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***  METAL TRANSPORT 04-MAR-99 1CC8  ***

elNémo ID: 22031014523741668

Job options:

ID        	=	 22031014523741668
JOBID     	=	 METAL TRANSPORT 04-MAR-99 1CC8
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    METAL TRANSPORT                         04-MAR-99   1CC8              
TITLE     CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (METALLOCHAPERONE ATX1);                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET11D;                                    
SOURCE   9 EXPRESSION_SYSTEM_GENE: ATX1                                         
KEYWDS    COPPER TRANSPORT, MERCURY COORDINATION, METAL TRANSPORT               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.ROSENZWEIG,D.L.HUFFMAN,M.Y.R.A.PUFAHL,T.V.O.HOU,A.K.WERNIMONT     
REVDAT   4   04-OCT-17 1CC8    1       REMARK                                   
REVDAT   3   24-FEB-09 1CC8    1       VERSN                                    
REVDAT   2   01-APR-03 1CC8    1       JRNL                                     
REVDAT   1   12-DEC-99 1CC8    0                                                
JRNL        AUTH   A.C.ROSENZWEIG,D.L.HUFFMAN,M.Y.HOU,A.K.WERNIMONT,R.A.PUFAHL, 
JRNL        AUTH 2 T.V.O'HALLORAN                                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE ATX1 METALLOCHAPERONE PROTEIN AT    
JRNL        TITL 2 1.02 A RESOLUTION.                                           
JRNL        REF    STRUCTURE FOLD.DES.           V.   7   605 1999              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   10404590                                                     
JRNL        DOI    10.1016/S0969-2126(99)80082-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.141                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.146                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.172                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000                 
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2812                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 25378                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.139                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.145                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.177                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 11.100                 
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2812                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 25378                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 567                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 19                                            
REMARK   3   SOLVENT ATOMS      : 117                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 701.50                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 596.00                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 0                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 5745                    
REMARK   3   NUMBER OF RESTRAINTS                     : 6701                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.010                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.052                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.130                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.108                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.055                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.039                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-228        
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CC8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000000585.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 5ID-B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0047                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24099                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200   FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.10600                            
REMARK 200   FOR SHELL         : 5.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT METHODS               
REMARK 200 SOFTWARE USED: SNB                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       28.32500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       14.80000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       28.32500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       14.80000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A  64   O   -  C   -  N   ANGL. DEV. = -10.8 DEGREES          
REMARK 500    ARG A  68   CD  -  NE  -  CZ  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ARG A  68   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
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                              HG A  74  HG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  14   OG1                                                    
REMARK 620 2 CYS A  15   SG  102.3                                              
REMARK 620 3 CYS A  15   N    61.9  74.8                                        
REMARK 620 4 CYS A  15   O   106.0  75.3  45.8                                  
REMARK 620 5 CYS A  18   SG   83.6 167.3  98.8  92.3                            
REMARK 620 6 CYS A  18   N   146.1  97.6  98.2  53.4  72.2                      
REMARK 620 7 HOH A1018   O   136.7  84.9 156.0 117.1  98.6  71.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 74                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 186                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 187                 
DBREF  1CC8 A    1    73  UNP    P38636   ATX1_YEAST       1     73             
SEQRES   1 A   73  MET ALA GLU ILE LYS HIS TYR GLN PHE ASN VAL VAL MET          
SEQRES   2 A   73  THR CYS SER GLY CYS SER GLY ALA VAL ASN LYS VAL LEU          
SEQRES   3 A   73  THR LYS LEU GLU PRO ASP VAL SER LYS ILE ASP ILE SER          
SEQRES   4 A   73  LEU GLU LYS GLN LEU VAL ASP VAL TYR THR THR LEU PRO          
SEQRES   5 A   73  TYR ASP PHE ILE LEU GLU LYS ILE LYS LYS THR GLY LYS          
SEQRES   6 A   73  GLU VAL ARG SER GLY LYS GLN LEU                              
HET     HG  A  74       1                                                       
HET    BEN  A 186       9                                                       
HET    BEN  A 187       9                                                       
HETNAM      HG MERCURY (II) ION                                                 
HETNAM     BEN BENZAMIDINE                                                      
FORMUL   2   HG    HG 2+                                                        
FORMUL   3  BEN    2(C7 H8 N2)                                                  
FORMUL   5  HOH   *117(H2 O)                                                    
HELIX    1   1 SER A   16  LEU A   29  1                                  14    
HELIX    2   2 TYR A   53  THR A   63  1                                  11    
SHEET    1   A 4 VAL A  67  LEU A  73  0                                        
SHEET    2   A 4 LYS A   5  VAL A  11 -1  N  ASN A  10   O  ARG A  68           
SHEET    3   A 4 LEU A  44  THR A  49 -1  N  THR A  49   O  LYS A   5           
SHEET    4   A 4 VAL A  33  SER A  39 -1  N  SER A  39   O  LEU A  44           
LINK        HG    HG A  74                 OG1 THR A  14     1555   1555  3.08  
LINK        HG    HG A  74                 SG  CYS A  15     1555   1555  2.33  
LINK        HG    HG A  74                 N   CYS A  15     1555   1555  3.26  
LINK        HG    HG A  74                 O   CYS A  15     1555   1555  3.46  
LINK        HG    HG A  74                 SG  CYS A  18     1555   1555  2.34  
LINK        HG    HG A  74                 N   CYS A  18     1555   1555  3.14  
LINK        HG    HG A  74                 O   HOH A1018     1555   1545  3.12  
CISPEP   1 GLU A   30    PRO A   31          0         7.72                     
SITE     1 AC1  3 THR A  14  CYS A  15  CYS A  18                               
SITE     1 AC2  8 ILE A   4  ASN A  23  GLU A  30  VAL A  33                    
SITE     2 AC2  8 SER A  34  ILE A  36  LEU A  73  HOH A1002                    
SITE     1 AC3  7 MET A  13  LEU A  40  GLN A  43  GLU A  58                    
SITE     2 AC3  7 HOH A1039  HOH A1100  HOH A1109                               
CRYST1   56.650   29.600   40.770  90.00 114.83  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017652  0.000000  0.008168        0.00000                         
SCALE2      0.000000  0.033784  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027026        0.00000                         
ATOM      1  N   ALA A   2      14.789  27.073  24.130  1.00 28.86           N  
ANISOU    1  N   ALA A   2     3076   5049   2840  -2878   -759    351       N  
ATOM      2  CA  ALA A   2      13.936  25.892  24.216  1.00  7.09           C  
ANISOU    2  CA  ALA A   2      553   1356    784    614   -124   -316       C  
ATOM      3  C   ALA A   2      12.753  25.845  23.241  1.00  5.37           C  
ANISOU    3  C   ALA A   2      588    916    538    215    -43   -189       C  
ATOM      4  O   ALA A   2      11.656  25.370  23.562  1.00  5.46           O  
ANISOU    4  O   ALA A   2      640    967    469    129    -16    -98       O  
ATOM      5  CB  ALA A   2      13.383  25.878  25.624  1.00  9.53           C  
ANISOU    5  CB  ALA A   2      769   2252    598    578   -420   -408       C  
ATOM      6  N   GLU A   3      12.966  26.360  22.030  1.00  5.21           N  
ANISOU    6  N   GLU A   3      592    679    706      0    -63    -89       N  
ATOM      7  CA  GLU A   3      11.910  26.317  21.014  1.00  4.69           C  
ANISOU    7  CA  GLU A   3      631    581    571     79     -1    -80       C  
ATOM      8  C   GLU A   3      11.584  24.887  20.616  1.00  4.64           C  
ANISOU    8  C   GLU A   3      616    679    469     45    -73    -40       C  
ATOM      9  O   GLU A   3      12.499  24.101  20.325  1.00  5.46           O  
ANISOU    9  O   GLU A   3      689    464    922    117    -94    -54       O  
ATOM     10  CB  GLU A   3      12.285  27.145  19.781  1.00  5.64           C  
ANISOU   10  CB  GLU A   3      822    683    639     69    126    -37       C  
ATOM     11  CG  GLU A   3      11.115  27.144  18.789  1.00  5.94           C  
ANISOU   11  CG  GLU A   3     1079    486    692     74     -2     20       C  
ATOM     12  CD  GLU A   3      11.234  27.841  17.482  1.00  7.46           C  
ANISOU   12  CD  GLU A   3      995   1044    798    -62    -37    131       C  
ATOM     13  OE1 GLU A   3      12.372  28.263  17.151  1.00  9.12           O  
ANISOU   13  OE1 GLU A   3     1241   1040   1185   -539    148     41       O  
ATOM     14  OE2 GLU A   3      10.207  27.911  16.746  1.00  9.19           O  
ANISOU   14  OE2 GLU A   3     1066   1386   1038    -77   -128    353       O  
ATOM     15  N   ILE A   4      10.277  24.574  20.552  1.00  4.55           N  
ANISOU   15  N   ILE A   4      564    662    505     32    -15    -74       N  
ATOM     16  CA  ILE A   4       9.792  23.327  19.967  1.00  4.41           C  
ANISOU   16  CA  ILE A   4      475    691    510     69     -6   -126       C  
ATOM     17  C   ILE A   4       9.357  23.647  18.539  1.00  3.83           C  
ANISOU   17  C   ILE A   4      475    444    537      3     22      0       C  
ATOM     18  O   ILE A   4       8.328  24.276  18.300  1.00  4.78           O  
ANISOU   18  O   ILE A   4      656    601    560    171    -29      2       O  
ATOM     19  CB  ILE A   4       8.616  22.720  20.759  1.00  4.48           C  
ANISOU   19  CB  ILE A   4      718    455    528      3     74    -41       C  
ATOM     20  CG1 ILE A   4       9.056  22.448  22.225  1.00  6.39           C  
ANISOU   20  CG1 ILE A   4     1068    843    517   -112      8    -35       C  
ATOM     21  CG2 ILE A   4       8.114  21.449  20.085  1.00  5.34           C  
ANISOU   21  CG2 ILE A   4      762    619    650   -103     37   -143       C  
ATOM     22  CD1 ILE A   4       7.923  21.909  23.050  1.00  7.37           C  
ANISOU   22  CD1 ILE A   4     1152    896    754    -51    195     92       C  
ATOM     23  N   LYS A   5      10.227  23.280  17.593  1.00  3.51           N  
ANISOU   23  N   LYS A   5      497    391    446      5    -51     -7       N  
ATOM     24  CA  LYS A   5      10.013  23.554  16.172  1.00  4.17           C  
ANISOU   24  CA  LYS A   5      579    529    478    -25     32    -51       C  
ATOM     25  C   LYS A   5       9.068  22.515  15.567  1.00  3.86           C  
ANISOU   25  C   LYS A   5      600    434    431     40     29     23       C  
ATOM     26  O   LYS A   5       8.929  21.410  16.084  1.00  5.26           O  
ANISOU   26  O   LYS A   5      876    500    622   -133   -261    140       O  
ATOM     27  CB  LYS A   5      11.389  23.588  15.457  1.00  5.00           C  
ANISOU   27  CB  LYS A   5      617    727    556     50     66     75       C  
ATOM     28  CG  LYS A   5      12.243  24.756  15.882  1.00 10.43           C  
ANISOU   28  CG  LYS A   5     1207   1595   1163   -895    -40    353       C  
ATOM     29  CD  LYS A   5      13.682  24.802  15.533  1.00 14.61           C  
ANISOU   29  CD  LYS A   5     1030   2809   1713   -664    -82   -281       C  
ATOM     30  CE  LYS A   5      14.575  23.992  16.439  1.00 19.41           C  
ANISOU   30  CE  LYS A   5     2451   2284   2639    664  -1203  -1621       C  
ATOM     31  NZ  LYS A   5      13.965  22.712  16.893  1.00 38.72           N  
ANISOU   31  NZ  LYS A   5     5436   3848   5425    160  -1237   1370       N  
ATOM     32  N   HIS A   6       8.414  22.903  14.476  1.00  4.20           N  
ANISOU   32  N   HIS A   6      736    432    428    -34    -42     -6       N  
ATOM     33  CA  HIS A   6       7.540  22.053  13.674  1.00  3.60           C  
ANISOU   33  CA  HIS A   6      605    280    483    -22     40    -23       C  
ATOM     34  C   HIS A   6       8.176  21.829  12.290  1.00  3.74           C  
ANISOU   34  C   HIS A   6      556    473    393    -26    -22     24       C  
ATOM     35  O   HIS A   6       8.293  22.786  11.525  1.00  4.69           O  
ANISOU   35  O   HIS A   6      872    449    460    157     24     49       O  
ATOM     36  CB  HIS A   6       6.136  22.626  13.528  1.00  4.74           C  
ANISOU   36  CB  HIS A   6      632    665    505     53     89    -94       C  
ATOM     37  CG  HIS A   6       5.147  21.852  12.719  1.00  4.34           C  
ANISOU   37  CG  HIS A   6      540    651    460     72     62    -38       C  
ATOM     38  ND1 HIS A   6       5.251  20.647  12.086  1.00  5.78           N  
ANISOU   38  ND1 HIS A   6      742    693    760     70    -17   -116       N  
ATOM     39  CD2 HIS A   6       3.856  22.252  12.484  1.00  4.30           C  
ANISOU   39  CD2 HIS A   6      643    506    485    167      6     10       C  
ATOM     40  CE1 HIS A   6       4.074  20.410  11.477  1.00  4.14           C  
ANISOU   40  CE1 HIS A   6      528    563    481     -6     -2      4       C  
ATOM     41  NE2 HIS A   6       3.203  21.352  11.720  1.00  6.28           N  
ANISOU   41  NE2 HIS A   6      740    753    893    -27    -48    -23       N  
ATOM     42  N   TYR A   7       8.581  20.599  12.002  1.00  3.70           N  
ANISOU   42  N   TYR A   7      559    455    392    -83     49     78       N  
ATOM     43  CA  TYR A   7       9.081  20.238  10.683  1.00  3.68           C  
ANISOU   43  CA  TYR A   7      554    431    413    -58     28    -19       C  
ATOM     44  C   TYR A   7       8.048  19.325  10.003  1.00  3.44           C  
ANISOU   44  C   TYR A   7      511    407    389    -19     77     16       C  
ATOM     45  O   TYR A   7       7.392  18.521  10.659  1.00  4.30           O  
ANISOU   45  O   TYR A   7      671    505    459   -117     41    110       O  
ATOM     46  CB  TYR A   7      10.440  19.521  10.802  1.00  4.48           C  
ANISOU   46  CB  TYR A   7      538    578    588     12    -51      8       C  
ATOM     47  CG  TYR A   7      11.482  20.202  11.665  1.00  4.07           C  
ANISOU   47  CG  TYR A   7      454    582    511     43     68    -30       C  
ATOM     48  CD1 TYR A   7      11.674  21.578  11.669  1.00  4.66           C  
ANISOU   48  CD1 TYR A   7      631    541    599    100    -57    -52       C  
ATOM     49  CD2 TYR A   7      12.357  19.470  12.474  1.00  4.94           C  
ANISOU   49  CD2 TYR A   7      647    622    610     73   -108    -10       C  
ATOM     50  CE1 TYR A   7      12.647  22.202  12.431  1.00  4.54           C  
ANISOU   50  CE1 TYR A   7      565    516    644     72      0    -89       C  
ATOM     51  CE2 TYR A   7      13.324  20.066  13.279  1.00  4.87           C  
ANISOU   51  CE2 TYR A   7      619    633    598     21    -50     32       C  
ATOM     52  CZ  TYR A   7      13.466  21.438  13.270  1.00  4.69           C  
ANISOU   52  CZ  TYR A   7      523    682    577    -29     15     20       C  
ATOM     53  OH  TYR A   7      14.414  22.059  14.069  1.00  5.73           O  
ANISOU   53  OH  TYR A   7      789    678    709      4   -160    -68       O  
ATOM     54  N   GLN A   8       7.900  19.488   8.690  1.00  4.23           N  
ANISOU   54  N   GLN A   8      797    450    358   -117    -25     64       N  
ATOM     55  CA  GLN A   8       6.984  18.675   7.906  1.00  4.23           C  
ANISOU   55  CA  GLN A   8      601    512    495   -145     57    -37       C  
ATOM     56  C   GLN A   8       7.702  18.097   6.697  1.00  4.30           C  
ANISOU   56  C   GLN A   8      627    575    433   -191    -20    -28       C  
ATOM     57  O   GLN A   8       8.315  18.866   5.973  1.00  6.24           O  
ANISOU   57  O   GLN A   8     1219    618    533   -270    336   -110       O  
ATOM     58  CB  GLN A   8       5.747  19.471   7.480  1.00  5.22           C  
ANISOU   58  CB  GLN A   8      806    631    546    -18    -26    -57       C  
ATOM     59  CG  GLN A   8       4.683  18.663   6.730  1.00  6.71           C  
ANISOU   59  CG  GLN A   8      973    921    656   -124   -282   -140       C  
ATOM     60  CD  GLN A   8       3.461  19.514   6.448  1.00  7.46           C  
ANISOU   60  CD  GLN A   8     1054    677   1102   -171   -375     12       C  
ATOM     61  OE1 GLN A   8       2.537  19.647   7.282  1.00 11.25           O  
ANISOU   61  OE1 GLN A   8     1271   1341   1661    114    -76   -178       O  
ATOM     62  NE2 GLN A   8       3.448  20.133   5.292  1.00 10.93           N  
ANISOU   62  NE2 GLN A   8     1810   1140   1202   -124   -652    251       N  
ATOM     63  N   PHE A   9       7.536  16.798   6.484  1.00  3.95           N  
ANISOU   63  N   PHE A   9      630    516    354   -104     58    -13       N  
ATOM     64  CA  PHE A   9       8.208  16.090   5.384  1.00  4.45           C  
ANISOU   64  CA  PHE A   9      630    646    416    -70     95    -82       C  
ATOM     65  C   PHE A   9       7.179  15.323   4.556  1.00  4.13           C  
ANISOU   65  C   PHE A   9      728    402    440   -141     47     -4       C  
ATOM     66  O   PHE A   9       6.279  14.697   5.098  1.00  5.48           O  
ANISOU   66  O   PHE A   9      859    862    361   -277     17     90       O  
ATOM     67  CB  PHE A   9       9.242  15.114   5.962  1.00  4.49           C  
ANISOU   67  CB  PHE A   9      649    564    493    -67    105     -2       C  
ATOM     68  CG  PHE A   9      10.265  15.755   6.880  1.00  4.88           C  
ANISOU   68  CG  PHE A   9      562    742    551     70     31    -69       C  
ATOM     69  CD1 PHE A   9      11.412  16.392   6.406  1.00  5.28           C  
ANISOU   69  CD1 PHE A   9      684    565    759    -41     80   -224       C  
ATOM     70  CD2 PHE A   9      10.059  15.727   8.257  1.00  5.24           C  
ANISOU   70  CD2 PHE A   9      719    739    533     72     45   -114       C  
ATOM     71  CE1 PHE A   9      12.307  16.969   7.285  1.00  6.64           C  
ANISOU   71  CE1 PHE A   9      533   1197    795     40    -37   -328       C  
ATOM     72  CE2 PHE A   9      10.965  16.277   9.125  1.00  5.56           C  
ANISOU   72  CE2 PHE A   9      821    595    698    135   -146    -54       C  
ATOM     73  CZ  PHE A   9      12.080  16.938   8.652  1.00  5.81           C  
ANISOU   73  CZ  PHE A   9      677    736    794    198    -69    -84       C  
ATOM     74  N   ASN A  10       7.351  15.309   3.240  1.00  4.40           N  
ANISOU   74  N   ASN A  10      762    445    464    -49     10     31       N  
ATOM     75  CA  ASN A  10       6.641  14.398   2.343  1.00  4.49           C  
ANISOU   75  CA  ASN A  10      747    549    409    -95     26     42       C  
ATOM     76  C   ASN A  10       7.530  13.156   2.194  1.00  4.59           C  
ANISOU   76  C   ASN A  10      673    604    466    -85    -36    -65       C  
ATOM     77  O   ASN A  10       8.627  13.265   1.622  1.00  5.32           O  
ANISOU   77  O   ASN A  10      720    686    615    -63     72     20       O  
ATOM     78  CB  ASN A  10       6.348  15.062   1.000  1.00  5.76           C  
ANISOU   78  CB  ASN A  10     1027    742    421     77    -63     71       C  
ATOM     79  CG  ASN A  10       5.675  14.199  -0.041  1.00  6.05           C  
ANISOU   79  CG  ASN A  10      914    906    477    -79    -97    109       C  
ATOM     80  OD1 ASN A  10       4.979  13.198   0.211  1.00  7.78           O  
ANISOU   80  OD1 ASN A  10     1321    943    692   -251     15     95       O  
ATOM     81  ND2 ASN A  10       5.899  14.580  -1.288  1.00  7.65           N  
ANISOU   81  ND2 ASN A  10     1303   1174    428   -522   -272    177       N  
ATOM     82  N   VAL A  11       7.086  12.065   2.788  1.00  4.41           N  
ANISOU   82  N   VAL A  11      670    605    401     -2    -18    -12       N  
ATOM     83  CA  VAL A  11       7.845  10.816   2.846  1.00  4.79           C  
ANISOU   83  CA  VAL A  11      614    682    524    -76    -13     37       C  
ATOM     84  C   VAL A  11       7.007   9.732   2.173  1.00  4.57           C  
ANISOU   84  C   VAL A  11      704    560    472    -24    -20    -47       C  
ATOM     85  O   VAL A  11       5.803   9.600   2.453  1.00  4.84           O  
ANISOU   85  O   VAL A  11      680    634    525    -75     30    -60       O  
ATOM     86  CB  VAL A  11       8.187  10.397   4.300  1.00  5.11           C  
ANISOU   86  CB  VAL A  11      749    755    439     43    -78    -27       C  
ATOM     87  CG1 VAL A  11       9.089   9.179   4.298  1.00  5.76           C  
ANISOU   87  CG1 VAL A  11      826    738    624     28   -117     -8       C  
ATOM     88  CG2 VAL A  11       8.858  11.533   5.058  1.00  5.19           C  
ANISOU   88  CG2 VAL A  11      781    740    453   -110    -40     65       C  
ATOM     89  N   VAL A  12       7.635   8.994   1.247  1.00  5.69           N  
ANISOU   89  N   VAL A  12      711    657    794    -57     69   -148       N  
ATOM     90  CA  VAL A  12       6.931   7.906   0.557  1.00  5.14           C  
ANISOU   90  CA  VAL A  12      749    655    550    -23    -51   -106       C  
ATOM     91  C   VAL A  12       6.780   6.711   1.489  1.00  4.76           C  
ANISOU   91  C   VAL A  12      665    637    507    -69    -41   -159       C  
ATOM     92  O   VAL A  12       7.775   6.137   1.954  1.00  6.29           O  
ANISOU   92  O   VAL A  12      674    928    788     32    -47     69       O  
ATOM     93  CB  VAL A  12       7.675   7.506  -0.719  1.00  5.87           C  
ANISOU   93  CB  VAL A  12      856    856    517    -55     11    -77       C  
ATOM     94  CG1 VAL A  12       6.907   6.395  -1.438  1.00  7.21           C  
ANISOU   94  CG1 VAL A  12     1216   1051    473   -111    -19   -176       C  
ATOM     95  CG2 VAL A  12       7.845   8.724  -1.608  1.00  7.08           C  
ANISOU   95  CG2 VAL A  12     1018   1023    651     -4     95     31       C  
ATOM     96  N   MET A  13       5.518   6.379   1.759  1.00  4.92           N  
ANISOU   96  N   MET A  13      626    588    654     39    -44    -29       N  
ATOM     97  CA  MET A  13       5.214   5.328   2.724  1.00  5.27           C  
ANISOU   97  CA  MET A  13      886    669    446     -1    -27    -12       C  
ATOM     98  C   MET A  13       4.120   4.418   2.161  1.00  5.44           C  
ANISOU   98  C   MET A  13      864    635    568     51    -31    -29       C  
ATOM     99  O   MET A  13       2.958   4.792   1.978  1.00  6.39           O  
ANISOU   99  O   MET A  13      804    704    921      6     13     60       O  
ATOM    100  CB  MET A  13       4.731   5.986   4.027  1.00  5.36           C  
ANISOU  100  CB  MET A  13      705    808    525     88    -40   -126       C  
ATOM    101  CG  MET A  13       5.808   6.810   4.714  1.00  5.58           C  
ANISOU  101  CG  MET A  13      813    680    626     29    -82   -136       C  
ATOM    102  SD  MET A  13       5.246   7.725   6.162  1.00  6.11           S  
ANISOU  102  SD  MET A  13     1001    821    499     60    -25    -73       S  
ATOM    103  CE  MET A  13       4.146   8.929   5.403  1.00  5.55           C  
ANISOU  103  CE  MET A  13      788    683    639    -42      7    -37       C  
ATOM    104  N   THR A  14       4.518   3.205   1.742  1.00  6.28           N  
ANISOU  104  N   THR A  14      883    673    829     73   -155   -202       N  
ATOM    105  CA  THR A  14       3.640   2.362   0.936  1.00  7.51           C  
ANISOU  105  CA  THR A  14      957    796   1099      0   -278   -224       C  
ATOM    106  C   THR A  14       2.710   1.491   1.778  1.00  8.27           C  
ANISOU  106  C   THR A  14     1168    754   1222   -123   -351   -177       C  
ATOM    107  O   THR A  14       1.795   0.867   1.231  1.00 10.62           O  
ANISOU  107  O   THR A  14     1058   1439   1540   -311   -525   -116       O  
ATOM    108  CB  THR A  14       4.490   1.444   0.012  1.00  8.43           C  
ANISOU  108  CB  THR A  14     1394    839    970    178   -436   -344       C  
ATOM    109  OG1 THR A  14       5.248   0.531   0.824  1.00 10.67           O  
ANISOU  109  OG1 THR A  14     1699   1325   1032    668   -427   -471       O  
ATOM    110  CG2 THR A  14       5.476   2.261  -0.802  1.00 10.68           C  
ANISOU  110  CG2 THR A  14     1570   1690    800    121    -87   -470       C  
ATOM    111  N   CYS A  15       3.027   1.377   3.058  1.00  8.39           N  
ANISOU  111  N   CYS A  15      940   1083   1167   -341   -156   -286       N  
ATOM    112  CA  CYS A  15       2.334   0.492   3.979  1.00  9.33           C  
ANISOU  112  CA  CYS A  15     1200   1053   1292   -338   -235   -125       C  
ATOM    113  C   CYS A  15       2.633   0.942   5.409  1.00  8.05           C  
ANISOU  113  C   CYS A  15      906    906   1246   -205    -30   -198       C  
ATOM    114  O   CYS A  15       3.538   1.770   5.603  1.00  6.65           O  
ANISOU  114  O   CYS A  15      866    632   1030    -87   -138     31       O  
ATOM    115  CB  CYS A  15       2.717  -0.959   3.746  1.00 10.10           C  
ANISOU  115  CB  CYS A  15     1576   1044   1218   -367   -299   -370       C  
ATOM    116  SG  CYS A  15       4.295  -1.582   4.367  1.00 10.15           S  
ANISOU  116  SG  CYS A  15     1694    975   1187   -103   -134   -385       S  
ATOM    117  N   SER A  16       1.954   0.326   6.368  1.00  8.76           N  
ANISOU  117  N   SER A  16     1116    899   1312   -299    -76    -18       N  
ATOM    118  CA  SER A  16       2.236   0.634   7.770  1.00  8.96           C  
ANISOU  118  CA  SER A  16     1149    981   1275   -301      4     52       C  
ATOM    119  C   SER A  16       3.663   0.355   8.226  1.00  7.75           C  
ANISOU  119  C   SER A  16     1138    890    916   -299     93    -88       C  
ATOM    120  O   SER A  16       4.136   0.918   9.229  1.00  9.28           O  
ANISOU  120  O   SER A  16     1266   1141   1118   -509    131   -349       O  
ATOM    121  CB  SER A  16       1.256  -0.115   8.679  1.00  9.60           C  
ANISOU  121  CB  SER A  16     1083   1305   1260   -301    -44    152       C  
ATOM    122  OG  SER A  16       1.457  -1.531   8.602  1.00 11.11           O  
ANISOU  122  OG  SER A  16     1685   1224   1311   -542   -172    278       O  
ATOM    123  N   GLY A  17       4.400  -0.515   7.533  1.00  7.54           N  
ANISOU  123  N   GLY A  17     1279    712    875   -179   -146   -104       N  
ATOM    124  CA  GLY A  17       5.791  -0.751   7.871  1.00  8.10           C  
ANISOU  124  CA  GLY A  17     1453    625   1000     24   -217     17       C  
ATOM    125  C   GLY A  17       6.672   0.451   7.612  1.00  7.08           C  
ANISOU  125  C   GLY A  17     1073    739    879     59    -16      2       C  
ATOM    126  O   GLY A  17       7.716   0.674   8.236  1.00  8.01           O  
ANISOU  126  O   GLY A  17     1503    690    852     38   -273      0       O  
ATOM    127  N   CYS A  18       6.290   1.268   6.628  1.00  6.44           N  
ANISOU  127  N   CYS A  18      934    678    833      5    -80    -55       N  
ATOM    128  CA  CYS A  18       7.064   2.467   6.286  1.00  5.96           C  
ANISOU  128  CA  CYS A  18      904    705    657     19    -84    -81       C  
ATOM    129  C   CYS A  18       6.862   3.548   7.327  1.00  5.04           C  
ANISOU  129  C   CYS A  18      828    471    615     45   -110     87       C  
ATOM    130  O   CYS A  18       7.814   4.249   7.732  1.00  6.10           O  
ANISOU  130  O   CYS A  18      924    676    718    -70    -75    -26       O  
ATOM    131  CB  CYS A  18       6.718   2.964   4.889  1.00  6.15           C  
ANISOU  131  CB  CYS A  18     1001    612    722    -31   -215    -57       C  
ATOM    132  SG  CYS A  18       7.264   1.891   3.548  1.00  7.81           S  
ANISOU  132  SG  CYS A  18     1067   1152    747    148   -112   -174       S  
ATOM    133  N   SER A  19       5.606   3.800   7.697  1.00  6.33           N  
ANISOU  133  N   SER A  19      856    753    796     31    -61    -57       N  
ATOM    134  CA  SER A  19       5.358   4.696   8.833  1.00  6.04           C  
ANISOU  134  CA  SER A  19      805    696    792    -16   -113   -155       C  
ATOM    135  C   SER A  19       6.083   4.200  10.078  1.00  5.93           C  
ANISOU  135  C   SER A  19      836    679    741   -210     26    -58       C  
ATOM    136  O   SER A  19       6.623   4.991  10.852  1.00  6.00           O  
ANISOU  136  O   SER A  19      747    734    798    -21   -111   -139       O  
ATOM    137  CB  SER A  19       3.860   4.890   9.023  1.00  7.59           C  
ANISOU  137  CB  SER A  19      794    982   1107    -64     18   -333       C  
ATOM    138  OG  SER A  19       3.166   3.680   9.117  1.00 11.58           O  
ANISOU  138  OG  SER A  19     1117   1157   2128   -304    161   -390       O  
ATOM    139  N   GLY A  20       6.124   2.886  10.277  1.00  6.30           N  
ANISOU  139  N   GLY A  20     1036    717    638   -272     57     60       N  
ATOM    140  CA  GLY A  20       6.834   2.327  11.416  1.00  6.25           C  
ANISOU  140  CA  GLY A  20     1012    735    630   -121     73    -90       C  
ATOM    141  C   GLY A  20       8.328   2.590  11.400  1.00  4.99           C  
ANISOU  141  C   GLY A  20     1012    405    478    -23     83     78       C  
ATOM    142  O   GLY A  20       8.953   2.898  12.415  1.00  5.60           O  
ANISOU  142  O   GLY A  20     1000    583    545   -107     48    -12       O  
ATOM    143  N   ALA A  21       8.953   2.496  10.228  1.00  5.53           N  
ANISOU  143  N   ALA A  21      973    539    589     27     61    126       N  
ATOM    144  CA  ALA A  21      10.391   2.781  10.119  1.00  5.58           C  
ANISOU  144  CA  ALA A  21      853    595    674    198     44     62       C  
ATOM    145  C   ALA A  21      10.720   4.212  10.519  1.00  5.14           C  
ANISOU  145  C   ALA A  21      837    554    564     45    133    157       C  
ATOM    146  O   ALA A  21      11.712   4.502  11.209  1.00  6.37           O  
ANISOU  146  O   ALA A  21      835    613    973     61    -61    119       O  
ATOM    147  CB  ALA A  21      10.850   2.513   8.682  1.00  7.58           C  
ANISOU  147  CB  ALA A  21     1146   1030    703    -10    169   -216       C  
ATOM    148  N   VAL A  22       9.857   5.130  10.078  1.00  5.02           N  
ANISOU  148  N   VAL A  22      782    532    592     50     40     15       N  
ATOM    149  CA  VAL A  22      10.040   6.556  10.372  1.00  4.77           C  
ANISOU  149  CA  VAL A  22      657    489    666    -53    -41     66       C  
ATOM    150  C   VAL A  22       9.831   6.826  11.860  1.00  4.59           C  
ANISOU  150  C   VAL A  22      617    439    689    -10    -21     36       C  
ATOM    151  O   VAL A  22      10.646   7.492  12.522  1.00  5.27           O  
ANISOU  151  O   VAL A  22      665    596    742    -13    -76     18       O  
ATOM    152  CB  VAL A  22       9.108   7.430   9.515  1.00  5.94           C  
ANISOU  152  CB  VAL A  22     1019    493    746     32   -160      6       C  
ATOM    153  CG1 VAL A  22       9.206   8.885   9.956  1.00  7.21           C  
ANISOU  153  CG1 VAL A  22     1367    379    993    -48   -439    186       C  
ATOM    154  CG2 VAL A  22       9.459   7.289   8.033  1.00  7.21           C  
ANISOU  154  CG2 VAL A  22     1310    777    650    -97    -27    265       C  
ATOM    155  N   ASN A  23       8.708   6.292  12.389  1.00  4.92           N  
ANISOU  155  N   ASN A  23      683    589    599    -55    -77    -90       N  
ATOM    156  CA  ASN A  23       8.471   6.397  13.835  1.00  5.51           C  
ANISOU  156  CA  ASN A  23      646    878    570    -11     34    -92       C  
ATOM    157  C   ASN A  23       9.691   5.925  14.628  1.00  5.44           C  
ANISOU  157  C   ASN A  23      611    963    494     -2    124    -94       C  
ATOM    158  O   ASN A  23      10.105   6.590  15.603  1.00  5.52           O  
ANISOU  158  O   ASN A  23      677    904    518    -36     32    -70       O  
ATOM    159  CB  ASN A  23       7.218   5.626  14.249  1.00  5.64           C  
ANISOU  159  CB  ASN A  23      660    803    680    -57     13   -157       C  
ATOM    160  CG  ASN A  23       6.934   5.642  15.753  1.00  6.65           C  
ANISOU  160  CG  ASN A  23      551   1171    803   -237    137   -261       C  
ATOM    161  OD1 ASN A  23       6.558   6.672  16.303  1.00 10.39           O  
ANISOU  161  OD1 ASN A  23     1009   1760   1177    187     50   -715       O  
ATOM    162  ND2 ASN A  23       7.197   4.535  16.408  1.00  8.82           N  
ANISOU  162  ND2 ASN A  23     1471   1327    553   -529    169    -73       N  
ATOM    163  N   LYS A  24      10.259   4.779  14.263  1.00  5.51           N  
ANISOU  163  N   LYS A  24      671    960    462     -3     -5    -61       N  
ATOM    164  CA  LYS A  24      11.332   4.190  15.054  1.00  6.02           C  
ANISOU  164  CA  LYS A  24      947    834    505    -51   -106    142       C  
ATOM    165  C   LYS A  24      12.521   5.141  15.236  1.00  5.39           C  
ANISOU  165  C   LYS A  24      657    743    646    165    -65     83       C  
ATOM    166  O   LYS A  24      13.033   5.305  16.338  1.00  5.77           O  
ANISOU  166  O   LYS A  24      759    882    551    118      1     64       O  
ATOM    167  CB  LYS A  24      11.821   2.881  14.486  1.00  7.49           C  
ANISOU  167  CB  LYS A  24     1096    808    943    -10   -167    159       C  
ATOM    168  CG  LYS A  24      12.868   2.168  15.338  1.00 13.79           C  
ANISOU  168  CG  LYS A  24     1949   1012   2280    274   -972    367       C  
ATOM    169  CD  LYS A  24      13.823   1.380  14.466  1.00 21.11           C  
ANISOU  169  CD  LYS A  24     2700   1606   3716   1235   -975    -88       C  
ATOM    170  CE  LYS A  24      13.099   0.289  13.687  1.00 23.71           C  
ANISOU  170  CE  LYS A  24     4921   1128   2960    578   -613    133       C  
ATOM    171  NZ  LYS A  24      13.010  -0.923  14.546  1.00 19.24           N  
ANISOU  171  NZ  LYS A  24     3050   2871   1389   -489    193    735       N  
ATOM    172  N   VAL A  25      12.958   5.793  14.149  1.00  5.74           N  
ANISOU  172  N   VAL A  25      721    931    528    -32    -16   -156       N  
ATOM    173  CA  VAL A  25      14.159   6.615  14.288  1.00  6.80           C  
ANISOU  173  CA  VAL A  25      688   1275    619   -196     86   -189       C  
ATOM    174  C   VAL A  25      13.874   7.828  15.168  1.00  5.58           C  
ANISOU  174  C   VAL A  25      601    938    581   -141     -3      0       C  
ATOM    175  O   VAL A  25      14.738   8.286  15.909  1.00  6.67           O  
ANISOU  175  O   VAL A  25      636    887   1013    -67   -123   -126       O  
ATOM    176  CB  VAL A  25      14.779   6.948  12.942  1.00  9.44           C  
ANISOU  176  CB  VAL A  25     1111   1829    648   -462    160   -268       C  
ATOM    177  CG1 VAL A  25      15.106   5.708  12.118  1.00 14.83           C  
ANISOU  177  CG1 VAL A  25     1993   2505   1138   -802    814   -908       C  
ATOM    178  CG2 VAL A  25      13.941   7.890  12.120  1.00 13.52           C  
ANISOU  178  CG2 VAL A  25     1224   2664   1250   -832   -130    667       C  
ATOM    179  N   LEU A  26      12.607   8.278  15.186  1.00  5.40           N  
ANISOU  179  N   LEU A  26      643    864    543   -103    -25    184       N  
ATOM    180  CA  LEU A  26      12.211   9.404  15.997  1.00  5.73           C  
ANISOU  180  CA  LEU A  26      602    682    892   -192    -52    135       C  
ATOM    181  C   LEU A  26      12.097   9.024  17.468  1.00  4.54           C  
ANISOU  181  C   LEU A  26      514    480    731    -93    -12    -30       C  
ATOM    182  O   LEU A  26      12.433   9.825  18.348  1.00  5.61           O  
ANISOU  182  O   LEU A  26      716    462    954    -57    -40    -15       O  
ATOM    183  CB  LEU A  26      10.967  10.060  15.392  1.00  6.79           C  
ANISOU  183  CB  LEU A  26      792    580   1206   -136   -162    306       C  
ATOM    184  CG  LEU A  26      11.135  10.585  13.951  1.00  7.50           C  
ANISOU  184  CG  LEU A  26     1035    746   1070     -9    -42    113       C  
ATOM    185  CD1 LEU A  26       9.823  10.920  13.288  1.00  8.21           C  
ANISOU  185  CD1 LEU A  26     1167   1044    908     55    -53    173       C  
ATOM    186  CD2 LEU A  26      12.045  11.806  13.984  1.00 13.14           C  
ANISOU  186  CD2 LEU A  26     1554   1546   1893   -744   -276    985       C  
ATOM    187  N   THR A  27      11.701   7.795  17.775  1.00  4.84           N  
ANISOU  187  N   THR A  27      692    561    584   -132     35    -39       N  
ATOM    188  CA  THR A  27      11.660   7.318  19.140  1.00  4.91           C  
ANISOU  188  CA  THR A  27      671    681    513    -47     79    -75       C  
ATOM    189  C   THR A  27      13.061   7.340  19.777  1.00  5.26           C  
ANISOU  189  C   THR A  27      744    745    510    -87     44    -23       C  
ATOM    190  O   THR A  27      13.190   7.539  20.985  1.00  7.27           O  
ANISOU  190  O   THR A  27      863   1294    604   -151    -33    -90       O  
ATOM    191  CB  THR A  27      11.031   5.927  19.297  1.00  4.80           C  
ANISOU  191  CB  THR A  27      721    718    384    -34    120     56       C  
ATOM    192  OG1 THR A  27      11.875   4.886  18.782  1.00  5.86           O  
ANISOU  192  OG1 THR A  27      761    643    823      5     13     44       O  
ATOM    193  CG2 THR A  27       9.633   5.892  18.697  1.00  5.09           C  
ANISOU  193  CG2 THR A  27      751    535    649   -132    119     78       C  
ATOM    194  N   LYS A  28      14.129   7.151  18.978  1.00  5.15           N  
ANISOU  194  N   LYS A  28      706    552    698    -25     50     -8       N  
ATOM    195  CA  LYS A  28      15.502   7.146  19.514  1.00  5.58           C  
ANISOU  195  CA  LYS A  28      729    701    688     90    -72     -5       C  
ATOM    196  C   LYS A  28      16.002   8.541  19.899  1.00  5.24           C  
ANISOU  196  C   LYS A  28      629    721    642      0     -4     63       C  
ATOM    197  O   LYS A  28      17.062   8.685  20.541  1.00  6.08           O  
ANISOU  197  O   LYS A  28      733    821    757    -50   -145     81       O  
ATOM    198  CB  LYS A  28      16.442   6.491  18.496  1.00  7.41           C  
ANISOU  198  CB  LYS A  28      796   1154    864    410   -163   -151       C  
ATOM    199  CG  LYS A  28      16.115   5.046  18.223  1.00  9.30           C  
ANISOU  199  CG  LYS A  28     1089   1097   1347    566   -358   -343       C  
ATOM    200  CD  LYS A  28      16.916   4.385  17.131  1.00 14.46           C  
ANISOU  200  CD  LYS A  28     1882   1610   2001    733    143   -558       C  
ATOM    201  CE  LYS A  28      16.469   2.959  16.857  1.00 19.20           C  
ANISOU  201  CE  LYS A  28     2729   2114   2454    342   -218  -1503       C  
ATOM    202  NZ  LYS A  28      17.498   2.216  16.081  1.00 21.45           N  
ANISOU  202  NZ  LYS A  28     2372   1474   4306   -414    931  -1223       N  
ATOM    203  N   LEU A  29      15.228   9.564  19.537  1.00  4.98           N  
ANISOU  203  N   LEU A  29      565    630    698    -76   -119    -69       N  
ATOM    204  CA  LEU A  29      15.543  10.949  19.817  1.00  5.42           C  
ANISOU  204  CA  LEU A  29      658    622    778    -60    117     11       C  
ATOM    205  C   LEU A  29      14.716  11.541  20.962  1.00  5.33           C  
ANISOU  205  C   LEU A  29      676    687    664   -228    -14   -171       C  
ATOM    206  O   LEU A  29      14.833  12.714  21.273  1.00  5.99           O  
ANISOU  206  O   LEU A  29      673    767    837   -185     28   -186       O  
ATOM    207  CB  LEU A  29      15.436  11.771  18.535  1.00  5.37           C  
ANISOU  207  CB  LEU A  29      697    557    785    -25     91      4       C  
ATOM    208  CG  LEU A  29      16.264  11.218  17.377  1.00  5.54           C  
ANISOU  208  CG  LEU A  29      785    665    655    -13      8     10       C  
ATOM    209  CD1 LEU A  29      16.093  12.128  16.161  1.00  6.17           C  
ANISOU  209  CD1 LEU A  29      994    644    704    -94    -39     73       C  
ATOM    210  CD2 LEU A  29      17.747  11.058  17.729  1.00  6.36           C  
ANISOU  210  CD2 LEU A  29      737   1007    673     63    127     22       C  
ATOM    211  N   GLU A  30      13.925  10.695  21.602  1.00  5.99           N  
ANISOU  211  N   GLU A  30      739    800    737   -223     83   -170       N  
ATOM    212  CA  GLU A  30      13.314  11.080  22.870  1.00  6.54           C  
ANISOU  212  CA  GLU A  30      868    820    799   -245    118   -133       C  
ATOM    213  C   GLU A  30      14.463  11.271  23.863  1.00  6.36           C  
ANISOU  213  C   GLU A  30      794    873    751   -175    139    -62       C  
ATOM    214  O   GLU A  30      15.527  10.650  23.720  1.00  8.73           O  
ANISOU  214  O   GLU A  30      902   1122   1292    -54   -116   -157       O  
ATOM    215  CB  GLU A  30      12.272  10.029  23.289  1.00  7.28           C  
ANISOU  215  CB  GLU A  30      883   1029    856   -286     50     91       C  
ATOM    216  CG  GLU A  30      11.065   9.945  22.397  1.00  7.04           C  
ANISOU  216  CG  GLU A  30      753    928    994   -144     49    -22       C  
ATOM    217  CD  GLU A  30      10.040   8.905  22.814  1.00  7.01           C  
ANISOU  217  CD  GLU A  30      884    880    900   -190     -9   -108       C  
ATOM    218  OE1 GLU A  30      10.317   7.698  22.650  1.00 12.74           O  
ANISOU  218  OE1 GLU A  30     1056    922   2864   -359    237   -337       O  
ATOM    219  OE2 GLU A  30       8.942   9.306  23.269  1.00  7.86           O  
ANISOU  219  OE2 GLU A  30      746   1204   1035   -194     13    138       O  
ATOM    220  N   PRO A  31      14.337  12.160  24.840  1.00  7.63           N  
ANISOU  220  N   PRO A  31     1084   1017    800   -207    -10   -113       N  
ATOM    221  CA  PRO A  31      13.114  12.891  25.169  1.00  7.72           C  
ANISOU  221  CA  PRO A  31     1297    977    661   -218    239   -270       C  
ATOM    222  C   PRO A  31      12.994  14.281  24.563  1.00  8.32           C  
ANISOU  222  C   PRO A  31     1154   1021    985    -34    172   -254       C  
ATOM    223  O   PRO A  31      12.274  15.120  25.133  1.00 11.06           O  
ANISOU  223  O   PRO A  31     1753   1381   1069    380    347   -113       O  
ATOM    224  CB  PRO A  31      13.224  12.992  26.707  1.00 11.03           C  
ANISOU  224  CB  PRO A  31     2150   1356    686   -233    -12   -372       C  
ATOM    225  CG  PRO A  31      14.695  13.178  26.943  1.00 13.28           C  
ANISOU  225  CG  PRO A  31     2194   1788   1062    294   -446   -416       C  
ATOM    226  CD  PRO A  31      15.367  12.371  25.878  1.00 11.83           C  
ANISOU  226  CD  PRO A  31     1963   1609    923    253   -541   -264       C  
ATOM    227  N   ASP A  32      13.579  14.539  23.391  1.00  6.51           N  
ANISOU  227  N   ASP A  32      799    958    716      0   -112   -189       N  
ATOM    228  CA  ASP A  32      13.521  15.839  22.747  1.00  6.56           C  
ANISOU  228  CA  ASP A  32      604    994    895    184   -240   -194       C  
ATOM    229  C   ASP A  32      12.659  15.859  21.494  1.00  6.83           C  
ANISOU  229  C   ASP A  32      916    931    749    -14   -283   -205       C  
ATOM    230  O   ASP A  32      12.772  16.782  20.698  1.00  9.92           O  
ANISOU  230  O   ASP A  32     1341   1499    930   -630   -563    131       O  
ATOM    231  CB  ASP A  32      14.926  16.413  22.506  1.00  8.05           C  
ANISOU  231  CB  ASP A  32      811   1039   1208   -100   -291     12       C  
ATOM    232  CG  ASP A  32      15.590  16.813  23.818  1.00 11.95           C  
ANISOU  232  CG  ASP A  32     1113   1990   1439   -643   -239   -307       C  
ATOM    233  OD1 ASP A  32      15.291  16.300  24.908  1.00 26.39           O  
ANISOU  233  OD1 ASP A  32     4716   3995   1315  -2828  -1059    189       O  
ATOM    234  OD2 ASP A  32      16.383  17.772  23.836  1.00 13.59           O  
ANISOU  234  OD2 ASP A  32     1515   1791   1856   -645   -554   -344       O  
ATOM    235  N   VAL A  33      11.775  14.887  21.332  1.00  7.69           N  
ANISOU  235  N   VAL A  33     1327    556   1041     94   -734    -72       N  
ATOM    236  CA  VAL A  33      10.718  14.857  20.308  1.00  7.03           C  
ANISOU  236  CA  VAL A  33     1029    578   1064    207   -573   -160       C  
ATOM    237  C   VAL A  33       9.377  14.898  21.012  1.00  6.40           C  
ANISOU  237  C   VAL A  33     1201    619    613   -119   -344     17       C  
ATOM    238  O   VAL A  33       8.999  13.922  21.662  1.00 10.84           O  
ANISOU  238  O   VAL A  33     2522    694    904   -235   -252    176       O  
ATOM    239  CB  VAL A  33      10.831  13.691  19.325  1.00  7.83           C  
ANISOU  239  CB  VAL A  33     1068    635   1271    238   -668   -343       C  
ATOM    240  CG1 VAL A  33       9.673  13.667  18.331  1.00  6.88           C  
ANISOU  240  CG1 VAL A  33      829    868    919    -77   -335    -87       C  
ATOM    241  CG2 VAL A  33      12.133  13.814  18.550  1.00 11.39           C  
ANISOU  241  CG2 VAL A  33      826   1287   2213    332   -498  -1112       C  
ATOM    242  N   SER A  34       8.664  16.001  20.938  1.00  5.62           N  
ANISOU  242  N   SER A  34      858    704    573   -225   -171     82       N  
ATOM    243  CA  SER A  34       7.425  16.201  21.677  1.00  6.95           C  
ANISOU  243  CA  SER A  34      954   1201    485   -232    -67   -146       C  
ATOM    244  C   SER A  34       6.210  15.507  21.054  1.00  5.57           C  
ANISOU  244  C   SER A  34      905    827    385   -176    -17    -30       C  
ATOM    245  O   SER A  34       5.281  15.082  21.768  1.00  7.44           O  
ANISOU  245  O   SER A  34     1029   1355    443   -316     58   -119       O  
ATOM    246  CB  SER A  34       7.160  17.724  21.731  1.00  9.48           C  
ANISOU  246  CB  SER A  34     1205   1125   1274   -248    274   -546       C  
ATOM    247  OG  SER A  34       8.013  18.401  22.611  1.00 15.95           O  
ANISOU  247  OG  SER A  34     1653   1680   2727   -110   -415  -1141       O  
ATOM    248  N   LYS A  35       6.126  15.484  19.737  1.00  5.14           N  
ANISOU  248  N   LYS A  35      738    752    462   -170    -20     -6       N  
ATOM    249  CA  LYS A  35       4.946  14.943  19.029  1.00  4.72           C  
ANISOU  249  CA  LYS A  35      700    671    422    -58     24    -85       C  
ATOM    250  C   LYS A  35       5.404  14.535  17.620  1.00  4.33           C  
ANISOU  250  C   LYS A  35      626    598    420    -75     -8    -25       C  
ATOM    251  O   LYS A  35       6.199  15.265  17.026  1.00  4.21           O  
ANISOU  251  O   LYS A  35      702    448    449   -132     29    -84       O  
ATOM    252  CB  LYS A  35       3.816  15.989  18.911  1.00  4.66           C  
ANISOU  252  CB  LYS A  35      740    541    491   -106     78    -47       C  
ATOM    253  CG  LYS A  35       2.568  15.547  18.178  1.00  6.06           C  
ANISOU  253  CG  LYS A  35      752    540   1012   -126   -129     52       C  
ATOM    254  CD  LYS A  35       1.454  16.559  18.094  1.00  6.76           C  
ANISOU  254  CD  LYS A  35      871    560   1136    -39    -71   -177       C  
ATOM    255  CE  LYS A  35       0.161  16.082  17.487  1.00 13.41           C  
ANISOU  255  CE  LYS A  35     1139   1189   2767    376   -887   -792       C  
ATOM    256  NZ  LYS A  35      -0.809  17.114  17.052  1.00  9.20           N  
ANISOU  256  NZ  LYS A  35     1086   1061   1347     -1   -275     -4       N  
ATOM    257  N   ILE A  36       4.842  13.432  17.145  1.00  3.74           N  
ANISOU  257  N   ILE A  36      448    632    339   -149     28     23       N  
ATOM    258  CA  ILE A  36       4.917  13.124  15.726  1.00  3.98           C  
ANISOU  258  CA  ILE A  36      561    637    314    -11      2     21       C  
ATOM    259  C   ILE A  36       3.498  12.814  15.215  1.00  4.15           C  
ANISOU  259  C   ILE A  36      613    473    490    -65    -60     10       C  
ATOM    260  O   ILE A  36       2.660  12.243  15.931  1.00  4.59           O  
ANISOU  260  O   ILE A  36      581    654    509   -134    -10      9       O  
ATOM    261  CB  ILE A  36       5.913  12.015  15.376  1.00  5.76           C  
ANISOU  261  CB  ILE A  36      714    735    741     77    -55   -330       C  
ATOM    262  CG1 ILE A  36       5.414  10.613  15.618  1.00  6.81           C  
ANISOU  262  CG1 ILE A  36      908    761    919    168   -140     11       C  
ATOM    263  CG2 ILE A  36       7.245  12.276  16.060  1.00  7.72           C  
ANISOU  263  CG2 ILE A  36      739   1382    814    214   -232   -375       C  
ATOM    264  CD1 ILE A  36       6.360   9.576  15.026  1.00  8.84           C  
ANISOU  264  CD1 ILE A  36     1227    715   1416    236   -265   -223       C  
ATOM    265  N   ASP A  37       3.248  13.192  13.967  1.00  4.14           N  
ANISOU  265  N   ASP A  37      588    612    373   -155      5    -35       N  
ATOM    266  CA  ASP A  37       1.997  12.842  13.257  1.00  4.17           C  
ANISOU  266  CA  ASP A  37      553    591    442   -232    -43     11       C  
ATOM    267  C   ASP A  37       2.425  12.229  11.924  1.00  4.49           C  
ANISOU  267  C   ASP A  37      615    667    423   -288    -38      9       C  
ATOM    268  O   ASP A  37       3.173  12.879  11.196  1.00  7.38           O  
ANISOU  268  O   ASP A  37     1250    971    583   -685    182   -120       O  
ATOM    269  CB  ASP A  37       1.072  14.019  13.057  1.00  6.66           C  
ANISOU  269  CB  ASP A  37      882    867    781     47    -75     69       C  
ATOM    270  CG  ASP A  37      -0.283  13.788  12.438  1.00  8.48           C  
ANISOU  270  CG  ASP A  37      898   1380    943    138   -277    174       C  
ATOM    271  OD1 ASP A  37      -0.304  13.152  11.355  1.00  9.80           O  
ANISOU  271  OD1 ASP A  37     1279   1361   1084   -142   -388    135       O  
ATOM    272  OD2 ASP A  37      -1.353  14.145  12.986  1.00 12.36           O  
ANISOU  272  OD2 ASP A  37     1020   1959   1715    141     12    179       O  
ATOM    273  N   ILE A  38       1.952  11.031  11.632  1.00  3.96           N  
ANISOU  273  N   ILE A  38      525    604    376   -167     33     67       N  
ATOM    274  CA  ILE A  38       2.213  10.420  10.324  1.00  4.50           C  
ANISOU  274  CA  ILE A  38      754    577    378   -182    -10      7       C  
ATOM    275  C   ILE A  38       0.856  10.158   9.653  1.00  4.86           C  
ANISOU  275  C   ILE A  38      778    700    370   -185    -22     -6       C  
ATOM    276  O   ILE A  38      -0.045   9.542  10.243  1.00  6.06           O  
ANISOU  276  O   ILE A  38      793    948    561   -354   -109     97       O  
ATOM    277  CB  ILE A  38       3.081   9.159  10.426  1.00  4.97           C  
ANISOU  277  CB  ILE A  38      785    636    468   -161     74    -35       C  
ATOM    278  CG1 ILE A  38       4.403   9.431  11.136  1.00  5.37           C  
ANISOU  278  CG1 ILE A  38      746    744    549    -45     -4     93       C  
ATOM    279  CG2 ILE A  38       3.292   8.573   9.037  1.00  7.02           C  
ANISOU  279  CG2 ILE A  38     1173   1024    470    199    -98   -131       C  
ATOM    280  CD1 ILE A  38       5.408   8.309  11.149  1.00  7.44           C  
ANISOU  280  CD1 ILE A  38     1007    907    914    191    107    -86       C  
ATOM    281  N   SER A  39       0.670  10.666   8.442  1.00  5.46           N  
ANISOU  281  N   SER A  39      772    819    485   -250    -51     51       N  
ATOM    282  CA  SER A  39      -0.500  10.425   7.615  1.00  6.35           C  
ANISOU  282  CA  SER A  39      757   1173    482   -228   -102      4       C  
ATOM    283  C   SER A  39      -0.137   9.699   6.321  1.00  5.67           C  
ANISOU  283  C   SER A  39      668    956    531    -95   -133     89       C  
ATOM    284  O   SER A  39       0.532  10.250   5.451  1.00  6.22           O  
ANISOU  284  O   SER A  39      898    986    479   -233    -53    -27       O  
ATOM    285  CB  SER A  39      -1.191  11.743   7.255  1.00  7.79           C  
ANISOU  285  CB  SER A  39      970   1568    423    248   -179   -224       C  
ATOM    286  OG  SER A  39      -2.325  11.423   6.466  1.00 10.08           O  
ANISOU  286  OG  SER A  39     1158   1848    823    383   -428   -456       O  
ATOM    287  N   LEU A  40      -0.610   8.455   6.192  1.00  5.93           N  
ANISOU  287  N   LEU A  40      692    884    676    -62   -112    100       N  
ATOM    288  CA  LEU A  40      -0.479   7.742   4.937  1.00  6.41           C  
ANISOU  288  CA  LEU A  40      700   1001    735   -145   -109    -30       C  
ATOM    289  C   LEU A  40      -1.382   8.354   3.874  1.00  5.70           C  
ANISOU  289  C   LEU A  40      694    835    635    -48    -55   -113       C  
ATOM    290  O   LEU A  40      -1.016   8.330   2.694  1.00  5.66           O  
ANISOU  290  O   LEU A  40      662    874    615    -36      9    -56       O  
ATOM    291  CB  LEU A  40      -0.768   6.250   5.096  1.00  7.84           C  
ANISOU  291  CB  LEU A  40     1148    941    891   -104   -230     12       C  
ATOM    292  CG  LEU A  40       0.080   5.489   6.129  1.00  8.63           C  
ANISOU  292  CG  LEU A  40     1023   1242   1016   -134   -176    204       C  
ATOM    293  CD1 LEU A  40      -0.434   4.065   6.265  1.00 11.70           C  
ANISOU  293  CD1 LEU A  40     1709   1072   1666    -24    167    341       C  
ATOM    294  CD2 LEU A  40       1.522   5.475   5.678  1.00 11.80           C  
ANISOU  294  CD2 LEU A  40     1102   1644   1737    165    112    300       C  
ATOM    295  N   GLU A  41      -2.517   8.926   4.268  1.00  5.81           N  
ANISOU  295  N   GLU A  41      588   1073    547    -46    -48    -76       N  
ATOM    296  CA  GLU A  41      -3.484   9.528   3.350  1.00  5.95           C  
ANISOU  296  CA  GLU A  41      551   1168    540      0    -48   -165       C  
ATOM    297  C   GLU A  41      -3.025  10.831   2.720  1.00  5.57           C  
ANISOU  297  C   GLU A  41      508   1156    455     76     61   -132       C  
ATOM    298  O   GLU A  41      -3.585  11.215   1.683  1.00  7.09           O  
ANISOU  298  O   GLU A  41      739   1374    581    -93   -244   -114       O  
ATOM    299  CB  GLU A  41      -4.833   9.741   4.064  1.00  8.35           C  
ANISOU  299  CB  GLU A  41      419   2065    687    -70    -64    -23       C  
ATOM    300  CG  GLU A  41      -5.456   8.460   4.547  1.00 13.01           C  
ANISOU  300  CG  GLU A  41      806   2276   1861   -417    469    -81       C  
ATOM    301  CD  GLU A  41      -5.146   7.988   5.946  1.00 26.08           C  
ANISOU  301  CD  GLU A  41     3050   3665   3192   -322    -41   2025       C  
ATOM    302  OE1 GLU A  41      -4.142   8.375   6.584  1.00 24.65           O  
ANISOU  302  OE1 GLU A  41     2347   5305   1713    702    400   1487       O  
ATOM    303  OE2 GLU A  41      -6.002   7.210   6.460  1.00 40.32           O  
ANISOU  303  OE2 GLU A  41     5144   5739   4437  -1774    585   2818       O  
ATOM    304  N   LYS A  42      -1.988  11.477   3.209  1.00  5.54           N  
ANISOU  304  N   LYS A  42      691    871    542    141   -161   -126       N  
ATOM    305  CA  LYS A  42      -1.344  12.665   2.737  1.00  6.26           C  
ANISOU  305  CA  LYS A  42      785    912    683     62    -59    -64       C  
ATOM    306  C   LYS A  42       0.154  12.448   2.481  1.00  5.14           C  
ANISOU  306  C   LYS A  42      761    707    484     42   -150   -119       C  
ATOM    307  O   LYS A  42       0.831  13.334   1.954  1.00  6.10           O  
ANISOU  307  O   LYS A  42      870    679    768     21    -36     -4       O  
ATOM    308  CB  LYS A  42      -1.589  13.856   3.630  1.00  7.64           C  
ANISOU  308  CB  LYS A  42      846    927   1132     67     62   -182       C  
ATOM    309  CG  LYS A  42      -3.024  14.308   3.780  1.00 12.24           C  
ANISOU  309  CG  LYS A  42      961   2375   1314    462     16   -795       C  
ATOM    310  CD  LYS A  42      -3.230  15.579   4.520  1.00 17.13           C  
ANISOU  310  CD  LYS A  42     1554   2373   2582    720    366  -1014       C  
ATOM    311  CE  LYS A  42      -2.426  16.805   4.204  1.00 26.23           C  
ANISOU  311  CE  LYS A  42     4005   2480   3481   -203     82   -788       C  
ATOM    312  NZ  LYS A  42      -2.995  17.672   3.140  1.00 38.73           N  
ANISOU  312  NZ  LYS A  42     6485   4165   4068   -381     59    712       N  
ATOM    313  N   GLN A  43       0.714  11.294   2.815  1.00  4.71           N  
ANISOU  313  N   GLN A  43      669    752    367     18   -111    -42       N  
ATOM    314  CA  GLN A  43       2.130  10.995   2.696  1.00  4.94           C  
ANISOU  314  CA  GLN A  43      565    828    486     19    -88    -40       C  
ATOM    315  C   GLN A  43       2.988  12.037   3.404  1.00  4.22           C  
ANISOU  315  C   GLN A  43      521    674    407     80    -85     81       C  
ATOM    316  O   GLN A  43       4.013  12.523   2.929  1.00  4.55           O  
ANISOU  316  O   GLN A  43      674    576    477     21      3    -13       O  
ATOM    317  CB  GLN A  43       2.563  10.738   1.243  1.00  5.01           C  
ANISOU  317  CB  GLN A  43      745    735    422     16    -23    -31       C  
ATOM    318  CG  GLN A  43       1.816   9.592   0.584  1.00  4.93           C  
ANISOU  318  CG  GLN A  43      623    835    417    -36     87    -54       C  
ATOM    319  CD  GLN A  43       2.384   8.230   0.903  1.00  5.18           C  
ANISOU  319  CD  GLN A  43      618    848    501    -22   -110   -189       C  
ATOM    320  OE1 GLN A  43       3.511   7.928   0.460  1.00  5.93           O  
ANISOU  320  OE1 GLN A  43      666    906    682     21     22    -88       O  
ATOM    321  NE2 GLN A  43       1.677   7.439   1.697  1.00  5.44           N  
ANISOU  321  NE2 GLN A  43      598    741    729     86    -14    -47       N  
ATOM    322  N   LEU A  44       2.558  12.417   4.629  1.00  4.97           N  
ANISOU  322  N   LEU A  44      574    880    436   -139    -39     23       N  
ATOM    323  CA  LEU A  44       3.171  13.463   5.406  1.00  5.15           C  
ANISOU  323  CA  LEU A  44      695    817    446    -46     13     -9       C  
ATOM    324  C   LEU A  44       3.632  12.973   6.781  1.00  4.51           C  
ANISOU  324  C   LEU A  44      701    574    440   -112     -5    -84       C  
ATOM    325  O   LEU A  44       2.912  12.214   7.428  1.00  6.82           O  
ANISOU  325  O   LEU A  44      971   1166    456   -558   -136    112       O  
ATOM    326  CB  LEU A  44       2.200  14.612   5.600  1.00  7.77           C  
ANISOU  326  CB  LEU A  44     1026   1133    794    298   -178   -153       C  
ATOM    327  CG  LEU A  44       1.927  15.518   4.401  1.00  8.90           C  
ANISOU  327  CG  LEU A  44     1403    816   1163     99   -516   -116       C  
ATOM    328  CD1 LEU A  44       0.944  16.611   4.818  1.00 17.01           C  
ANISOU  328  CD1 LEU A  44     1465    822   4178    452   -732   -209       C  
ATOM    329  CD2 LEU A  44       3.222  16.153   3.875  1.00 15.20           C  
ANISOU  329  CD2 LEU A  44     1675   1269   2833     49   -329   1063       C  
ATOM    330  N   VAL A  45       4.780  13.485   7.221  1.00  4.14           N  
ANISOU  330  N   VAL A  45      666    549    357   -165     39     -1       N  
ATOM    331  CA  VAL A  45       5.355  13.271   8.547  1.00  4.23           C  
ANISOU  331  CA  VAL A  45      752    470    385    -66      4     44       C  
ATOM    332  C   VAL A  45       5.561  14.652   9.180  1.00  3.97           C  
ANISOU  332  C   VAL A  45      610    580    318    -81    -97     44       C  
ATOM    333  O   VAL A  45       6.323  15.462   8.643  1.00  5.26           O  
ANISOU  333  O   VAL A  45     1040    520    438   -217    102    -72       O  
ATOM    334  CB  VAL A  45       6.684  12.497   8.507  1.00  4.71           C  
ANISOU  334  CB  VAL A  45      703    519    569   -111      0     44       C  
ATOM    335  CG1 VAL A  45       7.304  12.362   9.886  1.00  5.23           C  
ANISOU  335  CG1 VAL A  45      902    442    644    -77   -196    -46       C  
ATOM    336  CG2 VAL A  45       6.508  11.137   7.858  1.00  4.78           C  
ANISOU  336  CG2 VAL A  45      762    570    486      3     74    -69       C  
ATOM    337  N   ASP A  46       4.925  14.880  10.313  1.00  4.01           N  
ANISOU  337  N   ASP A  46      656    411    458   -142    -33     36       N  
ATOM    338  CA  ASP A  46       5.096  16.123  11.085  1.00  3.99           C  
ANISOU  338  CA  ASP A  46      610    463    443   -110     -9     -8       C  
ATOM    339  C   ASP A  46       5.880  15.768  12.361  1.00  4.02           C  
ANISOU  339  C   ASP A  46      692    447    387   -167     50      9       C  
ATOM    340  O   ASP A  46       5.501  14.819  13.057  1.00  5.16           O  
ANISOU  340  O   ASP A  46      870    670    420   -273    -72    109       O  
ATOM    341  CB  ASP A  46       3.742  16.750  11.416  1.00  5.32           C  
ANISOU  341  CB  ASP A  46      638    566    815    -60     85    -24       C  
ATOM    342  CG  ASP A  46       3.037  17.265  10.181  1.00  6.74           C  
ANISOU  342  CG  ASP A  46      852    592   1119     41   -364   -110       C  
ATOM    343  OD1 ASP A  46       3.316  18.391   9.784  1.00  6.49           O  
ANISOU  343  OD1 ASP A  46      861    710    893    -11   -293    -87       O  
ATOM    344  OD2 ASP A  46       2.243  16.529   9.560  1.00 18.09           O  
ANISOU  344  OD2 ASP A  46     2654    993   3226   -694  -2201    436       O  
ATOM    345  N   VAL A  47       6.947  16.502  12.662  1.00  3.54           N  
ANISOU  345  N   VAL A  47      622    395    327     -1      1     62       N  
ATOM    346  CA  VAL A  47       7.827  16.302  13.811  1.00  3.66           C  
ANISOU  346  CA  VAL A  47      672    414    305     12     41     51       C  
ATOM    347  C   VAL A  47       7.884  17.620  14.610  1.00  3.80           C  
ANISOU  347  C   VAL A  47      645    423    374   -117     42    -15       C  
ATOM    348  O   VAL A  47       8.258  18.656  14.068  1.00  4.46           O  
ANISOU  348  O   VAL A  47      901    451    344   -122     10    -27       O  
ATOM    349  CB  VAL A  47       9.258  15.899  13.423  1.00  4.33           C  
ANISOU  349  CB  VAL A  47      605    417    625    -40    -28    -83       C  
ATOM    350  CG1 VAL A  47      10.135  15.605  14.624  1.00  5.29           C  
ANISOU  350  CG1 VAL A  47      788    551    672     53   -114    -39       C  
ATOM    351  CG2 VAL A  47       9.226  14.692  12.472  1.00  5.56           C  
ANISOU  351  CG2 VAL A  47      694    685    735    152    -74   -286       C  
ATOM    352  N   TYR A  48       7.567  17.543  15.891  1.00  3.45           N  
ANISOU  352  N   TYR A  48      637    266    409    -15     24     33       N  
ATOM    353  CA  TYR A  48       7.676  18.685  16.808  1.00  3.47           C  
ANISOU  353  CA  TYR A  48      559    493    266    -62     17     -3       C  
ATOM    354  C   TYR A  48       8.835  18.369  17.774  1.00  4.06           C  
ANISOU  354  C   TYR A  48      615    572    356    -38     11      0       C  
ATOM    355  O   TYR A  48       8.769  17.363  18.496  1.00  4.72           O  
ANISOU  355  O   TYR A  48      806    512    477    -36    -86     67       O  
ATOM    356  CB  TYR A  48       6.345  18.905  17.547  1.00  4.10           C  
ANISOU  356  CB  TYR A  48      681    412    466     20     67    -74       C  
ATOM    357  CG  TYR A  48       5.176  19.220  16.626  1.00  4.15           C  
ANISOU  357  CG  TYR A  48      551    581    443     76    131   -126       C  
ATOM    358  CD1 TYR A  48       4.431  18.256  15.955  1.00  5.00           C  
ANISOU  358  CD1 TYR A  48      725    723    452     49     -3   -146       C  
ATOM    359  CD2 TYR A  48       4.769  20.534  16.442  1.00  4.59           C  
ANISOU  359  CD2 TYR A  48      714    572    458    -21    147     49       C  
ATOM    360  CE1 TYR A  48       3.353  18.563  15.125  1.00  5.18           C  
ANISOU  360  CE1 TYR A  48      716    676    574    -37    -34    -28       C  
ATOM    361  CE2 TYR A  48       3.681  20.866  15.636  1.00  5.14           C  
ANISOU  361  CE2 TYR A  48      707    551    694     39    166     90       C  
ATOM    362  CZ  TYR A  48       2.973  19.879  14.987  1.00  5.08           C  
ANISOU  362  CZ  TYR A  48      600    840    489     13    135     29       C  
ATOM    363  OH  TYR A  48       1.857  20.154  14.194  1.00  6.20           O  
ANISOU  363  OH  TYR A  48      791    842    724     96    -17    129       O  
ATOM    364  N   THR A  49       9.906  19.161  17.726  1.00  3.81           N  
ANISOU  364  N   THR A  49      498    550    398     48     17     71       N  
ATOM    365  CA  THR A  49      11.169  18.814  18.400  1.00  3.92           C  
ANISOU  365  CA  THR A  49      573    483    434     43    -65    -27       C  
ATOM    366  C   THR A  49      12.013  20.050  18.689  1.00  4.19           C  
ANISOU  366  C   THR A  49      686    536    370     17    -35    -84       C  
ATOM    367  O   THR A  49      11.956  21.042  17.968  1.00  3.96           O  
ANISOU  367  O   THR A  49      478    421    604     39   -104    -38       O  
ATOM    368  CB  THR A  49      11.970  17.834  17.516  1.00  4.52           C  
ANISOU  368  CB  THR A  49      611    502    603     90    -80    -64       C  
ATOM    369  OG1 THR A  49      13.221  17.453  18.106  1.00  5.03           O  
ANISOU  369  OG1 THR A  49      561    513    838     56      3      3       O  
ATOM    370  CG2 THR A  49      12.315  18.462  16.167  1.00  5.25           C  
ANISOU  370  CG2 THR A  49      619    795    583     29    114   -179       C  
ATOM    371  N   THR A  50      12.913  19.952  19.682  1.00  4.48           N  
ANISOU  371  N   THR A  50      701    508    492     15   -135    -66       N  
ATOM    372  CA  THR A  50      13.928  20.945  19.917  1.00  5.02           C  
ANISOU  372  CA  THR A  50      668    561    677     17   -199    -87       C  
ATOM    373  C   THR A  50      15.200  20.746  19.096  1.00  5.07           C  
ANISOU  373  C   THR A  50      823    481    622    -55   -103    -21       C  
ATOM    374  O   THR A  50      16.070  21.623  19.098  1.00  7.29           O  
ANISOU  374  O   THR A  50      850    854   1064   -193    -63   -276       O  
ATOM    375  CB  THR A  50      14.362  21.016  21.405  1.00  6.51           C  
ANISOU  375  CB  THR A  50     1029    849    595   -162   -248   -126       C  
ATOM    376  OG1 THR A  50      14.931  19.739  21.710  1.00  8.44           O  
ANISOU  376  OG1 THR A  50     1220   1083    903    139   -484     17       O  
ATOM    377  CG2 THR A  50      13.185  21.317  22.301  1.00  8.28           C  
ANISOU  377  CG2 THR A  50     1176   1296    674      7   -214   -279       C  
ATOM    378  N   LEU A  51      15.320  19.619  18.416  1.00  4.98           N  
ANISOU  378  N   LEU A  51      617    558    717     24   -158    -70       N  
ATOM    379  CA  LEU A  51      16.532  19.238  17.697  1.00  4.77           C  
ANISOU  379  CA  LEU A  51      514    576    723     28   -240    -15       C  
ATOM    380  C   LEU A  51      16.590  19.907  16.324  1.00  4.82           C  
ANISOU  380  C   LEU A  51      559    611    659    -39   -155    -76       C  
ATOM    381  O   LEU A  51      15.552  20.362  15.807  1.00  5.32           O  
ANISOU  381  O   LEU A  51      604    691    727     -6   -190    102       O  
ATOM    382  CB  LEU A  51      16.588  17.715  17.560  1.00  5.46           C  
ANISOU  382  CB  LEU A  51      684    603    790     82   -121    -53       C  
ATOM    383  CG  LEU A  51      16.556  16.962  18.887  1.00  4.93           C  
ANISOU  383  CG  LEU A  51      501    579    794    100   -146     22       C  
ATOM    384  CD1 LEU A  51      16.506  15.467  18.615  1.00  7.52           C  
ANISOU  384  CD1 LEU A  51     1228    633    997      2    114    -40       C  
ATOM    385  CD2 LEU A  51      17.757  17.303  19.760  1.00  7.09           C  
ANISOU  385  CD2 LEU A  51      782    975    936   -248   -235    342       C  
ATOM    386  N   PRO A  52      17.783  20.016  15.734  1.00  5.44           N  
ANISOU  386  N   PRO A  52      598    686    785    -70   -157     11       N  
ATOM    387  CA  PRO A  52      17.915  20.746  14.478  1.00  5.79           C  
ANISOU  387  CA  PRO A  52      687    627    887    -95    -92     92       C  
ATOM    388  C   PRO A  52      17.289  20.039  13.277  1.00  5.26           C  
ANISOU  388  C   PRO A  52      693    567    740      4    -17     45       C  
ATOM    389  O   PRO A  52      17.273  18.803  13.190  1.00  5.35           O  
ANISOU  389  O   PRO A  52      712    598    721     -1     45     45       O  
ATOM    390  CB  PRO A  52      19.416  20.919  14.283  1.00  9.74           C  
ANISOU  390  CB  PRO A  52      723   1647   1330   -450   -195    574       C  
ATOM    391  CG  PRO A  52      20.130  20.292  15.405  1.00  9.41           C  
ANISOU  391  CG  PRO A  52      689   1131   1754    -24    -60    756       C  
ATOM    392  CD  PRO A  52      19.101  19.700  16.309  1.00  6.08           C  
ANISOU  392  CD  PRO A  52      638    664   1009    -49   -148     48       C  
ATOM    393  N   TYR A  53      16.776  20.833  12.331  1.00  5.82           N  
ANISOU  393  N   TYR A  53      979    537    694    -29    -16     32       N  
ATOM    394  CA  TYR A  53      16.162  20.346  11.105  1.00  5.57           C  
ANISOU  394  CA  TYR A  53      833    645    641     64     24     -8       C  
ATOM    395  C   TYR A  53      17.063  19.378  10.371  1.00  5.34           C  
ANISOU  395  C   TYR A  53      798    564    667     11     17     73       C  
ATOM    396  O   TYR A  53      16.617  18.304   9.956  1.00  5.77           O  
ANISOU  396  O   TYR A  53      819    631    743     21    -10     30       O  
ATOM    397  CB  TYR A  53      15.781  21.541  10.213  1.00  5.54           C  
ANISOU  397  CB  TYR A  53      918    467    721     15     68     -1       C  
ATOM    398  CG  TYR A  53      15.187  21.118   8.892  1.00  5.61           C  
ANISOU  398  CG  TYR A  53      751    740    640     52     55    114       C  
ATOM    399  CD1 TYR A  53      13.842  20.784   8.774  1.00  6.73           C  
ANISOU  399  CD1 TYR A  53      878    928    751   -143    168   -101       C  
ATOM    400  CD2 TYR A  53      15.986  21.028   7.740  1.00  7.41           C  
ANISOU  400  CD2 TYR A  53      870   1254    693    -97    106    108       C  
ATOM    401  CE1 TYR A  53      13.280  20.395   7.571  1.00  7.12           C  
ANISOU  401  CE1 TYR A  53      906   1011    789   -278    114    -51       C  
ATOM    402  CE2 TYR A  53      15.456  20.573   6.553  1.00  6.70           C  
ANISOU  402  CE2 TYR A  53      887   1004    656    117    130     94       C  
ATOM    403  CZ  TYR A  53      14.115  20.257   6.473  1.00  6.96           C  
ANISOU  403  CZ  TYR A  53      994   1023    629      4     38    139       C  
ATOM    404  OH  TYR A  53      13.520  19.854   5.297  1.00  8.76           O  
ANISOU  404  OH  TYR A  53     1177   1384    766   -279     20     24       O  
ATOM    405  N   ASP A  54      18.340  19.755  10.172  1.00  5.67           N  
ANISOU  405  N   ASP A  54      742    700    712     45    -21     64       N  
ATOM    406  CA  ASP A  54      19.254  18.910   9.396  1.00  6.50           C  
ANISOU  406  CA  ASP A  54      861    800    808    -49    196     61       C  
ATOM    407  C   ASP A  54      19.380  17.525   9.996  1.00  6.04           C  
ANISOU  407  C   ASP A  54      730    740    824     40    -52    -29       C  
ATOM    408  O   ASP A  54      19.514  16.527   9.287  1.00  6.88           O  
ANISOU  408  O   ASP A  54      919    807    888     17     65    -74       O  
ATOM    409  CB  ASP A  54      20.653  19.533   9.272  1.00  7.84           C  
ANISOU  409  CB  ASP A  54      881   1008   1091   -112    282    115       C  
ATOM    410  CG  ASP A  54      21.453  19.490  10.557  1.00 10.53           C  
ANISOU  410  CG  ASP A  54     1063   1535   1405     42    -66   -316       C  
ATOM    411  OD1 ASP A  54      21.119  20.254  11.482  1.00 11.45           O  
ANISOU  411  OD1 ASP A  54     1406   1494   1452    114    -47   -275       O  
ATOM    412  OD2 ASP A  54      22.329  18.604  10.710  1.00 15.59           O  
ANISOU  412  OD2 ASP A  54     1867   2408   1648    929   -284   -297       O  
ATOM    413  N   PHE A  55      19.407  17.450  11.328  1.00  5.56           N  
ANISOU  413  N   PHE A  55      748    518    847    118     44    -78       N  
ATOM    414  CA  PHE A  55      19.585  16.192  12.040  1.00  5.41           C  
ANISOU  414  CA  PHE A  55      650    538    869    145    -37    -70       C  
ATOM    415  C   PHE A  55      18.355  15.301  11.868  1.00  4.89           C  
ANISOU  415  C   PHE A  55      751    547    560    127   -127    -20       C  
ATOM    416  O   PHE A  55      18.479  14.112  11.583  1.00  5.30           O  
ANISOU  416  O   PHE A  55      645    602    769    105    -67    -95       O  
ATOM    417  CB  PHE A  55      19.880  16.487  13.504  1.00  5.88           C  
ANISOU  417  CB  PHE A  55      724    597    914    -16   -128    -70       C  
ATOM    418  CG  PHE A  55      20.157  15.274  14.349  1.00  5.34           C  
ANISOU  418  CG  PHE A  55      554    634    843     -8   -216   -170       C  
ATOM    419  CD1 PHE A  55      21.251  14.443  14.111  1.00  5.94           C  
ANISOU  419  CD1 PHE A  55      591    627   1040     18   -234   -140       C  
ATOM    420  CD2 PHE A  55      19.324  15.001  15.420  1.00  6.18           C  
ANISOU  420  CD2 PHE A  55      722    593   1032    -90   -118   -122       C  
ATOM    421  CE1 PHE A  55      21.475  13.342  14.917  1.00  7.20           C  
ANISOU  421  CE1 PHE A  55      739    736   1261    124   -249    -70       C  
ATOM    422  CE2 PHE A  55      19.561  13.902  16.217  1.00  8.27           C  
ANISOU  422  CE2 PHE A  55     1178    923   1040    137    -10     58       C  
ATOM    423  CZ  PHE A  55      20.645  13.063  15.983  1.00  7.60           C  
ANISOU  423  CZ  PHE A  55      863    865   1158    -19   -337    108       C  
ATOM    424  N   ILE A  56      17.152  15.870  12.054  1.00  5.16           N  
ANISOU  424  N   ILE A  56      631    636    693     14     13   -146       N  
ATOM    425  CA  ILE A  56      15.911  15.110  11.856  1.00  4.54           C  
ANISOU  425  CA  ILE A  56      732    448    546     84    -40     32       C  
ATOM    426  C   ILE A  56      15.817  14.592  10.424  1.00  4.81           C  
ANISOU  426  C   ILE A  56      655    573    599     52      1    -30       C  
ATOM    427  O   ILE A  56      15.511  13.432  10.185  1.00  4.97           O  
ANISOU  427  O   ILE A  56      717    495    677     75     32    -72       O  
ATOM    428  CB  ILE A  56      14.658  15.953  12.215  1.00  4.88           C  
ANISOU  428  CB  ILE A  56      624    651    578    -26    154     28       C  
ATOM    429  CG1 ILE A  56      14.675  16.404  13.684  1.00  4.50           C  
ANISOU  429  CG1 ILE A  56      697    462    552     25     44    -22       C  
ATOM    430  CG2 ILE A  56      13.370  15.205  11.865  1.00  5.46           C  
ANISOU  430  CG2 ILE A  56      619    920    534    101    -41   -108       C  
ATOM    431  CD1 ILE A  56      14.707  15.264  14.677  1.00  5.53           C  
ANISOU  431  CD1 ILE A  56      903    608    592    -80     -5      1       C  
ATOM    432  N   LEU A  57      16.081  15.461   9.450  1.00  4.96           N  
ANISOU  432  N   LEU A  57      763    551    570    -71     78    -99       N  
ATOM    433  CA  LEU A  57      16.031  15.083   8.049  1.00  5.13           C  
ANISOU  433  CA  LEU A  57      691    668    588     40    113    -78       C  
ATOM    434  C   LEU A  57      16.996  13.930   7.777  1.00  5.55           C  
ANISOU  434  C   LEU A  57      837    640    633     96     25    -71       C  
ATOM    435  O   LEU A  57      16.591  12.949   7.150  1.00  5.68           O  
ANISOU  435  O   LEU A  57      930    605    625    107     55    -94       O  
ATOM    436  CB  LEU A  57      16.359  16.295   7.184  1.00  5.03           C  
ANISOU  436  CB  LEU A  57      655    615    643    -18     55    -57       C  
ATOM    437  CG  LEU A  57      16.425  16.033   5.667  1.00  5.86           C  
ANISOU  437  CG  LEU A  57      867    770    589     39    111    -76       C  
ATOM    438  CD1 LEU A  57      15.145  15.418   5.132  1.00  7.29           C  
ANISOU  438  CD1 LEU A  57      929   1235    608     82    -19   -254       C  
ATOM    439  CD2 LEU A  57      16.770  17.332   4.963  1.00  9.17           C  
ANISOU  439  CD2 LEU A  57     1732   1041    713    -97    128    145       C  
ATOM    440  N   GLU A  58      18.245  14.053   8.255  1.00  5.45           N  
ANISOU  440  N   GLU A  58      760    653    658     13     78    -75       N  
ATOM    441  CA  GLU A  58      19.235  13.015   8.044  1.00  7.19           C  
ANISOU  441  CA  GLU A  58      764    990    979    152    176    -60       C  
ATOM    442  C   GLU A  58      18.787  11.682   8.607  1.00  6.21           C  
ANISOU  442  C   GLU A  58      769    860    729    345    -49    -17       C  
ATOM    443  O   GLU A  58      18.945  10.610   7.990  1.00  7.48           O  
ANISOU  443  O   GLU A  58     1015   1002    825    141     64   -238       O  
ATOM    444  CB  GLU A  58      20.604  13.426   8.617  1.00 12.41           C  
ANISOU  444  CB  GLU A  58      721   1319   2674    208     51   -341       C  
ATOM    445  CG  GLU A  58      21.141  14.685   7.961  1.00 26.38           C  
ANISOU  445  CG  GLU A  58     2523   2641   4859  -1541    399    235       C  
ATOM    446  CD  GLU A  58      22.447  15.147   8.572  1.00 33.21           C  
ANISOU  446  CD  GLU A  58     3357   4027   5236  -2382   -140    214       C  
ATOM    447  OE1 GLU A  58      22.517  15.276   9.811  1.00 36.06           O  
ANISOU  447  OE1 GLU A  58     1808   6321   5573    833    384  -2540       O  
ATOM    448  OE2 GLU A  58      23.330  15.398   7.729  1.00 36.75           O  
ANISOU  448  OE2 GLU A  58     2515   5911   5539  -2329   -474    670       O  
ATOM    449  N   LYS A  59      18.296  11.698   9.847  1.00  6.15           N  
ANISOU  449  N   LYS A  59      945    688    704    289   -121    -79       N  
ATOM    450  CA  LYS A  59      17.859  10.436  10.468  1.00  6.12           C  
ANISOU  450  CA  LYS A  59     1076    654    594    327    -18   -127       C  
ATOM    451  C   LYS A  59      16.685   9.802   9.739  1.00  6.18           C  
ANISOU  451  C   LYS A  59      967    739    642    174    137    -64       C  
ATOM    452  O   LYS A  59      16.656   8.559   9.595  1.00  6.76           O  
ANISOU  452  O   LYS A  59     1096    674    800    158     57     16       O  
ATOM    453  CB  LYS A  59      17.580  10.635  11.951  1.00  8.27           C  
ANISOU  453  CB  LYS A  59     1449   1089    604    384    -25   -148       C  
ATOM    454  CG  LYS A  59      18.802  10.938  12.799  1.00  8.32           C  
ANISOU  454  CG  LYS A  59     1585    878    697    533   -232   -113       C  
ATOM    455  CD  LYS A  59      19.783   9.774  12.744  1.00  9.97           C  
ANISOU  455  CD  LYS A  59     1696   1116    977    720   -242   -124       C  
ATOM    456  CE  LYS A  59      20.807   9.770  13.830  1.00  9.75           C  
ANISOU  456  CE  LYS A  59     1321   1434    948    537    -83   -107       C  
ATOM    457  NZ  LYS A  59      21.884   8.753  13.662  1.00  9.84           N  
ANISOU  457  NZ  LYS A  59     1149   1180   1410    295   -419    -50       N  
ATOM    458  N   ILE A  60      15.740  10.604   9.251  1.00  5.74           N  
ANISOU  458  N   ILE A  60      844    696    642     57    118    -36       N  
ATOM    459  CA  ILE A  60      14.641  10.033   8.458  1.00  5.97           C  
ANISOU  459  CA  ILE A  60      990    662    618    -25    117     -7       C  
ATOM    460  C   ILE A  60      15.167   9.486   7.141  1.00  6.43           C  
ANISOU  460  C   ILE A  60     1072    693    677    -39     91    -96       C  
ATOM    461  O   ILE A  60      14.827   8.378   6.694  1.00  6.84           O  
ANISOU  461  O   ILE A  60      979    792    830    -95     80   -144       O  
ATOM    462  CB  ILE A  60      13.487  11.045   8.247  1.00  5.79           C  
ANISOU  462  CB  ILE A  60      825    671    703   -129     72    -61       C  
ATOM    463  CG1 ILE A  60      12.863  11.449   9.585  1.00  6.41           C  
ANISOU  463  CG1 ILE A  60      808    948    680   -113    198    -12       C  
ATOM    464  CG2 ILE A  60      12.414  10.483   7.306  1.00  8.64           C  
ANISOU  464  CG2 ILE A  60     1062   1562    658   -294    -23   -108       C  
ATOM    465  CD1 ILE A  60      11.805  12.515   9.470  1.00  7.91           C  
ANISOU  465  CD1 ILE A  60      830    989   1187    -74    194    -70       C  
ATOM    466  N   LYS A  61      16.051  10.219   6.469  1.00  6.27           N  
ANISOU  466  N   LYS A  61      910    749    723     18    141   -128       N  
ATOM    467  CA  LYS A  61      16.570   9.753   5.192  1.00  6.41           C  
ANISOU  467  CA  LYS A  61      843    845    748    -32     70   -217       C  
ATOM    468  C   LYS A  61      17.299   8.426   5.322  1.00  6.41           C  
ANISOU  468  C   LYS A  61      943    803    689    -34    167   -162       C  
ATOM    469  O   LYS A  61      17.294   7.607   4.419  1.00  7.79           O  
ANISOU  469  O   LYS A  61     1496    766    696    -23    204   -208       O  
ATOM    470  CB  LYS A  61      17.497  10.790   4.560  1.00  6.90           C  
ANISOU  470  CB  LYS A  61      811    891    921     54    212   -123       C  
ATOM    471  CG  LYS A  61      16.768  11.992   3.994  1.00  8.30           C  
ANISOU  471  CG  LYS A  61     1123   1030   1002    212    253     33       C  
ATOM    472  CD  LYS A  61      17.678  13.046   3.417  1.00 10.18           C  
ANISOU  472  CD  LYS A  61     1307   1246   1316    -16    215    202       C  
ATOM    473  CE  LYS A  61      18.353  12.594   2.138  1.00 12.92           C  
ANISOU  473  CE  LYS A  61     1829   1876   1203   -318    426    193       C  
ATOM    474  NZ  LYS A  61      17.448  12.693   0.961  1.00 15.09           N  
ANISOU  474  NZ  LYS A  61     2462   2002   1270   -495    111    152       N  
ATOM    475  N   LYS A  62      17.978   8.196   6.447  1.00  7.22           N  
ANISOU  475  N   LYS A  62      980   1005    760    165    116   -239       N  
ATOM    476  CA  LYS A  62      18.716   6.954   6.621  1.00  8.73           C  
ANISOU  476  CA  LYS A  62     1273    987   1057    221     38   -179       C  
ATOM    477  C   LYS A  62      17.866   5.731   6.872  1.00  8.90           C  
ANISOU  477  C   LYS A  62     1367    926   1090    279   -176   -176       C  
ATOM    478  O   LYS A  62      18.416   4.612   6.787  1.00 11.18           O  
ANISOU  478  O   LYS A  62     1669    849   1728    330   -375   -166       O  
ATOM    479  CB  LYS A  62      19.769   7.133   7.733  1.00  9.72           C  
ANISOU  479  CB  LYS A  62     1126   1121   1444    388   -130   -273       C  
ATOM    480  CG  LYS A  62      20.948   8.012   7.349  1.00 13.56           C  
ANISOU  480  CG  LYS A  62      987   1727   2438    302    118   -457       C  
ATOM    481  CD  LYS A  62      21.713   7.620   6.104  1.00 23.28           C  
ANISOU  481  CD  LYS A  62     2518   3485   2842     91   1286    -95       C  
ATOM    482  CE  LYS A  62      21.818   8.748   5.091  1.00 32.45           C  
ANISOU  482  CE  LYS A  62     5744   4321   2265    284    489    272       C  
ATOM    483  NZ  LYS A  62      20.804   8.719   4.004  1.00 40.97           N  
ANISOU  483  NZ  LYS A  62     5528   7104   2937   2119    187   -283       N  
ATOM    484  N   THR A  63      16.549   5.899   6.959  1.00  7.96           N  
ANISOU  484  N   THR A  63     1356    959    709     65    107   -137       N  
ATOM    485  CA  THR A  63      15.654   4.756   6.914  1.00  7.84           C  
ANISOU  485  CA  THR A  63     1559    764    657     81     29    103       C  
ATOM    486  C   THR A  63      15.606   4.122   5.527  1.00  7.79           C  
ANISOU  486  C   THR A  63     1319    882    760    176     89   -128       C  
ATOM    487  O   THR A  63      15.107   3.015   5.386  1.00  9.22           O  
ANISOU  487  O   THR A  63     1581    990    933    -10    271   -183       O  
ATOM    488  CB  THR A  63      14.188   5.085   7.273  1.00  8.00           C  
ANISOU  488  CB  THR A  63     1553    815    672    -76    291    -60       C  
ATOM    489  OG1 THR A  63      13.626   6.064   6.402  1.00  7.78           O  
ANISOU  489  OG1 THR A  63     1062   1071    823   -198    150      1       O  
ATOM    490  CG2 THR A  63      14.129   5.707   8.661  1.00  9.99           C  
ANISOU  490  CG2 THR A  63     1968   1224    606   -184    387     18       C  
ATOM    491  N   GLY A  64      15.989   4.881   4.509  1.00  7.62           N  
ANISOU  491  N   GLY A  64     1332    879    685     94    145   -199       N  
ATOM    492  CA  GLY A  64      15.825   4.452   3.119  1.00  6.80           C  
ANISOU  492  CA  GLY A  64     1194    715    674     71    141   -184       C  
ATOM    493  C   GLY A  64      14.500   4.734   2.483  1.00  6.55           C  
ANISOU  493  C   GLY A  64     1169    704    614     83    267    -61       C  
ATOM    494  O   GLY A  64      14.266   4.453   1.303  1.00  8.09           O  
ANISOU  494  O   GLY A  64     1494    959    620    -34    104    -85       O  
ATOM    495  N   LYS A  65      13.439   5.119   3.105  1.00  7.47           N  
ANISOU  495  N   LYS A  65     1087    916    836     63    198    214       N  
ATOM    496  CA  LYS A  65      12.188   5.682   2.694  1.00  7.25           C  
ANISOU  496  CA  LYS A  65     1114    786    856     86     88    -68       C  
ATOM    497  C   LYS A  65      12.433   7.056   2.070  1.00  7.62           C  
ANISOU  497  C   LYS A  65     1339    603    952    178     57   -135       C  
ATOM    498  O   LYS A  65      13.065   7.912   2.699  1.00 10.59           O  
ANISOU  498  O   LYS A  65     1847    810   1367   -129   -519    149       O  
ATOM    499  CB  LYS A  65      11.157   5.781   3.819  1.00  9.73           C  
ANISOU  499  CB  LYS A  65     1206   1545    945    240    217     88       C  
ATOM    500  CG  LYS A  65      10.977   4.532   4.639  1.00 10.05           C  
ANISOU  500  CG  LYS A  65     1007   1676   1136   -114    328    148       C  
ATOM    501  CD  LYS A  65      10.873   3.267   3.839  1.00 13.31           C  
ANISOU  501  CD  LYS A  65     1942   1862   1251  -1046    -36    138       C  
ATOM    502  CE  LYS A  65      10.898   2.062   4.788  1.00 12.85           C  
ANISOU  502  CE  LYS A  65     1810   1662   1412   -556     17     86       C  
ATOM    503  NZ  LYS A  65      11.010   0.835   3.951  1.00 18.00           N  
ANISOU  503  NZ  LYS A  65     3082   1873   1883   -838   -417   -361       N  
ATOM    504  N   GLU A  66      12.000   7.228   0.841  1.00  6.90           N  
ANISOU  504  N   GLU A  66     1061    653    907     86    204    -96       N  
ATOM    505  CA  GLU A  66      12.303   8.450   0.122  1.00  7.25           C  
ANISOU  505  CA  GLU A  66     1089    853    812     12    285    -91       C  
ATOM    506  C   GLU A  66      11.670   9.689   0.733  1.00  5.33           C  
ANISOU  506  C   GLU A  66      746    658    622      6     91    134       C  
ATOM    507  O   GLU A  66      10.453   9.744   0.938  1.00  6.35           O  
ANISOU  507  O   GLU A  66      721    748    943    -98     45   -113       O  
ATOM    508  CB  GLU A  66      11.812   8.309  -1.318  1.00  7.10           C  
ANISOU  508  CB  GLU A  66     1081    816    801    200    305   -171       C  
ATOM    509  CG  GLU A  66      12.036   9.527  -2.196  1.00 10.23           C  
ANISOU  509  CG  GLU A  66     1761   1039   1086     81    500    131       C  
ATOM    510  CD  GLU A  66      11.455   9.372  -3.591  1.00 13.96           C  
ANISOU  510  CD  GLU A  66     2544   1962    796    171    647    192       C  
ATOM    511  OE1 GLU A  66      10.956   8.283  -3.963  1.00 19.00           O  
ANISOU  511  OE1 GLU A  66     4210   2137    873    156    -10   -315       O  
ATOM    512  OE2 GLU A  66      11.587  10.332  -4.388  1.00 19.77           O  
ANISOU  512  OE2 GLU A  66     4208   2003   1300    994    607    523       O  
ATOM    513  N   VAL A  67      12.508  10.679   1.027  1.00  6.19           N  
ANISOU  513  N   VAL A  67      698    755    899    -71    298    -55       N  
ATOM    514  CA  VAL A  67      12.017  11.976   1.496  1.00  5.61           C  
ANISOU  514  CA  VAL A  67      700    757    674     24    163      2       C  
ATOM    515  C   VAL A  67      12.004  12.918   0.304  1.00  6.04           C  
ANISOU  515  C   VAL A  67      966    697    630   -227    241    -23       C  
ATOM    516  O   VAL A  67      13.066  13.265  -0.227  1.00  9.09           O  
ANISOU  516  O   VAL A  67     1006   1339   1110   -320    402    132       O  
ATOM    517  CB  VAL A  67      12.855  12.560   2.644  1.00  6.48           C  
ANISOU  517  CB  VAL A  67      780    817    865   -202     83     40       C  
ATOM    518  CG1 VAL A  67      12.264  13.902   3.087  1.00  7.86           C  
ANISOU  518  CG1 VAL A  67     1100    918    971   -136   -128   -209       C  
ATOM    519  CG2 VAL A  67      12.940  11.611   3.826  1.00  8.39           C  
ANISOU  519  CG2 VAL A  67     1060   1302    825     77    -11    181       C  
ATOM    520  N   ARG A  68      10.807  13.276  -0.158  1.00  6.01           N  
ANISOU  520  N   ARG A  68     1007    699    577    -10    242     82       N  
ATOM    521  CA  ARG A  68      10.607  14.095  -1.347  1.00  6.99           C  
ANISOU  521  CA  ARG A  68     1525    640    491   -123    279     97       C  
ATOM    522  C   ARG A  68      10.887  15.559  -1.085  1.00  7.57           C  
ANISOU  522  C   ARG A  68     1711    706    460   -110    129     23       C  
ATOM    523  O   ARG A  68      11.401  16.268  -1.957  1.00 11.29           O  
ANISOU  523  O   ARG A  68     2879    652    760   -368    702    -29       O  
ATOM    524  CB  ARG A  68       9.184  13.962  -1.904  1.00 10.48           C  
ANISOU  524  CB  ARG A  68     2196    998    786   -419   -485    331       C  
ATOM    525  CG  ARG A  68       8.775  12.602  -2.408  1.00 13.71           C  
ANISOU  525  CG  ARG A  68     2565   1412   1232   -717   -334   -176       C  
ATOM    526  CD  ARG A  68       9.259  12.294  -3.790  1.00 18.98           C  
ANISOU  526  CD  ARG A  68     2886   3143   1181    428   -881   -799       C  
ATOM    527  NE  ARG A  68       8.807  13.230  -4.786  1.00 18.68           N  
ANISOU  527  NE  ARG A  68     1876   4036   1187    -32   -216     44       N  
ATOM    528  CZ  ARG A  68       7.769  13.266  -5.593  1.00 20.12           C  
ANISOU  528  CZ  ARG A  68     2007   4223   1415   -469   -335    822       C  
ATOM    529  NH1 ARG A  68       6.837  12.332  -5.636  1.00 16.67           N  
ANISOU  529  NH1 ARG A  68     1397   3514   1425    208    -32    291       N  
ATOM    530  NH2 ARG A  68       7.625  14.319  -6.393  1.00 24.80           N  
ANISOU  530  NH2 ARG A  68     2792   4760   1870   -634   -293   1465       N  
ATOM    531  N   SER A  69      10.578  16.023   0.113  1.00  5.96           N  
ANISOU  531  N   SER A  69     1091    685    488   -117     87    -17       N  
ATOM    532  CA  SER A  69      10.732  17.421   0.476  1.00  7.46           C  
ANISOU  532  CA  SER A  69     1560    691    583   -204    179    -40       C  
ATOM    533  C   SER A  69      10.556  17.568   1.981  1.00  5.68           C  
ANISOU  533  C   SER A  69      931    598    630    -53    182    -35       C  
ATOM    534  O   SER A  69       9.965  16.699   2.649  1.00  5.80           O  
ANISOU  534  O   SER A  69      908    675    619   -128    168    -35       O  
ATOM    535  CB  SER A  69       9.705  18.273  -0.245  1.00 11.06           C  
ANISOU  535  CB  SER A  69     2766    755    682    271   -118     16       C  
ATOM    536  OG  SER A  69       8.399  18.028   0.253  1.00 13.17           O  
ANISOU  536  OG  SER A  69     1924    996   2083     74  -1030    -10       O  
ATOM    537  N   GLY A  70      10.975  18.696   2.522  1.00  6.33           N  
ANISOU  537  N   GLY A  70     1162    725    518   -214    281    -40       N  
ATOM    538  CA  GLY A  70      10.692  19.073   3.891  1.00  6.86           C  
ANISOU  538  CA  GLY A  70     1360    737    509    -23    218    -65       C  
ATOM    539  C   GLY A  70      10.662  20.576   4.022  1.00  6.31           C  
ANISOU  539  C   GLY A  70     1046    723    628   -248    137   -101       C  
ATOM    540  O   GLY A  70      11.256  21.320   3.223  1.00  7.28           O  
ANISOU  540  O   GLY A  70     1351    824    592   -258    273    -31       O  
ATOM    541  N   LYS A  71      10.068  21.016   5.118  1.00  5.82           N  
ANISOU  541  N   LYS A  71      940    635    635    -96    148    -49       N  
ATOM    542  CA  LYS A  71      10.043  22.435   5.445  1.00  7.15           C  
ANISOU  542  CA  LYS A  71     1539    615    561   -220     35    -34       C  
ATOM    543  C   LYS A  71       9.763  22.618   6.936  1.00  5.37           C  
ANISOU  543  C   LYS A  71      889    541    611   -148     50     48       C  
ATOM    544  O   LYS A  71       9.405  21.714   7.658  1.00  5.83           O  
ANISOU  544  O   LYS A  71     1115    546    554   -163     97     -9       O  
ATOM    545  CB  LYS A  71       9.031  23.196   4.599  1.00 10.00           C  
ANISOU  545  CB  LYS A  71     2209    950    639    295    -85     37       C  
ATOM    546  CG  LYS A  71       7.572  22.914   4.887  1.00 13.44           C  
ANISOU  546  CG  LYS A  71     1928   2011   1169    654   -244   -183       C  
ATOM    547  CD  LYS A  71       6.659  23.491   3.826  1.00 26.85           C  
ANISOU  547  CD  LYS A  71     2855   4573   2774    838  -1224    881       C  
ATOM    548  CE  LYS A  71       7.327  24.195   2.670  1.00 38.68           C  
ANISOU  548  CE  LYS A  71     5346   5535   3817    150  -1822   2874       C  
ATOM    549  NZ  LYS A  71       7.726  23.290   1.551  1.00 46.87           N  
ANISOU  549  NZ  LYS A  71     6669   8995   2144  -1201   -522   2540       N  
ATOM    550  N   GLN A  72       9.965  23.850   7.375  1.00  6.89           N  
ANISOU  550  N   GLN A  72     1401    637    579   -205    154    -63       N  
ATOM    551  CA  GLN A  72       9.665  24.303   8.718  1.00  6.42           C  
ANISOU  551  CA  GLN A  72     1394    538    508   -150    164     44       C  
ATOM    552  C   GLN A  72       8.374  25.123   8.751  1.00  6.85           C  
ANISOU  552  C   GLN A  72     1380    662    562   -114     36     66       C  
ATOM    553  O   GLN A  72       8.162  25.976   7.885  1.00 10.11           O  
ANISOU  553  O   GLN A  72     2096    767    979    170    243    427       O  
ATOM    554  CB  GLN A  72      10.861  25.024   9.327  1.00  8.10           C  
ANISOU  554  CB  GLN A  72     1407    624   1046    -43     10   -213       C  
ATOM    555  CG  GLN A  72      10.682  25.231  10.815  1.00 12.23           C  
ANISOU  555  CG  GLN A  72     2296   1378    973   -940    -96    -62       C  
ATOM    556  CD  GLN A  72      11.924  25.684  11.543  1.00 13.99           C  
ANISOU  556  CD  GLN A  72     2142   2093   1080   -840   -310    312       C  
ATOM    557  OE1 GLN A  72      13.051  25.847  11.046  1.00 19.15           O  
ANISOU  557  OE1 GLN A  72     2333   3203   1739  -1360   -103    755       O  
ATOM    558  NE2 GLN A  72      11.617  25.941  12.795  1.00 15.03           N  
ANISOU  558  NE2 GLN A  72     1717   2812   1182   -162   -670    -54       N  
ATOM    559  N   LEU A  73       7.512  24.889   9.738  1.00  6.95           N  
ANISOU  559  N   LEU A  73     1315    700    625    100     20    186       N  
ATOM    560  CA  LEU A  73       6.232  25.568   9.883  1.00  7.34           C  
ANISOU  560  CA  LEU A  73     1314    631    845    104    -50    131       C  
ATOM    561  C   LEU A  73       6.094  26.305  11.192  1.00  8.25           C  
ANISOU  561  C   LEU A  73     1325    870    941    203   -184   -112       C  
ATOM    562  O   LEU A  73       7.013  26.268  12.048  1.00 11.22           O  
ANISOU  562  O   LEU A  73     1497   1482   1285    114   -475   -222       O  
ATOM    563  CB  LEU A  73       5.112  24.529   9.739  1.00  7.88           C  
ANISOU  563  CB  LEU A  73     1387    880    726    -11   -271    188       C  
ATOM    564  CG  LEU A  73       4.927  23.861   8.378  1.00 10.53           C  
ANISOU  564  CG  LEU A  73     1715   1358    928    -18   -311   -126       C  
ATOM    565  CD1 LEU A  73       6.062  22.894   8.049  1.00 35.37           C  
ANISOU  565  CD1 LEU A  73     3072   6275   4091   2135   -527  -3333       C  
ATOM    566  CD2 LEU A  73       3.675  22.956   8.370  1.00 16.09           C  
ANISOU  566  CD2 LEU A  73     2993   1398   1723   -857   -240   -516       C  
ATOM    567  OXT LEU A  73       5.031  26.950  11.382  1.00  9.79           O  
ANISOU  567  OXT LEU A  73     1783    966    971    519   -234    -88       O  
TER     568      LEU A  73                                                      
HETATM  569 HG    HG A  74       5.897   0.005   3.783  1.00 10.60          HG  
ANISOU  569 HG    HG A  74     1577   1132   1320      5   -120   -260      HG  
HETATM  570  C1  BEN A 186       6.778  10.510  20.665  1.00  4.96           C  
ANISOU  570  C1  BEN A 186      813    498    574     -9    -69    117       C  
HETATM  571  C2  BEN A 186       5.994   9.710  19.842  1.00  5.48           C  
ANISOU  571  C2  BEN A 186      899    595    588    -45   -207     97       C  
HETATM  572  C3  BEN A 186       6.562   9.055  18.751  1.00  5.92           C  
ANISOU  572  C3  BEN A 186      957    769    524    -16   -165    126       C  
HETATM  573  C4  BEN A 186       7.916   9.259  18.444  1.00  6.52           C  
ANISOU  573  C4  BEN A 186      933    874    672     71   -207     54       C  
HETATM  574  C5  BEN A 186       8.711  10.120  19.210  1.00  5.95           C  
ANISOU  574  C5  BEN A 186      860    655    745     18      3    179       C  
HETATM  575  C6  BEN A 186       8.128  10.734  20.335  1.00  5.84           C  
ANISOU  575  C6  BEN A 186      830    599    789    -26    -92      6       C  
HETATM  576  C   BEN A 186       6.244  11.152  21.851  1.00  5.51           C  
ANISOU  576  C   BEN A 186      899    493    700    -26    -67    -37       C  
HETATM  577  N1  BEN A 186       7.014  11.257  22.910  1.00  6.98           N  
ANISOU  577  N1  BEN A 186     1213    829    611   -176   -186     69       N  
HETATM  578  N2  BEN A 186       4.965  11.590  21.821  1.00  6.99           N  
ANISOU  578  N2  BEN A 186      925    831    899     19     -1   -193       N  
HETATM  579  C1  BEN A 187      -2.553   3.433   3.188  1.00 13.65           C  
ANISOU  579  C1  BEN A 187     2212   1428   1546   -784   -551    418       C  
HETATM  580  C2  BEN A 187      -1.337   3.205   2.508  1.00 14.92           C  
ANISOU  580  C2  BEN A 187     2080   1994   1595   -402   -697    423       C  
HETATM  581  C3  BEN A 187      -0.791   4.128   1.629  1.00 13.52           C  
ANISOU  581  C3  BEN A 187     2237   1750   1150    267   -132    159       C  
HETATM  582  C4  BEN A 187      -1.550   5.259   1.337  1.00 12.54           C  
ANISOU  582  C4  BEN A 187     1769   1845   1150    141   -370    113       C  
HETATM  583  C5  BEN A 187      -2.797   5.495   1.902  1.00  9.96           C  
ANISOU  583  C5  BEN A 187     1462   1280   1042   -335   -575     31       C  
HETATM  584  C6  BEN A 187      -3.296   4.579   2.847  1.00 13.84           C  
ANISOU  584  C6  BEN A 187     1846   1682   1732   -707   -538    342       C  
HETATM  585  C   BEN A 187      -3.074   2.290   3.932  1.00 22.17           C  
ANISOU  585  C   BEN A 187     4745   1664   2013   -517    982    523       C  
HETATM  586  N1  BEN A 187      -3.970   2.454   4.841  1.00 23.93           N  
ANISOU  586  N1  BEN A 187     5527   1978   1589   -757   1200     52       N  
HETATM  587  N2  BEN A 187      -2.208   1.221   3.932  1.00 29.56           N  
ANISOU  587  N2  BEN A 187     7488   1359   2385    393   1779    447       N  
HETATM  588  O   HOH A1001      17.616   8.247  15.310  1.00  7.94           O  
ANISOU  588  O   HOH A1001     1006   1006   1006      0      0      0       O  
HETATM  589  O   HOH A1002       7.788  26.848  17.598  1.00  5.64           O  
ANISOU  589  O   HOH A1002      714    714    714      0      0      0       O  
HETATM  590  O   HOH A1003      19.740   7.804  17.090  1.00  8.59           O  
ANISOU  590  O   HOH A1003     1088   1088   1088      0      0      0       O  
HETATM  591  O   HOH A1004      15.306  24.210  20.260  1.00 11.37           O  
ANISOU  591  O   HOH A1004     1440   1440   1440      0      0      0       O  
HETATM  592  O   HOH A1005       9.088  25.617  13.651  1.00  9.23           O  
ANISOU  592  O   HOH A1005     1169   1169   1169      0      0      0       O  
HETATM  593  O   HOH A1006      18.284   6.706  10.932  1.00  9.47           O  
ANISOU  593  O   HOH A1006     1199   1199   1199      0      0      0       O  
HETATM  594  O   HOH A1007      15.474  10.474   0.756  1.00  9.84           O  
ANISOU  594  O   HOH A1007     1246   1246   1246      0      0      0       O  
HETATM  595  O   HOH A1008      -4.607  12.567   8.831  1.00  8.57           O  
ANISOU  595  O   HOH A1008     1085   1085   1085      0      0      0       O  
HETATM  596  O   HOH A1009       0.991  14.171   9.092  1.00  9.40           O  
ANISOU  596  O   HOH A1009     1191   1191   1191      0      0      0       O  
HETATM  597  O   HOH A1010       8.186   2.217  14.943  1.00  8.96           O  
ANISOU  597  O   HOH A1010     1135   1135   1135      0      0      0       O  
HETATM  598  O   HOH A1011      15.781   8.125   2.080  1.00 11.19           O  
ANISOU  598  O   HOH A1011     1417   1417   1417      0      0      0       O  
HETATM  599  O   HOH A1012       9.043  27.744   2.341  1.00  8.14           O  
ANISOU  599  O   HOH A1012     1031   1031   1031      0      0      0       O  
HETATM  600  O   HOH A1013      18.168   6.153  13.551  1.00 12.87           O  
ANISOU  600  O   HOH A1013     1630   1630   1630      0      0      0       O  
HETATM  601  O   HOH A1014      14.958  20.095   3.073  1.00 12.55           O  
ANISOU  601  O   HOH A1014     1589   1589   1589      0      0      0       O  
HETATM  602  O   HOH A1015      15.221   5.279  -0.979  1.00 13.31           O  
ANISOU  602  O   HOH A1015     1686   1686   1686      0      0      0       O  
HETATM  603  O   HOH A1016      10.901   4.955  -0.726  1.00 12.77           O  
ANISOU  603  O   HOH A1016     1617   1617   1617      0      0      0       O  
HETATM  604  O   HOH A1017      -0.368  -1.085   5.462  1.00 14.79           O  
ANISOU  604  O   HOH A1017     1873   1873   1873      0      0      0       O  
HETATM  605  O   HOH A1018       7.866  27.802   5.388  1.00 17.16           O  
ANISOU  605  O   HOH A1018     2173   2173   2173      0      0      0       O  
HETATM  606  O   HOH A1019      10.513   5.777  -3.346  1.00 14.90           O  
ANISOU  606  O   HOH A1019     1887   1887   1887      0      0      0       O  
HETATM  607  O   HOH A1020      19.321  22.451  10.785  1.00 14.94           O  
ANISOU  607  O   HOH A1020     1892   1892   1892      0      0      0       O  
HETATM  608  O   HOH A1021      13.882   2.702  11.385  1.00 14.52           O  
ANISOU  608  O   HOH A1021     1839   1839   1839      0      0      0       O  
HETATM  609  O   HOH A1022      -0.005  18.132  14.411  1.00 15.92           O  
ANISOU  609  O   HOH A1022     2016   2016   2016      0      0      0       O  
HETATM  610  O   HOH A1023       8.700   3.800   0.678  1.00 15.06           O  
ANISOU  610  O   HOH A1023     1907   1907   1907      0      0      0       O  
HETATM  611  O   HOH A1024      11.137  25.942   5.586  1.00 15.64           O  
ANISOU  611  O   HOH A1024     1981   1981   1981      0      0      0       O  
HETATM  612  O   HOH A1025      23.043  21.198  13.218  1.00 12.49           O  
ANISOU  612  O   HOH A1025     1582   1582   1582      0      0      0       O  
HETATM  613  O   HOH A1026      10.351  12.943  23.642  1.00 14.56           O  
ANISOU  613  O   HOH A1026     1844   1844   1844      0      0      0       O  
HETATM  614  O   HOH A1027      17.408  23.420  22.024  1.00 22.66           O  
ANISOU  614  O   HOH A1027     2870   2870   2870      0      0      0       O  
HETATM  615  O   HOH A1028      10.645  18.582  21.891  1.00 16.24           O  
ANISOU  615  O   HOH A1028     2057   2057   2057      0      0      0       O  
HETATM  616  O   HOH A1029       6.814  17.051  -1.761  1.00 16.27           O  
ANISOU  616  O   HOH A1029     2061   2061   2061      0      0      0       O  
HETATM  617  O   HOH A1030      24.879  21.422  11.090  1.00 19.36           O  
ANISOU  617  O   HOH A1030     2452   2452   2452      0      0      0       O  
HETATM  618  O   HOH A1031       2.062  -2.830  10.994  1.00 13.70           O  
ANISOU  618  O   HOH A1031     1735   1735   1735      0      0      0       O  
HETATM  619  O   HOH A1032      17.840   4.071   9.868  1.00 23.49           O  
ANISOU  619  O   HOH A1032     2975   2975   2975      0      0      0       O  
HETATM  620  O   HOH A1033      12.679   6.080  23.452  1.00 18.88           O  
ANISOU  620  O   HOH A1033     2391   2391   2391      0      0      0       O  
HETATM  621  O   HOH A1034      13.989   1.203   3.508  1.00 16.88           O  
ANISOU  621  O   HOH A1034     2138   2138   2138      0      0      0       O  
HETATM  622  O   HOH A1035       4.973  29.360  12.493  1.00 13.56           O  
ANISOU  622  O   HOH A1035     1717   1717   1717      0      0      0       O  
HETATM  623  O   HOH A1036      17.267  23.789  12.875  1.00 16.28           O  
ANISOU  623  O   HOH A1036     2062   2062   2062      0      0      0       O  
HETATM  624  O   HOH A1037      -2.194  15.327  15.082  1.00 19.05           O  
ANISOU  624  O   HOH A1037     2413   2413   2413      0      0      0       O  
HETATM  625  O   HOH A1038      17.725  22.862  17.146  1.00 17.23           O  
ANISOU  625  O   HOH A1038     2182   2182   2182      0      0      0       O  
HETATM  626  O   HOH A1039      -1.066   0.180   1.359  1.00 19.12           O  
ANISOU  626  O   HOH A1039     2422   2422   2422      0      0      0       O  
HETATM  627  O   HOH A1040      13.599  22.701   3.492  1.00 24.22           O  
ANISOU  627  O   HOH A1040     3067   3067   3067      0      0      0       O  
HETATM  628  O   HOH A1041      14.167   1.345   7.218  1.00 20.56           O  
ANISOU  628  O   HOH A1041     2604   2604   2604      0      0      0       O  
HETATM  629  O   HOH A1042      15.108   7.248  23.019  1.00 20.34           O  
ANISOU  629  O   HOH A1042     2576   2576   2576      0      0      0       O  
HETATM  630  O   HOH A1043       9.833  29.184  14.302  1.00 20.92           O  
ANISOU  630  O   HOH A1043     2650   2650   2650      0      0      0       O  
HETATM  631  O   HOH A1044      12.756  16.878  27.310  1.00 16.27           O  
ANISOU  631  O   HOH A1044     2061   2061   2061      0      0      0       O  
HETATM  632  O   HOH A1045       0.358   3.935   9.734  1.00 26.51           O  
ANISOU  632  O   HOH A1045     3358   3358   3358      0      0      0       O  
HETATM  633  O   HOH A1046      15.402  27.809  21.589  1.00 20.37           O  
ANISOU  633  O   HOH A1046     2580   2580   2580      0      0      0       O  
HETATM  634  O   HOH A1047      22.105   5.095  14.239  1.00 33.84           O  
ANISOU  634  O   HOH A1047     4286   4286   4286      0      0      0       O  
HETATM  635  O   HOH A1048       3.366   1.920  11.836  1.00 15.34           O  
ANISOU  635  O   HOH A1048     1943   1943   1943      0      0      0       O  
HETATM  636  O   HOH A1049      13.969  26.024   8.265  1.00 19.99           O  
ANISOU  636  O   HOH A1049     2532   2532   2532      0      0      0       O  
HETATM  637  O   HOH A1050       7.367  19.311   3.002  1.00 24.37           O  
ANISOU  637  O   HOH A1050     3086   3086   3086      0      0      0       O  
HETATM  638  O   HOH A1051      13.629   1.422  -1.238  1.00 38.99           O  
ANISOU  638  O   HOH A1051     4938   4938   4938      0      0      0       O  
HETATM  639  O   HOH A1052       9.816  -1.158   9.253  1.00 34.42           O  
ANISOU  639  O   HOH A1052     4359   4359   4359      0      0      0       O  
HETATM  640  O   HOH A1053       8.217   1.109   0.522  1.00 17.09           O  
ANISOU  640  O   HOH A1053     2164   2164   2164      0      0      0       O  
HETATM  641  O   HOH A1054      -1.422  15.069   7.675  1.00 27.26           O  
ANISOU  641  O   HOH A1054     3453   3453   3453      0      0      0       O  
HETATM  642  O   HOH A1055      15.533  25.642  12.903  1.00 28.86           O  
ANISOU  642  O   HOH A1055     3655   3655   3655      0      0      0       O  
HETATM  643  O   HOH A1056      -2.456   7.357   8.315  1.00 32.29           O  
ANISOU  643  O   HOH A1056     4090   4090   4090      0      0      0       O  
HETATM  644  O   HOH A1057      -3.865   4.934   7.261  1.00 25.36           O  
ANISOU  644  O   HOH A1057     3212   3212   3212      0      0      0       O  
HETATM  645  O   HOH A1058      10.154  15.808  -5.074  1.00 32.28           O  
ANISOU  645  O   HOH A1058     4088   4088   4088      0      0      0       O  
HETATM  646  O   HOH A1059      14.392  24.062   6.799  1.00 31.43           O  
ANISOU  646  O   HOH A1059     3981   3981   3981      0      0      0       O  
HETATM  647  O   HOH A1060       8.212   2.856  -2.729  1.00 37.74           O  
ANISOU  647  O   HOH A1060     4780   4780   4780      0      0      0       O  
HETATM  648  O   HOH A1061       8.669  28.931  12.142  1.00 19.02           O  
ANISOU  648  O   HOH A1061     2409   2409   2409      0      0      0       O  
HETATM  649  O   HOH A1062      16.476  26.837  19.562  1.00 26.77           O  
ANISOU  649  O   HOH A1062     3390   3390   3390      0      0      0       O  
HETATM  650  O   HOH A1063      14.493  30.605  19.958  1.00 31.26           O  
ANISOU  650  O   HOH A1063     3959   3959   3959      0      0      0       O  
HETATM  651  O   HOH A1064       4.811  19.687   2.798  1.00 19.34           O  
ANISOU  651  O   HOH A1064     2449   2449   2449      0      0      0       O  
HETATM  652  O   HOH A1065      26.289  12.649   6.622  1.00 27.59           O  
ANISOU  652  O   HOH A1065     3494   3494   3494      0      0      0       O  
HETATM  653  O   HOH A1066      21.051   6.421  10.619  1.00 20.88           O  
ANISOU  653  O   HOH A1066     2644   2644   2644      0      0      0       O  
HETATM  654  O   HOH A1067      16.739   2.308  11.902  1.00 27.03           O  
ANISOU  654  O   HOH A1067     3423   3423   3423      0      0      0       O  
HETATM  655  O   HOH A1068      11.027  28.995  11.387  1.00 34.49           O  
ANISOU  655  O   HOH A1068     4368   4368   4368      0      0      0       O  
HETATM  656  O   HOH A1069       0.659  -5.373  10.338  1.00 20.19           O  
ANISOU  656  O   HOH A1069     2557   2557   2557      0      0      0       O  
HETATM  657  O   HOH A1070      13.126  12.568  -4.040  1.00 30.85           O  
ANISOU  657  O   HOH A1070     3907   3907   3907      0      0      0       O  
HETATM  658  O   HOH A1071       4.262  -2.108   0.738  1.00 28.30           O  
ANISOU  658  O   HOH A1071     3584   3584   3584      0      0      0       O  
HETATM  659  O   HOH A1072      17.019   7.517  -0.249  1.00 22.35           O  
ANISOU  659  O   HOH A1072     2831   2831   2831      0      0      0       O  
HETATM  660  O   HOH A1073       0.989   1.466  12.601  1.00 23.75           O  
ANISOU  660  O   HOH A1073     3008   3008   3008      0      0      0       O  
HETATM  661  O   HOH A1074      22.437   8.753  10.589  1.00 35.20           O  
ANISOU  661  O   HOH A1074     4458   4458   4458      0      0      0       O  
HETATM  662  O   HOH A1075       8.127  17.699  -4.165  1.00 25.84           O  
ANISOU  662  O   HOH A1075     3273   3273   3273      0      0      0       O  
HETATM  663  O   HOH A1076       0.252  22.153   7.142  1.00 29.72           O  
ANISOU  663  O   HOH A1076     3764   3764   3764      0      0      0       O  
HETATM  664  O   HOH A1077      20.247   5.579  16.818  1.00 39.86           O  
ANISOU  664  O   HOH A1077     5048   5048   5048      0      0      0       O  
HETATM  665  O   HOH A1078      28.047  20.920  10.605  1.00 49.11           O  
ANISOU  665  O   HOH A1078     6220   6220   6220      0      0      0       O  
HETATM  666  O   HOH A1079      17.087  28.399  23.725  1.00 29.54           O  
ANISOU  666  O   HOH A1079     3741   3741   3741      0      0      0       O  
HETATM  667  O   HOH A1080      -1.538   3.888  12.049  1.00 42.97           O  
ANISOU  667  O   HOH A1080     5442   5442   5442      0      0      0       O  
HETATM  668  O   HOH A1081      22.919  10.104   8.434  1.00 30.92           O  
ANISOU  668  O   HOH A1081     3916   3916   3916      0      0      0       O  
HETATM  669  O   HOH A1082       2.561  22.712   4.893  1.00 35.03           O  
ANISOU  669  O   HOH A1082     4437   4437   4437      0      0      0       O  
HETATM  670  O   HOH A1083      -0.344  17.832   9.512  1.00 34.60           O  
ANISOU  670  O   HOH A1083     4382   4382   4382      0      0      0       O  
HETATM  671  O   HOH A1084       8.152  17.267  -8.285  1.00 29.67           O  
ANISOU  671  O   HOH A1084     3758   3758   3758      0      0      0       O  
HETATM  672  O   HOH A1085      -4.543  16.188   7.860  1.00 38.10           O  
ANISOU  672  O   HOH A1085     4825   4825   4825      0      0      0       O  
HETATM  673  O   HOH A1086      18.721   9.864   1.672  1.00 31.64           O  
ANISOU  673  O   HOH A1086     4007   4007   4007      0      0      0       O  
HETATM  674  O   HOH A1087       7.824   1.096  -4.715  1.00 44.70           O  
ANISOU  674  O   HOH A1087     5661   5661   5661      0      0      0       O  
HETATM  675  O   HOH A1088       2.661  24.863   3.932  1.00 30.82           O  
ANISOU  675  O   HOH A1088     3903   3903   3903      0      0      0       O  
HETATM  676  O   HOH A1089       0.175  -7.724  10.899  1.00 28.44           O  
ANISOU  676  O   HOH A1089     3602   3602   3602      0      0      0       O  
HETATM  677  O   HOH A1090      24.737  11.092   4.411  1.00 34.84           O  
ANISOU  677  O   HOH A1090     4413   4413   4413      0      0      0       O  
HETATM  678  O   HOH A1091      16.708  30.878  21.040  1.00 39.21           O  
ANISOU  678  O   HOH A1091     4966   4966   4966      0      0      0       O  
HETATM  679  O   HOH A1092      13.119   3.560  -0.566  1.00 34.87           O  
ANISOU  679  O   HOH A1092     4416   4416   4416      0      0      0       O  
HETATM  680  O   HOH A1093      -5.018  19.100   2.687  1.00 64.30           O  
ANISOU  680  O   HOH A1093     8144   8144   8144      0      0      0       O  
HETATM  681  O   HOH A1094      16.851  27.903  15.081  1.00 20.67           O  
ANISOU  681  O   HOH A1094     2618   2618   2618      0      0      0       O  
HETATM  682  O   HOH A1095      15.528   2.201   9.313  1.00 29.43           O  
ANISOU  682  O   HOH A1095     3727   3727   3727      0      0      0       O  
HETATM  683  O   HOH A1096       5.414  22.388  -0.132  1.00 47.90           O  
ANISOU  683  O   HOH A1096     6067   6067   6067      0      0      0       O  
HETATM  684  O   HOH A1097      -3.613   9.137   9.430  1.00 26.58           O  
ANISOU  684  O   HOH A1097     3366   3366   3366      0      0      0       O  
HETATM  685  O   HOH A1098      -1.637  -5.500  10.285  1.00 31.85           O  
ANISOU  685  O   HOH A1098     4034   4034   4034      0      0      0       O  
HETATM  686  O   HOH A1099      14.574   7.143  25.450  1.00 46.35           O  
ANISOU  686  O   HOH A1099     5870   5870   5870      0      0      0       O  
HETATM  687  O   HOH A1100      26.128  14.886   6.158  1.00 49.82           O  
ANISOU  687  O   HOH A1100     6310   6310   6310      0      0      0       O  
HETATM  688  O   HOH A1101      28.667  11.791   6.490  1.00 40.09           O  
ANISOU  688  O   HOH A1101     5077   5077   5077      0      0      0       O  
HETATM  689  O   HOH A1102      19.855  23.936  16.260  1.00 37.69           O  
ANISOU  689  O   HOH A1102     4773   4773   4773      0      0      0       O  
HETATM  690  O   HOH A1103      -0.301  -2.484   1.174  0.50 33.56           O  
ANISOU  690  O   HOH A1103     4250   4250   4250      0      0      0       O  
HETATM  691  O   HOH A1104      -3.492  14.956  11.321  1.00 28.59           O  
ANISOU  691  O   HOH A1104     3621   3621   3621      0      0      0       O  
HETATM  692  O   HOH A1105      14.744  26.844  17.123  1.00 51.02           O  
ANISOU  692  O   HOH A1105     6462   6462   6462      0      0      0       O  
HETATM  693  O   HOH A1106      14.544  12.895  -2.262  1.00 32.47           O  
ANISOU  693  O   HOH A1106     4112   4112   4112      0      0      0       O  
HETATM  694  O   HOH A1107      10.065   9.307  -6.233  1.00 35.80           O  
ANISOU  694  O   HOH A1107     4534   4534   4534      0      0      0       O  
HETATM  695  O   HOH A1108      23.449   5.213   9.064  1.00 38.80           O  
ANISOU  695  O   HOH A1108     4914   4914   4914      0      0      0       O  
HETATM  696  O   HOH A1109      24.477  13.613   4.617  1.00 35.58           O  
ANISOU  696  O   HOH A1109     4506   4506   4506      0      0      0       O  
HETATM  697  O   HOH A1110      19.307   2.563  12.439  1.00 30.95           O  
ANISOU  697  O   HOH A1110     3920   3920   3920      0      0      0       O  
HETATM  698  O   HOH A1111      11.668   2.082   0.348  1.00 53.60           O  
ANISOU  698  O   HOH A1111     6789   6789   6789      0      0      0       O  
HETATM  699  O   HOH A1112       2.128  15.527   0.790  1.00 40.18           O  
ANISOU  699  O   HOH A1112     5089   5089   5089      0      0      0       O  
HETATM  700  O   HOH A1113      11.617  28.291   6.349  0.50 24.45           O  
ANISOU  700  O   HOH A1113     3097   3097   3097      0      0      0       O  
HETATM  701  O   HOH A1114      17.590  28.365  21.334  1.00 34.65           O  
ANISOU  701  O   HOH A1114     4388   4388   4388      0      0      0       O  
HETATM  702  O   HOH A1115      24.804  19.497   9.633  1.00 49.69           O  
ANISOU  702  O   HOH A1115     6293   6293   6293      0      0      0       O  
HETATM  703  O   HOH A1116       9.141   4.823  -4.924  0.50 34.59           O  
ANISOU  703  O   HOH A1116     4381   4381   4381      0      0      0       O  
HETATM  704  O   HOH A1117       7.126  17.929  -6.363  1.00 45.52           O  
ANISOU  704  O   HOH A1117     5765   5765   5765      0      0      0       O  
CONECT  109  569                                                                
CONECT  111  569                                                                
CONECT  114  569                                                                
CONECT  116  569                                                                
CONECT  127  569                                                                
CONECT  132  569                                                                
CONECT  569  109  111  114  116                                                 
CONECT  569  127  132                                                           
CONECT  570  571  575  576                                                      
CONECT  571  570  572                                                           
CONECT  572  571  573                                                           
CONECT  573  572  574                                                           
CONECT  574  573  575                                                           
CONECT  575  570  574                                                           
CONECT  576  570  577  578                                                      
CONECT  577  576                                                                
CONECT  578  576                                                                
CONECT  579  580  584  585                                                      
CONECT  580  579  581                                                           
CONECT  581  580  582                                                           
CONECT  582  581  583                                                           
CONECT  583  582  584                                                           
CONECT  584  579  583                                                           
CONECT  585  579  586  587                                                      
CONECT  586  585                                                                
CONECT  587  585                                                                
MASTER      232    0    3    2    4    0    5    6  703    1   26    6          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.