOU  585  CB BPRO A  72      810    772   1141     41    146    115       C  
ATOM    586  CG APRO A  72       9.303  17.072   9.765  0.56  7.38           C  
ANISOU  586  CG APRO A  72      863    725   1216    154    172    -24       C  
ATOM    587  CG BPRO A  72      10.098  17.842  10.427  0.44  7.89           C  
ANISOU  587  CG BPRO A  72      823   1011   1162    -41    -62     69       C  
ATOM    588  CD APRO A  72       8.460  17.747  10.858  0.56  7.94           C  
ANISOU  588  CD APRO A  72     1091    821   1104    357    267    113       C  
ATOM    589  CD BPRO A  72       8.642  17.860  10.902  0.44  8.73           C  
ANISOU  589  CD BPRO A  72     1021   1076   1219    331    179    338       C  
ATOM    590  N   SER A  73       6.949  18.424   7.611  1.00  5.61           N  
ANISOU  590  N   SER A  73      862    512    758     60    191    -32       N  
ATOM    591  CA  SER A  73       6.145  18.285   6.413  1.00  6.41           C  
ANISOU  591  CA  SER A  73      903    677    854     77     27   -154       C  
ATOM    592  C   SER A  73       5.016  19.314   6.305  1.00  6.92           C  
ANISOU  592  C   SER A  73     1016    683    931    138    -11   -179       C  
ATOM    593  O   SER A  73       4.260  19.291   5.344  1.00  9.05           O  
ANISOU  593  O   SER A  73     1348   1029   1062    333   -237   -274       O  
ATOM    594  CB  SER A  73       5.551  16.881   6.324  1.00  7.71           C  
ANISOU  594  CB  SER A  73     1057    645   1227    102   -136   -140       C  
ATOM    595  OG  SER A  73       4.779  16.586   7.489  1.00 10.19           O  
ANISOU  595  OG  SER A  73     1501    980   1390   -324    160    -95       O  
ATOM    596  N   ALA A  74       4.894  20.215   7.290  1.00  6.59           N  
ANISOU  596  N   ALA A  74     1014    609    883    136     29   -107       N  
ATOM    597  CA  ALA A  74       3.879  21.262   7.191  1.00  6.95           C  
ANISOU  597  CA  ALA A  74     1071    622    947    181    108    -73       C  
ATOM    598  C   ALA A  74       4.148  22.203   6.036  1.00  6.90           C  
ANISOU  598  C   ALA A  74     1109    590    922    151     26   -151       C  
ATOM    599  O   ALA A  74       5.263  22.388   5.565  1.00  7.52           O  
ANISOU  599  O   ALA A  74     1082    786    988     76     33     12       O  
ATOM    600  CB  ALA A  74       3.903  22.092   8.474  1.00  8.36           C  
ANISOU  600  CB  ALA A  74     1320    933    924    433    158   -136       C  
ATOM    601  N   ARG A  75       3.050  22.819   5.581  1.00  6.68           N  
ANISOU  601  N   ARG A  75     1139    510    889    103     22    -92       N  
ATOM    602  CA  ARG A  75       3.158  23.721   4.443  1.00  6.85           C  
ANISOU  602  CA  ARG A  75     1215    612    776     98    -29   -138       C  
ATOM    603  C   ARG A  75       3.930  25.000   4.781  1.00  6.03           C  
ANISOU  603  C   ARG A  75     1105    531    654    101     13    -37       C  
ATOM    604  O   ARG A  75       3.954  25.465   5.919  1.00  5.96           O  
ANISOU  604  O   ARG A  75     1045    591    628     25     62    -37       O  
ATOM    605  CB  ARG A  75       1.771  24.094   3.917  1.00  6.88           C  
ANISOU  605  CB  ARG A  75     1177    614    823    115    -89   -153       C  
ATOM    606  CG  ARG A  75       0.925  24.962   4.846  1.00  6.33           C  
ANISOU  606  CG  ARG A  75     1149    458    799      1   -107    -85       C  
ATOM    607  CD  ARG A  75      -0.405  25.283   4.230  1.00  6.54           C  
ANISOU  607  CD  ARG A  75     1048    573    863    -36    -99   -138       C  
ATOM    608  NE  ARG A  75      -1.233  26.130   5.047  1.00  6.51           N  
ANISOU  608  NE  ARG A  75      891    624    958    -53    -95    -28       N  
ATOM    609  CZ  ARG A  75      -1.173  27.461   5.080  1.00  5.62           C  
ANISOU  609  CZ  ARG A  75      752    563    819    -25   -201     21       C  
ATOM    610  NH1 ARG A  75      -0.278  28.131   4.335  1.00  6.01           N  
ANISOU  610  NH1 ARG A  75      938    529    816    -31    -19    -13       N  
ATOM    611  NH2 ARG A  75      -2.028  28.147   5.841  1.00  5.99           N  
ANISOU  611  NH2 ARG A  75      758    550    969    -80    -15     70       N  
ATOM    612  N   ALA A  76       4.474  25.587   3.726  1.00  6.64           N  
ANISOU  612  N   ALA A  76     1237    615    671    188     60   -120       N  
ATOM    613  CA  ALA A  76       4.926  26.998   3.797  1.00  5.83           C  
ANISOU  613  CA  ALA A  76      949    639    627    110    169     27       C  
ATOM    614  C   ALA A  76       3.720  27.881   3.987  1.00  5.25           C  
ANISOU  614  C   ALA A  76      865    615    513     26      6      6       C  
ATOM    615  O   ALA A  76       2.637  27.628   3.458  1.00  6.11           O  
ANISOU  615  O   ALA A  76     1061    593    666     66    -75    -72       O  
ATOM    616  CB  ALA A  76       5.649  27.405   2.519  1.00  7.94           C  
ANISOU  616  CB  ALA A  76     1277   1036    703    272    270    138       C  
ATOM    617  N   LEU A  77       3.915  28.988   4.666  1.00  5.10           N  
ANISOU  617  N   LEU A  77      772    579    588     79    -31      8       N  
ATOM    618  CA  LEU A  77       2.952  30.084   4.633  1.00  5.06           C  
ANISOU  618  CA  LEU A  77      847    559    514     66     30     54       C  
ATOM    619  C   LEU A  77       2.992  30.701   3.222  1.00  5.26           C  
ANISOU  619  C   LEU A  77      739    670    590     86    -37     45       C  
ATOM    620  O   LEU A  77       4.004  30.742   2.577  1.00  6.45           O  
ANISOU  620  O   LEU A  77      926    809    717    113     81    150       O  
ATOM    621  CB  LEU A  77       3.278  31.134   5.683  1.00  5.11           C  
ANISOU  621  CB  LEU A  77      753    550    638    112    -22     -1       C  
ATOM    622  CG  LEU A  77       3.249  30.663   7.127  1.00  5.84           C  
ANISOU  622  CG  LEU A  77      798    771    650    211    -36    -20       C  
ATOM    623  CD1 LEU A  77       3.423  31.865   8.021  1.00  7.02           C  
ANISOU  623  CD1 LEU A  77      954   1006    708    180    -19   -211       C  
ATOM    624  CD2 LEU A  77       2.010  29.870   7.469  1.00  6.74           C  
ANISOU  624  CD2 LEU A  77     1040    731    788    105     65     89       C  
ATOM    625  N   THR A  78       1.794  31.187   2.799  1.00  5.26           N  
ANISOU  625  N   THR A  78      860    531    608     41    -80    -23       N  
ATOM    626  CA  THR A  78       1.781  31.908   1.547  1.00  5.61           C  
ANISOU  626  CA  THR A  78      892    598    641     97    -87    -14       C  
ATOM    627  C   THR A  78       2.535  33.231   1.723  1.00  5.66           C  
ANISOU  627  C   THR A  78      920    605    626     22    -73     63       C  
ATOM    628  O   THR A  78       2.814  33.682   2.849  1.00  5.53           O  
ANISOU  628  O   THR A  78      901    625    576    -26    -21     -3       O  
ATOM    629  CB  THR A  78       0.353  32.202   1.121  1.00  6.04           C  
ANISOU  629  CB  THR A  78     1033    585    678     46   -210    -13       C  
ATOM    630  OG1 THR A  78      -0.224  33.127   2.067  1.00  6.19           O  
ANISOU  630  OG1 THR A  78      935    620    797    104   -289    -19       O  
ATOM    631  CG2 THR A  78      -0.501  30.946   0.969  1.00  7.10           C  
ANISOU  631  CG2 THR A  78     1082    710    907    -72   -243    -53       C  
ATOM    632  N   ASP A  79       2.915  33.865   0.618  1.00  6.10           N  
ANISOU  632  N   ASP A  79     1125    615    578     -9     -2    -19       N  
ATOM    633  CA  ASP A  79       3.530  35.166   0.726  1.00  5.96           C  
ANISOU  633  CA  ASP A  79      990    679    595     -7     83     12       C  
ATOM    634  C   ASP A  79       2.622  36.150   1.450  1.00  5.72           C  
ANISOU  634  C   ASP A  79     1032    507    636    -22    -52     35       C  
ATOM    635  O   ASP A  79       3.117  36.981   2.239  1.00  6.31           O  
ANISOU  635  O   ASP A  79     1088    603    708      7      0    -81       O  
ATOM    636  CB  ASP A  79       3.868  35.704  -0.680  1.00  7.32           C  
ANISOU  636  CB  ASP A  79     1244    815    722    -60    164     32       C  
ATOM    637  CG  ASP A  79       5.009  34.948  -1.370  1.00  9.57           C  
ANISOU  637  CG  ASP A  79     1701    951    986   -117    506   -128       C  
ATOM    638  OD1 ASP A  79       5.743  34.152  -0.708  1.00 10.26           O  
ANISOU  638  OD1 ASP A  79     1567   1056   1276     83    607   -135       O  
ATOM    639  OD2 ASP A  79       5.131  35.216  -2.601  1.00 12.25           O  
ANISOU  639  OD2 ASP A  79     2096   1650    908    148    654   -151       O  
ATOM    640  N   ALA A  80       1.314  36.077   1.241  1.00  5.76           N  
ANISOU  640  N   ALA A  80     1051    557    580     68    -65     15       N  
ATOM    641  CA  ALA A  80       0.384  36.944   1.941  1.00  5.84           C  
ANISOU  641  CA  ALA A  80     1059    563    598     56    -94     68       C  
ATOM    642  C   ALA A  80       0.412  36.702   3.446  1.00  5.48           C  
ANISOU  642  C   ALA A  80      884    539    661     43   -106     -8       C  
ATOM    643  O   ALA A  80       0.456  37.646   4.243  1.00  5.56           O  
ANISOU  643  O   ALA A  80      921    504    685     82   -104     -9       O  
ATOM    644  CB  ALA A  80      -1.022  36.775   1.394  1.00  7.06           C  
ANISOU  644  CB  ALA A  80     1097    722    865     66   -283     80       C  
ATOM    645  N   GLU A  81       0.350  35.433   3.860  1.00  5.14           N  
ANISOU  645  N   GLU A  81      839    442    671     38   -159     20       N  
ATOM    646  CA  GLU A  81       0.391  35.100   5.267  1.00  5.16           C  
ANISOU  646  CA  GLU A  81      740    508    712     52    -96     -8       C  
ATOM    647  C   GLU A  81       1.712  35.551   5.900  1.00  4.79           C  
ANISOU  647  C   GLU A  81      828    378    615     25   -132      4       C  
ATOM    648  O   GLU A  81       1.728  36.058   7.015  1.00  5.39           O  
ANISOU  648  O   GLU A  81      750    557    741     33    -58    -69       O  
ATOM    649  CB  GLU A  81       0.220  33.584   5.460  1.00  5.17           C  
ANISOU  649  CB  GLU A  81      742    421    800     61   -112     34       C  
ATOM    650  CG  GLU A  81      -1.175  33.054   5.229  1.00  5.42           C  
ANISOU  650  CG  GLU A  81      743    534    784     35   -117     15       C  
ATOM    651  CD  GLU A  81      -1.231  31.523   5.086  1.00  5.04           C  
ANISOU  651  CD  GLU A  81      779    559    578     -8    -67     69       C  
ATOM    652  OE1 GLU A  81      -0.222  30.907   4.721  1.00  5.64           O  
ANISOU  652  OE1 GLU A  81      755    523    863     24     47     32       O  
ATOM    653  OE2 GLU A  81      -2.347  30.960   5.286  1.00  5.90           O  
ANISOU  653  OE2 GLU A  81      715    616    910    -46    -52     51       O  
ATOM    654  N   THR A  82       2.800  35.345   5.173  1.00  4.73           N  
ANISOU  654  N   THR A  82      767    460    572     65    -88    -20       N  
ATOM    655  CA  THR A  82       4.113  35.694   5.683  1.00  4.97           C  
ANISOU  655  CA  THR A  82      798    508    581      0    -70     63       C  
ATOM    656  C   THR A  82       4.202  37.196   5.971  1.00  4.85           C  
ANISOU  656  C   THR A  82      705    545    592     11    -61    -15       C  
ATOM    657  O   THR A  82       4.668  37.632   7.022  1.00  5.30           O  
ANISOU  657  O   THR A  82      768    595    650      8    -94     11       O  
ATOM    658  CB  THR A  82       5.201  35.276   4.678  1.00  5.53           C  
ANISOU  658  CB  THR A  82      777    538    788     90     -3      9       C  
ATOM    659  OG1 THR A  82       5.152  33.852   4.485  1.00  6.09           O  
ANISOU  659  OG1 THR A  82      936    549    829     93    -60    -73       O  
ATOM    660  CG2 THR A  82       6.575  35.621   5.145  1.00  6.81           C  
ANISOU  660  CG2 THR A  82      883    733    973     44    -59   -161       C  
ATOM    661  N   LYS A  83       3.791  37.990   4.981  1.00  5.30           N  
ANISOU  661  N   LYS A  83      892    485    635     15   -135     30       N  
ATOM    662  CA ALYS A  83       3.858  39.423   5.149  0.62  5.85           C  
ANISOU  662  CA ALYS A  83     1004    455    765     -6   -101     45       C  
ATOM    663  CA BLYS A  83       3.904  39.434   5.159  0.38  5.95           C  
ANISOU  663  CA BLYS A  83     1025    501    735     18   -106     66       C  
ATOM    664  C   LYS A  83       2.907  39.953   6.179  1.00  5.59           C  
ANISOU  664  C   LYS A  83      948    465    711     63   -258     69       C  
ATOM    665  O   LYS A  83       3.200  40.986   6.824  1.00  5.95           O  
ANISOU  665  O   LYS A  83     1018    496    747     -4   -189     -1       O  
ATOM    666  CB ALYS A  83       3.521  40.103   3.798  0.62  9.46           C  
ANISOU  666  CB ALYS A  83     2281    575    738    219   -110     58       C  
ATOM    667  CB BLYS A  83       3.748  40.174   3.818  0.38  7.70           C  
ANISOU  667  CB BLYS A  83     1676    470    778   -235   -119    136       C  
ATOM    668  CG ALYS A  83       4.681  40.143   2.880  0.62 10.85           C  
ANISOU  668  CG ALYS A  83     2469    805    848    -43    111      8       C  
ATOM    669  CG BLYS A  83       4.848  40.115   2.827  0.38 11.84           C  
ANISOU  669  CG BLYS A  83     2303   1268    928     62    326    117       C  
ATOM    670  CD ALYS A  83       5.655  41.207   3.305  0.62 12.39           C  
ANISOU  670  CD ALYS A  83     2656   1108    942   -268   -395    268       C  
ATOM    671  CD BLYS A  83       6.244  40.459   3.278  0.38 18.00           C  
ANISOU  671  CD BLYS A  83     2163   2364   2314   -783    864   -330       C  
ATOM    672  CE ALYS A  83       6.457  41.719   2.150  0.62 12.73           C  
ANISOU  672  CE ALYS A  83     1904   1674   1260   -238   -332    219       C  
ATOM    673  CE BLYS A  83       6.723  41.813   2.791  0.38 15.23           C  
ANISOU  673  CE BLYS A  83     1292   2520   1976    113     93    855       C  
ATOM    674  NZ ALYS A  83       7.399  40.701   1.677  0.62 17.68           N  
ANISOU  674  NZ ALYS A  83     3765   1981    972    681     25    284       N  
ATOM    675  NZ BLYS A  83       8.171  41.866   2.496  0.38 13.00           N  
ANISOU  675  NZ BLYS A  83     1241   2175   1525    194    114   1313       N  
ATOM    676  N   ALA A  84       1.746  39.331   6.359  1.00  5.57           N  
ANISOU  676  N   ALA A  84      924    474    717     72   -207    -38       N  
ATOM    677  CA  ALA A  84       0.849  39.738   7.385  1.00  6.10           C  
ANISOU  677  CA  ALA A  84      951    522    844     47   -235    -37       C  
ATOM    678  C   ALA A  84       1.423  39.479   8.794  1.00  5.26           C  
ANISOU  678  C   ALA A  84      673    551    776     12   -108    -58       C  
ATOM    679  O   ALA A  84       1.324  40.287   9.703  1.00  6.01           O  
ANISOU  679  O   ALA A  84      849    595    838     88   -145   -108       O  
ATOM    680  CB  ALA A  84      -0.503  39.024   7.240  1.00  6.73           C  
ANISOU  680  CB  ALA A  84      795    778    982    131   -230    -67       C  
ATOM    681  N   PHE A  85       2.066  38.308   8.942  1.00  5.19           N  
ANISOU  681  N   PHE A  85      741    501    728      7    -66      0       N  
ATOM    682  CA  PHE A  85       2.738  37.916  10.187  1.00  5.22           C  
ANISOU  682  CA  PHE A  85      781    510    691     70    -36     34       C  
ATOM    683  C   PHE A  85       3.804  38.954  10.520  1.00  4.96           C  
ANISOU  683  C   PHE A  85      728    557    600    130    -25    -18       C  
ATOM    684  O   PHE A  85       3.897  39.470  11.626  1.00  5.69           O  
ANISOU  684  O   PHE A  85      814    619    729     42    -67    -52       O  
ATOM    685  CB  PHE A  85       3.264  36.497   9.990  1.00  5.69           C  
ANISOU  685  CB  PHE A  85      935    512    716     89    -11    -30       C  
ATOM    686  CG  PHE A  85       3.712  35.722  11.179  1.00  5.09           C  
ANISOU  686  CG  PHE A  85      673    527    733     36     31     67       C  
ATOM    687  CD1 PHE A  85       3.832  36.228  12.428  1.00  6.54           C  
ANISOU  687  CD1 PHE A  85     1118    632    734    146    102     50       C  
ATOM    688  CD2 PHE A  85       3.957  34.349  10.987  1.00  5.71           C  
ANISOU  688  CD2 PHE A  85      703    595    873     90    -76     28       C  
ATOM    689  CE1 PHE A  85       4.208  35.371  13.494  1.00  7.72           C  
ANISOU  689  CE1 PHE A  85     1402    940    590    345     97    190       C  
ATOM    690  CE2 PHE A  85       4.360  33.553  12.030  1.00  6.47           C  
ANISOU  690  CE2 PHE A  85      806    632   1019    203      3    140       C  
ATOM    691  CZ  PHE A  85       4.495  34.058  13.288  1.00  6.68           C  
ANISOU  691  CZ  PHE A  85      903    827    809    141     61    228       C  
ATOM    692  N   LEU A  86       4.645  39.264   9.506  1.00  5.28           N  
ANISOU  692  N   LEU A  86      734    598    672     26    -45    -58       N  
ATOM    693  CA  LEU A  86       5.712  40.252   9.702  1.00  5.78           C  
ANISOU  693  CA  LEU A  86      716    713    766     10    -81    -70       C  
ATOM    694  C   LEU A  86       5.139  41.594  10.113  1.00  5.48           C  
ANISOU  694  C   LEU A  86      736    642    703    -93   -100    -73       C  
ATOM    695  O   LEU A  86       5.608  42.218  11.076  1.00  6.66           O  
ANISOU  695  O   LEU A  86      857    822    852   -104   -103   -177       O  
ATOM    696  CB  LEU A  86       6.522  40.391   8.402  1.00  6.02           C  
ANISOU  696  CB  LEU A  86      698    703    885     47     29      9       C  
ATOM    697  CG  LEU A  86       7.645  41.433   8.498  1.00  7.05           C  
ANISOU  697  CG  LEU A  86      800    950    930   -105     35    -41       C  
ATOM    698  CD1 LEU A  86       8.689  41.066   9.532  1.00  8.30           C  
ANISOU  698  CD1 LEU A  86      750   1226   1177    -90    -70     31       C  
ATOM    699  CD2 LEU A  86       8.256  41.655   7.134  1.00  9.52           C  
ANISOU  699  CD2 LEU A  86     1146   1314   1157   -202    290    -12       C  
ATOM    700  N   ALA A  87       4.134  42.099   9.387  1.00  5.76           N  
ANISOU  700  N   ALA A  87      790    585    814    -24     -1   -134       N  
ATOM    701  CA  ALA A  87       3.633  43.442   9.673  1.00  6.33           C  
ANISOU  701  CA  ALA A  87      976    536    893    -72    -81    -23       C  
ATOM    702  C   ALA A  87       3.035  43.540  11.054  1.00  6.35           C  
ANISOU  702  C   ALA A  87      867    632    914    -71    -23   -206       C  
ATOM    703  O   ALA A  87       3.165  44.585  11.713  1.00  8.29           O  
ANISOU  703  O   ALA A  87     1229    679   1242   -168    128   -295       O  
ATOM    704  CB  ALA A  87       2.599  43.843   8.634  1.00  7.18           C  
ANISOU  704  CB  ALA A  87     1214    554    960     73   -142      6       C  
ATOM    705  N   ASP A  88       2.357  42.477  11.486  1.00  6.03           N  
ANISOU  705  N   ASP A  88      754    654    881    -41     -2   -167       N  
ATOM    706  CA  ASP A  88       1.768  42.529  12.820  1.00  7.01           C  
ANISOU  706  CA  ASP A  88      904    722   1039    -14    150   -249       C  
ATOM    707  C   ASP A  88       2.797  42.538  13.915  1.00  7.24           C  
ANISOU  707  C   ASP A  88     1029    817    907   -205    197   -272       C  
ATOM    708  O   ASP A  88       2.568  43.194  14.909  1.00 11.26           O  
ANISOU  708  O   ASP A  88     1748   1397   1132   -116    241   -487       O  
ATOM    709  CB  ASP A  88       0.838  41.318  12.967  1.00  7.40           C  
ANISOU  709  CB  ASP A  88      763    835   1216     -6    107    -81       C  
ATOM    710  CG  ASP A  88       0.054  41.419  14.228  1.00 12.74           C  
ANISOU  710  CG  ASP A  88     2087    801   1951    -98   1042    -12       C  
ATOM    711  OD1 ASP A  88      -0.743  42.373  14.417  1.00 13.81           O  
ANISOU  711  OD1 ASP A  88     1473   1922   1854    280    427   -476       O  
ATOM    712  OD2 ASP A  88       0.162  40.524  15.032  1.00 22.67           O  
ANISOU  712  OD2 ASP A  88     5008   1117   2490    676   2398    309       O  
ATOM    713  N   GLY A  89       3.905  41.792  13.723  1.00  7.00           N  
ANISOU  713  N   GLY A  89     1012    970    678   -264      7   -177       N  
ATOM    714  CA  GLY A  89       4.878  41.656  14.770  1.00  8.18           C  
ANISOU  714  CA  GLY A  89     1177   1131    799   -385    -92     32       C  
ATOM    715  C   GLY A  89       5.985  42.656  14.774  1.00  6.80           C  
ANISOU  715  C   GLY A  89      988    912    682   -133    -19    -90       C  
ATOM    716  O   GLY A  89       6.642  42.866  15.824  1.00  6.67           O  
ANISOU  716  O   GLY A  89      919    869    746    -18    -99    -69       O  
ATOM    717  N   ASP A  90       6.284  43.276  13.653  1.00  6.64           N  
ANISOU  717  N   ASP A  90      876    865    782   -169    -81    -36       N  
ATOM    718  CA  ASP A  90       7.492  44.090  13.495  1.00  5.78           C  
ANISOU  718  CA  ASP A  90      736    711    748    -30    -71     42       C  
ATOM    719  C   ASP A  90       7.242  45.523  13.985  1.00  6.16           C  
ANISOU  719  C   ASP A  90      711    742    887     29   -183     15       C  
ATOM    720  O   ASP A  90       7.125  46.492  13.242  1.00  7.37           O  
ANISOU  720  O   ASP A  90      990    766   1042    125   -166     76       O  
ATOM    721  CB  ASP A  90       7.964  44.088  12.060  1.00  6.11           C  
ANISOU  721  CB  ASP A  90      854    698    770    -77   -120     39       C  
ATOM    722  CG  ASP A  90       9.241  44.862  11.862  1.00  5.88           C  
ANISOU  722  CG  ASP A  90      679    747    809     56   -134     61       C  
ATOM    723  OD1 ASP A  90       9.950  45.096  12.874  1.00  6.49           O  
ANISOU  723  OD1 ASP A  90      749    766    950     61   -175    128       O  
ATOM    724  OD2 ASP A  90       9.526  45.234  10.708  1.00  7.19           O  
ANISOU  724  OD2 ASP A  90      773   1008    951    -39   -131    133       O  
ATOM    725  N   LYS A  91       7.115  45.639  15.313  1.00  6.56           N  
ANISOU  725  N   LYS A  91      952    709    831    140    -57    -55       N  
ATOM    726  CA ALYS A  91       6.816  46.897  15.992  0.50  7.23           C  
ANISOU  726  CA ALYS A  91     1081    826    840    270   -121    -32       C  
ATOM    727  CA BLYS A  91       6.757  46.943  15.871  0.50  8.71           C  
ANISOU  727  CA BLYS A  91     1074    844   1393    305     67   -211       C  
ATOM    728  C   LYS A  91       7.893  47.939  15.862  1.00  7.40           C  
ANISOU  728  C   LYS A  91     1173    680    959    223   -174    -76       C  
ATOM    729  O   LYS A  91       7.592  49.106  16.076  1.00  8.58           O  
ANISOU  729  O   LYS A  91     1395    817   1047    308    -85   -108       O  
ATOM    730  CB ALYS A  91       6.452  46.596  17.461  0.50 10.35           C  
ANISOU  730  CB ALYS A  91     2026   1064    844     64    157    -78       C  
ATOM    731  CB BLYS A  91       6.166  46.675  17.266  0.50 10.01           C  
ANISOU  731  CB BLYS A  91     1252    928   1623    434    474   -134       C  
ATOM    732  CG ALYS A  91       5.068  45.977  17.634  0.50 11.88           C  
ANISOU  732  CG ALYS A  91     2259    821   1433   -110    518      8       C  
ATOM    733  CG BLYS A  91       4.828  45.958  17.228  0.50 11.27           C  
ANISOU  733  CG BLYS A  91     1380   1422   1479    259    561   -708       C  
ATOM    734  CD ALYS A  91       4.146  46.070  16.419  0.50 19.64           C  
ANISOU  734  CD ALYS A  91     2284   2602   2575    151   -312  -1279       C  
ATOM    735  CD BLYS A  91       3.683  46.574  16.421  0.50 14.81           C  
ANISOU  735  CD BLYS A  91     1306   1947   2372    596    242  -1028       C  
ATOM    736  CE ALYS A  91       2.755  45.458  16.542  0.50 19.51           C  
ANISOU  736  CE ALYS A  91     2230   2297   2888    466    -22   -611       C  
ATOM    737  CE BLYS A  91       2.348  45.781  16.590  0.50 14.32           C  
ANISOU  737  CE BLYS A  91     1266   2417   1758    701    618   -646       C  
ATOM    738  NZ ALYS A  91       2.171  45.953  17.819  0.50 20.12           N  
ANISOU  738  NZ ALYS A  91     2196   2709   2741   1446   -264   -278       N  
ATOM    739  NZ BLYS A  91       1.288  46.509  15.811  0.50 12.25           N  
ANISOU  739  NZ BLYS A  91     1355   2073   1228   -153    414   -338       N  
ATOM    740  N   ASP A  92       9.142  47.569  15.574  1.00  7.96           N  
ANISOU  740  N   ASP A  92     1061    708   1255    176   -292   -158       N  
ATOM    741  CA  ASP A  92      10.207  48.551  15.415  1.00  8.64           C  
ANISOU  741  CA  ASP A  92     1047    799   1439     54   -375   -188       C  
ATOM    742  C   ASP A  92      10.563  48.774  13.956  1.00  9.47           C  
ANISOU  742  C   ASP A  92     1161    769   1669    -14   -325    123       C  
ATOM    743  O   ASP A  92      11.394  49.664  13.657  1.00 12.51           O  
ANISOU  743  O   ASP A  92     1659    951   2144   -266   -191    202       O  
ATOM    744  CB  ASP A  92      11.436  48.235  16.260  1.00  9.68           C  
ANISOU  744  CB  ASP A  92     1184   1063   1431      3   -351   -352       C  
ATOM    745  CG  ASP A  92      12.183  47.011  15.931  1.00 10.36           C  
ANISOU  745  CG  ASP A  92     1092   1126   1719    192   -628   -400       C  
ATOM    746  OD1 ASP A  92      11.980  46.421  14.863  1.00  7.93           O  
ANISOU  746  OD1 ASP A  92      721    911   1381    -77   -123    -68       O  
ATOM    747  OD2 ASP A  92      13.075  46.669  16.772  1.00 15.53           O  
ANISOU  747  OD2 ASP A  92     1895   2021   1984    702  -1008   -477       O  
ATOM    748  N   GLY A  93       9.942  48.099  13.014  1.00  8.64           N  
ANISOU  748  N   GLY A  93     1169    775   1339     82   -120    180       N  
ATOM    749  CA  GLY A  93      10.092  48.437  11.632  1.00  9.55           C  
ANISOU  749  CA  GLY A  93     1230    942   1457    266    -34    250       C  
ATOM    750  C   GLY A  93      11.350  48.035  10.922  1.00 11.29           C  
ANISOU  750  C   GLY A  93     1603   1086   1600    356    258    594       C  
ATOM    751  O   GLY A  93      11.576  48.504   9.822  1.00 20.04           O  
ANISOU  751  O   GLY A  93     3239   2359   2017   1666   1168   1292       O  
ATOM    752  N   ASP A  94      12.170  47.172  11.523  1.00  8.29           N  
ANISOU  752  N   ASP A  94     1045    802   1302     21    -73    249       N  
ATOM    753  CA  ASP A  94      13.413  46.765  10.927  1.00  9.04           C  
ANISOU  753  CA  ASP A  94     1014   1094   1325   -196     79    364       C  
ATOM    754  C   ASP A  94      13.294  45.609   9.941  1.00  8.58           C  
ANISOU  754  C   ASP A  94      984   1038   1239    -15     68    344       C  
ATOM    755  O   ASP A  94      14.288  45.146   9.394  1.00 10.44           O  
ANISOU  755  O   ASP A  94     1017   1607   1344   -135    187    216       O  
ATOM    756  CB  ASP A  94      14.515  46.439  11.961  1.00  9.30           C  
ANISOU  756  CB  ASP A  94      834   1109   1590   -184      7    189       C  
ATOM    757  CG  ASP A  94      14.219  45.201  12.768  1.00  7.80           C  
ANISOU  757  CG  ASP A  94      723   1043   1195    -31    -84      1       C  
ATOM    758  OD1 ASP A  94      13.083  44.624  12.591  1.00  6.81           O  
ANISOU  758  OD1 ASP A  94      651    886   1049    -48    -49    139       O  
ATOM    759  OD2 ASP A  94      15.083  44.777  13.546  1.00  8.30           O  
ANISOU  759  OD2 ASP A  94      655   1188   1312     52    -99    134       O  
ATOM    760  N   GLY A  95      12.083  45.147   9.660  1.00  7.59           N  
ANISOU  760  N   GLY A  95      896   1028    960    124    -15    340       N  
ATOM    761  CA  GLY A  95      11.880  44.113   8.669  1.00  7.59           C  
ANISOU  761  CA  GLY A  95      959   1132    791     56     56    286       C  
ATOM    762  C   GLY A  95      12.059  42.691   9.183  1.00  6.69           C  
ANISOU  762  C   GLY A  95      717   1059    766     57     -8    166       C  
ATOM    763  O   GLY A  95      12.008  41.757   8.398  1.00  7.42           O  
ANISOU  763  O   GLY A  95      929   1104    787    -12     23     93       O  
ATOM    764  N   MET A  96      12.212  42.549  10.495  1.00  6.24           N  
ANISOU  764  N   MET A  96      764    859    747     14    -19    137       N  
ATOM    765  CA AMET A  96      12.496  41.285  11.151  0.64  6.15           C  
ANISOU  765  CA AMET A  96      813    832    690    -73      0    185       C  
ATOM    766  CA BMET A  96      12.345  41.200  11.067  0.36  6.11           C  
ANISOU  766  CA BMET A  96      673    845    806     76     18    176       C  
ATOM    767  C   MET A  96      11.762  41.222  12.470  1.00  5.44           C  
ANISOU  767  C   MET A  96      576    760    731    -22    -27     48       C  
ATOM    768  O   MET A  96      11.263  42.269  12.948  1.00  6.19           O  
ANISOU  768  O   MET A  96      795    765    791     45    -38     30       O  
ATOM    769  CB AMET A  96      13.995  41.087  11.426  0.64  9.52           C  
ANISOU  769  CB AMET A  96      991   1425   1202    612    477    778       C  
ATOM    770  CB BMET A  96      13.793  40.735  10.898  0.36  7.44           C  
ANISOU  770  CB BMET A  96      836   1206    787    195    142    188       C  
ATOM    771  CG AMET A  96      14.915  41.313  10.294  0.64  7.61           C  
ANISOU  771  CG AMET A  96      748   1181    964    -38    114    241       C  
ATOM    772  CG BMET A  96      14.797  41.691  11.545  0.36  8.59           C  
ANISOU  772  CG BMET A  96      804   1502    958   -276   -140    851       C  
ATOM    773  SD AMET A  96      16.626  41.076  10.772  0.64  8.20           S  
ANISOU  773  SD AMET A  96      733    923   1458   -108   -219    242       S  
ATOM    774  SD BMET A  96      16.471  41.410  10.941  0.36 12.94           S  
ANISOU  774  SD BMET A  96      902   1431   2584     -8   -162    427       S  
ATOM    775  CE AMET A  96      17.084  42.551  11.642  0.64  8.69           C  
ANISOU  775  CE AMET A  96      838    797   1665   -167    260    136       C  
ATOM    776  CE BMET A  96      17.315  42.823  11.675  0.36 15.09           C  
ANISOU  776  CE BMET A  96     1399   1704   2630   -964    131    893       C  
ATOM    777  N   ILE A  97      11.733  40.058  13.096  1.00  5.69           N  
ANISOU  777  N   ILE A  97      793    662    707     69     16     29       N  
ATOM    778  CA AILE A  97      11.135  39.972  14.431  0.38  5.93           C  
ANISOU  778  CA AILE A  97      722    860    672    148     27     87       C  
ATOM    779  CA BILE A  97      11.105  39.903  14.411  0.62  5.34           C  
ANISOU  779  CA BILE A  97      686    678    664    111     48     20       C  
ATOM    780  C   ILE A  97      12.180  39.534  15.434  1.00  5.29           C  
ANISOU  780  C   ILE A  97      657    734    620     82     51      1       C  
ATOM    781  O   ILE A  97      12.835  38.492  15.296  1.00  5.90           O  
ANISOU  781  O   ILE A  97      816    750    674    124    -15      8       O  
ATOM    782  CB AILE A  97       9.959  38.980  14.386  0.38  7.05           C  
ANISOU  782  CB AILE A  97      584   1117    976    105     10    181       C  
ATOM    783  CB BILE A  97      10.004  38.807  14.375  0.62  5.81           C  
ANISOU  783  CB BILE A  97      767    680    760     33    -23     50       C  
ATOM    784  CG1AILE A  97       8.827  39.632  13.567  0.38  6.35           C  
ANISOU  784  CG1AILE A  97      871    759    782     22   -180      6       C  
ATOM    785  CG1BILE A  97       8.905  39.074  13.337  0.62  5.62           C  
ANISOU  785  CG1BILE A  97      781    614    741     43    -20   -160       C  
ATOM    786  CG2AILE A  97       9.468  38.540  15.741  0.38  6.11           C  
ANISOU  786  CG2AILE A  97      676    681    963    284     59    175       C  
ATOM    787  CG2BILE A  97       9.387  38.666  15.768  0.62  7.45           C  
ANISOU  787  CG2BILE A  97      887   1152    792   -207    -14    287       C  
ATOM    788  CD1AILE A  97       7.665  38.699  13.330  0.38  8.80           C  
ANISOU  788  CD1AILE A  97     1000   1280   1061   -247   -439     78       C  
ATOM    789  CD1BILE A  97       8.118  40.369  13.542  0.62  6.71           C  
ANISOU  789  CD1BILE A  97      794    856    900    146   -232   -236       C  
ATOM    790  N   GLY A  98      12.354  40.365  16.453  1.00  5.63           N  
ANISOU  790  N   GLY A  98      789    711    638    127     82     59       N  
ATOM    791  CA  GLY A  98      13.281  40.058  17.536  1.00  6.12           C  
ANISOU  791  CA  GLY A  98      765    858    702    -54     37     16       C  
ATOM    792  C   GLY A  98      12.521  39.381  18.704  1.00  5.73           C  
ANISOU  792  C   GLY A  98      732    804    640      9     51     17       C  
ATOM    793  O   GLY A  98      11.300  39.242  18.701  1.00  6.08           O  
ANISOU  793  O   GLY A  98      704    950    656     95     53     10       O  
ATOM    794  N   VAL A  99      13.279  38.968  19.727  1.00  6.14           N  
ANISOU  794  N   VAL A  99      692    983    657    -24    -18     18       N  
ATOM    795  CA  VAL A  99      12.678  38.150  20.771  1.00  6.40           C  
ANISOU  795  CA  VAL A  99      776   1046    610    -51    -31     58       C  
ATOM    796  C   VAL A  99      11.573  38.873  21.493  1.00  6.41           C  
ANISOU  796  C   VAL A  99      749   1066    622     37    -88     61       C  
ATOM    797  O   VAL A  99      10.512  38.304  21.772  1.00  7.03           O  
ANISOU  797  O   VAL A  99      799   1071    800    -71     79     30       O  
ATOM    798  CB  VAL A  99      13.750  37.606  21.750  1.00  6.79           C  
ANISOU  798  CB  VAL A  99      768   1165    649    121    -61    -19       C  
ATOM    799  CG1 VAL A  99      14.509  38.669  22.520  1.00  8.15           C  
ANISOU  799  CG1 VAL A  99      992   1345    760    -15   -192     16       C  
ATOM    800  CG2 VAL A  99      13.116  36.576  22.684  1.00  7.80           C  
ANISOU  800  CG2 VAL A  99      983   1215    765    126    -36    186       C  
ATOM    801  N   ASP A 100      11.762  40.159  21.806  1.00  6.95           N  
ANISOU  801  N   ASP A 100      844   1105    694    -33    131    -32       N  
ATOM    802  CA  ASP A 100      10.736  40.893  22.533  1.00  7.44           C  
ANISOU  802  CA  ASP A 100      921   1198    706     33    115   -130       C  
ATOM    803  C   ASP A 100       9.469  41.080  21.669  1.00  7.09           C  
ANISOU  803  C   ASP A 100      937   1058    699      0    172     25       C  
ATOM    804  O   ASP A 100       8.357  41.007  22.174  1.00  7.83           O  
ANISOU  804  O   ASP A 100      882   1251    841     21    218    -70       O  
ATOM    805  CB  ASP A 100      11.266  42.243  23.034  1.00  9.46           C  
ANISOU  805  CB  ASP A 100     1101   1369   1122    -59    235   -506       C  
ATOM    806  CG  ASP A 100      12.324  42.101  24.123  1.00 11.97           C  
ANISOU  806  CG  ASP A 100     1600   2129    820   -548    267   -458       C  
ATOM    807  OD1 ASP A 100      12.413  41.039  24.767  1.00 11.87           O  
ANISOU  807  OD1 ASP A 100     1294   2239    978   -192    -14   -417       O  
ATOM    808  OD2 ASP A 100      12.993  43.136  24.238  1.00 17.85           O  
ANISOU  808  OD2 ASP A 100     2209   2663   1908  -1116   -331   -319       O  
ATOM    809  N   GLU A 101       9.653  41.304  20.377  1.00  6.76           N  
ANISOU  809  N   GLU A 101      818    991    760     56    150     17       N  
ATOM    810  CA  GLU A 101       8.527  41.415  19.460  1.00  6.54           C  
ANISOU  810  CA  GLU A 101      791    879    814    150    181     43       C  
ATOM    811  C   GLU A 101       7.774  40.099  19.370  1.00  6.58           C  
ANISOU  811  C   GLU A 101      670    969    859    140    170    111       C  
ATOM    812  O   GLU A 101       6.541  40.071  19.333  1.00  7.34           O  
ANISOU  812  O   GLU A 101      815    960   1015     81    149    169       O  
ATOM    813  CB  GLU A 101       8.970  41.825  18.056  1.00  6.18           C  
ANISOU  813  CB  GLU A 101      869    732    747    125    130    -53       C  
ATOM    814  CG  GLU A 101       9.334  43.291  17.942  1.00  6.30           C  
ANISOU  814  CG  GLU A 101      881    726    786    144    101      3       C  
ATOM    815  CD  GLU A 101      10.022  43.595  16.644  1.00  5.61           C  
ANISOU  815  CD  GLU A 101      664    697    771     65     -9    -78       C  
ATOM    816  OE1 GLU A 101      10.671  42.734  16.048  1.00  7.73           O  
ANISOU  816  OE1 GLU A 101     1242    781    915    191    328    125       O  
ATOM    817  OE2 GLU A 101       9.932  44.770  16.193  1.00  7.73           O  
ANISOU  817  OE2 GLU A 101     1111    729   1095    166    263     60       O  
ATOM    818  N   PHE A 102       8.490  38.997  19.355  1.00  6.45           N  
ANISOU  818  N   PHE A 102      780    853    818     66    153    110       N  
ATOM    819  CA  PHE A 102       7.870  37.683  19.301  1.00  6.33           C  
ANISOU  819  CA  PHE A 102      703    868    834     70    116     97       C  
ATOM    820  C   PHE A 102       7.015  37.438  20.556  1.00  6.55           C  
ANISOU  820  C   PHE A 102      718    963    807    132    115    119       C  
ATOM    821  O   PHE A 102       5.856  37.065  20.475  1.00  7.39           O  
ANISOU  821  O   PHE A 102      747   1046   1016     81    183    171       O  
ATOM    822  CB  PHE A 102       8.961  36.633  19.154  1.00  6.58           C  
ANISOU  822  CB  PHE A 102      705    912    885    105     37    112       C  
ATOM    823  CG  PHE A 102       8.505  35.213  19.048  1.00  6.62           C  
ANISOU  823  CG  PHE A 102      660    935    921     61     98     -4       C  
ATOM    824  CD1 PHE A 102       8.080  34.662  17.845  1.00  7.73           C  
ANISOU  824  CD1 PHE A 102      854   1136    948     47     29    -31       C  
ATOM    825  CD2 PHE A 102       8.557  34.390  20.154  1.00  6.84           C  
ANISOU  825  CD2 PHE A 102      755    918    926    134     99    112       C  
ATOM    826  CE1 PHE A 102       7.760  33.297  17.768  1.00  8.93           C  
ANISOU  826  CE1 PHE A 102     1045   1184   1165    -48    195   -349       C  
ATOM    827  CE2 PHE A 102       8.214  33.045  20.087  1.00  8.12           C  
ANISOU  827  CE2 PHE A 102      863    918   1305    129    124    205       C  
ATOM    828  CZ  PHE A 102       7.845  32.543  18.903  1.00  8.97           C  
ANISOU  828  CZ  PHE A 102      971    991   1446    -30    409    -48       C  
ATOM    829  N   ALA A 103       7.615  37.719  21.709  1.00  7.10           N  
ANISOU  829  N   ALA A 103      770   1094    835     36    104    173       N  
ATOM    830  CA  ALA A 103       6.870  37.544  22.939  1.00  8.38           C  
ANISOU  830  CA  ALA A 103      824   1537    822     33    127    329       C  
ATOM    831  C   ALA A 103       5.661  38.450  22.982  1.00  7.86           C  
ANISOU  831  C   ALA A 103      873   1398    717    -11    129    128       C  
ATOM    832  O   ALA A 103       4.594  38.044  23.466  1.00  8.50           O  
ANISOU  832  O   ALA A 103      832   1549    847    -60    149    113       O  
ATOM    833  CB  ALA A 103       7.779  37.768  24.141  1.00  9.77           C  
ANISOU  833  CB  ALA A 103     1011   1772    928    -51     28    309       C  
ATOM    834  N   ALA A 104       5.773  39.675  22.498  1.00  8.42           N  
ANISOU  834  N   ALA A 104      866   1366    969     48    252     72       N  
ATOM    835  CA  ALA A 104       4.671  40.643  22.527  1.00  9.17           C  
ANISOU  835  CA  ALA A 104     1020   1308   1157    189    291   -124       C  
ATOM    836  C   ALA A 104       3.483  40.159  21.714  1.00  8.44           C  
ANISOU  836  C   ALA A 104      940   1199   1069    259    242     67       C  
ATOM    837  O   ALA A 104       2.342  40.421  22.084  1.00 10.98           O  
ANISOU  837  O   ALA A 104     1002   1776   1392    344    212   -150       O  
ATOM    838  CB  ALA A 104       5.081  41.998  22.078  1.00 10.27           C  
ANISOU  838  CB  ALA A 104     1289   1298   1317    160    328    -35       C  
ATOM    839  N   MET A 105       3.712  39.477  20.576  1.00  8.06           N  
ANISOU  839  N   MET A 105     1055   1132    875    368    189    224       N  
ATOM    840  CA AMET A 105       2.620  38.983  19.770  0.67  9.11           C  
ANISOU  840  CA AMET A 105     1069   1549    844    641    -11     92       C  
ATOM    841  CA BMET A 105       2.617  38.980  19.753  0.33 10.14           C  
ANISOU  841  CA BMET A 105     1339   1752    761    414    -52    211       C  
ATOM    842  C   MET A 105       1.863  37.849  20.484  1.00  8.62           C  
ANISOU  842  C   MET A 105     1143   1245    886    365   -235    -66       C  
ATOM    843  O   MET A 105       0.676  37.668  20.283  1.00 12.94           O  
ANISOU  843  O   MET A 105     1360   1389   2169    178   -772    111       O  
ATOM    844  CB AMET A 105       3.115  38.384  18.453  0.67 13.06           C  
ANISOU  844  CB AMET A 105     1697   2730    537    551   -136    175       C  
ATOM    845  CB BMET A 105       2.878  38.283  18.402  0.33  8.26           C  
ANISOU  845  CB BMET A 105     1090    625   1422   -508    163    -94       C  
ATOM    846  CG AMET A 105       3.360  39.287  17.323  0.67 11.23           C  
ANISOU  846  CG AMET A 105     2104   1230    934   -559     56    -90       C  
ATOM    847  CG BMET A 105       4.274  37.968  18.034  0.33  8.84           C  
ANISOU  847  CG BMET A 105     1041   1284   1034   -344     10   -283       C  
ATOM    848  SD AMET A 105       3.792  38.492  15.786  0.67 10.24           S  
ANISOU  848  SD AMET A 105     1501   1536    854   -654     23   -143       S  
ATOM    849  SD BMET A 105       4.926  38.233  16.372  0.33  8.93           S  
ANISOU  849  SD BMET A 105     1220   1119   1054   -142    104   -274       S  
ATOM    850  CE AMET A 105       5.419  37.807  16.156  0.67 12.20           C  
ANISOU  850  CE AMET A 105     1715   1991    928   -393    -29     80       C  
ATOM    851  CE BMET A 105       3.402  38.489  15.421  0.33 18.29           C  
ANISOU  851  CE BMET A 105     2450   3349   1149   1438   -656  -1155       C  
ATOM    852  N   ILE A 106       2.592  37.086  21.239  1.00  8.50           N  
ANISOU  852  N   ILE A 106      887   1275   1067    246   -209     38       N  
ATOM    853  CA  ILE A 106       2.062  35.882  21.863  1.00  8.14           C  
ANISOU  853  CA  ILE A 106      833   1098   1160     88   -173    -88       C  
ATOM    854  C   ILE A 106       1.383  36.162  23.176  1.00  7.78           C  
ANISOU  854  C   ILE A 106      862    929   1165    148    -81    -95       C  
ATOM    855  O   ILE A 106       0.395  35.494  23.510  1.00  9.36           O  
ANISOU  855  O   ILE A 106      815   1117   1626    -51      2    -79       O  
ATOM    856  CB  ILE A 106       3.215  34.854  22.047  1.00  7.60           C  
ANISOU  856  CB  ILE A 106      775    968   1145     67   -182   -205       C  
ATOM    857  CG1 ILE A 106       3.626  34.400  20.662  1.00  8.85           C  
ANISOU  857  CG1 ILE A 106      879   1293   1190     88   -268   -407       C  
ATOM    858  CG2 ILE A 106       2.843  33.713  22.930  1.00  8.21           C  
ANISOU  858  CG2 ILE A 106      800    892   1429     95    -14   -127       C  
ATOM    859  CD1 ILE A 106       4.981  33.670  20.597  1.00  9.45           C  
ANISOU  859  CD1 ILE A 106      937   1504   1151    101   -121   -409       C  
ATOM    860  N   LYS A 107       1.959  37.083  23.925  1.00  7.78           N  
ANISOU  860  N   LYS A 107      835   1125    995    -38    172    -63       N  
ATOM    861  CA  LYS A 107       1.468  37.427  25.265  1.00  7.84           C  
ANISOU  861  CA  LYS A 107      821   1219    940    119    157   -136       C  
ATOM    862  C   LYS A 107       0.575  38.689  25.292  1.00  8.04           C  
ANISOU  862  C   LYS A 107     1053   1210    793    127     32   -127       C  
ATOM    863  O   LYS A 107       0.216  39.106  26.328  1.00 13.30           O  
ANISOU  863  O   LYS A 107     2038   1874   1142    828    458     -4       O  
ATOM    864  CB  LYS A 107       2.675  37.474  26.184  1.00  9.45           C  
ANISOU  864  CB  LYS A 107     1177   1432    980    355    142    -61       C  
ATOM    865  CG  LYS A 107       3.471  36.175  26.330  1.00  9.76           C  
ANISOU  865  CG  LYS A 107     1183   1637    890    366      0     35       C  
ATOM    866  CD  LYS A 107       2.680  34.975  26.794  1.00 19.51           C  
ANISOU  866  CD  LYS A 107     3066   1796   2552    970   1576   1117       C  
ATOM    867  CE ALYS A 107       1.959  35.187  28.071  0.53 18.08           C  
ANISOU  867  CE ALYS A 107     2061   1725   3083   1113   1619    819       C  
ATOM    868  CE BLYS A 107       2.151  35.140  28.200  0.47 20.84           C  
ANISOU  868  CE BLYS A 107     3980   2155   1782    711    804   1440       C  
ATOM    869  NZ ALYS A 107       1.479  33.920  28.697  0.53  9.17           N  
ANISOU  869  NZ ALYS A 107     1385   1433    665    322    -14    -11       N  
ATOM    870  NZ BLYS A 107       3.276  35.064  29.180  0.47 23.81           N  
ANISOU  870  NZ BLYS A 107     3199   2463   3386   1301    371  -1926       N  
ATOM    871  N   ALA A 108       0.166  39.151  24.125  1.00 10.08           N  
ANISOU  871  N   ALA A 108     1264   1577    987    285    -13   -109       N  
ATOM    872  CA  ALA A 108      -0.696  40.304  24.011  1.00 10.56           C  
ANISOU  872  CA  ALA A 108     1092   1517   1403    244    -65   -160       C  
ATOM    873  C   ALA A 108      -1.929  40.222  24.914  1.00  9.40           C  
ANISOU  873  C   ALA A 108     1119   1264   1190    220    -68    -52       C  
ATOM    874  O   ALA A 108      -2.327  41.299  25.441  1.00 11.25           O  
ANISOU  874  O   ALA A 108     1390   1417   1469    172    334     -8       O  
ATOM    875  CB  ALA A 108      -1.122  40.462  22.528  1.00 11.69           C  
ANISOU  875  CB  ALA A 108      981   2065   1395    288    114    131       C  
ATOM    876  OXT ALA A 108      -2.534  39.147  24.987  1.00 12.46           O  
ANISOU  876  OXT ALA A 108     1306   1501   1928     34    118   -405       O  
TER     877      ALA A 108                                                      
HETATM  878 CA    CA A 110      17.153  34.014  11.880  1.00  5.67          CA  
ANISOU  878 CA    CA A 110      574    856    725     25     32    -19      CA  
HETATM  879 CA    CA A 111      11.520  44.191  14.302  1.00  5.60          CA  
ANISOU  879 CA    CA A 111      598    718    812     31    -92     60      CA  
HETATM  880  N   NH4 A 200      17.205  34.073   7.423  1.00  8.52           N  
ANISOU  880  N   NH4 A 200     1107   1304    826    400    173    -15       N  
HETATM  881  C   FMT A 150       0.543  36.728  30.783  1.00  8.35           C  
ANISOU  881  C   FMT A 150     1255    876   1042     93     13     14       C  
HETATM  882  O1  FMT A 150      -0.031  37.145  32.124  1.00 13.52           O  
ANISOU  882  O1  FMT A 150     2045   1752   1339    294    162    -19       O  
HETATM  883  O2  FMT A 150       1.508  37.792  30.198  1.00 13.59           O  
ANISOU  883  O2  FMT A 150     1938   1420   1804     60    317    108       O  
HETATM  884  C   FMT A 151       0.767  33.924  -2.279  1.00  8.67           C  
ANISOU  884  C   FMT A 151     1631   1083    582    196    -46     72       C  
HETATM  885  O1  FMT A 151       2.218  33.182  -2.070  1.00 11.53           O  
ANISOU  885  O1  FMT A 151     1742   1480   1160     83    -34    -25       O  
HETATM  886  O2  FMT A 151       0.268  34.803  -1.195  1.00  9.62           O  
ANISOU  886  O2  FMT A 151     1770   1019    866    192   -343    -22       O  
HETATM  887  O   HOH A 201      13.527  43.258  15.138  1.00  8.43           O  
ANISOU  887  O   HOH A 201      665   1274   1264    118   -173    242       O  
HETATM  888  O   HOH A 202       5.424  27.358   7.374  1.00  5.75           O  
ANISOU  888  O   HOH A 202      903    738    544   -101     -1     73       O  
HETATM  889  O   HOH A 203       5.494  42.448  18.329  1.00  7.26           O  
ANISOU  889  O   HOH A 203      923    909    928    169     97    -27       O  
HETATM  890  O   HOH A 204      11.508  29.242  11.126  1.00  6.65           O  
ANISOU  890  O   HOH A 204      856    780    889   -101   -110    259       O  
HETATM  891  O   HOH A 205      -1.000  39.908   3.441  1.00  7.27           O  
ANISOU  891  O   HOH A 205     1210    696    855    260   -140     42       O  
HETATM  892  O   HOH A 206     -11.408  32.786  13.184  1.00  8.37           O  
ANISOU  892  O   HOH A 206      851   1210   1121    142   -212   -131       O  
HETATM  893  O   HOH A 207       1.395  15.133  16.638  1.00  8.25           O  
ANISOU  893  O   HOH A 207     1535    760    839   -359    -82    -63       O  
HETATM  894  O   HOH A 208      -9.351  35.761  15.188  1.00  8.74           O  
ANISOU  894  O   HOH A 208      950   1271   1098    220   -130   -148       O  
HETATM  895  O   HOH A 209       4.514  18.955  21.061  1.00 10.07           O  
ANISOU  895  O   HOH A 209     1373   1457    996   -603    236   -257       O  
HETATM  896  O   HOH A 210       7.925  45.135   8.520  1.00  9.61           O  
ANISOU  896  O   HOH A 210     1358   1155   1138    339   -413    -58       O  
HETATM  897  O   HOH A 211      -1.154  23.529   8.235  1.00  9.80           O  
ANISOU  897  O   HOH A 211     1253   1073   1397     30     58     32       O  
HETATM  898  O   HOH A 212      17.352  31.209   8.158  1.00 10.59           O  
ANISOU  898  O   HOH A 212     1692   1264   1067    601    193   -108       O  
HETATM  899  O   HOH A 213      12.280  42.673  19.507  1.00 10.45           O  
ANISOU  899  O   HOH A 213      974   1565   1432    189    138     78       O  
HETATM  900  O   HOH A 214      -4.135  29.554  12.053  1.00  8.46           O  
ANISOU  900  O   HOH A 214     1230    892   1093    -56    154     94       O  
HETATM  901  O   HOH A 215      -6.746  29.397  13.032  1.00 10.76           O  
ANISOU  901  O   HOH A 215     1260   1267   1562    264     87   -152       O  
HETATM  902  O   HOH A 216       0.209  22.680  24.105  1.00  9.00           O  
ANISOU  902  O   HOH A 216     1401   1079    941    375    -91    -27       O  
HETATM  903  O   HOH A 217      -1.808  18.145  11.920  1.00  8.11           O  
ANISOU  903  O   HOH A 217     1464    732    885   -213   -185    -31       O  
HETATM  904  O   HOH A 218      -7.791  25.659   7.093  1.00  8.19           O  
ANISOU  904  O   HOH A 218     1036   1092    984    -46   -152    -98       O  
HETATM  905  O   HOH A 219      -3.807  27.369  13.969  1.00 10.44           O  
ANISOU  905  O   HOH A 219     1455    828   1684   -137   -545     28       O  
HETATM  906  O   HOH A 220       9.913  20.122  13.134  1.00 10.19           O  
ANISOU  906  O   HOH A 220     1594    992   1285    220    -49    326       O  
HETATM  907  O   HOH A 221      18.313  31.502  17.908  1.00 10.50           O  
ANISOU  907  O   HOH A 221     1050   1801   1139    -25     76      4       O  
HETATM  908  O   HOH A 222      -2.404  29.129  24.492  1.00 10.82           O  
ANISOU  908  O   HOH A 222     1712   1262   1139    -69   -106    -11       O  
HETATM  909  O   HOH A 223       0.828  39.176  -0.819  1.00 10.92           O  
ANISOU  909  O   HOH A 223     1817    974   1360    277    340     58       O  
HETATM  910  O   HOH A 224      13.418  39.620   7.306  1.00 10.31           O  
ANISOU  910  O   HOH A 224     1803    863   1250   -268    -30      2       O  
HETATM  911  O   HOH A 225       5.246  50.214  16.984  1.00 13.38           O  
ANISOU  911  O   HOH A 225     2379   1699   1004   1189    386    344       O  
HETATM  912  O   HOH A 226       0.584  39.926  28.952  1.00 14.52           O  
ANISOU  912  O   HOH A 226     2844   1400   1273    638   -360   -522       O  
HETATM  913  O   HOH A 227      -7.070  29.236  17.734  1.00 13.69           O  
ANISOU  913  O   HOH A 227     1052   1215   2936     67    191   -209       O  
HETATM  914  O   HOH A 228      12.573  25.303   7.625  1.00 11.48           O  
ANISOU  914  O   HOH A 228     1054   1708   1600    158    -72    302       O  
HETATM  915  O   HOH A 229      -6.083  33.746   7.574  1.00 10.90           O  
ANISOU  915  O   HOH A 229     1667   1324   1150    316    -70    -98       O  
HETATM  916  O   HOH A 230       0.453  21.951   6.657  1.00 15.47           O  
ANISOU  916  O   HOH A 230     2289    942   2646    158    864    455       O  
HETATM  917  O   HOH A 231      13.818  44.094  17.677  1.00 11.85           O  
ANISOU  917  O   HOH A 231     1206   2138   1160   -233   -254    307       O  
HETATM  918  O   HOH A 232      14.305  36.504   4.657  1.00 15.35           O  
ANISOU  918  O   HOH A 232     1673   2523   1635   -346    171    613       O  
HETATM  919  O   HOH A 233      17.175  46.165  14.493  1.00 17.56           O  
ANISOU  919  O   HOH A 233     1447   1227   3997   -150  -1246   -113       O  
HETATM  920  O   HOH A 234       0.645  25.960  27.349  1.00 17.75           O  
ANISOU  920  O   HOH A 234     4009   1573   1161   -169    -52    315       O  
HETATM  921  O   HOH A 235       5.197  28.190  31.035  1.00 11.48           O  
ANISOU  921  O   HOH A 235     1657   1428   1277    196   -170    201       O  
HETATM  922  O   HOH A 236       2.239  17.362  10.017  1.00 13.30           O  
ANISOU  922  O   HOH A 236     1563   2195   1295   -672   -322    116       O  
HETATM  923  O   HOH A 237      -3.318  36.426  13.650  1.00 14.93           O  
ANISOU  923  O   HOH A 237     1794   1593   2287    825   -379     63       O  
HETATM  924  O   HOH A 238      -2.885  40.665  27.996  1.00 13.91           O  
ANISOU  924  O   HOH A 238     2982   1373    929   -659      4   -281       O  
HETATM  925  O   HOH A 239      20.295  35.792   8.779  1.00 14.03           O  
ANISOU  925  O   HOH A 239     1378   1890   2062     63    -61    245       O  
HETATM  926  O   HOH A 240      -6.414  27.667  15.300  1.00 13.05           O  
ANISOU  926  O   HOH A 240     2112   1356   1490    270   -330   -321       O  
HETATM  927  O   HOH A 241      17.882  37.894  21.224  1.00 13.52           O  
ANISOU  927  O   HOH A 241     1660   2180   1297   -438   -258    363       O  
HETATM  928  O   HOH A 242      -8.844  23.821   8.850  1.00 13.56           O  
ANISOU  928  O   HOH A 242     1238   1725   2189   -254   -375    713       O  
HETATM  929  O   HOH A 243      17.389  24.628  10.092  1.00 15.65           O  
ANISOU  929  O   HOH A 243     3223   1010   1714    317    743    136       O  
HETATM  930  O   HOH A 244       7.886  41.287  24.837  1.00 21.56           O  
ANISOU  930  O   HOH A 244     1592   5326   1273   -527    271   -710       O  
HETATM  931  O   HOH A 245       4.462  24.075   1.216  1.00 19.37           O  
ANISOU  931  O   HOH A 245     3928   2359   1072    699    -22   -774       O  
HETATM  932  O   HOH A 246      -0.208  35.432   9.130  1.00 13.38           O  
ANISOU  932  O   HOH A 246     1589   1358   2138    -59    201    459       O  
HETATM  933  O   HOH A 247      11.928  30.396   3.259  1.00 14.56           O  
ANISOU  933  O   HOH A 247     1876   1929   1729   -402   -296    102       O  
HETATM  934  O   HOH A 248       0.792  17.241  12.292  1.00  9.51           O  
ANISOU  934  O   HOH A 248     1547    711   1356   -164   -295     65       O  
HETATM  935  O   HOH A 249       8.385  33.745  -1.764  1.00 13.25           O  
ANISOU  935  O   HOH A 249     1389   2612   1032    241   -153   -363       O  
HETATM  936  O   HOH A 250       0.698  23.394  26.644  1.00 18.56           O  
ANISOU  936  O   HOH A 250     3790   1974   1289   1017   -558   -179       O  
HETATM  937  O   HOH A 251      20.169  32.715   6.738  1.00 13.45           O  
ANISOU  937  O   HOH A 251     2080   1502   1529    750    609    205       O  
HETATM  938  O   HOH A 252      23.463  37.924  13.342  1.00 13.71           O  
ANISOU  938  O   HOH A 252     1759   1390   2060   -135    -10   -408       O  
HETATM  939  O   HOH A 253      14.449  40.735  26.510  1.00 15.33           O  
ANISOU  939  O   HOH A 253     1378   2766   1683   -203   -173     56       O  
HETATM  940  O   HOH A 254       8.626  18.996  15.181  1.00 19.91           O  
ANISOU  940  O   HOH A 254     2331   2400   2833   1143   1234   1392       O  
HETATM  941  O   HOH A 255      11.222  45.041  20.834  1.00 17.27           O  
ANISOU  941  O   HOH A 255     2808   2091   1662    -29     60   -167       O  
HETATM  942  O   HOH A 256      -4.998  16.758  17.908  1.00 19.13           O  
ANISOU  942  O   HOH A 256     2024   2208   3036   -776   -928   -152       O  
HETATM  943  O   HOH A 257      11.497  42.246   5.702  1.00 21.04           O  
ANISOU  943  O   HOH A 257     2004   4611   1379   -763   -281   1131       O  
HETATM  944  O   HOH A 258      15.913  36.323  25.382  1.00 18.90           O  
ANISOU  944  O   HOH A 258     2955   2979   1247   -430    325    104       O  
HETATM  945  O   HOH A 259      -4.729  31.155  24.590  1.00 20.74           O  
ANISOU  945  O   HOH A 259     2657   3466   1757    408   -113   -115       O  
HETATM  946  O   HOH A 260       2.863  43.020  18.770  1.00 18.01           O  
ANISOU  946  O   HOH A 260     1071   2097   3675    208   -252   -735       O  
HETATM  947  O   HOH A 261      -2.735  35.732   8.277  1.00 16.32           O  
ANISOU  947  O   HOH A 261     1968   1417   2817   -453   -592    577       O  
HETATM  948  O   HOH A 262      -7.081  27.343  21.991  1.00 21.05           O  
ANISOU  948  O   HOH A 262     1791   3640   2568   1234    263    180       O  
HETATM  949  O   HOH A 263      -3.015  36.500   5.563  1.00 18.80           O  
ANISOU  949  O   HOH A 263     2119   2243   2782    179   -192    825       O  
HETATM  950  O   HOH A 264       2.020  46.639  13.013  1.00 16.16           O  
ANISOU  950  O   HOH A 264     1895   1250   2994   -429    886   -863       O  
HETATM  951  O   HOH A 265     -10.045  27.165   6.409  1.00 14.97           O  
ANISOU  951  O   HOH A 265     1602   1903   2184    148   -427    -36       O  
HETATM  952  O   HOH A 266       3.329  39.247  -0.205  1.00 21.47           O  
ANISOU  952  O   HOH A 266     2361    811   4984    263  -1705   -220       O  
HETATM  953  O   HOH A 267      -2.334  36.497  24.182  1.00 18.76           O  
ANISOU  953  O   HOH A 267     2374   1795   2959   -545   1044   -880       O  
HETATM  954  O   HOH A 268      10.437  40.026  26.350  1.00 20.38           O  
ANISOU  954  O   HOH A 268     3749   1981   2014    126    688    342       O  
HETATM  955  O   HOH A 269      15.945  31.937   2.166  1.00 17.65           O  
ANISOU  955  O   HOH A 269     1196   3526   1984   -177    339   -781       O  
HETATM  956  O   HOH A 270      11.572  32.713   1.532  1.00 17.31           O  
ANISOU  956  O   HOH A 270     2761   1980   1835   -568   -657    396       O  
HETATM  957  O   HOH A 271      12.725  25.895  31.980  1.00 15.35           O  
ANISOU  957  O   HOH A 271     2494   1891   1449    655    404   -128       O  
HETATM  958  O   HOH A 272      -2.705  34.010  20.984  1.00 14.57           O  
ANISOU  958  O   HOH A 272     2282   1517   1739    427     10     13       O  
HETATM  959  O   HOH A 273      11.020  20.655  19.731  1.00 16.06           O  
ANISOU  959  O   HOH A 273     1238   2757   2105    145    379    576       O  
HETATM  960  O   HOH A 274      -3.419  39.016   4.402  1.00 16.43           O  
ANISOU  960  O   HOH A 274     1972   1290   2979    -50    587    -24       O  
HETATM  961  O   HOH A 275      11.089  22.491  16.675  1.00 20.16           O  
ANISOU  961  O   HOH A 275     1881   2352   3429    257   -965   -100       O  
HETATM  962  O   HOH A 276      -2.053  38.131  27.937  1.00 18.20           O  
ANISOU  962  O   HOH A 276     2677   2029   2210    -35    -28   -363       O  
HETATM  963  O   HOH A 277       4.150  37.670  -3.612  1.00 20.46           O  
ANISOU  963  O   HOH A 277     2004   3336   2434    285    165   1726       O  
HETATM  964  O   HOH A 278      -7.544  28.866  10.483  1.00 17.04           O  
ANISOU  964  O   HOH A 278     2959   1622   1894   -291    262    -49       O  
HETATM  965  O   HOH A 279       9.983  46.431  18.601  1.00 18.94           O  
ANISOU  965  O   HOH A 279     3391   1688   2118     46   -276   -531       O  
HETATM  966  O   HOH A 280      -3.623  37.098  10.915  1.00 19.24           O  
ANISOU  966  O   HOH A 280     2230   2880   2200   1033   -169    287       O  
HETATM  967  O   HOH A 281      10.380  24.984  24.549  1.00 20.45           O  
ANISOU  967  O   HOH A 281     1767   2370   3634   -346    188  -1084       O  
HETATM  968  O   HOH A 282     -10.006  30.643  12.105  1.00 30.64           O  
ANISOU  968  O   HOH A 282     2332   4208   5101   1594  -1872  -3089       O  
HETATM  969  O   HOH A 283      -6.445  29.112  23.927  1.00 20.43           O  
ANISOU  969  O   HOH A 283     2909   3011   1843   -457    377    -63       O  
HETATM  970  O   HOH A 284       1.552  27.365   0.997  1.00 31.63           O  
ANISOU  970  O   HOH A 284     6337   3980   1701   1321  -1970   -674       O  
HETATM  971  O   HOH A 285       8.600  26.992  24.272  1.00 24.51           O  
ANISOU  971  O   HOH A 285     4374   1685   3253    504  -1766   -684       O  
HETATM  972  O   HOH A 286      16.259  25.997  15.353  1.00 16.43           O  
ANISOU  972  O   HOH A 286     1592   1826   2826    481   -379   -989       O  
HETATM  973  O   HOH A 287       3.543  13.437  17.503  1.00 20.34           O  
ANISOU  973  O   HOH A 287     2458   2324   2948    904  -1382   -853       O  
HETATM  974  O   HOH A 288       6.519  44.555  20.048  1.00 15.63           O  
ANISOU  974  O   HOH A 288     2139   1737   2063   -311    746   -392       O  
HETATM  975  O   HOH A 289      15.546  47.848  16.317  1.00 20.80           O  
ANISOU  975  O   HOH A 289     2017   2932   2953    -61   -575   -297       O  
HETATM  976  O   HOH A 290       9.990  26.345  32.346  1.00 20.98           O  
ANISOU  976  O   HOH A 290     3150   2536   2287   1297    681    800       O  
HETATM  977  O   HOH A 291      20.230  36.669  19.972  1.00 23.42           O  
ANISOU  977  O   HOH A 291     1645   5270   1983  -1165    114    -10       O  
HETATM  978  O   HOH A 292       5.050  18.696   2.172  1.00 34.09           O  
ANISOU  978  O   HOH A 292     2238   7446   3268   1946   1237   1906       O  
HETATM  979  O   HOH A 293      17.068  36.045   5.392  1.00 26.22           O  
ANISOU  979  O   HOH A 293     3429   3801   2733    269    549   -733       O  
HETATM  980  O   HOH A 294      -7.982  21.677  14.715  1.00 21.18           O  
ANISOU  980  O   HOH A 294     1192   3131   3726   -350   -168   -302       O  
HETATM  981  O   HOH A 295      19.475  39.203   9.954  1.00 28.69           O  
ANISOU  981  O   HOH A 295     3888   3518   3496  -1579    394    849       O  
HETATM  982  O   HOH A 296      12.516  45.420  23.196  1.00 24.76           O  
ANISOU  982  O   HOH A 296     3394   3101   2913  -1422   -940   -344       O  
HETATM  983  O   HOH A 297       4.399  45.631  21.449  1.00 23.46           O  
ANISOU  983  O   HOH A 297     3846   3076   1992   1698    581    -94       O  
HETATM  984  O   HOH A 298       9.241  26.488   0.541  1.00 20.92           O  
ANISOU  984  O   HOH A 298     3049   2917   1985    265    516   -315       O  
HETATM  985  O   HOH A 299      -4.470  33.902  23.181  1.00 23.26           O  
ANISOU  985  O   HOH A 299     3632   3451   1752   1351    805    443       O  
HETATM  986  O   HOH A 300       8.655  44.547  21.592  1.00 21.25           O  
ANISOU  986  O   HOH A 300     2231   3351   2493    206    347   -683       O  
HETATM  987  O   HOH A 301      -1.163  35.441  26.540  1.00 17.04           O  
ANISOU  987  O   HOH A 301     2213   1400   2862    140    282     45       O  
HETATM  988  O   HOH A 302      -0.675  44.210  10.175  1.00 27.89           O  
ANISOU  988  O   HOH A 302     2750   1194   6655    152   1330    422       O  
HETATM  989  O   HOH A 303       7.342  16.398  13.960  1.00 20.75           O  
ANISOU  989  O   HOH A 303     3684   2283   1918    335    523    438       O  
HETATM  990  O   HOH A 304       2.925  21.065   1.760  1.00 25.10           O  
ANISOU  990  O   HOH A 304     4267   2999   2271   1586    500   -370       O  
HETATM  991  O   HOH A 305       5.589  15.822  12.286  1.00 22.53           O  
ANISOU  991  O   HOH A 305     3210   1319   4034    466   1226    627       O  
HETATM  992  O   HOH A 306       1.313  30.594  32.173  1.00 25.01           O  
ANISOU  992  O   HOH A 306     5636   2556   1313   -514    797   -363       O  
HETATM  993  O   HOH A 307       9.443  45.414   6.363  1.00 24.46           O  
ANISOU  993  O   HOH A 307     2162   5199   1935    478   -392    859       O  
HETATM  994  O   HOH A 308      18.302  32.809   4.888  1.00 39.47           O  
ANISOU  994  O   HOH A 308     3052   7163   4780   1825   2121  -1175       O  
HETATM  995  O   HOH A 309      -8.246  30.310   3.117  1.00 29.87           O  
ANISOU  995  O   HOH A 309     2507   4046   4795    284  -1364   1247       O  
HETATM  996  O   HOH A 310      -8.472  25.903  15.890  1.00 25.55           O  
ANISOU  996  O   HOH A 310     2062   5116   2530   -302    662    207       O  
HETATM  997  O   HOH A 311      -4.716  24.818  23.377  1.00 44.90           O  
ANISOU  997  O   HOH A 311     5985   5309   5766  -1142   3986   1709       O  
HETATM  998  O   HOH A 312      11.907  35.674  30.836  1.00 30.71           O  
ANISOU  998  O   HOH A 312     6425   2641   2603   -659  -1861    477       O  
HETATM  999  O   HOH A 313       3.133  29.496  -0.949  1.00 35.81           O  
ANISOU  999  O   HOH A 313     5521   5510   2575   1334    418  -1422       O  
HETATM 1000  O   HOH A 314       2.232  22.903   0.529  1.00 25.78           O  
ANISOU 1000  O   HOH A 314     3612   3050   3132    110    221   1228       O  
HETATM 1001  O   HOH A 315      15.445  38.281  26.861  1.00 22.45           O  
ANISOU 1001  O   HOH A 315     2408   3859   2264    498    603    843       O  
HETATM 1002  O   HOH A 316      -2.558  24.588   1.688  1.00 18.50           O  
ANISOU 1002  O   HOH A 316     2670   2817   1544    265    -46     76       O  
HETATM 1003  O   HOH A 317      -9.368  31.673   6.265  1.00 31.70           O  
ANISOU 1003  O   HOH A 317     2457   5404   4185    630    496    -35       O  
HETATM 1004  O   HOH A 318      16.858  45.905   9.015  1.00 19.90           O  
ANISOU 1004  O   HOH A 318     1422   3969   2172   -512    175    228       O  
HETATM 1005  O   HOH A 319       6.810  20.828   4.216  1.00 18.69           O  
ANISOU 1005  O   HOH A 319     2526   2402   2172    612    723    335       O  
HETATM 1006  O   HOH A 320      -9.061  29.784  16.131  1.00 27.97           O  
ANISOU 1006  O   HOH A 320     2889   3840   3901    802   1591   -142       O  
HETATM 1007  O   HOH A 321      14.066  33.740  30.624  1.00 23.07           O  
ANISOU 1007  O   HOH A 321     3208   2514   3045    356  -1053    132       O  
HETATM 1008  O   HOH A 322      12.766  40.638  29.405  1.00 35.95           O  
ANISOU 1008  O   HOH A 322     6432   3966   3261    749   1092   1138       O  
HETATM 1009  O   HOH A 323      -2.541  34.224  -1.225  1.00 36.79           O  
ANISOU 1009  O   HOH A 323     3112   8506   2360  -2586  -1213   1763       O  
HETATM 1010  O   HOH A 324       4.855  10.416  23.951  1.00 40.33           O  
ANISOU 1010  O   HOH A 324     6319   2913   6092  -2090   2072    667       O  
HETATM 1011  O   HOH A 325      10.920  28.636   1.019  1.00 31.90           O  
ANISOU 1011  O   HOH A 325     3425   4404   4291  -1896   -860   -476       O  
HETATM 1012  O   HOH A 326       2.498  15.088   6.391  1.00 21.99           O  
ANISOU 1012  O   HOH A 326     2191   1937   4227   -112    475   -440       O  
HETATM 1013  O   HOH A 327      -6.105  31.794  -1.101  1.00 39.90           O  
ANISOU 1013  O   HOH A 327     3971   6983   4206  -2330  -2241    -79       O  
HETATM 1014  O   HOH A 328      -5.617  15.415  25.420  1.00 32.15           O  
ANISOU 1014  O   HOH A 328     1660   5306   5249    598    889    571       O  
HETATM 1015  O   HOH A 329      11.438  51.916  15.034  1.00 31.96           O  
ANISOU 1015  O   HOH A 329     5421   2549   4175  -1459   -555    207       O  
HETATM 1016  O   HOH A 330      14.070  49.934  12.877  1.00 25.03           O  
ANISOU 1016  O   HOH A 330     2615   2723   4173   -202    392   -568       O  
HETATM 1017  O   HOH A 331      -3.673  22.172  26.276  1.00 27.32           O  
ANISOU 1017  O   HOH A 331     3104   5702   1574   -799   1160   -580       O  
HETATM 1018  O   HOH A 332       6.275  15.373   9.214  1.00 28.98           O  
ANISOU 1018  O   HOH A 332     3450   5843   1720    459    612     37       O  
HETATM 1019  O   HOH A 333      10.394  34.603   2.359  1.00 28.12           O  
ANISOU 1019  O   HOH A 333     4040   2937   3708    -10  -1466   1387       O  
HETATM 1020  O   HOH A 334       6.006  13.658  23.344  1.00 38.41           O  
ANISOU 1020  O   HOH A 334     7261   4688   2644   1062   2123      2       O  
HETATM 1021  O   HOH A 335      -1.615  22.342  27.918  1.00 39.60           O  
ANISOU 1021  O   HOH A 335     4995   4068   5983  -1938   1213   1123       O  
HETATM 1022  O   HOH A 336     -10.204  28.740   4.120  1.00 27.41           O  
ANISOU 1022  O   HOH A 336     2580   4216   3619   1195    -87    688       O  
HETATM 1023  O   HOH A 337       9.246  14.545  12.216  1.00 29.98           O  
ANISOU 1023  O   HOH A 337     4048   4187   3154    338   -523   1436       O  
HETATM 1024  O   HOH A 338       6.698  14.173  20.182  1.00 34.17           O  
ANISOU 1024  O   HOH A 338     2445   4950   5588    472  -1455    943       O  
HETATM 1025  O   HOH A 339       5.385  38.898  -1.814  1.00 38.97           O  
ANISOU 1025  O   HOH A 339     4925   4482   5401   1624  -1560   1630       O  
HETATM 1026  O   HOH A 340       8.469  49.083  19.613  1.00 38.74           O  
ANISOU 1026  O   HOH A 340     5387   6297   3036    835  -1714    824       O  
HETATM 1027  O   HOH A 341      -4.821  19.673  27.578  1.00 42.12           O  
ANISOU 1027  O   HOH A 341     5292   6718   3994  -1189   1701   2122       O  
HETATM 1028  O   HOH A 342      -0.347  44.492  19.791  1.00 41.43           O  
ANISOU 1028  O   HOH A 342     2191   7574   5975   -513  -1362    377       O  
HETATM 1029  O   HOH A 343       6.896  27.777  -0.953  1.00 31.45           O  
ANISOU 1029  O   HOH A 343     5356   3040   3552   -274   -825  -1019       O  
HETATM 1030  O   HOH A 344       3.699  25.298  31.775  1.00 30.50           O  
ANISOU 1030  O   HOH A 344     3146   3546   4898   -431   1186   -136       O  
HETATM 1031  O   HOH A 345      -0.637  44.668  17.166  1.00 27.18           O  
ANISOU 1031  O   HOH A 345     1583   5082   3660   -141    296   1409       O  
HETATM 1032  O   HOH A 346       2.148  44.247  20.844  1.00 26.22           O  
ANISOU 1032  O   HOH A 346     3113   4649   2198   1562    -69  -1008       O  
HETATM 1033  O   HOH A 347      12.881  47.632  19.548  1.00 29.69           O  
ANISOU 1033  O   HOH A 347     2465   6527   2290   1695   -692  -1261       O  
HETATM 1034  O   HOH A 348      13.003  47.817   7.278  1.00 35.81           O  
ANISOU 1034  O   HOH A 348     6479   4033   3093   2580    333    732       O  
HETATM 1035  O   HOH A 349       7.054  34.633   1.803  1.00 30.01           O  
ANISOU 1035  O   HOH A 349     3910   4890   2601   2500    703     10       O  
HETATM 1036  O   HOH A 350       9.566  41.930   0.037  1.00 38.56           O  
ANISOU 1036  O   HOH A 350     4441   5102   5107   -979   1212  -3165       O  
HETATM 1037  O   HOH A 351      10.082  52.260  16.836  1.00 39.90           O  
ANISOU 1037  O   HOH A 351     4795   4638   5727   -166   -117  -2827       O  
HETATM 1038  O   HOH A 352      -5.486  19.928  24.616  1.00 37.08           O  
ANISOU 1038  O   HOH A 352     2834   7247   4006   -852   1124   2752       O  
HETATM 1039  O   HOH A 353       2.922  12.164  19.992  1.00 23.99           O  
ANISOU 1039  O   HOH A 353     2547   2538   4031    290    567   -175       O  
HETATM 1040  O   HOH A 354       5.822  38.406   0.373  1.00 30.18           O  
ANISOU 1040  O   HOH A 354     5028   3316   3123   1908   -400   -366       O  
HETATM 1041  O   HOH A 355      -4.326  36.143  -0.056  1.00 29.15           O  
ANISOU 1041  O   HOH A 355     4234   2844   3997  -1459   -921   1141       O  
HETATM 1042  O   HOH A 356      17.171  38.617   5.518  1.00 46.91           O  
ANISOU 1042  O   HOH A 356     8342   5040   4443    624   2887    894       O  
HETATM 1043  O   HOH A 357      -9.505  22.143  12.707  1.00 34.75           O  
ANISOU 1043  O   HOH A 357     3042   5760   4402   -661  -1310   1607       O  
HETATM 1044  O   HOH A 358      15.762  40.264   6.275  1.00 33.76           O  
ANISOU 1044  O   HOH A 358     3455   3860   5510    622   1762   2236       O  
HETATM 1045  O   HOH A 359       2.739  22.067  29.879  1.00 42.65           O  
ANISOU 1045  O   HOH A 359     6975   3688   5543    965   -165  -2241       O  
HETATM 1046  O   HOH A 360      -5.828  36.544   2.570  1.00 39.35           O  
ANISOU 1046  O   HOH A 360     6179   3772   5001   1202   -649    672       O  
HETATM 1047  O   HOH A 361      16.251  48.952   8.974  1.00 46.44           O  
ANISOU 1047  O   HOH A 361     5005   5154   7485  -2322   1137   1344       O  
HETATM 1048  O   HOH A 362      -5.360  22.899  21.082  1.00 19.02           O  
ANISOU 1048  O   HOH A 362     2060   2450   2716   -218     15    932       O  
HETATM 1049  O   HOH A 363      23.641  30.968  10.348  1.00 14.46           O  
ANISOU 1049  O   HOH A 363     1349   1450   2695    -14    796   -304       O  
HETATM 1050  O   HOH A 364       2.407  21.572  27.657  1.00 16.60           O  
ANISOU 1050  O   HOH A 364     1986   1619   2703     55   -971    128       O  
HETATM 1051  O   HOH A 365      -4.030  35.316   3.875  1.00 30.49           O  
ANISOU 1051  O   HOH A 365     2820   2696   6069    519   -247    386       O  
HETATM 1052  O   HOH A 366       0.904  41.810  17.563  1.00 19.65           O  
ANISOU 1052  O   HOH A 366     2086   2621   2759    276   -539   -171       O  
HETATM 1053  O   HOH A 367       7.024  25.264  24.843  1.00 18.73           O  
ANISOU 1053  O   HOH A 367     2597   2214   2307   -552    235     34       O  
HETATM 1054  O   HOH A 368      -0.918  42.053   9.538  1.00 20.02           O  
ANISOU 1054  O   HOH A 368     1802   3573   2231   -117   -122     99       O  
HETATM 1055  O   HOH A 369      13.933  23.788   5.614  1.00 35.92           O  
ANISOU 1055  O   HOH A 369     2134   6479   5034   -236  -1446   2327       O  
HETATM 1056  O   HOH A 370      -5.275  14.237  23.171  1.00 23.83           O  
ANISOU 1056  O   HOH A 370     3308   3386   2362  -1619     46     71       O  
HETATM 1057  O   HOH A 371       0.607  49.428  16.790  1.00 29.75           O  
ANISOU 1057  O   HOH A 371     5912   2310   3082    -51    -65    765       O  
HETATM 1058  O   HOH A 372       7.917  44.277  24.521  1.00 40.62           O  
ANISOU 1058  O   HOH A 372     4609   6416   4408   2065   -608  -2336       O  
HETATM 1059  O   HOH A 373       4.319  49.911  19.263  1.00 38.91           O  
ANISOU 1059  O   HOH A 373     6107   6418   2260    285    966  -1457       O  
HETATM 1060  O   HOH A 374       1.588  19.042   4.938  1.00 37.20           O  
ANISOU 1060  O   HOH A 374     2257   5589   6288   -560  -1217  -2551       O  
HETATM 1061  O   HOH A 375      10.617  41.028  30.951  1.00 38.39           O  
ANISOU 1061  O   HOH A 375     4910   3949   5728   -468   1427  -1013       O  
HETATM 1062  O   HOH A 376      -6.844  20.506  21.175  1.00 43.51           O  
ANISOU 1062  O   HOH A 376     7753   5734   3043    957   -826    950       O  
HETATM 1063  O   HOH A 377      -0.783  47.599  18.622  1.00 37.52           O  
ANISOU 1063  O   HOH A 377     3311   5321   5624    -67   1291    213       O  
HETATM 1064  O   HOH A 378       8.192  24.720  30.804  1.00 29.55           O  
ANISOU 1064  O   HOH A 378     4989   3128   3111   1347   -127   -339       O  
HETATM 1065  O   HOH A 379      13.960  33.633   1.056  1.00 40.50           O  
ANISOU 1065  O   HOH A 379     4102   4874   6413  -2011    464  -1058       O  
HETATM 1066  O   HOH A 380      -5.244  26.781  24.449  1.00 45.53           O  
ANISOU 1066  O   HOH A 380     7336   5210   4752  -1389   -102    412       O  
HETATM 1067  O   HOH A 381      -7.231  28.450   0.130  1.00 36.12           O  
ANISOU 1067  O   HOH A 381     4216   5495   4015   -942  -2394   -579       O  
HETATM 1068  O   HOH A 382     -10.027  30.438   9.295  1.00 40.64           O  
ANISOU 1068  O   HOH A 382     5948   4941   4553    254   3024    796       O  
HETATM 1069  O   HOH A 383       7.559  38.160  -1.352  1.00 41.14           O  
ANISOU 1069  O   HOH A 383     5192   4545   5893     73   2809  -1490       O  
HETATM 1070  O   HOH A 384       8.579  44.240   3.164  1.00 48.68           O  
ANISOU 1070  O   HOH A 384     6347   4456   7693   3466      5   -628       O  
HETATM 1071  O   HOH A 385      -9.822  26.179  10.561  1.00 27.53           O  
ANISOU 1071  O   HOH A 385     1368   4039   5055    226   -268    -63       O  
HETATM 1072  O   HOH A 386      -1.328  34.166  29.837  1.00 43.94           O  
ANISOU 1072  O   HOH A 386     2838   8741   5118   1225   -936   1511       O  
HETATM 1073  O   HOH A 387       9.648  28.610  32.348  1.00 45.42           O  
ANISOU 1073  O   HOH A 387     7710   6195   3354    524   -587   1226       O  
HETATM 1074  O   HOH A 388     -10.258  28.422  14.318  1.00 38.51           O  
ANISOU 1074  O   HOH A 388     1662   8198   4771   -299   -252    693       O  
HETATM 1075  O   HOH A 389      -0.170  46.029  13.021  1.00 36.39           O  
ANISOU 1075  O   HOH A 389     5160   3664   5002  -1269   1545   -898       O  
HETATM 1076  O   HOH A 390      -3.264  26.955  31.202  1.00 39.35           O  
ANISOU 1076  O   HOH A 390     7156   4824   2972  -1756    755    220       O  
HETATM 1077  O   HOH A 391      19.861  36.882  24.411  1.00 46.81           O  
ANISOU 1077  O   HOH A 391     5741   4677   7369  -2316  -1809  -1740       O  
HETATM 1078  O   HOH A 392       6.847  36.896   1.862  1.00 32.88           O  
ANISOU 1078  O   HOH A 392     3512   6090   2890   -170   -735   1147       O  
HETATM 1079  O   HOH A 393       9.318  36.123  -1.181  1.00 47.29           O  
ANISOU 1079  O   HOH A 393     5894   7449   4627   -422  -3427   -851       O  
HETATM 1080  O   HOH A 394      17.244  25.683  18.693  1.00 25.38           O  
ANISOU 1080  O   HOH A 394     3865   2626   3152    833   1769    427       O  
HETATM 1081  O   HOH A 395       0.123  27.596  -1.213  1.00 54.28           O  
ANISOU 1081  O   HOH A 395     4578   7518   8527  -1827   1535    120       O  
HETATM 1082  O   HOH A 396       0.432  47.976  21.724  1.00 40.79           O  
ANISOU 1082  O   HOH A 396     5991   3875   5633  -1561   -989  -1240       O  
HETATM 1083  O   HOH A 397      -6.635  15.335  20.459  1.00 42.98           O  
ANISOU 1083  O   HOH A 397     3645   6347   6339   1366   2504   1248       O  
HETATM 1084  O   HOH A 398      -6.617  16.073  23.084  1.00 38.05           O  
ANISOU 1084  O   HOH A 398     4101   4387   5968   1416   2297   -353       O  
HETATM 1085  O   HOH A 399      -6.810  36.320   7.280  1.00 44.85           O  
ANISOU 1085  O   HOH A 399     5607   4722   6711    705   1418    603       O  
HETATM 1086  O   HOH A 400       3.851   9.987  20.867  1.00 29.63           O  
ANISOU 1086  O   HOH A 400     4103   4076   3081   1830    -42    737       O  
HETATM 1087  O   HOH A 401      14.263  46.258   6.163  1.00 47.71           O  
ANISOU 1087  O   HOH A 401     5296   6608   6222   -695   2312    752       O  
HETATM 1088  O   HOH A 402      -2.786  25.893  26.306  1.00 47.51           O  
ANISOU 1088  O   HOH A 402     4515   5888   7647   -974   3906   -470       O  
HETATM 1089  O   HOH A 403      21.376  34.580  20.347  1.00 36.76           O  
ANISOU 1089  O   HOH A 403     5139   4569   4258    878   2120   1719       O  
HETATM 1090  O   HOH A 404      10.450  18.319  16.933  1.00 45.59           O  
ANISOU 1090  O   HOH A 404     5686   5562   6076   -279   -787   1850       O  
HETATM 1091  O   HOH A 405       8.491  41.020  27.037  1.00 34.02           O  
ANISOU 1091  O   HOH A 405     3209   4565   5151   1302   2080   2093       O  
HETATM 1092  O   HOH A 406      18.657  27.479  19.594  1.00 31.58           O  
ANISOU 1092  O   HOH A 406     5312   1775   4911    589  -2738    390       O  
HETATM 1093  O   HOH A 407      -7.657  23.673  22.401  1.00 41.10           O  
ANISOU 1093  O   HOH A 407     2600   6256   6760    852   1896    317       O  
HETATM 1094  O   HOH A 408      14.849  49.907  10.724  1.00 33.58           O  
ANISOU 1094  O   HOH A 408     3317   4671   4771   -290    337    412       O  
HETATM 1095  O   HOH A 409     -10.365  24.592  18.461  1.00 47.58           O  
ANISOU 1095  O   HOH A 409     6230   4571   7277   2538  -2320  -2007       O  
HETATM 1096  O   HOH A 410      -1.423  29.150  32.136  1.00 36.85           O  
ANISOU 1096  O   HOH A 410     4673   5428   3900   1463   -147    -90       O  
HETATM 1097  O   HOH A 411      15.217  43.507   7.331  1.00 44.94           O  
ANISOU 1097  O   HOH A 411     5805   6457   4814   -680   2377    792       O  
CONECT    1    2    3    4                                                      
CONECT    2    1                                                                
CONECT    3    1                                                                
CONECT    4    1                                                                
CONECT  400  878                                                                
CONECT  417  878                                                                
CONECT  433  878                                                                
CONECT  441  878                                                                
CONECT  464  878                                                                
CONECT  496  878                                                                
CONECT  497  878                                                                
CONECT  723  879                                                                
CONECT  746  879                                                                
CONECT  758  879                                                                
CONECT  768  879                                                                
CONECT  816  879                                                                
CONECT  817  879                                                                
CONECT  878  400  417  433  441                                                 
CONECT  878  464  496  497                                                      
CONECT  879  723  746  758  768                                                 
CONECT  879  816  817  887                                                      
CONECT  881  882  883                                                           
CONECT  882  881                                                                
CONECT  883  881                                                                
CONECT  884  885  886                                                           
CONECT  885  884                                                                
CONECT  886  884                                                                
CONECT  887  879                                                                
MASTER      285    0    6    8    0    0   14    6 1096    1   28    9          
END