path: root/plip/test/pdb/4dst.pdb

HEADER    HYDROLASE                               19-FEB-12   4DST              
TITLE     SMALL-MOLECULE LIGANDS BIND TO A DISTINCT POCKET IN RAS AND INHIBIT   
TITLE    2 SOS-MEDIATED NUCLEOTIDE EXCHANGE ACTIVITY                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE KRAS, ISOFORM 2B;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: KRAS 4B, K-RAS 2, KI-RAS, C-K-RAS, C-KI-RAS, GTPASE KRAS, N-
COMPND   5 TERMINALLY PROCESSED;                                                
COMPND   6 EC: 3.6.-.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KRAS, KRAS2, RASK2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SMALL G-PROTEIN, SIGNALING, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.OH,T.MAURER,L.S.GARRENTON,K.PITTS,D.J.ANDERSON,N.J.SKELTON,         
AUTHOR   2 B.P.FAUBER,B.PAN,S.MALEK,D.STOKOE,M.LUDLAM,K.K.BOWMAN,J.WU,          
AUTHOR   3 A.M.GIANNETTI,M.A.STAROVASNIK,I.MELLMAN,P.K.JACKSON,J.RULDOLPH,      
AUTHOR   4 G.FANG,W.WANG                                                        
REVDAT   3   06-JUN-12 4DST    1       COMPND DBREF  SEQADV REMARK              
REVDAT   2   18-APR-12 4DST    1       JRNL                                     
REVDAT   1   04-APR-12 4DST    0                                                
JRNL        AUTH   T.MAURER,L.S.GARRENTON,A.OH,K.PITTS,D.J.ANDERSON,            
JRNL        AUTH 2 N.J.SKELTON,B.P.FAUBER,B.PAN,S.MALEK,D.STOKOE,M.J.LUDLAM,    
JRNL        AUTH 3 K.K.BOWMAN,J.WU,A.M.GIANNETTI,M.A.STAROVASNIK,I.MELLMAN,     
JRNL        AUTH 4 P.K.JACKSON,J.RUDOLPH,W.WANG,G.FANG                          
JRNL        TITL   SMALL-MOLECULE LIGANDS BIND TO A DISTINCT POCKET IN RAS AND  
JRNL        TITL 2 INHIBIT SOS-MEDIATED NUCLEOTIDE EXCHANGE ACTIVITY.           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109  5299 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22431598                                                     
JRNL        DOI    10.1073/PNAS.1116510109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.79                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 7716                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 393                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 25.7941 -  3.3102    1.00     2570   147  0.1597 0.2015        
REMARK   3     2  3.3102 -  2.6282    1.00     2567   134  0.1530 0.2053        
REMARK   3     3  2.3800 -  2.3000    0.84     2186   112  0.1691 0.2472        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 46.26                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.950           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.55140                                             
REMARK   3    B22 (A**2) : -3.55140                                             
REMARK   3    B33 (A**2) : 7.10290                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           1520                                  
REMARK   3   ANGLE     :  1.005           2058                                  
REMARK   3   CHIRALITY :  0.059            227                                  
REMARK   3   PLANARITY :  0.003            263                                  
REMARK   3   DIHEDRAL  : 14.818            567                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7262   9.8187   0.2962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1244 T22:   0.1504                                     
REMARK   3      T33:   0.1346 T12:  -0.0101                                     
REMARK   3      T13:  -0.0095 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2115 L22:   0.9535                                     
REMARK   3      L33:   1.1451 L12:   0.1333                                     
REMARK   3      L13:   0.2607 L23:  -0.5664                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0648 S12:  -0.0179 S13:   0.1087                       
REMARK   3      S21:   0.0390 S22:  -0.0849 S23:  -0.0407                       
REMARK   3      S31:  -0.0642 S32:   0.1230 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4DST COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070737.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97740                            
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN COOLED DUAL        
REMARK 200                                   CRYSTAL                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 8242                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL + 0.2 UL DROPS CONTAINING 40      
REMARK 280  MG/ML KRAS, 0.1 M TRISCL, 25% POLYETHYLENE GLYCOL 4000, 0.2 M       
REMARK 280  NAOAC, 2% BENZAMIDINE-HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.46150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.78311            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       26.21033            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       39.46150            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       22.78311            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       26.21033            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       39.46150            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       22.78311            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       26.21033            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       45.56622            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       52.42067            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       45.56622            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       52.42067            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       45.56622            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       52.42067            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     SER A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     CYS A   185                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     ILE A   187                                                      
REMARK 465     MET A   188                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     LYS A 176    CG   CD   CE   NZ                                   
REMARK 470     LYS A 177    CG   CD   CE   NZ                                   
REMARK 470     LYS A 178    CG   CD   CE   NZ                                   
REMARK 470     LYS A 179    CG   CD   CE   NZ                                   
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  36      -62.88    -92.11                                   
REMARK 500    GLU A  37      136.96   -171.00                                   
REMARK 500    SER A 122       33.71    -85.85                                   
REMARK 500    ARG A 149        7.62     80.40                                   
REMARK 500    LYS A 176       47.69   -100.90                                   
REMARK 500    LYS A 177     -110.27    166.72                                   
REMARK 500    LYS A 178      -20.90   -146.48                                   
REMARK 500    LYS A 179      111.62    127.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              MG A 203  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GCP A 202   O2B                                                    
REMARK 620 2 GCP A 202   O1G  92.5                                              
REMARK 620 3 SER A  17   OG   93.8 173.1                                        
REMARK 620 4 HOH A 302   O    86.3  98.2  79.5                                  
REMARK 620 5 HOH A 301   O   101.7  85.6  95.8 171.0                            
REMARK 620 6 THR A  35   OG1 168.2  95.8  77.6  84.2  87.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 208  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A  96   OH                                                     
REMARK 620 2 HOH A 305   O   104.8                                              
REMARK 620 3 HOH A 308   O    89.9  89.5                                        
REMARK 620 4 GLY A  60   O    92.2 163.0  91.2                                  
REMARK 620 5 GLY A  10   O    76.3  93.5 166.2  89.9                            
REMARK 620 6 ALA A  59   O   175.4  79.2  92.3  83.8 101.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9LI A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GCP A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 206                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 207                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 208                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DSN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DSO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4DSU   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE MATCHES UNIPROT ENTRY P01116, ISOFORM 2B WITH           
REMARK 999 IDENTIFIER P01116-2.                                                 
DBREF  4DST A    2   188  UNP    P01116   RASK_HUMAN       2    188             
SEQADV 4DST GLY A    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 4DST SER A    1  UNP  P01116              EXPRESSION TAG                 
SEQADV 4DST ASP A   12  UNP  P01116    GLY    12 ENGINEERED MUTATION            
SEQRES   1 A  189  GLY SER THR GLU TYR LYS LEU VAL VAL VAL GLY ALA ASP          
SEQRES   2 A  189  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 A  189  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 A  189  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 A  189  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 A  189  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 A  189  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 A  189  GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 A  189  LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 A  189  LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN          
SEQRES  11 A  189  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE          
SEQRES  12 A  189  GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA          
SEQRES  13 A  189  PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU          
SEQRES  14 A  189  LYS MET SER LYS ASP GLY LYS LYS LYS LYS LYS LYS SER          
SEQRES  15 A  189  LYS THR LYS CYS VAL ILE MET                                  
HET    9LI  A 201      15                                                       
HET    GCP  A 202      32                                                       
HET     MG  A 203       1                                                       
HET    GOL  A 204       6                                                       
HET    EDO  A 205       4                                                       
HET    DMS  A 206       4                                                       
HET    ACT  A 207       4                                                       
HET     MG  A 208       1                                                       
HETNAM     9LI 2-(4,6-DICHLORO-2-METHYL-1H-INDOL-3-YL)ETHANAMINE                
HETNAM     GCP PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     ACT ACETATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  9LI    C11 H12 CL2 N2                                               
FORMUL   3  GCP    C11 H18 N5 O13 P3                                            
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  EDO    C2 H6 O2                                                     
FORMUL   7  DMS    C2 H6 O S                                                    
FORMUL   8  ACT    C2 H3 O2 1-                                                  
FORMUL  10  HOH   *90(H2 O)                                                     
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 TYR A   64  GLY A   75  1                                  12    
HELIX    3   3 ASN A   86  ASP A  105  1                                  20    
HELIX    4   4 ASP A  126  GLY A  138  1                                  13    
HELIX    5   5 GLY A  151  ASP A  173  1                                  23    
SHEET    1   A 6 GLU A  37  ILE A  46  0                                        
SHEET    2   A 6 GLU A  49  THR A  58 -1  O  CYS A  51   N  VAL A  44           
SHEET    3   A 6 THR A   2  GLY A  10  1  N  TYR A   4   O  ASP A  54           
SHEET    4   A 6 GLY A  77  ALA A  83  1  O  VAL A  81   N  VAL A   9           
SHEET    5   A 6 MET A 111  ASN A 116  1  O  ASN A 116   N  PHE A  82           
SHEET    6   A 6 PHE A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
LINK         O2B GCP A 202                MG    MG A 203     1555   1555  2.17  
LINK         O1G GCP A 202                MG    MG A 203     1555   1555  2.19  
LINK         OG  SER A  17                MG    MG A 203     1555   1555  2.28  
LINK        MG    MG A 203                 O   HOH A 302     1555   1555  2.32  
LINK        MG    MG A 203                 O   HOH A 301     1555   1555  2.34  
LINK         OH  TYR A  96                MG    MG A 208     1555   1555  2.44  
LINK         OG1 THR A  35                MG    MG A 203     1555   1555  2.45  
LINK        MG    MG A 208                 O   HOH A 305     1555   1555  2.53  
LINK        MG    MG A 208                 O   HOH A 308     1555   1555  2.54  
LINK         O   GLY A  60                MG    MG A 208     1555   1555  2.60  
LINK         O   GLY A  10                MG    MG A 208     1555   1555  2.62  
LINK         O   ALA A  59                MG    MG A 208     1555   1555  2.67  
CISPEP   1 ASP A  173    GLY A  174          0        -0.44                     
CISPEP   2 LYS A  177    LYS A  178          0         1.72                     
SITE     1 AC1 11 LYS A   5  VAL A   7  SER A  39  LEU A  56                    
SITE     2 AC1 11 THR A  74  GLY A  75  CYS A 118  ASP A 119                    
SITE     3 AC1 11 LEU A 120  ARG A 123  HOH A 376                               
SITE     1 AC2 27 ASP A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC2 27 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC2 27 VAL A  29  ASP A  30  GLU A  31  TYR A  32                    
SITE     4 AC2 27 PRO A  34  THR A  35  GLY A  60  ASN A 116                    
SITE     5 AC2 27 LYS A 117  ASP A 119  LEU A 120  SER A 145                    
SITE     6 AC2 27 ALA A 146   MG A 203  HOH A 301  HOH A 302                    
SITE     7 AC2 27 HOH A 303  HOH A 310  HOH A 342                               
SITE     1 AC3  5 SER A  17  THR A  35  GCP A 202  HOH A 301                    
SITE     2 AC3  5 HOH A 302                                                     
SITE     1 AC4  3 ASP A  92  TYR A  96  GLN A  99                               
SITE     1 AC5  4 LYS A 101  ARG A 102  ASP A 105  SER A 106                    
SITE     1 AC6  5 ASP A  33  ILE A  36  GLU A  37  ASP A  38                    
SITE     2 AC6  5 HOH A 339                                                     
SITE     1 AC7  3 ARG A  97  VAL A 109  GLY A 138                               
SITE     1 AC8  6 GLY A  10  ALA A  59  GLY A  60  TYR A  96                    
SITE     2 AC8  6 HOH A 305  HOH A 308                                          
CRYST1   78.923   78.923   78.631  90.00  90.00 120.00 H 3           9          
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      0.012671  0.007315  0.000000        0.00000                         
SCALE2      0.000000  0.014631  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012718        0.00000                         
ATOM      1  N   SER A   1      38.831  18.260   0.753  1.00 95.57           N  
ANISOU    1  N   SER A   1    10900  12964  12449  -1114   -926   1477       N  
ATOM      2  CA  SER A   1      38.659  19.544   1.423  1.00 95.43           C  
ANISOU    2  CA  SER A   1    10964  12837  12459  -1244  -1073   1440       C  
ATOM      3  C   SER A   1      37.224  19.770   1.888  1.00 88.42           C  
ANISOU    3  C   SER A   1    10243  11811  11543  -1209  -1080   1253       C  
ATOM      4  O   SER A   1      36.966  19.896   3.085  1.00 93.99           O  
ANISOU    4  O   SER A   1    11027  12459  12225  -1241  -1151   1167       O  
ATOM      5  CB  SER A   1      39.080  20.695   0.506  1.00100.74           C  
ANISOU    5  CB  SER A   1    11592  13498  13189  -1341  -1130   1547       C  
ATOM      6  OG  SER A   1      40.426  20.558   0.091  1.00106.40           O  
ANISOU    6  OG  SER A   1    12143  14351  13933  -1381  -1125   1730       O  
ATOM      7  N   THR A   2      36.294  19.824   0.939  1.00 72.50           N  
ANISOU    7  N   THR A   2     8275   9747   9524  -1142  -1007   1196       N  
ATOM      8  CA  THR A   2      34.925  20.234   1.245  1.00 58.63           C  
ANISOU    8  CA  THR A   2     6663   7857   7755  -1117  -1020   1036       C  
ATOM      9  C   THR A   2      34.093  19.155   1.936  1.00 48.59           C  
ANISOU    9  C   THR A   2     5455   6582   6424  -1012   -945    911       C  
ATOM     10  O   THR A   2      34.149  17.973   1.586  1.00 39.37           O  
ANISOU   10  O   THR A   2     4236   5497   5227   -919   -838    928       O  
ATOM     11  CB  THR A   2      34.173  20.737  -0.011  1.00 53.78           C  
ANISOU   11  CB  THR A   2     6077   7193   7164  -1090   -980   1027       C  
ATOM     12  OG1 THR A   2      34.938  21.764  -0.654  1.00 54.72           O  
ANISOU   12  OG1 THR A   2     6137   7316   7339  -1194  -1053   1155       O  
ATOM     13  CG2 THR A   2      32.806  21.296   0.373  1.00 46.56           C  
ANISOU   13  CG2 THR A   2     5303   6137   6251  -1070  -1008    874       C  
ATOM     14  N   GLU A   3      33.311  19.589   2.915  1.00 50.17           N  
ANISOU   14  N   GLU A   3     5770   6683   6608  -1029  -1001    785       N  
ATOM     15  CA  GLU A   3      32.459  18.699   3.682  1.00 51.17           C  
ANISOU   15  CA  GLU A   3     5962   6801   6678   -944   -941    668       C  
ATOM     16  C   GLU A   3      31.001  18.772   3.209  1.00 49.57           C  
ANISOU   16  C   GLU A   3     5846   6517   6472   -869   -881    552       C  
ATOM     17  O   GLU A   3      30.443  19.860   3.038  1.00 50.36           O  
ANISOU   17  O   GLU A   3     6012   6517   6606   -904   -936    505       O  
ATOM     18  CB  GLU A   3      32.561  19.059   5.162  1.00 57.37           C  
ANISOU   18  CB  GLU A   3     6813   7550   7434  -1007  -1036    606       C  
ATOM     19  CG  GLU A   3      31.520  18.398   6.036  1.00 67.09           C  
ANISOU   19  CG  GLU A   3     8130   8758   8604   -932   -985    473       C  
ATOM     20  CD  GLU A   3      31.422  19.047   7.400  1.00 74.96           C  
ANISOU   20  CD  GLU A   3     9218   9699   9565   -999  -1083    389       C  
ATOM     21  OE1 GLU A   3      32.404  19.704   7.815  1.00 77.04           O  
ANISOU   21  OE1 GLU A   3     9462   9968   9842  -1106  -1191    451       O  
ATOM     22  OE2 GLU A   3      30.362  18.908   8.050  1.00 75.86           O  
ANISOU   22  OE2 GLU A   3     9424   9768   9634   -947  -1051    262       O  
ATOM     23  N   TYR A   4      30.395  17.607   2.995  1.00 44.05           N  
ANISOU   23  N   TYR A   4     5144   5857   5737   -766   -773    512       N  
ATOM     24  CA  TYR A   4      28.989  17.527   2.608  1.00 36.48           C  
ANISOU   24  CA  TYR A   4     4258   4834   4771   -694   -716    408       C  
ATOM     25  C   TYR A   4      28.191  16.737   3.630  1.00 33.87           C  
ANISOU   25  C   TYR A   4     3985   4497   4389   -636   -676    304       C  
ATOM     26  O   TYR A   4      28.604  15.656   4.050  1.00 35.06           O  
ANISOU   26  O   TYR A   4     4096   4719   4505   -603   -633    330       O  
ATOM     27  CB  TYR A   4      28.839  16.860   1.241  1.00 33.00           C  
ANISOU   27  CB  TYR A   4     3765   4441   4331   -629   -622    454       C  
ATOM     28  CG  TYR A   4      29.495  17.619   0.124  1.00 32.23           C  
ANISOU   28  CG  TYR A   4     3611   4360   4275   -679   -648    558       C  
ATOM     29  CD1 TYR A   4      28.779  18.537  -0.627  1.00 33.99           C  
ANISOU   29  CD1 TYR A   4     3875   4508   4531   -694   -671    539       C  
ATOM     30  CD2 TYR A   4      30.837  17.424  -0.178  1.00 34.08           C  
ANISOU   30  CD2 TYR A   4     3744   4688   4517   -712   -649    685       C  
ATOM     31  CE1 TYR A   4      29.381  19.246  -1.655  1.00 35.83           C  
ANISOU   31  CE1 TYR A   4     4054   4760   4799   -746   -698    646       C  
ATOM     32  CE2 TYR A   4      31.445  18.120  -1.202  1.00 36.42           C  
ANISOU   32  CE2 TYR A   4     3980   5010   4847   -762   -669    791       C  
ATOM     33  CZ  TYR A   4      30.714  19.032  -1.938  1.00 36.43           C  
ANISOU   33  CZ  TYR A   4     4029   4937   4877   -782   -694    772       C  
ATOM     34  OH  TYR A   4      31.320  19.729  -2.957  1.00 38.99           O  
ANISOU   34  OH  TYR A   4     4293   5291   5232   -838   -716    889       O  
ATOM     35  N   LYS A   5      27.040  17.275   4.015  1.00 32.82           N  
ANISOU   35  N   LYS A   5     3940   4276   4252   -620   -687    192       N  
ATOM     36  CA  LYS A   5      26.147  16.598   4.949  1.00 32.77           C  
ANISOU   36  CA  LYS A   5     3989   4266   4195   -565   -643     94       C  
ATOM     37  C   LYS A   5      25.021  15.889   4.195  1.00 32.17           C  
ANISOU   37  C   LYS A   5     3919   4186   4118   -478   -550     53       C  
ATOM     38  O   LYS A   5      24.096  16.530   3.701  1.00 32.30           O  
ANISOU   38  O   LYS A   5     3975   4135   4162   -461   -549      3       O  
ATOM     39  CB  LYS A   5      25.555  17.600   5.940  1.00 35.07           C  
ANISOU   39  CB  LYS A   5     4373   4474   4477   -594   -707     -9       C  
ATOM     40  CG  LYS A   5      26.579  18.406   6.718  1.00 40.19           C  
ANISOU   40  CG  LYS A   5     5035   5112   5124   -691   -815     17       C  
ATOM     41  CD  LYS A   5      25.889  19.427   7.614  1.00 47.77           C  
ANISOU   41  CD  LYS A   5     6104   5976   6071   -710   -872   -104       C  
ATOM     42  CE  LYS A   5      26.893  20.266   8.393  1.00 54.69           C  
ANISOU   42  CE  LYS A   5     7008   6831   6942   -816   -991    -87       C  
ATOM     43  NZ  LYS A   5      27.742  19.434   9.293  1.00 56.98           N  
ANISOU   43  NZ  LYS A   5     7259   7222   7167   -846  -1004    -42       N  
ATOM     44  N   LEU A   6      25.103  14.565   4.102  1.00 30.48           N  
ANISOU   44  N   LEU A   6     3667   4040   3875   -427   -477     78       N  
ATOM     45  CA  LEU A   6      24.076  13.795   3.409  1.00 25.08           C  
ANISOU   45  CA  LEU A   6     2991   3351   3186   -354   -395     42       C  
ATOM     46  C   LEU A   6      23.176  13.093   4.416  1.00 25.65           C  
ANISOU   46  C   LEU A   6     3106   3423   3218   -314   -359    -36       C  
ATOM     47  O   LEU A   6      23.654  12.517   5.396  1.00 28.24           O  
ANISOU   47  O   LEU A   6     3427   3792   3509   -321   -362    -25       O  
ATOM     48  CB  LEU A   6      24.707  12.767   2.460  1.00 22.65           C  
ANISOU   48  CB  LEU A   6     2619   3109   2878   -319   -334    119       C  
ATOM     49  CG  LEU A   6      25.958  13.175   1.676  1.00 26.40           C  
ANISOU   49  CG  LEU A   6     3028   3626   3379   -358   -358    223       C  
ATOM     50  CD1 LEU A   6      26.251  12.171   0.574  1.00 28.39           C  
ANISOU   50  CD1 LEU A   6     3232   3933   3623   -301   -277    273       C  
ATOM     51  CD2 LEU A   6      25.830  14.565   1.090  1.00 24.75           C  
ANISOU   51  CD2 LEU A   6     2834   3362   3208   -410   -418    230       C  
ATOM     52  N   VAL A   7      21.870  13.156   4.176  1.00 25.07           N  
ANISOU   52  N   VAL A   7     3070   3305   3150   -275   -326   -106       N  
ATOM     53  CA  VAL A   7      20.892  12.476   5.018  1.00 18.48           C  
ANISOU   53  CA  VAL A   7     2267   2476   2280   -236   -283   -172       C  
ATOM     54  C   VAL A   7      20.111  11.442   4.200  1.00 18.68           C  
ANISOU   54  C   VAL A   7     2277   2511   2309   -183   -212   -172       C  
ATOM     55  O   VAL A   7      19.497  11.775   3.188  1.00 17.15           O  
ANISOU   55  O   VAL A   7     2085   2285   2147   -170   -204   -180       O  
ATOM     56  CB  VAL A   7      19.899  13.478   5.646  1.00 18.83           C  
ANISOU   56  CB  VAL A   7     2369   2461   2324   -233   -307   -262       C  
ATOM     57  CG1 VAL A   7      18.858  12.739   6.493  1.00 19.39           C  
ANISOU   57  CG1 VAL A   7     2462   2553   2354   -191   -252   -320       C  
ATOM     58  CG2 VAL A   7      20.641  14.534   6.490  1.00 13.65           C  
ANISOU   58  CG2 VAL A   7     1746   1782   1659   -290   -385   -276       C  
ATOM     59  N   VAL A   8      20.136  10.188   4.643  1.00 20.54           N  
ANISOU   59  N   VAL A   8     2501   2787   2515   -159   -168   -159       N  
ATOM     60  CA  VAL A   8      19.406   9.121   3.962  1.00 21.97           C  
ANISOU   60  CA  VAL A   8     2677   2970   2700   -116   -108   -162       C  
ATOM     61  C   VAL A   8      18.045   8.911   4.626  1.00 22.49           C  
ANISOU   61  C   VAL A   8     2772   3023   2752    -97    -82   -226       C  
ATOM     62  O   VAL A   8      17.979   8.563   5.811  1.00 20.20           O  
ANISOU   62  O   VAL A   8     2492   2758   2426    -99    -76   -239       O  
ATOM     63  CB  VAL A   8      20.221   7.810   3.960  1.00 21.76           C  
ANISOU   63  CB  VAL A   8     2622   2985   2660    -98    -73   -104       C  
ATOM     64  CG1 VAL A   8      19.470   6.708   3.239  1.00 16.80           C  
ANISOU   64  CG1 VAL A   8     2002   2345   2038    -59    -19   -115       C  
ATOM     65  CG2 VAL A   8      21.618   8.049   3.328  1.00 11.62           C  
ANISOU   65  CG2 VAL A   8     1296   1728   1392   -111    -92    -33       C  
ATOM     66  N   VAL A   9      16.966   9.140   3.868  1.00 15.68           N  
ANISOU   66  N   VAL A   9     1917   2128   1914    -79    -69   -258       N  
ATOM     67  CA  VAL A   9      15.614   9.065   4.418  1.00 13.34           C  
ANISOU   67  CA  VAL A   9     1634   1823   1612    -60    -44   -312       C  
ATOM     68  C   VAL A   9      14.721   8.104   3.625  1.00 14.65           C  
ANISOU   68  C   VAL A   9     1789   1986   1792    -41     -5   -306       C  
ATOM     69  O   VAL A   9      15.015   7.774   2.480  1.00 15.61           O  
ANISOU   69  O   VAL A   9     1904   2100   1928    -41     -4   -277       O  
ATOM     70  CB  VAL A   9      14.937  10.467   4.493  1.00 22.91           C  
ANISOU   70  CB  VAL A   9     2863   2993   2848    -56    -72   -364       C  
ATOM     71  CG1 VAL A   9      15.799  11.447   5.278  1.00 23.59           C  
ANISOU   71  CG1 VAL A   9     2973   3069   2920    -82   -120   -377       C  
ATOM     72  CG2 VAL A   9      14.658  11.015   3.095  1.00 19.26           C  
ANISOU   72  CG2 VAL A   9     2391   2494   2433    -55    -91   -349       C  
ATOM     73  N   GLY A  10      13.631   7.657   4.245  1.00 16.29           N  
ANISOU   73  N   GLY A  10     1996   2205   1990    -28     24   -333       N  
ATOM     74  CA  GLY A  10      12.708   6.729   3.608  1.00 19.03           C  
ANISOU   74  CA  GLY A  10     2333   2548   2352    -22     52   -326       C  
ATOM     75  C   GLY A  10      11.985   5.838   4.604  1.00 21.09           C  
ANISOU   75  C   GLY A  10     2586   2837   2591    -20     87   -327       C  
ATOM     76  O   GLY A  10      12.353   5.782   5.776  1.00 23.83           O  
ANISOU   76  O   GLY A  10     2939   3215   2902    -21     95   -328       O  
ATOM     77  N   ALA A  11      10.958   5.133   4.135  1.00 23.45           N  
ANISOU   77  N   ALA A  11     2873   3131   2909    -22    105   -322       N  
ATOM     78  CA  ALA A  11      10.139   4.276   4.993  1.00 22.92           C  
ANISOU   78  CA  ALA A  11     2790   3092   2827    -28    137   -312       C  
ATOM     79  C   ALA A  11      10.923   3.107   5.598  1.00 23.32           C  
ANISOU   79  C   ALA A  11     2853   3155   2853    -39    151   -271       C  
ATOM     80  O   ALA A  11      12.104   2.912   5.306  1.00 22.99           O  
ANISOU   80  O   ALA A  11     2829   3100   2807    -36    138   -252       O  
ATOM     81  CB  ALA A  11       8.919   3.750   4.211  1.00 21.73           C  
ANISOU   81  CB  ALA A  11     2619   2927   2710    -41    141   -305       C  
ATOM     82  N   ASP A  12      10.246   2.339   6.446  1.00 21.34           N  
ANISOU   82  N   ASP A  12     2588   2933   2587    -50    178   -251       N  
ATOM     83  CA  ASP A  12      10.799   1.133   7.044  1.00 22.87           C  
ANISOU   83  CA  ASP A  12     2791   3134   2765    -62    189   -201       C  
ATOM     84  C   ASP A  12      11.186   0.138   5.974  1.00 22.77           C  
ANISOU   84  C   ASP A  12     2800   3065   2788    -66    180   -178       C  
ATOM     85  O   ASP A  12      10.371  -0.210   5.124  1.00 24.12           O  
ANISOU   85  O   ASP A  12     2972   3205   2988    -79    176   -186       O  
ATOM     86  CB  ASP A  12       9.738   0.441   7.913  1.00 28.37           C  
ANISOU   86  CB  ASP A  12     3463   3867   3450    -82    217   -174       C  
ATOM     87  CG  ASP A  12       9.490   1.149   9.225  1.00 34.34           C  
ANISOU   87  CG  ASP A  12     4204   4692   4152    -73    239   -191       C  
ATOM     88  OD1 ASP A  12       8.313   1.439   9.520  1.00 37.62           O  
ANISOU   88  OD1 ASP A  12     4588   5140   4564    -71    265   -206       O  
ATOM     89  OD2 ASP A  12      10.462   1.391   9.974  1.00 37.25           O  
ANISOU   89  OD2 ASP A  12     4590   5086   4478    -69    230   -187       O  
ATOM     90  N   GLY A  13      12.414  -0.354   6.036  1.00 23.21           N  
ANISOU   90  N   GLY A  13     2871   3109   2838    -53    176   -148       N  
ATOM     91  CA  GLY A  13      12.780  -1.539   5.287  1.00 24.50           C  
ANISOU   91  CA  GLY A  13     3060   3218   3030    -47    179   -124       C  
ATOM     92  C   GLY A  13      13.174  -1.346   3.839  1.00 25.68           C  
ANISOU   92  C   GLY A  13     3232   3328   3198    -30    170   -152       C  
ATOM     93  O   GLY A  13      13.409  -2.329   3.129  1.00 27.48           O  
ANISOU   93  O   GLY A  13     3490   3506   3444    -20    177   -146       O  
ATOM     94  N   VAL A  14      13.250  -0.097   3.389  1.00 19.33           N  
ANISOU   94  N   VAL A  14     2417   2543   2386    -26    156   -184       N  
ATOM     95  CA  VAL A  14      13.580   0.166   1.988  1.00 21.58           C  
ANISOU   95  CA  VAL A  14     2719   2802   2678    -14    148   -204       C  
ATOM     96  C   VAL A  14      15.059  -0.096   1.655  1.00 20.61           C  
ANISOU   96  C   VAL A  14     2603   2677   2551     19    159   -178       C  
ATOM     97  O   VAL A  14      15.416  -0.249   0.488  1.00 21.80           O  
ANISOU   97  O   VAL A  14     2774   2808   2701     35    166   -189       O  
ATOM     98  CB  VAL A  14      13.151   1.587   1.546  1.00 20.31           C  
ANISOU   98  CB  VAL A  14     2542   2658   2518    -23    125   -234       C  
ATOM     99  CG1 VAL A  14      11.657   1.770   1.747  1.00 17.89           C  
ANISOU   99  CG1 VAL A  14     2221   2354   2224    -45    119   -255       C  
ATOM    100  CG2 VAL A  14      13.933   2.655   2.305  1.00 14.57           C  
ANISOU  100  CG2 VAL A  14     1795   1964   1778    -17    113   -229       C  
ATOM    101  N   GLY A  15      15.913  -0.153   2.676  1.00 21.87           N  
ANISOU  101  N   GLY A  15     2742   2865   2702     29    163   -141       N  
ATOM    102  CA  GLY A  15      17.321  -0.466   2.472  1.00 20.67           C  
ANISOU  102  CA  GLY A  15     2582   2720   2553     63    175   -104       C  
ATOM    103  C   GLY A  15      18.256   0.711   2.691  1.00 20.78           C  
ANISOU  103  C   GLY A  15     2561   2780   2555     59    153    -85       C  
ATOM    104  O   GLY A  15      19.348   0.768   2.118  1.00 20.77           O  
ANISOU  104  O   GLY A  15     2542   2792   2557     83    161    -56       O  
ATOM    105  N   LYS A  16      17.831   1.658   3.518  1.00 18.30           N  
ANISOU  105  N   LYS A  16     2237   2491   2226     28    126   -102       N  
ATOM    106  CA  LYS A  16      18.648   2.826   3.802  1.00 22.47           C  
ANISOU  106  CA  LYS A  16     2741   3053   2744     12     93    -90       C  
ATOM    107  C   LYS A  16      20.021   2.422   4.353  1.00 28.69           C  
ANISOU  107  C   LYS A  16     3499   3874   3529     23     90    -26       C  
ATOM    108  O   LYS A  16      21.057   2.918   3.907  1.00 26.36           O  
ANISOU  108  O   LYS A  16     3175   3599   3241     25     77      7       O  
ATOM    109  CB  LYS A  16      17.924   3.744   4.787  1.00 19.71           C  
ANISOU  109  CB  LYS A  16     2399   2717   2375    -18     67   -128       C  
ATOM    110  CG  LYS A  16      16.588   4.276   4.270  1.00 19.73           C  
ANISOU  110  CG  LYS A  16     2417   2691   2389    -22     69   -184       C  
ATOM    111  CD  LYS A  16      15.963   5.284   5.234  1.00 17.35           C  
ANISOU  111  CD  LYS A  16     2121   2401   2069    -38     51   -226       C  
ATOM    112  CE  LYS A  16      15.573   4.633   6.556  1.00 18.06           C  
ANISOU  112  CE  LYS A  16     2214   2524   2125    -41     70   -223       C  
ATOM    113  NZ  LYS A  16      14.474   3.654   6.414  1.00 16.15           N  
ANISOU  113  NZ  LYS A  16     1970   2272   1893    -34    106   -223       N  
ATOM    114  N   SER A  17      20.025   1.508   5.315  1.00 27.57           N  
ANISOU  114  N   SER A  17     3357   3740   3379     28     99      2       N  
ATOM    115  CA  SER A  17      21.271   1.080   5.938  1.00 26.21           C  
ANISOU  115  CA  SER A  17     3151   3603   3206     39     90     73       C  
ATOM    116  C   SER A  17      22.150   0.274   4.995  1.00 26.05           C  
ANISOU  116  C   SER A  17     3111   3567   3219     91    124    114       C  
ATOM    117  O   SER A  17      23.362   0.470   4.948  1.00 34.37           O  
ANISOU  117  O   SER A  17     4119   4657   4281    102    115    170       O  
ATOM    118  CB  SER A  17      20.984   0.265   7.198  1.00 26.25           C  
ANISOU  118  CB  SER A  17     3161   3621   3193     31     91    100       C  
ATOM    119  OG  SER A  17      20.533   1.102   8.245  1.00 24.36           O  
ANISOU  119  OG  SER A  17     2931   3418   2908    -12     59     72       O  
ATOM    120  N   ALA A  18      21.538  -0.640   4.252  1.00 24.93           N  
ANISOU  120  N   ALA A  18     3003   3373   3095    122    164     87       N  
ATOM    121  CA  ALA A  18      22.277  -1.499   3.339  1.00 24.76           C  
ANISOU  121  CA  ALA A  18     2979   3329   3101    182    205    111       C  
ATOM    122  C   ALA A  18      23.021  -0.680   2.284  1.00 23.07           C  
ANISOU  122  C   ALA A  18     2738   3144   2884    194    211    114       C  
ATOM    123  O   ALA A  18      24.157  -0.987   1.939  1.00 24.07           O  
ANISOU  123  O   ALA A  18     2826   3294   3026    239    236    165       O  
ATOM    124  CB  ALA A  18      21.336  -2.507   2.680  1.00 23.69           C  
ANISOU  124  CB  ALA A  18     2901   3122   2978    202    236     64       C  
ATOM    125  N   LEU A  19      22.370   0.364   1.777  1.00 20.25           N  
ANISOU  125  N   LEU A  19     2395   2789   2509    155    190     67       N  
ATOM    126  CA  LEU A  19      22.978   1.249   0.789  1.00 20.96           C  
ANISOU  126  CA  LEU A  19     2460   2909   2593    154    190     77       C  
ATOM    127  C   LEU A  19      24.180   1.957   1.385  1.00 24.27           C  
ANISOU  127  C   LEU A  19     2816   3387   3018    135    158    145       C  
ATOM    128  O   LEU A  19      25.264   1.988   0.802  1.00 27.49           O  
ANISOU  128  O   LEU A  19     3178   3834   3435    162    178    199       O  
ATOM    129  CB  LEU A  19      21.970   2.311   0.333  1.00 19.75           C  
ANISOU  129  CB  LEU A  19     2334   2742   2428    108    160     22       C  
ATOM    130  CG  LEU A  19      20.835   1.886  -0.601  1.00 24.91           C  
ANISOU  130  CG  LEU A  19     3040   3350   3073    116    181    -38       C  
ATOM    131  CD1 LEU A  19      19.820   3.006  -0.701  1.00 23.13           C  
ANISOU  131  CD1 LEU A  19     2828   3116   2846     70    141    -77       C  
ATOM    132  CD2 LEU A  19      21.394   1.530  -1.983  1.00 24.39           C  
ANISOU  132  CD2 LEU A  19     2981   3291   2995    156    222    -32       C  
ATOM    133  N   THR A  20      23.955   2.561   2.544  1.00 22.26           N  
ANISOU  133  N   THR A  20     2559   3143   2755     86    108    143       N  
ATOM    134  CA  THR A  20      24.984   3.311   3.229  1.00 24.35           C  
ANISOU  134  CA  THR A  20     2773   3459   3020     50     60    201       C  
ATOM    135  C   THR A  20      26.173   2.405   3.514  1.00 25.64           C  
ANISOU  135  C   THR A  20     2883   3659   3201     92     81    284       C  
ATOM    136  O   THR A  20      27.301   2.765   3.229  1.00 24.14           O  
ANISOU  136  O   THR A  20     2631   3516   3024     92     73    350       O  
ATOM    137  CB  THR A  20      24.445   3.875   4.550  1.00 27.75           C  
ANISOU  137  CB  THR A  20     3228   3889   3426     -3      8    172       C  
ATOM    138  OG1 THR A  20      23.258   4.638   4.292  1.00 25.07           O  
ANISOU  138  OG1 THR A  20     2936   3511   3077    -27     -2     93       O  
ATOM    139  CG2 THR A  20      25.483   4.754   5.222  1.00 27.65           C  
ANISOU  139  CG2 THR A  20     3175   3924   3408    -53    -55    223       C  
ATOM    140  N  AILE A  21      25.911   1.226   4.069  0.57 25.59           N  
ANISOU  140  N  AILE A  21     2895   3630   3199    127    107    287       N  
ATOM    141  N  BILE A  21      25.906   1.224   4.064  0.43 25.63           N  
ANISOU  141  N  BILE A  21     2899   3634   3204    127    107    287       N  
ATOM    142  CA AILE A  21      26.983   0.301   4.428  0.57 26.57           C  
ANISOU  142  CA AILE A  21     2967   3781   3348    174    124    371       C  
ATOM    143  CA BILE A  21      26.967   0.288   4.431  0.43 26.63           C  
ANISOU  143  CA BILE A  21     2975   3787   3355    174    124    370       C  
ATOM    144  C  AILE A  21      27.720  -0.257   3.208  0.57 28.92           C  
ANISOU  144  C  AILE A  21     3235   4079   3674    249    188    398       C  
ATOM    145  C  BILE A  21      27.712  -0.272   3.215  0.43 28.77           C  
ANISOU  145  C  BILE A  21     3217   4060   3656    249    188    398       C  
ATOM    146  O  AILE A  21      28.914  -0.554   3.281  0.57 29.81           O  
ANISOU  146  O  AILE A  21     3277   4237   3812    285    198    482       O  
ATOM    147  O  BILE A  21      28.899  -0.588   3.300  0.43 29.80           O  
ANISOU  147  O  BILE A  21     3277   4235   3811    286    199    481       O  
ATOM    148  CB AILE A  21      26.468  -0.850   5.321  0.57 26.45           C  
ANISOU  148  CB AILE A  21     2982   3732   3336    192    133    373       C  
ATOM    149  CB BILE A  21      26.427  -0.872   5.294  0.43 26.27           C  
ANISOU  149  CB BILE A  21     2962   3706   3313    193    135    371       C  
ATOM    150  CG1AILE A  21      26.050  -0.301   6.684  0.57 25.77           C  
ANISOU  150  CG1AILE A  21     2908   3673   3211    122     73    369       C  
ATOM    151  CG1BILE A  21      25.762  -0.326   6.559  0.43 25.09           C  
ANISOU  151  CG1BILE A  21     2836   3574   3123    123     80    349       C  
ATOM    152  CG2AILE A  21      27.533  -1.916   5.501  0.57 25.53           C  
ANISOU  152  CG2AILE A  21     2815   3628   3259    256    158    461       C  
ATOM    153  CG2BILE A  21      27.541  -1.835   5.663  0.43 25.67           C  
ANISOU  153  CG2BILE A  21     2830   3651   3272    247    149    465       C  
ATOM    154  CD1AILE A  21      27.144   0.497   7.371  0.57 24.66           C  
ANISOU  154  CD1AILE A  21     2708   3603   3058     78     13    434       C  
ATOM    155  CD1BILE A  21      25.236  -1.398   7.478  0.43 23.05           C  
ANISOU  155  CD1BILE A  21     2603   3294   2862    131     87    364       C  
ATOM    156  N   GLN A  22      27.018  -0.401   2.088  1.00 28.18           N  
ANISOU  156  N   GLN A  22     3192   3941   3572    274    231    329       N  
ATOM    157  CA  GLN A  22      27.684  -0.787   0.845  1.00 29.23           C  
ANISOU  157  CA  GLN A  22     3307   4085   3716    343    295    343       C  
ATOM    158  C   GLN A  22      28.681   0.304   0.472  1.00 32.38           C  
ANISOU  158  C   GLN A  22     3629   4561   4111    317    278    404       C  
ATOM    159  O   GLN A  22      29.820   0.023   0.100  1.00 36.75           O  
ANISOU  159  O   GLN A  22     4115   5164   4684    370    316    474       O  
ATOM    160  CB  GLN A  22      26.691  -0.996  -0.304  1.00 28.93           C  
ANISOU  160  CB  GLN A  22     3346   3993   3655    358    332    253       C  
ATOM    161  CG  GLN A  22      26.225  -2.433  -0.499  1.00 25.50           C  
ANISOU  161  CG  GLN A  22     2971   3483   3233    419    379    213       C  
ATOM    162  CD  GLN A  22      27.300  -3.349  -1.088  1.00 28.79           C  
ANISOU  162  CD  GLN A  22     3363   3905   3673    519    448    251       C  
ATOM    163  OE1 GLN A  22      28.454  -2.955  -1.253  1.00 31.48           O  
ANISOU  163  OE1 GLN A  22     3623   4317   4020    544    464    320       O  
ATOM    164  NE2 GLN A  22      26.914  -4.582  -1.410  1.00 22.17           N  
ANISOU  164  NE2 GLN A  22     2590   2987   2847    576    489    205       N  
ATOM    165  N   LEU A  23      28.255   1.556   0.579  1.00 32.72           N  
ANISOU  165  N   LEU A  23     3680   4615   4135    237    220    381       N  
ATOM    166  CA  LEU A  23      29.132   2.668   0.234  1.00 31.34           C  
ANISOU  166  CA  LEU A  23     3440   4506   3963    197    192    442       C  
ATOM    167  C   LEU A  23      30.360   2.712   1.144  1.00 34.99           C  
ANISOU  167  C   LEU A  23     3815   5029   4449    185    157    544       C  
ATOM    168  O   LEU A  23      31.488   2.875   0.678  1.00 39.14           O  
ANISOU  168  O   LEU A  23     4259   5621   4993    203    174    626       O  
ATOM    169  CB  LEU A  23      28.380   3.997   0.312  1.00 28.67           C  
ANISOU  169  CB  LEU A  23     3137   4149   3609    112    126    397       C  
ATOM    170  CG  LEU A  23      29.206   5.219  -0.108  1.00 30.40           C  
ANISOU  170  CG  LEU A  23     3295   4421   3835     59     88    461       C  
ATOM    171  CD1 LEU A  23      29.200   5.389  -1.625  1.00 29.92           C  
ANISOU  171  CD1 LEU A  23     3233   4375   3761     86    139    459       C  
ATOM    172  CD2 LEU A  23      28.706   6.485   0.579  1.00 29.76           C  
ANISOU  172  CD2 LEU A  23     3243   4312   3753    -32      0    431       C  
ATOM    173  N   ILE A  24      30.133   2.563   2.446  1.00 34.62           N  
ANISOU  173  N   ILE A  24     3784   4969   4402    152    107    542       N  
ATOM    174  CA  ILE A  24      31.191   2.718   3.436  1.00 34.63           C  
ANISOU  174  CA  ILE A  24     3710   5030   4418    120     53    636       C  
ATOM    175  C   ILE A  24      32.061   1.471   3.588  1.00 42.68           C  
ANISOU  175  C   ILE A  24     4669   6076   5471    204    101    714       C  
ATOM    176  O   ILE A  24      33.283   1.559   3.544  1.00 47.77           O  
ANISOU  176  O   ILE A  24     5218   6791   6143    214     97    816       O  
ATOM    177  CB  ILE A  24      30.611   3.097   4.811  1.00 32.95           C  
ANISOU  177  CB  ILE A  24     3543   4801   4177     48    -23    603       C  
ATOM    178  CG1 ILE A  24      29.621   4.255   4.673  1.00 31.43           C  
ANISOU  178  CG1 ILE A  24     3417   4567   3957    -17    -61    513       C  
ATOM    179  CG2 ILE A  24      31.726   3.490   5.770  1.00 33.27           C  
ANISOU  179  CG2 ILE A  24     3509   4909   4222     -5    -96    698       C  
ATOM    180  CD1 ILE A  24      30.280   5.566   4.265  1.00 34.00           C  
ANISOU  180  CD1 ILE A  24     3702   4925   4292    -80   -113    550       C  
ATOM    181  N   GLN A  25      31.433   0.311   3.757  1.00 46.20           N  
ANISOU  181  N   GLN A  25     5170   6464   5922    263    145    673       N  
ATOM    182  CA  GLN A  25      32.162  -0.913   4.093  1.00 46.73           C  
ANISOU  182  CA  GLN A  25     5190   6538   6028    342    181    747       C  
ATOM    183  C   GLN A  25      32.265  -1.940   2.958  1.00 46.05           C  
ANISOU  183  C   GLN A  25     5115   6414   5968    456    281    728       C  
ATOM    184  O   GLN A  25      32.893  -2.987   3.122  1.00 47.86           O  
ANISOU  184  O   GLN A  25     5308   6638   6239    537    319    786       O  
ATOM    185  CB  GLN A  25      31.562  -1.567   5.342  1.00 47.03           C  
ANISOU  185  CB  GLN A  25     5271   6538   6058    324    145    739       C  
ATOM    186  CG  GLN A  25      31.637  -0.698   6.587  1.00 51.78           C  
ANISOU  186  CG  GLN A  25     5859   7189   6626    223     49    766       C  
ATOM    187  CD  GLN A  25      30.963  -1.331   7.794  1.00 57.25           C  
ANISOU  187  CD  GLN A  25     6600   7856   7297    203     22    756       C  
ATOM    188  OE1 GLN A  25      30.583  -2.504   7.771  1.00 59.49           O  
ANISOU  188  OE1 GLN A  25     6913   8085   7604    266     69    752       O  
ATOM    189  NE2 GLN A  25      30.808  -0.550   8.857  1.00 57.61           N  
ANISOU  189  NE2 GLN A  25     6657   7939   7294    115    -56    754       N  
ATOM    190  N   ASN A  26      31.652  -1.645   1.816  1.00 40.84           N  
ANISOU  190  N   ASN A  26     4510   5726   5282    463    322    646       N  
ATOM    191  CA  ASN A  26      31.779  -2.506   0.641  1.00 42.99           C  
ANISOU  191  CA  ASN A  26     4802   5968   5564    566    417    617       C  
ATOM    192  C   ASN A  26      31.240  -3.914   0.832  1.00 42.32           C  
ANISOU  192  C   ASN A  26     4786   5790   5502    634    454    576       C  
ATOM    193  O   ASN A  26      31.706  -4.849   0.181  1.00 46.56           O  
ANISOU  193  O   ASN A  26     5323   6304   6065    737    529    579       O  
ATOM    194  CB  ASN A  26      33.241  -2.596   0.191  1.00 49.84           C  
ANISOU  194  CB  ASN A  26     5559   6917   6461    636    465    717       C  
ATOM    195  CG  ASN A  26      33.844  -1.238  -0.108  1.00 55.63           C  
ANISOU  195  CG  ASN A  26     6218   7743   7177    566    429    771       C  
ATOM    196  OD1 ASN A  26      33.165  -0.336  -0.603  1.00 56.22           O  
ANISOU  196  OD1 ASN A  26     6339   7810   7212    499    405    711       O  
ATOM    197  ND2 ASN A  26      35.130  -1.085   0.191  1.00 57.59           N  
ANISOU  197  ND2 ASN A  26     6345   8077   7459    578    422    892       N  
ATOM    198  N   HIS A  27      30.270  -4.076   1.722  1.00 41.38           N  
ANISOU  198  N   HIS A  27     4728   5619   5377    578    404    538       N  
ATOM    199  CA  HIS A  27      29.612  -5.368   1.873  1.00 41.01           C  
ANISOU  199  CA  HIS A  27     4753   5475   5353    625    430    499       C  
ATOM    200  C   HIS A  27      28.109  -5.214   2.090  1.00 39.79           C  
ANISOU  200  C   HIS A  27     4689   5263   5166    551    395    410       C  
ATOM    201  O   HIS A  27      27.636  -4.190   2.586  1.00 38.40           O  
ANISOU  201  O   HIS A  27     4510   5124   4957    465    339    397       O  
ATOM    202  CB  HIS A  27      30.246  -6.186   3.002  1.00 44.09           C  
ANISOU  202  CB  HIS A  27     5096   5864   5791    656    413    592       C  
ATOM    203  CG  HIS A  27      29.940  -5.663   4.370  1.00 48.63           C  
ANISOU  203  CG  HIS A  27     5657   6476   6346    562    330    628       C  
ATOM    204  ND1 HIS A  27      28.828  -6.059   5.084  1.00 49.19           N  
ANISOU  204  ND1 HIS A  27     5796   6490   6403    516    301    588       N  
ATOM    205  CD2 HIS A  27      30.590  -4.768   5.146  1.00 50.71           C  
ANISOU  205  CD2 HIS A  27     5847   6828   6594    501    269    696       C  
ATOM    206  CE1 HIS A  27      28.812  -5.431   6.246  1.00 50.49           C  
ANISOU  206  CE1 HIS A  27     5933   6713   6538    439    234    627       C  
ATOM    207  NE2 HIS A  27      29.868  -4.641   6.312  1.00 51.58           N  
ANISOU  207  NE2 HIS A  27     5991   6934   6673    426    209    689       N  
ATOM    208  N   PHE A  28      27.369  -6.245   1.705  1.00 37.98           N  
ANISOU  208  N   PHE A  28     4539   4941   4950    587    427    351       N  
ATOM    209  CA  PHE A  28      25.923  -6.237   1.795  1.00 35.47           C  
ANISOU  209  CA  PHE A  28     4301   4567   4608    522    400    274       C  
ATOM    210  C   PHE A  28      25.446  -6.828   3.115  1.00 40.18           C  
ANISOU  210  C   PHE A  28     4907   5137   5224    488    361    311       C  
ATOM    211  O   PHE A  28      25.779  -7.963   3.455  1.00 45.72           O  
ANISOU  211  O   PHE A  28     5613   5788   5971    541    378    354       O  
ATOM    212  CB  PHE A  28      25.327  -7.023   0.628  1.00 33.08           C  
ANISOU  212  CB  PHE A  28     4083   4180   4306    565    446    192       C  
ATOM    213  CG  PHE A  28      23.834  -7.192   0.707  1.00 32.34           C  
ANISOU  213  CG  PHE A  28     4065   4025   4198    500    415    124       C  
ATOM    214  CD1 PHE A  28      22.995  -6.084   0.739  1.00 29.97           C  
ANISOU  214  CD1 PHE A  28     3765   3764   3857    419    376     87       C  
ATOM    215  CD2 PHE A  28      23.268  -8.454   0.733  1.00 29.19           C  
ANISOU  215  CD2 PHE A  28     3733   3526   3831    519    424    102       C  
ATOM    216  CE1 PHE A  28      21.619  -6.236   0.806  1.00 26.30           C  
ANISOU  216  CE1 PHE A  28     3355   3252   3384    363    350     34       C  
ATOM    217  CE2 PHE A  28      21.896  -8.610   0.797  1.00 29.50           C  
ANISOU  217  CE2 PHE A  28     3831   3516   3861    451    392     50       C  
ATOM    218  CZ  PHE A  28      21.070  -7.497   0.833  1.00 28.01           C  
ANISOU  218  CZ  PHE A  28     3632   3380   3632    375    358     19       C  
ATOM    219  N  AVAL A  29      24.669  -6.046   3.857  0.52 38.38           N  
ANISOU  219  N  AVAL A  29     4680   4941   4960    403    311    295       N  
ATOM    220  N  BVAL A  29      24.662  -6.053   3.856  0.48 38.41           N  
ANISOU  220  N  BVAL A  29     4685   4945   4964    403    311    295       N  
ATOM    221  CA AVAL A  29      24.080  -6.510   5.106  0.52 38.83           C  
ANISOU  221  CA AVAL A  29     4749   4987   5019    362    278    326       C  
ATOM    222  CA BVAL A  29      24.098  -6.519   5.117  0.48 38.82           C  
ANISOU  222  CA BVAL A  29     4746   4986   5019    362    278    328       C  
ATOM    223  C  AVAL A  29      22.769  -7.244   4.838  0.52 38.28           C  
ANISOU  223  C  AVAL A  29     4755   4833   4957    343    287    266       C  
ATOM    224  C  BVAL A  29      22.769  -7.235   4.886  0.48 38.26           C  
ANISOU  224  C  BVAL A  29     4751   4833   4954    342    285    268       C  
ATOM    225  O  AVAL A  29      21.768  -6.642   4.443  0.52 36.07           O  
ANISOU  225  O  AVAL A  29     4507   4552   4648    296    278    197       O  
ATOM    226  O  BVAL A  29      21.755  -6.609   4.566  0.48 36.17           O  
ANISOU  226  O  BVAL A  29     4516   4569   4658    291    274    202       O  
ATOM    227  CB AVAL A  29      23.832  -5.349   6.094  0.52 39.00           C  
ANISOU  227  CB AVAL A  29     4740   5087   4990    283    226    333       C  
ATOM    228  CB BVAL A  29      23.895  -5.356   6.109  0.48 38.44           C  
ANISOU  228  CB BVAL A  29     4666   5018   4921    285    226    337       C  
ATOM    229  CG1AVAL A  29      23.019  -4.244   5.434  0.52 38.31           C  
ANISOU  229  CG1AVAL A  29     4679   5010   4869    239    219    249       C  
ATOM    230  CG1BVAL A  29      23.125  -5.829   7.333  0.48 38.65           C  
ANISOU  230  CG1BVAL A  29     4711   5041   4934    240    200    360       C  
ATOM    231  CG2AVAL A  29      23.133  -5.857   7.346  0.52 38.66           C  
ANISOU  231  CG2AVAL A  29     4712   5042   4936    241    200    362       C  
ATOM    232  CG2BVAL A  29      25.237  -4.760   6.508  0.48 35.40           C  
ANISOU  232  CG2BVAL A  29     4206   4712   4533    291    203    410       C  
ATOM    233  N   ASP A  30      22.787  -8.553   5.050  1.00 39.69           N  
ANISOU  233  N   ASP A  30     4960   4940   5182    380    300    300       N  
ATOM    234  CA  ASP A  30      21.620  -9.386   4.808  1.00 40.91           C  
ANISOU  234  CA  ASP A  30     5186   5004   5353    358    302    255       C  
ATOM    235  C   ASP A  30      20.611  -9.288   5.953  1.00 38.66           C  
ANISOU  235  C   ASP A  30     4898   4746   5047    277    264    277       C  
ATOM    236  O   ASP A  30      19.409  -9.470   5.754  1.00 37.77           O  
ANISOU  236  O   ASP A  30     4828   4594   4929    230    257    232       O  
ATOM    237  CB  ASP A  30      22.077 -10.836   4.604  1.00 48.92           C  
ANISOU  237  CB  ASP A  30     6234   5919   6433    428    327    286       C  
ATOM    238  CG  ASP A  30      20.927 -11.818   4.576  1.00 55.74           C  
ANISOU  238  CG  ASP A  30     7172   6683   7325    393    315    259       C  
ATOM    239  OD1 ASP A  30      20.163 -11.808   3.586  1.00 56.06           O  
ANISOU  239  OD1 ASP A  30     7271   6676   7353    375    321    174       O  
ATOM    240  OD2 ASP A  30      20.801 -12.611   5.536  1.00 60.78           O  
ANISOU  240  OD2 ASP A  30     7807   7290   7997    378    294    331       O  
ATOM    241  N   GLU A  31      21.103  -8.996   7.152  1.00 40.11           N  
ANISOU  241  N   GLU A  31     5028   5002   5211    259    240    350       N  
ATOM    242  CA  GLU A  31      20.239  -8.900   8.323  1.00 42.45           C  
ANISOU  242  CA  GLU A  31     5318   5339   5473    188    212    376       C  
ATOM    243  C   GLU A  31      19.368  -7.644   8.250  1.00 40.95           C  
ANISOU  243  C   GLU A  31     5127   5206   5226    133    203    303       C  
ATOM    244  O   GLU A  31      19.757  -6.642   7.653  1.00 39.93           O  
ANISOU  244  O   GLU A  31     4984   5110   5078    143    204    259       O  
ATOM    245  CB  GLU A  31      21.079  -8.879   9.602  1.00 49.76           C  
ANISOU  245  CB  GLU A  31     6190   6335   6380    184    186    471       C  
ATOM    246  CG  GLU A  31      22.427  -9.596   9.488  1.00 60.72           C  
ANISOU  246  CG  GLU A  31     7550   7697   7822    258    194    544       C  
ATOM    247  CD  GLU A  31      22.303 -11.114   9.422  1.00 69.48           C  
ANISOU  247  CD  GLU A  31     8696   8700   9003    296    208    586       C  
ATOM    248  OE1 GLU A  31      23.350 -11.789   9.286  1.00 71.48           O  
ANISOU  248  OE1 GLU A  31     8929   8919   9312    369    220    644       O  
ATOM    249  OE2 GLU A  31      21.166 -11.633   9.509  1.00 71.04           O  
ANISOU  249  OE2 GLU A  31     8940   8846   9206    252    205    566       O  
ATOM    250  N   TYR A  32      18.183  -7.710   8.847  1.00 35.82           N  
ANISOU  250  N   TYR A  32     4488   4566   4554     78    196    296       N  
ATOM    251  CA  TYR A  32      17.322  -6.544   8.988  1.00 35.47           C  
ANISOU  251  CA  TYR A  32     4436   4581   4458     33    190    237       C  
ATOM    252  C   TYR A  32      17.395  -6.051  10.433  1.00 34.85           C  
ANISOU  252  C   TYR A  32     4327   4596   4321     -1    173    278       C  
ATOM    253  O   TYR A  32      16.724  -6.586  11.316  1.00 31.76           O  
ANISOU  253  O   TYR A  32     3933   4223   3912    -34    174    318       O  
ATOM    254  CB  TYR A  32      15.882  -6.912   8.623  1.00 36.23           C  
ANISOU  254  CB  TYR A  32     4560   4636   4569     -3    199    201       C  
ATOM    255  CG  TYR A  32      14.894  -5.758   8.588  1.00 34.22           C  
ANISOU  255  CG  TYR A  32     4294   4432   4276    -36    199    138       C  
ATOM    256  CD1 TYR A  32      15.115  -4.587   9.308  1.00 33.11           C  
ANISOU  256  CD1 TYR A  32     4126   4373   4080    -44    192    123       C  
ATOM    257  CD2 TYR A  32      13.734  -5.848   7.832  1.00 33.59           C  
ANISOU  257  CD2 TYR A  32     4231   4315   4217    -60    203     94       C  
ATOM    258  CE1 TYR A  32      14.199  -3.543   9.277  1.00 30.77           C  
ANISOU  258  CE1 TYR A  32     3822   4112   3756    -64    195     63       C  
ATOM    259  CE2 TYR A  32      12.824  -4.814   7.788  1.00 34.30           C  
ANISOU  259  CE2 TYR A  32     4302   4449   4280    -82    204     44       C  
ATOM    260  CZ  TYR A  32      13.057  -3.665   8.511  1.00 31.97           C  
ANISOU  260  CZ  TYR A  32     3982   4228   3937    -78    204     27       C  
ATOM    261  OH  TYR A  32      12.131  -2.650   8.457  1.00 30.56           O  
ANISOU  261  OH  TYR A  32     3788   4083   3740    -90    208    -25       O  
ATOM    262  N   ASP A  33      18.224  -5.042  10.675  1.00 33.27           N  
ANISOU  262  N   ASP A  33     4102   4453   4084      4    155    269       N  
ATOM    263  CA  ASP A  33      18.353  -4.476  12.013  1.00 33.48           C  
ANISOU  263  CA  ASP A  33     4111   4569   4043    -31    132    295       C  
ATOM    264  C   ASP A  33      17.859  -3.027  12.020  1.00 30.14           C  
ANISOU  264  C   ASP A  33     3694   4189   3571    -53    126    211       C  
ATOM    265  O   ASP A  33      18.564  -2.124  11.572  1.00 26.46           O  
ANISOU  265  O   ASP A  33     3221   3729   3105    -44    107    181       O  
ATOM    266  CB  ASP A  33      19.805  -4.566  12.491  1.00 35.97           C  
ANISOU  266  CB  ASP A  33     4395   4918   4355    -15    102    367       C  
ATOM    267  CG  ASP A  33      20.025  -3.875  13.819  1.00 41.97           C  
ANISOU  267  CG  ASP A  33     5143   5773   5032    -59     68    386       C  
ATOM    268  OD1 ASP A  33      21.136  -3.343  14.036  1.00 43.18           O  
ANISOU  268  OD1 ASP A  33     5271   5964   5169    -60     31    412       O  
ATOM    269  OD2 ASP A  33      19.085  -3.861  14.644  1.00 45.11           O  
ANISOU  269  OD2 ASP A  33     5555   6210   5376    -93     78    375       O  
ATOM    270  N   PRO A  34      16.636  -2.808  12.527  1.00 30.39           N  
ANISOU  270  N   PRO A  34     3734   4248   3566    -81    144    177       N  
ATOM    271  CA  PRO A  34      15.974  -1.498  12.505  1.00 28.21           C  
ANISOU  271  CA  PRO A  34     3466   3998   3253    -91    146     92       C  
ATOM    272  C   PRO A  34      16.877  -0.393  13.045  1.00 31.57           C  
ANISOU  272  C   PRO A  34     3893   4471   3630   -100    109     73       C  
ATOM    273  O   PRO A  34      17.510  -0.557  14.087  1.00 28.21           O  
ANISOU  273  O   PRO A  34     3462   4101   3155   -119     87    122       O  
ATOM    274  CB  PRO A  34      14.774  -1.698  13.435  1.00 26.22           C  
ANISOU  274  CB  PRO A  34     3212   3796   2956   -115    175     92       C  
ATOM    275  CG  PRO A  34      14.484  -3.160  13.367  1.00 27.28           C  
ANISOU  275  CG  PRO A  34     3340   3895   3133   -121    190    164       C  
ATOM    276  CD  PRO A  34      15.830  -3.825  13.229  1.00 30.11           C  
ANISOU  276  CD  PRO A  34     3696   4222   3522   -102    164    227       C  
ATOM    277  N   THR A  35      16.929   0.729  12.336  1.00 31.46           N  
ANISOU  277  N   THR A  35     3888   4435   3629    -93     96      7       N  
ATOM    278  CA  THR A  35      17.792   1.831  12.726  1.00 26.17           C  
ANISOU  278  CA  THR A  35     3225   3796   2924   -110     52    -13       C  
ATOM    279  C   THR A  35      17.121   2.806  13.682  1.00 28.66           C  
ANISOU  279  C   THR A  35     3568   4153   3167   -129     49    -80       C  
ATOM    280  O   THR A  35      15.937   3.131  13.553  1.00 30.98           O  
ANISOU  280  O   THR A  35     3871   4438   3461   -116     83   -138       O  
ATOM    281  CB  THR A  35      18.316   2.587  11.492  1.00 26.78           C  
ANISOU  281  CB  THR A  35     3298   3823   3053    -98     32    -40       C  
ATOM    282  OG1 THR A  35      19.335   1.802  10.867  1.00 30.94           O  
ANISOU  282  OG1 THR A  35     3797   4333   3626    -79     30     28       O  
ATOM    283  CG2 THR A  35      18.912   3.934  11.879  1.00 25.17           C  
ANISOU  283  CG2 THR A  35     3108   3639   2817   -126    -18    -75       C  
ATOM    284  N   ILE A  36      17.894   3.251  14.662  1.00 29.19           N  
ANISOU  284  N   ILE A  36     3647   4272   3172   -158      7    -70       N  
ATOM    285  CA  ILE A  36      17.512   4.377  15.486  1.00 28.52           C  
ANISOU  285  CA  ILE A  36     3603   4219   3017   -174     -6   -149       C  
ATOM    286  C   ILE A  36      18.115   5.593  14.806  1.00 29.04           C  
ANISOU  286  C   ILE A  36     3683   4235   3116   -182    -54   -195       C  
ATOM    287  O   ILE A  36      17.399   6.472  14.321  1.00 27.04           O  
ANISOU  287  O   ILE A  36     3450   3938   2885   -164    -42   -271       O  
ATOM    288  CB  ILE A  36      18.063   4.222  16.916  1.00 30.04           C  
ANISOU  288  CB  ILE A  36     3810   4492   3112   -212    -36   -116       C  
ATOM    289  CG1 ILE A  36      17.403   3.020  17.606  1.00 28.31           C  
ANISOU  289  CG1 ILE A  36     3573   4324   2858   -208     12    -59       C  
ATOM    290  CG2 ILE A  36      17.865   5.509  17.727  1.00 21.64           C  
ANISOU  290  CG2 ILE A  36     2802   3453   1967   -230    -60   -210       C  
ATOM    291  CD1 ILE A  36      17.944   2.724  19.006  1.00 29.50           C  
ANISOU  291  CD1 ILE A  36     3735   4566   2910   -247    -18     -9       C  
ATOM    292  N   GLU A  37      19.443   5.605  14.739  1.00 31.89           N  
ANISOU  292  N   GLU A  37     4027   4603   3489   -210   -109   -137       N  
ATOM    293  CA  GLU A  37      20.190   6.627  14.025  1.00 33.57           C  
ANISOU  293  CA  GLU A  37     4241   4773   3743   -227   -160   -154       C  
ATOM    294  C   GLU A  37      21.657   6.213  13.964  1.00 33.52           C  
ANISOU  294  C   GLU A  37     4188   4792   3754   -252   -206    -57       C  
ATOM    295  O   GLU A  37      22.213   5.719  14.951  1.00 35.91           O  
ANISOU  295  O   GLU A  37     4484   5156   4006   -277   -231     -3       O  
ATOM    296  CB  GLU A  37      20.038   7.975  14.727  1.00 42.57           C  
ANISOU  296  CB  GLU A  37     5438   5909   4829   -257   -202   -241       C  
ATOM    297  CG  GLU A  37      20.763   9.128  14.054  1.00 52.14           C  
ANISOU  297  CG  GLU A  37     6656   7068   6086   -285   -264   -256       C  
ATOM    298  CD  GLU A  37      20.436  10.469  14.693  1.00 56.51           C  
ANISOU  298  CD  GLU A  37     7281   7595   6595   -308   -304   -357       C  
ATOM    299  OE1 GLU A  37      19.624  11.215  14.101  1.00 59.45           O  
ANISOU  299  OE1 GLU A  37     7678   7903   7008   -277   -284   -426       O  
ATOM    300  OE2 GLU A  37      20.982  10.771  15.780  1.00 53.20           O  
ANISOU  300  OE2 GLU A  37     6897   7215   6101   -354   -356   -367       O  
ATOM    301  N   ASP A  38      22.278   6.390  12.802  1.00 29.12           N  
ANISOU  301  N   ASP A  38     3597   4198   3269   -243   -215    -26       N  
ATOM    302  CA  ASP A  38      23.681   6.026  12.631  1.00 31.86           C  
ANISOU  302  CA  ASP A  38     3888   4575   3643   -257   -250     73       C  
ATOM    303  C   ASP A  38      24.440   7.080  11.828  1.00 35.82           C  
ANISOU  303  C   ASP A  38     4371   5050   4187   -285   -297     78       C  
ATOM    304  O   ASP A  38      23.933   7.587  10.829  1.00 39.44           O  
ANISOU  304  O   ASP A  38     4842   5456   4688   -266   -275     34       O  
ATOM    305  CB  ASP A  38      23.808   4.649  11.980  1.00 31.84           C  
ANISOU  305  CB  ASP A  38     3841   4567   3690   -202   -192    140       C  
ATOM    306  CG  ASP A  38      23.384   3.527  12.905  1.00 37.29           C  
ANISOU  306  CG  ASP A  38     4537   5288   4343   -189   -165    169       C  
ATOM    307  OD1 ASP A  38      23.941   3.428  14.018  1.00 42.04           O  
ANISOU  307  OD1 ASP A  38     5133   5948   4893   -224   -207    213       O  
ATOM    308  OD2 ASP A  38      22.486   2.748  12.526  1.00 39.54           O  
ANISOU  308  OD2 ASP A  38     4834   5541   4650   -150   -106    152       O  
ATOM    309  N   SER A  39      25.649   7.409  12.280  1.00 36.12           N  
ANISOU  309  N   SER A  39     4379   5130   4215   -335   -366    140       N  
ATOM    310  CA  SER A  39      26.453   8.463  11.660  1.00 38.90           C  
ANISOU  310  CA  SER A  39     4709   5465   4606   -378   -423    159       C  
ATOM    311  C   SER A  39      27.694   7.892  11.011  1.00 38.76           C  
ANISOU  311  C   SER A  39     4601   5487   4641   -366   -421    277       C  
ATOM    312  O   SER A  39      28.457   7.168  11.646  1.00 44.40           O  
ANISOU  312  O   SER A  39     5270   6259   5342   -370   -437    357       O  
ATOM    313  CB  SER A  39      26.870   9.505  12.693  1.00 41.47           C  
ANISOU  313  CB  SER A  39     5073   5803   4879   -460   -518    134       C  
ATOM    314  OG  SER A  39      25.735  10.054  13.329  1.00 46.00           O  
ANISOU  314  OG  SER A  39     5735   6343   5400   -460   -511     18       O  
ATOM    315  N   TYR A  40      27.902   8.225   9.744  1.00 32.58           N  
ANISOU  315  N   TYR A  40     3787   4677   3916   -349   -400    293       N  
ATOM    316  CA  TYR A  40      29.044   7.688   9.021  1.00 35.11           C  
ANISOU  316  CA  TYR A  40     4016   5039   4284   -326   -382    402       C  
ATOM    317  C   TYR A  40      29.882   8.773   8.392  1.00 39.56           C  
ANISOU  317  C   TYR A  40     4539   5609   4883   -380   -436    447       C  
ATOM    318  O   TYR A  40      29.407   9.884   8.143  1.00 35.14           O  
ANISOU  318  O   TYR A  40     4028   4999   4326   -421   -471    385       O  
ATOM    319  CB  TYR A  40      28.598   6.702   7.941  1.00 31.74           C  
ANISOU  319  CB  TYR A  40     3578   4590   3891   -237   -284    398       C  
ATOM    320  CG  TYR A  40      27.881   5.500   8.491  1.00 32.45           C  
ANISOU  320  CG  TYR A  40     3699   4671   3958   -186   -233    374       C  
ATOM    321  CD1 TYR A  40      26.495   5.452   8.526  1.00 28.47           C  
ANISOU  321  CD1 TYR A  40     3267   4117   3434   -171   -200    278       C  
ATOM    322  CD2 TYR A  40      28.589   4.411   8.979  1.00 34.13           C  
ANISOU  322  CD2 TYR A  40     3864   4927   4179   -155   -221    457       C  
ATOM    323  CE1 TYR A  40      25.829   4.345   9.031  1.00 28.75           C  
ANISOU  323  CE1 TYR A  40     3325   4146   3452   -134   -157    267       C  
ATOM    324  CE2 TYR A  40      27.933   3.296   9.484  1.00 33.08           C  
ANISOU  324  CE2 TYR A  40     3759   4779   4031   -115   -179    444       C  
ATOM    325  CZ  TYR A  40      26.555   3.272   9.514  1.00 34.45           C  
ANISOU  325  CZ  TYR A  40     4005   4904   4181   -109   -149    350       C  
ATOM    326  OH  TYR A  40      25.905   2.163  10.017  1.00 38.48           O  
ANISOU  326  OH  TYR A  40     4538   5402   4679    -77   -111    349       O  
ATOM    327  N   ARG A  41      31.134   8.423   8.124  1.00 46.77           N  
ANISOU  327  N   ARG A  41     5357   6585   5829   -378   -441    563       N  
ATOM    328  CA  ARG A  41      32.085   9.323   7.504  1.00 49.05           C  
ANISOU  328  CA  ARG A  41     5584   6898   6155   -432   -489    634       C  
ATOM    329  C   ARG A  41      32.772   8.597   6.359  1.00 49.00           C  
ANISOU  329  C   ARG A  41     5488   6936   6194   -361   -410    720       C  
ATOM    330  O   ARG A  41      33.351   7.528   6.553  1.00 49.04           O  
ANISOU  330  O   ARG A  41     5434   6990   6208   -306   -371    787       O  
ATOM    331  CB  ARG A  41      33.129   9.750   8.530  1.00 53.55           C  
ANISOU  331  CB  ARG A  41     6112   7521   6714   -519   -592    708       C  
ATOM    332  CG  ARG A  41      33.367  11.233   8.570  1.00 59.06           C  
ANISOU  332  CG  ARG A  41     6832   8189   7418   -624   -691    697       C  
ATOM    333  CD  ARG A  41      33.952  11.724   7.263  1.00 62.47           C  
ANISOU  333  CD  ARG A  41     7193   8633   7910   -630   -675    769       C  
ATOM    334  NE  ARG A  41      33.864  13.175   7.186  1.00 64.90           N  
ANISOU  334  NE  ARG A  41     7546   8881   8230   -725   -763    738       N  
ATOM    335  CZ  ARG A  41      34.695  14.004   7.805  1.00 66.87           C  
ANISOU  335  CZ  ARG A  41     7775   9146   8485   -834   -879    791       C  
ATOM    336  NH1 ARG A  41      35.688  13.523   8.544  1.00 65.79           N  
ANISOU  336  NH1 ARG A  41     7566   9092   8339   -863   -921    884       N  
ATOM    337  NH2 ARG A  41      34.532  15.314   7.683  1.00 68.92           N  
ANISOU  337  NH2 ARG A  41     8090   9334   8764   -916   -958    755       N  
ATOM    338  N   LYS A  42      32.702   9.165   5.162  1.00 47.36           N  
ANISOU  338  N   LYS A  42     5271   6711   6012   -358   -384    718       N  
ATOM    339  CA  LYS A  42      33.470   8.626   4.050  1.00 47.73           C  
ANISOU  339  CA  LYS A  42     5230   6814   6092   -297   -311    803       C  
ATOM    340  C   LYS A  42      34.194   9.726   3.286  1.00 47.42           C  
ANISOU  340  C   LYS A  42     5131   6805   6082   -361   -350    875       C  
ATOM    341  O   LYS A  42      33.613  10.759   2.948  1.00 42.93           O  
ANISOU  341  O   LYS A  42     4618   6181   5513   -415   -389    824       O  
ATOM    342  CB  LYS A  42      32.593   7.817   3.095  1.00 48.34           C  
ANISOU  342  CB  LYS A  42     5353   6854   6162   -201   -205    734       C  
ATOM    343  CG  LYS A  42      33.402   7.124   2.008  1.00 50.75           C  
ANISOU  343  CG  LYS A  42     5577   7219   6489   -124   -119    811       C  
ATOM    344  CD  LYS A  42      32.542   6.260   1.114  1.00 53.96           C  
ANISOU  344  CD  LYS A  42     6042   7583   6878    -33    -21    734       C  
ATOM    345  CE  LYS A  42      33.402   5.433   0.169  1.00 56.41           C  
ANISOU  345  CE  LYS A  42     6278   7953   7202     58     71    802       C  
ATOM    346  NZ  LYS A  42      34.380   4.593   0.919  1.00 59.15           N  
ANISOU  346  NZ  LYS A  42     6549   8349   7578    100     79    886       N  
ATOM    347  N   GLN A  43      35.473   9.498   3.023  1.00 50.99           N  
ANISOU  347  N   GLN A  43     5465   7345   6563   -355   -340   1003       N  
ATOM    348  CA  GLN A  43      36.238  10.413   2.197  1.00 53.90           C  
ANISOU  348  CA  GLN A  43     5760   7759   6962   -411   -365   1093       C  
ATOM    349  C   GLN A  43      36.380   9.819   0.808  1.00 54.50           C  
ANISOU  349  C   GLN A  43     5790   7878   7041   -316   -245   1122       C  
ATOM    350  O   GLN A  43      36.971   8.751   0.636  1.00 56.09           O  
ANISOU  350  O   GLN A  43     5925   8139   7249   -227   -167   1174       O  
ATOM    351  CB  GLN A  43      37.612  10.686   2.804  1.00 57.80           C  
ANISOU  351  CB  GLN A  43     6140   8336   7487   -479   -440   1230       C  
ATOM    352  CG  GLN A  43      38.426  11.703   2.019  1.00 65.17           C  
ANISOU  352  CG  GLN A  43     6989   9318   8454   -555   -476   1336       C  
ATOM    353  CD  GLN A  43      39.848  11.849   2.536  1.00 71.55           C  
ANISOU  353  CD  GLN A  43     7664  10224   9299   -619   -544   1489       C  
ATOM    354  OE1 GLN A  43      40.807  11.790   1.765  1.00 73.39           O  
ANISOU  354  OE1 GLN A  43     7771  10552   9563   -602   -501   1616       O  
ATOM    355  NE2 GLN A  43      39.989  12.047   3.843  1.00 72.91           N  
ANISOU  355  NE2 GLN A  43     7860  10379   9463   -694   -650   1483       N  
ATOM    356  N   VAL A  44      35.813  10.504  -0.178  1.00 52.90           N  
ANISOU  356  N   VAL A  44     5628   7641   6829   -333   -231   1085       N  
ATOM    357  CA  VAL A  44      35.946  10.087  -1.564  1.00 54.21           C  
ANISOU  357  CA  VAL A  44     5759   7855   6984   -256   -125   1111       C  
ATOM    358  C   VAL A  44      36.425  11.245  -2.421  1.00 53.50           C  
ANISOU  358  C   VAL A  44     5615   7803   6909   -331   -157   1194       C  
ATOM    359  O   VAL A  44      36.427  12.398  -1.989  1.00 53.42           O  
ANISOU  359  O   VAL A  44     5619   7756   6923   -443   -265   1209       O  
ATOM    360  CB  VAL A  44      34.619   9.566  -2.141  1.00 55.10           C  
ANISOU  360  CB  VAL A  44     5983   7894   7057   -186    -57    980       C  
ATOM    361  CG1 VAL A  44      34.266   8.223  -1.534  1.00 57.39           C  
ANISOU  361  CG1 VAL A  44     6311   8158   7336    -98     -4    918       C  
ATOM    362  CG2 VAL A  44      33.506  10.578  -1.914  1.00 55.54           C  
ANISOU  362  CG2 VAL A  44     6139   7854   7110   -261   -134    891       C  
ATOM    363  N   VAL A  45      36.844  10.925  -3.637  1.00 51.97           N  
ANISOU  363  N   VAL A  45     5361   7684   6699   -270    -62   1250       N  
ATOM    364  CA  VAL A  45      37.190  11.946  -4.604  1.00 50.35           C  
ANISOU  364  CA  VAL A  45     5109   7522   6499   -335    -79   1331       C  
ATOM    365  C   VAL A  45      36.135  11.929  -5.694  1.00 45.49           C  
ANISOU  365  C   VAL A  45     4582   6865   5836   -293    -19   1243       C  
ATOM    366  O   VAL A  45      35.830  10.881  -6.266  1.00 41.82           O  
ANISOU  366  O   VAL A  45     4144   6415   5329   -185     86   1188       O  
ATOM    367  CB  VAL A  45      38.585  11.721  -5.202  1.00 53.03           C  
ANISOU  367  CB  VAL A  45     5296   8003   6849   -309    -18   1483       C  
ATOM    368  CG1 VAL A  45      38.934  12.854  -6.152  1.00 53.68           C  
ANISOU  368  CG1 VAL A  45     5327   8133   6936   -391    -43   1580       C  
ATOM    369  CG2 VAL A  45      39.618  11.615  -4.090  1.00 53.32           C  
ANISOU  369  CG2 VAL A  45     5238   8086   6934   -345    -78   1575       C  
ATOM    370  N   ILE A  46      35.564  13.097  -5.956  1.00 45.02           N  
ANISOU  370  N   ILE A  46     4572   6747   5787   -381    -95   1231       N  
ATOM    371  CA  ILE A  46      34.495  13.236  -6.928  1.00 42.62           C  
ANISOU  371  CA  ILE A  46     4352   6399   5444   -358    -61   1156       C  
ATOM    372  C   ILE A  46      34.830  14.393  -7.859  1.00 44.68           C  
ANISOU  372  C   ILE A  46     4566   6696   5712   -438    -96   1257       C  
ATOM    373  O   ILE A  46      34.954  15.539  -7.420  1.00 47.20           O  
ANISOU  373  O   ILE A  46     4882   6970   6084   -545   -205   1300       O  
ATOM    374  CB  ILE A  46      33.149  13.497  -6.225  1.00 40.43           C  
ANISOU  374  CB  ILE A  46     4199   5988   5175   -378   -124   1021       C  
ATOM    375  CG1 ILE A  46      32.875  12.398  -5.189  1.00 38.48           C  
ANISOU  375  CG1 ILE A  46     3989   5710   4922   -312    -98    938       C  
ATOM    376  CG2 ILE A  46      32.019  13.597  -7.242  1.00 37.99           C  
ANISOU  376  CG2 ILE A  46     3968   5638   4829   -352    -92    952       C  
ATOM    377  CD1 ILE A  46      31.721  12.699  -4.248  1.00 35.65           C  
ANISOU  377  CD1 ILE A  46     3734   5236   4574   -340   -164    822       C  
ATOM    378  N   ASP A  47      34.998  14.089  -9.141  1.00 44.55           N  
ANISOU  378  N   ASP A  47     4519   6764   5644   -387     -4   1298       N  
ATOM    379  CA  ASP A  47      35.330  15.114 -10.122  1.00 49.95           C  
ANISOU  379  CA  ASP A  47     5153   7498   6326   -460    -26   1407       C  
ATOM    380  C   ASP A  47      36.581  15.892  -9.718  1.00 53.47           C  
ANISOU  380  C   ASP A  47     5482   8002   6832   -555    -95   1557       C  
ATOM    381  O   ASP A  47      36.648  17.113  -9.881  1.00 53.91           O  
ANISOU  381  O   ASP A  47     5527   8030   6928   -665   -186   1629       O  
ATOM    382  CB  ASP A  47      34.153  16.075 -10.299  1.00 51.63           C  
ANISOU  382  CB  ASP A  47     5466   7597   6552   -524   -109   1346       C  
ATOM    383  CG  ASP A  47      32.893  15.373 -10.758  1.00 52.46           C  
ANISOU  383  CG  ASP A  47     5678   7652   6600   -443    -51   1211       C  
ATOM    384  OD1 ASP A  47      32.999  14.399 -11.536  1.00 53.45           O  
ANISOU  384  OD1 ASP A  47     5796   7856   6656   -354     59   1197       O  
ATOM    385  OD2 ASP A  47      31.797  15.796 -10.336  1.00 51.99           O  
ANISOU  385  OD2 ASP A  47     5711   7477   6567   -467   -118   1120       O  
ATOM    386  N   GLY A  48      37.569  15.184  -9.182  1.00 54.39           N  
ANISOU  386  N   GLY A  48     5509   8196   6961   -515    -56   1610       N  
ATOM    387  CA  GLY A  48      38.822  15.806  -8.796  1.00 56.57           C  
ANISOU  387  CA  GLY A  48     5659   8541   7294   -604   -119   1763       C  
ATOM    388  C   GLY A  48      38.733  16.679  -7.558  1.00 57.52           C  
ANISOU  388  C   GLY A  48     5816   8555   7483   -720   -272   1749       C  
ATOM    389  O   GLY A  48      39.556  17.573  -7.365  1.00 60.09           O  
ANISOU  389  O   GLY A  48     6063   8908   7861   -833   -360   1873       O  
ATOM    390  N   GLU A  49      37.729  16.431  -6.723  1.00 55.05           N  
ANISOU  390  N   GLU A  49     5626   8123   7169   -696   -305   1598       N  
ATOM    391  CA  GLU A  49      37.635  17.099  -5.430  1.00 54.67           C  
ANISOU  391  CA  GLU A  49     5624   7978   7171   -789   -438   1563       C  
ATOM    392  C   GLU A  49      37.560  16.078  -4.302  1.00 54.16           C  
ANISOU  392  C   GLU A  49     5584   7901   7094   -723   -420   1483       C  
ATOM    393  O   GLU A  49      36.786  15.121  -4.368  1.00 51.60           O  
ANISOU  393  O   GLU A  49     5325   7552   6727   -618   -336   1374       O  
ATOM    394  CB  GLU A  49      36.412  18.013  -5.365  1.00 58.11           C  
ANISOU  394  CB  GLU A  49     6190   8269   7619   -838   -514   1459       C  
ATOM    395  CG  GLU A  49      36.254  18.698  -4.009  1.00 63.23           C  
ANISOU  395  CG  GLU A  49     6902   8810   8310   -923   -644   1403       C  
ATOM    396  CD  GLU A  49      34.958  19.487  -3.879  1.00 66.52           C  
ANISOU  396  CD  GLU A  49     7455   9080   8741   -945   -703   1282       C  
ATOM    397  OE1 GLU A  49      34.969  20.537  -3.201  1.00 69.56           O  
ANISOU  397  OE1 GLU A  49     7883   9374   9172  -1045   -824   1274       O  
ATOM    398  OE2 GLU A  49      33.927  19.056  -4.439  1.00 64.30           O  
ANISOU  398  OE2 GLU A  49     7238   8769   8424   -862   -630   1193       O  
ATOM    399  N   THR A  50      38.364  16.280  -3.266  1.00 53.84           N  
ANISOU  399  N   THR A  50     5492   7876   7090   -792   -504   1541       N  
ATOM    400  CA  THR A  50      38.298  15.411  -2.100  1.00 51.01           C  
ANISOU  400  CA  THR A  50     5159   7504   6718   -746   -504   1475       C  
ATOM    401  C   THR A  50      37.098  15.809  -1.255  1.00 47.39           C  
ANISOU  401  C   THR A  50     4850   6907   6250   -773   -573   1323       C  
ATOM    402  O   THR A  50      37.022  16.931  -0.753  1.00 47.84           O  
ANISOU  402  O   THR A  50     4950   6892   6336   -882   -691   1315       O  
ATOM    403  CB  THR A  50      39.577  15.483  -1.240  1.00 52.54           C  
ANISOU  403  CB  THR A  50     5244   7771   6947   -815   -578   1595       C  
ATOM    404  OG1 THR A  50      40.731  15.368  -2.081  1.00 53.52           O  
ANISOU  404  OG1 THR A  50     5216   8029   7092   -807   -524   1756       O  
ATOM    405  CG2 THR A  50      39.589  14.357  -0.212  1.00 49.35           C  
ANISOU  405  CG2 THR A  50     4849   7378   6524   -744   -553   1547       C  
ATOM    406  N   CYS A  51      36.156  14.888  -1.106  1.00 42.96           N  
ANISOU  406  N   CYS A  51     4367   6307   5649   -672   -499   1202       N  
ATOM    407  CA  CYS A  51      34.932  15.187  -0.383  1.00 41.67           C  
ANISOU  407  CA  CYS A  51     4338   6024   5472   -683   -544   1058       C  
ATOM    408  C   CYS A  51      34.861  14.432   0.928  1.00 41.32           C  
ANISOU  408  C   CYS A  51     4321   5974   5404   -658   -556   1003       C  
ATOM    409  O   CYS A  51      35.015  13.209   0.967  1.00 42.09           O  
ANISOU  409  O   CYS A  51     4386   6125   5482   -568   -473   1008       O  
ATOM    410  CB  CYS A  51      33.708  14.852  -1.236  1.00 39.52           C  
ANISOU  410  CB  CYS A  51     4141   5702   5171   -602   -461    960       C  
ATOM    411  SG  CYS A  51      33.669  15.710  -2.814  1.00 45.34           S  
ANISOU  411  SG  CYS A  51     4855   6450   5923   -629   -447   1024       S  
ATOM    412  N   LEU A  52      34.629  15.172   2.002  1.00 39.69           N  
ANISOU  412  N   LEU A  52     4180   5700   5199   -738   -661    950       N  
ATOM    413  CA  LEU A  52      34.368  14.557   3.288  1.00 45.23           C  
ANISOU  413  CA  LEU A  52     4929   6391   5866   -720   -676    884       C  
ATOM    414  C   LEU A  52      32.853  14.435   3.461  1.00 41.33           C  
ANISOU  414  C   LEU A  52     4558   5806   5341   -666   -640    731       C  
ATOM    415  O   LEU A  52      32.158  15.429   3.681  1.00 40.74           O  
ANISOU  415  O   LEU A  52     4567   5643   5271   -715   -700    655       O  
ATOM    416  CB  LEU A  52      35.014  15.374   4.408  1.00 53.63           C  
ANISOU  416  CB  LEU A  52     5996   7446   6935   -837   -809    911       C  
ATOM    417  CG  LEU A  52      36.502  15.676   4.161  1.00 61.23           C  
ANISOU  417  CG  LEU A  52     6828   8498   7940   -909   -860   1076       C  
ATOM    418  CD1 LEU A  52      37.106  16.530   5.270  1.00 63.37           C  
ANISOU  418  CD1 LEU A  52     7111   8753   8214  -1040  -1008   1099       C  
ATOM    419  CD2 LEU A  52      37.313  14.392   3.972  1.00 62.76           C  
ANISOU  419  CD2 LEU A  52     6904   8809   8133   -827   -774   1173       C  
ATOM    420  N   LEU A  53      32.344  13.213   3.325  1.00 37.26           N  
ANISOU  420  N   LEU A  53     4050   5309   4798   -565   -541    692       N  
ATOM    421  CA  LEU A  53      30.905  12.966   3.401  1.00 36.68           C  
ANISOU  421  CA  LEU A  53     4077   5163   4699   -511   -498    563       C  
ATOM    422  C   LEU A  53      30.462  12.651   4.825  1.00 33.92           C  
ANISOU  422  C   LEU A  53     3786   4793   4308   -515   -526    491       C  
ATOM    423  O   LEU A  53      30.913  11.673   5.416  1.00 35.10           O  
ANISOU  423  O   LEU A  53     3900   4999   4439   -485   -503    528       O  
ATOM    424  CB  LEU A  53      30.491  11.823   2.461  1.00 32.42           C  
ANISOU  424  CB  LEU A  53     3523   4645   4149   -408   -382    553       C  
ATOM    425  CG  LEU A  53      30.837  11.972   0.974  1.00 31.11           C  
ANISOU  425  CG  LEU A  53     3306   4511   4004   -389   -335    615       C  
ATOM    426  CD1 LEU A  53      30.299  10.807   0.160  1.00 28.74           C  
ANISOU  426  CD1 LEU A  53     3018   4220   3682   -288   -226    580       C  
ATOM    427  CD2 LEU A  53      30.315  13.287   0.431  1.00 30.14           C  
ANISOU  427  CD2 LEU A  53     3224   4325   3901   -448   -388    591       C  
ATOM    428  N   ASP A  54      29.586  13.489   5.370  1.00 32.95           N  
ANISOU  428  N   ASP A  54     3753   4593   4172   -549   -575    393       N  
ATOM    429  CA  ASP A  54      28.970  13.229   6.665  1.00 36.14           C  
ANISOU  429  CA  ASP A  54     4226   4981   4526   -545   -588    310       C  
ATOM    430  C   ASP A  54      27.590  12.661   6.414  1.00 32.28           C  
ANISOU  430  C   ASP A  54     3791   4452   4021   -465   -506    218       C  
ATOM    431  O   ASP A  54      26.653  13.408   6.123  1.00 32.22           O  
ANISOU  431  O   ASP A  54     3842   4375   4025   -463   -510    142       O  
ATOM    432  CB  ASP A  54      28.842  14.514   7.483  1.00 45.52           C  
ANISOU  432  CB  ASP A  54     5484   6109   5702   -625   -688    250       C  
ATOM    433  CG  ASP A  54      30.161  14.969   8.064  1.00 56.76           C  
ANISOU  433  CG  ASP A  54     6864   7574   7127   -718   -786    333       C  
ATOM    434  OD1 ASP A  54      30.464  16.181   7.991  1.00 59.84           O  
ANISOU  434  OD1 ASP A  54     7276   7914   7546   -797   -871    335       O  
ATOM    435  OD2 ASP A  54      30.894  14.111   8.600  1.00 62.82           O  
ANISOU  435  OD2 ASP A  54     7575   8423   7872   -715   -782    401       O  
ATOM    436  N   ILE A  55      27.461  11.344   6.525  1.00 27.46           N  
ANISOU  436  N   ILE A  55     3160   3884   3391   -402   -435    231       N  
ATOM    437  CA  ILE A  55      26.210  10.680   6.177  1.00 27.96           C  
ANISOU  437  CA  ILE A  55     3264   3915   3445   -332   -358    160       C  
ATOM    438  C   ILE A  55      25.386  10.273   7.393  1.00 30.14           C  
ANISOU  438  C   ILE A  55     3594   4185   3671   -320   -349     90       C  
ATOM    439  O   ILE A  55      25.843   9.511   8.244  1.00 31.96           O  
ANISOU  439  O   ILE A  55     3807   4465   3871   -319   -350    126       O  
ATOM    440  CB  ILE A  55      26.458   9.451   5.285  1.00 23.97           C  
ANISOU  440  CB  ILE A  55     2707   3443   2956   -265   -278    213       C  
ATOM    441  CG1 ILE A  55      27.237   9.867   4.030  1.00 24.95           C  
ANISOU  441  CG1 ILE A  55     2777   3586   3119   -272   -274    282       C  
ATOM    442  CG2 ILE A  55      25.134   8.789   4.910  1.00 23.78           C  
ANISOU  442  CG2 ILE A  55     2730   3380   2924   -207   -210    140       C  
ATOM    443  CD1 ILE A  55      27.993   8.723   3.356  1.00 22.41           C  
ANISOU  443  CD1 ILE A  55     2389   3318   2806   -212   -206    356       C  
ATOM    444  N   LEU A  56      24.163  10.788   7.468  1.00 27.86           N  
ANISOU  444  N   LEU A  56     3369   3842   3374   -309   -340     -4       N  
ATOM    445  CA  LEU A  56      23.248  10.396   8.528  1.00 25.88           C  
ANISOU  445  CA  LEU A  56     3166   3594   3073   -290   -317    -71       C  
ATOM    446  C   LEU A  56      22.252   9.355   8.013  1.00 24.14           C  
ANISOU  446  C   LEU A  56     2943   3367   2860   -226   -235    -89       C  
ATOM    447  O   LEU A  56      21.543   9.578   7.035  1.00 23.86           O  
ANISOU  447  O   LEU A  56     2916   3291   2860   -201   -208   -118       O  
ATOM    448  CB  LEU A  56      22.511  11.616   9.080  1.00 25.48           C  
ANISOU  448  CB  LEU A  56     3183   3493   3006   -313   -355   -165       C  
ATOM    449  CG  LEU A  56      21.631  11.402  10.315  1.00 26.50           C  
ANISOU  449  CG  LEU A  56     3363   3637   3069   -297   -334   -238       C  
ATOM    450  CD1 LEU A  56      22.473  10.977  11.509  1.00 25.82           C  
ANISOU  450  CD1 LEU A  56     3273   3617   2921   -335   -369   -199       C  
ATOM    451  CD2 LEU A  56      20.855  12.669  10.642  1.00 28.04           C  
ANISOU  451  CD2 LEU A  56     3624   3771   3257   -301   -359   -338       C  
ATOM    452  N   ASP A  57      22.220   8.206   8.674  1.00 22.78           N  
ANISOU  452  N   ASP A  57     2763   3236   2659   -205   -201    -66       N  
ATOM    453  CA  ASP A  57      21.299   7.140   8.324  1.00 19.73           C  
ANISOU  453  CA  ASP A  57     2377   2839   2278   -155   -132    -78       C  
ATOM    454  C   ASP A  57      20.175   7.147   9.360  1.00 26.07           C  
ANISOU  454  C   ASP A  57     3222   3647   3036   -153   -117   -142       C  
ATOM    455  O   ASP A  57      20.420   6.985  10.554  1.00 25.33           O  
ANISOU  455  O   ASP A  57     3139   3597   2890   -174   -134   -134       O  
ATOM    456  CB  ASP A  57      22.042   5.806   8.298  1.00 21.83           C  
ANISOU  456  CB  ASP A  57     2604   3138   2553   -131   -104      1       C  
ATOM    457  CG  ASP A  57      21.155   4.646   7.916  1.00 28.82           C  
ANISOU  457  CG  ASP A  57     3498   4002   3451    -87    -42     -9       C  
ATOM    458  OD1 ASP A  57      20.096   4.885   7.304  1.00 31.73           O  
ANISOU  458  OD1 ASP A  57     3890   4332   3832    -75    -19    -65       O  
ATOM    459  OD2 ASP A  57      21.523   3.490   8.227  1.00 31.78           O  
ANISOU  459  OD2 ASP A  57     3855   4393   3826    -66    -20     44       O  
ATOM    460  N   THR A  58      18.946   7.351   8.890  1.00 26.42           N  
ANISOU  460  N   THR A  58     3286   3655   3097   -129    -84   -201       N  
ATOM    461  CA  THR A  58      17.826   7.654   9.767  1.00 25.52           C  
ANISOU  461  CA  THR A  58     3205   3546   2944   -122    -66   -268       C  
ATOM    462  C   THR A  58      16.886   6.466   9.944  1.00 26.85           C  
ANISOU  462  C   THR A  58     3364   3734   3104    -97     -7   -258       C  
ATOM    463  O   THR A  58      16.987   5.478   9.225  1.00 28.90           O  
ANISOU  463  O   THR A  58     3601   3984   3398    -82     17   -212       O  
ATOM    464  CB  THR A  58      17.032   8.857   9.230  1.00 21.78           C  
ANISOU  464  CB  THR A  58     2754   3021   2501   -111    -74   -337       C  
ATOM    465  OG1 THR A  58      16.397   8.504   7.993  1.00 18.84           O  
ANISOU  465  OG1 THR A  58     2361   2617   2181    -85    -44   -329       O  
ATOM    466  CG2 THR A  58      17.963  10.052   9.017  1.00 19.87           C  
ANISOU  466  CG2 THR A  58     2525   2748   2275   -145   -140   -340       C  
ATOM    467  N   ALA A  59      15.971   6.574  10.907  1.00 21.14           N  
ANISOU  467  N   ALA A  59     2659   3038   2335    -91     17   -302       N  
ATOM    468  CA  ALA A  59      15.008   5.513  11.173  1.00 23.96           C  
ANISOU  468  CA  ALA A  59     3000   3419   2683    -76     70   -285       C  
ATOM    469  C   ALA A  59      13.878   5.524  10.148  1.00 23.22           C  
ANISOU  469  C   ALA A  59     2894   3285   2645    -52     99   -311       C  
ATOM    470  O   ALA A  59      13.520   6.576   9.621  1.00 21.29           O  
ANISOU  470  O   ALA A  59     2657   3005   2426    -40     86   -361       O  
ATOM    471  CB  ALA A  59      14.442   5.653  12.587  1.00 24.66           C  
ANISOU  471  CB  ALA A  59     3106   3568   2696    -80     90   -315       C  
ATOM    472  N   GLY A  60      13.315   4.354   9.870  1.00 26.88           N  
ANISOU  472  N   GLY A  60     3336   3749   3128    -49    132   -273       N  
ATOM    473  CA  GLY A  60      12.179   4.256   8.966  1.00 23.49           C  
ANISOU  473  CA  GLY A  60     2891   3288   2745    -36    154   -291       C  
ATOM    474  C   GLY A  60      11.011   5.043   9.525  1.00 25.70           C  
ANISOU  474  C   GLY A  60     3165   3593   3009    -20    178   -344       C  
ATOM    475  O   GLY A  60      10.228   5.646   8.794  1.00 29.66           O  
ANISOU  475  O   GLY A  60     3654   4065   3552     -2    179   -375       O  
ATOM    476  N   GLN A  61      10.913   5.053  10.844  1.00 29.92           N  
ANISOU  476  N   GLN A  61     3705   4184   3480    -21    198   -351       N  
ATOM    477  CA  GLN A  61       9.816   5.708  11.532  1.00 41.56           C  
ANISOU  477  CA  GLN A  61     5171   5693   4926      5    235   -403       C  
ATOM    478  C   GLN A  61      10.341   6.371  12.795  1.00 44.11           C  
ANISOU  478  C   GLN A  61     5531   6058   5169      6    230   -442       C  
ATOM    479  O   GLN A  61      10.928   5.714  13.652  1.00 45.94           O  
ANISOU  479  O   GLN A  61     5773   6340   5344    -20    228   -403       O  
ATOM    480  CB  GLN A  61       8.758   4.671  11.892  1.00 47.65           C  
ANISOU  480  CB  GLN A  61     5901   6512   5691     -1    285   -360       C  
ATOM    481  CG  GLN A  61       7.377   5.222  12.116  1.00 54.28           C  
ANISOU  481  CG  GLN A  61     6708   7383   6534     33    331   -398       C  
ATOM    482  CD  GLN A  61       6.323   4.129  12.090  1.00 60.45           C  
ANISOU  482  CD  GLN A  61     7434   8199   7334     15    368   -337       C  
ATOM    483  OE1 GLN A  61       6.733   2.913  11.730  1.00 65.68           O  
ANISOU  483  OE1 GLN A  61     8054   8905   7997     39    414   -349       O  
ATOM    484  NE2 GLN A  61       5.155   4.375  12.384  1.00 59.01           N  
ANISOU  484  NE2 GLN A  61     7251   7995   7173    -26    349   -270       N  
ATOM    485  N   GLU A  62      10.141   7.677  12.900  1.00 44.59           N  
ANISOU  485  N   GLU A  62     5619   6096   5226     34    222   -520       N  
ATOM    486  CA  GLU A  62      10.572   8.416  14.074  1.00 47.70           C  
ANISOU  486  CA  GLU A  62     6063   6522   5539     34    212   -575       C  
ATOM    487  C   GLU A  62       9.409   8.531  15.059  1.00 53.47           C  
ANISOU  487  C   GLU A  62     6787   7320   6211     71    281   -617       C  
ATOM    488  O   GLU A  62       8.277   8.823  14.669  1.00 53.86           O  
ANISOU  488  O   GLU A  62     6802   7358   6303    115    322   -642       O  
ATOM    489  CB  GLU A  62      11.063   9.803  13.661  1.00 49.00           C  
ANISOU  489  CB  GLU A  62     6271   6613   5735     42    160   -640       C  
ATOM    490  CG  GLU A  62      12.171  10.369  14.527  1.00 51.39           C  
ANISOU  490  CG  GLU A  62     6633   6924   5970      8    108   -669       C  
ATOM    491  CD  GLU A  62      13.490   9.638  14.353  1.00 49.52           C  
ANISOU  491  CD  GLU A  62     6385   6698   5733    -46     58   -586       C  
ATOM    492  OE1 GLU A  62      13.947   9.011  15.333  1.00 51.75           O  
ANISOU  492  OE1 GLU A  62     6675   7048   5941    -74     57   -554       O  
ATOM    493  OE2 GLU A  62      14.075   9.701  13.246  1.00 43.23           O  
ANISOU  493  OE2 GLU A  62     5570   5846   5008    -59     22   -550       O  
ATOM    494  N   GLU A  63       9.684   8.285  16.335  1.00 60.01           N  
ANISOU  494  N   GLU A  63     7641   8223   6937     55    295   -619       N  
ATOM    495  CA  GLU A  63       8.650   8.386  17.359  1.00 66.97           C  
ANISOU  495  CA  GLU A  63     8517   9184   7744     91    368   -658       C  
ATOM    496  C   GLU A  63       8.380   9.847  17.698  1.00 67.72           C  
ANISOU  496  C   GLU A  63     8666   9249   7815    142    374   -778       C  
ATOM    497  O   GLU A  63       7.252  10.219  18.021  1.00 68.24           O  
ANISOU  497  O   GLU A  63     8715   9347   7868    202    443   -826       O  
ATOM    498  CB  GLU A  63       9.051   7.615  18.618  1.00 71.68           C  
ANISOU  498  CB  GLU A  63     9127   9881   8228     54    381   -615       C  
ATOM    499  CG  GLU A  63      10.268   8.183  19.324  1.00 75.77           C  
ANISOU  499  CG  GLU A  63     9719  10400   8669     20    317   -652       C  
ATOM    500  CD  GLU A  63      11.309   7.128  19.631  1.00 79.86           C  
ANISOU  500  CD  GLU A  63    10228  10955   9159    -43    274   -551       C  
ATOM    501  OE1 GLU A  63      12.507   7.477  19.703  1.00 82.27           O  
ANISOU  501  OE1 GLU A  63    10573  11236   9451    -81    199   -552       O  
ATOM    502  OE2 GLU A  63      10.929   5.950  19.800  1.00 80.89           O  
ANISOU  502  OE2 GLU A  63    10309  11138   9286    -56    311   -465       O  
ATOM    503  N   TYR A  64       9.421  10.671  17.620  1.00 66.28           N  
ANISOU  503  N   TYR A  64     8549   9003   7632    120    300   -822       N  
ATOM    504  CA  TYR A  64       9.286  12.098  17.887  1.00 65.41           C  
ANISOU  504  CA  TYR A  64     8505   8840   7509    162    290   -939       C  
ATOM    505  C   TYR A  64       9.540  12.935  16.640  1.00 57.86           C  
ANISOU  505  C   TYR A  64     7553   7762   6670    169    233   -955       C  
ATOM    506  O   TYR A  64      10.604  12.849  16.025  1.00 52.56           O  
ANISOU  506  O   TYR A  64     6887   7046   6038    113    160   -907       O  
ATOM    507  CB  TYR A  64      10.222  12.532  19.018  1.00 72.69           C  
ANISOU  507  CB  TYR A  64     9512   9788   8318    124    245   -991       C  
ATOM    508  CG  TYR A  64       9.857  11.943  20.361  1.00 80.79           C  
ANISOU  508  CG  TYR A  64    10545  10940   9210    125    306   -992       C  
ATOM    509  CD1 TYR A  64       8.673  12.297  20.997  1.00 85.86           C  
ANISOU  509  CD1 TYR A  64    11190  11632   9800    199    397  -1065       C  
ATOM    510  CD2 TYR A  64      10.696  11.035  20.995  1.00 84.13           C  
ANISOU  510  CD2 TYR A  64    10969  11439   9559     57    275   -915       C  
ATOM    511  CE1 TYR A  64       8.331  11.761  22.228  1.00 90.04           C  
ANISOU  511  CE1 TYR A  64    11724  12289  10197    199    458  -1060       C  
ATOM    512  CE2 TYR A  64      10.365  10.493  22.225  1.00 88.33           C  
ANISOU  512  CE2 TYR A  64    11507  12091   9962     54    328   -907       C  
ATOM    513  CZ  TYR A  64       9.182  10.860  22.838  1.00 91.92           C  
ANISOU  513  CZ  TYR A  64    11966  12601  10358    123    421   -980       C  
ATOM    514  OH  TYR A  64       8.849  10.324  24.062  1.00 95.58           O  
ANISOU  514  OH  TYR A  64    12433  13197  10685    118    479   -965       O  
ATOM    515  N   SER A  65       8.552  13.743  16.275  1.00 58.49           N  
ANISOU  515  N   SER A  65     7626   7794   6806    239    268  -1016       N  
ATOM    516  CA  SER A  65       8.671  14.643  15.132  1.00 62.16           C  
ANISOU  516  CA  SER A  65     8096   8142   7380    250    215  -1030       C  
ATOM    517  C   SER A  65       9.914  15.530  15.204  1.00 61.55           C  
ANISOU  517  C   SER A  65     8100   7991   7297    202    122  -1068       C  
ATOM    518  O   SER A  65      10.551  15.798  14.185  1.00 60.19           O  
ANISOU  518  O   SER A  65     7920   7747   7204    168     57  -1026       O  
ATOM    519  CB  SER A  65       7.415  15.508  14.994  1.00 64.47           C  
ANISOU  519  CB  SER A  65     8378   8395   7722    342    266  -1100       C  
ATOM    520  OG  SER A  65       6.307  14.731  14.571  1.00 65.72           O  
ANISOU  520  OG  SER A  65     8443   8608   7919    374    333  -1041       O  
ATOM    521  N   ALA A  66      10.257  15.981  16.407  1.00 61.14           N  
ANISOU  521  N   ALA A  66     8125   7961   7146    196    114  -1144       N  
ATOM    522  CA  ALA A  66      11.380  16.896  16.590  1.00 60.28           C  
ANISOU  522  CA  ALA A  66     8099   7779   7025    144     18  -1188       C  
ATOM    523  C   ALA A  66      12.703  16.277  16.141  1.00 61.22           C  
ANISOU  523  C   ALA A  66     8193   7909   7157     52    -56  -1085       C  
ATOM    524  O   ALA A  66      13.625  16.981  15.726  1.00 62.41           O  
ANISOU  524  O   ALA A  66     8376   7986   7350      3   -143  -1081       O  
ATOM    525  CB  ALA A  66      11.465  17.356  18.043  1.00 58.62           C  
ANISOU  525  CB  ALA A  66     7981   7606   6688    148     24  -1289       C  
ATOM    526  N   MET A  67      12.795  14.957  16.220  1.00 60.21           N  
ANISOU  526  N   MET A  67     8004   7875   6999     31    -21   -998       N  
ATOM    527  CA  MET A  67      14.004  14.274  15.790  1.00 57.66           C  
ANISOU  527  CA  MET A  67     7649   7567   6693    -41    -79   -897       C  
ATOM    528  C   MET A  67      14.109  14.273  14.262  1.00 52.52           C  
ANISOU  528  C   MET A  67     6944   6849   6161    -41    -98   -836       C  
ATOM    529  O   MET A  67      15.203  14.385  13.712  1.00 51.27           O  
ANISOU  529  O   MET A  67     6779   6662   6039    -93   -164   -783       O  
ATOM    530  CB  MET A  67      14.044  12.853  16.349  1.00 60.35           C  
ANISOU  530  CB  MET A  67     7945   8016   6970    -57    -36   -823       C  
ATOM    531  CG  MET A  67      15.437  12.248  16.420  1.00 60.78           C  
ANISOU  531  CG  MET A  67     7985   8101   7008   -128    -99   -735       C  
ATOM    532  SD  MET A  67      15.444  10.696  17.337  1.00 95.77           S  
ANISOU  532  SD  MET A  67    12380  12654  11356   -142    -54   -655       S  
ATOM    533  CE  MET A  67      17.141  10.173  17.110  1.00 62.27           C  
ANISOU  533  CE  MET A  67     8109   8421   7131   -212   -137   -547       C  
ATOM    534  N   ARG A  68      12.970  14.153  13.582  1.00 50.99           N  
ANISOU  534  N   ARG A  68     6710   6639   6026     17    -39   -841       N  
ATOM    535  CA  ARG A  68      12.935  14.258  12.124  1.00 52.41           C  
ANISOU  535  CA  ARG A  68     6847   6758   6310     20    -57   -793       C  
ATOM    536  C   ARG A  68      13.284  15.679  11.689  1.00 46.45           C  
ANISOU  536  C   ARG A  68     6137   5902   5610     13   -124   -836       C  
ATOM    537  O   ARG A  68      14.052  15.886  10.748  1.00 42.35           O  
ANISOU  537  O   ARG A  68     5603   5341   5148    -26   -178   -780       O  
ATOM    538  CB  ARG A  68      11.549  13.911  11.576  1.00 58.93           C  
ANISOU  538  CB  ARG A  68     7621   7589   7180     79     11   -792       C  
ATOM    539  CG  ARG A  68      10.903  12.679  12.170  1.00 66.43           C  
ANISOU  539  CG  ARG A  68     8532   8631   8077     92     82   -763       C  
ATOM    540  CD  ARG A  68       9.431  12.945  12.490  1.00 74.35           C  
ANISOU  540  CD  ARG A  68     9517   9650   9082    160    151   -816       C  
ATOM    541  NE  ARG A  68       8.506  12.061  11.782  1.00 76.97           N  
ANISOU  541  NE  ARG A  68     9774  10009   9461    175    196   -757       N  
ATOM    542  CZ  ARG A  68       7.312  11.702  12.249  1.00 79.28           C  
ANISOU  542  CZ  ARG A  68    10027  10360   9737    215    266   -764       C  
ATOM    543  NH1 ARG A  68       6.901  12.139  13.433  1.00 79.63           N  
ANISOU  543  NH1 ARG A  68    10097  10446   9711    253    311   -830       N  
ATOM    544  NH2 ARG A  68       6.532  10.896  11.540  1.00 81.09           N  
ANISOU  544  NH2 ARG A  68    10188  10608  10015    214    292   -704       N  
ATOM    545  N   ASP A  69      12.701  16.658  12.371  1.00 43.89           N  
ANISOU  545  N   ASP A  69     5870   5538   5269     53   -117   -935       N  
ATOM    546  CA  ASP A  69      12.924  18.053  12.021  1.00 43.60           C  
ANISOU  546  CA  ASP A  69     5886   5389   5292     51   -182   -983       C  
ATOM    547  C   ASP A  69      14.403  18.412  12.138  1.00 40.09           C  
ANISOU  547  C   ASP A  69     5479   4921   4833    -37   -276   -955       C  
ATOM    548  O   ASP A  69      14.918  19.212  11.355  1.00 43.82           O  
ANISOU  548  O   ASP A  69     5959   5311   5378    -68   -344   -932       O  
ATOM    549  CB  ASP A  69      12.074  18.988  12.893  1.00 47.30           C  
ANISOU  549  CB  ASP A  69     6420   5816   5734    117   -154  -1106       C  
ATOM    550  CG  ASP A  69      10.577  18.860  12.616  1.00 49.19           C  
ANISOU  550  CG  ASP A  69     6610   6068   6014    210    -67  -1125       C  
ATOM    551  OD1 ASP A  69      10.197  18.126  11.680  1.00 46.71           O  
ANISOU  551  OD1 ASP A  69     6215   5782   5751    214    -41  -1044       O  
ATOM    552  OD2 ASP A  69       9.778  19.504  13.332  1.00 51.12           O  
ANISOU  552  OD2 ASP A  69     6894   6292   6235    280    -25  -1221       O  
ATOM    553  N   GLN A  70      15.085  17.812  13.108  1.00 32.52           N  
ANISOU  553  N   GLN A  70     4536   4039   3781    -80   -284   -947       N  
ATOM    554  CA  GLN A  70      16.486  18.136  13.345  1.00 35.64           C  
ANISOU  554  CA  GLN A  70     4961   4424   4158   -168   -378   -917       C  
ATOM    555  C   GLN A  70      17.393  17.776  12.169  1.00 38.87           C  
ANISOU  555  C   GLN A  70     5300   4832   4636   -216   -416   -798       C  
ATOM    556  O   GLN A  70      18.242  18.575  11.775  1.00 44.55           O  
ANISOU  556  O   GLN A  70     6035   5493   5400   -273   -498   -774       O  
ATOM    557  CB  GLN A  70      17.002  17.490  14.630  1.00 38.14           C  
ANISOU  557  CB  GLN A  70     5300   4835   4357   -204   -380   -921       C  
ATOM    558  CG  GLN A  70      18.488  17.712  14.840  1.00 43.31           C  
ANISOU  558  CG  GLN A  70     5968   5492   4995   -301   -482   -870       C  
ATOM    559  CD  GLN A  70      18.927  17.513  16.275  1.00 51.21           C  
ANISOU  559  CD  GLN A  70     7020   6564   5872   -341   -507   -903       C  
ATOM    560  OE1 GLN A  70      18.786  18.409  17.111  1.00 57.02           O  
ANISOU  560  OE1 GLN A  70     7851   7262   6553   -349   -541  -1009       O  
ATOM    561  NE2 GLN A  70      19.476  16.341  16.568  1.00 52.34           N  
ANISOU  561  NE2 GLN A  70     7107   6809   5971   -368   -495   -813       N  
ATOM    562  N   TYR A  71      17.233  16.581  11.608  1.00 31.94           N  
ANISOU  562  N   TYR A  71     4348   4021   3768   -196   -358   -723       N  
ATOM    563  CA  TYR A  71      18.070  16.220  10.470  1.00 30.01           C  
ANISOU  563  CA  TYR A  71     4041   3780   3583   -231   -382   -619       C  
ATOM    564  C   TYR A  71      17.626  16.902   9.168  1.00 30.14           C  
ANISOU  564  C   TYR A  71     4041   3719   3691   -210   -389   -609       C  
ATOM    565  O   TYR A  71      18.440  17.173   8.289  1.00 31.53           O  
ANISOU  565  O   TYR A  71     4188   3875   3916   -252   -434   -539       O  
ATOM    566  CB  TYR A  71      18.254  14.699  10.327  1.00 28.71           C  
ANISOU  566  CB  TYR A  71     3812   3704   3393   -221   -327   -542       C  
ATOM    567  CG  TYR A  71      17.036  13.862   9.980  1.00 29.11           C  
ANISOU  567  CG  TYR A  71     3833   3776   3452   -158   -242   -550       C  
ATOM    568  CD1 TYR A  71      16.545  12.911  10.875  1.00 29.55           C  
ANISOU  568  CD1 TYR A  71     3885   3899   3443   -136   -187   -560       C  
ATOM    569  CD2 TYR A  71      16.412  13.977   8.741  1.00 26.84           C  
ANISOU  569  CD2 TYR A  71     3517   3447   3235   -128   -221   -537       C  
ATOM    570  CE1 TYR A  71      15.453  12.120  10.555  1.00 29.58           C  
ANISOU  570  CE1 TYR A  71     3856   3922   3459    -89   -116   -557       C  
ATOM    571  CE2 TYR A  71      15.315  13.189   8.411  1.00 26.51           C  
ANISOU  571  CE2 TYR A  71     3446   3426   3201    -81   -154   -538       C  
ATOM    572  CZ  TYR A  71      14.841  12.261   9.320  1.00 30.67           C  
ANISOU  572  CZ  TYR A  71     3967   4015   3670    -63   -102   -548       C  
ATOM    573  OH  TYR A  71      13.750  11.473   8.997  1.00 28.86           O  
ANISOU  573  OH  TYR A  71     3705   3806   3453    -27    -42   -542       O  
ATOM    574  N   MET A  72      16.345  17.226   9.064  1.00 27.93           N  
ANISOU  574  N   MET A  72     3776   3402   3435   -146   -345   -672       N  
ATOM    575  CA  MET A  72      15.869  17.977   7.912  1.00 29.90           C  
ANISOU  575  CA  MET A  72     4014   3574   3772   -126   -360   -663       C  
ATOM    576  C   MET A  72      16.417  19.414   7.877  1.00 31.65           C  
ANISOU  576  C   MET A  72     4289   3698   4038   -166   -447   -685       C  
ATOM    577  O   MET A  72      16.532  20.014   6.807  1.00 34.63           O  
ANISOU  577  O   MET A  72     4648   4019   4490   -180   -484   -639       O  
ATOM    578  CB  MET A  72      14.341  17.972   7.873  1.00 30.35           C  
ANISOU  578  CB  MET A  72     4066   3619   3848    -46   -294   -719       C  
ATOM    579  CG  MET A  72      13.752  16.582   7.664  1.00 28.49           C  
ANISOU  579  CG  MET A  72     3772   3468   3587    -18   -219   -681       C  
ATOM    580  SD  MET A  72      11.971  16.593   7.403  1.00 32.43           S  
ANISOU  580  SD  MET A  72     4242   3957   4123     65   -152   -721       S  
ATOM    581  CE  MET A  72      11.748  14.980   6.653  1.00 25.81           C  
ANISOU  581  CE  MET A  72     3334   3198   3276     56   -103   -639       C  
ATOM    582  N   ARG A  73      16.745  19.966   9.042  1.00 25.79           N  
ANISOU  582  N   ARG A  73     3616   2935   3249   -188   -485   -756       N  
ATOM    583  CA  ARG A  73      17.337  21.300   9.107  1.00 28.48           C  
ANISOU  583  CA  ARG A  73     4018   3174   3629   -237   -579   -781       C  
ATOM    584  C   ARG A  73      18.815  21.275   8.742  1.00 28.69           C  
ANISOU  584  C   ARG A  73     4014   3222   3665   -334   -654   -681       C  
ATOM    585  O   ARG A  73      19.307  22.150   8.033  1.00 29.08           O  
ANISOU  585  O   ARG A  73     4065   3198   3785   -381   -723   -639       O  
ATOM    586  CB  ARG A  73      17.197  21.887  10.508  1.00 29.96           C  
ANISOU  586  CB  ARG A  73     4301   3331   3753   -232   -598   -899       C  
ATOM    587  CG  ARG A  73      15.802  22.329  10.866  1.00 33.97           C  
ANISOU  587  CG  ARG A  73     4849   3790   4266   -133   -537  -1007       C  
ATOM    588  CD  ARG A  73      15.827  23.192  12.111  1.00 37.96           C  
ANISOU  588  CD  ARG A  73     5467   4240   4716   -134   -572  -1131       C  
ATOM    589  NE  ARG A  73      16.160  22.409  13.292  1.00 35.95           N  
ANISOU  589  NE  ARG A  73     5230   4093   4336   -157   -549  -1156       N  
ATOM    590  CZ  ARG A  73      15.254  21.848  14.081  1.00 33.81           C  
ANISOU  590  CZ  ARG A  73     4963   3894   3990    -86   -457  -1218       C  
ATOM    591  NH1 ARG A  73      15.636  21.150  15.142  1.00 32.19           N  
ANISOU  591  NH1 ARG A  73     4774   3790   3668   -116   -444  -1228       N  
ATOM    592  NH2 ARG A  73      13.963  21.994  13.806  1.00 32.34           N  
ANISOU  592  NH2 ARG A  73     4760   3683   3845     13   -379  -1263       N  
ATOM    593  N   THR A  74      19.520  20.267   9.242  1.00 26.36           N  
ANISOU  593  N   THR A  74     3684   3029   3301   -365   -639   -637       N  
ATOM    594  CA  THR A  74      20.973  20.205   9.126  1.00 29.01           C  
ANISOU  594  CA  THR A  74     3986   3399   3636   -454   -709   -544       C  
ATOM    595  C   THR A  74      21.456  19.643   7.788  1.00 29.27           C  
ANISOU  595  C   THR A  74     3926   3475   3720   -462   -687   -423       C  
ATOM    596  O   THR A  74      22.466  20.093   7.246  1.00 28.31           O  
ANISOU  596  O   THR A  74     3774   3344   3638   -530   -751   -342       O  
ATOM    597  CB  THR A  74      21.574  19.380  10.283  1.00 30.18           C  
ANISOU  597  CB  THR A  74     4135   3642   3691   -482   -707   -541       C  
ATOM    598  OG1 THR A  74      20.980  18.076  10.301  1.00 31.28           O  
ANISOU  598  OG1 THR A  74     4228   3864   3792   -417   -609   -529       O  
ATOM    599  CG2 THR A  74      21.286  20.061  11.611  1.00 32.03           C  
ANISOU  599  CG2 THR A  74     4470   3838   3861   -491   -742   -659       C  
ATOM    600  N   GLY A  75      20.738  18.660   7.256  1.00 26.64           N  
ANISOU  600  N   GLY A  75     3549   3191   3382   -395   -598   -411       N  
ATOM    601  CA  GLY A  75      21.147  18.032   6.013  1.00 25.46           C  
ANISOU  601  CA  GLY A  75     3322   3087   3266   -394   -569   -310       C  
ATOM    602  C   GLY A  75      21.281  19.019   4.869  1.00 24.13           C  
ANISOU  602  C   GLY A  75     3142   2852   3172   -420   -614   -265       C  
ATOM    603  O   GLY A  75      20.392  19.837   4.639  1.00 20.61           O  
ANISOU  603  O   GLY A  75     2737   2325   2770   -394   -624   -318       O  
ATOM    604  N   GLU A  76      22.389  18.945   4.141  1.00 25.20           N  
ANISOU  604  N   GLU A  76     3219   3028   3327   -470   -640   -159       N  
ATOM    605  CA  GLU A  76      22.548  19.769   2.944  1.00 27.74           C  
ANISOU  605  CA  GLU A  76     3519   3305   3715   -499   -676    -96       C  
ATOM    606  C   GLU A  76      21.934  19.072   1.737  1.00 25.75           C  
ANISOU  606  C   GLU A  76     3225   3090   3468   -442   -601    -64       C  
ATOM    607  O   GLU A  76      21.407  19.716   0.836  1.00 27.24           O  
ANISOU  607  O   GLU A  76     3417   3229   3703   -436   -614    -50       O  
ATOM    608  CB  GLU A  76      24.019  20.086   2.693  1.00 31.50           C  
ANISOU  608  CB  GLU A  76     3946   3815   4208   -583   -737     12       C  
ATOM    609  CG  GLU A  76      24.652  20.939   3.784  1.00 38.66           C  
ANISOU  609  CG  GLU A  76     4900   4673   5116   -658   -833    -13       C  
ATOM    610  CD  GLU A  76      26.139  21.145   3.570  1.00 44.33           C  
ANISOU  610  CD  GLU A  76     5553   5439   5850   -748   -895    108       C  
ATOM    611  OE1 GLU A  76      26.856  20.144   3.362  1.00 42.77           O  
ANISOU  611  OE1 GLU A  76     5277   5350   5623   -739   -848    184       O  
ATOM    612  OE2 GLU A  76      26.587  22.310   3.605  1.00 50.61           O  
ANISOU  612  OE2 GLU A  76     6374   6163   6694   -828   -992    130       O  
ATOM    613  N   GLY A  77      22.000  17.746   1.731  1.00 28.13           N  
ANISOU  613  N   GLY A  77     3491   3476   3720   -403   -528    -52       N  
ATOM    614  CA  GLY A  77      21.417  16.962   0.655  1.00 28.92           C  
ANISOU  614  CA  GLY A  77     3561   3611   3814   -352   -459    -33       C  
ATOM    615  C   GLY A  77      20.718  15.731   1.192  1.00 29.44           C  
ANISOU  615  C   GLY A  77     3637   3715   3835   -293   -388    -90       C  
ATOM    616  O   GLY A  77      21.140  15.163   2.205  1.00 30.51           O  
ANISOU  616  O   GLY A  77     3774   3885   3934   -296   -380   -103       O  
ATOM    617  N   PHE A  78      19.652  15.317   0.513  1.00 21.42           N  
ANISOU  617  N   PHE A  78     2624   2692   2822   -247   -342   -115       N  
ATOM    618  CA  PHE A  78      18.851  14.194   0.983  1.00 22.44           C  
ANISOU  618  CA  PHE A  78     2763   2848   2917   -198   -280   -165       C  
ATOM    619  C   PHE A  78      18.734  13.087  -0.057  1.00 22.62           C  
ANISOU  619  C   PHE A  78     2758   2914   2921   -171   -224   -132       C  
ATOM    620  O   PHE A  78      18.350  13.332  -1.200  1.00 21.07           O  
ANISOU  620  O   PHE A  78     2555   2708   2743   -168   -225   -112       O  
ATOM    621  CB  PHE A  78      17.454  14.674   1.394  1.00 23.90           C  
ANISOU  621  CB  PHE A  78     2982   2979   3119   -167   -278   -244       C  
ATOM    622  CG  PHE A  78      17.469  15.667   2.526  1.00 26.08           C  
ANISOU  622  CG  PHE A  78     3300   3208   3403   -181   -323   -298       C  
ATOM    623  CD1 PHE A  78      17.366  15.239   3.846  1.00 26.15           C  
ANISOU  623  CD1 PHE A  78     3331   3240   3364   -170   -303   -349       C  
ATOM    624  CD2 PHE A  78      17.610  17.022   2.275  1.00 22.40           C  
ANISOU  624  CD2 PHE A  78     2855   2671   2986   -208   -387   -297       C  
ATOM    625  CE1 PHE A  78      17.399  16.148   4.896  1.00 26.63           C  
ANISOU  625  CE1 PHE A  78     3440   3259   3417   -184   -344   -408       C  
ATOM    626  CE2 PHE A  78      17.637  17.943   3.321  1.00 22.04           C  
ANISOU  626  CE2 PHE A  78     2860   2570   2944   -221   -431   -357       C  
ATOM    627  CZ  PHE A  78      17.532  17.505   4.631  1.00 24.47           C  
ANISOU  627  CZ  PHE A  78     3195   2907   3195   -208   -408   -418       C  
ATOM    628  N   LEU A  79      19.068  11.867   0.352  1.00 18.32           N  
ANISOU  628  N   LEU A  79     2203   2416   2341   -151   -179   -126       N  
ATOM    629  CA  LEU A  79      18.870  10.697  -0.484  1.00 21.73           C  
ANISOU  629  CA  LEU A  79     2625   2877   2754   -120   -124   -112       C  
ATOM    630  C   LEU A  79      17.512  10.115  -0.126  1.00 24.15           C  
ANISOU  630  C   LEU A  79     2956   3165   3055    -92    -96   -173       C  
ATOM    631  O   LEU A  79      17.323   9.587   0.975  1.00 23.55           O  
ANISOU  631  O   LEU A  79     2888   3097   2962    -82    -80   -199       O  
ATOM    632  CB  LEU A  79      19.984   9.674  -0.236  1.00 23.48           C  
ANISOU  632  CB  LEU A  79     2822   3150   2951   -108    -92    -69       C  
ATOM    633  CG  LEU A  79      20.506   8.851  -1.414  1.00 23.33           C  
ANISOU  633  CG  LEU A  79     2784   3164   2916    -83    -47    -28       C  
ATOM    634  CD1 LEU A  79      21.291   9.716  -2.407  1.00 19.19           C  
ANISOU  634  CD1 LEU A  79     2230   2661   2401   -108    -69     31       C  
ATOM    635  CD2 LEU A  79      21.368   7.697  -0.900  1.00 24.70           C  
ANISOU  635  CD2 LEU A  79     2938   3373   3073    -54     -9      1       C  
ATOM    636  N   CYS A  80      16.564  10.226  -1.053  1.00 21.48           N  
ANISOU  636  N   CYS A  80     2624   2807   2731    -84    -94   -187       N  
ATOM    637  CA  CYS A  80      15.186   9.834  -0.788  1.00 19.45           C  
ANISOU  637  CA  CYS A  80     2379   2533   2479    -65    -75   -234       C  
ATOM    638  C   CYS A  80      14.895   8.440  -1.313  1.00 23.65           C  
ANISOU  638  C   CYS A  80     2915   3082   2987    -51    -34   -231       C  
ATOM    639  O   CYS A  80      14.609   8.259  -2.497  1.00 20.09           O  
ANISOU  639  O   CYS A  80     2469   2631   2533    -53    -34   -221       O  
ATOM    640  CB  CYS A  80      14.232  10.853  -1.394  1.00 19.26           C  
ANISOU  640  CB  CYS A  80     2353   2472   2491    -66   -107   -248       C  
ATOM    641  SG  CYS A  80      14.407  12.506  -0.658  1.00 29.63           S  
ANISOU  641  SG  CYS A  80     3676   3740   3843    -76   -159   -266       S  
ATOM    642  N   VAL A  81      14.952   7.464  -0.407  1.00 24.20           N  
ANISOU  642  N   VAL A  81     2990   3166   3039    -40     -3   -240       N  
ATOM    643  CA  VAL A  81      14.926   6.054  -0.772  1.00 22.15           C  
ANISOU  643  CA  VAL A  81     2742   2912   2762    -28     33   -234       C  
ATOM    644  C   VAL A  81      13.540   5.405  -0.662  1.00 23.57           C  
ANISOU  644  C   VAL A  81     2930   3077   2949    -30     44   -262       C  
ATOM    645  O   VAL A  81      12.860   5.506   0.365  1.00 19.22           O  
ANISOU  645  O   VAL A  81     2369   2530   2404    -30     48   -281       O  
ATOM    646  CB  VAL A  81      15.922   5.250   0.095  1.00 17.27           C  
ANISOU  646  CB  VAL A  81     2120   2314   2127    -16     56   -209       C  
ATOM    647  CG1 VAL A  81      16.041   3.828  -0.421  1.00 16.92           C  
ANISOU  647  CG1 VAL A  81     2094   2261   2074      4     92   -201       C  
ATOM    648  CG2 VAL A  81      17.293   5.932   0.107  1.00 12.36           C  
ANISOU  648  CG2 VAL A  81     1478   1716   1503    -20     39   -171       C  
ATOM    649  N   PHE A  82      13.125   4.741  -1.734  1.00 20.01           N  
ANISOU  649  N   PHE A  82     2497   2614   2494    -34     49   -265       N  
ATOM    650  CA  PHE A  82      11.968   3.869  -1.665  1.00 19.28           C  
ANISOU  650  CA  PHE A  82     2412   2507   2408    -46     56   -281       C  
ATOM    651  C   PHE A  82      12.389   2.490  -2.155  1.00 19.90           C  
ANISOU  651  C   PHE A  82     2527   2568   2469    -41     79   -277       C  
ATOM    652  O   PHE A  82      13.462   2.340  -2.740  1.00 21.90           O  
ANISOU  652  O   PHE A  82     2795   2824   2702    -21     92   -266       O  
ATOM    653  CB  PHE A  82      10.784   4.440  -2.468  1.00 19.02           C  
ANISOU  653  CB  PHE A  82     2369   2467   2393    -65     25   -292       C  
ATOM    654  CG  PHE A  82      10.977   4.414  -3.969  1.00 14.87           C  
ANISOU  654  CG  PHE A  82     1867   1936   1846    -75      8   -287       C  
ATOM    655  CD1 PHE A  82      10.528   3.335  -4.726  1.00 15.96           C  
ANISOU  655  CD1 PHE A  82     2039   2059   1967    -93      7   -299       C  
ATOM    656  CD2 PHE A  82      11.581   5.477  -4.625  1.00 13.95           C  
ANISOU  656  CD2 PHE A  82     1743   1832   1726    -72    -11   -271       C  
ATOM    657  CE1 PHE A  82      10.696   3.311  -6.118  1.00 16.39           C  
ANISOU  657  CE1 PHE A  82     2124   2116   1988   -103     -8   -300       C  
ATOM    658  CE2 PHE A  82      11.748   5.463  -6.016  1.00 16.94           C  
ANISOU  658  CE2 PHE A  82     2143   2218   2074    -83    -24   -261       C  
ATOM    659  CZ  PHE A  82      11.306   4.375  -6.762  1.00 12.87           C  
ANISOU  659  CZ  PHE A  82     1667   1694   1530    -97    -21   -279       C  
ATOM    660  N   ALA A  83      11.571   1.477  -1.902  1.00 16.72           N  
ANISOU  660  N   ALA A  83     2136   2143   2073    -57     85   -284       N  
ATOM    661  CA  ALA A  83      11.858   0.161  -2.451  1.00 16.33           C  
ANISOU  661  CA  ALA A  83     2133   2058   2013    -53    100   -288       C  
ATOM    662  C   ALA A  83      10.911  -0.074  -3.615  1.00 18.57           C  
ANISOU  662  C   ALA A  83     2444   2320   2291    -85     72   -312       C  
ATOM    663  O   ALA A  83       9.727   0.248  -3.524  1.00 18.55           O  
ANISOU  663  O   ALA A  83     2415   2325   2307   -118     45   -312       O  
ATOM    664  CB  ALA A  83      11.701  -0.918  -1.392  1.00 16.37           C  
ANISOU  664  CB  ALA A  83     2141   2043   2034    -56    118   -272       C  
ATOM    665  N   ILE A  84      11.432  -0.614  -4.715  1.00 14.94           N  
ANISOU  665  N   ILE A  84     2035   1840   1801    -75     78   -330       N  
ATOM    666  CA  ILE A  84      10.624  -0.796  -5.920  1.00 19.02           C  
ANISOU  666  CA  ILE A  84     2587   2342   2297   -110     44   -355       C  
ATOM    667  C   ILE A  84       9.502  -1.812  -5.746  1.00 20.99           C  
ANISOU  667  C   ILE A  84     2858   2550   2569   -156     20   -365       C  
ATOM    668  O   ILE A  84       8.613  -1.909  -6.594  1.00 22.83           O  
ANISOU  668  O   ILE A  84     3110   2773   2791   -200    -22   -379       O  
ATOM    669  CB  ILE A  84      11.475  -1.211  -7.128  1.00 22.45           C  
ANISOU  669  CB  ILE A  84     3082   2767   2680    -86     62   -381       C  
ATOM    670  CG1 ILE A  84      12.126  -2.573  -6.865  1.00 25.70           C  
ANISOU  670  CG1 ILE A  84     3545   3127   3094    -53    100   -397       C  
ATOM    671  CG2 ILE A  84      12.501  -0.136  -7.441  1.00 20.76           C  
ANISOU  671  CG2 ILE A  84     2838   2605   2445    -52     80   -359       C  
ATOM    672  CD1 ILE A  84      12.623  -3.271  -8.108  1.00 28.46           C  
ANISOU  672  CD1 ILE A  84     3972   3451   3391    -30    118   -440       C  
ATOM    673  N   ASN A  85       9.544  -2.569  -4.653  1.00 23.06           N  
ANISOU  673  N   ASN A  85     3113   2787   2860   -151     41   -349       N  
ATOM    674  CA  ASN A  85       8.482  -3.525  -4.336  1.00 21.17           C  
ANISOU  674  CA  ASN A  85     2884   2510   2650   -202     17   -342       C  
ATOM    675  C   ASN A  85       7.676  -3.056  -3.127  1.00 23.62           C  
ANISOU  675  C   ASN A  85     3117   2861   2995   -220     17   -304       C  
ATOM    676  O   ASN A  85       7.082  -3.859  -2.408  1.00 29.12           O  
ANISOU  676  O   ASN A  85     3805   3539   3719   -251     15   -279       O  
ATOM    677  CB  ASN A  85       9.075  -4.908  -4.061  1.00 20.69           C  
ANISOU  677  CB  ASN A  85     2881   2383   2598   -186     39   -346       C  
ATOM    678  CG  ASN A  85       9.850  -4.961  -2.755  1.00 26.35           C  
ANISOU  678  CG  ASN A  85     3562   3116   3334   -146     80   -308       C  
ATOM    679  OD1 ASN A  85      10.396  -3.956  -2.300  1.00 27.57           O  
ANISOU  679  OD1 ASN A  85     3669   3327   3478   -114     98   -294       O  
ATOM    680  ND2 ASN A  85       9.894  -6.138  -2.140  1.00 31.38           N  
ANISOU  680  ND2 ASN A  85     4225   3701   3999   -151     87   -287       N  
ATOM    681  N   ASN A  86       7.679  -1.749  -2.901  1.00 19.66           N  
ANISOU  681  N   ASN A  86     2563   2415   2492   -199     21   -299       N  
ATOM    682  CA  ASN A  86       6.988  -1.155  -1.770  1.00 18.21           C  
ANISOU  682  CA  ASN A  86     2311   2275   2333   -201     31   -274       C  
ATOM    683  C   ASN A  86       6.336   0.150  -2.207  1.00 18.22           C  
ANISOU  683  C   ASN A  86     2267   2312   2343   -200      7   -280       C  
ATOM    684  O   ASN A  86       6.946   1.220  -2.129  1.00 14.60           O  
ANISOU  684  O   ASN A  86     1796   1874   1877   -164     16   -288       O  
ATOM    685  CB  ASN A  86       7.961  -0.906  -0.609  1.00 17.79           C  
ANISOU  685  CB  ASN A  86     2246   2245   2270   -159     71   -264       C  
ATOM    686  CG  ASN A  86       7.253  -0.457   0.661  1.00 20.21           C  
ANISOU  686  CG  ASN A  86     2493   2598   2588   -160     88   -245       C  
ATOM    687  OD1 ASN A  86       6.155   0.087   0.610  1.00 21.20           O  
ANISOU  687  OD1 ASN A  86     2575   2749   2732   -174     76   -244       O  
ATOM    688  ND2 ASN A  86       7.890  -0.668   1.806  1.00 21.35           N  
ANISOU  688  ND2 ASN A  86     2634   2761   2718   -141    118   -228       N  
ATOM    689  N   THR A  87       5.091   0.047  -2.666  1.00 17.83           N  
ANISOU  689  N   THR A  87     2193   2267   2316   -243    -27   -269       N  
ATOM    690  CA  THR A  87       4.328   1.190  -3.160  1.00 18.14           C  
ANISOU  690  CA  THR A  87     2184   2336   2373   -242    -56   -264       C  
ATOM    691  C   THR A  87       4.181   2.285  -2.114  1.00 21.83           C  
ANISOU  691  C   THR A  87     2592   2840   2861   -198    -26   -260       C  
ATOM    692  O   THR A  87       4.359   3.471  -2.415  1.00 22.69           O  
ANISOU  692  O   THR A  87     2687   2957   2976   -169    -36   -269       O  
ATOM    693  CB  THR A  87       2.931   0.748  -3.636  1.00 18.89           C  
ANISOU  693  CB  THR A  87     2248   2435   2495   -300    -99   -239       C  
ATOM    694  OG1 THR A  87       3.077  -0.156  -4.736  1.00 17.25           O  
ANISOU  694  OG1 THR A  87     2108   2185   2259   -344   -136   -254       O  
ATOM    695  CG2 THR A  87       2.084   1.946  -4.074  1.00 21.22           C  
ANISOU  695  CG2 THR A  87     2479   2764   2818   -293   -129   -223       C  
ATOM    696  N   LYS A  88       3.855   1.890  -0.885  1.00 21.33           N  
ANISOU  696  N   LYS A  88     2500   2800   2806   -194     10   -247       N  
ATOM    697  CA  LYS A  88       3.698   2.854   0.198  1.00 22.88           C  
ANISOU  697  CA  LYS A  88     2649   3034   3009   -150     45   -254       C  
ATOM    698  C   LYS A  88       4.975   3.679   0.394  1.00 20.86           C  
ANISOU  698  C   LYS A  88     2429   2768   2729   -108     55   -284       C  
ATOM    699  O   LYS A  88       4.905   4.898   0.567  1.00 22.20           O  
ANISOU  699  O   LYS A  88     2578   2945   2912    -73     55   -302       O  
ATOM    700  CB  LYS A  88       3.288   2.148   1.494  1.00 27.52           C  
ANISOU  700  CB  LYS A  88     3208   3656   3591   -156     87   -232       C  
ATOM    701  CG  LYS A  88       3.358   3.002   2.762  1.00 28.29           C  
ANISOU  701  CG  LYS A  88     3278   3798   3673   -107    132   -251       C  
ATOM    702  CD  LYS A  88       2.159   3.915   2.908  1.00 36.43           C  
ANISOU  702  CD  LYS A  88     4240   4864   4737    -79    143   -252       C  
ATOM    703  CE  LYS A  88       1.976   4.339   4.365  1.00 38.59           C  
ANISOU  703  CE  LYS A  88     4485   5191   4984    -37    201   -268       C  
ATOM    704  NZ  LYS A  88       3.252   4.824   4.968  1.00 40.86           N  
ANISOU  704  NZ  LYS A  88     4832   5466   5228     -9    211   -309       N  
ATOM    705  N   SER A  89       6.136   3.026   0.351  1.00 17.98           N  
ANISOU  705  N   SER A  89     2116   2382   2335   -112     62   -286       N  
ATOM    706  CA  SER A  89       7.403   3.737   0.519  1.00 17.17           C  
ANISOU  706  CA  SER A  89     2039   2275   2211    -81     66   -302       C  
ATOM    707  C   SER A  89       7.622   4.761  -0.594  1.00 17.96           C  
ANISOU  707  C   SER A  89     2145   2358   2322    -74     32   -310       C  
ATOM    708  O   SER A  89       8.232   5.804  -0.371  1.00 20.02           O  
ANISOU  708  O   SER A  89     2406   2618   2584    -52     26   -321       O  
ATOM    709  CB  SER A  89       8.584   2.765   0.589  1.00 15.11           C  
ANISOU  709  CB  SER A  89     1820   1998   1922    -83     80   -291       C  
ATOM    710  OG  SER A  89       8.875   2.214  -0.681  1.00 15.95           O  
ANISOU  710  OG  SER A  89     1963   2074   2025    -96     63   -291       O  
ATOM    711  N   PHE A  90       7.118   4.460  -1.789  1.00 18.60           N  
ANISOU  711  N   PHE A  90     2232   2425   2410   -100      3   -302       N  
ATOM    712  CA  PHE A  90       7.215   5.380  -2.923  1.00 15.99           C  
ANISOU  712  CA  PHE A  90     1904   2086   2085   -100    -34   -298       C  
ATOM    713  C   PHE A  90       6.304   6.573  -2.686  1.00 15.43           C  
ANISOU  713  C   PHE A  90     1784   2021   2058    -82    -50   -298       C  
ATOM    714  O   PHE A  90       6.687   7.719  -2.906  1.00 18.18           O  
ANISOU  714  O   PHE A  90     2130   2357   2420    -63    -69   -298       O  
ATOM    715  CB  PHE A  90       6.830   4.659  -4.225  1.00 19.59           C  
ANISOU  715  CB  PHE A  90     2384   2533   2525   -137    -63   -290       C  
ATOM    716  CG  PHE A  90       6.745   5.567  -5.436  1.00 20.98           C  
ANISOU  716  CG  PHE A  90     2559   2712   2702   -145   -106   -276       C  
ATOM    717  CD1 PHE A  90       7.891   6.099  -6.004  1.00 19.39           C  
ANISOU  717  CD1 PHE A  90     2384   2511   2474   -133   -107   -270       C  
ATOM    718  CD2 PHE A  90       5.518   5.874  -6.010  1.00 19.45           C  
ANISOU  718  CD2 PHE A  90     2330   2525   2535   -168   -147   -258       C  
ATOM    719  CE1 PHE A  90       7.820   6.920  -7.115  1.00 19.38           C  
ANISOU  719  CE1 PHE A  90     2378   2516   2469   -145   -147   -246       C  
ATOM    720  CE2 PHE A  90       5.437   6.705  -7.127  1.00 18.68           C  
ANISOU  720  CE2 PHE A  90     2229   2432   2437   -177   -192   -234       C  
ATOM    721  CZ  PHE A  90       6.588   7.226  -7.678  1.00 21.34           C  
ANISOU  721  CZ  PHE A  90     2597   2767   2742   -167   -192   -229       C  
ATOM    722  N   GLU A  91       5.089   6.297  -2.235  1.00 15.94           N  
ANISOU  722  N   GLU A  91     1806   2103   2148    -86    -42   -292       N  
ATOM    723  CA  GLU A  91       4.137   7.354  -1.914  1.00 20.75           C  
ANISOU  723  CA  GLU A  91     2360   2720   2804    -55    -47   -292       C  
ATOM    724  C   GLU A  91       4.640   8.253  -0.778  1.00 22.20           C  
ANISOU  724  C   GLU A  91     2547   2900   2989     -8    -17   -325       C  
ATOM    725  O   GLU A  91       4.311   9.438  -0.723  1.00 21.86           O  
ANISOU  725  O   GLU A  91     2482   2840   2982     28    -28   -336       O  
ATOM    726  CB  GLU A  91       2.774   6.740  -1.572  1.00 21.08           C  
ANISOU  726  CB  GLU A  91     2345   2793   2869    -69    -35   -272       C  
ATOM    727  CG  GLU A  91       2.174   5.950  -2.730  1.00 20.81           C  
ANISOU  727  CG  GLU A  91     2311   2759   2838   -126    -80   -241       C  
ATOM    728  CD  GLU A  91       0.968   5.125  -2.336  1.00 24.32           C  
ANISOU  728  CD  GLU A  91     2702   3236   3305   -156    -72   -212       C  
ATOM    729  OE1 GLU A  91       0.795   4.830  -1.132  1.00 26.42           O  
ANISOU  729  OE1 GLU A  91     2944   3527   3569   -139    -22   -215       O  
ATOM    730  OE2 GLU A  91       0.191   4.770  -3.243  1.00 22.17           O  
ANISOU  730  OE2 GLU A  91     2410   2967   3047   -203   -120   -182       O  
ATOM    731  N   ASP A  92       5.444   7.689   0.121  1.00 21.38           N  
ANISOU  731  N   ASP A  92     2473   2806   2844     -8     17   -341       N  
ATOM    732  CA  ASP A  92       6.000   8.448   1.244  1.00 20.71           C  
ANISOU  732  CA  ASP A  92     2401   2721   2746     26     39   -375       C  
ATOM    733  C   ASP A  92       6.971   9.539   0.789  1.00 23.88           C  
ANISOU  733  C   ASP A  92     2834   3084   3157     34      3   -384       C  
ATOM    734  O   ASP A  92       7.188  10.524   1.491  1.00 26.33           O  
ANISOU  734  O   ASP A  92     3154   3377   3473     61      2   -416       O  
ATOM    735  CB  ASP A  92       6.730   7.516   2.213  1.00 22.55           C  
ANISOU  735  CB  ASP A  92     2659   2979   2930     15     72   -376       C  
ATOM    736  CG  ASP A  92       5.789   6.789   3.154  1.00 28.97           C  
ANISOU  736  CG  ASP A  92     3438   3836   3733     16    115   -371       C  
ATOM    737  OD1 ASP A  92       4.593   7.139   3.194  1.00 32.08           O  
ANISOU  737  OD1 ASP A  92     3784   4246   4158     34    125   -372       O  
ATOM    738  OD2 ASP A  92       6.252   5.876   3.867  1.00 33.30           O  
ANISOU  738  OD2 ASP A  92     4002   4407   4244      0    138   -358       O  
ATOM    739  N   ILE A  93       7.572   9.349  -0.379  1.00 22.33           N  
ANISOU  739  N   ILE A  93     2656   2873   2956      5    -28   -355       N  
ATOM    740  CA  ILE A  93       8.560  10.292  -0.883  1.00 22.37           C  
ANISOU  740  CA  ILE A  93     2684   2850   2967      2    -63   -347       C  
ATOM    741  C   ILE A  93       7.994  11.713  -0.931  1.00 26.14           C  
ANISOU  741  C   ILE A  93     3145   3289   3497     29    -92   -359       C  
ATOM    742  O   ILE A  93       8.637  12.666  -0.504  1.00 27.78           O  
ANISOU  742  O   ILE A  93     3374   3465   3715     38   -109   -375       O  
ATOM    743  CB  ILE A  93       9.065   9.880  -2.280  1.00 24.76           C  
ANISOU  743  CB  ILE A  93     2999   3154   3253    -28    -85   -309       C  
ATOM    744  CG1 ILE A  93       9.734   8.501  -2.220  1.00 20.66           C  
ANISOU  744  CG1 ILE A  93     2504   2659   2688    -43    -53   -304       C  
ATOM    745  CG2 ILE A  93      10.045  10.921  -2.818  1.00 24.90           C  
ANISOU  745  CG2 ILE A  93     3031   3151   3279    -36   -120   -287       C  
ATOM    746  CD1 ILE A  93      10.941   8.456  -1.279  1.00 18.05           C  
ANISOU  746  CD1 ILE A  93     2188   2336   2333    -36    -35   -308       C  
ATOM    747  N   HIS A  94       6.780  11.852  -1.443  1.00 29.69           N  
ANISOU  747  N   HIS A  94     3558   3737   3984     40   -101   -347       N  
ATOM    748  CA  HIS A  94       6.147  13.162  -1.498  1.00 31.35           C  
ANISOU  748  CA  HIS A  94     3749   3907   4256     76   -127   -354       C  
ATOM    749  C   HIS A  94       6.124  13.841  -0.129  1.00 31.02           C  
ANISOU  749  C   HIS A  94     3719   3846   4221    122    -99   -411       C  
ATOM    750  O   HIS A  94       6.423  15.032  -0.005  1.00 29.93           O  
ANISOU  750  O   HIS A  94     3602   3652   4117    142   -127   -430       O  
ATOM    751  CB  HIS A  94       4.724  13.062  -2.044  1.00 32.96           C  
ANISOU  751  CB  HIS A  94     3896   4125   4500     88   -133   -329       C  
ATOM    752  CG  HIS A  94       4.034  14.386  -2.130  1.00 42.59           C  
ANISOU  752  CG  HIS A  94     5089   5299   5793    136   -158   -329       C  
ATOM    753  ND1 HIS A  94       4.436  15.373  -3.007  1.00 46.99           N  
ANISOU  753  ND1 HIS A  94     5661   5808   6386    128   -215   -297       N  
ATOM    754  CD2 HIS A  94       3.004  14.903  -1.424  1.00 45.60           C  
ANISOU  754  CD2 HIS A  94     5430   5675   6221    196   -131   -354       C  
ATOM    755  CE1 HIS A  94       3.671  16.438  -2.844  1.00 46.96           C  
ANISOU  755  CE1 HIS A  94     5629   5759   6454    182   -227   -303       C  
ATOM    756  NE2 HIS A  94       2.793  16.179  -1.891  1.00 49.50           N  
ANISOU  756  NE2 HIS A  94     5917   6107   6783    229   -174   -341       N  
ATOM    757  N   HIS A  95       5.774  13.076   0.898  1.00 29.48           N  
ANISOU  757  N   HIS A  95     3515   3695   3991    134    -46   -440       N  
ATOM    758  CA  HIS A  95       5.673  13.609   2.250  1.00 31.42           C  
ANISOU  758  CA  HIS A  95     3775   3938   4226    178    -11   -500       C  
ATOM    759  C   HIS A  95       7.031  14.004   2.829  1.00 32.12           C  
ANISOU  759  C   HIS A  95     3926   4002   4278    159    -30   -527       C  
ATOM    760  O   HIS A  95       7.129  14.989   3.556  1.00 31.59           O  
ANISOU  760  O   HIS A  95     3888   3896   4217    190    -34   -579       O  
ATOM    761  CB  HIS A  95       4.961  12.611   3.163  1.00 36.69           C  
ANISOU  761  CB  HIS A  95     4413   4674   4856    189     51   -509       C  
ATOM    762  CG  HIS A  95       3.640  12.150   2.628  1.00 44.53           C  
ANISOU  762  CG  HIS A  95     5337   5696   5885    195     64   -472       C  
ATOM    763  ND1 HIS A  95       2.499  12.922   2.696  1.00 47.95           N  
ANISOU  763  ND1 HIS A  95     5721   6123   6374    252     77   -482       N  
ATOM    764  CD2 HIS A  95       3.284  11.006   1.998  1.00 42.97           C  
ANISOU  764  CD2 HIS A  95     5111   5533   5681    150     61   -423       C  
ATOM    765  CE1 HIS A  95       1.495  12.269   2.139  1.00 47.50           C  
ANISOU  765  CE1 HIS A  95     5600   6104   6343    237     79   -432       C  
ATOM    766  NE2 HIS A  95       1.944  11.103   1.707  1.00 44.36           N  
ANISOU  766  NE2 HIS A  95     5219   5728   5907    171     66   -399       N  
ATOM    767  N   TYR A  96       8.075  13.242   2.518  1.00 32.86           N  
ANISOU  767  N   TYR A  96     4037   4117   4332    109    -41   -493       N  
ATOM    768  CA  TYR A  96       9.416  13.618   2.955  1.00 29.52           C  
ANISOU  768  CA  TYR A  96     3659   3677   3880     84    -68   -503       C  
ATOM    769  C   TYR A  96       9.846  14.922   2.296  1.00 25.87           C  
ANISOU  769  C   TYR A  96     3216   3146   3468     77   -127   -495       C  
ATOM    770  O   TYR A  96      10.394  15.803   2.958  1.00 24.09           O  
ANISOU  770  O   TYR A  96     3029   2880   3243     77   -153   -531       O  
ATOM    771  CB  TYR A  96      10.444  12.528   2.641  1.00 30.14           C  
ANISOU  771  CB  TYR A  96     3741   3794   3916     40    -65   -456       C  
ATOM    772  CG  TYR A  96      10.376  11.333   3.558  1.00 29.36           C  
ANISOU  772  CG  TYR A  96     3638   3751   3765     39    -17   -461       C  
ATOM    773  CD1 TYR A  96      10.742  11.433   4.898  1.00 29.69           C  
ANISOU  773  CD1 TYR A  96     3703   3813   3763     43     -4   -495       C  
ATOM    774  CD2 TYR A  96       9.964  10.100   3.081  1.00 24.88           C  
ANISOU  774  CD2 TYR A  96     3048   3214   3192     30      9   -428       C  
ATOM    775  CE1 TYR A  96      10.678  10.334   5.737  1.00 25.85           C  
ANISOU  775  CE1 TYR A  96     3211   3382   3228     39     37   -487       C  
ATOM    776  CE2 TYR A  96       9.905   9.004   3.903  1.00 26.28           C  
ANISOU  776  CE2 TYR A  96     3221   3434   3329     25     48   -422       C  
ATOM    777  CZ  TYR A  96      10.255   9.126   5.230  1.00 25.35           C  
ANISOU  777  CZ  TYR A  96     3120   3342   3169     31     63   -447       C  
ATOM    778  OH  TYR A  96      10.179   8.022   6.039  1.00 24.62           O  
ANISOU  778  OH  TYR A  96     3022   3296   3036     23     99   -430       O  
ATOM    779  N   ARG A  97       9.607  15.042   0.991  1.00 26.35           N  
ANISOU  779  N   ARG A  97     3252   3191   3568     67   -153   -446       N  
ATOM    780  CA  ARG A  97      10.030  16.244   0.276  1.00 33.58           C  
ANISOU  780  CA  ARG A  97     4182   4044   4534     53   -214   -422       C  
ATOM    781  C   ARG A  97       9.310  17.488   0.794  1.00 32.25           C  
ANISOU  781  C   ARG A  97     4027   3806   4422    101   -229   -473       C  
ATOM    782  O   ARG A  97       9.918  18.553   0.924  1.00 31.44           O  
ANISOU  782  O   ARG A  97     3960   3636   4348     90   -277   -483       O  
ATOM    783  CB  ARG A  97       9.861  16.109  -1.241  1.00 36.37           C  
ANISOU  783  CB  ARG A  97     4505   4405   4908     31   -238   -354       C  
ATOM    784  CG  ARG A  97      10.237  17.389  -1.977  1.00 41.66           C  
ANISOU  784  CG  ARG A  97     5185   5012   5633     15   -303   -317       C  
ATOM    785  CD  ARG A  97      10.552  17.165  -3.449  1.00 45.95           C  
ANISOU  785  CD  ARG A  97     5709   5583   6168    -25   -328   -238       C  
ATOM    786  NE  ARG A  97      10.832  18.428  -4.136  1.00 49.48           N  
ANISOU  786  NE  ARG A  97     6159   5970   6669    -43   -391   -191       N  
ATOM    787  CZ  ARG A  97      12.047  18.942  -4.318  1.00 50.02           C  
ANISOU  787  CZ  ARG A  97     6244   6025   6735    -88   -426   -151       C  
ATOM    788  NH1 ARG A  97      13.123  18.305  -3.877  1.00 49.30           N  
ANISOU  788  NH1 ARG A  97     6162   5979   6589   -115   -403   -153       N  
ATOM    789  NH2 ARG A  97      12.188  20.096  -4.954  1.00 53.71           N  
ANISOU  789  NH2 ARG A  97     6713   6434   7259   -109   -488   -100       N  
ATOM    790  N   GLU A  98       8.022  17.335   1.101  1.00 31.83           N  
ANISOU  790  N   GLU A  98     3943   3765   4385    155   -188   -502       N  
ATOM    791  CA  GLU A  98       7.201  18.423   1.619  1.00 35.94           C  
ANISOU  791  CA  GLU A  98     4470   4224   4961    219   -187   -555       C  
ATOM    792  C   GLU A  98       7.661  18.886   2.991  1.00 32.07           C  
ANISOU  792  C   GLU A  98     4039   3710   4436    237   -174   -636       C  
ATOM    793  O   GLU A  98       7.811  20.081   3.219  1.00 27.09           O  
ANISOU  793  O   GLU A  98     3452   2994   3849    257   -212   -675       O  
ATOM    794  CB  GLU A  98       5.729  18.010   1.695  1.00 44.15           C  
ANISOU  794  CB  GLU A  98     5450   5304   6022    275   -136   -560       C  
ATOM    795  CG  GLU A  98       5.050  17.934   0.350  1.00 53.33           C  
ANISOU  795  CG  GLU A  98     6557   6470   7236    267   -165   -487       C  
ATOM    796  CD  GLU A  98       5.061  19.265  -0.369  1.00 63.74           C  
ANISOU  796  CD  GLU A  98     7885   7699   8634    281   -228   -463       C  
ATOM    797  OE1 GLU A  98       5.239  19.275  -1.606  1.00 67.57           O  
ANISOU  797  OE1 GLU A  98     8353   8183   9138    239   -277   -390       O  
ATOM    798  OE2 GLU A  98       4.891  20.302   0.307  1.00 66.71           O  
ANISOU  798  OE2 GLU A  98     8290   8005   9054    335   -230   -518       O  
ATOM    799  N   GLN A  99       7.865  17.940   3.904  1.00 31.61           N  
ANISOU  799  N   GLN A  99     3986   3724   4300    227   -126   -662       N  
ATOM    800  CA  GLN A  99       8.307  18.272   5.252  1.00 33.31           C  
ANISOU  800  CA  GLN A  99     4259   3932   4463    237   -114   -738       C  
ATOM    801  C   GLN A  99       9.687  18.918   5.236  1.00 34.00           C  
ANISOU  801  C   GLN A  99     4404   3966   4547    177   -186   -734       C  
ATOM    802  O   GLN A  99       9.966  19.812   6.035  1.00 35.23           O  
ANISOU  802  O   GLN A  99     4622   4067   4697    187   -210   -801       O  
ATOM    803  CB  GLN A  99       8.303  17.036   6.158  1.00 35.57           C  
ANISOU  803  CB  GLN A  99     4535   4318   4663    228    -53   -747       C  
ATOM    804  CG  GLN A  99       7.104  16.951   7.099  1.00 46.20           C  
ANISOU  804  CG  GLN A  99     5864   5703   5988    298     20   -804       C  
ATOM    805  CD  GLN A  99       7.006  18.138   8.061  1.00 57.69           C  
ANISOU  805  CD  GLN A  99     7382   7102   7436    349     22   -902       C  
ATOM    806  OE1 GLN A  99       6.101  18.969   7.952  1.00 61.88           O  
ANISOU  806  OE1 GLN A  99     7904   7582   8026    419     36   -939       O  
ATOM    807  NE2 GLN A  99       7.931  18.210   9.016  1.00 60.50           N  
ANISOU  807  NE2 GLN A  99     7804   7466   7717    315      5   -946       N  
ATOM    808  N   ILE A 100      10.546  18.466   4.324  1.00 32.58           N  
ANISOU  808  N   ILE A 100     4204   3806   4369    116   -220   -654       N  
ATOM    809  CA  ILE A 100      11.886  19.031   4.203  1.00 33.05           C  
ANISOU  809  CA  ILE A 100     4299   3828   4430     53   -288   -629       C  
ATOM    810  C   ILE A 100      11.795  20.481   3.735  1.00 34.49           C  
ANISOU  810  C   ILE A 100     4510   3900   4695     59   -351   -636       C  
ATOM    811  O   ILE A 100      12.431  21.368   4.308  1.00 34.63           O  
ANISOU  811  O   ILE A 100     4586   3854   4718     35   -402   -674       O  
ATOM    812  CB  ILE A 100      12.775  18.206   3.245  1.00 29.71           C  
ANISOU  812  CB  ILE A 100     3837   3459   3991     -4   -299   -536       C  
ATOM    813  CG1 ILE A 100      13.149  16.869   3.890  1.00 28.72           C  
ANISOU  813  CG1 ILE A 100     3698   3424   3789    -16   -250   -531       C  
ATOM    814  CG2 ILE A 100      14.028  18.965   2.897  1.00 25.89           C  
ANISOU  814  CG2 ILE A 100     3373   2935   3530    -67   -372   -492       C  
ATOM    815  CD1 ILE A 100      13.688  15.830   2.911  1.00 23.72           C  
ANISOU  815  CD1 ILE A 100     3022   2847   3142    -45   -237   -451       C  
ATOM    816  N   LYS A 101      10.979  20.718   2.710  1.00 33.52           N  
ANISOU  816  N   LYS A 101     4349   3752   4636     89   -352   -598       N  
ATOM    817  CA  LYS A 101      10.752  22.065   2.192  1.00 37.70           C  
ANISOU  817  CA  LYS A 101     4897   4172   5254    103   -410   -594       C  
ATOM    818  C   LYS A 101      10.108  22.996   3.224  1.00 39.90           C  
ANISOU  818  C   LYS A 101     5231   4371   5560    169   -404   -697       C  
ATOM    819  O   LYS A 101      10.387  24.195   3.251  1.00 39.71           O  
ANISOU  819  O   LYS A 101     5258   4237   5594    164   -466   -718       O  
ATOM    820  CB  LYS A 101       9.905  22.010   0.918  1.00 41.25           C  
ANISOU  820  CB  LYS A 101     5287   4626   5761    125   -410   -526       C  
ATOM    821  CG  LYS A 101      10.699  21.673  -0.335  1.00 43.25           C  
ANISOU  821  CG  LYS A 101     5509   4916   6008     54   -445   -422       C  
ATOM    822  CD  LYS A 101       9.783  21.270  -1.477  1.00 45.56           C  
ANISOU  822  CD  LYS A 101     5743   5244   6323     72   -432   -363       C  
ATOM    823  CE  LYS A 101       8.693  22.303  -1.696  1.00 48.70           C  
ANISOU  823  CE  LYS A 101     6132   5561   6813    132   -456   -371       C  
ATOM    824  NZ  LYS A 101       7.665  21.813  -2.653  1.00 50.62           N  
ANISOU  824  NZ  LYS A 101     6311   5851   7071    151   -443   -318       N  
ATOM    825  N   ARG A 102       9.239  22.444   4.064  1.00 42.65           N  
ANISOU  825  N   ARG A 102     5568   4771   5866    233   -327   -762       N  
ATOM    826  CA  ARG A 102       8.632  23.211   5.147  1.00 45.87           C  
ANISOU  826  CA  ARG A 102     6028   5121   6279    306   -303   -872       C  
ATOM    827  C   ARG A 102       9.730  23.658   6.100  1.00 43.39           C  
ANISOU  827  C   ARG A 102     5803   4770   5914    257   -347   -932       C  
ATOM    828  O   ARG A 102       9.937  24.847   6.328  1.00 45.00           O  
ANISOU  828  O   ARG A 102     6075   4858   6163    263   -402   -982       O  
ATOM    829  CB  ARG A 102       7.636  22.342   5.917  1.00 49.16           C  
ANISOU  829  CB  ARG A 102     6408   5633   6638    370   -204   -916       C  
ATOM    830  CG  ARG A 102       6.207  22.830   5.890  1.00 57.92           C  
ANISOU  830  CG  ARG A 102     7482   6713   7812    475   -158   -949       C  
ATOM    831  CD  ARG A 102       5.376  22.080   4.855  1.00 64.30           C  
ANISOU  831  CD  ARG A 102     8189   7585   8658    481   -134   -858       C  
ATOM    832  NE  ARG A 102       4.872  22.971   3.814  1.00 70.72           N  
ANISOU  832  NE  ARG A 102     8976   8314   9582    511   -181   -812       N  
ATOM    833  CZ  ARG A 102       5.177  22.868   2.524  1.00 72.89           C  
ANISOU  833  CZ  ARG A 102     9216   8583   9895    453   -238   -714       C  
ATOM    834  NH1 ARG A 102       4.673  23.729   1.649  1.00 75.97           N  
ANISOU  834  NH1 ARG A 102     9583   8899  10385    482   -284   -669       N  
ATOM    835  NH2 ARG A 102       5.982  21.901   2.108  1.00 69.79           N  
ANISOU  835  NH2 ARG A 102     8814   8264   9439    369   -248   -659       N  
ATOM    836  N   VAL A 103      10.428  22.669   6.648  1.00 41.13           N  
ANISOU  836  N   VAL A 103     5514   4581   5533    205   -326   -922       N  
ATOM    837  CA  VAL A 103      11.505  22.861   7.609  1.00 42.05           C  
ANISOU  837  CA  VAL A 103     5702   4691   5583    148   -367   -967       C  
ATOM    838  C   VAL A 103      12.608  23.798   7.103  1.00 48.81           C  
ANISOU  838  C   VAL A 103     6597   5454   6492     71   -474   -928       C  
ATOM    839  O   VAL A 103      13.172  24.585   7.867  1.00 52.84           O  
ANISOU  839  O   VAL A 103     7190   5898   6988     42   -528   -992       O  
ATOM    840  CB  VAL A 103      12.116  21.495   7.973  1.00 39.74           C  
ANISOU  840  CB  VAL A 103     5375   4527   5196    100   -333   -923       C  
ATOM    841  CG1 VAL A 103      13.455  21.659   8.662  1.00 41.79           C  
ANISOU  841  CG1 VAL A 103     5689   4787   5401     19   -398   -930       C  
ATOM    842  CG2 VAL A 103      11.142  20.686   8.826  1.00 34.25           C  
ANISOU  842  CG2 VAL A 103     4661   3918   4435    164   -237   -974       C  
ATOM    843  N   LYS A 104      12.912  23.709   5.813  1.00 51.34           N  
ANISOU  843  N   LYS A 104     6861   5775   6872     32   -505   -821       N  
ATOM    844  CA  LYS A 104      13.930  24.559   5.206  1.00 51.15           C  
ANISOU  844  CA  LYS A 104     6858   5674   6902    -46   -602   -762       C  
ATOM    845  C   LYS A 104      13.359  25.908   4.786  1.00 52.59           C  
ANISOU  845  C   LYS A 104     7077   5715   7190    -10   -650   -784       C  
ATOM    846  O   LYS A 104      14.107  26.816   4.426  1.00 54.97           O  
ANISOU  846  O   LYS A 104     7411   5929   7548    -73   -740   -746       O  
ATOM    847  CB  LYS A 104      14.524  23.878   3.975  1.00 47.45           C  
ANISOU  847  CB  LYS A 104     6310   5277   6443   -100   -608   -633       C  
ATOM    848  CG  LYS A 104      15.254  22.583   4.257  1.00 47.46           C  
ANISOU  848  CG  LYS A 104     6274   5403   6356   -138   -570   -597       C  
ATOM    849  CD  LYS A 104      16.606  22.832   4.881  1.00 46.42           C  
ANISOU  849  CD  LYS A 104     6177   5271   6191   -221   -635   -586       C  
ATOM    850  CE  LYS A 104      17.519  21.627   4.704  1.00 45.43           C  
ANISOU  850  CE  LYS A 104     5990   5264   6007   -264   -610   -506       C  
ATOM    851  NZ  LYS A 104      18.892  21.898   5.214  1.00 46.71           N  
ANISOU  851  NZ  LYS A 104     6168   5433   6146   -350   -681   -475       N  
ATOM    852  N   ASP A 105      12.036  26.032   4.825  1.00 49.91           N  
ANISOU  852  N   ASP A 105     6727   5353   6883     91   -593   -836       N  
ATOM    853  CA  ASP A 105      11.364  27.202   4.281  1.00 52.96           C  
ANISOU  853  CA  ASP A 105     7131   5611   7381    140   -630   -840       C  
ATOM    854  C   ASP A 105      11.975  27.552   2.933  1.00 53.79           C  
ANISOU  854  C   ASP A 105     7197   5685   7555     67   -705   -711       C  
ATOM    855  O   ASP A 105      12.392  28.686   2.707  1.00 52.25           O  
ANISOU  855  O   ASP A 105     7051   5368   7435     34   -790   -697       O  
ATOM    856  CB  ASP A 105      11.474  28.400   5.225  1.00 55.43           C  
ANISOU  856  CB  ASP A 105     7553   5788   7720    159   -677   -950       C  
ATOM    857  CG  ASP A 105      10.605  29.567   4.782  1.00 57.16           C  
ANISOU  857  CG  ASP A 105     7792   5865   8061    235   -703   -968       C  
ATOM    858  OD1 ASP A 105      11.013  30.736   4.969  1.00 54.50           O  
ANISOU  858  OD1 ASP A 105     7539   5383   7785    214   -784  -1004       O  
ATOM    859  OD2 ASP A 105       9.509  29.307   4.238  1.00 57.01           O  
ANISOU  859  OD2 ASP A 105     7702   5877   8082    314   -645   -941       O  
ATOM    860  N   SER A 106      12.032  26.568   2.044  1.00 54.62           N  
ANISOU  860  N   SER A 106     7220   5901   7631     42   -673   -617       N  
ATOM    861  CA  SER A 106      12.718  26.732   0.771  1.00 54.52           C  
ANISOU  861  CA  SER A 106     7167   5891   7657    -33   -731   -490       C  
ATOM    862  C   SER A 106      12.144  25.799  -0.289  1.00 58.72           C  
ANISOU  862  C   SER A 106     7614   6524   8173    -15   -681   -414       C  
ATOM    863  O   SER A 106      11.662  24.707   0.018  1.00 58.51           O  
ANISOU  863  O   SER A 106     7556   6594   8083     20   -605   -445       O  
ATOM    864  CB  SER A 106      14.222  26.485   0.944  1.00 49.68           C  
ANISOU  864  CB  SER A 106     6564   5322   6990   -135   -772   -448       C  
ATOM    865  OG  SER A 106      14.888  26.431  -0.306  1.00 46.88           O  
ANISOU  865  OG  SER A 106     6156   5003   6654   -202   -807   -318       O  
ATOM    866  N   GLU A 107      12.197  26.243  -1.538  1.00 62.58           N  
ANISOU  866  N   GLU A 107     8069   6989   8718    -46   -729   -313       N  
ATOM    867  CA  GLU A 107      11.698  25.458  -2.657  1.00 62.26           C  
ANISOU  867  CA  GLU A 107     7958   7040   8660    -40   -696   -237       C  
ATOM    868  C   GLU A 107      12.824  24.611  -3.241  1.00 56.33           C  
ANISOU  868  C   GLU A 107     7176   6393   7833   -118   -689   -162       C  
ATOM    869  O   GLU A 107      12.581  23.565  -3.842  1.00 51.96           O  
ANISOU  869  O   GLU A 107     6578   5939   7226   -114   -640   -131       O  
ATOM    870  CB  GLU A 107      11.129  26.387  -3.733  1.00 68.48           C  
ANISOU  870  CB  GLU A 107     8725   7755   9540    -31   -752   -161       C  
ATOM    871  CG  GLU A 107      10.256  25.686  -4.760  1.00 73.13           C  
ANISOU  871  CG  GLU A 107     9246   8425  10114     -8   -721   -103       C  
ATOM    872  CD  GLU A 107       8.962  25.170  -4.160  1.00 75.91           C  
ANISOU  872  CD  GLU A 107     9578   8800  10465     80   -655   -181       C  
ATOM    873  OE1 GLU A 107       8.473  25.785  -3.185  1.00 77.22           O  
ANISOU  873  OE1 GLU A 107     9778   8887  10676    144   -645   -266       O  
ATOM    874  OE2 GLU A 107       8.440  24.149  -4.658  1.00 76.14           O  
ANISOU  874  OE2 GLU A 107     9557   8927  10446     84   -612   -157       O  
ATOM    875  N   ASP A 108      14.056  25.079  -3.059  1.00 57.06           N  
ANISOU  875  N   ASP A 108     7294   6460   7925   -188   -739   -132       N  
ATOM    876  CA  ASP A 108      15.233  24.404  -3.595  1.00 55.84           C  
ANISOU  876  CA  ASP A 108     7105   6403   7708   -258   -734    -52       C  
ATOM    877  C   ASP A 108      15.977  23.643  -2.518  1.00 51.24           C  
ANISOU  877  C   ASP A 108     6537   5878   7056   -272   -699   -106       C  
ATOM    878  O   ASP A 108      16.637  24.238  -1.667  1.00 54.47           O  
ANISOU  878  O   ASP A 108     6987   6232   7475   -306   -744   -137       O  
ATOM    879  CB  ASP A 108      16.190  25.410  -4.225  1.00 59.30           C  
ANISOU  879  CB  ASP A 108     7542   6792   8195   -337   -816     45       C  
ATOM    880  CG  ASP A 108      15.697  25.920  -5.551  1.00 66.44           C  
ANISOU  880  CG  ASP A 108     8416   7680   9150   -341   -847    135       C  
ATOM    881  OD1 ASP A 108      15.118  25.115  -6.314  1.00 67.73           O  
ANISOU  881  OD1 ASP A 108     8539   7925   9270   -312   -798    158       O  
ATOM    882  OD2 ASP A 108      15.885  27.125  -5.825  1.00 70.72           O  
ANISOU  882  OD2 ASP A 108     8977   8123   9772   -377   -927    186       O  
ATOM    883  N   VAL A 109      15.870  22.323  -2.558  1.00 41.69           N  
ANISOU  883  N   VAL A 109     5295   4772   5773   -248   -625   -114       N  
ATOM    884  CA  VAL A 109      16.630  21.489  -1.642  1.00 36.03           C  
ANISOU  884  CA  VAL A 109     4581   4119   4989   -262   -591   -145       C  
ATOM    885  C   VAL A 109      17.246  20.337  -2.424  1.00 29.01           C  
ANISOU  885  C   VAL A 109     3640   3341   4041   -279   -544    -76       C  
ATOM    886  O   VAL A 109      16.539  19.599  -3.106  1.00 26.95           O  
ANISOU  886  O   VAL A 109     3358   3125   3759   -244   -497    -72       O  
ATOM    887  CB  VAL A 109      15.752  20.963  -0.502  1.00 34.01           C  
ANISOU  887  CB  VAL A 109     4353   3866   4703   -200   -539   -252       C  
ATOM    888  CG1 VAL A 109      16.622  20.345   0.587  1.00 35.63           C  
ANISOU  888  CG1 VAL A 109     4571   4122   4845   -224   -524   -279       C  
ATOM    889  CG2 VAL A 109      14.905  22.094   0.070  1.00 29.52           C  
ANISOU  889  CG2 VAL A 109     3833   3189   4195   -161   -570   -325       C  
ATOM    890  N   PRO A 110      18.577  20.195  -2.357  1.00 26.64           N  
ANISOU  890  N   PRO A 110     3320   3085   3715   -333   -559    -21       N  
ATOM    891  CA  PRO A 110      19.197  19.148  -3.174  1.00 27.49           C  
ANISOU  891  CA  PRO A 110     3378   3296   3771   -337   -508     46       C  
ATOM    892  C   PRO A 110      18.755  17.760  -2.708  1.00 26.82           C  
ANISOU  892  C   PRO A 110     3293   3268   3629   -284   -431    -11       C  
ATOM    893  O   PRO A 110      18.836  17.448  -1.518  1.00 23.46           O  
ANISOU  893  O   PRO A 110     2888   2843   3184   -274   -422    -66       O  
ATOM    894  CB  PRO A 110      20.699  19.360  -2.947  1.00 22.24           C  
ANISOU  894  CB  PRO A 110     2687   2663   3100   -400   -542    113       C  
ATOM    895  CG  PRO A 110      20.817  20.744  -2.386  1.00 25.88           C  
ANISOU  895  CG  PRO A 110     3186   3025   3623   -446   -629    101       C  
ATOM    896  CD  PRO A 110      19.572  20.964  -1.595  1.00 26.24           C  
ANISOU  896  CD  PRO A 110     3290   2997   3685   -391   -624    -11       C  
ATOM    897  N   MET A 111      18.270  16.958  -3.651  1.00 29.29           N  
ANISOU  897  N   MET A 111     3588   3627   3914   -256   -383      3       N  
ATOM    898  CA  MET A 111      17.768  15.617  -3.375  1.00 28.02           C  
ANISOU  898  CA  MET A 111     3430   3510   3707   -211   -316    -44       C  
ATOM    899  C   MET A 111      18.047  14.717  -4.557  1.00 23.07           C  
ANISOU  899  C   MET A 111     2780   2950   3037   -204   -272      3       C  
ATOM    900  O   MET A 111      18.166  15.186  -5.687  1.00 23.07           O  
ANISOU  900  O   MET A 111     2766   2960   3041   -224   -290     59       O  
ATOM    901  CB  MET A 111      16.259  15.633  -3.154  1.00 28.18           C  
ANISOU  901  CB  MET A 111     3471   3489   3747   -171   -307   -110       C  
ATOM    902  CG  MET A 111      15.782  16.558  -2.063  1.00 35.80           C  
ANISOU  902  CG  MET A 111     4466   4386   4752   -162   -339   -169       C  
ATOM    903  SD  MET A 111      14.014  16.339  -1.729  1.00 46.08           S  
ANISOU  903  SD  MET A 111     5774   5663   6070   -102   -307   -241       S  
ATOM    904  CE  MET A 111      13.804  17.475  -0.361  1.00 44.80           C  
ANISOU  904  CE  MET A 111     5653   5427   5942    -86   -337   -314       C  
ATOM    905  N   VAL A 112      18.150  13.422  -4.284  1.00 20.42           N  
ANISOU  905  N   VAL A 112     2445   2658   2658   -175   -215    -20       N  
ATOM    906  CA  VAL A 112      18.193  12.401  -5.323  1.00 18.39           C  
ANISOU  906  CA  VAL A 112     2182   2451   2355   -155   -166     -2       C  
ATOM    907  C   VAL A 112      17.149  11.357  -4.954  1.00 20.67           C  
ANISOU  907  C   VAL A 112     2496   2729   2628   -121   -130    -67       C  
ATOM    908  O   VAL A 112      17.088  10.923  -3.803  1.00 20.08           O  
ANISOU  908  O   VAL A 112     2427   2645   2555   -107   -116   -103       O  
ATOM    909  CB  VAL A 112      19.586  11.730  -5.425  1.00 19.14           C  
ANISOU  909  CB  VAL A 112     2249   2607   2415   -151   -128     46       C  
ATOM    910  CG1 VAL A 112      19.545  10.533  -6.369  1.00 18.63           C  
ANISOU  910  CG1 VAL A 112     2195   2583   2299   -116    -68     42       C  
ATOM    911  CG2 VAL A 112      20.632  12.740  -5.888  1.00 18.27           C  
ANISOU  911  CG2 VAL A 112     2103   2519   2321   -192   -163    126       C  
ATOM    912  N   LEU A 113      16.318  10.981  -5.922  1.00 21.55           N  
ANISOU  912  N   LEU A 113     2620   2844   2723   -114   -121    -77       N  
ATOM    913  CA  LEU A 113      15.323   9.932  -5.725  1.00 19.73           C  
ANISOU  913  CA  LEU A 113     2411   2605   2480    -93    -93   -128       C  
ATOM    914  C   LEU A 113      15.957   8.587  -6.024  1.00 22.85           C  
ANISOU  914  C   LEU A 113     2821   3035   2828    -73    -40   -128       C  
ATOM    915  O   LEU A 113      16.538   8.379  -7.095  1.00 21.68           O  
ANISOU  915  O   LEU A 113     2677   2919   2642    -72    -24   -100       O  
ATOM    916  CB  LEU A 113      14.121  10.146  -6.641  1.00 17.90           C  
ANISOU  916  CB  LEU A 113     2187   2361   2254   -103   -118   -134       C  
ATOM    917  CG  LEU A 113      12.978   9.131  -6.529  1.00 20.34           C  
ANISOU  917  CG  LEU A 113     2511   2661   2555    -94   -101   -178       C  
ATOM    918  CD1 LEU A 113      12.306   9.212  -5.165  1.00 18.44           C  
ANISOU  918  CD1 LEU A 113     2259   2396   2353    -80    -98   -214       C  
ATOM    919  CD2 LEU A 113      11.958   9.364  -7.627  1.00 18.84           C  
ANISOU  919  CD2 LEU A 113     2322   2471   2365   -113   -136   -169       C  
ATOM    920  N   VAL A 114      15.846   7.673  -5.071  1.00 22.60           N  
ANISOU  920  N   VAL A 114     2798   2993   2795    -54    -12   -159       N  
ATOM    921  CA  VAL A 114      16.517   6.389  -5.179  1.00 19.08           C  
ANISOU  921  CA  VAL A 114     2367   2565   2317    -28     37   -159       C  
ATOM    922  C   VAL A 114      15.513   5.257  -5.057  1.00 19.29           C  
ANISOU  922  C   VAL A 114     2426   2564   2339    -21     53   -203       C  
ATOM    923  O   VAL A 114      14.824   5.146  -4.043  1.00 17.10           O  
ANISOU  923  O   VAL A 114     2144   2268   2086    -26     47   -223       O  
ATOM    924  CB  VAL A 114      17.579   6.244  -4.072  1.00 16.28           C  
ANISOU  924  CB  VAL A 114     1989   2225   1972    -14     52   -136       C  
ATOM    925  CG1 VAL A 114      18.218   4.855  -4.095  1.00 14.82           C  
ANISOU  925  CG1 VAL A 114     1816   2049   1766     24    104   -132       C  
ATOM    926  CG2 VAL A 114      18.634   7.321  -4.225  1.00 20.00           C  
ANISOU  926  CG2 VAL A 114     2425   2724   2451    -31     29    -85       C  
ATOM    927  N   GLY A 115      15.436   4.420  -6.090  1.00 16.73           N  
ANISOU  927  N   GLY A 115     2137   2240   1981    -13     74   -216       N  
ATOM    928  CA  GLY A 115      14.572   3.250  -6.071  1.00 14.09           C  
ANISOU  928  CA  GLY A 115     1841   1871   1643    -15     83   -254       C  
ATOM    929  C   GLY A 115      15.417   2.014  -5.827  1.00 17.27           C  
ANISOU  929  C   GLY A 115     2267   2263   2033     23    130   -257       C  
ATOM    930  O   GLY A 115      16.101   1.512  -6.730  1.00 18.38           O  
ANISOU  930  O   GLY A 115     2435   2412   2138     50    161   -260       O  
ATOM    931  N   ASN A 116      15.378   1.524  -4.596  1.00 14.83           N  
ANISOU  931  N   ASN A 116     1946   1935   1752     29    139   -253       N  
ATOM    932  CA  ASN A 116      16.283   0.465  -4.178  1.00 18.64           C  
ANISOU  932  CA  ASN A 116     2439   2406   2236     70    180   -241       C  
ATOM    933  C   ASN A 116      15.686  -0.935  -4.327  1.00 21.05           C  
ANISOU  933  C   ASN A 116     2799   2655   2544     73    192   -272       C  
ATOM    934  O   ASN A 116      14.490  -1.089  -4.550  1.00 21.71           O  
ANISOU  934  O   ASN A 116     2904   2713   2631     34    164   -300       O  
ATOM    935  CB  ASN A 116      16.756   0.702  -2.739  1.00 14.91           C  
ANISOU  935  CB  ASN A 116     1925   1952   1789     73    178   -206       C  
ATOM    936  CG  ASN A 116      17.958  -0.147  -2.375  1.00 19.34           C  
ANISOU  936  CG  ASN A 116     2479   2515   2354    119    215   -173       C  
ATOM    937  OD1 ASN A 116      18.887  -0.278  -3.163  1.00 21.77           O  
ANISOU  937  OD1 ASN A 116     2786   2838   2647    156    244   -160       O  
ATOM    938  ND2 ASN A 116      17.939  -0.735  -1.178  1.00 18.89           N  
ANISOU  938  ND2 ASN A 116     2413   2446   2318    120    216   -154       N  
ATOM    939  N   LYS A 117      16.543  -1.946  -4.202  1.00 20.14           N  
ANISOU  939  N   LYS A 117     2703   2517   2432    119    231   -263       N  
ATOM    940  CA  LYS A 117      16.157  -3.337  -4.387  1.00 19.66           C  
ANISOU  940  CA  LYS A 117     2704   2388   2379    128    242   -293       C  
ATOM    941  C   LYS A 117      15.775  -3.631  -5.835  1.00 23.38           C  
ANISOU  941  C   LYS A 117     3240   2835   2810    123    241   -346       C  
ATOM    942  O   LYS A 117      14.853  -4.412  -6.088  1.00 29.18           O  
ANISOU  942  O   LYS A 117     4028   3512   3548     91    218   -382       O  
ATOM    943  CB  LYS A 117      14.999  -3.719  -3.457  1.00 18.04           C  
ANISOU  943  CB  LYS A 117     2497   2151   2207     79    211   -290       C  
ATOM    944  CG  LYS A 117      15.181  -3.311  -2.001  1.00 19.45           C  
ANISOU  944  CG  LYS A 117     2616   2364   2409     74    208   -243       C  
ATOM    945  CD  LYS A 117      14.279  -4.152  -1.096  1.00 19.45           C  
ANISOU  945  CD  LYS A 117     2624   2329   2438     41    195   -231       C  
ATOM    946  CE  LYS A 117      14.419  -3.762   0.369  1.00 23.27           C  
ANISOU  946  CE  LYS A 117     3054   2858   2930     35    195   -186       C  
ATOM    947  NZ  LYS A 117      13.562  -4.588   1.274  1.00 24.84           N  
ANISOU  947  NZ  LYS A 117     3254   3034   3150      1    188   -163       N  
ATOM    948  N   CYS A 118      16.478  -3.028  -6.792  1.00 21.15           N  
ANISOU  948  N   CYS A 118     2954   2599   2485    149    261   -348       N  
ATOM    949  CA  CYS A 118      16.150  -3.266  -8.205  1.00 25.81           C  
ANISOU  949  CA  CYS A 118     3609   3178   3019    143    260   -400       C  
ATOM    950  C   CYS A 118      16.538  -4.675  -8.658  1.00 27.10           C  
ANISOU  950  C   CYS A 118     3851   3276   3168    193    300   -445       C  
ATOM    951  O   CYS A 118      16.283  -5.071  -9.796  1.00 27.95           O  
ANISOU  951  O   CYS A 118     4032   3364   3223    190    301   -500       O  
ATOM    952  CB  CYS A 118      16.741  -2.193  -9.129  1.00 29.16           C  
ANISOU  952  CB  CYS A 118     4006   3679   3394    151    271   -382       C  
ATOM    953  SG  CYS A 118      18.531  -2.202  -9.260  1.00 34.74           S  
ANISOU  953  SG  CYS A 118     4677   4437   4085    236    346   -343       S  
ATOM    954  N   ASP A 119      17.134  -5.437  -7.748  1.00 28.30           N  
ANISOU  954  N   ASP A 119     3994   3390   3369    237    330   -422       N  
ATOM    955  CA  ASP A 119      17.468  -6.833  -8.004  1.00 27.29           C  
ANISOU  955  CA  ASP A 119     3942   3181   3247    291    365   -462       C  
ATOM    956  C   ASP A 119      16.269  -7.776  -7.836  1.00 30.80           C  
ANISOU  956  C   ASP A 119     4454   3530   3717    235    317   -500       C  
ATOM    957  O   ASP A 119      16.313  -8.916  -8.292  1.00 35.78           O  
ANISOU  957  O   ASP A 119     5172   4077   4347    263    332   -550       O  
ATOM    958  CB  ASP A 119      18.603  -7.276  -7.077  1.00 30.64           C  
ANISOU  958  CB  ASP A 119     4321   3600   3721    363    411   -408       C  
ATOM    959  CG  ASP A 119      18.263  -7.088  -5.599  1.00 29.93           C  
ANISOU  959  CG  ASP A 119     4169   3514   3689    321    375   -347       C  
ATOM    960  OD1 ASP A 119      18.409  -5.958  -5.094  1.00 24.43           O  
ANISOU  960  OD1 ASP A 119     3396   2895   2991    296    359   -303       O  
ATOM    961  OD2 ASP A 119      17.852  -8.067  -4.940  1.00 33.00           O  
ANISOU  961  OD2 ASP A 119     4588   3828   4122    312    361   -344       O  
ATOM    962  N   LEU A 120      15.210  -7.308  -7.177  1.00 31.00           N  
ANISOU  962  N   LEU A 120     4440   3568   3770    156    262   -474       N  
ATOM    963  CA  LEU A 120      14.034  -8.144  -6.910  1.00 32.48           C  
ANISOU  963  CA  LEU A 120     4673   3679   3990     92    213   -491       C  
ATOM    964  C   LEU A 120      13.110  -8.270  -8.122  1.00 33.99           C  
ANISOU  964  C   LEU A 120     4935   3845   4135     36    169   -554       C  
ATOM    965  O   LEU A 120      13.019  -7.352  -8.940  1.00 35.46           O  
ANISOU  965  O   LEU A 120     5109   4097   4268     23    160   -568       O  
ATOM    966  CB  LEU A 120      13.234  -7.608  -5.711  1.00 32.96           C  
ANISOU  966  CB  LEU A 120     4654   3774   4094     34    177   -434       C  
ATOM    967  CG  LEU A 120      13.898  -7.558  -4.330  1.00 32.87           C  
ANISOU  967  CG  LEU A 120     4578   3786   4125     67    204   -369       C  
ATOM    968  CD1 LEU A 120      12.917  -7.027  -3.296  1.00 26.12           C  
ANISOU  968  CD1 LEU A 120     3659   2969   3295      4    170   -329       C  
ATOM    969  CD2 LEU A 120      14.423  -8.938  -3.916  1.00 32.67           C  
ANISOU  969  CD2 LEU A 120     4599   3675   4140    108    227   -359       C  
ATOM    970  N   PRO A 121      12.420  -9.418  -8.237  1.00 36.79           N  
ANISOU  970  N   PRO A 121     5366   4102   4509     -2    135   -588       N  
ATOM    971  CA  PRO A 121      11.395  -9.662  -9.262  1.00 39.28           C  
ANISOU  971  CA  PRO A 121     5752   4385   4786    -75     76   -644       C  
ATOM    972  C   PRO A 121      10.013  -9.155  -8.836  1.00 42.41           C  
ANISOU  972  C   PRO A 121     6087   4815   5213   -174      7   -602       C  
ATOM    973  O   PRO A 121       9.085  -9.114  -9.647  1.00 46.94           O  
ANISOU  973  O   PRO A 121     6693   5386   5756   -244    -52   -631       O  
ATOM    974  CB  PRO A 121      11.379 -11.186  -9.366  1.00 36.70           C  
ANISOU  974  CB  PRO A 121     5532   3928   4484    -71     69   -689       C  
ATOM    975  CG  PRO A 121      11.734 -11.648  -7.995  1.00 33.96           C  
ANISOU  975  CG  PRO A 121     5136   3549   4217    -42     94   -625       C  
ATOM    976  CD  PRO A 121      12.694 -10.625  -7.435  1.00 35.61           C  
ANISOU  976  CD  PRO A 121     5248   3861   4423     24    150   -573       C  
ATOM    977  N   SER A 122       9.901  -8.764  -7.570  1.00 41.94           N  
ANISOU  977  N   SER A 122     5935   4791   5208   -176     17   -534       N  
ATOM    978  CA  SER A 122       8.643  -8.334  -6.960  1.00 44.14           C  
ANISOU  978  CA  SER A 122     6142   5105   5523   -254    -32   -487       C  
ATOM    979  C   SER A 122       8.310  -6.841  -7.166  1.00 48.53           C  
ANISOU  979  C   SER A 122     6620   5762   6056   -263    -43   -468       C  
ATOM    980  O   SER A 122       7.701  -6.217  -6.299  1.00 55.90           O  
ANISOU  980  O   SER A 122     7470   6745   7026   -286    -51   -420       O  
ATOM    981  CB  SER A 122       8.676  -8.665  -5.458  1.00 39.22           C  
ANISOU  981  CB  SER A 122     5463   4476   4962   -248    -11   -425       C  
ATOM    982  OG  SER A 122       7.538  -8.162  -4.781  1.00 37.24           O  
ANISOU  982  OG  SER A 122     5133   4277   4741   -309    -42   -377       O  
ATOM    983  N   ARG A 123       8.687  -6.272  -8.308  1.00 42.63           N  
ANISOU  983  N   ARG A 123     5902   5046   5249   -245    -43   -504       N  
ATOM    984  CA  ARG A 123       8.442  -4.849  -8.567  1.00 38.75           C  
ANISOU  984  CA  ARG A 123     5342   4641   4742   -252    -56   -481       C  
ATOM    985  C   ARG A 123       6.958  -4.466  -8.625  1.00 39.99           C  
ANISOU  985  C   ARG A 123     5452   4820   4922   -329   -122   -456       C  
ATOM    986  O   ARG A 123       6.175  -5.115  -9.319  1.00 44.10           O  
ANISOU  986  O   ARG A 123     6022   5305   5431   -391   -175   -478       O  
ATOM    987  CB  ARG A 123       9.116  -4.416  -9.869  1.00 35.42           C  
ANISOU  987  CB  ARG A 123     4965   4248   4246   -224    -47   -516       C  
ATOM    988  CG  ARG A 123       8.840  -2.970 -10.252  1.00 33.37           C  
ANISOU  988  CG  ARG A 123     4641   4067   3972   -237    -71   -484       C  
ATOM    989  CD  ARG A 123       9.477  -2.620 -11.590  1.00 31.74           C  
ANISOU  989  CD  ARG A 123     4481   3895   3686   -219    -63   -509       C  
ATOM    990  NE  ARG A 123      10.932  -2.715 -11.526  1.00 32.70           N  
ANISOU  990  NE  ARG A 123     4616   4025   3785   -142     10   -516       N  
ATOM    991  CZ  ARG A 123      11.751  -1.683 -11.325  1.00 35.76           C  
ANISOU  991  CZ  ARG A 123     4943   4471   4174   -103     41   -475       C  
ATOM    992  NH1 ARG A 123      11.263  -0.456 -11.173  1.00 32.42           N  
ANISOU  992  NH1 ARG A 123     4451   4092   3775   -131      5   -432       N  
ATOM    993  NH2 ARG A 123      13.064  -1.879 -11.278  1.00 35.69           N  
ANISOU  993  NH2 ARG A 123     4940   4472   4148    -36    105   -474       N  
ATOM    994  N   THR A 124       6.586  -3.406  -7.902  1.00 29.81           N  
ANISOU  994  N   THR A 124     4069   3589   3668   -325   -120   -411       N  
ATOM    995  CA  THR A 124       5.244  -2.834  -7.997  1.00 25.93           C  
ANISOU  995  CA  THR A 124     3517   3132   3203   -381   -175   -381       C  
ATOM    996  C   THR A 124       5.295  -1.349  -8.329  1.00 28.14           C  
ANISOU  996  C   THR A 124     3742   3475   3476   -357   -180   -363       C  
ATOM    997  O   THR A 124       4.265  -0.721  -8.552  1.00 28.43           O  
ANISOU  997  O   THR A 124     3725   3544   3535   -391   -225   -335       O  
ATOM    998  CB  THR A 124       4.437  -3.011  -6.701  1.00 24.99           C  
ANISOU  998  CB  THR A 124     3328   3021   3148   -401   -169   -338       C  
ATOM    999  OG1 THR A 124       5.174  -2.472  -5.603  1.00 27.72           O  
ANISOU  999  OG1 THR A 124     3631   3392   3507   -340   -111   -324       O  
ATOM   1000  CG2 THR A 124       4.162  -4.473  -6.438  1.00 30.79           C  
ANISOU 1000  CG2 THR A 124     4110   3689   3899   -444   -181   -341       C  
ATOM   1001  N   VAL A 125       6.500  -0.788  -8.338  1.00 29.35           N  
ANISOU 1001  N   VAL A 125     3904   3644   3604   -298   -136   -371       N  
ATOM   1002  CA  VAL A 125       6.692   0.606  -8.711  1.00 25.95           C  
ANISOU 1002  CA  VAL A 125     3431   3261   3167   -277   -144   -351       C  
ATOM   1003  C   VAL A 125       7.517   0.664  -9.990  1.00 28.20           C  
ANISOU 1003  C   VAL A 125     3776   3556   3382   -267   -144   -371       C  
ATOM   1004  O   VAL A 125       8.670   0.245 -10.011  1.00 32.40           O  
ANISOU 1004  O   VAL A 125     4349   4078   3884   -226    -95   -391       O  
ATOM   1005  CB  VAL A 125       7.389   1.414  -7.593  1.00 21.37           C  
ANISOU 1005  CB  VAL A 125     2801   2700   2619   -225   -101   -332       C  
ATOM   1006  CG1 VAL A 125       7.459   2.896  -7.974  1.00 20.27           C  
ANISOU 1006  CG1 VAL A 125     2620   2595   2485   -212   -121   -308       C  
ATOM   1007  CG2 VAL A 125       6.642   1.251  -6.276  1.00 16.50           C  
ANISOU 1007  CG2 VAL A 125     2133   2081   2054   -229    -90   -318       C  
ATOM   1008  N   ASP A 126       6.919   1.177 -11.058  1.00 27.65           N  
ANISOU 1008  N   ASP A 126     3707   3513   3286   -305   -196   -360       N  
ATOM   1009  CA  ASP A 126       7.571   1.199 -12.360  1.00 33.51           C  
ANISOU 1009  CA  ASP A 126     4508   4275   3947   -304   -198   -377       C  
ATOM   1010  C   ASP A 126       8.626   2.289 -12.455  1.00 28.62           C  
ANISOU 1010  C   ASP A 126     3860   3698   3317   -258   -166   -347       C  
ATOM   1011  O   ASP A 126       8.450   3.391 -11.935  1.00 25.11           O  
ANISOU 1011  O   ASP A 126     3347   3270   2925   -250   -178   -306       O  
ATOM   1012  CB  ASP A 126       6.539   1.408 -13.469  1.00 45.19           C  
ANISOU 1012  CB  ASP A 126     5997   5778   5395   -367   -273   -366       C  
ATOM   1013  CG  ASP A 126       5.497   0.315 -13.505  1.00 59.90           C  
ANISOU 1013  CG  ASP A 126     7892   7601   7265   -427   -317   -391       C  
ATOM   1014  OD1 ASP A 126       5.858  -0.858 -13.266  1.00 67.30           O  
ANISOU 1014  OD1 ASP A 126     8893   8487   8189   -420   -288   -438       O  
ATOM   1015  OD2 ASP A 126       4.316   0.628 -13.768  1.00 64.40           O  
ANISOU 1015  OD2 ASP A 126     8421   8189   7859   -482   -385   -359       O  
ATOM   1016  N   THR A 127       9.714   1.980 -13.145  1.00 26.14           N  
ANISOU 1016  N   THR A 127     3597   3400   2935   -229   -125   -366       N  
ATOM   1017  CA  THR A 127      10.759   2.961 -13.402  1.00 29.75           C  
ANISOU 1017  CA  THR A 127     4026   3905   3374   -197    -98   -327       C  
ATOM   1018  C   THR A 127      10.182   4.287 -13.892  1.00 30.78           C  
ANISOU 1018  C   THR A 127     4107   4071   3519   -230   -155   -273       C  
ATOM   1019  O   THR A 127      10.548   5.352 -13.399  1.00 34.00           O  
ANISOU 1019  O   THR A 127     4458   4489   3973   -213   -155   -230       O  
ATOM   1020  CB  THR A 127      11.768   2.433 -14.430  1.00 33.01           C  
ANISOU 1020  CB  THR A 127     4501   4347   3694   -170    -52   -351       C  
ATOM   1021  OG1 THR A 127      12.342   1.214 -13.944  1.00 35.59           O  
ANISOU 1021  OG1 THR A 127     4872   4631   4020   -128      3   -399       O  
ATOM   1022  CG2 THR A 127      12.873   3.453 -14.664  1.00 35.87           C  
ANISOU 1022  CG2 THR A 127     4820   4768   4042   -142    -23   -296       C  
ATOM   1023  N   LYS A 128       9.266   4.213 -14.850  1.00 32.85           N  
ANISOU 1023  N   LYS A 128     4392   4345   3743   -279   -212   -274       N  
ATOM   1024  CA  LYS A 128       8.696   5.406 -15.467  1.00 33.65           C  
ANISOU 1024  CA  LYS A 128     4451   4482   3855   -311   -273   -215       C  
ATOM   1025  C   LYS A 128       7.971   6.310 -14.472  1.00 27.46           C  
ANISOU 1025  C   LYS A 128     3585   3671   3176   -306   -301   -180       C  
ATOM   1026  O   LYS A 128       8.221   7.511 -14.435  1.00 29.46           O  
ANISOU 1026  O   LYS A 128     3793   3935   3464   -294   -315   -130       O  
ATOM   1027  CB  LYS A 128       7.759   5.032 -16.620  1.00 40.15           C  
ANISOU 1027  CB  LYS A 128     5314   5325   4617   -371   -336   -221       C  
ATOM   1028  CG  LYS A 128       7.498   6.173 -17.600  1.00 46.62           C  
ANISOU 1028  CG  LYS A 128     6104   6195   5413   -401   -394   -151       C  
ATOM   1029  CD  LYS A 128       6.003   6.393 -17.817  1.00 56.64           C  
ANISOU 1029  CD  LYS A 128     7337   7462   6722   -455   -481   -121       C  
ATOM   1030  CE  LYS A 128       5.723   7.377 -18.958  1.00 61.12           C  
ANISOU 1030  CE  LYS A 128     7885   8083   7254   -491   -546    -48       C  
ATOM   1031  NZ  LYS A 128       6.316   8.728 -18.725  1.00 61.62           N  
ANISOU 1031  NZ  LYS A 128     7889   8151   7371   -456   -537     19       N  
ATOM   1032  N   GLN A 129       7.068   5.750 -13.673  1.00 26.60           N  
ANISOU 1032  N   GLN A 129     3459   3527   3119   -314   -309   -204       N  
ATOM   1033  CA  GLN A 129       6.375   6.570 -12.685  1.00 29.56           C  
ANISOU 1033  CA  GLN A 129     3758   3883   3588   -298   -324   -178       C  
ATOM   1034  C   GLN A 129       7.359   7.247 -11.733  1.00 26.01           C  
ANISOU 1034  C   GLN A 129     3286   3421   3176   -248   -277   -175       C  
ATOM   1035  O   GLN A 129       7.150   8.387 -11.326  1.00 21.26           O  
ANISOU 1035  O   GLN A 129     2634   2810   2634   -231   -295   -145       O  
ATOM   1036  CB  GLN A 129       5.260   5.806 -11.937  1.00 36.45           C  
ANISOU 1036  CB  GLN A 129     4610   4734   4507   -315   -331   -198       C  
ATOM   1037  CG  GLN A 129       5.622   4.461 -11.331  1.00 41.30           C  
ANISOU 1037  CG  GLN A 129     5270   5320   5100   -311   -284   -248       C  
ATOM   1038  CD  GLN A 129       4.411   3.742 -10.722  1.00 39.72           C  
ANISOU 1038  CD  GLN A 129     5043   5105   4945   -343   -303   -252       C  
ATOM   1039  OE1 GLN A 129       4.394   2.515 -10.602  1.00 36.31           O  
ANISOU 1039  OE1 GLN A 129     4657   4646   4492   -365   -291   -283       O  
ATOM   1040  NE2 GLN A 129       3.399   4.509 -10.335  1.00 41.48           N  
ANISOU 1040  NE2 GLN A 129     5187   5342   5232   -344   -330   -215       N  
ATOM   1041  N   ALA A 130       8.446   6.558 -11.408  1.00 25.84           N  
ANISOU 1041  N   ALA A 130     3302   3396   3119   -224   -220   -205       N  
ATOM   1042  CA  ALA A 130       9.484   7.139 -10.568  1.00 22.01           C  
ANISOU 1042  CA  ALA A 130     2797   2905   2660   -186   -183   -197       C  
ATOM   1043  C   ALA A 130      10.287   8.220 -11.304  1.00 22.98           C  
ANISOU 1043  C   ALA A 130     2911   3055   2767   -187   -198   -149       C  
ATOM   1044  O   ALA A 130      10.630   9.243 -10.724  1.00 25.54           O  
ANISOU 1044  O   ALA A 130     3200   3365   3140   -173   -205   -124       O  
ATOM   1045  CB  ALA A 130      10.396   6.060 -10.049  1.00 23.53           C  
ANISOU 1045  CB  ALA A 130     3024   3092   2823   -161   -124   -230       C  
ATOM   1046  N   GLN A 131      10.589   7.990 -12.578  1.00 20.98           N  
ANISOU 1046  N   GLN A 131     2691   2839   2443   -206   -203   -135       N  
ATOM   1047  CA  GLN A 131      11.270   8.990 -13.398  1.00 23.72           C  
ANISOU 1047  CA  GLN A 131     3024   3221   2766   -216   -220    -76       C  
ATOM   1048  C   GLN A 131      10.429  10.248 -13.517  1.00 25.18           C  
ANISOU 1048  C   GLN A 131     3165   3388   3013   -236   -286    -28       C  
ATOM   1049  O   GLN A 131      10.946  11.360 -13.435  1.00 26.20           O  
ANISOU 1049  O   GLN A 131     3265   3511   3178   -234   -303     20       O  
ATOM   1050  CB  GLN A 131      11.525   8.454 -14.807  1.00 31.06           C  
ANISOU 1050  CB  GLN A 131     4002   4204   3595   -236   -214    -72       C  
ATOM   1051  CG  GLN A 131      12.647   7.449 -14.921  1.00 44.79           C  
ANISOU 1051  CG  GLN A 131     5782   5966   5268   -203   -141   -106       C  
ATOM   1052  CD  GLN A 131      12.744   6.843 -16.318  1.00 56.31           C  
ANISOU 1052  CD  GLN A 131     7301   7476   6617   -218   -132   -120       C  
ATOM   1053  OE1 GLN A 131      11.854   7.028 -17.152  1.00 58.22           O  
ANISOU 1053  OE1 GLN A 131     7559   7733   6829   -261   -188   -109       O  
ATOM   1054  NE2 GLN A 131      13.828   6.114 -16.575  1.00 58.26           N  
ANISOU 1054  NE2 GLN A 131     7582   7751   6802   -179    -60   -143       N  
ATOM   1055  N   ASP A 132       9.132  10.060 -13.738  1.00 26.01           N  
ANISOU 1055  N   ASP A 132     3264   3484   3134   -256   -328    -36       N  
ATOM   1056  CA  ASP A 132       8.202  11.174 -13.889  1.00 24.79           C  
ANISOU 1056  CA  ASP A 132     3063   3312   3045   -267   -392     12       C  
ATOM   1057  C   ASP A 132       8.092  11.989 -12.602  1.00 24.55           C  
ANISOU 1057  C   ASP A 132     2990   3227   3112   -229   -386      5       C  
ATOM   1058  O   ASP A 132       7.964  13.214 -12.641  1.00 23.92           O  
ANISOU 1058  O   ASP A 132     2878   3120   3089   -223   -426     51       O  
ATOM   1059  CB  ASP A 132       6.814  10.664 -14.305  1.00 26.50           C  
ANISOU 1059  CB  ASP A 132     3272   3535   3260   -295   -436      7       C  
ATOM   1060  CG  ASP A 132       6.808  10.033 -15.697  1.00 33.96           C  
ANISOU 1060  CG  ASP A 132     4267   4533   4104   -342   -459     15       C  
ATOM   1061  OD1 ASP A 132       7.822  10.152 -16.411  1.00 35.45           O  
ANISOU 1061  OD1 ASP A 132     4488   4758   4224   -346   -440     33       O  
ATOM   1062  OD2 ASP A 132       5.785   9.423 -16.086  1.00 39.48           O  
ANISOU 1062  OD2 ASP A 132     4973   5242   4788   -377   -498      4       O  
ATOM   1063  N   LEU A 133       8.120  11.310 -11.459  1.00 21.72           N  
ANISOU 1063  N   LEU A 133     2635   2849   2769   -203   -339    -52       N  
ATOM   1064  CA  LEU A 133       8.091  12.016 -10.185  1.00 26.66           C  
ANISOU 1064  CA  LEU A 133     3231   3429   3468   -166   -327    -70       C  
ATOM   1065  C   LEU A 133       9.338  12.883 -10.027  1.00 26.02           C  
ANISOU 1065  C   LEU A 133     3157   3335   3395   -160   -325    -46       C  
ATOM   1066  O   LEU A 133       9.244  14.063  -9.706  1.00 30.72           O  
ANISOU 1066  O   LEU A 133     3731   3888   4054   -148   -356    -27       O  
ATOM   1067  CB  LEU A 133       7.972  11.042  -9.010  1.00 26.56           C  
ANISOU 1067  CB  LEU A 133     3225   3411   3454   -145   -276   -129       C  
ATOM   1068  CG  LEU A 133       7.810  11.758  -7.668  1.00 26.37           C  
ANISOU 1068  CG  LEU A 133     3176   3350   3494   -106   -262   -154       C  
ATOM   1069  CD1 LEU A 133       6.483  12.499  -7.655  1.00 25.85           C  
ANISOU 1069  CD1 LEU A 133     3064   3263   3496    -89   -296   -141       C  
ATOM   1070  CD2 LEU A 133       7.919  10.798  -6.480  1.00 20.92           C  
ANISOU 1070  CD2 LEU A 133     2495   2665   2788    -90   -208   -203       C  
ATOM   1071  N   ALA A 134      10.505  12.287 -10.253  1.00 24.21           N  
ANISOU 1071  N   ALA A 134     2956   3139   3104   -169   -289    -45       N  
ATOM   1072  CA  ALA A 134      11.766  13.015 -10.167  1.00 23.20           C  
ANISOU 1072  CA  ALA A 134     2825   3010   2978   -174   -288    -11       C  
ATOM   1073  C   ALA A 134      11.766  14.213 -11.106  1.00 22.88           C  
ANISOU 1073  C   ALA A 134     2768   2965   2960   -200   -345     61       C  
ATOM   1074  O   ALA A 134      12.175  15.303 -10.728  1.00 26.04           O  
ANISOU 1074  O   ALA A 134     3154   3325   3414   -203   -374     89       O  
ATOM   1075  CB  ALA A 134      12.933  12.095 -10.494  1.00 20.05           C  
ANISOU 1075  CB  ALA A 134     2448   2663   2506   -175   -237     -9       C  
ATOM   1076  N   ARG A 135      11.314  14.003 -12.338  1.00 24.86           N  
ANISOU 1076  N   ARG A 135     3025   3256   3166   -223   -366     93       N  
ATOM   1077  CA  ARG A 135      11.261  15.079 -13.319  1.00 27.11           C  
ANISOU 1077  CA  ARG A 135     3293   3544   3464   -253   -423    174       C  
ATOM   1078  C   ARG A 135      10.404  16.242 -12.807  1.00 24.12           C  
ANISOU 1078  C   ARG A 135     2884   3089   3190   -238   -478    187       C  
ATOM   1079  O   ARG A 135      10.734  17.409 -13.007  1.00 22.80           O  
ANISOU 1079  O   ARG A 135     2703   2888   3071   -251   -522    246       O  
ATOM   1080  CB  ARG A 135      10.737  14.563 -14.660  1.00 30.71           C  
ANISOU 1080  CB  ARG A 135     3764   4059   3845   -282   -441    199       C  
ATOM   1081  CG  ARG A 135      11.012  15.498 -15.824  1.00 40.36           C  
ANISOU 1081  CG  ARG A 135     4974   5311   5050   -320   -489    295       C  
ATOM   1082  CD  ARG A 135      11.416  14.723 -17.066  1.00 47.61           C  
ANISOU 1082  CD  ARG A 135     5925   6321   5843   -347   -466    311       C  
ATOM   1083  NE  ARG A 135      10.551  13.568 -17.292  1.00 53.75           N  
ANISOU 1083  NE  ARG A 135     6737   7117   6571   -347   -458    247       N  
ATOM   1084  CZ  ARG A 135      10.990  12.323 -17.467  1.00 54.26           C  
ANISOU 1084  CZ  ARG A 135     6848   7220   6549   -338   -399    187       C  
ATOM   1085  NH1 ARG A 135      12.292  12.063 -17.449  1.00 53.26           N  
ANISOU 1085  NH1 ARG A 135     6733   7128   6376   -321   -336    186       N  
ATOM   1086  NH2 ARG A 135      10.126  11.337 -17.665  1.00 52.89           N  
ANISOU 1086  NH2 ARG A 135     6708   7048   6338   -347   -405    131       N  
ATOM   1087  N   SER A 136       9.317  15.918 -12.119  1.00 22.84           N  
ANISOU 1087  N   SER A 136     2712   2898   3069   -207   -472    132       N  
ATOM   1088  CA  SER A 136       8.439  16.954 -11.594  1.00 27.06           C  
ANISOU 1088  CA  SER A 136     3215   3362   3703   -177   -512    136       C  
ATOM   1089  C   SER A 136       9.143  17.807 -10.553  1.00 26.71           C  
ANISOU 1089  C   SER A 136     3180   3253   3716   -156   -508    115       C  
ATOM   1090  O   SER A 136       8.951  19.017 -10.517  1.00 24.46           O  
ANISOU 1090  O   SER A 136     2884   2903   3508   -146   -556    146       O  
ATOM   1091  CB  SER A 136       7.175  16.342 -11.001  1.00 27.52           C  
ANISOU 1091  CB  SER A 136     3253   3418   3786   -144   -494     83       C  
ATOM   1092  OG  SER A 136       6.596  15.448 -11.931  1.00 38.88           O  
ANISOU 1092  OG  SER A 136     4691   4915   5166   -176   -503     98       O  
ATOM   1093  N   TYR A 137       9.946  17.160  -9.709  1.00 25.86           N  
ANISOU 1093  N   TYR A 137     3094   3160   3572   -151   -456     63       N  
ATOM   1094  CA  TYR A 137      10.671  17.833  -8.636  1.00 21.52           C  
ANISOU 1094  CA  TYR A 137     2559   2557   3062   -139   -455     36       C  
ATOM   1095  C   TYR A 137      11.897  18.548  -9.159  1.00 22.06           C  
ANISOU 1095  C   TYR A 137     2632   2622   3126   -184   -487    103       C  
ATOM   1096  O   TYR A 137      12.412  19.447  -8.508  1.00 25.00           O  
ANISOU 1096  O   TYR A 137     3016   2935   3549   -188   -515    101       O  
ATOM   1097  CB  TYR A 137      11.159  16.821  -7.604  1.00 20.61           C  
ANISOU 1097  CB  TYR A 137     2461   2471   2901   -126   -394    -30       C  
ATOM   1098  CG  TYR A 137      10.080  16.136  -6.804  1.00 24.64           C  
ANISOU 1098  CG  TYR A 137     2964   2982   3416    -86   -357    -96       C  
ATOM   1099  CD1 TYR A 137       8.835  16.723  -6.625  1.00 25.66           C  
ANISOU 1099  CD1 TYR A 137     3071   3071   3608    -51   -376   -110       C  
ATOM   1100  CD2 TYR A 137      10.317  14.900  -6.210  1.00 25.51           C  
ANISOU 1100  CD2 TYR A 137     3085   3135   3471    -82   -301   -138       C  
ATOM   1101  CE1 TYR A 137       7.846  16.088  -5.877  1.00 25.88           C  
ANISOU 1101  CE1 TYR A 137     3081   3112   3640    -16   -337   -161       C  
ATOM   1102  CE2 TYR A 137       9.340  14.261  -5.464  1.00 25.60           C  
ANISOU 1102  CE2 TYR A 137     3087   3153   3488    -52   -268   -187       C  
ATOM   1103  CZ  TYR A 137       8.110  14.859  -5.299  1.00 26.26           C  
ANISOU 1103  CZ  TYR A 137     3141   3206   3629    -21   -284   -197       C  
ATOM   1104  OH  TYR A 137       7.145  14.219  -4.556  1.00 31.84           O  
ANISOU 1104  OH  TYR A 137     3828   3931   4340      6   -246   -237       O  
ATOM   1105  N   GLY A 138      12.392  18.116 -10.314  1.00 23.78           N  
ANISOU 1105  N   GLY A 138     2845   2910   3280   -219   -483    163       N  
ATOM   1106  CA  GLY A 138      13.630  18.651 -10.858  1.00 23.07           C  
ANISOU 1106  CA  GLY A 138     2749   2840   3174   -264   -502    238       C  
ATOM   1107  C   GLY A 138      14.855  18.017 -10.219  1.00 26.48           C  
ANISOU 1107  C   GLY A 138     3187   3312   3564   -269   -453    218       C  
ATOM   1108  O   GLY A 138      15.890  18.667 -10.037  1.00 26.76           O  
ANISOU 1108  O   GLY A 138     3213   3337   3618   -302   -475    262       O  
ATOM   1109  N   ILE A 139      14.745  16.739  -9.870  1.00 25.61           N  
ANISOU 1109  N   ILE A 139     3087   3243   3399   -241   -392    157       N  
ATOM   1110  CA  ILE A 139      15.858  16.041  -9.232  1.00 22.68           C  
ANISOU 1110  CA  ILE A 139     2716   2910   2991   -238   -345    141       C  
ATOM   1111  C   ILE A 139      16.256  14.792 -10.000  1.00 23.34           C  
ANISOU 1111  C   ILE A 139     2803   3076   2989   -228   -285    146       C  
ATOM   1112  O   ILE A 139      15.463  14.257 -10.777  1.00 23.51           O  
ANISOU 1112  O   ILE A 139     2840   3118   2975   -221   -276    132       O  
ATOM   1113  CB  ILE A 139      15.542  15.651  -7.764  1.00 23.99           C  
ANISOU 1113  CB  ILE A 139     2897   3038   3179   -205   -323     58       C  
ATOM   1114  CG1 ILE A 139      14.480  14.547  -7.698  1.00 22.54           C  
ANISOU 1114  CG1 ILE A 139     2726   2868   2968   -171   -284     -2       C  
ATOM   1115  CG2 ILE A 139      15.107  16.872  -6.957  1.00 25.38           C  
ANISOU 1115  CG2 ILE A 139     3081   3129   3433   -204   -376     36       C  
ATOM   1116  CD1 ILE A 139      14.073  14.167  -6.256  1.00 19.20           C  
ANISOU 1116  CD1 ILE A 139     2314   2418   2563   -141   -260    -74       C  
ATOM   1117  N   PRO A 140      17.492  14.318  -9.781  1.00 23.64           N  
ANISOU 1117  N   PRO A 140     2828   3159   2994   -227   -245    164       N  
ATOM   1118  CA  PRO A 140      17.934  13.061 -10.388  1.00 24.82           C  
ANISOU 1118  CA  PRO A 140     2986   3379   3067   -203   -178    157       C  
ATOM   1119  C   PRO A 140      17.213  11.840  -9.811  1.00 22.12           C  
ANISOU 1119  C   PRO A 140     2675   3019   2708   -165   -140     74       C  
ATOM   1120  O   PRO A 140      16.776  11.841  -8.657  1.00 18.96           O  
ANISOU 1120  O   PRO A 140     2280   2573   2352   -154   -149     28       O  
ATOM   1121  CB  PRO A 140      19.434  13.014 -10.050  1.00 28.62           C  
ANISOU 1121  CB  PRO A 140     3432   3903   3540   -206   -150    204       C  
ATOM   1122  CG  PRO A 140      19.811  14.441  -9.755  1.00 27.81           C  
ANISOU 1122  CG  PRO A 140     3303   3766   3499   -253   -217    261       C  
ATOM   1123  CD  PRO A 140      18.594  15.013  -9.090  1.00 25.51           C  
ANISOU 1123  CD  PRO A 140     3039   3387   3266   -252   -266    203       C  
ATOM   1124  N   PHE A 141      17.081  10.812 -10.642  1.00 22.67           N  
ANISOU 1124  N   PHE A 141     2772   3128   2714   -148    -98     55       N  
ATOM   1125  CA  PHE A 141      16.530   9.539 -10.224  1.00 22.36           C  
ANISOU 1125  CA  PHE A 141     2767   3072   2658   -118    -62    -15       C  
ATOM   1126  C   PHE A 141      17.525   8.430 -10.543  1.00 22.87           C  
ANISOU 1126  C   PHE A 141     2844   3181   2664    -83      6    -19       C  
ATOM   1127  O   PHE A 141      18.092   8.376 -11.638  1.00 23.48           O  
ANISOU 1127  O   PHE A 141     2925   3312   2685    -81     30     13       O  
ATOM   1128  CB  PHE A 141      15.199   9.271 -10.925  1.00 19.28           C  
ANISOU 1128  CB  PHE A 141     2408   2668   2251   -131    -87    -46       C  
ATOM   1129  CG  PHE A 141      14.669   7.886 -10.691  1.00 15.79           C  
ANISOU 1129  CG  PHE A 141     2004   2209   1786   -112    -55   -110       C  
ATOM   1130  CD1 PHE A 141      14.544   7.392  -9.405  1.00 15.76           C  
ANISOU 1130  CD1 PHE A 141     1996   2171   1822    -93    -38   -145       C  
ATOM   1131  CD2 PHE A 141      14.314   7.074 -11.754  1.00 18.01           C  
ANISOU 1131  CD2 PHE A 141     2331   2509   2004   -117    -45   -134       C  
ATOM   1132  CE1 PHE A 141      14.066   6.115  -9.180  1.00 21.60           C  
ANISOU 1132  CE1 PHE A 141     2770   2889   2547    -81    -12   -193       C  
ATOM   1133  CE2 PHE A 141      13.832   5.793 -11.538  1.00 21.32           C  
ANISOU 1133  CE2 PHE A 141     2792   2900   2409   -106    -23   -192       C  
ATOM   1134  CZ  PHE A 141      13.705   5.313 -10.249  1.00 20.61           C  
ANISOU 1134  CZ  PHE A 141     2692   2772   2368    -88     -7   -217       C  
ATOM   1135  N   ILE A 142      17.742   7.546  -9.580  1.00 22.20           N  
ANISOU 1135  N   ILE A 142     2766   3076   2594    -53     39    -54       N  
ATOM   1136  CA  ILE A 142      18.684   6.450  -9.755  1.00 23.07           C  
ANISOU 1136  CA  ILE A 142     2886   3216   2663     -8    106    -58       C  
ATOM   1137  C   ILE A 142      18.145   5.197  -9.084  1.00 22.54           C  
ANISOU 1137  C   ILE A 142     2857   3102   2605     18    128   -119       C  
ATOM   1138  O   ILE A 142      17.718   5.233  -7.930  1.00 24.27           O  
ANISOU 1138  O   ILE A 142     3066   3286   2871     10    108   -134       O  
ATOM   1139  CB  ILE A 142      20.081   6.812  -9.196  1.00 30.08           C  
ANISOU 1139  CB  ILE A 142     3717   4140   3571      4    124      1       C  
ATOM   1140  CG1 ILE A 142      20.635   8.033  -9.936  1.00 36.22           C  
ANISOU 1140  CG1 ILE A 142     4455   4964   4342    -30     99     73       C  
ATOM   1141  CG2 ILE A 142      21.045   5.644  -9.324  1.00 30.49           C  
ANISOU 1141  CG2 ILE A 142     3771   4222   3592     63    197      2       C  
ATOM   1142  CD1 ILE A 142      22.081   8.345  -9.630  1.00 39.82           C  
ANISOU 1142  CD1 ILE A 142     4848   5470   4810    -25    117    145       C  
ATOM   1143  N   GLU A 143      18.137   4.097  -9.828  1.00 23.23           N  
ANISOU 1143  N   GLU A 143     2994   3189   2643     47    169   -155       N  
ATOM   1144  CA  GLU A 143      17.744   2.804  -9.284  1.00 26.88           C  
ANISOU 1144  CA  GLU A 143     3497   3600   3115     70    191   -207       C  
ATOM   1145  C   GLU A 143      18.978   2.072  -8.775  1.00 25.91           C  
ANISOU 1145  C   GLU A 143     3359   3487   3000    128    248   -188       C  
ATOM   1146  O   GLU A 143      20.038   2.123  -9.391  1.00 29.05           O  
ANISOU 1146  O   GLU A 143     3738   3934   3366    162    290   -157       O  
ATOM   1147  CB  GLU A 143      16.994   1.976 -10.332  1.00 31.66           C  
ANISOU 1147  CB  GLU A 143     4176   4183   3671     66    194   -262       C  
ATOM   1148  CG  GLU A 143      15.496   2.281 -10.361  1.00 42.50           C  
ANISOU 1148  CG  GLU A 143     5562   5526   5061      8    130   -285       C  
ATOM   1149  CD  GLU A 143      14.735   1.492 -11.409  1.00 51.73           C  
ANISOU 1149  CD  GLU A 143     6803   6675   6177    -11    118   -335       C  
ATOM   1150  OE1 GLU A 143      13.614   1.027 -11.111  1.00 50.60           O  
ANISOU 1150  OE1 GLU A 143     6680   6487   6059    -45     82   -364       O  
ATOM   1151  OE2 GLU A 143      15.250   1.354 -12.537  1.00 60.47           O  
ANISOU 1151  OE2 GLU A 143     7946   7816   7214      5    143   -344       O  
ATOM   1152  N   THR A 144      18.844   1.403  -7.638  1.00 21.37           N  
ANISOU 1152  N   THR A 144     2784   2869   2467    139    251   -199       N  
ATOM   1153  CA  THR A 144      19.996   0.786  -7.007  1.00 17.24           C  
ANISOU 1153  CA  THR A 144     2235   2355   1962    191    295   -168       C  
ATOM   1154  C   THR A 144      19.679  -0.594  -6.466  1.00 19.87           C  
ANISOU 1154  C   THR A 144     2612   2624   2314    219    314   -202       C  
ATOM   1155  O   THR A 144      18.524  -0.998  -6.362  1.00 21.41           O  
ANISOU 1155  O   THR A 144     2850   2769   2516    186    287   -245       O  
ATOM   1156  CB  THR A 144      20.510   1.635  -5.818  1.00 14.36           C  
ANISOU 1156  CB  THR A 144     1801   2017   1638    171    266   -114       C  
ATOM   1157  OG1 THR A 144      19.494   1.704  -4.817  1.00 17.65           O  
ANISOU 1157  OG1 THR A 144     2226   2395   2084    134    226   -138       O  
ATOM   1158  CG2 THR A 144      20.850   3.044  -6.251  1.00 14.39           C  
ANISOU 1158  CG2 THR A 144     1762   2072   1635    136    237    -74       C  
ATOM   1159  N   SER A 145      20.735  -1.307  -6.116  1.00 19.63           N  
ANISOU 1159  N   SER A 145     2564   2596   2299    278    360   -174       N  
ATOM   1160  CA  SER A 145      20.631  -2.546  -5.384  1.00 21.08           C  
ANISOU 1160  CA  SER A 145     2777   2717   2515    307    374   -185       C  
ATOM   1161  C   SER A 145      21.809  -2.557  -4.425  1.00 20.97           C  
ANISOU 1161  C   SER A 145     2695   2738   2536    343    391   -114       C  
ATOM   1162  O   SER A 145      22.953  -2.478  -4.852  1.00 19.78           O  
ANISOU 1162  O   SER A 145     2507   2633   2377    392    431    -77       O  
ATOM   1163  CB  SER A 145      20.728  -3.729  -6.335  1.00 22.34           C  
ANISOU 1163  CB  SER A 145     3009   2826   2652    362    421   -234       C  
ATOM   1164  OG  SER A 145      20.668  -4.943  -5.612  1.00 26.10           O  
ANISOU 1164  OG  SER A 145     3516   3231   3172    390    431   -238       O  
ATOM   1165  N   ALA A 146      21.531  -2.607  -3.129  1.00 21.96           N  
ANISOU 1165  N   ALA A 146     2799   2849   2695    314    358    -89       N  
ATOM   1166  CA  ALA A 146      22.589  -2.655  -2.135  1.00 21.04           C  
ANISOU 1166  CA  ALA A 146     2620   2767   2608    338    362    -18       C  
ATOM   1167  C   ALA A 146      23.146  -4.068  -2.073  1.00 24.31           C  
ANISOU 1167  C   ALA A 146     3053   3134   3050    412    408     -4       C  
ATOM   1168  O   ALA A 146      24.210  -4.306  -1.515  1.00 26.33           O  
ANISOU 1168  O   ALA A 146     3254   3419   3332    454    423     62       O  
ATOM   1169  CB  ALA A 146      22.065  -2.217  -0.773  1.00 19.34           C  
ANISOU 1169  CB  ALA A 146     2382   2559   2406    280    310      0       C  
ATOM   1170  N   LYS A 147      22.418  -5.004  -2.667  1.00 25.47           N  
ANISOU 1170  N   LYS A 147     3278   3205   3194    428    425    -66       N  
ATOM   1171  CA  LYS A 147      22.848  -6.387  -2.710  1.00 26.67           C  
ANISOU 1171  CA  LYS A 147     3466   3290   3378    501    467    -65       C  
ATOM   1172  C   LYS A 147      23.880  -6.613  -3.813  1.00 30.32           C  
ANISOU 1172  C   LYS A 147     3927   3771   3821    587    535    -72       C  
ATOM   1173  O   LYS A 147      24.891  -7.278  -3.583  1.00 33.06           O  
ANISOU 1173  O   LYS A 147     4244   4114   4203    666    576    -26       O  
ATOM   1174  CB  LYS A 147      21.647  -7.310  -2.902  1.00 28.10           C  
ANISOU 1174  CB  LYS A 147     3739   3372   3566    475    451   -130       C  
ATOM   1175  CG  LYS A 147      22.007  -8.777  -3.102  1.00 26.84           C  
ANISOU 1175  CG  LYS A 147     3637   3119   3442    551    491   -144       C  
ATOM   1176  CD  LYS A 147      20.730  -9.598  -3.231  1.00 30.64           C  
ANISOU 1176  CD  LYS A 147     4210   3500   3933    503    459   -203       C  
ATOM   1177  CE  LYS A 147      21.015 -11.089  -3.322  1.00 34.91           C  
ANISOU 1177  CE  LYS A 147     4818   3927   4520    571    488   -217       C  
ATOM   1178  NZ  LYS A 147      19.746 -11.874  -3.317  1.00 37.05           N  
ANISOU 1178  NZ  LYS A 147     5172   4097   4809    507    442   -261       N  
ATOM   1179  N   THR A 148      23.627  -6.059  -5.001  1.00 26.68           N  
ANISOU 1179  N   THR A 148     3496   3338   3305    575    547   -124       N  
ATOM   1180  CA  THR A 148      24.551  -6.188  -6.130  1.00 28.22           C  
ANISOU 1180  CA  THR A 148     3690   3567   3464    655    618   -133       C  
ATOM   1181  C   THR A 148      25.482  -4.980  -6.177  1.00 29.69           C  
ANISOU 1181  C   THR A 148     3774   3871   3636    647    623    -59       C  
ATOM   1182  O   THR A 148      26.555  -5.030  -6.783  1.00 33.09           O  
ANISOU 1182  O   THR A 148     4165   4355   4052    719    687    -29       O  
ATOM   1183  CB  THR A 148      23.815  -6.268  -7.496  1.00 29.45           C  
ANISOU 1183  CB  THR A 148     3937   3699   3552    644    629   -226       C  
ATOM   1184  OG1 THR A 148      23.249  -4.994  -7.812  1.00 32.52           O  
ANISOU 1184  OG1 THR A 148     4303   4150   3902    561    583   -224       O  
ATOM   1185  CG2 THR A 148      22.711  -7.292  -7.475  1.00 26.00           C  
ANISOU 1185  CG2 THR A 148     3603   3147   3128    622    602   -299       C  
ATOM   1186  N   ARG A 149      25.045  -3.899  -5.536  1.00 25.90           N  
ANISOU 1186  N   ARG A 149     3254   3427   3161    559    556    -31       N  
ATOM   1187  CA  ARG A 149      25.746  -2.613  -5.510  1.00 25.74           C  
ANISOU 1187  CA  ARG A 149     3146   3503   3132    526    539     36       C  
ATOM   1188  C   ARG A 149      25.518  -1.777  -6.771  1.00 26.46           C  
ANISOU 1188  C   ARG A 149     3251   3639   3163    499    545     11       C  
ATOM   1189  O   ARG A 149      26.142  -0.726  -6.952  1.00 26.28           O  
ANISOU 1189  O   ARG A 149     3159   3694   3131    473    534     70       O  
ATOM   1190  CB  ARG A 149      27.249  -2.760  -5.221  1.00 31.14           C  
ANISOU 1190  CB  ARG A 149     3739   4248   3844    591    581    125       C  
ATOM   1191  CG  ARG A 149      27.881  -1.448  -4.732  1.00 38.04           C  
ANISOU 1191  CG  ARG A 149     4519   5208   4728    530    534    207       C  
ATOM   1192  CD  ARG A 149      29.404  -1.455  -4.831  1.00 46.47           C  
ANISOU 1192  CD  ARG A 149     5487   6358   5814    589    580    302       C  
ATOM   1193  NE  ARG A 149      29.987  -0.171  -4.442  1.00 45.56           N  
ANISOU 1193  NE  ARG A 149     5285   6320   5707    517    525    382       N  
ATOM   1194  CZ  ARG A 149      30.539   0.069  -3.257  1.00 43.48           C  
ANISOU 1194  CZ  ARG A 149     4956   6080   5484    485    474    453       C  
ATOM   1195  NH1 ARG A 149      31.045   1.265  -2.987  1.00 44.63           N  
ANISOU 1195  NH1 ARG A 149     5033   6288   5635    412    417    519       N  
ATOM   1196  NH2 ARG A 149      30.593  -0.890  -2.342  1.00 39.47           N  
ANISOU 1196  NH2 ARG A 149     4454   5532   5012    522    474    462       N  
ATOM   1197  N   GLN A 150      24.619  -2.224  -7.638  1.00 25.22           N  
ANISOU 1197  N   GLN A 150     3183   3434   2965    498    554    -72       N  
ATOM   1198  CA  GLN A 150      24.255  -1.403  -8.787  1.00 24.76           C  
ANISOU 1198  CA  GLN A 150     3143   3419   2846    461    546    -92       C  
ATOM   1199  C   GLN A 150      23.779  -0.027  -8.339  1.00 24.45           C  
ANISOU 1199  C   GLN A 150     3061   3407   2823    370    470    -58       C  
ATOM   1200  O   GLN A 150      22.876   0.084  -7.513  1.00 24.08           O  
ANISOU 1200  O   GLN A 150     3031   3311   2809    322    416    -81       O  
ATOM   1201  CB  GLN A 150      23.156  -2.064  -9.618  1.00 25.32           C  
ANISOU 1201  CB  GLN A 150     3321   3427   2873    453    544   -187       C  
ATOM   1202  CG  GLN A 150      22.713  -1.212 -10.805  1.00 29.65           C  
ANISOU 1202  CG  GLN A 150     3889   4025   3353    407    527   -202       C  
ATOM   1203  CD  GLN A 150      21.638  -1.867 -11.667  1.00 37.86           C  
ANISOU 1203  CD  GLN A 150     5036   5009   4342    391    516   -293       C  
ATOM   1204  OE1 GLN A 150      21.050  -2.884 -11.297  1.00 33.38           O  
ANISOU 1204  OE1 GLN A 150     4529   4355   3798    399    508   -347       O  
ATOM   1205  NE2 GLN A 150      21.376  -1.272 -12.827  1.00 42.87           N  
ANISOU 1205  NE2 GLN A 150     5692   5694   4904    362    508   -303       N  
ATOM   1206  N   GLY A 151      24.395   1.016  -8.884  1.00 28.13           N  
ANISOU 1206  N   GLY A 151     3470   3950   3267    351    469     -3       N  
ATOM   1207  CA  GLY A 151      23.928   2.377  -8.700  1.00 25.38           C  
ANISOU 1207  CA  GLY A 151     3093   3617   2931    268    398     24       C  
ATOM   1208  C   GLY A 151      24.272   3.060  -7.390  1.00 22.67           C  
ANISOU 1208  C   GLY A 151     2689   3278   2648    231    348     75       C  
ATOM   1209  O   GLY A 151      23.969   4.245  -7.220  1.00 23.65           O  
ANISOU 1209  O   GLY A 151     2793   3408   2786    167    288     95       O  
ATOM   1210  N   VAL A 152      24.901   2.332  -6.471  1.00 21.21           N  
ANISOU 1210  N   VAL A 152     2478   3085   2495    270    368     97       N  
ATOM   1211  CA  VAL A 152      25.172   2.849  -5.123  1.00 22.05           C  
ANISOU 1211  CA  VAL A 152     2537   3193   2647    231    316    138       C  
ATOM   1212  C   VAL A 152      26.105   4.076  -5.102  1.00 27.04           C  
ANISOU 1212  C   VAL A 152     3092   3892   3291    188    283    219       C  
ATOM   1213  O   VAL A 152      25.737   5.133  -4.583  1.00 29.69           O  
ANISOU 1213  O   VAL A 152     3423   4214   3644    121    215    222       O  
ATOM   1214  CB  VAL A 152      25.725   1.737  -4.185  1.00 28.35           C  
ANISOU 1214  CB  VAL A 152     3320   3978   3475    282    343    157       C  
ATOM   1215  CG1 VAL A 152      26.250   2.324  -2.877  1.00 26.06           C  
ANISOU 1215  CG1 VAL A 152     2972   3712   3218    240    288    214       C  
ATOM   1216  CG2 VAL A 152      24.654   0.684  -3.912  1.00 27.09           C  
ANISOU 1216  CG2 VAL A 152     3237   3739   3317    299    351     84       C  
ATOM   1217  N   ASP A 153      27.309   3.935  -5.649  1.00 29.34           N  
ANISOU 1217  N   ASP A 153     3322   4251   3574    228    331    287       N  
ATOM   1218  CA  ASP A 153      28.246   5.059  -5.727  1.00 31.63           C  
ANISOU 1218  CA  ASP A 153     3532   4609   3877    181    299    377       C  
ATOM   1219  C   ASP A 153      27.599   6.232  -6.449  1.00 30.21           C  
ANISOU 1219  C   ASP A 153     3375   4423   3680    116    255    367       C  
ATOM   1220  O   ASP A 153      27.710   7.380  -6.022  1.00 31.79           O  
ANISOU 1220  O   ASP A 153     3548   4623   3910     44    184    404       O  
ATOM   1221  CB  ASP A 153      29.512   4.662  -6.485  1.00 32.65           C  
ANISOU 1221  CB  ASP A 153     3590   4823   3992    242    374    451       C  
ATOM   1222  CG  ASP A 153      30.297   3.577  -5.787  1.00 40.51           C  
ANISOU 1222  CG  ASP A 153     4547   5829   5016    313    416    481       C  
ATOM   1223  OD1 ASP A 153      30.429   3.633  -4.550  1.00 41.32           O  
ANISOU 1223  OD1 ASP A 153     4628   5914   5159    283    362    503       O  
ATOM   1224  OD2 ASP A 153      30.785   2.664  -6.483  1.00 49.27           O  
ANISOU 1224  OD2 ASP A 153     5649   6964   6106    403    504    482       O  
ATOM   1225  N   ASP A 154      26.930   5.922  -7.552  1.00 27.01           N  
ANISOU 1225  N   ASP A 154     3024   4008   3229    140    293    316       N  
ATOM   1226  CA  ASP A 154      26.295   6.923  -8.400  1.00 33.67           C  
ANISOU 1226  CA  ASP A 154     3890   4851   4052     86    256    313       C  
ATOM   1227  C   ASP A 154      25.249   7.742  -7.654  1.00 30.56           C  
ANISOU 1227  C   ASP A 154     3531   4384   3696     23    172    272       C  
ATOM   1228  O   ASP A 154      25.161   8.955  -7.834  1.00 32.25           O  
ANISOU 1228  O   ASP A 154     3729   4597   3929    -37    115    307       O  
ATOM   1229  CB  ASP A 154      25.651   6.243  -9.607  1.00 44.17           C  
ANISOU 1229  CB  ASP A 154     5284   6181   5319    126    308    254       C  
ATOM   1230  CG  ASP A 154      26.261   6.684 -10.910  1.00 60.92           C  
ANISOU 1230  CG  ASP A 154     7374   8386   7387    127    343    313       C  
ATOM   1231  OD1 ASP A 154      27.382   6.223 -11.225  1.00 64.49           O  
ANISOU 1231  OD1 ASP A 154     7776   8909   7819    180    412    363       O  
ATOM   1232  OD2 ASP A 154      25.620   7.495 -11.614  1.00 67.71           O  
ANISOU 1232  OD2 ASP A 154     8256   9245   8226     76    302    316       O  
ATOM   1233  N   ALA A 155      24.451   7.072  -6.827  1.00 27.36           N  
ANISOU 1233  N   ALA A 155     3173   3918   3306     39    167    200       N  
ATOM   1234  CA  ALA A 155      23.412   7.747  -6.056  1.00 23.86           C  
ANISOU 1234  CA  ALA A 155     2761   3410   2893     -7    101    155       C  
ATOM   1235  C   ALA A 155      24.019   8.781  -5.119  1.00 23.03           C  
ANISOU 1235  C   ALA A 155     2613   3307   2829    -58     40    201       C  
ATOM   1236  O   ALA A 155      23.550   9.910  -5.045  1.00 25.45           O  
ANISOU 1236  O   ALA A 155     2930   3580   3161   -107    -20    197       O  
ATOM   1237  CB  ALA A 155      22.579   6.741  -5.271  1.00 20.51           C  
ANISOU 1237  CB  ALA A 155     2383   2936   2473     21    115     84       C  
ATOM   1238  N   PHE A 156      25.069   8.389  -4.408  1.00 20.33           N  
ANISOU 1238  N   PHE A 156     2227   3000   2498    -45     52    246       N  
ATOM   1239  CA  PHE A 156      25.719   9.280  -3.461  1.00 20.66           C  
ANISOU 1239  CA  PHE A 156     2232   3047   2573   -100    -13    290       C  
ATOM   1240  C   PHE A 156      26.513  10.402  -4.135  1.00 28.12           C  
ANISOU 1240  C   PHE A 156     3125   4028   3531   -151    -48    372       C  
ATOM   1241  O   PHE A 156      26.512  11.537  -3.660  1.00 30.44           O  
ANISOU 1241  O   PHE A 156     3420   4291   3857   -216   -123    383       O  
ATOM   1242  CB  PHE A 156      26.634   8.474  -2.538  1.00 21.52           C  
ANISOU 1242  CB  PHE A 156     2299   3191   2686    -75      5    325       C  
ATOM   1243  CG  PHE A 156      25.900   7.755  -1.441  1.00 24.98           C  
ANISOU 1243  CG  PHE A 156     2785   3586   3121    -56      5    259       C  
ATOM   1244  CD1 PHE A 156      25.550   8.418  -0.271  1.00 22.50           C  
ANISOU 1244  CD1 PHE A 156     2492   3240   2817   -105    -59    230       C  
ATOM   1245  CD2 PHE A 156      25.561   6.419  -1.575  1.00 23.95           C  
ANISOU 1245  CD2 PHE A 156     2679   3446   2976      9     69    226       C  
ATOM   1246  CE1 PHE A 156      24.878   7.756   0.746  1.00 22.49           C  
ANISOU 1246  CE1 PHE A 156     2530   3213   2805    -88    -53    177       C  
ATOM   1247  CE2 PHE A 156      24.884   5.750  -0.564  1.00 21.48           C  
ANISOU 1247  CE2 PHE A 156     2404   3097   2662     20     68    179       C  
ATOM   1248  CZ  PHE A 156      24.542   6.417   0.594  1.00 22.13           C  
ANISOU 1248  CZ  PHE A 156     2499   3161   2747    -29     10    157       C  
ATOM   1249  N   TYR A 157      27.199  10.079  -5.230  1.00 27.82           N  
ANISOU 1249  N   TYR A 157     3044   4056   3469   -122      8    430       N  
ATOM   1250  CA  TYR A 157      28.010  11.060  -5.941  1.00 27.83           C  
ANISOU 1250  CA  TYR A 157     2986   4107   3479   -172    -17    525       C  
ATOM   1251  C   TYR A 157      27.137  12.105  -6.602  1.00 24.87           C  
ANISOU 1251  C   TYR A 157     2653   3686   3111   -219    -64    507       C  
ATOM   1252  O   TYR A 157      27.433  13.299  -6.555  1.00 22.02           O  
ANISOU 1252  O   TYR A 157     2269   3311   2786   -290   -135    561       O  
ATOM   1253  CB  TYR A 157      28.869  10.388  -7.008  1.00 32.48           C  
ANISOU 1253  CB  TYR A 157     3522   4790   4030   -118     70    587       C  
ATOM   1254  CG  TYR A 157      29.980   9.555  -6.437  1.00 41.33           C  
ANISOU 1254  CG  TYR A 157     4578   5967   5159    -73    112    635       C  
ATOM   1255  CD1 TYR A 157      30.077   9.347  -5.069  1.00 44.79           C  
ANISOU 1255  CD1 TYR A 157     5016   6372   5631    -85     70    619       C  
ATOM   1256  CD2 TYR A 157      30.940   8.990  -7.260  1.00 46.64           C  
ANISOU 1256  CD2 TYR A 157     5185   6732   5805    -17    194    702       C  
ATOM   1257  CE1 TYR A 157      31.089   8.587  -4.535  1.00 49.06           C  
ANISOU 1257  CE1 TYR A 157     5491   6965   6183    -44    102    674       C  
ATOM   1258  CE2 TYR A 157      31.961   8.236  -6.735  1.00 53.05           C  
ANISOU 1258  CE2 TYR A 157     5929   7595   6634     32    233    754       C  
ATOM   1259  CZ  TYR A 157      32.030   8.034  -5.371  1.00 55.23           C  
ANISOU 1259  CZ  TYR A 157     6204   7833   6950     16    183    743       C  
ATOM   1260  OH  TYR A 157      33.046   7.279  -4.836  1.00 62.68           O  
ANISOU 1260  OH  TYR A 157     7073   8827   7914     65    215    806       O  
ATOM   1261  N   THR A 158      26.068  11.642  -7.235  1.00 19.22           N  
ANISOU 1261  N   THR A 158     1997   2942   2363   -181    -31    437       N  
ATOM   1262  CA  THR A 158      25.109  12.542  -7.848  1.00 26.99           C  
ANISOU 1262  CA  THR A 158     3020   3880   3355   -218    -77    419       C  
ATOM   1263  C   THR A 158      24.558  13.510  -6.806  1.00 29.55           C  
ANISOU 1263  C   THR A 158     3372   4119   3739   -265   -161    385       C  
ATOM   1264  O   THR A 158      24.376  14.700  -7.078  1.00 30.82           O  
ANISOU 1264  O   THR A 158     3534   4243   3934   -318   -224    416       O  
ATOM   1265  CB  THR A 158      23.956  11.761  -8.475  1.00 26.23           C  
ANISOU 1265  CB  THR A 158     2985   3765   3218   -171    -36    341       C  
ATOM   1266  OG1 THR A 158      24.478  10.860  -9.461  1.00 25.91           O  
ANISOU 1266  OG1 THR A 158     2932   3798   3115   -124     44    361       O  
ATOM   1267  CG2 THR A 158      22.971  12.710  -9.123  1.00 23.28           C  
ANISOU 1267  CG2 THR A 158     2640   3348   2856   -209    -88    336       C  
ATOM   1268  N   LEU A 159      24.295  12.999  -5.608  1.00 25.48           N  
ANISOU 1268  N   LEU A 159     2880   3568   3232   -245   -161    321       N  
ATOM   1269  CA  LEU A 159      23.783  13.852  -4.545  1.00 23.52           C  
ANISOU 1269  CA  LEU A 159     2665   3244   3027   -281   -231    276       C  
ATOM   1270  C   LEU A 159      24.790  14.958  -4.248  1.00 27.41           C  
ANISOU 1270  C   LEU A 159     3121   3736   3558   -351   -301    349       C  
ATOM   1271  O   LEU A 159      24.427  16.130  -4.191  1.00 29.45           O  
ANISOU 1271  O   LEU A 159     3403   3928   3857   -396   -369    345       O  
ATOM   1272  CB  LEU A 159      23.467  13.046  -3.284  1.00 16.18           C  
ANISOU 1272  CB  LEU A 159     1761   2298   2087   -249   -213    206       C  
ATOM   1273  CG  LEU A 159      22.906  13.913  -2.157  1.00 18.77           C  
ANISOU 1273  CG  LEU A 159     2131   2554   2446   -279   -277    149       C  
ATOM   1274  CD1 LEU A 159      21.710  14.707  -2.648  1.00 14.16           C  
ANISOU 1274  CD1 LEU A 159     1586   1904   1890   -279   -302    106       C  
ATOM   1275  CD2 LEU A 159      22.539  13.059  -0.940  1.00 18.33           C  
ANISOU 1275  CD2 LEU A 159     2100   2497   2367   -247   -251     84       C  
ATOM   1276  N   VAL A 160      26.058  14.584  -4.073  1.00 27.78           N  
ANISOU 1276  N   VAL A 160     3107   3853   3595   -361   -286    420       N  
ATOM   1277  CA  VAL A 160      27.124  15.564  -3.885  1.00 24.86           C  
ANISOU 1277  CA  VAL A 160     2689   3495   3261   -437   -355    507       C  
ATOM   1278  C   VAL A 160      27.115  16.613  -4.999  1.00 27.09           C  
ANISOU 1278  C   VAL A 160     2959   3767   3568   -484   -390    571       C  
ATOM   1279  O   VAL A 160      27.262  17.813  -4.743  1.00 29.28           O  
ANISOU 1279  O   VAL A 160     3244   3987   3894   -556   -477    598       O  
ATOM   1280  CB  VAL A 160      28.518  14.908  -3.846  1.00 23.09           C  
ANISOU 1280  CB  VAL A 160     2380   3371   3022   -433   -320    597       C  
ATOM   1281  CG1 VAL A 160      29.607  15.983  -3.850  1.00 23.37           C  
ANISOU 1281  CG1 VAL A 160     2354   3427   3098   -524   -396    706       C  
ATOM   1282  CG2 VAL A 160      28.659  14.018  -2.628  1.00 21.05           C  
ANISOU 1282  CG2 VAL A 160     2128   3119   2750   -401   -306    553       C  
ATOM   1283  N   ARG A 161      26.933  16.156  -6.234  1.00 22.96           N  
ANISOU 1283  N   ARG A 161     2421   3296   3007   -445   -325    596       N  
ATOM   1284  CA  ARG A 161      26.886  17.060  -7.375  1.00 26.83           C  
ANISOU 1284  CA  ARG A 161     2897   3789   3509   -487   -352    666       C  
ATOM   1285  C   ARG A 161      25.694  18.005  -7.303  1.00 29.88           C  
ANISOU 1285  C   ARG A 161     3351   4062   3938   -508   -418    608       C  
ATOM   1286  O   ARG A 161      25.793  19.159  -7.719  1.00 34.35           O  
ANISOU 1286  O   ARG A 161     3911   4593   4549   -570   -485    671       O  
ATOM   1287  CB  ARG A 161      26.877  16.279  -8.690  1.00 29.49           C  
ANISOU 1287  CB  ARG A 161     3215   4212   3779   -435   -264    692       C  
ATOM   1288  CG  ARG A 161      28.221  15.642  -9.003  1.00 34.38           C  
ANISOU 1288  CG  ARG A 161     3751   4948   4365   -418   -200    778       C  
ATOM   1289  CD  ARG A 161      28.192  14.784 -10.260  1.00 39.04           C  
ANISOU 1289  CD  ARG A 161     4335   5621   4876   -355   -102    784       C  
ATOM   1290  NE  ARG A 161      29.469  14.097 -10.444  1.00 43.69           N  
ANISOU 1290  NE  ARG A 161     4845   6320   5437   -320    -30    856       N  
ATOM   1291  CZ  ARG A 161      29.613  12.777 -10.526  1.00 43.48           C  
ANISOU 1291  CZ  ARG A 161     4822   6335   5362   -230     63    809       C  
ATOM   1292  NH1 ARG A 161      30.822  12.256 -10.682  1.00 45.75           N  
ANISOU 1292  NH1 ARG A 161     5029   6722   5634   -194    128    884       N  
ATOM   1293  NH2 ARG A 161      28.554  11.978 -10.461  1.00 41.14           N  
ANISOU 1293  NH2 ARG A 161     4610   5982   5039   -176     91    693       N  
ATOM   1294  N   GLU A 162      24.574  17.519  -6.770  1.00 27.39           N  
ANISOU 1294  N   GLU A 162     3097   3693   3616   -456   -400    495       N  
ATOM   1295  CA  GLU A 162      23.376  18.344  -6.618  1.00 26.39           C  
ANISOU 1295  CA  GLU A 162     3030   3463   3534   -461   -454    435       C  
ATOM   1296  C   GLU A 162      23.589  19.457  -5.586  1.00 28.07           C  
ANISOU 1296  C   GLU A 162     3265   3588   3811   -515   -542    423       C  
ATOM   1297  O   GLU A 162      23.180  20.599  -5.798  1.00 24.28           O  
ANISOU 1297  O   GLU A 162     2810   3027   3387   -549   -609    435       O  
ATOM   1298  CB  GLU A 162      22.165  17.481  -6.250  1.00 22.99           C  
ANISOU 1298  CB  GLU A 162     2647   3010   3080   -391   -406    325       C  
ATOM   1299  CG  GLU A 162      21.622  16.654  -7.419  1.00 22.04           C  
ANISOU 1299  CG  GLU A 162     2525   2944   2907   -349   -344    326       C  
ATOM   1300  CD  GLU A 162      21.116  17.526  -8.563  1.00 28.11           C  
ANISOU 1300  CD  GLU A 162     3295   3693   3692   -376   -382    377       C  
ATOM   1301  OE1 GLU A 162      20.096  18.229  -8.376  1.00 28.46           O  
ANISOU 1301  OE1 GLU A 162     3372   3655   3786   -374   -429    338       O  
ATOM   1302  OE2 GLU A 162      21.736  17.505  -9.650  1.00 30.42           O  
ANISOU 1302  OE2 GLU A 162     3553   4057   3948   -394   -364    459       O  
ATOM   1303  N   ILE A 163      24.235  19.113  -4.477  1.00 28.94           N  
ANISOU 1303  N   ILE A 163     3372   3712   3913   -523   -545    400       N  
ATOM   1304  CA  ILE A 163      24.619  20.093  -3.466  1.00 31.08           C  
ANISOU 1304  CA  ILE A 163     3669   3911   4230   -584   -633    389       C  
ATOM   1305  C   ILE A 163      25.507  21.199  -4.059  1.00 36.37           C  
ANISOU 1305  C   ILE A 163     4301   4570   4948   -671   -707    503       C  
ATOM   1306  O   ILE A 163      25.245  22.389  -3.870  1.00 34.84           O  
ANISOU 1306  O   ILE A 163     4150   4273   4815   -717   -790    494       O  
ATOM   1307  CB  ILE A 163      25.335  19.407  -2.288  1.00 30.12           C  
ANISOU 1307  CB  ILE A 163     3535   3832   4075   -586   -624    367       C  
ATOM   1308  CG1 ILE A 163      24.404  18.366  -1.653  1.00 30.00           C  
ANISOU 1308  CG1 ILE A 163     3560   3822   4018   -506   -557    261       C  
ATOM   1309  CG2 ILE A 163      25.808  20.441  -1.265  1.00 23.99           C  
ANISOU 1309  CG2 ILE A 163     2791   2987   3338   -660   -724    356       C  
ATOM   1310  CD1 ILE A 163      25.059  17.503  -0.590  1.00 29.47           C  
ANISOU 1310  CD1 ILE A 163     3477   3810   3911   -499   -537    250       C  
ATOM   1311  N   ARG A 164      26.551  20.802  -4.781  1.00 39.29           N  
ANISOU 1311  N   ARG A 164     4589   5045   5292   -692   -675    613       N  
ATOM   1312  CA  ARG A 164      27.413  21.763  -5.468  1.00 39.64           C  
ANISOU 1312  CA  ARG A 164     4583   5099   5377   -778   -735    741       C  
ATOM   1313  C   ARG A 164      26.626  22.742  -6.335  1.00 40.22           C  
ANISOU 1313  C   ARG A 164     4689   5096   5495   -795   -777    760       C  
ATOM   1314  O   ARG A 164      26.840  23.949  -6.254  1.00 41.51           O  
ANISOU 1314  O   ARG A 164     4867   5177   5726   -871   -873    804       O  
ATOM   1315  CB  ARG A 164      28.439  21.045  -6.338  1.00 38.20           C  
ANISOU 1315  CB  ARG A 164     4304   5062   5149   -773   -666    854       C  
ATOM   1316  CG  ARG A 164      29.537  20.337  -5.582  1.00 40.50           C  
ANISOU 1316  CG  ARG A 164     4537   5432   5418   -777   -645    883       C  
ATOM   1317  CD  ARG A 164      30.415  19.620  -6.587  1.00 45.34           C  
ANISOU 1317  CD  ARG A 164     5054   6186   5987   -752   -561    989       C  
ATOM   1318  NE  ARG A 164      31.505  18.861  -5.984  1.00 45.35           N  
ANISOU 1318  NE  ARG A 164     4984   6275   5972   -742   -530   1032       N  
ATOM   1319  CZ  ARG A 164      32.136  17.874  -6.610  1.00 45.01           C  
ANISOU 1319  CZ  ARG A 164     4869   6352   5882   -680   -431   1086       C  
ATOM   1320  NH1 ARG A 164      31.763  17.532  -7.836  1.00 43.65           N  
ANISOU 1320  NH1 ARG A 164     4697   6225   5663   -628   -353   1093       N  
ATOM   1321  NH2 ARG A 164      33.124  17.221  -6.015  1.00 46.66           N  
ANISOU 1321  NH2 ARG A 164     5007   6634   6087   -667   -408   1131       N  
ATOM   1322  N   LYS A 165      25.725  22.223  -7.169  1.00 39.16           N  
ANISOU 1322  N   LYS A 165     4568   4986   5325   -728   -712    730       N  
ATOM   1323  CA  LYS A 165      24.926  23.070  -8.055  1.00 36.92           C  
ANISOU 1323  CA  LYS A 165     4309   4640   5078   -739   -750    757       C  
ATOM   1324  C   LYS A 165      24.051  24.037  -7.273  1.00 38.28           C  
ANISOU 1324  C   LYS A 165     4559   4658   5327   -742   -828    674       C  
ATOM   1325  O   LYS A 165      23.826  25.167  -7.701  1.00 41.50           O  
ANISOU 1325  O   LYS A 165     4983   4984   5802   -785   -901    723       O  
ATOM   1326  CB  LYS A 165      24.041  22.232  -8.978  1.00 36.84           C  
ANISOU 1326  CB  LYS A 165     4304   4686   5007   -666   -670    728       C  
ATOM   1327  CG  LYS A 165      24.808  21.339  -9.936  1.00 44.58           C  
ANISOU 1327  CG  LYS A 165     5220   5812   5907   -653   -589    803       C  
ATOM   1328  CD  LYS A 165      23.944  20.907 -11.117  1.00 48.87           C  
ANISOU 1328  CD  LYS A 165     5777   6396   6396   -610   -541    798       C  
ATOM   1329  CE  LYS A 165      22.656  20.256 -10.665  1.00 52.20           C  
ANISOU 1329  CE  LYS A 165     6259   6766   6808   -539   -514    667       C  
ATOM   1330  NZ  LYS A 165      21.890  19.700 -11.816  1.00 54.86           N  
ANISOU 1330  NZ  LYS A 165     6608   7154   7083   -503   -470    664       N  
ATOM   1331  N   HIS A 166      23.543  23.584  -6.134  1.00 36.16           N  
ANISOU 1331  N   HIS A 166     4340   4352   5049   -693   -809    550       N  
ATOM   1332  CA  HIS A 166      22.711  24.427  -5.289  1.00 35.18           C  
ANISOU 1332  CA  HIS A 166     4291   4089   4986   -682   -868    456       C  
ATOM   1333  C   HIS A 166      23.546  25.526  -4.628  1.00 39.97           C  
ANISOU 1333  C   HIS A 166     4919   4614   5653   -769   -970    485       C  
ATOM   1334  O   HIS A 166      23.086  26.653  -4.492  1.00 43.82           O  
ANISOU 1334  O   HIS A 166     5461   4973   6216   -788  -1045    464       O  
ATOM   1335  CB  HIS A 166      21.977  23.579  -4.243  1.00 34.26           C  
ANISOU 1335  CB  HIS A 166     4216   3972   4829   -605   -810    322       C  
ATOM   1336  CG  HIS A 166      21.103  24.371  -3.319  1.00 36.11           C  
ANISOU 1336  CG  HIS A 166     4528   4077   5114   -580   -855    215       C  
ATOM   1337  ND1 HIS A 166      21.391  24.534  -1.982  1.00 37.65           N  
ANISOU 1337  ND1 HIS A 166     4771   4231   5304   -594   -884    138       N  
ATOM   1338  CD2 HIS A 166      19.945  25.040  -3.539  1.00 41.24           C  
ANISOU 1338  CD2 HIS A 166     5217   4634   5820   -537   -872    173       C  
ATOM   1339  CE1 HIS A 166      20.449  25.270  -1.415  1.00 41.81           C  
ANISOU 1339  CE1 HIS A 166     5368   4644   5876   -556   -911     44       C  
ATOM   1340  NE2 HIS A 166      19.563  25.592  -2.340  1.00 45.18           N  
ANISOU 1340  NE2 HIS A 166     5786   5035   6346   -518   -904     66       N  
ATOM   1341  N   LYS A 167      24.771  25.203  -4.221  1.00 41.64           N  
ANISOU 1341  N   LYS A 167     5088   4897   5835   -824   -978    534       N  
ATOM   1342  CA  LYS A 167      25.672  26.220  -3.681  1.00 48.36           C  
ANISOU 1342  CA  LYS A 167     5950   5682   6741   -925  -1085    579       C  
ATOM   1343  C   LYS A 167      25.999  27.243  -4.759  1.00 54.86           C  
ANISOU 1343  C   LYS A 167     6743   6470   7630   -998  -1150    708       C  
ATOM   1344  O   LYS A 167      26.024  28.448  -4.505  1.00 53.58           O  
ANISOU 1344  O   LYS A 167     6631   6179   7548  -1060  -1253    715       O  
ATOM   1345  CB  LYS A 167      26.969  25.594  -3.171  1.00 46.75           C  
ANISOU 1345  CB  LYS A 167     5685   5584   6493   -972  -1079    632       C  
ATOM   1346  CG  LYS A 167      26.853  24.825  -1.865  1.00 45.95           C  
ANISOU 1346  CG  LYS A 167     5621   5498   6338   -929  -1048    517       C  
ATOM   1347  CD  LYS A 167      28.213  24.259  -1.488  1.00 46.64           C  
ANISOU 1347  CD  LYS A 167     5634   5696   6392   -981  -1051    597       C  
ATOM   1348  CE  LYS A 167      28.255  23.739  -0.064  1.00 47.37           C  
ANISOU 1348  CE  LYS A 167     5768   5791   6439   -966  -1054    500       C  
ATOM   1349  NZ  LYS A 167      29.629  23.260   0.277  1.00 49.68           N  
ANISOU 1349  NZ  LYS A 167     5978   6191   6708  -1023  -1068    594       N  
ATOM   1350  N   GLU A 168      26.267  26.743  -5.962  1.00 59.62           N  
ANISOU 1350  N   GLU A 168     7268   7189   8197   -990  -1089    813       N  
ATOM   1351  CA  GLU A 168      26.526  27.588  -7.118  1.00 63.31           C  
ANISOU 1351  CA  GLU A 168     7696   7648   8709  -1054  -1136    949       C  
ATOM   1352  C   GLU A 168      25.337  28.504  -7.335  1.00 64.70           C  
ANISOU 1352  C   GLU A 168     7947   7680   8957  -1030  -1187    903       C  
ATOM   1353  O   GLU A 168      25.486  29.721  -7.441  1.00 64.46           O  
ANISOU 1353  O   GLU A 168     7939   7540   9013  -1102  -1289    961       O  
ATOM   1354  CB  GLU A 168      26.748  26.725  -8.359  1.00 67.57           C  
ANISOU 1354  CB  GLU A 168     8155   8345   9173  -1023  -1040   1037       C  
ATOM   1355  CG  GLU A 168      27.113  27.504  -9.610  1.00 74.95           C  
ANISOU 1355  CG  GLU A 168     9038   9303  10136  -1093  -1078   1195       C  
ATOM   1356  CD  GLU A 168      28.569  27.933  -9.626  1.00 80.51           C  
ANISOU 1356  CD  GLU A 168     9667  10062  10862  -1201  -1128   1334       C  
ATOM   1357  OE1 GLU A 168      29.423  27.151  -9.155  1.00 80.92           O  
ANISOU 1357  OE1 GLU A 168     9666  10214  10866  -1198  -1081   1338       O  
ATOM   1358  OE2 GLU A 168      28.858  29.052 -10.105  1.00 82.74           O  
ANISOU 1358  OE2 GLU A 168     9937  10288  11214  -1291  -1216   1447       O  
ATOM   1359  N   LYS A 169      24.153  27.901  -7.396  1.00 66.12           N  
ANISOU 1359  N   LYS A 169     8159   7858   9104   -928  -1119    804       N  
ATOM   1360  CA  LYS A 169      22.906  28.643  -7.520  1.00 69.76           C  
ANISOU 1360  CA  LYS A 169     8683   8191   9632   -884  -1155    750       C  
ATOM   1361  C   LYS A 169      22.767  29.625  -6.357  1.00 73.03           C  
ANISOU 1361  C   LYS A 169     9181   8440  10127   -903  -1242    664       C  
ATOM   1362  O   LYS A 169      22.772  30.830  -6.570  1.00 74.80           O  
ANISOU 1362  O   LYS A 169     9435   8544  10443   -955  -1336    714       O  
ATOM   1363  CB  LYS A 169      21.714  27.683  -7.563  1.00 71.17           C  
ANISOU 1363  CB  LYS A 169     8876   8410   9757   -772  -1063    649       C  
ATOM   1364  CG  LYS A 169      20.495  28.213  -8.305  1.00 74.66           C  
ANISOU 1364  CG  LYS A 169     9336   8782  10248   -728  -1080    654       C  
ATOM   1365  CD  LYS A 169      19.393  27.164  -8.358  1.00 78.02           C  
ANISOU 1365  CD  LYS A 169     9763   9264  10615   -630   -991    566       C  
ATOM   1366  CE  LYS A 169      18.212  27.621  -9.206  1.00 81.73           C  
ANISOU 1366  CE  LYS A 169    10236   9687  11131   -591  -1010    590       C  
ATOM   1367  NZ  LYS A 169      17.282  28.513  -8.454  1.00 83.62           N  
ANISOU 1367  NZ  LYS A 169    10535   9771  11467   -544  -1057    506       N  
ATOM   1368  N   MET A 170      22.653  29.102  -5.136  1.00 73.73           N  
ANISOU 1368  N   MET A 170     9313   8524  10178   -862  -1212    535       N  
ATOM   1369  CA  MET A 170      22.573  29.923  -3.921  1.00 75.42           C  
ANISOU 1369  CA  MET A 170     9616   8596  10445   -877  -1286    435       C  
ATOM   1370  C   MET A 170      23.399  31.207  -3.996  1.00 81.37           C  
ANISOU 1370  C   MET A 170    10388   9244  11285   -992  -1412    521       C  
ATOM   1371  O   MET A 170      22.899  32.290  -3.693  1.00 81.71           O  
ANISOU 1371  O   MET A 170    10510   9123  11415   -992  -1488    472       O  
ATOM   1372  CB  MET A 170      23.006  29.113  -2.696  1.00 73.20           C  
ANISOU 1372  CB  MET A 170     9350   8375  10088   -868  -1250    344       C  
ATOM   1373  CG  MET A 170      21.975  28.116  -2.204  1.00 71.69           C  
ANISOU 1373  CG  MET A 170     9176   8229   9833   -753  -1148    221       C  
ATOM   1374  SD  MET A 170      20.895  28.815  -0.948  1.00 99.07           S  
ANISOU 1374  SD  MET A 170    12762  11543  13338   -687  -1172     47       S  
ATOM   1375  CE  MET A 170      22.074  29.148   0.360  1.00 77.65           C  
ANISOU 1375  CE  MET A 170    10101   8802  10602   -779  -1251      9       C  
ATOM   1376  N   SER A 171      24.665  31.081  -4.387  1.00 86.43           N  
ANISOU 1376  N   SER A 171    10954   9978  11906  -1088  -1435    650       N  
ATOM   1377  CA  SER A 171      25.537  32.243  -4.533  1.00 92.36           C  
ANISOU 1377  CA  SER A 171    11708  10646  12740  -1213  -1558    755       C  
ATOM   1378  C   SER A 171      24.917  33.251  -5.488  1.00100.52           C  
ANISOU 1378  C   SER A 171    12758  11571  13866  -1218  -1611    824       C  
ATOM   1379  O   SER A 171      24.727  34.411  -5.138  1.00103.38           O  
ANISOU 1379  O   SER A 171    13199  11757  14325  -1254  -1713    798       O  
ATOM   1380  CB  SER A 171      26.918  31.831  -5.047  1.00 90.61           C  
ANISOU 1380  CB  SER A 171    11376  10575  12478  -1305  -1554    910       C  
ATOM   1381  OG  SER A 171      27.594  31.016  -4.107  1.00 89.08           O  
ANISOU 1381  OG  SER A 171    11164  10468  12214  -1310  -1524    861       O  
ATOM   1382  N   LYS A 172      24.598  32.789  -6.692  1.00106.19           N  
ANISOU 1382  N   LYS A 172    13404  12390  14551  -1182  -1543    911       N  
ATOM   1383  CA  LYS A 172      24.037  33.636  -7.738  1.00114.29           C  
ANISOU 1383  CA  LYS A 172    14430  13342  15654  -1189  -1589   1001       C  
ATOM   1384  C   LYS A 172      22.527  33.788  -7.590  1.00121.54           C  
ANISOU 1384  C   LYS A 172    15416  14155  16608  -1072  -1566    880       C  
ATOM   1385  O   LYS A 172      21.903  34.601  -8.273  1.00121.40           O  
ANISOU 1385  O   LYS A 172    15413  14044  16671  -1064  -1615    935       O  
ATOM   1386  CB  LYS A 172      24.344  33.033  -9.107  1.00113.55           C  
ANISOU 1386  CB  LYS A 172    14232  13419  15494  -1202  -1524   1145       C  
ATOM   1387  CG  LYS A 172      25.741  32.448  -9.234  1.00113.66           C  
ANISOU 1387  CG  LYS A 172    14157  13589  15438  -1278  -1497   1244       C  
ATOM   1388  CD  LYS A 172      25.903  31.653 -10.524  1.00113.13           C  
ANISOU 1388  CD  LYS A 172    13997  13703  15282  -1260  -1404   1352       C  
ATOM   1389  CE  LYS A 172      25.520  32.472 -11.749  1.00114.38           C  
ANISOU 1389  CE  LYS A 172    14140  13830  15488  -1292  -1450   1479       C  
ATOM   1390  NZ  LYS A 172      24.046  32.527 -11.972  1.00114.81           N  
ANISOU 1390  NZ  LYS A 172    14253  13806  15563  -1196  -1436   1393       N  
ATOM   1391  N   ASP A 173      21.948  33.000  -6.690  1.00128.21           N  
ANISOU 1391  N   ASP A 173    16297  15022  17396   -980  -1492    725       N  
ATOM   1392  CA  ASP A 173      20.505  32.969  -6.494  1.00134.80           C  
ANISOU 1392  CA  ASP A 173    17180  15787  18252   -860  -1451    610       C  
ATOM   1393  C   ASP A 173      20.058  34.067  -5.540  1.00141.78           C  
ANISOU 1393  C   ASP A 173    18169  16468  19233   -841  -1528    504       C  
ATOM   1394  O   ASP A 173      20.614  34.227  -4.452  1.00142.74           O  
ANISOU 1394  O   ASP A 173    18346  16542  19347   -876  -1562    425       O  
ATOM   1395  CB  ASP A 173      20.065  31.599  -5.969  1.00134.04           C  
ANISOU 1395  CB  ASP A 173    17070  15812  18049   -773  -1334    499       C  
ATOM   1396  CG  ASP A 173      19.147  30.871  -6.932  1.00134.04           C  
ANISOU 1396  CG  ASP A 173    17018  15903  18008   -700  -1255    523       C  
ATOM   1397  OD1 ASP A 173      18.662  29.777  -6.574  1.00133.67           O  
ANISOU 1397  OD1 ASP A 173    16962  15943  17885   -629  -1164    438       O  
ATOM   1398  OD2 ASP A 173      18.912  31.393  -8.044  1.00134.40           O  
ANISOU 1398  OD2 ASP A 173    17034  15934  18097   -719  -1290    632       O  
ATOM   1399  N   GLY A 174      19.050  34.825  -5.956  1.00146.99           N  
ANISOU 1399  N   GLY A 174    18857  17009  19983   -784  -1558    503       N  
ATOM   1400  CA  GLY A 174      18.419  34.624  -7.248  1.00150.38           C  
ANISOU 1400  CA  GLY A 174    19218  17505  20415   -753  -1527    606       C  
ATOM   1401  C   GLY A 174      17.759  35.908  -7.700  1.00154.92           C  
ANISOU 1401  C   GLY A 174    19829  17909  21127   -739  -1613    652       C  
ATOM   1402  O   GLY A 174      17.625  36.174  -8.895  1.00154.82           O  
ANISOU 1402  O   GLY A 174    19762  17919  21141   -765  -1639    791       O  
ATOM   1403  N   LYS A 175      17.346  36.706  -6.724  1.00159.61           N  
ANISOU 1403  N   LYS A 175    20516  18325  21802   -695  -1658    534       N  
ATOM   1404  CA  LYS A 175      16.773  38.016  -6.983  1.00164.71           C  
ANISOU 1404  CA  LYS A 175    21212  18777  22595   -676  -1747    563       C  
ATOM   1405  C   LYS A 175      17.381  39.024  -6.016  1.00169.92           C  
ANISOU 1405  C   LYS A 175    21976  19255  23329   -731  -1844    496       C  
ATOM   1406  O   LYS A 175      17.436  40.221  -6.302  1.00172.72           O  
ANISOU 1406  O   LYS A 175    22375  19441  23810   -771  -1951    560       O  
ATOM   1407  CB  LYS A 175      15.261  37.973  -6.832  1.00164.33           C  
ANISOU 1407  CB  LYS A 175    21176  18679  22583   -524  -1690    466       C  
ATOM   1408  N   LYS A 176      17.847  38.526  -4.874  1.00170.94           N  
ANISOU 1408  N   LYS A 176    22149  19420  23379   -738  -1812    370       N  
ATOM   1409  CA  LYS A 176      18.408  39.380  -3.834  1.00172.46           C  
ANISOU 1409  CA  LYS A 176    22453  19452  23623   -791  -1902    284       C  
ATOM   1410  C   LYS A 176      19.935  39.385  -3.825  1.00173.54           C  
ANISOU 1410  C   LYS A 176    22567  19644  23725   -954  -1972    381       C  
ATOM   1411  O   LYS A 176      20.549  39.223  -2.771  1.00174.31           O  
ANISOU 1411  O   LYS A 176    22717  19742  23769   -994  -1986    287       O  
ATOM   1412  CB  LYS A 176      17.866  38.981  -2.464  1.00171.32           C  
ANISOU 1412  CB  LYS A 176    22386  19292  23417   -691  -1833     72       C  
ATOM   1413  N   LYS A 177      20.528  39.559  -5.005  1.00173.73           N  
ANISOU 1413  N   LYS A 177    22508  19725  23777  -1048  -2015    575       N  
ATOM   1414  CA  LYS A 177      21.967  39.817  -5.151  1.00174.17           C  
ANISOU 1414  CA  LYS A 177    22532  19812  23832  -1212  -2099    700       C  
ATOM   1415  C   LYS A 177      22.469  39.658  -6.615  1.00166.20           C  
ANISOU 1415  C   LYS A 177    21399  18935  22815  -1287  -2097    922       C  
ATOM   1416  O   LYS A 177      22.104  40.491  -7.446  1.00167.50           O  
ANISOU 1416  O   LYS A 177    21562  19003  23078  -1299  -2158   1024       O  
ATOM   1417  CB  LYS A 177      22.792  39.034  -4.124  1.00173.13           C  
ANISOU 1417  CB  LYS A 177    22404  19787  23592  -1252  -2069    618       C  
ATOM   1418  N   LYS A 178      23.266  38.643  -6.975  1.00164.39           N  
ANISOU 1418  N   LYS A 178    21067  18920  22472  -1332  -2029   1000       N  
ATOM   1419  CA  LYS A 178      23.734  37.566  -6.111  1.00162.60           C  
ANISOU 1419  CA  LYS A 178    20827  18826  22128  -1317  -1953    904       C  
ATOM   1420  C   LYS A 178      25.140  37.088  -6.477  1.00161.43           C  
ANISOU 1420  C   LYS A 178    20576  18842  21917  -1435  -1953   1047       C  
ATOM   1421  O   LYS A 178      25.815  36.478  -5.644  1.00160.58           O  
ANISOU 1421  O   LYS A 178    20462  18810  21740  -1458  -1932    991       O  
ATOM   1422  CB  LYS A 178      22.750  36.412  -6.112  1.00161.40           C  
ANISOU 1422  CB  LYS A 178    20653  18788  21885  -1175  -1813    802       C  
ATOM   1423  N   LYS A 179      25.562  37.362  -7.715  1.00161.14           N  
ANISOU 1423  N   LYS A 179    20455  18866  21903  -1504  -1974   1235       N  
ATOM   1424  CA  LYS A 179      26.922  37.072  -8.195  1.00160.46           C  
ANISOU 1424  CA  LYS A 179    20262  18935  21773  -1620  -1978   1398       C  
ATOM   1425  C   LYS A 179      26.954  36.263  -9.489  1.00159.91           C  
ANISOU 1425  C   LYS A 179    20077  19063  21617  -1591  -1874   1519       C  
ATOM   1426  O   LYS A 179      26.610  35.085  -9.493  1.00158.76           O  
ANISOU 1426  O   LYS A 179    19905  19051  21368  -1494  -1752   1444       O  
ATOM   1427  CB  LYS A 179      27.730  36.371  -7.146  1.00159.25           C  
ANISOU 1427  CB  LYS A 179    20099  18861  21548  -1643  -1956   1326       C  
ATOM   1428  N   LYS A 180      27.399  36.898 -10.572  1.00160.68           N  
ANISOU 1428  N   LYS A 180    20113  19181  21756  -1679  -1924   1708       N  
ATOM   1429  CA  LYS A 180      27.535  36.243 -11.875  1.00159.71           C  
ANISOU 1429  CA  LYS A 180    19885  19252  21546  -1667  -1833   1838       C  
ATOM   1430  C   LYS A 180      26.196  36.092 -12.593  1.00158.71           C  
ANISOU 1430  C   LYS A 180    19786  19112  21406  -1558  -1783   1798       C  
ATOM   1431  O   LYS A 180      26.126  36.176 -13.819  1.00158.63           O  
ANISOU 1431  O   LYS A 180    19718  19183  21373  -1576  -1768   1935       O  
ATOM   1432  CB  LYS A 180      28.231  34.890 -11.733  1.00158.45           C  
ANISOU 1432  CB  LYS A 180    19648  19301  21255  -1635  -1714   1818       C  
TER    1433      LYS A 180                                                      
HETATM 1434  C1  9LI A 201      24.262  14.237  15.368  1.00 66.49           C  
ANISOU 1434  C1  9LI A 201     8631   8773   7859   -579   -679   -346       C  
HETATM 1435 CL1  9LI A 201      26.612  12.662  10.139  1.00 52.34          CL  
ANISOU 1435 CL1  9LI A 201     6490   6997   6400   -514   -585     48      CL  
HETATM 1436  C2  9LI A 201      24.320  14.376  13.871  1.00 66.16           C  
ANISOU 1436  C2  9LI A 201     8533   8679   7927   -555   -656   -299       C  
HETATM 1437 CL2  9LI A 201      23.161  16.242   8.077  1.00 49.64          CL  
ANISOU 1437 CL2  9LI A 201     6338   6332   6191   -460   -583   -233      CL  
HETATM 1438  C3  9LI A 201      25.146  13.702  13.046  1.00 65.80           C  
ANISOU 1438  C3  9LI A 201     8396   8669   7936   -556   -648   -183       C  
HETATM 1439  C4  9LI A 201      24.857  14.154  11.671  1.00 61.10           C  
ANISOU 1439  C4  9LI A 201     7779   8008   7427   -529   -624   -179       C  
HETATM 1440  C5  9LI A 201      23.828  15.115  11.812  1.00 58.85           C  
ANISOU 1440  C5  9LI A 201     7576   7645   7140   -513   -625   -294       C  
HETATM 1441  N6  9LI A 201      23.530  15.224  13.151  1.00 63.82           N  
ANISOU 1441  N6  9LI A 201     8273   8294   7684   -525   -641   -368       N  
HETATM 1442  C8  9LI A 201      23.319  15.746  10.689  1.00 52.10           C  
ANISOU 1442  C8  9LI A 201     6721   6716   6359   -488   -611   -311       C  
HETATM 1443  C9  9LI A 201      23.819  15.430   9.450  1.00 46.29           C  
ANISOU 1443  C9  9LI A 201     5911   5992   5686   -484   -594   -219       C  
HETATM 1444  C10 9LI A 201      24.825  14.489   9.287  1.00 47.22           C  
ANISOU 1444  C10 9LI A 201     5952   6189   5801   -494   -584   -114       C  
HETATM 1445  C11 9LI A 201      25.355  13.845  10.387  1.00 55.51           C  
ANISOU 1445  C11 9LI A 201     6995   7305   6790   -515   -600    -91       C  
HETATM 1446  C14 9LI A 201      26.172  12.687  13.479  1.00 66.80           C  
ANISOU 1446  C14 9LI A 201     8455   8888   8038   -577   -660    -74       C  
HETATM 1447  C15 9LI A 201      27.434  13.399  13.980  1.00 66.97           C  
ANISOU 1447  C15 9LI A 201     8468   8930   8048   -675   -776    -24       C  
HETATM 1448  N16 9LI A 201      28.434  12.402  14.387  1.00 64.29           N  
ANISOU 1448  N16 9LI A 201     8051   8685   7692   -690   -789     93       N  
HETATM 1449  PG  GCP A 202      14.988   0.822   9.002  1.00 25.43           P  
ANISOU 1449  PG  GCP A 202     3136   3521   3006    -51    145    -97       P  
HETATM 1450  O1G GCP A 202      16.239   1.557   9.373  1.00 27.28           O  
ANISOU 1450  O1G GCP A 202     3368   3782   3217    -53    112    -87       O  
HETATM 1451  O2G GCP A 202      14.391   0.084  10.167  1.00 27.49           O  
ANISOU 1451  O2G GCP A 202     3391   3821   3234    -67    166    -64       O  
HETATM 1452  O3G GCP A 202      14.009   1.694   8.258  1.00 30.09           O  
ANISOU 1452  O3G GCP A 202     3729   4089   3615    -48    149   -160       O  
HETATM 1453  C3B GCP A 202      15.455  -0.509   7.867  1.00 14.31           C  
ANISOU 1453  C3B GCP A 202     1734   2049   1655    -30    157    -55       C  
HETATM 1454  PB  GCP A 202      16.345   0.048   6.384  1.00 23.42           P  
ANISOU 1454  PB  GCP A 202     2892   3168   2840     -4    145    -74       P  
HETATM 1455  O1B GCP A 202      15.449   0.948   5.565  1.00 20.37           O  
ANISOU 1455  O1B GCP A 202     2513   2765   2463    -12    140   -132       O  
HETATM 1456  O2B GCP A 202      17.690   0.595   6.748  1.00 23.04           O  
ANISOU 1456  O2B GCP A 202     2824   3154   2777      0    122    -43       O  
HETATM 1457  O3A GCP A 202      16.623  -1.273   5.512  1.00 23.25           O  
ANISOU 1457  O3A GCP A 202     2887   3091   2855     23    168    -48       O  
HETATM 1458  PA  GCP A 202      17.923  -2.210   5.673  1.00 24.57           P  
ANISOU 1458  PA  GCP A 202     3046   3252   3039     58    177     15       P  
HETATM 1459  O1A GCP A 202      19.057  -1.658   4.848  1.00 26.52           O  
ANISOU 1459  O1A GCP A 202     3276   3509   3293     87    176     21       O  
HETATM 1460  O2A GCP A 202      18.135  -2.514   7.136  1.00 26.04           O  
ANISOU 1460  O2A GCP A 202     3213   3478   3203     42    166     67       O  
HETATM 1461  O5' GCP A 202      17.428  -3.541   4.923  1.00 24.06           O  
ANISOU 1461  O5' GCP A 202     3020   3112   3011     76    201     10       O  
HETATM 1462  C5' GCP A 202      16.166  -4.133   5.241  1.00 22.63           C  
ANISOU 1462  C5' GCP A 202     2857   2905   2835     43    202      1       C  
HETATM 1463  C4' GCP A 202      16.114  -5.543   4.668  1.00 23.09           C  
ANISOU 1463  C4' GCP A 202     2957   2882   2934     62    216     12       C  
HETATM 1464  O4' GCP A 202      16.076  -5.482   3.238  1.00 23.77           O  
ANISOU 1464  O4' GCP A 202     3076   2926   3028     80    223    -42       O  
HETATM 1465  C3' GCP A 202      17.382  -6.294   5.027  1.00 24.66           C  
ANISOU 1465  C3' GCP A 202     3147   3067   3154    109    227     72       C  
HETATM 1466  O3' GCP A 202      17.037  -7.667   5.210  1.00 27.83           O  
ANISOU 1466  O3' GCP A 202     3582   3398   3594    109    231    101       O  
HETATM 1467  C2' GCP A 202      18.267  -6.140   3.807  1.00 27.41           C  
ANISOU 1467  C2' GCP A 202     3507   3397   3511    162    247     44       C  
HETATM 1468  O2' GCP A 202      19.145  -7.254   3.634  1.00 34.04           O  
ANISOU 1468  O2' GCP A 202     4362   4185   4388    222    271     80       O  
HETATM 1469  C1' GCP A 202      17.257  -6.069   2.679  1.00 24.92           C  
ANISOU 1469  C1' GCP A 202     3237   3040   3191    141    247    -28       C  
HETATM 1470  N9  GCP A 202      17.754  -5.211   1.585  1.00 23.03           N  
ANISOU 1470  N9  GCP A 202     2995   2826   2931    163    256    -66       N  
HETATM 1471  C8  GCP A 202      18.223  -3.958   1.704  1.00 16.12           C  
ANISOU 1471  C8  GCP A 202     2074   2019   2031    157    245    -60       C  
HETATM 1472  N7  GCP A 202      18.579  -3.474   0.488  1.00 18.57           N  
ANISOU 1472  N7  GCP A 202     2393   2336   2327    177    257    -90       N  
HETATM 1473  C5  GCP A 202      18.341  -4.432  -0.432  1.00 19.75           C  
ANISOU 1473  C5  GCP A 202     2598   2423   2483    200    279   -124       C  
HETATM 1474  C6  GCP A 202      18.483  -4.590  -1.901  1.00 20.33           C  
ANISOU 1474  C6  GCP A 202     2715   2473   2535    229    302   -170       C  
HETATM 1475  O6  GCP A 202      18.939  -3.672  -2.611  1.00 21.68           O  
ANISOU 1475  O6  GCP A 202     2864   2694   2678    236    307   -174       O  
HETATM 1476  N1  GCP A 202      18.103  -5.749  -2.455  1.00 19.27           N  
ANISOU 1476  N1  GCP A 202     2649   2263   2411    244    314   -207       N  
HETATM 1477  C2  GCP A 202      17.612  -6.764  -1.719  1.00 20.57           C  
ANISOU 1477  C2  GCP A 202     2838   2366   2611    231    304   -194       C  
HETATM 1478  N2  GCP A 202      17.250  -7.912  -2.335  1.00 18.65           N  
ANISOU 1478  N2  GCP A 202     2672   2034   2381    242    310   -234       N  
HETATM 1479  N3  GCP A 202      17.450  -6.687  -0.378  1.00 21.35           N  
ANISOU 1479  N3  GCP A 202     2892   2488   2731    204    285   -142       N  
HETATM 1480  C4  GCP A 202      17.794  -5.573   0.302  1.00 20.56           C  
ANISOU 1480  C4  GCP A 202     2727   2468   2615    190    274   -110       C  
HETATM 1481 MG    MG A 203      18.308   1.342   8.691  1.00 32.23          MG  
ANISOU 1481 MG    MG A 203     3972   4398   3875    -35     83    -19      MG  
HETATM 1482  C1  GOL A 204       5.212  10.645   6.656  1.00 63.80           C  
ANISOU 1482  C1  GOL A 204     7868   8267   8108    185    191   -558       C  
HETATM 1483  O1  GOL A 204       5.115   9.582   5.732  1.00 62.30           O  
ANISOU 1483  O1  GOL A 204     7652   8084   7937    141    176   -496       O  
HETATM 1484  C2  GOL A 204       6.594  11.290   6.593  1.00 64.31           C  
ANISOU 1484  C2  GOL A 204     7996   8282   8158    167    142   -579       C  
HETATM 1485  O2  GOL A 204       7.483  10.574   7.424  1.00 63.57           O  
ANISOU 1485  O2  GOL A 204     7931   8227   7996    135    151   -572       O  
HETATM 1486  C3  GOL A 204       6.487  12.740   7.069  1.00 66.37           C  
ANISOU 1486  C3  GOL A 204     8287   8498   8433    215    134   -649       C  
HETATM 1487  O3  GOL A 204       7.751  13.371   7.056  1.00 65.74           O  
ANISOU 1487  O3  GOL A 204     8264   8371   8342    187     81   -664       O  
HETATM 1488  C1  EDO A 205       6.854  26.557   0.905  1.00 61.60           C  
ANISOU 1488  C1  EDO A 205     7922   6784   8698    384   -500   -638       C  
HETATM 1489  O1  EDO A 205       6.789  25.191   0.486  1.00 62.51           O  
ANISOU 1489  O1  EDO A 205     7972   7039   8741    349   -454   -585       O  
HETATM 1490  C2  EDO A 205       8.303  26.886   1.229  1.00 59.16           C  
ANISOU 1490  C2  EDO A 205     7688   6435   8356    296   -560   -648       C  
HETATM 1491  O2  EDO A 205       8.829  25.858   2.072  1.00 56.13           O  
ANISOU 1491  O2  EDO A 205     7314   6153   7859    265   -509   -692       O  
HETATM 1492  S   DMS A 206      22.117   0.734  16.054  1.00 88.65           S  
ANISOU 1492  S   DMS A 206    11063  11913  10706   -198   -116    281       S  
HETATM 1493  O   DMS A 206      21.220   2.214  15.552  1.00 36.99           O  
ANISOU 1493  O   DMS A 206     4569   5337   4150   -205   -107    143       O  
HETATM 1494  C1  DMS A 206      21.120  -0.721  15.629  1.00 40.77           C  
ANISOU 1494  C1  DMS A 206     4997   5799   4695   -154    -43    308       C  
HETATM 1495  C2  DMS A 206      23.559   0.480  14.975  1.00 20.88           C  
ANISOU 1495  C2  DMS A 206     2421   3297   2217   -167   -136    355       C  
HETATM 1496  C   ACT A 207      16.488  20.907  -6.366  1.00 61.01           C  
ANISOU 1496  C   ACT A 207     7614   7433   8133   -306   -576    135       C  
HETATM 1497  O   ACT A 207      16.636  20.294  -7.447  1.00 59.76           O  
ANISOU 1497  O   ACT A 207     7427   7353   7926   -315   -548    192       O  
HETATM 1498  OXT ACT A 207      15.320  20.930  -5.908  1.00 59.91           O  
ANISOU 1498  OXT ACT A 207     7494   7248   8020   -254   -566     63       O  
HETATM 1499  CH3 ACT A 207      17.646  21.569  -5.670  1.00 60.91           C  
ANISOU 1499  CH3 ACT A 207     7613   7389   8143   -357   -620    152       C  
HETATM 1500 MG    MG A 208      11.818   7.424   7.750  1.00 37.97          MG  
ANISOU 1500 MG    MG A 208     4746   5042   4638     -4     98   -410      MG  
HETATM 1501  O   HOH A 301      18.246   3.658   8.352  1.00 29.29           O  
ANISOU 1501  O   HOH A 301     3612   4027   3491    -61     37   -102       O  
HETATM 1502  O   HOH A 302      18.621  -0.878   9.277  1.00 24.70           O  
ANISOU 1502  O   HOH A 302     3009   3436   2941    -13    113     81       O  
HETATM 1503  O   HOH A 303      12.131  -0.798  10.168  1.00 21.53           O  
ANISOU 1503  O   HOH A 303     2620   3062   2500    -88    213    -66       O  
HETATM 1504  O   HOH A 304      10.363   5.818   1.362  1.00 16.92           O  
ANISOU 1504  O   HOH A 304     2044   2245   2141    -30     57   -324       O  
HETATM 1505  O   HOH A 305      13.822   8.899   7.271  1.00 20.45           O  
ANISOU 1505  O   HOH A 305     2562   2776   2432    -32     11   -409       O  
HETATM 1506  O   HOH A 306      27.118   3.193  -9.037  1.00 27.50           O  
ANISOU 1506  O   HOH A 306     3167   4077   3205    323    476    226       O  
HETATM 1507  O   HOH A 307      -0.641   2.761  -0.147  1.00 16.43           O  
ANISOU 1507  O   HOH A 307     1614   2314   2314   -220      5   -148       O  
HETATM 1508  O   HOH A 308      10.885   9.226   9.269  1.00 39.47           O  
ANISOU 1508  O   HOH A 308     4968   5245   4786     36    110   -522       O  
HETATM 1509  O   HOH A 309      25.066  -3.333   2.944  1.00 24.41           O  
ANISOU 1509  O   HOH A 309     2853   3297   3124    333    279    256       O  
HETATM 1510  O   HOH A 310      19.797  -3.972   8.479  1.00 26.66           O  
ANISOU 1510  O   HOH A 310     3255   3579   3296     74    159    209       O  
HETATM 1511  O   HOH A 311      21.580  -5.196  -9.682  1.00 33.67           O  
ANISOU 1511  O   HOH A 311     4603   4244   3946    502    557   -364       O  
HETATM 1512  O   HOH A 312      23.346   2.098   9.633  1.00 42.44           O  
ANISOU 1512  O   HOH A 312     5143   5821   5162    -62    -44    195       O  
HETATM 1513  O   HOH A 313      18.694   4.264 -12.940  1.00 32.87           O  
ANISOU 1513  O   HOH A 313     4265   4521   3704     51    211   -137       O  
HETATM 1514  O   HOH A 314      11.533   4.489 -19.199  1.00 42.67           O  
ANISOU 1514  O   HOH A 314     5785   5797   4629   -285   -162   -248       O  
HETATM 1515  O   HOH A 315      18.427  17.986  -6.363  1.00 32.23           O  
ANISOU 1515  O   HOH A 315     3919   4019   4308   -305   -428    155       O  
HETATM 1516  O   HOH A 316       4.236  -1.174   2.199  1.00 30.15           O  
ANISOU 1516  O   HOH A 316     3631   3930   3896   -235    102   -174       O  
HETATM 1517  O   HOH A 317      12.324  23.514  12.099  1.00 32.34           O  
ANISOU 1517  O   HOH A 317     4736   3487   4065    143   -361  -1288       O  
HETATM 1518  O   HOH A 318      10.923  -4.009   0.369  1.00 31.50           O  
ANISOU 1518  O   HOH A 318     4092   3876   3999    -93    138   -217       O  
HETATM 1519  O   HOH A 319      25.970  12.427 -11.390  1.00 46.30           O  
ANISOU 1519  O   HOH A 319     5412   6516   5663   -196     36    561       O  
HETATM 1520  O   HOH A 320      17.780  11.273 -13.484  1.00 33.06           O  
ANISOU 1520  O   HOH A 320     4086   4567   3906   -184    -91    165       O  
HETATM 1521  O   HOH A 321      14.535  -7.310   1.054  1.00 28.29           O  
ANISOU 1521  O   HOH A 321     3780   3326   3641     56    216   -132       O  
HETATM 1522  O   HOH A 322       7.652   0.471   4.562  1.00 29.89           O  
ANISOU 1522  O   HOH A 322     3643   3956   3759   -110    173   -217       O  
HETATM 1523  O   HOH A 323       7.918   6.690   5.917  1.00 24.34           O  
ANISOU 1523  O   HOH A 323     2920   3300   3026     28    158   -404       O  
HETATM 1524  O   HOH A 324      27.101  37.346  -3.596  1.00 57.20           O  
ANISOU 1524  O   HOH A 324     7489   5556   8687  -1611  -2104    884       O  
HETATM 1525  O   HOH A 325       7.386   3.419   7.587  1.00 38.52           O  
ANISOU 1525  O   HOH A 325     4688   5190   4759    -31    233   -298       O  
HETATM 1526  O   HOH A 326      16.688   8.881  12.690  1.00 35.58           O  
ANISOU 1526  O   HOH A 326     4570   4885   4065   -136    -70   -407       O  
HETATM 1527  O   HOH A 327       5.640  10.142  -3.936  1.00 28.00           O  
ANISOU 1527  O   HOH A 327     3320   3569   3752    -35   -143   -270       O  
HETATM 1528  O   HOH A 328      39.408  19.703  -2.130  1.00 52.05           O  
ANISOU 1528  O   HOH A 328     5256   7519   7000  -1184   -883   1698       O  
HETATM 1529  O   HOH A 329      20.839  24.006   5.372  1.00 36.45           O  
ANISOU 1529  O   HOH A 329     4931   3995   4921   -523   -890   -417       O  
HETATM 1530  O   HOH A 330       0.453   6.335   1.139  1.00 33.14           O  
ANISOU 1530  O   HOH A 330     3727   4432   4432    -22     77   -255       O  
HETATM 1531  O   HOH A 331      38.104  20.517  -7.720  1.00 58.33           O  
ANISOU 1531  O   HOH A 331     6014   8429   7721  -1069   -603   1845       O  
HETATM 1532  O   HOH A 332      -0.073   9.042   0.952  1.00 37.08           O  
ANISOU 1532  O   HOH A 332     4181   4898   5010     94     67   -295       O  
HETATM 1533  O   HOH A 333       2.115   7.794   2.418  1.00 41.29           O  
ANISOU 1533  O   HOH A 333     4836   5435   5419     60    118   -343       O  
HETATM 1534  O   HOH A 334      10.190  -2.266   2.251  1.00 47.41           O  
ANISOU 1534  O   HOH A 334     6005   6010   5999   -104    146   -194       O  
HETATM 1535  O   HOH A 335      13.390   9.128  10.636  1.00 32.30           O  
ANISOU 1535  O   HOH A 335     4113   4377   3782    -29     44   -490       O  
HETATM 1536  O   HOH A 336      28.127   1.257  -7.576  1.00 27.54           O  
ANISOU 1536  O   HOH A 336     3144   4044   3278    442    540    238       O  
HETATM 1537  O   HOH A 337      27.713  19.918  -9.885  1.00 50.92           O  
ANISOU 1537  O   HOH A 337     5861   6863   6622   -665   -476    950       O  
HETATM 1538  O   HOH A 338       9.695  -4.316   4.429  1.00 46.54           O  
ANISOU 1538  O   HOH A 338     5880   5900   5903   -145    172    -95       O  
HETATM 1539  O   HOH A 339      26.546   0.244 -10.697  1.00 51.68           O  
ANISOU 1539  O   HOH A 339     6409   7062   6165    500    637     48       O  
HETATM 1540  O   HOH A 340      17.346 -10.270  10.006  1.00 44.62           O  
ANISOU 1540  O   HOH A 340     5635   5582   5737     45    188    429       O  
HETATM 1541  O   HOH A 341       3.040  23.736   5.244  1.00 40.51           O  
ANISOU 1541  O   HOH A 341     5138   4464   5789    699    -69   -947       O  
HETATM 1542  O   HOH A 342      14.128   2.233  11.873  1.00 22.17           O  
ANISOU 1542  O   HOH A 342     2730   3244   2450    -81    151   -151       O  
HETATM 1543  O   HOH A 343      11.268   2.649  12.522  1.00 29.78           O  
ANISOU 1543  O   HOH A 343     3670   4259   3385    -66    233   -223       O  
HETATM 1544  O   HOH A 344       7.772   6.140   8.336  1.00 34.82           O  
ANISOU 1544  O   HOH A 344     4247   4724   4260     34    223   -410       O  
HETATM 1545  O   HOH A 345      28.202  39.437 -11.112  1.00 51.69           O  
ANISOU 1545  O   HOH A 345     6336   5116   8186  -1916  -2192   1960       O  
HETATM 1546  O   HOH A 346      20.799  15.187  18.764  1.00 39.21           O  
ANISOU 1546  O   HOH A 346     5462   5334   4102   -469   -555   -749       O  
HETATM 1547  O   HOH A 347      16.791   1.304 -14.857  1.00 62.17           O  
ANISOU 1547  O   HOH A 347     8215   8143   7264     58    225   -343       O  
HETATM 1548  O   HOH A 348      12.471  20.569  15.983  1.00 53.85           O  
ANISOU 1548  O   HOH A 348     7488   6623   6350    121   -189  -1369       O  
HETATM 1549  O   HOH A 349       8.235  -2.712   5.830  1.00 57.29           O  
ANISOU 1549  O   HOH A 349     7149   7390   7227   -160    195   -102       O  
HETATM 1550  O   HOH A 350      24.203   9.462  15.252  1.00 40.54           O  
ANISOU 1550  O   HOH A 350     5138   5699   4566   -437   -462    -88       O  
HETATM 1551  O   HOH A 351      14.472  19.628  17.461  1.00 49.87           O  
ANISOU 1551  O   HOH A 351     7032   6257   5661    -39   -280  -1317       O  
HETATM 1552  O   HOH A 352      37.756  12.489  -9.521  1.00 58.93           O  
ANISOU 1552  O   HOH A 352     6077   8868   7447   -252    184   1510       O  
HETATM 1553  O   HOH A 353      28.823  -8.614   0.818  1.00 33.64           O  
ANISOU 1553  O   HOH A 353     3994   4292   4495    812    554    394       O  
HETATM 1554  O   HOH A 354       4.138  19.103   5.775  1.00 53.69           O  
ANISOU 1554  O   HOH A 354     6717   6519   7165    483     35   -824       O  
HETATM 1555  O   HOH A 355      19.863  17.591  20.126  1.00 56.65           O  
ANISOU 1555  O   HOH A 355     7899   7423   6203   -457   -601  -1037       O  
HETATM 1556  O   HOH A 356      19.846  10.623  18.315  1.00 44.50           O  
ANISOU 1556  O   HOH A 356     5893   6226   4789   -352   -316   -474       O  
HETATM 1557  O   HOH A 357      18.345  -9.984   1.858  1.00 39.44           O  
ANISOU 1557  O   HOH A 357     5209   4627   5150    272    302      4       O  
HETATM 1558  O   HOH A 358      30.159  18.914  -9.630  1.00 49.46           O  
ANISOU 1558  O   HOH A 358     5520   6876   6398   -668   -395   1090       O  
HETATM 1559  O   HOH A 359      22.055  -2.702   9.552  1.00 38.72           O  
ANISOU 1559  O   HOH A 359     4703   5228   4780     64     96    293       O  
HETATM 1560  O   HOH A 360       7.662  19.236  -4.065  1.00 45.39           O  
ANISOU 1560  O   HOH A 360     5582   5386   6277     76   -389   -233       O  
HETATM 1561  O   HOH A 361      25.943  23.241   6.259  1.00 40.40           O  
ANISOU 1561  O   HOH A 361     5276   4738   5338   -854  -1092   -104       O  
HETATM 1562  O   HOH A 362      34.769  11.360 -10.037  1.00 55.67           O  
ANISOU 1562  O   HOH A 362     5967   8249   6935   -134    242   1170       O  
HETATM 1563  O   HOH A 363      16.749   5.200 -14.344  1.00 49.85           O  
ANISOU 1563  O   HOH A 363     6457   6672   5811    -43    106   -146       O  
HETATM 1564  O   HOH A 364       3.600  -1.853 -12.051  1.00 41.48           O  
ANISOU 1564  O   HOH A 364     5556   5167   5038   -523   -365   -403       O  
HETATM 1565  O   HOH A 365      21.372   2.185 -11.841  1.00 51.92           O  
ANISOU 1565  O   HOH A 365     6646   6948   6133    216    378   -129       O  
HETATM 1566  O   HOH A 366      17.923 -11.105  -5.592  1.00 46.53           O  
ANISOU 1566  O   HOH A 366     6491   5299   5888    395    395   -427       O  
HETATM 1567  O   HOH A 367      16.420  -0.832 -13.240  1.00 53.38           O  
ANISOU 1567  O   HOH A 367     7163   6881   6239    102    251   -428       O  
HETATM 1568  O   HOH A 368      13.975  11.882 -14.364  1.00 42.12           O  
ANISOU 1568  O   HOH A 368     5280   5624   5100   -238   -237    115       O  
HETATM 1569  O   HOH A 369       2.834   0.441 -11.154  1.00 47.21           O  
ANISOU 1569  O   HOH A 369     6094   5983   5859   -483   -367   -306       O  
HETATM 1570  O   HOH A 370      12.192   9.603  17.380  1.00 51.11           O  
ANISOU 1570  O   HOH A 370     6643   7070   5705    -17    156   -681       O  
HETATM 1571  O   HOH A 371      18.570  18.849 -10.541  1.00 49.04           O  
ANISOU 1571  O   HOH A 371     5986   6260   6388   -378   -462    399       O  
HETATM 1572  O   HOH A 372      14.774  14.340 -13.308  1.00 46.16           O  
ANISOU 1572  O   HOH A 372     5718   6062   5758   -260   -308    211       O  
HETATM 1573  O   HOH A 373      12.185  -5.325   3.972  1.00 33.92           O  
ANISOU 1573  O   HOH A 373     4347   4229   4314    -69    184    -75       O  
HETATM 1574  O   HOH A 374      14.395   1.101  16.331  1.00 54.28           O  
ANISOU 1574  O   HOH A 374     6805   7552   6267   -149    166    -38       O  
HETATM 1575  O   HOH A 375      24.047  15.296 -11.083  1.00 46.95           O  
ANISOU 1575  O   HOH A 375     5554   6411   5875   -337   -179    561       O  
HETATM 1576  O   HOH A 376      21.851  17.219  13.696  1.00 69.26           O  
ANISOU 1576  O   HOH A 376     9125   8830   8361   -489   -654   -596       O  
HETATM 1577  O   HOH A 377      17.246  19.519  19.131  1.00 47.68           O  
ANISOU 1577  O   HOH A 377     6850   6063   5202   -260   -477  -1275       O  
HETATM 1578  O   HOH A 378       2.083   2.043  -7.954  1.00 43.89           O  
ANISOU 1578  O   HOH A 378     5459   5608   5609   -383   -277   -234       O  
HETATM 1579  O   HOH A 379       4.472   9.573 -11.571  1.00 34.55           O  
ANISOU 1579  O   HOH A 379     4207   4488   4432   -253   -401    -80       O  
HETATM 1580  O   HOH A 380       7.178  13.700 -18.122  1.00 46.25           O  
ANISOU 1580  O   HOH A 380     5745   6146   5682   -395   -613    276       O  
HETATM 1581  O   HOH A 381       6.682   7.972   9.859  1.00 56.45           O  
ANISOU 1581  O   HOH A 381     6985   7508   6956    110    274   -516       O  
HETATM 1582  O   HOH A 382       5.879   1.990   5.314  1.00 40.45           O  
ANISOU 1582  O   HOH A 382     4900   5366   5102    -87    198   -247       O  
HETATM 1583  O   HOH A 383      28.059  -6.985  -2.959  1.00 47.01           O  
ANISOU 1583  O   HOH A 383     5793   6041   6029    805    650    175       O  
HETATM 1584  O   HOH A 384      27.989  -3.865   9.323  1.00 54.38           O  
ANISOU 1584  O   HOH A 384     6428   7329   6906    224     67    655       O  
HETATM 1585  O   HOH A 385      27.507  -8.332   7.171  1.00 62.37           O  
ANISOU 1585  O   HOH A 385     7549   8034   8114    500    263    644       O  
HETATM 1586  O   HOH A 386      25.205  -8.744   8.494  1.00 63.99           O  
ANISOU 1586  O   HOH A 386     7856   8188   8269    376    215    595       O  
HETATM 1587  O   HOH A 387      17.271 -10.697  -0.530  1.00 41.16           O  
ANISOU 1587  O   HOH A 387     5573   4715   5353    266    306   -148       O  
HETATM 1588  O   HOH A 388      10.995  -2.167  12.699  1.00 45.51           O  
ANISOU 1588  O   HOH A 388     5621   6220   5452   -139    262     39       O  
HETATM 1589  O   HOH A 389      34.681  20.006  -8.985  1.00 52.44           O  
ANISOU 1589  O   HOH A 389     5555   7495   6873   -887   -490   1522       O  
HETATM 1590  O   HOH A 390       8.783   9.385  10.550  1.00 45.66           O  
ANISOU 1590  O   HOH A 390     5723   6094   5531     98    202   -585       O  
CONECT   76 1500                                                                
CONECT  119 1481                                                                
CONECT  282 1481                                                                
CONECT  470 1500                                                                
CONECT  475 1500                                                                
CONECT  778 1500                                                                
CONECT 1434 1436                                                                
CONECT 1435 1445                                                                
CONECT 1436 1434 1438 1441                                                      
CONECT 1437 1443                                                                
CONECT 1438 1436 1439 1446                                                      
CONECT 1439 1438 1440 1445                                                      
CONECT 1440 1439 1441 1442                                                      
CONECT 1441 1436 1440                                                           
CONECT 1442 1440 1443                                                           
CONECT 1443 1437 1442 1444                                                      
CONECT 1444 1443 1445                                                           
CONECT 1445 1435 1439 1444                                                      
CONECT 1446 1438 1447                                                           
CONECT 1447 1446 1448                                                           
CONECT 1448 1447                                                                
CONECT 1449 1450 1451 1452 1453                                                 
CONECT 1450 1449 1481                                                           
CONECT 1451 1449                                                                
CONECT 1452 1449                                                                
CONECT 1453 1449 1454                                                           
CONECT 1454 1453 1455 1456 1457                                                 
CONECT 1455 1454                                                                
CONECT 1456 1454 1481                                                           
CONECT 1457 1454 1458                                                           
CONECT 1458 1457 1459 1460 1461                                                 
CONECT 1459 1458                                                                
CONECT 1460 1458                                                                
CONECT 1461 1458 1462                                                           
CONECT 1462 1461 1463                                                           
CONECT 1463 1462 1464 1465                                                      
CONECT 1464 1463 1469                                                           
CONECT 1465 1463 1466 1467                                                      
CONECT 1466 1465                                                                
CONECT 1467 1465 1468 1469                                                      
CONECT 1468 1467                                                                
CONECT 1469 1464 1467 1470                                                      
CONECT 1470 1469 1471 1480                                                      
CONECT 1471 1470 1472                                                           
CONECT 1472 1471 1473                                                           
CONECT 1473 1472 1474 1480                                                      
CONECT 1474 1473 1475 1476                                                      
CONECT 1475 1474                                                                
CONECT 1476 1474 1477                                                           
CONECT 1477 1476 1478 1479                                                      
CONECT 1478 1477                                                                
CONECT 1479 1477 1480                                                           
CONECT 1480 1470 1473 1479                                                      
CONECT 1481  119  282 1450 1456                                                 
CONECT 1481 1501 1502                                                           
CONECT 1482 1483 1484                                                           
CONECT 1483 1482                                                                
CONECT 1484 1482 1485 1486                                                      
CONECT 1485 1484                                                                
CONECT 1486 1484 1487                                                           
CONECT 1487 1486                                                                
CONECT 1488 1489 1490                                                           
CONECT 1489 1488                                                                
CONECT 1490 1488 1491                                                           
CONECT 1491 1490                                                                
CONECT 1492 1493 1494 1495                                                      
CONECT 1493 1492                                                                
CONECT 1494 1492                                                                
CONECT 1495 1492                                                                
CONECT 1496 1497 1498 1499                                                      
CONECT 1497 1496                                                                
CONECT 1498 1496                                                                
CONECT 1499 1496                                                                
CONECT 1500   76  470  475  778                                                 
CONECT 1500 1505 1508                                                           
CONECT 1501 1481                                                                
CONECT 1502 1481                                                                
CONECT 1505 1500                                                                
CONECT 1508 1500                                                                
MASTER      351    0    8    5    6    0   19    6 1574    1   79   15          
END