CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  vignesh_p1  ***

elNémo ID: 220124011540115778

Job options:

ID        	=	 220124011540115778
JOBID     	=	 vignesh_p1
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 vignesh_p1

HEADER    OXIDOREDUCTASE                          14-MAR-05   1Z3N              
TITLE     HUMAN ALDOSE REDUCTASE IN COMPLEX WITH NADP+ AND THE                  
TITLE    2 INHIBITOR LIDORESTAT AT 1.04 ANGSTROM                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDOSE REDUCTASE;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.1.1.21;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
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_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    OXIDOREDUCTASE, NADP+, LIDORESTAT                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.VAN ZANDT,M.L.JONES,D.E.GUNN,L.S.GERACI,J.H.JONES,                
AUTHOR   2 D.R.SAWICKI,J.SREDY,J.L.JACOT,A.T.DICIOCCIO,T.PETROVA,               
AUTHOR   3 A.MITSCHLER,A.D.PODJARNY                                             
REVDAT   2   24-FEB-09 1Z3N    1       VERSN                                    
REVDAT   1   14-MAR-06 1Z3N    0                                                
JRNL        AUTH   M.C.VAN ZANDT,M.L.JONES,D.E.GUNN,L.S.GERACI,                 
JRNL        AUTH 2 J.H.JONES,D.R.SAWICKI,J.SREDY,J.L.JACOT,                     
JRNL        AUTH 3 A.T.DICIOCCIO,T.PETROVA,A.MITSCHLER,A.D.PODJARNY             
JRNL        TITL   DISCOVERY OF                                                 
JRNL        TITL 2 3-[(4,5,7-TRIFLUOROBENZOTHIAZOL-2-YL)METHYL]INDOLE-          
JRNL        TITL 3 N-ACETIC ACID (LIDORESTAT) AND CONGENERS AS HIGHLY           
JRNL        TITL 4 POTENT AND SELECTIVE INHIBITORS OF ALDOSE                    
JRNL        TITL 5 REDUCTASE FOR TREATMENT OF CHRONIC DIABETIC                  
JRNL        TITL 6 COMPLICATIONS                                                
JRNL        REF    J.MED.CHEM.                   V.  48  3141 2005              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   15857120                                                     
JRNL        DOI    10.1021/JM0492094                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.04 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) : 1.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.3                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
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) : 0.098                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.097                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.125                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 6975                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 132616                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.090                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.118                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 6201                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 117067                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2974                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 74                                            
REMARK   3   SOLVENT ATOMS      : 398                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2963.86                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 107                     
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 31049                   
REMARK   3   NUMBER OF RESTRAINTS                     : 43650                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.017                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.032                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.112                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.105                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.031                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.050                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.122                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Z3N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032256.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LURE                               
REMARK 200  BEAMLINE                       : DW32                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 139636                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.2                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04000                            
REMARK 200   FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.25200                            
REMARK 200   FOR SHELL         : 4.050                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR, O                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ALDOSE REDUCTASE, LIDORESTAT, NADP+      
REMARK 280  , PEG 6000, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       33.67000            
REMARK 290   SMTRY3   2  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     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS 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    MET A   0   CG  -  SD  -  CE  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    ARG A   3   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A   3   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A   3   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A  40   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  63   CG  -  CD  -  NE  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    ARG A  63   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG A  63   CD  -  NE  -  CZ  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG A  63   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ASP A 149   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TYR A 198   CB  -  CG  -  CD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    CYS A 298   CA  -  CB  -  SG  ANGL. DEV. = -11.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLU A  60         0.12    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A  40        -12.78                                           
REMARK 500    ARG A  40         15.74                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2139        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH A2226        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH A2259        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A2271        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH A2273        DISTANCE =  8.57 ANGSTROMS                       
REMARK 525    HOH A2287        DISTANCE =  5.00 ANGSTROMS                       
REMARK 525    HOH A2315        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH A2342        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH A2369        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A2417        DISTANCE =  6.92 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDP A 318                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3NA A 320                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1US0   RELATED DB: PDB                                   
DBREF  1Z3N A    0   315  GB     178489   AAA51714         1    316             
SEQADV 1Z3N GLY A   -3  GB   178489              EXPRESSION TAG                 
SEQADV 1Z3N SER A   -2  GB   178489              EXPRESSION TAG                 
SEQADV 1Z3N HIS A   -1  GB   178489              EXPRESSION TAG                 
SEQRES   1 A  319  GLY SER HIS MET ALA SER ARG ILE LEU LEU ASN ASN GLY          
SEQRES   2 A  319  ALA LYS MET PRO ILE LEU GLY LEU GLY THR TRP LYS SER          
SEQRES   3 A  319  PRO PRO GLY GLN VAL THR GLU ALA VAL LYS VAL ALA ILE          
SEQRES   4 A  319  ASP VAL GLY TYR ARG HIS ILE ASP CYS ALA HIS VAL TYR          
SEQRES   5 A  319  GLN ASN GLU ASN GLU VAL GLY VAL ALA ILE GLN GLU LYS          
SEQRES   6 A  319  LEU ARG GLU GLN VAL VAL LYS ARG GLU GLU LEU PHE ILE          
SEQRES   7 A  319  VAL SER LYS LEU TRP CYS THR TYR HIS GLU LYS GLY LEU          
SEQRES   8 A  319  VAL LYS GLY ALA CYS GLN LYS THR LEU SER ASP LEU LYS          
SEQRES   9 A  319  LEU ASP TYR LEU ASP LEU TYR LEU ILE HIS TRP PRO THR          
SEQRES  10 A  319  GLY PHE LYS PRO GLY LYS GLU PHE PHE PRO LEU ASP GLU          
SEQRES  11 A  319  SER GLY ASN VAL VAL PRO SER ASP THR ASN ILE LEU ASP          
SEQRES  12 A  319  THR TRP ALA ALA MET GLU GLU LEU VAL ASP GLU GLY LEU          
SEQRES  13 A  319  VAL LYS ALA ILE GLY ILE SER ASN PHE ASN HIS LEU GLN          
SEQRES  14 A  319  VAL GLU MET ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS          
SEQRES  15 A  319  PRO ALA VAL ASN GLN ILE GLU CYS HIS PRO TYR LEU THR          
SEQRES  16 A  319  GLN GLU LYS LEU ILE GLN TYR CYS GLN SER LYS GLY ILE          
SEQRES  17 A  319  VAL VAL THR ALA TYR SER PRO LEU GLY SER PRO ASP ARG          
SEQRES  18 A  319  PRO TRP ALA LYS PRO GLU ASP PRO SER LEU LEU GLU ASP          
SEQRES  19 A  319  PRO ARG ILE LYS ALA ILE ALA ALA LYS HIS ASN LYS THR          
SEQRES  20 A  319  THR ALA GLN VAL LEU ILE ARG PHE PRO MET GLN ARG ASN          
SEQRES  21 A  319  LEU VAL VAL ILE PRO LYS SER VAL THR PRO GLU ARG ILE          
SEQRES  22 A  319  ALA GLU ASN PHE LYS VAL PHE ASP PHE GLU LEU SER SER          
SEQRES  23 A  319  GLN ASP MET THR THR LEU LEU SER TYR ASN ARG ASN TRP          
SEQRES  24 A  319  ARG VAL CYS ALA LEU LEU SER CYS THR SER HIS LYS ASP          
SEQRES  25 A  319  TYR PRO PHE HIS GLU GLU PHE                                  
HET    NDP  A 318      48                                                       
HET    3NA  A 320      26                                                       
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     3NA {3-[(4,5,7-TRIFLUORO-1,3-BENZOTHIAZOL-2-YL)METHYL]-1H-           
HETNAM   2 3NA  INDOL-1-YL}ACETIC ACID                                          
HETSYN     3NA 3-[(4,5,7-TRIFLUOROBENZOTHIAZOL-2-YL)METHYL]INDOLE-N-            
HETSYN   2 3NA  ACETIC ACID                                                     
FORMUL   2  NDP    C21 H30 N7 O17 P3                                            
FORMUL   3  3NA    C18 H11 F3 N2 O2 S                                           
FORMUL   4  HOH   *397(H2 O)                                                    
HELIX    1   1 PRO A   23  GLY A   38  1                                  16    
HELIX    2   2 ALA A   45  GLN A   49  5                                   5    
HELIX    3   3 ASN A   50  GLU A   64  1                                  15    
HELIX    4   4 LYS A   68  LEU A   72  5                                   5    
HELIX    5   5 TRP A   79  HIS A   83  5                                   5    
HELIX    6   6 GLU A   84  GLY A   86  5                                   3    
HELIX    7   7 LEU A   87  LYS A  100  1                                  14    
HELIX    8   8 ASN A  136  GLU A  150  1                                  15    
HELIX    9   9 ASN A  162  ASN A  171  1                                  10    
HELIX   10  10 GLN A  192  LYS A  202  1                                  11    
HELIX   11  11 SER A  226  GLU A  229  5                                   4    
HELIX   12  12 ASP A  230  ASN A  241  1                                  12    
HELIX   13  13 THR A  243  GLN A  254  1                                  12    
HELIX   14  14 THR A  265  LYS A  274  1                                  10    
HELIX   15  15 SER A  281  SER A  290  1                                  10    
HELIX   16  16 LEU A  300  THR A  304  5                                   5    
SHEET    1   A 2 ARG A   3  LEU A   5  0                                        
SHEET    2   A 2 LYS A  11  PRO A  13 -1  O  MET A  12   N  ILE A   4           
SHEET    1   B 8 GLY A  16  GLY A  18  0                                        
SHEET    2   B 8 HIS A  41  ASP A  43  1  O  ASP A  43   N  LEU A  17           
SHEET    3   B 8 PHE A  73  LEU A  78  1  O  VAL A  75   N  ILE A  42           
SHEET    4   B 8 LEU A 106  ILE A 109  1  O  LEU A 108   N  LEU A  78           
SHEET    5   B 8 ILE A 156  SER A 159  1  O  GLY A 157   N  ILE A 109           
SHEET    6   B 8 VAL A 181  GLU A 185  1  O  VAL A 181   N  ILE A 158           
SHEET    7   B 8 VAL A 205  TYR A 209  1  O  THR A 207   N  ILE A 184           
SHEET    8   B 8 VAL A 258  VAL A 259  1  O  VAL A 258   N  ALA A 208           
SITE     1 AC1 36 GLY A  18  THR A  19  TRP A  20  LYS A  21                    
SITE     2 AC1 36 ASP A  43  TYR A  48  HIS A 110  TRP A 111                    
SITE     3 AC1 36 SER A 159  ASN A 160  GLN A 183  TYR A 209                    
SITE     4 AC1 36 SER A 210  PRO A 211  LEU A 212  GLY A 213                    
SITE     5 AC1 36 SER A 214  PRO A 215  ASP A 216  ALA A 245                    
SITE     6 AC1 36 ILE A 260  PRO A 261  LYS A 262  SER A 263                    
SITE     7 AC1 36 VAL A 264  THR A 265  ARG A 268  GLU A 271                    
SITE     8 AC1 36 ASN A 272  3NA A 320  HOH A2085  HOH A2147                    
SITE     9 AC1 36 HOH A2149  HOH A2167  HOH A2168  HOH A2169                    
SITE     1 AC2 16 TRP A  20  TYR A  48  TRP A  79  CYS A  80                    
SITE     2 AC2 16 HIS A 110  TRP A 111  THR A 113  PHE A 115                    
SITE     3 AC2 16 PHE A 122  TRP A 219  CYS A 298  ALA A 299                    
SITE     4 AC2 16 LEU A 300  CYS A 303  TYR A 309  NDP A 318                    
CRYST1   50.140   67.340   47.880  90.00  92.50  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019944  0.000000  0.000871        0.00000                         
SCALE2      0.000000  0.014850  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020905        0.00000                         
ATOM      1  N  AMET A   0      18.400  13.971  41.030  0.80 49.24           N  
ANISOU    1  N  AMET A   0     4639   7240   6829   1284  -1886  -4011       N  
ATOM      2  CA AMET A   0      17.757  13.319  39.882  0.80 49.81           C  
ANISOU    2  CA AMET A   0     4305   9438   5182  -1375    543  -4032       C  
ATOM      3  C  AMET A   0      16.522  12.519  40.183  0.80 46.13           C  
ANISOU    3  C  AMET A   0     3646   8788   5092   -415    685  -3060       C  
ATOM      4  O  AMET A   0      16.373  11.494  40.815  0.80 42.33           O  
ANISOU    4  O  AMET A   0     3162   9556   3364   -425   -677  -2752       O  
ATOM      5  CB AMET A   0      18.765  12.408  39.180  0.80 45.55           C  
ANISOU    5  CB AMET A   0     3000   9417   4890  -1770     38  -3957       C  
ATOM      6  CG AMET A   0      18.342  11.278  38.321  0.80 44.52           C  
ANISOU    6  CG AMET A   0     2790   8475   5649  -2864   1866  -3726       C  
ATOM      7  SD AMET A   0      19.017  11.232  36.683  0.80 39.05           S  
ANISOU    7  SD AMET A   0     4866   5286   4684  -1325   1121  -2605       S  
ATOM      8  CE AMET A   0      20.293  12.369  36.440  0.80 36.52           C  
ANISOU    8  CE AMET A   0     2920   7652   3305  -1201    856  -2232       C  
ATOM      9  N   ALA A   1      15.459  13.033  39.615  1.00 43.46           N  
ANISOU    9  N   ALA A   1     4670   5838   6004  -1498   -724  -2937       N  
ATOM     10  CA  ALA A   1      14.138  12.406  39.571  1.00 35.34           C  
ANISOU   10  CA  ALA A   1     4204   4150   5072   -642   -518  -2348       C  
ATOM     11  C   ALA A   1      14.138  11.063  38.856  1.00 31.21           C  
ANISOU   11  C   ALA A   1     3454   4302   4104   -321   -386  -2269       C  
ATOM     12  O   ALA A   1      14.828  10.805  37.881  1.00 38.63           O  
ANISOU   12  O   ALA A   1     3970   5858   4852  -1395    465  -2867       O  
ATOM     13  CB  ALA A   1      13.156  13.371  38.906  1.00 39.20           C  
ANISOU   13  CB  ALA A   1     5313   4674   4906    450   -614  -2852       C  
ATOM     14  N   SER A   2      13.312  10.152  39.373  1.00 22.65           N  
ANISOU   14  N   SER A   2     3171   3180   2254    817  -1070  -1625       N  
ATOM     15  CA  SER A   2      13.300   8.812  38.848  1.00 21.27           C  
ANISOU   15  CA  SER A   2     3409   2994   1680   1241  -1075  -1157       C  
ATOM     16  C   SER A   2      12.394   8.613  37.628  1.00 13.13           C  
ANISOU   16  C   SER A   2     1955   1768   1265    463   -261   -613       C  
ATOM     17  O   SER A   2      12.455   7.527  37.058  1.00 12.39           O  
ANISOU   17  O   SER A   2     1904   1615   1189    374    -81   -396       O  
ATOM     18  CB  SER A   2      12.832   7.776  39.883  1.00 28.51           C  
ANISOU   18  CB  SER A   2     5513   3497   1824   1299  -1707   -270       C  
ATOM     19  OG  SER A   2      11.484   8.028  40.261  1.00 35.67           O  
ANISOU   19  OG  SER A   2     6879   4745   1929   1254    978     27       O  
ATOM     20  N  AARG A   3      11.548   9.566  37.283  0.60 12.85           N  
ANISOU   20  N  AARG A   3     2052   1582   1248    363   -144   -502       N  
ATOM     21  N  BARG A   3      11.647   9.639  37.274  0.40 14.30           N  
ANISOU   21  N  BARG A   3     2513   1589   1331    447   -348   -459       N  
ATOM     22  CA AARG A   3      10.612   9.478  36.151  0.60 11.29           C  
ANISOU   22  CA AARG A   3     1865   1224   1201    170   -115   -340       C  
ATOM     23  CA BARG A   3      10.837   9.516  36.058  0.40 12.65           C  
ANISOU   23  CA BARG A   3     1895   1615   1296     45   -161    -80       C  
ATOM     24  C  AARG A   3      10.718  10.744  35.280  0.60 11.99           C  
ANISOU   24  C  AARG A   3     2096   1137   1324    134     16   -389       C  
ATOM     25  C  BARG A   3      11.011  10.782  35.215  0.40 11.78           C  
ANISOU   25  C  BARG A   3     1801   1175   1500     -5   -344   -326       C  
ATOM     26  O  AARG A   3      10.873  11.830  35.852  0.60 16.54           O  
ANISOU   26  O  AARG A   3     3192   1258   1834   -135   -266   -548       O  
ATOM     27  O  BARG A   3      11.462  11.825  35.676  0.40 15.55           O  
ANISOU   27  O  BARG A   3     2694   1419   1793   -105   -292   -696       O  
ATOM     28  CB AARG A   3       9.164   9.288  36.617  0.60 14.28           C  
ANISOU   28  CB AARG A   3     1924   1748   1753    252     32    183       C  
ATOM     29  CB BARG A   3       9.371   9.279  36.394  0.40 12.60           C  
ANISOU   29  CB BARG A   3     2022   1379   1386    343    338   -359       C  
ATOM     30  CG AARG A   3       8.901   7.963  37.341  0.60 15.94           C  
ANISOU   30  CG AARG A   3     2231   1753   2072    308    476    230       C  
ATOM     31  CG BARG A   3       9.146   8.095  37.335  0.40 14.42           C  
ANISOU   31  CG BARG A   3     2216   1897   1367    250    453    -73       C  
ATOM     32  CD AARG A   3       7.419   7.577  37.442  0.60 20.90           C  
ANISOU   32  CD AARG A   3     2409   2089   3441    -82    645    155       C  
ATOM     33  CD BARG A   3       7.660   7.727  37.428  0.40 20.06           C  
ANISOU   33  CD BARG A   3     2223   2271   3128    319    872    389       C  
ATOM     34  NE AARG A   3       7.167   6.304  38.093  0.60 18.43           N  
ANISOU   34  NE AARG A   3     2307   2022   2672   -111    372    -25       N  
ATOM     35  NE BARG A   3       6.942   8.631  38.314  0.40 22.54           N  
ANISOU   35  NE BARG A   3     2671   2747   3147    967   1234    835       N  
ATOM     36  CZ AARG A   3       6.360   5.325  37.663  0.60 18.29           C  
ANISOU   36  CZ AARG A   3     3231   1783   1935      0    147   -214       C  
ATOM     37  CZ BARG A   3       5.645   8.651  38.574  0.40 28.40           C  
ANISOU   37  CZ BARG A   3     2895   3425   4471   1280   1845   1481       C  
ATOM     38  NH1AARG A   3       5.657   5.436  36.488  0.60 17.41           N  
ANISOU   38  NH1AARG A   3     1793   2852   1970    256    524    132       N  
ATOM     39  NH1BARG A   3       4.776   7.799  38.035  0.40 38.42           N  
ANISOU   39  NH1BARG A   3     2858   4822   6920   -243   2286   1681       N  
ATOM     40  NH2AARG A   3       6.291   4.216  38.455  0.60 15.60           N  
ANISOU   40  NH2AARG A   3     2334   1670   1925    -80    118   -308       N  
ATOM     41  NH2BARG A   3       5.213   9.568  39.423  0.40 35.65           N  
ANISOU   41  NH2BARG A   3     4798   4256   4490   2624   2833   1899       N  
ATOM     42  N   ILE A   4      10.585  10.611  33.979  1.00 11.68           N  
ANISOU   42  N   ILE A   4     1990   1125   1323     76   -167   -201       N  
ATOM     43  CA  ILE A   4      10.631  11.707  32.994  1.00 12.29           C  
ANISOU   43  CA  ILE A   4     1982   1101   1586     24    -49   -103       C  
ATOM     44  C   ILE A   4       9.212  11.874  32.405  1.00 11.71           C  
ANISOU   44  C   ILE A   4     2021    919   1509     64     29   -114       C  
ATOM     45  O   ILE A   4       8.501  10.917  32.130  1.00 13.15           O  
ANISOU   45  O   ILE A   4     2026    908   2062     49   -230    -20       O  
ATOM     46  CB  ILE A   4      11.685  11.426  31.901  1.00 13.30           C  
ANISOU   46  CB  ILE A   4     1998   1436   1618    -35     76    -83       C  
ATOM     47  CG1 ILE A   4      11.883  12.647  30.941  1.00 19.44           C  
ANISOU   47  CG1 ILE A   4     3121   1680   2584     79    814    463       C  
ATOM     48  CG2 ILE A   4      11.360  10.195  31.073  1.00 17.79           C  
ANISOU   48  CG2 ILE A   4     3030   1695   2036   -119    523   -495       C  
ATOM     49  CD1 ILE A   4      13.252  12.442  30.237  1.00 24.33           C  
ANISOU   49  CD1 ILE A   4     3409   3009   2828   -793   1259   -293       C  
ATOM     50  N   LEU A   5       8.793  13.130  32.222  1.00 13.22           N  
ANISOU   50  N   LEU A   5     2378    983   1661    197   -322   -220       N  
ATOM     51  CA  LEU A   5       7.460  13.434  31.707  1.00 13.42           C  
ANISOU   51  CA  LEU A   5     2453   1136   1512    379   -212   -287       C  
ATOM     52  C   LEU A   5       7.429  13.262  30.186  1.00 12.73           C  
ANISOU   52  C   LEU A   5     2219   1178   1442    291   -123    -24       C  
ATOM     53  O   LEU A   5       8.237  13.832  29.467  1.00 16.27           O  
ANISOU   53  O   LEU A   5     2830   1661   1690     -9     -6     51       O  
ATOM     54  CB  LEU A   5       7.149  14.889  32.067  1.00 16.35           C  
ANISOU   54  CB  LEU A   5     3185   1068   1960    639   -109   -178       C  
ATOM     55  CG  LEU A   5       5.767  15.384  31.769  1.00 21.95           C  
ANISOU   55  CG  LEU A   5     3476   1571   3293    922   -513   -616       C  
ATOM     56  CD1 LEU A   5       4.702  14.629  32.588  1.00 25.43           C  
ANISOU   56  CD1 LEU A   5     3144   2180   4340    740    141  -1066       C  
ATOM     57  CD2 LEU A   5       5.671  16.920  32.018  1.00 28.27           C  
ANISOU   57  CD2 LEU A   5     4652   1495   4592   1370   -998   -499       C  
ATOM     58  N   LEU A   6       6.434  12.500  29.712  1.00 13.06           N  
ANISOU   58  N   LEU A   6     2437   1077   1448    429   -328   -185       N  
ATOM     59  CA  LEU A   6       6.202  12.338  28.289  1.00 12.94           C  
ANISOU   59  CA  LEU A   6     2546   1135   1235    688   -186   -178       C  
ATOM     60  C   LEU A   6       5.159  13.363  27.811  1.00 14.23           C  
ANISOU   60  C   LEU A   6     2695   1243   1470    813   -248   -261       C  
ATOM     61  O   LEU A   6       4.472  14.002  28.585  1.00 14.75           O  
ANISOU   61  O   LEU A   6     2580   1377   1647    799   -161   -308       O  
ATOM     62  CB  LEU A   6       5.610  10.935  28.045  1.00 12.14           C  
ANISOU   62  CB  LEU A   6     2074   1196   1343    569   -269   -158       C  
ATOM     63  CG  LEU A   6       6.536   9.778  28.441  1.00 12.10           C  
ANISOU   63  CG  LEU A   6     1871   1048   1681    376     93     -4       C  
ATOM     64  CD1 LEU A   6       5.853   8.459  28.058  1.00 16.41           C  
ANISOU   64  CD1 LEU A   6     2288   1136   2810     44   -438     -3       C  
ATOM     65  CD2 LEU A   6       7.924   9.872  27.811  1.00 15.56           C  
ANISOU   65  CD2 LEU A   6     1896   1307   2711    382    320     81       C  
ATOM     66  N   ASN A   7       5.019  13.458  26.466  1.00 18.04           N  
ANISOU   66  N   ASN A   7     4043   1416   1398   1445   -334    -49       N  
ATOM     67  CA  ASN A   7       4.119  14.448  25.840  1.00 19.60           C  
ANISOU   67  CA  ASN A   7     4331   1632   1484   1520   -434   -267       C  
ATOM     68  C  AASN A   7       2.640  14.189  26.180  0.43 19.13           C  
ANISOU   68  C  AASN A   7     4165   1447   1656   1458   -805   -333       C  
ATOM     69  C  BASN A   7       2.656  14.038  25.870  0.57 21.24           C  
ANISOU   69  C  BASN A   7     4421   1676   1972   1225  -1391   -296       C  
ATOM     70  O  AASN A   7       1.782  15.052  26.018  0.43 21.51           O  
ANISOU   70  O  AASN A   7     4327   1900   1946   1711  -1091   -457       O  
ATOM     71  O  BASN A   7       1.875  14.794  25.294  0.57 23.67           O  
ANISOU   71  O  BASN A   7     4796   1818   2379   1494  -1500   -340       O  
ATOM     72  CB AASN A   7       4.201  14.363  24.322  0.43 18.22           C  
ANISOU   72  CB AASN A   7     4061   1322   1540    913   -905   -240       C  
ATOM     73  CB BASN A   7       4.795  14.885  24.511  0.57 21.01           C  
ANISOU   73  CB BASN A   7     5438   1178   1366   1556   -543   -203       C  
ATOM     74  CG AASN A   7       3.652  13.130  23.653  0.43 13.80           C  
ANISOU   74  CG AASN A   7     2442   1327   1474    858   -215   -132       C  
ATOM     75  CG BASN A   7       5.089  13.867  23.448  0.57 13.89           C  
ANISOU   75  CG BASN A   7     2618   1151   1509    749   -134    -74       C  
ATOM     76  OD1AASN A   7       2.829  12.322  24.110  0.43 22.37           O  
ANISOU   76  OD1AASN A   7     4039   2921   1540   -466    323   -360       O  
ATOM     77  OD1BASN A   7       5.758  14.026  22.424  0.57 19.88           O  
ANISOU   77  OD1BASN A   7     3722   1890   1939    303    529    143       O  
ATOM     78  ND2AASN A   7       4.125  12.980  22.420  0.43 13.39           N  
ANISOU   78  ND2AASN A   7     2245   1431   1410    597   -300   -128       N  
ATOM     79  ND2BASN A   7       4.472  12.732  23.692  0.57 13.00           N  
ANISOU   79  ND2BASN A   7     1957   1226   1757    775    -20    -85       N  
ATOM     80  N   ASN A   8       2.298  12.960  26.587  1.00 22.05           N  
ANISOU   80  N   ASN A   8     4193   1623   2562    737  -1854   -270       N  
ATOM     81  CA  ASN A   8       0.916  12.594  26.871  1.00 24.45           C  
ANISOU   81  CA  ASN A   8     3955   1742   3591    683  -2191   -277       C  
ATOM     82  C   ASN A   8       0.581  12.860  28.341  1.00 24.17           C  
ANISOU   82  C   ASN A   8     3018   2056   4109   1310  -1600   -637       C  
ATOM     83  O   ASN A   8      -0.536  12.516  28.820  1.00 29.14           O  
ANISOU   83  O   ASN A   8     2940   3011   5121   1153  -1519   -594       O  
ATOM     84  CB  ASN A   8       0.627  11.122  26.486  1.00 25.42           C  
ANISOU   84  CB  ASN A   8     4031   1765   3862    778  -2323   -401       C  
ATOM     85  CG  ASN A   8       1.275  10.150  27.500  1.00 18.43           C  
ANISOU   85  CG  ASN A   8     2641   1659   2700    550  -1109   -387       C  
ATOM     86  OD1 ASN A   8       2.252  10.525  28.155  1.00 18.07           O  
ANISOU   86  OD1 ASN A   8     2725   1633   2507    523  -1098   -402       O  
ATOM     87  ND2 ASN A   8       0.746   8.914  27.587  1.00 16.45           N  
ANISOU   87  ND2 ASN A   8     2131   1747   2373    536   -293   -698       N  
ATOM     88  N   GLY A   9       1.529  13.466  29.100  1.00 20.68           N  
ANISOU   88  N   GLY A   9     3298   1618   2942    949  -1141   -337       N  
ATOM     89  CA  GLY A   9       1.349  13.784  30.506  1.00 20.71           C  
ANISOU   89  CA  GLY A   9     2779   1948   3141    698   -233   -274       C  
ATOM     90  C   GLY A   9       1.673  12.615  31.447  1.00 18.46           C  
ANISOU   90  C   GLY A   9     2374   2077   2562    809   -170   -558       C  
ATOM     91  O   GLY A   9       1.585  12.836  32.663  1.00 22.80           O  
ANISOU   91  O   GLY A   9     3747   2277   2638    845    319   -648       O  
ATOM     92  N   ALA A  10       2.025  11.439  30.954  1.00 16.69           N  
ANISOU   92  N   ALA A  10     2412   1925   2006    688   -437   -377       N  
ATOM     93  CA  ALA A  10       2.444  10.321  31.803  1.00 15.14           C  
ANISOU   93  CA  ALA A  10     1887   1878   1987    352   -249   -381       C  
ATOM     94  C   ALA A  10       3.921  10.447  32.160  1.00 12.68           C  
ANISOU   94  C   ALA A  10     1710   1549   1561    438     79   -391       C  
ATOM     95  O   ALA A  10       4.717  11.061  31.450  1.00 16.47           O  
ANISOU   95  O   ALA A  10     2126   2211   1920     91    118    -69       O  
ATOM     96  CB  ALA A  10       2.183   9.000  31.057  1.00 18.21           C  
ANISOU   96  CB  ALA A  10     2508   1877   2535     39   -756   -365       C  
ATOM     97  N   LYS A  11       4.266   9.832  33.280  1.00 13.02           N  
ANISOU   97  N   LYS A  11     1706   1550   1690    335     -4   -260       N  
ATOM     98  CA  LYS A  11       5.634   9.800  33.748  1.00 13.01           C  
ANISOU   98  CA  LYS A  11     1647   1476   1821    373    -23   -428       C  
ATOM     99  C   LYS A  11       6.250   8.426  33.518  1.00 11.90           C  
ANISOU   99  C   LYS A  11     1762   1267   1493    256    242    -65       C  
ATOM    100  O   LYS A  11       5.702   7.402  33.905  1.00 17.44           O  
ANISOU  100  O   LYS A  11     2402   1388   2836    117   1111    -71       O  
ATOM    101  CB  LYS A  11       5.688  10.158  35.217  1.00 16.90           C  
ANISOU  101  CB  LYS A  11     1947   2314   2161    732   -280  -1071       C  
ATOM    102  CG  LYS A  11       5.214  11.612  35.443  1.00 25.79           C  
ANISOU  102  CG  LYS A  11     3832   2471   3496   1135   -973  -1774       C  
ATOM    103  CD  LYS A  11       5.843  12.200  36.691  0.50 27.50           C  
ANISOU  103  CD  LYS A  11     5821   2259   2369   1585  -1246  -1067       C  
ATOM    104  CE  LYS A  11       5.461  13.653  36.905  0.50 34.50           C  
ANISOU  104  CE  LYS A  11     7107   2369   3634   1724  -1792  -1773       C  
ATOM    105  NZ  LYS A  11       5.359  14.009  38.342  0.50 48.76           N  
ANISOU  105  NZ  LYS A  11    10435   4105   3988   3592   -476  -2118       N  
ATOM    106  N   MET A  12       7.402   8.377  32.879  1.00 10.29           N  
ANISOU  106  N   MET A  12     1479   1114   1318    274    -72   -140       N  
ATOM    107  CA  MET A  12       8.084   7.143  32.504  1.00  9.71           C  
ANISOU  107  CA  MET A  12     1638    901   1149    241   -177   -170       C  
ATOM    108  C   MET A  12       9.310   6.936  33.358  1.00  8.24           C  
ANISOU  108  C   MET A  12     1357    829    944     54     25   -153       C  
ATOM    109  O   MET A  12      10.179   7.822  33.435  1.00  9.87           O  
ANISOU  109  O   MET A  12     1551    927   1273    -51    -47    -91       O  
ATOM    110  CB  MET A  12       8.509   7.259  31.011  1.00 10.46           C  
ANISOU  110  CB  MET A  12     1703   1186   1085    251   -207   -145       C  
ATOM    111  CG  MET A  12       9.216   6.018  30.475  1.00 10.31           C  
ANISOU  111  CG  MET A  12     1602   1217   1097    202    -75   -145       C  
ATOM    112  SD  MET A  12       9.427   6.245  28.688  1.00 12.48           S  
ANISOU  112  SD  MET A  12     1967   1591   1185    361    -21   -115       S  
ATOM    113  CE  MET A  12      10.048   4.666  28.170  1.00 13.60           C  
ANISOU  113  CE  MET A  12     1734   1867   1564    456   -258   -573       C  
ATOM    114  N   PRO A  13       9.451   5.796  34.045  1.00  8.50           N  
ANISOU  114  N   PRO A  13     1333    864   1032     48     18   -166       N  
ATOM    115  CA  PRO A  13      10.674   5.538  34.845  1.00  8.49           C  
ANISOU  115  CA  PRO A  13     1317    998    910    121    -14   -109       C  
ATOM    116  C   PRO A  13      11.924   5.565  33.952  1.00  8.11           C  
ANISOU  116  C   PRO A  13     1311    851    922    183      4   -160       C  
ATOM    117  O   PRO A  13      11.956   4.927  32.889  1.00  9.11           O  
ANISOU  117  O   PRO A  13     1364   1107    990    -23     25   -278       O  
ATOM    118  CB  PRO A  13      10.417   4.175  35.486  1.00  9.46           C  
ANISOU  118  CB  PRO A  13     1414   1086   1095     49     54    -93       C  
ATOM    119  CG  PRO A  13       8.910   4.001  35.452  1.00 10.09           C  
ANISOU  119  CG  PRO A  13     1412   1284   1138    128     57     49       C  
ATOM    120  CD  PRO A  13       8.477   4.675  34.148  1.00  9.66           C  
ANISOU  120  CD  PRO A  13     1480   1020   1170   -105    -43     28       C  
ATOM    121  N   ILE A  14      12.964   6.239  34.427  1.00  8.23           N  
ANISOU  121  N   ILE A  14     1246    891    988     44    -15   -163       N  
ATOM    122  CA  ILE A  14      14.184   6.402  33.618  1.00  8.83           C  
ANISOU  122  CA  ILE A  14     1325    923   1107     95     83   -139       C  
ATOM    123  C   ILE A  14      15.039   5.164  33.574  1.00  8.19           C  
ANISOU  123  C   ILE A  14     1380    893    839    129     -3   -180       C  
ATOM    124  O   ILE A  14      15.905   5.078  32.707  1.00 10.42           O  
ANISOU  124  O   ILE A  14     1818   1204    937    270    358    -61       O  
ATOM    125  CB  ILE A  14      14.996   7.625  34.087  1.00 11.49           C  
ANISOU  125  CB  ILE A  14     1596    956   1813    -64     20   -331       C  
ATOM    126  CG1 ILE A  14      15.605   7.442  35.470  1.00 14.13           C  
ANISOU  126  CG1 ILE A  14     1985   1509   1873     25   -286   -563       C  
ATOM    127  CG2 ILE A  14      14.161   8.892  33.865  1.00 15.26           C  
ANISOU  127  CG2 ILE A  14     2207   1083   2507    132    -57   -294       C  
ATOM    128  CD1 ILE A  14      16.525   8.667  35.769  1.00 18.77           C  
ANISOU  128  CD1 ILE A  14     2058   1927   3146    -32   -480  -1156       C  
ATOM    129  N   LEU A  15      14.828   4.195  34.474  1.00  8.00           N  
ANISOU  129  N   LEU A  15     1235    828    977     25     64   -167       N  
ATOM    130  CA  LEU A  15      15.536   2.914  34.424  1.00  8.25           C  
ANISOU  130  CA  LEU A  15     1338    827    970     68    -70   -151       C  
ATOM    131  C   LEU A  15      14.487   1.815  34.205  1.00  8.13           C  
ANISOU  131  C   LEU A  15     1297    804    987     -3    279   -109       C  
ATOM    132  O   LEU A  15      13.454   1.768  34.867  1.00 12.81           O  
ANISOU  132  O   LEU A  15     1949   1274   1645   -376    821   -448       O  
ATOM    133  CB  LEU A  15      16.255   2.671  35.748  1.00 12.14           C  
ANISOU  133  CB  LEU A  15     1764   1698   1151    463   -351   -248       C  
ATOM    134  CG ALEU A  15      17.131   1.450  35.845  0.84 13.71           C  
ANISOU  134  CG ALEU A  15     1932   2132   1145    755     24     83       C  
ATOM    135  CG BLEU A  15      17.632   2.055  35.894  0.16 13.58           C  
ANISOU  135  CG BLEU A  15     1687   1635   1836    294   -520    -27       C  
ATOM    136  CD1ALEU A  15      18.165   1.313  34.723  0.84 14.04           C  
ANISOU  136  CD1ALEU A  15     1574   2055   1706    447    183    -30       C  
ATOM    137  CD1BLEU A  15      17.649   0.558  35.595  0.16 16.55           C  
ANISOU  137  CD1BLEU A  15     2389   1963   1935    793     47   -862       C  
ATOM    138  CD2ALEU A  15      17.854   1.544  37.157  0.84 21.86           C  
ANISOU  138  CD2ALEU A  15     2617   4292   1395   1376   -487    382       C  
ATOM    139  CD2BLEU A  15      18.645   2.762  34.997  0.16 19.23           C  
ANISOU  139  CD2BLEU A  15     1790   3401   2114   -389   -211   -288       C  
ATOM    140  N   GLY A  16      14.741   0.960  33.216  1.00  7.94           N  
ANISOU  140  N   GLY A  16     1365    762    891     22    102   -108       N  
ATOM    141  CA  GLY A  16      13.881  -0.204  33.011  1.00  7.83           C  
ANISOU  141  CA  GLY A  16     1092    682   1201     41    119    -52       C  
ATOM    142  C   GLY A  16      14.704  -1.455  32.782  1.00  7.20           C  
ANISOU  142  C   GLY A  16     1194    808    734     26     75    -48       C  
ATOM    143  O   GLY A  16      15.938  -1.394  32.632  1.00  9.72           O  
ANISOU  143  O   GLY A  16     1211    888   1592     46    294     19       O  
ATOM    144  N   LEU A  17      14.005  -2.596  32.771  1.00  7.04           N  
ANISOU  144  N   LEU A  17     1211    711    753     43     41    -98       N  
ATOM    145  CA  LEU A  17      14.642  -3.900  32.547  1.00  6.83           C  
ANISOU  145  CA  LEU A  17     1248    725    623     24     56    -46       C  
ATOM    146  C   LEU A  17      14.394  -4.323  31.096  1.00  6.43           C  
ANISOU  146  C   LEU A  17     1098    629    718      8     -6    -53       C  
ATOM    147  O   LEU A  17      13.257  -4.460  30.661  1.00  8.01           O  
ANISOU  147  O   LEU A  17     1002   1150    892      9    -45   -102       O  
ATOM    148  CB  LEU A  17      13.998  -4.954  33.481  1.00  8.25           C  
ANISOU  148  CB  LEU A  17     1490    896    750     44    128     23       C  
ATOM    149  CG  LEU A  17      14.608  -6.366  33.356  1.00  9.02           C  
ANISOU  149  CG  LEU A  17     1703    825    899     52    127    108       C  
ATOM    150  CD1 LEU A  17      16.030  -6.399  33.852  1.00 12.85           C  
ANISOU  150  CD1 LEU A  17     1796   1278   1808    270   -179    245       C  
ATOM    151  CD2 LEU A  17      13.684  -7.367  34.059  1.00 12.14           C  
ANISOU  151  CD2 LEU A  17     2363   1026   1224   -163    395    163       C  
ATOM    152  N   GLY A  18      15.498  -4.608  30.374  1.00  6.39           N  
ANISOU  152  N   GLY A  18     1058    738    632     12     76    -51       N  
ATOM    153  CA  GLY A  18      15.387  -5.202  29.043  1.00  7.05           C  
ANISOU  153  CA  GLY A  18     1344    668    668    -84    141    -79       C  
ATOM    154  C   GLY A  18      15.157  -6.700  29.087  1.00  6.38           C  
ANISOU  154  C   GLY A  18     1037    761    626      6     56     20       C  
ATOM    155  O   GLY A  18      15.570  -7.389  30.044  1.00  7.94           O  
ANISOU  155  O   GLY A  18     1440    776    800     36    -83     -1       O  
ATOM    156  N   THR A  19      14.536  -7.230  28.031  1.00  6.68           N  
ANISOU  156  N   THR A  19     1162    666    709    -46    -35    -74       N  
ATOM    157  CA  THR A  19      14.172  -8.660  27.959  1.00  6.87           C  
ANISOU  157  CA  THR A  19     1114    695    802    -65     97    -42       C  
ATOM    158  C   THR A  19      14.584  -9.354  26.655  1.00  6.97           C  
ANISOU  158  C   THR A  19     1153    722    774    -53     31    -59       C  
ATOM    159  O   THR A  19      14.261 -10.530  26.472  1.00  8.34           O  
ANISOU  159  O   THR A  19     1435    726   1010   -111    202   -117       O  
ATOM    160  CB  THR A  19      12.668  -8.867  28.230  1.00  7.44           C  
ANISOU  160  CB  THR A  19     1189    821    815    -13     56      5       C  
ATOM    161  OG1 THR A  19      11.898  -8.246  27.206  1.00  7.74           O  
ANISOU  161  OG1 THR A  19     1149    823    968      6    -86   -114       O  
ATOM    162  CG2 THR A  19      12.240  -8.344  29.610  1.00  8.78           C  
ANISOU  162  CG2 THR A  19     1348   1149    841    -51    210    -36       C  
ATOM    163  N   TRP A  20      15.292  -8.665  25.753  1.00  6.68           N  
ANISOU  163  N   TRP A  20     1055    701    781     23     84    -70       N  
ATOM    164  CA  TRP A  20      15.774  -9.375  24.547  1.00  7.08           C  
ANISOU  164  CA  TRP A  20     1224    759    707     93     46    -26       C  
ATOM    165  C   TRP A  20      16.842 -10.393  24.956  1.00  7.05           C  
ANISOU  165  C   TRP A  20     1143    758    779     52    -13    -77       C  
ATOM    166  O   TRP A  20      17.810 -10.014  25.657  1.00  8.15           O  
ANISOU  166  O   TRP A  20     1254    884    961     95      1   -130       O  
ATOM    167  CB  TRP A  20      16.334  -8.347  23.542  1.00  7.83           C  
ANISOU  167  CB  TRP A  20     1425    759    793     29    109    -28       C  
ATOM    168  CG  TRP A  20      16.922  -8.974  22.302  1.00  7.61           C  
ANISOU  168  CG  TRP A  20     1348    791    751     89     55     39       C  
ATOM    169  CD1 TRP A  20      16.464 -10.072  21.611  1.00  8.14           C  
ANISOU  169  CD1 TRP A  20     1401    962    731    101     17   -133       C  
ATOM    170  CD2 TRP A  20      18.104  -8.512  21.618  1.00  8.49           C  
ANISOU  170  CD2 TRP A  20     1478    959    788     -7     93    -12       C  
ATOM    171  NE1 TRP A  20      17.314 -10.332  20.543  1.00  9.17           N  
ANISOU  171  NE1 TRP A  20     1582   1010    891     15    105   -166       N  
ATOM    172  CE2 TRP A  20      18.326  -9.379  20.528  1.00  8.90           C  
ANISOU  172  CE2 TRP A  20     1416   1034    931    113    155   -179       C  
ATOM    173  CE3 TRP A  20      18.991  -7.443  21.828  1.00  8.96           C  
ANISOU  173  CE3 TRP A  20     1363   1008   1034     25     45     -7       C  
ATOM    174  CZ2 TRP A  20      19.412  -9.216  19.656  1.00 10.32           C  
ANISOU  174  CZ2 TRP A  20     1502   1394   1025    106    177    -88       C  
ATOM    175  CZ3 TRP A  20      20.053  -7.281  20.980  1.00 10.86           C  
ANISOU  175  CZ3 TRP A  20     1615   1339   1173   -154    275      0       C  
ATOM    176  CH2 TRP A  20      20.245  -8.170  19.894  1.00 11.26           C  
ANISOU  176  CH2 TRP A  20     1678   1517   1082     16    251     -6       C  
ATOM    177  N   LYS A  21      16.679 -11.630  24.511  1.00  7.90           N  
ANISOU  177  N   LYS A  21     1329    718    956     51    137    -29       N  
ATOM    178  CA  LYS A  21      17.619 -12.768  24.746  1.00  8.57           C  
ANISOU  178  CA  LYS A  21     1420    731   1105     89    196     28       C  
ATOM    179  C   LYS A  21      17.408 -13.349  26.129  1.00  9.15           C  
ANISOU  179  C   LYS A  21     1602    813   1060    235    174     81       C  
ATOM    180  O   LYS A  21      18.101 -14.314  26.470  1.00 14.58           O  
ANISOU  180  O   LYS A  21     2238   1689   1613    871    587    629       O  
ATOM    181  CB  LYS A  21      19.100 -12.423  24.557  1.00  9.39           C  
ANISOU  181  CB  LYS A  21     1452    976   1138    215    177     81       C  
ATOM    182  CG  LYS A  21      19.408 -11.719  23.235  1.00  9.80           C  
ANISOU  182  CG  LYS A  21     1436   1271   1015     25    184     15       C  
ATOM    183  CD  LYS A  21      20.832 -11.150  23.184  1.00 11.48           C  
ANISOU  183  CD  LYS A  21     1594   1546   1221   -206     85    -62       C  
ATOM    184  CE  LYS A  21      21.001  -9.660  23.571  1.00 11.94           C  
ANISOU  184  CE  LYS A  21     1781   1276   1481    -75    142    226       C  
ATOM    185  NZ  LYS A  21      20.549  -9.389  24.994  1.00 10.09           N  
ANISOU  185  NZ  LYS A  21     1518    908   1408    119    -77     87       N  
ATOM    186  N   SER A  22      16.481 -12.878  26.947  1.00  8.75           N  
ANISOU  186  N   SER A  22     1455    821   1047    -19    196     12       N  
ATOM    187  CA  SER A  22      16.219 -13.490  28.237  1.00  9.14           C  
ANISOU  187  CA  SER A  22     1717    788    968     26    213     65       C  
ATOM    188  C   SER A  22      15.426 -14.774  28.013  1.00 10.24           C  
ANISOU  188  C   SER A  22     1950    885   1057    -88    292     68       C  
ATOM    189  O   SER A  22      14.303 -14.743  27.439  1.00 11.80           O  
ANISOU  189  O   SER A  22     2161    994   1330   -338     26     20       O  
ATOM    190  CB  SER A  22      15.369 -12.526  29.094  1.00  9.27           C  
ANISOU  190  CB  SER A  22     1673    890    961    -68    162    -50       C  
ATOM    191  OG  SER A  22      16.176 -11.369  29.292  1.00 10.39           O  
ANISOU  191  OG  SER A  22     1732   1003   1211   -216    182   -108       O  
ATOM    192  N   PRO A  23      15.999 -15.943  28.365  1.00 11.92           N  
ANISOU  192  N   PRO A  23     2225    845   1458    -23    446    101       N  
ATOM    193  CA  PRO A  23      15.335 -17.186  27.992  1.00 14.38           C  
ANISOU  193  CA  PRO A  23     2820    827   1816   -158    956   -164       C  
ATOM    194  C   PRO A  23      14.004 -17.313  28.708  1.00 11.71           C  
ANISOU  194  C   PRO A  23     2530    759   1159   -168    471   -223       C  
ATOM    195  O   PRO A  23      13.805 -16.871  29.813  1.00 11.55           O  
ANISOU  195  O   PRO A  23     2358    883   1148   -101    405   -177       O  
ATOM    196  CB  PRO A  23      16.335 -18.247  28.518  1.00 18.99           C  
ANISOU  196  CB  PRO A  23     3001    805   3408    343   1686    261       C  
ATOM    197  CG  PRO A  23      17.670 -17.577  28.590  1.00 18.07           C  
ANISOU  197  CG  PRO A  23     3080   1297   2488    435    513   -135       C  
ATOM    198  CD  PRO A  23      17.309 -16.167  28.991  1.00 14.72           C  
ANISOU  198  CD  PRO A  23     2308   1168   2117    477    394    436       C  
ATOM    199  N   PRO A  24      13.050 -17.977  28.081  1.00 13.52           N  
ANISOU  199  N   PRO A  24     2837   1150   1150   -315    383   -295       N  
ATOM    200  CA  PRO A  24      11.712 -18.106  28.635  1.00 14.32           C  
ANISOU  200  CA  PRO A  24     2683   1285   1472   -502    169   -256       C  
ATOM    201  C   PRO A  24      11.758 -18.781  29.998  1.00 13.62           C  
ANISOU  201  C   PRO A  24     2488   1134   1554   -316    425    -79       C  
ATOM    202  O   PRO A  24      10.916 -18.429  30.858  1.00 16.07           O  
ANISOU  202  O   PRO A  24     2375   1967   1762     41    393    -55       O  
ATOM    203  CB  PRO A  24      10.955 -18.930  27.602  1.00 19.20           C  
ANISOU  203  CB  PRO A  24     2881   2479   1935   -352   -109   -899       C  
ATOM    204  CG APRO A  24      12.058 -19.542  26.755  0.43 15.59           C  
ANISOU  204  CG APRO A  24     3030   1516   1377   -294   -116   -360       C  
ATOM    205  CG BPRO A  24      11.705 -18.625  26.330  0.57 19.93           C  
ANISOU  205  CG BPRO A  24     4001   2114   1460   -280   -287   -466       C  
ATOM    206  CD  PRO A  24      13.166 -18.535  26.686  1.00 18.30           C  
ANISOU  206  CD  PRO A  24     3731   1948   1274   -883    451   -652       C  
ATOM    207  N   GLY A  25      12.671 -19.718  30.234  1.00 14.07           N  
ANISOU  207  N   GLY A  25     2743    879   1725   -269    581    -75       N  
ATOM    208  CA  GLY A  25      12.751 -20.399  31.534  1.00 15.94           C  
ANISOU  208  CA  GLY A  25     3157    971   1929   -224    365     63       C  
ATOM    209  C  AGLY A  25      13.367 -19.564  32.632  0.75 14.26           C  
ANISOU  209  C  AGLY A  25     3124    866   1428    230    780    -33       C  
ATOM    210  C  BGLY A  25      13.619 -19.676  32.537  0.25 14.56           C  
ANISOU  210  C  BGLY A  25     2664    956   1913    213    307    112       C  
ATOM    211  O  AGLY A  25      13.259 -20.040  33.768  0.75 18.42           O  
ANISOU  211  O  AGLY A  25     4087   1284   1628    274    817    373       O  
ATOM    212  O  BGLY A  25      13.939 -20.221  33.595  0.25 21.43           O  
ANISOU  212  O  BGLY A  25     3059   1834   3251   -148   -946   1032       O  
ATOM    213  N  AGLN A  26      13.949 -18.421  32.353  0.52 12.19           N  
ANISOU  213  N  AGLN A  26     2351    913   1368    172     64    181       N  
ATOM    214  N  BGLN A  26      14.014 -18.446  32.258  0.48 11.83           N  
ANISOU  214  N  BGLN A  26     1849    900   1747    227    481   -165       N  
ATOM    215  CA AGLN A  26      14.645 -17.551  33.300  0.52 12.47           C  
ANISOU  215  CA AGLN A  26     2239   1274   1225    484     44    -66       C  
ATOM    216  CA BGLN A  26      14.664 -17.588  33.263  0.48 12.53           C  
ANISOU  216  CA BGLN A  26     2231   1110   1422    435    128    -41       C  
ATOM    217  C  AGLN A  26      14.058 -16.142  33.400  0.52 11.77           C  
ANISOU  217  C  AGLN A  26     2155   1287   1031    430     68   -173       C  
ATOM    218  C  BGLN A  26      13.935 -16.259  33.446  0.48 10.87           C  
ANISOU  218  C  BGLN A  26     1975   1125   1032    303    129   -149       C  
ATOM    219  O  AGLN A  26      14.396 -15.407  34.351  0.52 10.91           O  
ANISOU  219  O  AGLN A  26     1559   1371   1215    168     62   -160       O  
ATOM    220  O  BGLN A  26      13.995 -15.652  34.537  0.48 10.86           O  
ANISOU  220  O  BGLN A  26     1975   1232    919    139    239    -35       O  
ATOM    221  CB AGLN A  26      16.122 -17.362  32.876  0.52 15.31           C  
ANISOU  221  CB AGLN A  26     2064   1212   2542    421    -59     24       C  
ATOM    222  CB BGLN A  26      16.142 -17.365  32.857  0.48 15.59           C  
ANISOU  222  CB BGLN A  26     2049   1338   2536    275     58   -911       C  
ATOM    223  CG AGLN A  26      16.966 -18.636  32.908  0.52 20.43           C  
ANISOU  223  CG AGLN A  26     2157   1659   3945    726   -259   -276       C  
ATOM    224  CG BGLN A  26      17.009 -18.610  33.009  0.48 19.96           C  
ANISOU  224  CG BGLN A  26     2362   1723   3500    668    448   -851       C  
ATOM    225  CD AGLN A  26      18.330 -18.416  32.265  0.52 22.98           C  
ANISOU  225  CD AGLN A  26     2113   1633   4987    462    -75   -619       C  
ATOM    226  CD BGLN A  26      18.394 -18.619  32.402  0.48 25.20           C  
ANISOU  226  CD BGLN A  26     2144   2436   4994    728    521    247       C  
ATOM    227  OE1AGLN A  26      18.919 -17.347  32.401  0.52 37.81           O  
ANISOU  227  OE1AGLN A  26     2873   2881   8612   -721    514  -2272       O  
ATOM    228  OE1BGLN A  26      18.863 -17.721  31.694  0.48 25.55           O  
ANISOU  228  OE1BGLN A  26     3500   2620   3589   -664    570   -883       O  
ATOM    229  NE2AGLN A  26      18.859 -19.427  31.561  0.52 25.64           N  
ANISOU  229  NE2AGLN A  26     3053   1924   4766    899    479   -341       N  
ATOM    230  NE2BGLN A  26      19.122 -19.717  32.689  0.48 33.79           N  
ANISOU  230  NE2BGLN A  26     2334   2274   8229   1025     -4   -599       N  
ATOM    231  N   VAL A  27      13.228 -15.753  32.436  1.00 10.60           N  
ANISOU  231  N   VAL A  27     2077    955    998    300    108   -129       N  
ATOM    232  CA  VAL A  27      12.763 -14.355  32.443  1.00  9.68           C  
ANISOU  232  CA  VAL A  27     1819    942    916    120    141   -135       C  
ATOM    233  C   VAL A  27      11.674 -14.134  33.493  1.00  8.68           C  
ANISOU  233  C   VAL A  27     1583    856    859     35      0   -155       C  
ATOM    234  O   VAL A  27      11.555 -13.015  33.991  1.00  9.54           O  
ANISOU  234  O   VAL A  27     1851    899    875    -32    192   -169       O  
ATOM    235  CB  VAL A  27      12.339 -13.914  31.045  1.00  9.38           C  
ANISOU  235  CB  VAL A  27     1677    952    934    -48     92   -167       C  
ATOM    236  CG1 VAL A  27      10.979 -14.507  30.614  1.00 11.61           C  
ANISOU  236  CG1 VAL A  27     1901   1355   1156   -221   -118    -92       C  
ATOM    237  CG2 VAL A  27      12.309 -12.368  30.960  1.00 10.78           C  
ANISOU  237  CG2 VAL A  27     1906    936   1254    123    221    -22       C  
ATOM    238  N   THR A  28      10.880 -15.146  33.831  1.00  9.34           N  
ANISOU  238  N   THR A  28     1775    921    851      9     49    -48       N  
ATOM    239  CA  THR A  28       9.854 -14.925  34.862  1.00  9.37           C  
ANISOU  239  CA  THR A  28     1790    859    910    -44    106   -101       C  
ATOM    240  C   THR A  28      10.519 -14.564  36.184  1.00  8.91           C  
ANISOU  240  C   THR A  28     1680    812    896      6     66    -90       C  
ATOM    241  O   THR A  28      10.131 -13.597  36.844  1.00  9.72           O  
ANISOU  241  O   THR A  28     1701   1059    932     49     64   -146       O  
ATOM    242  CB  THR A  28       8.926 -16.167  35.009  1.00 10.78           C  
ANISOU  242  CB  THR A  28     2172   1001    923   -301      5    -41       C  
ATOM    243  OG1 THR A  28       8.281 -16.396  33.712  1.00 11.86           O  
ANISOU  243  OG1 THR A  28     2253   1092   1161   -343   -223     20       O  
ATOM    244  CG2 THR A  28       7.860 -15.987  36.058  1.00 12.90           C  
ANISOU  244  CG2 THR A  28     2148   1468   1287   -422    197     51       C  
ATOM    245  N   GLU A  29      11.506 -15.353  36.609  1.00  9.79           N  
ANISOU  245  N   GLU A  29     1679   1101    939     55     27    -35       N  
ATOM    246  CA  GLU A  29      12.217 -15.009  37.830  1.00 10.63           C  
ANISOU  246  CA  GLU A  29     1776   1240   1021    166   -136    -58       C  
ATOM    247  C   GLU A  29      12.923 -13.671  37.734  1.00  9.97           C  
ANISOU  247  C   GLU A  29     1786   1179    822    127    -83    -18       C  
ATOM    248  O   GLU A  29      12.955 -12.908  38.709  1.00 11.19           O  
ANISOU  248  O   GLU A  29     1951   1367    932    156     29   -256       O  
ATOM    249  CB  GLU A  29      13.181 -16.155  38.186  1.00 14.39           C  
ANISOU  249  CB  GLU A  29     2472   1304   1690    427   -557     58       C  
ATOM    250  CG AGLU A  29      12.476 -17.339  38.811  0.33 16.17           C  
ANISOU  250  CG AGLU A  29     3140   1415   1588    406   -306    202       C  
ATOM    251  CG BGLU A  29      13.918 -15.922  39.502  0.33 19.01           C  
ANISOU  251  CG BGLU A  29     2725   2780   1718    739   -745    206       C  
ATOM    252  CG CGLU A  29      14.070 -15.781  39.372  0.33 15.98           C  
ANISOU  252  CG CGLU A  29     2322   2077   1671    639   -610    105       C  
ATOM    253  CD AGLU A  29      11.146 -17.094  39.467  0.33 23.36           C  
ANISOU  253  CD AGLU A  29     3116   3122   2636    354    136    731       C  
ATOM    254  CD BGLU A  29      13.156 -15.729  40.781  0.33 22.55           C  
ANISOU  254  CD BGLU A  29     3053   3675   1841    691   -561   -264       C  
ATOM    255  CD CGLU A  29      15.266 -16.676  39.573  0.33 18.22           C  
ANISOU  255  CD CGLU A  29     3383   1727   1813   1156  -1007    127       C  
ATOM    256  OE1AGLU A  29      10.169 -16.581  38.883  0.33 42.05           O  
ANISOU  256  OE1AGLU A  29     4347   8863   2768   3322    -29     89       O  
ATOM    257  OE1BGLU A  29      11.952 -16.068  40.940  0.33 19.08           O  
ANISOU  257  OE1BGLU A  29     3742   2040   1466   -149   -299    504       O  
ATOM    258  OE1CGLU A  29      15.467 -17.710  38.903  0.33 34.50           O  
ANISOU  258  OE1CGLU A  29     7428   2198   3484   2864  -2784   -690       O  
ATOM    259  OE2AGLU A  29      10.961 -17.451  40.654  0.33 34.74           O  
ANISOU  259  OE2AGLU A  29     5382   4942   2877   2615   1479   1153       O  
ATOM    260  OE2BGLU A  29      13.777 -15.196  41.755  0.33 28.15           O  
ANISOU  260  OE2BGLU A  29     3205   4694   2799    149    -48  -1556       O  
ATOM    261  OE2CGLU A  29      16.063 -16.292  40.486  0.33 16.35           O  
ANISOU  261  OE2CGLU A  29     1817   2328   2068    273   -411    506       O  
ATOM    262  N   ALA A  30      13.527 -13.348  36.579  1.00  9.71           N  
ANISOU  262  N   ALA A  30     1547   1203    941    162     31   -208       N  
ATOM    263  CA  ALA A  30      14.234 -12.080  36.441  1.00  9.63           C  
ANISOU  263  CA  ALA A  30     1426   1191   1041      1     87   -332       C  
ATOM    264  C   ALA A  30      13.276 -10.901  36.679  1.00  8.90           C  
ANISOU  264  C   ALA A  30     1417   1174    792     12     79   -219       C  
ATOM    265  O   ALA A  30      13.640  -9.938  37.382  1.00  9.84           O  
ANISOU  265  O   ALA A  30     1530   1246    962    -49     34   -378       O  
ATOM    266  CB  ALA A  30      14.880 -11.988  35.067  1.00 11.06           C  
ANISOU  266  CB  ALA A  30     1476   1511   1217    -53    305   -361       C  
ATOM    267  N   VAL A  31      12.088 -10.946  36.076  1.00  8.26           N  
ANISOU  267  N   VAL A  31     1323    958    859    -43     82   -148       N  
ATOM    268  CA  VAL A  31      11.130  -9.847  36.230  1.00  8.05           C  
ANISOU  268  CA  VAL A  31     1349    968    740    -89    100   -157       C  
ATOM    269  C   VAL A  31      10.611  -9.797  37.671  1.00  8.19           C  
ANISOU  269  C   VAL A  31     1417    915    781    -29     99   -118       C  
ATOM    270  O   VAL A  31      10.428  -8.695  38.212  1.00  9.14           O  
ANISOU  270  O   VAL A  31     1623    971    880     22    109   -188       O  
ATOM    271  CB  VAL A  31      10.019  -9.981  35.202  1.00  8.65           C  
ANISOU  271  CB  VAL A  31     1425    999    862    -76     50   -107       C  
ATOM    272  CG1 VAL A  31       8.914  -8.963  35.450  1.00 10.45           C  
ANISOU  272  CG1 VAL A  31     1513   1197   1261     79    -97   -169       C  
ATOM    273  CG2 VAL A  31      10.587  -9.802  33.762  0.95 10.23           C  
ANISOU  273  CG2 VAL A  31     1791   1323    774    -49     16     74       C  
ATOM    274  N   LYS A  32      10.346 -10.963  38.301  1.00  8.57           N  
ANISOU  274  N   LYS A  32     1521    966    768   -101    183    -72       N  
ATOM    275  CA  LYS A  32       9.885 -10.928  39.712  1.00  9.03           C  
ANISOU  275  CA  LYS A  32     1575   1089    766   -164    122    -21       C  
ATOM    276  C   LYS A  32      10.939 -10.286  40.607  1.00  8.67           C  
ANISOU  276  C   LYS A  32     1586    974    736    -78    203    -24       C  
ATOM    277  O   LYS A  32      10.609  -9.446  41.453  1.00  9.88           O  
ANISOU  277  O   LYS A  32     1818   1094    843    -81    243   -178       O  
ATOM    278  CB  LYS A  32       9.646 -12.380  40.155  1.00  9.95           C  
ANISOU  278  CB  LYS A  32     1767   1149    864   -300    115     38       C  
ATOM    279  CG  LYS A  32       8.349 -12.963  39.584  1.00 11.45           C  
ANISOU  279  CG  LYS A  32     1788   1443   1118   -354    239   -203       C  
ATOM    280  CD  LYS A  32       8.198 -14.469  39.941  1.00 19.82           C  
ANISOU  280  CD  LYS A  32     3167   2064   2300  -1469    137    387       C  
ATOM    281  CE  LYS A  32       8.061 -14.836  41.346  1.00 27.34           C  
ANISOU  281  CE  LYS A  32     4951   2806   2633  -1647  -1143   1164       C  
ATOM    282  NZ  LYS A  32       7.764 -16.341  41.198  1.00 26.77           N  
ANISOU  282  NZ  LYS A  32     4161   2220   3792   -603   -119   1663       N  
ATOM    283  N   VAL A  33      12.214 -10.684  40.462  1.00  9.11           N  
ANISOU  283  N   VAL A  33     1539   1014    908    -40      6     -1       N  
ATOM    284  CA  VAL A  33      13.284 -10.067  41.286  1.00  9.31           C  
ANISOU  284  CA  VAL A  33     1654   1045    839     19    -77   -146       C  
ATOM    285  C   VAL A  33      13.393  -8.577  40.987  1.00  8.47           C  
ANISOU  285  C   VAL A  33     1453   1052    714    -27     88   -136       C  
ATOM    286  O   VAL A  33      13.528  -7.754  41.908  1.00  9.53           O  
ANISOU  286  O   VAL A  33     1743   1090    787    -56     52   -161       O  
ATOM    287  CB  VAL A  33      14.618 -10.811  41.057  1.00 11.19           C  
ANISOU  287  CB  VAL A  33     1777   1216   1258    264   -261   -164       C  
ATOM    288  CG1 VAL A  33      15.826 -10.003  41.617  1.00 14.16           C  
ANISOU  288  CG1 VAL A  33     1736   1789   1854    107   -337   -298       C  
ATOM    289  CG2 VAL A  33      14.501 -12.226  41.633  1.00 13.70           C  
ANISOU  289  CG2 VAL A  33     2264   1356   1588    326   -262    -16       C  
ATOM    290  N   ALA A  34      13.334  -8.189  39.715  1.00  8.68           N  
ANISOU  290  N   ALA A  34     1548    971    780    -36     86   -115       N  
ATOM    291  CA  ALA A  34      13.439  -6.770  39.351  1.00  8.63           C  
ANISOU  291  CA  ALA A  34     1561    978    741      3    166   -139       C  
ATOM    292  C   ALA A  34      12.351  -5.964  40.041  1.00  7.69           C  
ANISOU  292  C   ALA A  34     1363    965    595   -128     83    -28       C  
ATOM    293  O   ALA A  34      12.602  -4.907  40.615  1.00  8.76           O  
ANISOU  293  O   ALA A  34     1649    909    771   -128    173   -129       O  
ATOM    294  CB  ALA A  34      13.330  -6.633  37.823  1.00  9.63           C  
ANISOU  294  CB  ALA A  34     1708   1219    730    -46    199    -99       C  
ATOM    295  N   ILE A  35      11.089  -6.448  39.992  1.00  8.31           N  
ANISOU  295  N   ILE A  35     1428    977    752    -20    147    -65       N  
ATOM    296  CA  ILE A  35      10.004  -5.702  40.665  1.00  8.54           C  
ANISOU  296  CA  ILE A  35     1395   1004    845    -14    177   -175       C  
ATOM    297  C   ILE A  35      10.280  -5.631  42.176  1.00  8.70           C  
ANISOU  297  C   ILE A  35     1495   1022    788    -53    206    -88       C  
ATOM    298  O   ILE A  35      10.051  -4.575  42.795  1.00  9.95           O  
ANISOU  298  O   ILE A  35     1879   1021    882    -77    214   -174       O  
ATOM    299  CB  ILE A  35       8.647  -6.328  40.300  1.00  9.24           C  
ANISOU  299  CB  ILE A  35     1422   1164    925    -53    180   -130       C  
ATOM    300  CG1 ILE A  35       8.317  -6.012  38.798  1.00 11.43           C  
ANISOU  300  CG1 ILE A  35     1687   1557   1098    -25    -84   -148       C  
ATOM    301  CG2 ILE A  35       7.545  -5.810  41.240  1.00 11.72           C  
ANISOU  301  CG2 ILE A  35     1357   1554   1540    -39    268   -490       C  
ATOM    302  CD1 ILE A  35       7.179  -6.780  38.228  1.00 14.54           C  
ANISOU  302  CD1 ILE A  35     1600   2532   1394    -11   -237   -393       C  
ATOM    303  N   ASP A  36      10.740  -6.730  42.780  1.00  9.16           N  
ANISOU  303  N   ASP A  36     1709   1004    766    -68    188     -7       N  
ATOM    304  CA  ASP A  36      11.024  -6.702  44.238  1.00  9.17           C  
ANISOU  304  CA  ASP A  36     1664   1061    759   -114    124    -65       C  
ATOM    305  C   ASP A  36      12.080  -5.669  44.598  1.00  9.94           C  
ANISOU  305  C   ASP A  36     1896   1116    767   -171    253   -127       C  
ATOM    306  O   ASP A  36      11.989  -5.114  45.704  1.00 13.17           O  
ANISOU  306  O   ASP A  36     2365   1610   1030   -483    439   -478       O  
ATOM    307  CB  ASP A  36      11.499  -8.070  44.704  1.00  9.90           C  
ANISOU  307  CB  ASP A  36     1805   1025    931   -160    131     78       C  
ATOM    308  CG  ASP A  36      10.379  -9.099  44.747  1.00 10.00           C  
ANISOU  308  CG  ASP A  36     1862   1132    806   -117     10    115       C  
ATOM    309  OD1 ASP A  36       9.189  -8.762  44.681  1.00 11.43           O  
ANISOU  309  OD1 ASP A  36     1783   1325   1234   -157    144     91       O  
ATOM    310  OD2 ASP A  36      10.738 -10.315  44.875  1.00 12.43           O  
ANISOU  310  OD2 ASP A  36     2270   1119   1332   -188   -101    250       O  
ATOM    311  N   VAL A  37      13.080  -5.439  43.754  1.00  9.16           N  
ANISOU  311  N   VAL A  37     1699   1115    668   -159    101     12       N  
ATOM    312  CA  VAL A  37      14.163  -4.510  44.110  1.00  9.80           C  
ANISOU  312  CA  VAL A  37     1703   1154    866    -99    -33     19       C  
ATOM    313  C   VAL A  37      13.914  -3.090  43.648  1.00 10.27           C  
ANISOU  313  C   VAL A  37     2041   1175    686   -154   -147    -25       C  
ATOM    314  O   VAL A  37      14.681  -2.200  43.974  1.00 14.61           O  
ANISOU  314  O   VAL A  37     2630   1353   1567   -496   -759     85       O  
ATOM    315  CB  VAL A  37      15.576  -5.023  43.760  1.00 13.05           C  
ANISOU  315  CB  VAL A  37     1782   1871   1304     71    164     18       C  
ATOM    316  CG1 VAL A  37      15.841  -6.392  44.331  1.00 16.70           C  
ANISOU  316  CG1 VAL A  37     2127   1549   2669    279   -362   -124       C  
ATOM    317  CG2 VAL A  37      15.738  -4.988  42.293  1.00 16.12           C  
ANISOU  317  CG2 VAL A  37     1924   3016   1184     29    -50   -545       C  
ATOM    318  N   GLY A  38      12.781  -2.828  42.935  1.00  9.59           N  
ANISOU  318  N   GLY A  38     1845   1070    730    -25      6    -23       N  
ATOM    319  CA  GLY A  38      12.354  -1.473  42.655  1.00 11.01           C  
ANISOU  319  CA  GLY A  38     2325   1060    797    132     17    -24       C  
ATOM    320  C   GLY A  38      12.092  -1.122  41.210  1.00  8.67           C  
ANISOU  320  C   GLY A  38     1563    907    825    -48     33    -94       C  
ATOM    321  O   GLY A  38      11.613  -0.024  40.934  1.00 10.02           O  
ANISOU  321  O   GLY A  38     1913    945    948    114     69    -39       O  
ATOM    322  N   TYR A  39      12.395  -2.032  40.254  1.00  8.57           N  
ANISOU  322  N   TYR A  39     1511   1011    733    -17     10   -112       N  
ATOM    323  CA  TYR A  39      12.101  -1.683  38.852  1.00  7.97           C  
ANISOU  323  CA  TYR A  39     1293   1093    642     86     89    -66       C  
ATOM    324  C   TYR A  39      10.592  -1.563  38.662  1.00  8.39           C  
ANISOU  324  C   TYR A  39     1389   1119    680     80    119    -37       C  
ATOM    325  O   TYR A  39       9.797  -2.369  39.176  1.00  9.34           O  
ANISOU  325  O   TYR A  39     1364   1211    973    -35    153     25       O  
ATOM    326  CB  TYR A  39      12.605  -2.731  37.882  1.00  8.48           C  
ANISOU  326  CB  TYR A  39     1278   1122    824     67     43   -144       C  
ATOM    327  CG  TYR A  39      14.098  -2.880  37.731  1.00  8.05           C  
ANISOU  327  CG  TYR A  39     1370    946    743     88     12    -88       C  
ATOM    328  CD1 TYR A  39      14.921  -3.429  38.714  1.00  7.96           C  
ANISOU  328  CD1 TYR A  39     1314    922    790    -14     -4     -6       C  
ATOM    329  CD2 TYR A  39      14.715  -2.520  36.536  1.00  9.17           C  
ANISOU  329  CD2 TYR A  39     1411   1339    733    148    136     31       C  
ATOM    330  CE1 TYR A  39      16.250  -3.580  38.536  1.00  8.07           C  
ANISOU  330  CE1 TYR A  39     1315    910    840    -16     69     55       C  
ATOM    331  CE2 TYR A  39      16.073  -2.709  36.338  1.00  9.99           C  
ANISOU  331  CE2 TYR A  39     1444   1526    826    254    107    155       C  
ATOM    332  CZ  TYR A  39      16.839  -3.241  37.325  1.00  8.72           C  
ANISOU  332  CZ  TYR A  39     1368   1120    826     33     69    -14       C  
ATOM    333  OH  TYR A  39      18.195  -3.456  37.109  1.00 10.53           O  
ANISOU  333  OH  TYR A  39     1262   1621   1119    161    221    150       O  
ATOM    334  N   ARG A  40      10.223  -0.572  37.805  1.00  8.57           N  
ANISOU  334  N   ARG A  40     1313   1230    712    149     68      1       N  
ATOM    335  CA  ARG A  40       8.804  -0.335  37.495  1.00  9.21           C  
ANISOU  335  CA  ARG A  40     1340   1391    767    278    153      0       C  
ATOM    336  C   ARG A  40       8.559  -0.280  36.004  1.00  9.26           C  
ANISOU  336  C   ARG A  40     1124   1551    842    249     62     76       C  
ATOM    337  O  AARG A  40       7.427  -0.564  35.504  0.54 12.66           O  
ANISOU  337  O  AARG A  40     1278   2451   1080    242    -85    256       O  
ATOM    338  O  BARG A  40       7.552   0.379  35.650  0.46 10.43           O  
ANISOU  338  O  BARG A  40     1518   1751    694    668    104   -178       O  
ATOM    339  CB  ARG A  40       8.273   0.942  38.185  1.00 10.54           C  
ANISOU  339  CB  ARG A  40     1713   1323    968    411    270     77       C  
ATOM    340  CG  ARG A  40       8.348   0.843  39.723  1.00 11.81           C  
ANISOU  340  CG  ARG A  40     2154   1358    977    170    448    -82       C  
ATOM    341  CD  ARG A  40       7.307  -0.107  40.270  1.00 12.72           C  
ANISOU  341  CD  ARG A  40     2114   1708   1012    171    494    -28       C  
ATOM    342  NE  ARG A  40       7.323  -0.227  41.728  1.00 13.59           N  
ANISOU  342  NE  ARG A  40     2276   1797   1092    327    594    -15       N  
ATOM    343  CZ  ARG A  40       7.978  -1.149  42.409  1.00 13.20           C  
ANISOU  343  CZ  ARG A  40     2273   1755    988      4    431    -17       C  
ATOM    344  NH1 ARG A  40       8.771  -2.075  41.834  1.00 12.44           N  
ANISOU  344  NH1 ARG A  40     2082   1319   1326     70    373    104       N  
ATOM    345  NH2 ARG A  40       7.869  -1.146  43.768  1.00 18.08           N  
ANISOU  345  NH2 ARG A  40     3217   2630   1024    174    639     43       N  
ATOM    346  N   HIS A  41       9.576  -0.395  35.200  1.00  8.17           N  
ANISOU  346  N   HIS A  41     1222   1249    635    129    100   -208       N  
ATOM    347  CA  HIS A  41       9.504  -0.280  33.720  1.00  7.91           C  
ANISOU  347  CA  HIS A  41     1247   1045    713    111    113   -146       C  
ATOM    348  C   HIS A  41      10.166  -1.529  33.161  1.00  6.89           C  
ANISOU  348  C   HIS A  41     1071    922    623     10     23    -77       C  
ATOM    349  O   HIS A  41      11.279  -1.885  33.542  1.00  7.78           O  
ANISOU  349  O   HIS A  41     1150    986    820     77    -17   -135       O  
ATOM    350  CB  HIS A  41      10.302   0.998  33.366  1.00  7.97           C  
ANISOU  350  CB  HIS A  41     1188    992    847     78     50   -161       C  
ATOM    351  CG  HIS A  41      10.620   1.216  31.927  1.00  7.25           C  
ANISOU  351  CG  HIS A  41     1073    825    858     59    -14   -118       C  
ATOM    352  ND1 HIS A  41      11.441   2.253  31.562  1.00  9.29           N  
ANISOU  352  ND1 HIS A  41     1474   1039   1018   -227     53    -88       N  
ATOM    353  CD2 HIS A  41      10.335   0.585  30.749  1.00  8.10           C  
ANISOU  353  CD2 HIS A  41     1436    899    742    -30     89    -14       C  
ATOM    354  CE1 HIS A  41      11.634   2.188  30.244  1.00  9.64           C  
ANISOU  354  CE1 HIS A  41     1588   1078    996   -230     27   -130       C  
ATOM    355  NE2 HIS A  41      10.980   1.191  29.699  1.00  8.91           N  
ANISOU  355  NE2 HIS A  41     1521    987    878   -130     91     14       N  
ATOM    356  N   ILE A  42       9.400  -2.204  32.262  1.00  7.07           N  
ANISOU  356  N   ILE A  42     1113    912    662    -17    135   -113       N  
ATOM    357  CA  ILE A  42       9.903  -3.419  31.593  1.00  6.94           C  
ANISOU  357  CA  ILE A  42     1308    769    560    -47     75    -62       C  
ATOM    358  C   ILE A  42       9.761  -3.191  30.085  1.00  6.64           C  
ANISOU  358  C   ILE A  42     1152    745    625      9     -6    -38       C  
ATOM    359  O   ILE A  42       8.690  -2.772  29.614  1.00  7.94           O  
ANISOU  359  O   ILE A  42     1135   1160    724    181     45     -5       O  
ATOM    360  CB  ILE A  42       9.103  -4.679  32.026  1.00  8.41           C  
ANISOU  360  CB  ILE A  42     1391    943    863   -132     93    125       C  
ATOM    361  CG1 ILE A  42       8.936  -4.770  33.529  1.00 10.64           C  
ANISOU  361  CG1 ILE A  42     1888   1269    886   -192    198    180       C  
ATOM    362  CG2 ILE A  42       9.757  -5.921  31.398  1.00 10.14           C  
ANISOU  362  CG2 ILE A  42     1924    821   1106   -113    -18    -35       C  
ATOM    363  CD1AILE A  42      10.153  -5.056  34.319  0.74 12.85           C  
ANISOU  363  CD1AILE A  42     2018   1833   1033   -312     12    427       C  
ATOM    364  CD1BILE A  42       8.014  -5.776  34.071  0.26 11.85           C  
ANISOU  364  CD1BILE A  42     1687   1183   1632    156    466    631       C  
ATOM    365  N   ASP A  43      10.862  -3.453  29.352  1.00  6.14           N  
ANISOU  365  N   ASP A  43     1046    747    542    -25     21    -43       N  
ATOM    366  CA  ASP A  43      10.876  -3.313  27.892  1.00  6.21           C  
ANISOU  366  CA  ASP A  43     1095    691    575    -74     42     -4       C  
ATOM    367  C   ASP A  43      10.731  -4.690  27.257  1.00  5.88           C  
ANISOU  367  C   ASP A  43     1070    615    549      9     27     27       C  
ATOM    368  O   ASP A  43      11.568  -5.564  27.467  1.00  7.73           O  
ANISOU  368  O   ASP A  43     1242    711    985     62   -211   -108       O  
ATOM    369  CB  ASP A  43      12.195  -2.661  27.439  1.00  6.70           C  
ANISOU  369  CB  ASP A  43     1077    859    609   -132     18     12       C  
ATOM    370  CG  ASP A  43      12.177  -2.424  25.927  1.00  6.30           C  
ANISOU  370  CG  ASP A  43     1004    734    655     15     33      0       C  
ATOM    371  OD1 ASP A  43      11.509  -1.483  25.479  1.00  7.34           O  
ANISOU  371  OD1 ASP A  43     1271    803    714    136     71     89       O  
ATOM    372  OD2 ASP A  43      12.812  -3.242  25.186  1.00  7.03           O  
ANISOU  372  OD2 ASP A  43     1088    928    655    116    -17    -19       O  
ATOM    373  N   CYS A  44       9.657  -4.842  26.450  1.00  6.25           N  
ANISOU  373  N   CYS A  44     1045    699    631    -36    -35    -12       N  
ATOM    374  CA  CYS A  44       9.261  -6.128  25.867  1.00  6.21           C  
ANISOU  374  CA  CYS A  44     1087    646    627   -130    -39    -30       C  
ATOM    375  C   CYS A  44       9.166  -5.993  24.356  1.00  6.21           C  
ANISOU  375  C   CYS A  44     1000    683    675    -46     55    -38       C  
ATOM    376  O   CYS A  44       9.185  -4.887  23.777  1.00  7.14           O  
ANISOU  376  O   CYS A  44     1232    774    706    -19     10     44       O  
ATOM    377  CB  CYS A  44       7.881  -6.550  26.403  1.00  7.51           C  
ANISOU  377  CB  CYS A  44     1157   1006    691   -199    168     15       C  
ATOM    378  SG  CYS A  44       7.801  -6.659  28.190  1.00 11.70           S  
ANISOU  378  SG  CYS A  44     1812   1879    755   -576    145    119       S  
ATOM    379  N   ALA A  45       8.991  -7.143  23.697  1.00  6.86           N  
ANISOU  379  N   ALA A  45     1148    836    623    -90     49    -84       N  
ATOM    380  CA  ALA A  45       8.616  -7.124  22.259  1.00  6.92           C  
ANISOU  380  CA  ALA A  45     1227    885    517   -114    -43    -30       C  
ATOM    381  C   ALA A  45       8.113  -8.498  21.887  1.00  7.26           C  
ANISOU  381  C   ALA A  45     1247    879    634    -86      3    -39       C  
ATOM    382  O   ALA A  45       8.616  -9.532  22.334  1.00  8.02           O  
ANISOU  382  O   ALA A  45     1423    928    698   -122    -43    -51       O  
ATOM    383  CB  ALA A  45       9.816  -6.807  21.342  1.00  7.94           C  
ANISOU  383  CB  ALA A  45     1239   1126    653   -151     68     22       C  
ATOM    384  N   HIS A  46       7.151  -8.526  20.918  1.00  7.86           N  
ANISOU  384  N   HIS A  46     1251    957    777    -46    -44   -169       N  
ATOM    385  CA  HIS A  46       6.687  -9.818  20.417  1.00  8.01           C  
ANISOU  385  CA  HIS A  46     1173   1012    857   -107   -106   -220       C  
ATOM    386  C   HIS A  46       7.816 -10.660  19.822  1.00  7.60           C  
ANISOU  386  C   HIS A  46     1244    861    782   -154    -96   -134       C  
ATOM    387  O   HIS A  46       7.841 -11.880  19.984  1.00  8.71           O  
ANISOU  387  O   HIS A  46     1344    898   1069   -151    -35   -105       O  
ATOM    388  CB  HIS A  46       5.597  -9.560  19.361  1.00  9.22           C  
ANISOU  388  CB  HIS A  46     1302   1208    994    -32   -227   -260       C  
ATOM    389  CG  HIS A  46       5.086 -10.818  18.726  1.00  9.24           C  
ANISOU  389  CG  HIS A  46     1194   1295   1021     73   -208   -293       C  
ATOM    390  ND1 HIS A  46       4.382 -11.759  19.417  1.00 11.16           N  
ANISOU  390  ND1 HIS A  46     1496   1280   1463   -268   -210   -422       N  
ATOM    391  CD2 HIS A  46       5.187 -11.266  17.470  1.00 11.93           C  
ANISOU  391  CD2 HIS A  46     1506   1731   1296   -110   -217   -623       C  
ATOM    392  CE1 HIS A  46       4.008 -12.761  18.611  1.00 13.45           C  
ANISOU  392  CE1 HIS A  46     1952   1679   1481   -270    -78   -687       C  
ATOM    393  NE2 HIS A  46       4.500 -12.487  17.408  1.00 14.52           N  
ANISOU  393  NE2 HIS A  46     1908   2046   1562   -415    -21   -829       N  
ATOM    394  N   VAL A  47       8.760  -9.991  19.101  1.00  7.92           N  
ANISOU  394  N   VAL A  47     1253   1061    694     -4    -42    -69       N  
ATOM    395  CA  VAL A  47       9.827 -10.750  18.417  1.00  8.04           C  
ANISOU  395  CA  VAL A  47     1329   1013    711     41     30    -29       C  
ATOM    396  C   VAL A  47      10.766 -11.431  19.418  1.00  7.99           C  
ANISOU  396  C   VAL A  47     1411    862    762     -4     90     -4       C  
ATOM    397  O   VAL A  47      11.549 -12.309  19.007  1.00  9.90           O  
ANISOU  397  O   VAL A  47     1682   1177    902    321    138    -10       O  
ATOM    398  CB  VAL A  47      10.569  -9.824  17.413  1.00  8.56           C  
ANISOU  398  CB  VAL A  47     1610    982    659     24     67    -80       C  
ATOM    399  CG1 VAL A  47      11.557  -8.935  18.114  1.00 10.28           C  
ANISOU  399  CG1 VAL A  47     1735   1166   1006   -274     -6     81       C  
ATOM    400  CG2 VAL A  47      11.254 -10.610  16.301  1.00 12.17           C  
ANISOU  400  CG2 VAL A  47     2347   1277   1002    164    509   -121       C  
ATOM    401  N   TYR A  48      10.740 -11.028  20.701  1.00  7.20           N  
ANISOU  401  N   TYR A  48     1201    859    677   -111     19     41       N  
ATOM    402  CA  TYR A  48      11.647 -11.664  21.679  1.00  8.06           C  
ANISOU  402  CA  TYR A  48     1382    880    802    -65      0    111       C  
ATOM    403  C   TYR A  48      11.148 -13.029  22.104  1.00  7.85           C  
ANISOU  403  C   TYR A  48     1283    807    892     -2    -17     10       C  
ATOM    404  O   TYR A  48      11.898 -13.781  22.739  1.00  9.49           O  
ANISOU  404  O   TYR A  48     1405    952   1249    -30    -79    185       O  
ATOM    405  CB  TYR A  48      11.829 -10.781  22.949  1.00  8.25           C  
ANISOU  405  CB  TYR A  48     1425    963    746   -230     58     19       C  
ATOM    406  CG  TYR A  48      12.404  -9.385  22.648  1.00  7.07           C  
ANISOU  406  CG  TYR A  48     1092    885    711    -27    -18     20       C  
ATOM    407  CD1 TYR A  48      12.999  -9.050  21.456  1.00  7.18           C  
ANISOU  407  CD1 TYR A  48     1168    871    687    -50    -12     34       C  
ATOM    408  CD2 TYR A  48      12.295  -8.382  23.620  1.00  7.34           C  
ANISOU  408  CD2 TYR A  48     1097    989    703   -105    -55    -37       C  
ATOM    409  CE1 TYR A  48      13.492  -7.774  21.207  1.00  7.25           C  
ANISOU  409  CE1 TYR A  48     1179    850    724     21     25    -27       C  
ATOM    410  CE2 TYR A  48      12.785  -7.077  23.385  1.00  7.56           C  
ANISOU  410  CE2 TYR A  48     1151    968    754    -45    -19    -35       C  
ATOM    411  CZ  TYR A  48      13.377  -6.792  22.174  1.00  7.05           C  
ANISOU  411  CZ  TYR A  48     1119    823    734    -53      0     17       C  
ATOM    412  OH  TYR A  48      13.801  -5.483  21.934  1.00  8.00           O  
ANISOU  412  OH  TYR A  48     1352    833    853   -104     11    -22       O  
ATOM    413  N   GLN A  49       9.905 -13.402  21.765  1.00  7.96           N  
ANISOU  413  N   GLN A  49     1266    887    870   -142     59    -47       N  
ATOM    414  CA  GLN A  49       9.358 -14.759  21.953  1.00  8.39           C  
ANISOU  414  CA  GLN A  49     1552    753    883    -82     68   -143       C  
ATOM    415  C   GLN A  49       9.265 -15.152  23.424  1.00  8.41           C  
ANISOU  415  C   GLN A  49     1470    770    955   -175    166    -92       C  
ATOM    416  O   GLN A  49       9.300 -16.324  23.757  1.00 12.92           O  
ANISOU  416  O   GLN A  49     3036    655   1217   -155    576    -53       O  
ATOM    417  CB  GLN A  49      10.152 -15.833  21.154  1.00 10.46           C  
ANISOU  417  CB  GLN A  49     1892   1187    896    115     52   -255       C  
ATOM    418  CG  GLN A  49      10.036 -15.619  19.647  1.00 12.76           C  
ANISOU  418  CG  GLN A  49     2573   1401    875      5    157   -322       C  
ATOM    419  CD  GLN A  49      10.733 -16.724  18.821  1.00 15.63           C  
ANISOU  419  CD  GLN A  49     3105   1711   1122    738    145   -289       C  
ATOM    420  OE1 GLN A  49      11.529 -16.449  17.937  1.00 21.55           O  
ANISOU  420  OE1 GLN A  49     3636   2992   1560   1424    663     87       O  
ATOM    421  NE2 GLN A  49      10.432 -18.007  19.116  1.00 19.91           N  
ANISOU  421  NE2 GLN A  49     3689   1583   2293    444   -391   -642       N  
ATOM    422  N   ASN A  50       9.107 -14.186  24.340  1.00  7.65           N  
ANISOU  422  N   ASN A  50     1466    669    770    -28    100    -53       N  
ATOM    423  CA  ASN A  50       9.045 -14.456  25.756  1.00  7.52           C  
ANISOU  423  CA  ASN A  50     1352    731    776   -102     62    -16       C  
ATOM    424  C   ASN A  50       7.982 -13.598  26.460  1.00  7.00           C  
ANISOU  424  C   ASN A  50     1294    651    714   -144     50     39       C  
ATOM    425  O   ASN A  50       7.997 -13.531  27.699  1.00  8.24           O  
ANISOU  425  O   ASN A  50     1430    878    822    -81    102     25       O  
ATOM    426  CB  ASN A  50      10.419 -14.311  26.417  1.00  7.88           C  
ANISOU  426  CB  ASN A  50     1411    703    878   -167    -47    -38       C  
ATOM    427  CG  ASN A  50      10.983 -12.898  26.228  1.00  7.95           C  
ANISOU  427  CG  ASN A  50     1431    751    839   -185      7   -121       C  
ATOM    428  OD1 ASN A  50      10.288 -12.010  25.738  1.00  8.96           O  
ANISOU  428  OD1 ASN A  50     1580    642   1183   -155      2     15       O  
ATOM    429  ND2 ASN A  50      12.235 -12.707  26.605  1.00  9.86           N  
ANISOU  429  ND2 ASN A  50     1523   1111   1113   -394    -10    -29       N  
ATOM    430  N   GLU A  51       7.067 -12.965  25.734  1.00  7.43           N  
ANISOU  430  N   GLU A  51     1361    661    800    -79    132     19       N  
ATOM    431  CA  GLU A  51       6.082 -12.095  26.405  1.00  7.41           C  
ANISOU  431  CA  GLU A  51     1238    754    824    -86     71     42       C  
ATOM    432  C   GLU A  51       5.164 -12.886  27.319  1.00  7.42           C  
ANISOU  432  C   GLU A  51     1300    738    781   -145     84     37       C  
ATOM    433  O   GLU A  51       4.745 -12.343  28.364  1.00  8.46           O  
ANISOU  433  O   GLU A  51     1498    857    861   -198    199    -40       O  
ATOM    434  CB  GLU A  51       5.309 -11.246  25.399  1.00  7.84           C  
ANISOU  434  CB  GLU A  51     1264    774    939   -157    -32    111       C  
ATOM    435  CG  GLU A  51       6.184 -10.151  24.779  1.00  8.58           C  
ANISOU  435  CG  GLU A  51     1295    930   1034   -148     -9    221       C  
ATOM    436  CD  GLU A  51       5.427  -9.093  23.979  1.00  7.50           C  
ANISOU  436  CD  GLU A  51     1260    805    783   -131     35     33       C  
ATOM    437  OE1 GLU A  51       4.515  -9.456  23.177  1.00  8.70           O  
ANISOU  437  OE1 GLU A  51     1390    944    970   -120   -129    -18       O  
ATOM    438  OE2 GLU A  51       5.811  -7.919  24.112  1.00  9.00           O  
ANISOU  438  OE2 GLU A  51     1548    806   1067   -132   -172     61       O  
ATOM    439  N   ASN A  52       4.787 -14.132  26.991  1.00  7.84           N  
ANISOU  439  N   ASN A  52     1357    722    900   -212    105     22       N  
ATOM    440  CA  ASN A  52       3.915 -14.870  27.918  1.00  8.46           C  
ANISOU  440  CA  ASN A  52     1558    818    839   -388    100    -85       C  
ATOM    441  C   ASN A  52       4.550 -15.012  29.297  1.00  7.97           C  
ANISOU  441  C   ASN A  52     1410    706    913   -315    101     41       C  
ATOM    442  O   ASN A  52       3.920 -14.825  30.342  1.00  9.51           O  
ANISOU  442  O   ASN A  52     1660   1053    902   -302    253    -17       O  
ATOM    443  CB  ASN A  52       3.602 -16.269  27.298  1.00  9.45           C  
ANISOU  443  CB  ASN A  52     1684    816   1091   -445     65   -109       C  
ATOM    444  CG AASN A  52       2.436 -16.099  26.338  0.08 11.77           C  
ANISOU  444  CG AASN A  52     2155    871   1448   -566   -381    -52       C  
ATOM    445  CG BASN A  52       2.554 -16.997  28.113  0.92  9.62           C  
ANISOU  445  CG BASN A  52     1475    947   1234   -393    108   -162       C  
ATOM    446  OD1AASN A  52       2.586 -15.989  25.122  0.08 20.05           O  
ANISOU  446  OD1AASN A  52     2604   3339   1676  -1430   -541   1288       O  
ATOM    447  OD1BASN A  52       1.518 -16.416  28.451  0.92 13.37           O  
ANISOU  447  OD1BASN A  52     1707   1219   2155   -443    514   -337       O  
ATOM    448  ND2AASN A  52       1.252 -16.072  26.945  0.08 16.37           N  
ANISOU  448  ND2AASN A  52     1915   2536   1768     91   -538   -291       N  
ATOM    449  ND2BASN A  52       2.759 -18.288  28.337  0.92 12.87           N  
ANISOU  449  ND2BASN A  52     1865   1109   1915   -394    232    333       N  
ATOM    450  N   GLU A  53       5.868 -15.327  29.305  1.00  8.39           N  
ANISOU  450  N   GLU A  53     1478    827    882   -249     11     33       N  
ATOM    451  CA  GLU A  53       6.615 -15.568  30.553  1.00  8.71           C  
ANISOU  451  CA  GLU A  53     1541    823    944   -311    -37     32       C  
ATOM    452  C   GLU A  53       6.856 -14.271  31.307  1.00  7.99           C  
ANISOU  452  C   GLU A  53     1328    858    848   -212     52     31       C  
ATOM    453  O   GLU A  53       6.844 -14.268  32.544  1.00  9.54           O  
ANISOU  453  O   GLU A  53     1817    950    856   -316    -14     81       O  
ATOM    454  CB  GLU A  53       7.912 -16.337  30.230  1.00 10.16           C  
ANISOU  454  CB  GLU A  53     1774    862   1224     16   -143      1       C  
ATOM    455  CG  GLU A  53       7.645 -17.769  29.757  1.00 12.57           C  
ANISOU  455  CG  GLU A  53     2407    883   1487    -68   -194     26       C  
ATOM    456  CD  GLU A  53       7.392 -17.939  28.295  1.00 13.28           C  
ANISOU  456  CD  GLU A  53     2562   1001   1484   -445   -100   -115       C  
ATOM    457  OE1 GLU A  53       7.335 -16.991  27.489  1.00 11.67           O  
ANISOU  457  OE1 GLU A  53     2197   1034   1204   -170    147   -153       O  
ATOM    458  OE2 GLU A  53       7.365 -19.143  27.858  1.00 18.51           O  
ANISOU  458  OE2 GLU A  53     3512   1058   2461   -207   -699   -338       O  
ATOM    459  N   VAL A  54       7.085 -13.162  30.585  1.00  8.09           N  
ANISOU  459  N   VAL A  54     1446    740    886   -259     25     11       N  
ATOM    460  CA  VAL A  54       7.122 -11.848  31.262  1.00  8.10           C  
ANISOU  460  CA  VAL A  54     1501    825    751   -266     52     26       C  
ATOM    461  C   VAL A  54       5.785 -11.590  31.940  1.00  7.87           C  
ANISOU  461  C   VAL A  54     1487    761    741   -259     44    -38       C  
ATOM    462  O   VAL A  54       5.712 -11.148  33.102  1.00  8.97           O  
ANISOU  462  O   VAL A  54     1587   1017    803   -260     72    -56       O  
ATOM    463  CB  VAL A  54       7.477 -10.738  30.254  1.00  8.44           C  
ANISOU  463  CB  VAL A  54     1502    793    912   -255    113     19       C  
ATOM    464  CG1 VAL A  54       7.321  -9.360  30.931  1.00 10.10           C  
ANISOU  464  CG1 VAL A  54     1913    806   1117   -248    214    -35       C  
ATOM    465  CG2 VAL A  54       8.897 -10.900  29.712  1.00 10.12           C  
ANISOU  465  CG2 VAL A  54     1477   1169   1201   -285    234    -32       C  
ATOM    466  N   GLY A  55       4.695 -11.877  31.215  1.00  8.18           N  
ANISOU  466  N   GLY A  55     1383    894    830   -174     79     -7       N  
ATOM    467  CA  GLY A  55       3.340 -11.651  31.753  1.00  9.21           C  
ANISOU  467  CA  GLY A  55     1445   1116    936   -115    186     92       C  
ATOM    468  C   GLY A  55       3.069 -12.450  33.020  1.00  8.21           C  
ANISOU  468  C   GLY A  55     1306    897    918   -121     59    -61       C  
ATOM    469  O   GLY A  55       2.402 -11.935  33.939  1.00  9.45           O  
ANISOU  469  O   GLY A  55     1567   1102    923    -89    175    -82       O  
ATOM    470  N   VAL A  56       3.532 -13.687  33.090  1.00  8.35           N  
ANISOU  470  N   VAL A  56     1360    919    895   -218     72     21       N  
ATOM    471  CA  VAL A  56       3.350 -14.494  34.317  1.00  8.48           C  
ANISOU  471  CA  VAL A  56     1494    860    869   -285     93     12       C  
ATOM    472  C   VAL A  56       3.952 -13.783  35.508  1.00  8.52           C  
ANISOU  472  C   VAL A  56     1514    917    806   -272    111     16       C  
ATOM    473  O   VAL A  56       3.327 -13.716  36.602  1.00  9.63           O  
ANISOU  473  O   VAL A  56     1575   1182    901   -379    214    -35       O  
ATOM    474  CB  VAL A  56       3.979 -15.879  34.138  1.00  9.44           C  
ANISOU  474  CB  VAL A  56     1800    878    910   -166     42    -17       C  
ATOM    475  CG1 VAL A  56       3.947 -16.647  35.491  1.00 12.80           C  
ANISOU  475  CG1 VAL A  56     2707   1022   1137   -204     46    192       C  
ATOM    476  CG2 VAL A  56       3.257 -16.707  33.071  1.00 10.54           C  
ANISOU  476  CG2 VAL A  56     1835   1040   1130   -440     89   -164       C  
ATOM    477  N   ALA A  57       5.153 -13.205  35.360  1.00  8.40           N  
ANISOU  477  N   ALA A  57     1419    871    902   -238     74    -27       N  
ATOM    478  CA  ALA A  57       5.808 -12.485  36.475  1.00  8.53           C  
ANISOU  478  CA  ALA A  57     1403    913    925   -157     35    -25       C  
ATOM    479  C   ALA A  57       5.006 -11.265  36.900  1.00  8.37           C  
ANISOU  479  C   ALA A  57     1387    978    815   -226     32   -104       C  
ATOM    480  O   ALA A  57       4.850 -11.013  38.102  1.00  9.68           O  
ANISOU  480  O   ALA A  57     1465   1306    908   -170     58   -129       O  
ATOM    481  CB  ALA A  57       7.194 -12.071  36.052  1.00  9.71           C  
ANISOU  481  CB  ALA A  57     1365   1206   1118   -262     62     21       C  
ATOM    482  N   ILE A  58       4.574 -10.465  35.907  1.00  9.07           N  
ANISOU  482  N   ILE A  58     1661    860    927    -93     39    -99       N  
ATOM    483  CA  ILE A  58       3.813  -9.272  36.244  1.00  9.50           C  
ANISOU  483  CA  ILE A  58     1584    957   1067    -80     34   -146       C  
ATOM    484  C   ILE A  58       2.533  -9.649  37.001  1.00  9.72           C  
ANISOU  484  C   ILE A  58     1635   1082    975    -79     18   -194       C  
ATOM    485  O   ILE A  58       2.193  -9.029  38.026  1.00 10.63           O  
ANISOU  485  O   ILE A  58     1654   1296   1090    -70    100   -295       O  
ATOM    486  CB  ILE A  58       3.498  -8.468  34.956  1.00 10.56           C  
ANISOU  486  CB  ILE A  58     1837    994   1180      6     52    -19       C  
ATOM    487  CG1 ILE A  58       4.797  -7.933  34.307  1.00 12.75           C  
ANISOU  487  CG1 ILE A  58     2179   1035   1632   -243    137    250       C  
ATOM    488  CG2 ILE A  58       2.459  -7.385  35.290  1.00 14.52           C  
ANISOU  488  CG2 ILE A  58     2496   1419   1600    599    -24    -15       C  
ATOM    489  CD1 ILE A  58       4.585  -7.395  32.907  1.00 15.86           C  
ANISOU  489  CD1 ILE A  58     2973   1392   1660    -73    368    323       C  
ATOM    490  N  AGLN A  59       1.795 -10.650  36.526  0.40  9.87           N  
ANISOU  490  N  AGLN A  59     1493   1223   1034    -77     48   -283       N  
ATOM    491  N  BGLN A  59       1.827 -10.663  36.473  0.60 10.62           N  
ANISOU  491  N  BGLN A  59     1542   1371   1122   -201     68   -351       N  
ATOM    492  CA AGLN A  59       0.555 -11.003  37.230  0.40 11.63           C  
ANISOU  492  CA AGLN A  59     1483   1678   1256   -295     -2   -356       C  
ATOM    493  CA BGLN A  59       0.571 -11.071  37.101  0.60 10.36           C  
ANISOU  493  CA BGLN A  59     1461   1380   1095    -49     59   -245       C  
ATOM    494  C  AGLN A  59       0.825 -11.524  38.630  0.40 10.81           C  
ANISOU  494  C  AGLN A  59     1426   1448   1235   -310    263   -332       C  
ATOM    495  C  BGLN A  59       0.785 -11.553  38.530  0.60 10.68           C  
ANISOU  495  C  BGLN A  59     1522   1486   1050   -192     24   -342       C  
ATOM    496  O  AGLN A  59       0.063 -11.287  39.574  0.40 11.24           O  
ANISOU  496  O  AGLN A  59     1323   1687   1259   -263    148   -602       O  
ATOM    497  O  BGLN A  59      -0.046 -11.228  39.387  0.60 13.47           O  
ANISOU  497  O  BGLN A  59     1717   2261   1139   -334    274   -308       O  
ATOM    498  CB AGLN A  59      -0.143 -12.064  36.389  0.40 11.97           C  
ANISOU  498  CB AGLN A  59     1262   1663   1624     26     -8   -693       C  
ATOM    499  CB BGLN A  59      -0.087 -12.201  36.297  0.60 14.33           C  
ANISOU  499  CB BGLN A  59     1924   2094   1427   -557   -471   -268       C  
ATOM    500  CG AGLN A  59      -1.486 -12.508  36.832  0.40 16.93           C  
ANISOU  500  CG AGLN A  59     2004   2956   1474  -1211    135   -405       C  
ATOM    501  CG BGLN A  59      -0.851 -11.621  35.114  0.60 17.93           C  
ANISOU  501  CG BGLN A  59     2833   2450   1529   -155   -735   -296       C  
ATOM    502  CD AGLN A  59      -1.736 -13.694  37.706  0.40 35.60           C  
ANISOU  502  CD AGLN A  59     4302   5051   4174  -1957   -148   1920       C  
ATOM    503  CD BGLN A  59      -1.986 -10.697  35.626  0.60 26.22           C  
ANISOU  503  CD BGLN A  59     2478   4267   3218    662  -1548  -1187       C  
ATOM    504  OE1AGLN A  59      -0.998 -14.648  38.004  0.40 46.67           O  
ANISOU  504  OE1AGLN A  59     4583   5859   7290  -2664  -2298   3964       O  
ATOM    505  OE1BGLN A  59      -2.724 -10.844  36.601  0.60 29.07           O  
ANISOU  505  OE1BGLN A  59     2728   5027   3289   1750  -1240  -1309       O  
ATOM    506  NE2AGLN A  59      -2.977 -13.719  38.246  0.40 43.16           N  
ANISOU  506  NE2AGLN A  59     6016   6121   4261  -2362   1907   1751       N  
ATOM    507  NE2BGLN A  59      -2.075  -9.604  34.961  0.60 31.05           N  
ANISOU  507  NE2BGLN A  59     4337   3859   3599   1555  -1055  -1509       N  
ATOM    508  N  AGLU A  60       1.907 -12.275  38.822  0.32  9.25           N  
ANISOU  508  N  AGLU A  60     1442   1213    860   -371    368   -306       N  
ATOM    509  N  BGLU A  60       1.844 -12.327  38.784  0.68 11.44           N  
ANISOU  509  N  BGLU A  60     1742   1402   1202   -210   -149   -116       N  
ATOM    510  CA AGLU A  60       2.258 -12.785  40.146  0.32 10.21           C  
ANISOU  510  CA AGLU A  60     1560   1427    893   -416    426   -182       C  
ATOM    511  CA BGLU A  60       2.107 -12.795  40.163  0.68 11.68           C  
ANISOU  511  CA BGLU A  60     1817   1422   1199   -310    -71    -85       C  
ATOM    512  C  AGLU A  60       2.530 -11.666  41.143  0.32  9.69           C  
ANISOU  512  C  AGLU A  60     1762   1137    783    -22     12     43       C  
ATOM    513  C  BGLU A  60       2.356 -11.581  41.070  0.68 11.12           C  
ANISOU  513  C  BGLU A  60     1447   1690   1087   -418    159   -184       C  
ATOM    514  O  AGLU A  60       2.195 -11.776  42.325  0.32  9.70           O  
ANISOU  514  O  AGLU A  60     1421   1499    766    -51     53   -116       O  
ATOM    515  O  BGLU A  60       1.811 -11.514  42.179  0.68 11.91           O  
ANISOU  515  O  BGLU A  60     1588   1897   1042   -279    220     11       O  
ATOM    516  CB AGLU A  60       3.527 -13.640  39.997  0.32 12.90           C  
ANISOU  516  CB AGLU A  60     2260   1511   1132    178    222   -252       C  
ATOM    517  CB BGLU A  60       3.297 -13.771  40.175  0.68 11.46           C  
ANISOU  517  CB BGLU A  60     1898   1255   1202   -318    268    345       C  
ATOM    518  CG AGLU A  60       3.990 -14.205  41.321  0.32 15.02           C  
ANISOU  518  CG AGLU A  60     2790   1365   1551    -64    273    381       C  
ATOM    519  CG BGLU A  60       3.049 -15.137  39.593  0.68 12.82           C  
ANISOU  519  CG BGLU A  60     2035   1376   1460   -216      9     90       C  
ATOM    520  CD BGLU A  60       4.155 -16.169  39.548  0.68 17.98           C  
ANISOU  520  CD BGLU A  60     2575   1757   2499    400   -981   -186       C  
ATOM    521  OE1BGLU A  60       5.216 -15.793  39.993  0.68 37.78           O  
ANISOU  521  OE1BGLU A  60     2593   2758   9005   -116  -2059   -225       O  
ATOM    522  OE2BGLU A  60       4.051 -17.305  39.130  0.68 24.14           O  
ANISOU  522  OE2BGLU A  60     3532   1781   3858    346   -450   -466       O  
ATOM    523  N   LYS A  61       3.159 -10.598  40.656  1.00  9.67           N  
ANISOU  523  N   LYS A  61     1459   1281    935   -185     24    -80       N  
ATOM    524  CA  LYS A  61       3.469  -9.484  41.565  1.00 10.03           C  
ANISOU  524  CA  LYS A  61     1468   1341   1002   -178    132   -208       C  
ATOM    525  C   LYS A  61       2.271  -8.560  41.783  1.00 10.45           C  
ANISOU  525  C   LYS A  61     1499   1509    963   -167     80   -389       C  
ATOM    526  O   LYS A  61       2.131  -7.993  42.858  1.00 12.64           O  
ANISOU  526  O   LYS A  61     1817   1879   1106    -76    122   -476       O  
ATOM    527  CB  LYS A  61       4.692  -8.710  41.027  1.00 10.26           C  
ANISOU  527  CB  LYS A  61     1422   1412   1066   -135     72   -141       C  
ATOM    528  CG  LYS A  61       5.972  -9.548  41.155  1.00 10.51           C  
ANISOU  528  CG  LYS A  61     1407   1668    917    -73     50    -91       C  
ATOM    529  CD  LYS A  61       6.402  -9.770  42.614  1.00 10.61           C  
ANISOU  529  CD  LYS A  61     1662   1406    961     58    -57   -196       C  
ATOM    530  CE  LYS A  61       7.458 -10.860  42.717  1.00 11.13           C  
ANISOU  530  CE  LYS A  61     1677   1575    976     21    -36   -111       C  
ATOM    531  NZ  LYS A  61       7.727 -11.162  44.188  1.00 11.58           N  
ANISOU  531  NZ  LYS A  61     1856   1461   1084    -81    -50     64       N  
ATOM    532  N   LEU A  62       1.367  -8.447  40.782  1.00 10.42           N  
ANISOU  532  N   LEU A  62     1413   1382   1164    -67     77   -338       N  
ATOM    533  CA  LEU A  62       0.108  -7.755  41.010  1.00 11.72           C  
ANISOU  533  CA  LEU A  62     1518   1497   1439      3     41   -396       C  
ATOM    534  C   LEU A  62      -0.747  -8.540  41.995  1.00 12.63           C  
ANISOU  534  C   LEU A  62     1490   1813   1493   -136    276   -515       C  
ATOM    535  O   LEU A  62      -1.320  -7.969  42.961  1.00 16.62           O  
ANISOU  535  O   LEU A  62     1843   2370   2101   -218    647   -844       O  
ATOM    536  CB  LEU A  62      -0.654  -7.588  39.673  1.00 13.06           C  
ANISOU  536  CB  LEU A  62     1648   1867   1447    151   -141   -558       C  
ATOM    537  CG  LEU A  62      -0.043  -6.626  38.651  1.00 14.16           C  
ANISOU  537  CG  LEU A  62     2126   1806   1448    366   -145   -277       C  
ATOM    538  CD1 LEU A  62      -0.778  -6.717  37.307  1.00 17.51           C  
ANISOU  538  CD1 LEU A  62     2838   2295   1518    508   -418   -512       C  
ATOM    539  CD2 LEU A  62      -0.098  -5.172  39.135  1.00 17.05           C  
ANISOU  539  CD2 LEU A  62     3023   1817   1640    302   -143   -384       C  
ATOM    540  N  AARG A  63      -0.759  -9.862  41.903  0.57 13.68           N  
ANISOU  540  N  AARG A  63     1472   1763   1961   -315    438   -417       N  
ATOM    541  N  BARG A  63      -0.954  -9.831  41.795  0.43 12.73           N  
ANISOU  541  N  BARG A  63     1623   1995   1218   -521    192   -510       N  
ATOM    542  CA AARG A  63      -1.558 -10.687  42.835  0.57 14.48           C  
ANISOU  542  CA AARG A  63     1642   2069   1790   -309    586   -459       C  
ATOM    543  CA BARG A  63      -1.878 -10.601  42.653  0.43 15.75           C  
ANISOU  543  CA BARG A  63     1743   2365   1875   -941    500   -709       C  
ATOM    544  C  AARG A  63      -0.979 -10.661  44.240  0.57 14.73           C  
ANISOU  544  C  AARG A  63     1531   2301   1765   -631    743   -680       C  
ATOM    545  C  BARG A  63      -1.422 -10.590  44.100  0.43 15.99           C  
ANISOU  545  C  BARG A  63     1871   2396   1808   -569    617    252       C  
ATOM    546  O  AARG A  63      -1.698 -10.668  45.275  0.57 17.12           O  
ANISOU  546  O  AARG A  63     1697   2967   1841   -753    763   -705       O  
ATOM    547  O  BARG A  63      -2.254 -10.560  45.051  0.43 18.05           O  
ANISOU  547  O  BARG A  63     1907   2979   1972   -706    703   -389       O  
ATOM    548  CB AARG A  63      -1.667 -12.100  42.260  0.57 17.30           C  
ANISOU  548  CB AARG A  63     2724   2142   1706  -1159    259   -301       C  
ATOM    549  CB BARG A  63      -1.969 -12.011  42.050  0.43 18.89           C  
ANISOU  549  CB BARG A  63     2246   2001   2930   -588   1157   -607       C  
ATOM    550  CG AARG A  63      -2.739 -12.920  42.958  0.57 26.50           C  
ANISOU  550  CG AARG A  63     3129   2798   4144  -1113   1410    202       C  
ATOM    551  CG BARG A  63      -1.605 -13.075  43.091  0.43 26.40           C  
ANISOU  551  CG BARG A  63     3973   2575   3485   -132    201   -456       C  
ATOM    552  CD AARG A  63      -3.847 -12.103  43.583  0.57 44.48           C  
ANISOU  552  CD AARG A  63     4523   4775   7602    725   3487   1964       C  
ATOM    553  CD BARG A  63      -2.862 -13.848  43.376  0.43 35.71           C  
ANISOU  553  CD BARG A  63     5378   3309   4881  -1145    239   1565       C  
ATOM    554  NE AARG A  63      -4.911 -11.453  42.872  0.57 53.94           N  
ANISOU  554  NE AARG A  63     5011   5511   9973   1165   2600   2111       N  
ATOM    555  NE BARG A  63      -2.888 -14.986  44.220  0.43 43.00           N  
ANISOU  555  NE BARG A  63     7514   3686   5140  -1042   -749   1945       N  
ATOM    556  CZ AARG A  63      -6.123 -11.853  42.525  0.57 52.38           C  
ANISOU  556  CZ AARG A  63     4617   5443   9841   1074   3088   2957       C  
ATOM    557  CZ BARG A  63      -2.039 -15.618  44.998  0.43 47.03           C  
ANISOU  557  CZ BARG A  63     8725   4171   4972   -290  -1419   1291       C  
ATOM    558  NH1AARG A  63      -6.538 -13.079  42.835  0.57 56.99           N  
ANISOU  558  NH1AARG A  63     5243   6588   9821    486   2627   4688       N  
ATOM    559  NH1BARG A  63      -0.783 -15.222  45.153  0.43 43.22           N  
ANISOU  559  NH1BARG A  63     9674   3929   2819  -1019  -3013    411       N  
ATOM    560  NH2AARG A  63      -6.946 -11.052  41.858  0.57 52.26           N  
ANISOU  560  NH2AARG A  63     6607   3838   9411    355    756   1538       N  
ATOM    561  NH2BARG A  63      -2.516 -16.694  45.624  0.43 48.03           N  
ANISOU  561  NH2BARG A  63     9839   4395   4015  -1162  -3283   1512       N  
ATOM    562  N  AGLU A  64       0.356 -10.667  44.364  0.57 13.13           N  
ANISOU  562  N  AGLU A  64     1564   1804   1622   -433    589   -779       N  
ATOM    563  N  BGLU A  64      -0.111 -10.609  44.331  0.43 14.30           N  
ANISOU  563  N  BGLU A  64     1930   2297   1207   -419    691     75       N  
ATOM    564  CA AGLU A  64       1.000 -10.559  45.673  0.57 14.46           C  
ANISOU  564  CA AGLU A  64     1953   2189   1353   -654    647   -628       C  
ATOM    565  CA BGLU A  64       0.571 -10.655  45.604  0.43 15.23           C  
ANISOU  565  CA BGLU A  64     2263   2296   1229   -532    583   -105       C  
ATOM    566  C  AGLU A  64       0.805  -9.164  46.272  0.57 15.07           C  
ANISOU  566  C  AGLU A  64     2251   2236   1239   -710    654   -696       C  
ATOM    567  C  BGLU A  64       0.565  -9.263  46.250  0.43 16.40           C  
ANISOU  567  C  BGLU A  64     2097   2499   1634   -559    947   -417       C  
ATOM    568  O  AGLU A  64       1.181  -8.927  47.423  0.57 18.09           O  
ANISOU  568  O  AGLU A  64     2708   2835   1331   -978    602   -795       O  
ATOM    569  O  BGLU A  64       0.895  -9.232  47.432  0.43 19.24           O  
ANISOU  569  O  BGLU A  64     3021   2673   1615  -1028    842   -380       O  
ATOM    570  CB AGLU A  64       2.527 -10.843  45.604  0.57 14.15           C  
ANISOU  570  CB AGLU A  64     1868   1988   1521   -742    446   -244       C  
ATOM    571  CB BGLU A  64       2.037 -11.084  45.479  0.43 16.15           C  
ANISOU  571  CB BGLU A  64     2426   2164   1546   -232    101   -308       C  
ATOM    572  CG AGLU A  64       2.870 -12.296  45.332  0.57 15.86           C  
ANISOU  572  CG AGLU A  64     2079   2079   1868   -602    571   -239       C  
ATOM    573  CG BGLU A  64       2.448 -12.528  45.309  0.43 21.54           C  
ANISOU  573  CG BGLU A  64     2871   2183   3129   -165      4   -293       C  
ATOM    574  CD AGLU A  64       4.343 -12.569  45.508  0.57 19.15           C  
ANISOU  574  CD AGLU A  64     2161   2055   3061   -515    642    581       C  
ATOM    575  CD BGLU A  64       3.915 -12.684  44.938  0.43 22.02           C  
ANISOU  575  CD BGLU A  64     3215   2536   2616    681    285    529       C  
ATOM    576  OE1AGLU A  64       5.185 -11.797  45.061  0.57 18.14           O  
ANISOU  576  OE1AGLU A  64     2192   2194   2506   -907    919   -338       O  
ATOM    577  OE1BGLU A  64       4.765 -11.790  45.101  0.43 19.91           O  
ANISOU  577  OE1BGLU A  64     2202   3268   2097    816    432    501       O  
ATOM    578  OE2AGLU A  64       4.729 -13.592  46.118  0.57 28.68           O  
ANISOU  578  OE2AGLU A  64     3000   3244   4655   -258    169   1748       O  
ATOM    579  OE2BGLU A  64       4.291 -13.777  44.442  0.43 26.64           O  
ANISOU  579  OE2BGLU A  64     4509   3495   2120   1181    296   -203       O  
ATOM    580  N   GLN A  65       0.261  -8.207  45.523  1.00 16.37           N  
ANISOU  580  N   GLN A  65     2059   2248   1914   -431    527   -681       N  
ATOM    581  CA  GLN A  65       0.148  -6.831  46.033  1.00 17.99           C  
ANISOU  581  CA  GLN A  65     1834   2556   2448    -18    274  -1174       C  
ATOM    582  C   GLN A  65       1.506  -6.211  46.354  1.00 13.40           C  
ANISOU  582  C   GLN A  65     1869   1954   1270    -33    224   -495       C  
ATOM    583  O   GLN A  65       1.654  -5.365  47.231  1.00 16.59           O  
ANISOU  583  O   GLN A  65     2222   2414   1668      0    420   -973       O  
ATOM    584  CB  GLN A  65      -0.761  -6.730  47.255  1.00 27.87           C  
ANISOU  584  CB  GLN A  65     2356   4103   4130   -695   1484  -2329       C  
ATOM    585  CG  GLN A  65      -2.099  -7.457  47.092  1.00 36.91           C  
ANISOU  585  CG  GLN A  65     2871   4403   6750  -1390   2047  -2296       C  
ATOM    586  CD  GLN A  65      -2.791  -7.174  48.435  1.00 47.53           C  
ANISOU  586  CD  GLN A  65     4346   5473   8241  -1784   3959  -2295       C  
ATOM    587  OE1 GLN A  65      -2.770  -7.910  49.416  1.00 62.87           O  
ANISOU  587  OE1 GLN A  65     6891   8296   8702  -1613   5294   -872       O  
ATOM    588  NE2 GLN A  65      -3.393  -5.997  48.396  1.00 66.60           N  
ANISOU  588  NE2 GLN A  65     5058   9471  10778   2331   4244  -2172       N  
ATOM    589  N   VAL A  66       2.527  -6.609  45.584  1.00 11.58           N  
ANISOU  589  N   VAL A  66     1778   1652    971    129     81   -284       N  
ATOM    590  CA  VAL A  66       3.837  -5.922  45.624  1.00 10.83           C  
ANISOU  590  CA  VAL A  66     1638   1496    982    110    -69   -292       C  
ATOM    591  C   VAL A  66       3.779  -4.584  44.937  1.00 10.97           C  
ANISOU  591  C   VAL A  66     1570   1608    989    183     38   -306       C  
ATOM    592  O   VAL A  66       4.456  -3.625  45.326  1.00 13.47           O  
ANISOU  592  O   VAL A  66     1972   1638   1509    -36   -167   -376       O  
ATOM    593  CB  VAL A  66       4.931  -6.842  45.007  1.00 11.62           C  
ANISOU  593  CB  VAL A  66     1804   1763    849    328    -65   -286       C  
ATOM    594  CG1 VAL A  66       6.275  -6.118  44.940  1.00 15.09           C  
ANISOU  594  CG1 VAL A  66     1574   2734   1428    318     70   -415       C  
ATOM    595  CG2 VAL A  66       5.078  -8.123  45.803  1.00 14.90           C  
ANISOU  595  CG2 VAL A  66     2554   1839   1269    685   -437   -243       C  
ATOM    596  N   VAL A  67       2.995  -4.504  43.852  1.00 11.14           N  
ANISOU  596  N   VAL A  67     1504   1660   1067    164    -23   -131       N  
ATOM    597  CA  VAL A  67       2.816  -3.299  43.060  1.00 12.08           C  
ANISOU  597  CA  VAL A  67     1725   1833   1032    147    125     67       C  
ATOM    598  C   VAL A  67       1.340  -3.291  42.576  1.00 11.81           C  
ANISOU  598  C   VAL A  67     1815   1806    865    314     88     17       C  
ATOM    599  O   VAL A  67       0.697  -4.335  42.558  1.00 13.86           O  
ANISOU  599  O   VAL A  67     1804   1968   1495    241   -223   -279       O  
ATOM    600  CB  VAL A  67       3.714  -3.314  41.825  1.00 14.39           C  
ANISOU  600  CB  VAL A  67     1911   2145   1412     94    409     10       C  
ATOM    601  CG1AVAL A  67       5.142  -2.927  42.177  0.66 17.35           C  
ANISOU  601  CG1AVAL A  67     1964   2575   2052   -311    524   -164       C  
ATOM    602  CG1BVAL A  67       3.220  -4.360  40.817  0.34 13.97           C  
ANISOU  602  CG1BVAL A  67     1471   2884    954    276    159    -60       C  
ATOM    603  CG2AVAL A  67       3.719  -4.645  41.078  0.66 13.35           C  
ANISOU  603  CG2AVAL A  67     1364   2464   1243    571     73   -244       C  
ATOM    604  CG2BVAL A  67       3.907  -1.982  41.135  0.34 19.10           C  
ANISOU  604  CG2BVAL A  67     3392   2751   1112   -127    248    552       C  
ATOM    605  N   LYS A  68       0.888  -2.079  42.217  1.00 13.42           N  
ANISOU  605  N   LYS A  68     2018   2065   1018    546    128    109       N  
ATOM    606  CA  LYS A  68      -0.351  -1.860  41.511  1.00 15.23           C  
ANISOU  606  CA  LYS A  68     1972   2824    989    878    267    243       C  
ATOM    607  C   LYS A  68      -0.108  -1.614  40.044  1.00 12.26           C  
ANISOU  607  C   LYS A  68     1598   2040   1018    375    304    113       C  
ATOM    608  O   LYS A  68       0.957  -1.128  39.666  1.00 12.33           O  
ANISOU  608  O   LYS A  68     1691   1896   1096    262    140    -18       O  
ATOM    609  CB  LYS A  68      -1.106  -0.616  42.121  1.00 20.96           C  
ANISOU  609  CB  LYS A  68     2849   4048   1068   1826    353     60       C  
ATOM    610  CG BLYS A  68      -1.554  -0.890  43.524  0.34 17.32           C  
ANISOU  610  CG BLYS A  68     2193   3339   1047   1469    168     15       C  
ATOM    611  CD BLYS A  68      -2.306   0.340  44.069  0.34 20.72           C  
ANISOU  611  CD BLYS A  68     3699   3216    958   1518    414   -132       C  
ATOM    612  CE BLYS A  68      -1.539   1.626  43.864  0.34 23.43           C  
ANISOU  612  CE BLYS A  68     3580   3459   1862   1275    484   -489       C  
ATOM    613  NZ BLYS A  68      -0.565   2.009  44.918  0.34 33.72           N  
ANISOU  613  NZ BLYS A  68     3692   4899   4220   1665   -479  -2026       N  
ATOM    614  N   ARG A  69      -1.083  -1.868  39.181  1.00 12.38           N  
ANISOU  614  N   ARG A  69     1634   2078    992    204    319    140       N  
ATOM    615  CA  ARG A  69      -0.869  -1.711  37.735  1.00 11.32           C  
ANISOU  615  CA  ARG A  69     1459   1841   1002     80    231    104       C  
ATOM    616  C   ARG A  69      -0.467  -0.311  37.392  1.00 10.99           C  
ANISOU  616  C   ARG A  69     1453   1765    958    206    212     -8       C  
ATOM    617  O   ARG A  69       0.396  -0.115  36.479  1.00 11.25           O  
ANISOU  617  O   ARG A  69     1348   1972    955    -83    244   -132       O  
ATOM    618  CB  ARG A  69      -2.162  -2.124  36.986  1.00 13.00           C  
ANISOU  618  CB  ARG A  69     1488   2269   1180   -108    171    111       C  
ATOM    619  CG  ARG A  69      -2.124  -1.815  35.456  1.00 12.98           C  
ANISOU  619  CG  ARG A  69     1422   2308   1202     35     90     -4       C  
ATOM    620  CD  ARG A  69      -1.088  -2.677  34.754  1.00 12.22           C  
ANISOU  620  CD  ARG A  69     1532   1929   1181   -216    208      2       C  
ATOM    621  NE  ARG A  69      -0.938  -2.351  33.347  1.00 11.08           N  
ANISOU  621  NE  ARG A  69     1404   1708   1097   -183     18     35       N  
ATOM    622  CZ  ARG A  69      -0.026  -1.526  32.839  1.00  9.66           C  
ANISOU  622  CZ  ARG A  69     1177   1548    944     19     40      1       C  
ATOM    623  NH1 ARG A  69       0.801  -0.842  33.636  1.00 10.43           N  
ANISOU  623  NH1 ARG A  69     1378   1605    979    -12     73    -56       N  
ATOM    624  NH2 ARG A  69       0.106  -1.375  31.516  1.00 10.09           N  
ANISOU  624  NH2 ARG A  69     1348   1585    901     84     41     10       N  
ATOM    625  N   GLU A  70      -1.057   0.694  38.023  1.00 11.87           N  
ANISOU  625  N   GLU A  70     1410   1905   1196    266    255     36       N  
ATOM    626  CA  GLU A  70      -0.778   2.095  37.667  1.00 13.27           C  
ANISOU  626  CA  GLU A  70     1726   1770   1547    324    181     65       C  
ATOM    627  C   GLU A  70       0.673   2.474  37.968  1.00 12.02           C  
ANISOU  627  C   GLU A  70     1751   1674   1143    256    332     -9       C  
ATOM    628  O   GLU A  70       1.098   3.476  37.396  1.00 15.53           O  
ANISOU  628  O   GLU A  70     2070   1886   1945    127    328    400       O  
ATOM    629  CB  GLU A  70      -1.774   2.973  38.372  1.00 17.81           C  
ANISOU  629  CB  GLU A  70     1875   2170   2723    638    447   -117       C  
ATOM    630  CG AGLU A  70      -1.713   2.922  39.879  0.64 26.77           C  
ANISOU  630  CG AGLU A  70     3733   3841   2598   1209    902   -866       C  
ATOM    631  CG BGLU A  70      -3.222   2.700  38.019  0.36 24.19           C  
ANISOU  631  CG BGLU A  70     1809   3035   4348    764     98    585       C  
ATOM    632  CD AGLU A  70      -2.938   2.121  40.343  0.64 34.70           C  
ANISOU  632  CD AGLU A  70     4854   5771   2559    397   1861   -445       C  
ATOM    633  CD BGLU A  70      -4.029   1.828  38.958  0.36 28.69           C  
ANISOU  633  CD BGLU A  70     1911   3872   5117    379    651    676       C  
ATOM    634  OE1AGLU A  70      -3.162   1.000  39.803  0.64 24.55           O  
ANISOU  634  OE1AGLU A  70     2256   4513   2561   1277    460    832       O  
ATOM    635  OE1BGLU A  70      -3.673   0.667  39.297  0.36 17.24           O  
ANISOU  635  OE1BGLU A  70     1421   3351   1780     70    665   -392       O  
ATOM    636  OE2AGLU A  70      -3.596   2.739  41.205  0.64 38.96           O  
ANISOU  636  OE2AGLU A  70     3486   7652   3665   1487   1112  -1325       O  
ATOM    637  OE2BGLU A  70      -5.103   2.347  39.367  0.36 36.51           O  
ANISOU  637  OE2BGLU A  70     2977   5529   5366   2088   1279   2499       O  
ATOM    638  N   GLU A  71       1.355   1.732  38.827  1.00 11.28           N  
ANISOU  638  N   GLU A  71     1586   1731    971    367    312   -171       N  
ATOM    639  CA  GLU A  71       2.758   2.037  39.128  1.00 11.69           C  
ANISOU  639  CA  GLU A  71     1767   1619   1056    281    192   -379       C  
ATOM    640  C   GLU A  71       3.717   1.440  38.102  1.00 10.06           C  
ANISOU  640  C   GLU A  71     1580   1345    895    100    199   -197       C  
ATOM    641  O   GLU A  71       4.912   1.796  38.108  1.00 13.24           O  
ANISOU  641  O   GLU A  71     1647   1633   1752    -31    337   -633       O  
ATOM    642  CB  GLU A  71       3.113   1.437  40.523  1.00 14.16           C  
ANISOU  642  CB  GLU A  71     2045   2452    883    252    132   -381       C  
ATOM    643  CG  GLU A  71       2.322   2.147  41.659  1.00 17.74           C  
ANISOU  643  CG  GLU A  71     2796   2756   1188    297    636   -324       C  
ATOM    644  CD  GLU A  71       2.502   1.426  42.977  1.00 24.23           C  
ANISOU  644  CD  GLU A  71     4567   3511   1127    916    737   -220       C  
ATOM    645  OE1 GLU A  71       2.644   0.187  43.111  1.00 20.24           O  
ANISOU  645  OE1 GLU A  71     2921   3195   1574   -435     43    151       O  
ATOM    646  OE2 GLU A  71       2.485   2.171  43.996  1.00 37.54           O  
ANISOU  646  OE2 GLU A  71     8867   3963   1434   -107    112   -575       O  
ATOM    647  N   LEU A  72       3.256   0.490  37.303  1.00  9.76           N  
ANISOU  647  N   LEU A  72     1493   1487    728     69    254   -211       N  
ATOM    648  CA  LEU A  72       4.152  -0.161  36.295  1.00  8.88           C  
ANISOU  648  CA  LEU A  72     1403   1232    739     38    284   -171       C  
ATOM    649  C   LEU A  72       4.038   0.597  34.998  1.00  8.14           C  
ANISOU  649  C   LEU A  72     1223   1105    766     83    147   -143       C  
ATOM    650  O   LEU A  72       3.031   1.204  34.644  1.00 10.44           O  
ANISOU  650  O   LEU A  72     1343   1663    961    312    227     32       O  
ATOM    651  CB  LEU A  72       3.687  -1.613  36.072  1.00 10.17           C  
ANISOU  651  CB  LEU A  72     1729   1232    905    -12    201    -56       C  
ATOM    652  CG  LEU A  72       3.901  -2.568  37.252  1.00 11.68           C  
ANISOU  652  CG  LEU A  72     1951   1365   1122     37    284     75       C  
ATOM    653  CD1 LEU A  72       3.312  -3.920  36.908  1.00 15.76           C  
ANISOU  653  CD1 LEU A  72     2881   1377   1730   -377    404    135       C  
ATOM    654  CD2 LEU A  72       5.381  -2.679  37.649  1.00 17.22           C  
ANISOU  654  CD2 LEU A  72     2117   1966   2460     48   -232    805       C  
ATOM    655  N   PHE A  73       5.151   0.506  34.222  1.00  7.87           N  
ANISOU  655  N   PHE A  73     1243   1104    642     31    156    -86       N  
ATOM    656  CA  PHE A  73       5.251   1.142  32.905  1.00  7.65           C  
ANISOU  656  CA  PHE A  73     1268    950    688     84    131   -101       C  
ATOM    657  C   PHE A  73       5.730   0.039  31.943  1.00  6.94           C  
ANISOU  657  C   PHE A  73     1106    870    661     48     87    -61       C  
ATOM    658  O   PHE A  73       6.907  -0.338  31.950  1.00  8.17           O  
ANISOU  658  O   PHE A  73     1071   1085    950     86     55   -221       O  
ATOM    659  CB  PHE A  73       6.211   2.315  32.956  1.00  8.15           C  
ANISOU  659  CB  PHE A  73     1367    884    846    -19     26    -94       C  
ATOM    660  CG  PHE A  73       6.058   3.223  31.751  1.00  7.97           C  
ANISOU  660  CG  PHE A  73     1254    931    844     -4    -38   -101       C  
ATOM    661  CD1 PHE A  73       6.675   2.919  30.526  1.00  9.14           C  
ANISOU  661  CD1 PHE A  73     1540   1098    834   -126     11   -125       C  
ATOM    662  CD2 PHE A  73       5.280   4.385  31.802  1.00  9.16           C  
ANISOU  662  CD2 PHE A  73     1260   1000   1221     89     46      4       C  
ATOM    663  CE1 PHE A  73       6.506   3.727  29.420  1.00  9.51           C  
ANISOU  663  CE1 PHE A  73     1731   1003    881   -106    -13    -20       C  
ATOM    664  CE2 PHE A  73       5.113   5.194  30.708  1.00 10.02           C  
ANISOU  664  CE2 PHE A  73     1383   1069   1353     88   -158    -28       C  
ATOM    665  CZ  PHE A  73       5.708   4.869  29.501  1.00 10.54           C  
ANISOU  665  CZ  PHE A  73     1704   1084   1216   -164    -71    -64       C  
ATOM    666  N   ILE A  74       4.780  -0.506  31.168  1.00  7.32           N  
ANISOU  666  N   ILE A  74     1152    986    643     36     60   -123       N  
ATOM    667  CA  ILE A  74       5.059  -1.674  30.331  1.00  7.40           C  
ANISOU  667  CA  ILE A  74     1202    909    700     13     88    -99       C  
ATOM    668  C   ILE A  74       5.082  -1.217  28.876  1.00  7.26           C  
ANISOU  668  C   ILE A  74     1090    970    697    105     18   -100       C  
ATOM    669  O   ILE A  74       4.142  -0.582  28.385  1.00  8.26           O  
ANISOU  669  O   ILE A  74     1083   1280    776    197     63    -37       O  
ATOM    670  CB  ILE A  74       4.037  -2.785  30.552  1.00  8.77           C  
ANISOU  670  CB  ILE A  74     1407   1014    912   -169    113    -85       C  
ATOM    671  CG1 ILE A  74       3.891  -3.126  32.055  1.00 10.30           C  
ANISOU  671  CG1 ILE A  74     1631   1364    920   -245    230    113       C  
ATOM    672  CG2 ILE A  74       4.440  -4.035  29.730  1.00 11.04           C  
ANISOU  672  CG2 ILE A  74     1859   1164   1174   -297    287   -325       C  
ATOM    673  CD1 ILE A  74       5.161  -3.582  32.726  1.00 11.86           C  
ANISOU  673  CD1 ILE A  74     2009   1444   1055     39     44    187       C  
ATOM    674  N   VAL A  75       6.209  -1.569  28.196  1.00  6.75           N  
ANISOU  674  N   VAL A  75     1047    954    564     86     52    -71       N  
ATOM    675  CA  VAL A  75       6.472  -1.184  26.817  1.00  6.79           C  
ANISOU  675  CA  VAL A  75     1136    856    588    157     15    -85       C  
ATOM    676  C   VAL A  75       6.510  -2.416  25.951  1.00  6.42           C  
ANISOU  676  C   VAL A  75     1025    818    594     54     49      3       C  
ATOM    677  O   VAL A  75       7.171  -3.398  26.309  1.00  7.77           O  
ANISOU  677  O   VAL A  75     1336    905    711    202    -62    -52       O  
ATOM    678  CB  VAL A  75       7.823  -0.443  26.724  1.00  7.31           C  
ANISOU  678  CB  VAL A  75     1072    981    725     68     62    -72       C  
ATOM    679  CG1 VAL A  75       8.065   0.037  25.267  1.00  9.10           C  
ANISOU  679  CG1 VAL A  75     1488   1157    813    -84    130     41       C  
ATOM    680  CG2 VAL A  75       7.883   0.722  27.699  1.00  9.11           C  
ANISOU  680  CG2 VAL A  75     1455   1001   1007     10   -112   -164       C  
ATOM    681  N   SER A  76       5.859  -2.388  24.776  1.00  6.32           N  
ANISOU  681  N   SER A  76      998    827    578     53     54    -23       N  
ATOM    682  CA  SER A  76       6.132  -3.423  23.772  1.00  6.36           C  
ANISOU  682  CA  SER A  76     1123    750    544     21     48    -26       C  
ATOM    683  C   SER A  76       6.219  -2.722  22.408  1.00  6.00           C  
ANISOU  683  C   SER A  76      916    754    612    -22     14    -11       C  
ATOM    684  O   SER A  76       6.185  -1.501  22.300  1.00  6.96           O  
ANISOU  684  O   SER A  76     1215    772    656     60     78      9       O  
ATOM    685  CB  SER A  76       5.114  -4.557  23.827  1.00  7.23           C  
ANISOU  685  CB  SER A  76     1175    732    840    -77    118    -34       C  
ATOM    686  OG  SER A  76       5.487  -5.602  22.938  1.00  8.18           O  
ANISOU  686  OG  SER A  76     1444    820    844    -90    169   -101       O  
ATOM    687  N   LYS A  77       6.397  -3.569  21.368  1.00  6.69           N  
ANISOU  687  N   LYS A  77     1180    819    542    -11     37    -49       N  
ATOM    688  CA  LYS A  77       6.770  -3.057  20.046  1.00  6.41           C  
ANISOU  688  CA  LYS A  77     1056    823    556    -33     24    -23       C  
ATOM    689  C   LYS A  77       6.123  -3.903  18.968  1.00  6.36           C  
ANISOU  689  C   LYS A  77      954    831    634     60      8    -94       C  
ATOM    690  O   LYS A  77       6.046  -5.133  19.065  1.00  7.66           O  
ANISOU  690  O   LYS A  77     1298    785    827    -29    -46    -69       O  
ATOM    691  CB  LYS A  77       8.306  -3.086  19.839  1.00  7.33           C  
ANISOU  691  CB  LYS A  77     1097   1013    675    -83    -40   -107       C  
ATOM    692  CG  LYS A  77       9.112  -2.629  21.080  1.00  7.09           C  
ANISOU  692  CG  LYS A  77     1101    924    667   -133     -2    -33       C  
ATOM    693  CD  LYS A  77      10.594  -2.482  20.799  1.00  7.78           C  
ANISOU  693  CD  LYS A  77     1092   1132    733   -178    -66     29       C  
ATOM    694  CE  LYS A  77      11.405  -2.288  22.077  1.00  7.56           C  
ANISOU  694  CE  LYS A  77     1211    912    749    -94   -118     58       C  
ATOM    695  NZ  LYS A  77      11.580  -3.560  22.844  1.00  6.87           N  
ANISOU  695  NZ  LYS A  77     1050    870    692    -17      0     25       N  
ATOM    696  N   LEU A  78       5.694  -3.205  17.915  1.00  6.99           N  
ANISOU  696  N   LEU A  78     1233    839    585      2    -48    -89       N  
ATOM    697  CA  LEU A  78       5.051  -3.776  16.714  1.00  6.86           C  
ANISOU  697  CA  LEU A  78     1150    882    575      2    -65   -120       C  
ATOM    698  C   LEU A  78       6.132  -4.309  15.773  1.00  6.54           C  
ANISOU  698  C   LEU A  78     1055    799    630    -98    -62    -80       C  
ATOM    699  O   LEU A  78       6.963  -3.531  15.310  1.00  7.56           O  
ANISOU  699  O   LEU A  78     1138    990    744    -85     45    -89       O  
ATOM    700  CB  LEU A  78       4.295  -2.616  16.008  1.00  7.95           C  
ANISOU  700  CB  LEU A  78     1320    897    802    101   -144   -101       C  
ATOM    701  CG  LEU A  78       3.594  -3.031  14.698  1.00  8.27           C  
ANISOU  701  CG  LEU A  78     1276   1077    790     59   -214    -77       C  
ATOM    702  CD1 LEU A  78       2.304  -3.782  14.978  1.00 10.94           C  
ANISOU  702  CD1 LEU A  78     1289   1574   1295   -138   -198   -198       C  
ATOM    703  CD2 LEU A  78       3.360  -1.769  13.847  1.00 11.53           C  
ANISOU  703  CD2 LEU A  78     1962   1350   1070    111   -427    146       C  
ATOM    704  N   TRP A  79       6.120  -5.613  15.486  1.00  7.25           N  
ANISOU  704  N   TRP A  79     1204    903    649     64    -21   -147       N  
ATOM    705  CA  TRP A  79       7.152  -6.172  14.617  1.00  7.91           C  
ANISOU  705  CA  TRP A  79     1429    958    617    222     35   -123       C  
ATOM    706  C   TRP A  79       6.909  -5.791  13.148  1.00  7.40           C  
ANISOU  706  C   TRP A  79     1320    861    631     99    -38   -109       C  
ATOM    707  O   TRP A  79       5.834  -5.375  12.704  1.00  8.38           O  
ANISOU  707  O   TRP A  79     1364   1099    718    113    -57    -78       O  
ATOM    708  CB  TRP A  79       7.235  -7.739  14.858  1.00  8.26           C  
ANISOU  708  CB  TRP A  79     1387    845    907    118     22    -66       C  
ATOM    709  CG  TRP A  79       8.410  -8.253  14.066  1.00  8.04           C  
ANISOU  709  CG  TRP A  79     1443    867    742     89    -69    -79       C  
ATOM    710  CD1 TRP A  79       8.356  -9.109  13.010  1.00  8.92           C  
ANISOU  710  CD1 TRP A  79     1610    924    853    179    -39    -55       C  
ATOM    711  CD2 TRP A  79       9.780  -7.861  14.191  1.00  7.96           C  
ANISOU  711  CD2 TRP A  79     1441    901    684    184    -11      4       C  
ATOM    712  NE1 TRP A  79       9.612  -9.300  12.463  1.00  9.38           N  
ANISOU  712  NE1 TRP A  79     1706    982    878    258    -96   -118       N  
ATOM    713  CE2 TRP A  79      10.507  -8.535  13.180  1.00  8.97           C  
ANISOU  713  CE2 TRP A  79     1559   1069    780    213    -28     -5       C  
ATOM    714  CE3 TRP A  79      10.480  -6.998  15.074  1.00  8.28           C  
ANISOU  714  CE3 TRP A  79     1413   1007    725    -29    -69    105       C  
ATOM    715  CZ2 TRP A  79      11.903  -8.384  13.001  1.00 10.16           C  
ANISOU  715  CZ2 TRP A  79     1533   1407    922    286    107    165       C  
ATOM    716  CZ3 TRP A  79      11.850  -6.837  14.915  1.00  9.36           C  
ANISOU  716  CZ3 TRP A  79     1378   1193    987     36     40    254       C  
ATOM    717  CH2 TRP A  79      12.544  -7.541  13.892  1.00 10.44           C  
ANISOU  717  CH2 TRP A  79     1505   1358   1102     88    114    286       C  
ATOM    718  N   CYS A  80       7.992  -5.932  12.355  1.00  7.48           N  
ANISOU  718  N   CYS A  80     1270    963    608     53     32    -31       N  
ATOM    719  CA  CYS A  80       8.069  -5.467  10.988  1.00  7.83           C  
ANISOU  719  CA  CYS A  80     1342   1053    582    113    -33   -103       C  
ATOM    720  C   CYS A  80       7.067  -6.142  10.040  1.00  7.72           C  
ANISOU  720  C   CYS A  80     1299   1044    590     95     -1    -85       C  
ATOM    721  O   CYS A  80       6.729  -5.547   9.018  1.00  8.91           O  
ANISOU  721  O   CYS A  80     1521   1157    709     67   -131    -76       O  
ATOM    722  CB  CYS A  80       9.500  -5.725  10.453  1.00  8.50           C  
ANISOU  722  CB  CYS A  80     1336   1164    729    -28     78   -128       C  
ATOM    723  SG  CYS A  80      10.755  -4.806  11.388  1.00  9.14           S  
ANISOU  723  SG  CYS A  80     1386   1210    876      1     -8    -48       S  
ATOM    724  N   THR A  81       6.644  -7.378  10.328  1.00  8.33           N  
ANISOU  724  N   THR A  81     1407    940    819     79    -93   -190       N  
ATOM    725  CA  THR A  81       5.684  -8.097   9.477  1.00  8.78           C  
ANISOU  725  CA  THR A  81     1460    973    902    109   -119   -281       C  
ATOM    726  C   THR A  81       4.255  -7.697   9.741  1.00  9.32           C  
ANISOU  726  C   THR A  81     1440   1099   1001     30   -108   -237       C  
ATOM    727  O   THR A  81       3.334  -8.260   9.095  1.00 12.07           O  
ANISOU  727  O   THR A  81     1514   1581   1489    137   -318   -711       O  
ATOM    728  CB  THR A  81       5.867  -9.610   9.690  1.00  9.53           C  
ANISOU  728  CB  THR A  81     1610   1054    957    101   -185   -169       C  
ATOM    729  OG1 THR A  81       5.769  -9.831  11.089  1.00 10.96           O  
ANISOU  729  OG1 THR A  81     1965   1239    960   -108   -153   -100       O  
ATOM    730  CG2 THR A  81       7.224 -10.100   9.186  1.00 10.97           C  
ANISOU  730  CG2 THR A  81     1751   1214   1201    348   -198   -266       C  
ATOM    731  N   TYR A  82       4.011  -6.703  10.592  1.00  9.02           N  
ANISOU  731  N   TYR A  82     1371   1163    892    101    -78   -296       N  
ATOM    732  CA  TYR A  82       2.657  -6.233  10.903  1.00  9.72           C  
ANISOU  732  CA  TYR A  82     1363   1311   1019    131    -27   -179       C  
ATOM    733  C   TYR A  82       2.473  -4.740  10.626  1.00  9.53           C  
ANISOU  733  C   TYR A  82     1399   1244    980    114   -129   -195       C  
ATOM    734  O   TYR A  82       1.649  -4.088  11.255  1.00 11.45           O  
ANISOU  734  O   TYR A  82     1643   1486   1223    378     91   -119       O  
ATOM    735  CB ATYR A  82       2.322  -6.553  12.377  0.56 10.27           C  
ANISOU  735  CB ATYR A  82     1518   1400    985   -210    -16   -113       C  
ATOM    736  CB BTYR A  82       2.379  -6.484  12.409  0.44 11.44           C  
ANISOU  736  CB BTYR A  82     1941   1348   1059    317    228    -75       C  
ATOM    737  CG ATYR A  82       2.575  -7.960  12.840  0.56 10.66           C  
ANISOU  737  CG ATYR A  82     1540   1436   1074   -167    207    -70       C  
ATOM    738  CG BTYR A  82       2.372  -7.952  12.769  0.44 12.43           C  
ANISOU  738  CG BTYR A  82     1963   1471   1288     85   -142    105       C  
ATOM    739  CD1ATYR A  82       1.775  -9.047  12.460  0.56 14.77           C  
ANISOU  739  CD1ATYR A  82     2146   1326   2141   -132   -444   -146       C  
ATOM    740  CD1BTYR A  82       1.218  -8.712  12.539  0.44 15.31           C  
ANISOU  740  CD1BTYR A  82     1944   1506   2369     72   -209     92       C  
ATOM    741  CD2ATYR A  82       3.628  -8.205  13.725  0.56 14.26           C  
ANISOU  741  CD2ATYR A  82     2270   1542   1608   -268   -430    235       C  
ATOM    742  CD2BTYR A  82       3.476  -8.573  13.339  0.44 13.01           C  
ANISOU  742  CD2BTYR A  82     1983   1526   1433     68   -131    280       C  
ATOM    743  CE1ATYR A  82       2.053 -10.346  12.929  0.56 15.07           C  
ANISOU  743  CE1ATYR A  82     2525   1362   1839   -280   -466   -137       C  
ATOM    744  CE1BTYR A  82       1.178 -10.052  12.861  0.44 17.33           C  
ANISOU  744  CE1BTYR A  82     2282   1921   2383   -386   -388    774       C  
ATOM    745  CE2ATYR A  82       3.869  -9.494  14.180  0.56 14.81           C  
ANISOU  745  CE2ATYR A  82     2214   1665   1749   -370   -431    296       C  
ATOM    746  CE2BTYR A  82       3.463  -9.933  13.679  0.44 14.75           C  
ANISOU  746  CE2BTYR A  82     2353   1611   1641     38   -345    380       C  
ATOM    747  CZ ATYR A  82       3.089 -10.567  13.802  0.56 13.79           C  
ANISOU  747  CZ ATYR A  82     2245   1313   1680     19    -75   -116       C  
ATOM    748  CZ BTYR A  82       2.300 -10.643  13.419  0.44 15.47           C  
ANISOU  748  CZ BTYR A  82     2236   1578   2064    -37    -30    457       C  
ATOM    749  OH ATYR A  82       3.378 -11.816  14.281  0.56 17.02           O  
ANISOU  749  OH ATYR A  82     2942   1542   1982   -126   -304    242       O  
ATOM    750  OH BTYR A  82       2.212 -11.969  13.732  0.44 18.76           O  
ANISOU  750  OH BTYR A  82     3133   1642   2351   -213   -157    504       O  
ATOM    751  N   HIS A  83       3.235  -4.178   9.664  1.00  9.74           N  
ANISOU  751  N   HIS A  83     1476   1137   1087    127    -90   -201       N  
ATOM    752  CA  HIS A  83       3.085  -2.746   9.349  1.00  9.75           C  
ANISOU  752  CA  HIS A  83     1538   1206    962    136   -207    -84       C  
ATOM    753  C   HIS A  83       1.809  -2.406   8.588  1.00 11.11           C  
ANISOU  753  C   HIS A  83     1702   1293   1226    162   -345   -156       C  
ATOM    754  O   HIS A  83       1.398  -1.255   8.592  1.00 13.58           O  
ANISOU  754  O   HIS A  83     1903   1529   1729    416   -652   -290       O  
ATOM    755  CB  HIS A  83       4.301  -2.176   8.630  1.00 10.12           C  
ANISOU  755  CB  HIS A  83     1682   1271    893     93   -188   -157       C  
ATOM    756  CG  HIS A  83       5.474  -1.909   9.521  1.00  8.93           C  
ANISOU  756  CG  HIS A  83     1565   1026    801    186   -112   -112       C  
ATOM    757  ND1 HIS A  83       6.401  -0.940   9.176  1.00  9.61           N  
ANISOU  757  ND1 HIS A  83     1471   1153   1026    174   -120    -49       N  
ATOM    758  CD2 HIS A  83       5.891  -2.456  10.698  1.00  9.55           C  
ANISOU  758  CD2 HIS A  83     1559   1208    860    168   -207   -149       C  
ATOM    759  CE1 HIS A  83       7.353  -0.888  10.097  1.00 10.16           C  
ANISOU  759  CE1 HIS A  83     1556   1263   1043    164   -176   -133       C  
ATOM    760  NE2 HIS A  83       7.052  -1.794  11.034  1.00  9.82           N  
ANISOU  760  NE2 HIS A  83     1540   1221    972    267   -118   -167       N  
ATOM    761  N   GLU A  84       1.204  -3.373   7.898  1.00 12.33           N  
ANISOU  761  N   GLU A  84     1587   1809   1288     60   -369   -347       N  
ATOM    762  CA  GLU A  84      -0.039  -3.072   7.144  1.00 13.00           C  
ANISOU  762  CA  GLU A  84     1568   2079   1291    224   -347   -256       C  
ATOM    763  C   GLU A  84      -1.106  -2.581   8.111  1.00 12.80           C  
ANISOU  763  C   GLU A  84     1703   2005   1155    292   -328   -157       C  
ATOM    764  O   GLU A  84      -1.254  -3.121   9.220  1.00 13.87           O  
ANISOU  764  O   GLU A  84     1723   2362   1186    288   -409      3       O  
ATOM    765  CB  GLU A  84      -0.608  -4.317   6.481  1.00 17.90           C  
ANISOU  765  CB  GLU A  84     2081   2936   1785     14   -542  -1156       C  
ATOM    766  CG  GLU A  84       0.157  -4.599   5.196  1.00 26.69           C  
ANISOU  766  CG  GLU A  84     2517   4067   3557   -475    461  -2477       C  
ATOM    767  CD  GLU A  84       1.499  -5.276   5.410  1.00 27.90           C  
ANISOU  767  CD  GLU A  84     3872   3371   3355    743    686  -1971       C  
ATOM    768  OE1 GLU A  84       1.889  -5.602   6.577  1.00 27.59           O  
ANISOU  768  OE1 GLU A  84     3338   3893   3253   -816    485  -1595       O  
ATOM    769  OE2 GLU A  84       2.069  -5.472   4.301  1.00 27.95           O  
ANISOU  769  OE2 GLU A  84     3737   3357   3527    717   1395    -53       O  
ATOM    770  N  ALYS A  85      -1.861  -1.562   7.699  0.40 13.57           N  
ANISOU  770  N  ALYS A  85     1726   2273   1156    521   -496   -140       N  
ATOM    771  N  BLYS A  85      -1.858  -1.568   7.693  0.40 13.47           N  
ANISOU  771  N  BLYS A  85     1812   2189   1117    512   -459   -172       N  
ATOM    772  CA ALYS A  85      -2.761  -0.937   8.663  0.40 15.37           C  
ANISOU  772  CA ALYS A  85     1990   2273   1578    644   -218    -26       C  
ATOM    773  CA BLYS A  85      -2.816  -0.933   8.584  0.40 14.62           C  
ANISOU  773  CA BLYS A  85     1742   2442   1373    641   -399    -36       C  
ATOM    774  C   LYS A  85      -3.758  -1.927   9.248  1.00 17.02           C  
ANISOU  774  C   LYS A  85     2162   2803   1501    400   -130    -62       C  
ATOM    775  O   LYS A  85      -4.051  -1.772  10.441  1.00 21.25           O  
ANISOU  775  O   LYS A  85     2839   3581   1653    396    391   -314       O  
ATOM    776  CB ALYS A  85      -3.423   0.248   7.960  0.40 18.12           C  
ANISOU  776  CB ALYS A  85     2709   2509   1669   1066   -361    -58       C  
ATOM    777  CB BLYS A  85      -3.546   0.119   7.731  0.40 20.35           C  
ANISOU  777  CB BLYS A  85     2685   2722   2326   1210   -408    369       C  
ATOM    778  CG ALYS A  85      -4.198  -0.125   6.710  0.40 26.65           C  
ANISOU  778  CG ALYS A  85     4040   3554   2533   1345  -1575   -274       C  
ATOM    779  CG BLYS A  85      -2.825   1.467   7.721  0.40 23.09           C  
ANISOU  779  CG BLYS A  85     3243   2573   2958   1145   -810    379       C  
ATOM    780  CD ALYS A  85      -4.644   1.158   5.982  0.60 37.22           C  
ANISOU  780  CD ALYS A  85     5953   4593   3598    867  -2412   1148       C  
ATOM    781  CD BLYS A  85      -3.574   2.481   8.582  0.40 31.55           C  
ANISOU  781  CD BLYS A  85     4186   3546   4254   1125   -889  -1087       C  
ATOM    782  CE ALYS A  85      -3.626   2.248   6.286  0.60 42.25           C  
ANISOU  782  CE ALYS A  85     6743   4221   5088    359   -995    823       C  
ATOM    783  CE BLYS A  85      -3.533   3.899   8.066  0.40 24.95           C  
ANISOU  783  CE BLYS A  85     2403   2772   4306    295  -1078  -2201       C  
ATOM    784  NZ ALYS A  85      -4.002   3.140   7.422  0.60 40.01           N  
ANISOU  784  NZ ALYS A  85     5915   3828   5457    637  -1279    755       N  
ATOM    785  NZ BLYS A  85      -4.762   4.274   7.285  0.40 32.94           N  
ANISOU  785  NZ BLYS A  85     3617   3519   5381    359  -1987   -889       N  
ATOM    786  N   GLY A  86      -4.228  -2.940   8.489  1.00 16.50           N  
ANISOU  786  N   GLY A  86     1638   2860   1769    384   -558     35       N  
ATOM    787  CA  GLY A  86      -5.214  -3.905   9.009  1.00 18.71           C  
ANISOU  787  CA  GLY A  86     1734   3462   1913    142   -541    117       C  
ATOM    788  C   GLY A  86      -4.624  -4.941   9.926  1.00 16.31           C  
ANISOU  788  C   GLY A  86     1685   2799   1712    -15   -438   -194       C  
ATOM    789  O   GLY A  86      -5.392  -5.667  10.550  1.00 21.31           O  
ANISOU  789  O   GLY A  86     1849   3795   2454   -396   -475    403       O  
ATOM    790  N   LEU A  87      -3.288  -4.997  10.092  1.00 13.61           N  
ANISOU  790  N   LEU A  87     1599   2311   1260     65   -355   -300       N  
ATOM    791  CA  LEU A  87      -2.660  -5.989  10.972  1.00 13.34           C  
ANISOU  791  CA  LEU A  87     1736   1919   1413    118   -294   -477       C  
ATOM    792  C   LEU A  87      -2.232  -5.400  12.302  1.00 12.09           C  
ANISOU  792  C   LEU A  87     1708   1625   1261    -14   -253   -246       C  
ATOM    793  O   LEU A  87      -1.889  -6.181  13.234  1.00 12.97           O  
ANISOU  793  O   LEU A  87     1916   1598   1413     67   -245   -267       O  
ATOM    794  CB  LEU A  87      -1.407  -6.585  10.282  1.00 14.58           C  
ANISOU  794  CB  LEU A  87     1759   2220   1560     89   -157   -651       C  
ATOM    795  CG  LEU A  87      -1.755  -7.360   8.980  1.00 16.49           C  
ANISOU  795  CG  LEU A  87     1946   2492   1829     43   -275  -1033       C  
ATOM    796  CD1 LEU A  87      -0.459  -7.968   8.429  1.00 20.32           C  
ANISOU  796  CD1 LEU A  87     2567   3391   1763    407    100  -1112       C  
ATOM    797  CD2 LEU A  87      -2.754  -8.471   9.220  1.00 22.50           C  
ANISOU  797  CD2 LEU A  87     2978   2974   2596   -690     72  -1338       C  
ATOM    798  N   VAL A  88      -2.199  -4.082  12.469  1.00 11.65           N  
ANISOU  798  N   VAL A  88     1574   1653   1197     89   -254   -257       N  
ATOM    799  CA  VAL A  88      -1.572  -3.468  13.655  1.00 10.67           C  
ANISOU  799  CA  VAL A  88     1547   1420   1087     81   -135   -183       C  
ATOM    800  C   VAL A  88      -2.383  -3.822  14.899  1.00 11.04           C  
ANISOU  800  C   VAL A  88     1499   1507   1190     92   -243     -2       C  
ATOM    801  O   VAL A  88      -1.812  -4.173  15.949  1.00 11.58           O  
ANISOU  801  O   VAL A  88     1581   1575   1244    130   -258     69       O  
ATOM    802  CB  VAL A  88      -1.470  -1.939  13.405  1.00 10.90           C  
ANISOU  802  CB  VAL A  88     1397   1465   1278     79   -150    -86       C  
ATOM    803  CG1 VAL A  88      -1.171  -1.221  14.719  1.00 12.87           C  
ANISOU  803  CG1 VAL A  88     2104   1504   1282    125    -96   -266       C  
ATOM    804  CG2 VAL A  88      -0.452  -1.645  12.337  1.00 12.25           C  
ANISOU  804  CG2 VAL A  88     1607   1748   1300    315     87     98       C  
ATOM    805  N   LYS A  89      -3.727  -3.664  14.849  1.00 11.63           N  
ANISOU  805  N   LYS A  89     1433   1598   1389    109   -121    -89       N  
ATOM    806  CA  LYS A  89      -4.522  -3.947  16.069  1.00 12.10           C  
ANISOU  806  CA  LYS A  89     1485   1705   1406    196   -202    -56       C  
ATOM    807  C   LYS A  89      -4.368  -5.359  16.539  1.00 11.33           C  
ANISOU  807  C   LYS A  89     1467   1599   1240    -68   -195   -127       C  
ATOM    808  O   LYS A  89      -4.201  -5.628  17.740  1.00 12.36           O  
ANISOU  808  O   LYS A  89     1631   1837   1228     14   -190    -75       O  
ATOM    809  CB  LYS A  89      -5.992  -3.556  15.805  1.00 14.67           C  
ANISOU  809  CB  LYS A  89     1344   2420   1810    310    -77    -48       C  
ATOM    810  CG  LYS A  89      -6.830  -3.709  17.087  1.00 17.09           C  
ANISOU  810  CG  LYS A  89     1617   3107   1769    416    -38    107       C  
ATOM    811  CD  LYS A  89      -8.266  -3.237  16.875  1.00 22.92           C  
ANISOU  811  CD  LYS A  89     1648   3524   3536    716    389    -56       C  
ATOM    812  CE  LYS A  89      -9.128  -3.527  18.106  1.00 27.32           C  
ANISOU  812  CE  LYS A  89     1933   4150   4295    467    792    247       C  
ATOM    813  NZ  LYS A  89     -10.585  -3.369  17.761  1.00 48.28           N  
ANISOU  813  NZ  LYS A  89     1653  10570   6122    648    839   -867       N  
ATOM    814  N   GLY A  90      -4.407  -6.349  15.628  1.00 11.99           N  
ANISOU  814  N   GLY A  90     1532   1634   1388    -73   -252   -189       N  
ATOM    815  CA  GLY A  90      -4.273  -7.738  16.062  1.00 12.58           C  
ANISOU  815  CA  GLY A  90     1641   1585   1553   -193   -372   -107       C  
ATOM    816  C   GLY A  90      -2.900  -8.038  16.631  1.00 10.89           C  
ANISOU  816  C   GLY A  90     1528   1312   1298   -125   -142   -219       C  
ATOM    817  O   GLY A  90      -2.796  -8.828  17.575  1.00 12.24           O  
ANISOU  817  O   GLY A  90     1633   1559   1459   -205   -168    -26       O  
ATOM    818  N   ALA A  91      -1.843  -7.406  16.123  1.00 10.70           N  
ANISOU  818  N   ALA A  91     1427   1349   1291    -46   -157   -178       N  
ATOM    819  CA  ALA A  91      -0.494  -7.587  16.721  1.00 10.52           C  
ANISOU  819  CA  ALA A  91     1380   1433   1185    -44   -107    -64       C  
ATOM    820  C   ALA A  91      -0.487  -7.033  18.128  1.00  9.30           C  
ANISOU  820  C   ALA A  91     1124   1231   1176     34    -89    -92       C  
ATOM    821  O   ALA A  91       0.071  -7.659  19.054  1.00 10.75           O  
ANISOU  821  O   ALA A  91     1532   1249   1303      4   -123     49       O  
ATOM    822  CB  ALA A  91       0.515  -6.846  15.842  1.00 12.42           C  
ANISOU  822  CB  ALA A  91     1495   1852   1372    -53    169    -16       C  
ATOM    823  N   CYS A  92      -1.080  -5.871  18.352  1.00  9.81           N  
ANISOU  823  N   CYS A  92     1269   1276   1181     -1   -100   -106       N  
ATOM    824  CA  CYS A  92      -1.151  -5.285  19.705  1.00  9.35           C  
ANISOU  824  CA  CYS A  92     1387   1156   1011    -79    -93    -37       C  
ATOM    825  C   CYS A  92      -1.948  -6.205  20.627  1.00  9.73           C  
ANISOU  825  C   CYS A  92     1359   1134   1206    -51   -172    -11       C  
ATOM    826  O   CYS A  92      -1.558  -6.447  21.788  1.00 10.55           O  
ANISOU  826  O   CYS A  92     1592   1222   1195   -170   -147    126       O  
ATOM    827  CB  CYS A  92      -1.723  -3.906  19.607  1.00 10.38           C  
ANISOU  827  CB  CYS A  92     1665   1113   1167    113   -142    -47       C  
ATOM    828  SG  CYS A  92      -1.732  -3.009  21.198  1.00 13.35           S  
ANISOU  828  SG  CYS A  92     2397   1356   1321    114    -49   -197       S  
ATOM    829  N  AGLN A  93      -3.072  -6.699  20.108  0.49 10.40           N  
ANISOU  829  N  AGLN A  93     1187   1321   1444   -135    -67     69       N  
ATOM    830  N  BGLN A  93      -3.088  -6.699  20.161  0.51 10.32           N  
ANISOU  830  N  BGLN A  93     1331   1367   1224   -226     30   -149       N  
ATOM    831  CA AGLN A  93      -3.949  -7.569  20.913  0.49 10.94           C  
ANISOU  831  CA AGLN A  93     1448   1422   1288   -274     18    -31       C  
ATOM    832  CA BGLN A  93      -3.904  -7.552  21.055  0.51 10.55           C  
ANISOU  832  CA BGLN A  93     1370   1335   1304   -267   -214    113       C  
ATOM    833  C  AGLN A  93      -3.242  -8.855  21.320  0.49 10.74           C  
ANISOU  833  C  AGLN A  93     1235   1364   1483   -453     74     51       C  
ATOM    834  C  BGLN A  93      -3.193  -8.859  21.374  0.51 11.03           C  
ANISOU  834  C  BGLN A  93     1628   1370   1193   -150   -340   -157       C  
ATOM    835  O  AGLN A  93      -3.501  -9.326  22.447  0.49 13.94           O  
ANISOU  835  O  AGLN A  93     1946   2008   1344   -197     -8    260       O  
ATOM    836  O  BGLN A  93      -3.373  -9.397  22.487  0.51 10.31           O  
ANISOU  836  O  BGLN A  93     1117   1273   1529   -192    -58    112       O  
ATOM    837  CB AGLN A  93      -5.248  -7.865  20.139  0.49 13.09           C  
ANISOU  837  CB AGLN A  93     1444   1679   1850   -466   -125    214       C  
ATOM    838  CB BGLN A  93      -5.276  -7.775  20.407  0.51 13.23           C  
ANISOU  838  CB BGLN A  93     1222   1961   1844   -230   -133     94       C  
ATOM    839  CG AGLN A  93      -6.226  -6.673  20.186  0.49 16.39           C  
ANISOU  839  CG AGLN A  93     1684   2103   2443    -61    -94    552       C  
ATOM    840  CG BGLN A  93      -6.044  -6.433  20.269  0.51 21.14           C  
ANISOU  840  CG BGLN A  93     2187   3013   2831   1031   -329     12       C  
ATOM    841  CD AGLN A  93      -7.466  -6.880  19.354  0.49 20.34           C  
ANISOU  841  CD AGLN A  93     2111   2488   3131   -293   -700   1178       C  
ATOM    842  CD BGLN A  93      -7.527  -6.709  20.227  0.51 24.03           C  
ANISOU  842  CD BGLN A  93     2240   2926   3964    886   -504    260       C  
ATOM    843  OE1AGLN A  93      -8.609  -6.561  19.724  0.49 29.24           O  
ANISOU  843  OE1AGLN A  93     2253   4849   4006    710  -1354     53       O  
ATOM    844  OE1BGLN A  93      -8.359  -6.151  20.957  0.51 26.01           O  
ANISOU  844  OE1BGLN A  93     2043   4273   3567    861   -412    322       O  
ATOM    845  NE2AGLN A  93      -7.299  -7.477  18.189  0.49 26.75           N  
ANISOU  845  NE2AGLN A  93     1962   5323   2878   -282  -1061    623       N  
ATOM    846  NE2BGLN A  93      -7.874  -7.610  19.306  0.51 29.76           N  
ANISOU  846  NE2BGLN A  93     2835   5041   3432    336   -806   -254       N  
ATOM    847  N   LYS A  94      -2.406  -9.412  20.433  1.00 11.17           N  
ANISOU  847  N   LYS A  94     1386   1326   1532   -248   -124    -91       N  
ATOM    848  CA  LYS A  94      -1.642 -10.659  20.815  1.00 11.31           C  
ANISOU  848  CA  LYS A  94     1594   1227   1476   -297   -121   -103       C  
ATOM    849  C   LYS A  94      -0.683 -10.328  21.954  1.00  9.89           C  
ANISOU  849  C   LYS A  94     1472    942   1343   -217    -10    -83       C  
ATOM    850  O   LYS A  94      -0.540 -11.106  22.907  1.00 10.83           O  
ANISOU  850  O   LYS A  94     1678    981   1454   -213     40     29       O  
ATOM    851  CB  LYS A  94      -0.934 -11.212  19.574  1.00 13.27           C  
ANISOU  851  CB  LYS A  94     2093   1423   1525    -20   -155   -398       C  
ATOM    852  CG  LYS A  94       0.057 -12.364  19.839  1.00 14.89           C  
ANISOU  852  CG  LYS A  94     2382   1357   1917     41    -27   -234       C  
ATOM    853  CD  LYS A  94      -0.522 -13.557  20.579  1.00 18.73           C  
ANISOU  853  CD  LYS A  94     3259   1454   2403   -224    351   -243       C  
ATOM    854  CE  LYS A  94       0.432 -14.740  20.584  1.00 22.46           C  
ANISOU  854  CE  LYS A  94     4789   1376   2369    389    176   -171       C  
ATOM    855  NZ  LYS A  94       0.114 -15.753  21.602  1.00 25.07           N  
ANISOU  855  NZ  LYS A  94     5503   1607   2415   -317    -52   -241       N  
ATOM    856  N   THR A  95       0.063  -9.229  21.847  1.00  9.68           N  
ANISOU  856  N   THR A  95     1361   1005   1312   -244    -46    -54       N  
ATOM    857  CA  THR A  95       0.947  -8.826  22.943  1.00  9.00           C  
ANISOU  857  CA  THR A  95     1285   1019   1116   -239     30     26       C  
ATOM    858  C   THR A  95       0.161  -8.603  24.236  1.00  9.27           C  
ANISOU  858  C   THR A  95     1280   1087   1156   -189     -6     21       C  
ATOM    859  O   THR A  95       0.620  -9.036  25.305  1.00 10.00           O  
ANISOU  859  O   THR A  95     1401   1192   1207   -163    -69    233       O  
ATOM    860  CB  THR A  95       1.752  -7.552  22.484  1.00  9.35           C  
ANISOU  860  CB  THR A  95     1273   1000   1282   -192    138    -29       C  
ATOM    861  OG1 THR A  95       2.821  -7.985  21.663  1.00  9.51           O  
ANISOU  861  OG1 THR A  95     1316   1179   1117    -98     36    137       O  
ATOM    862  CG2 THR A  95       2.273  -6.753  23.672  1.00 10.62           C  
ANISOU  862  CG2 THR A  95     1278   1148   1608   -191     99   -236       C  
ATOM    863  N   LEU A  96      -0.991  -7.911  24.189  1.00  9.26           N  
ANISOU  863  N   LEU A  96     1245   1083   1190    -62    -25     42       N  
ATOM    864  CA  LEU A  96      -1.793  -7.735  25.408  1.00  9.83           C  
ANISOU  864  CA  LEU A  96     1286   1235   1215   -116     24     34       C  
ATOM    865  C   LEU A  96      -2.204  -9.076  26.003  1.00 10.07           C  
ANISOU  865  C   LEU A  96     1233   1308   1287    -25     27    159       C  
ATOM    866  O   LEU A  96      -2.193  -9.244  27.257  1.00 11.70           O  
ANISOU  866  O   LEU A  96     1615   1535   1294     49    132    170       O  
ATOM    867  CB  LEU A  96      -3.027  -6.879  25.134  1.00 10.29           C  
ANISOU  867  CB  LEU A  96     1338   1259   1313    -16    -56     68       C  
ATOM    868  CG  LEU A  96      -2.734  -5.377  24.913  1.00 11.72           C  
ANISOU  868  CG  LEU A  96     1758   1261   1435     43    126    110       C  
ATOM    869  CD1 LEU A  96      -4.007  -4.688  24.420  1.00 15.72           C  
ANISOU  869  CD1 LEU A  96     2450   1456   2067    522   -176     50       C  
ATOM    870  CD2 LEU A  96      -2.257  -4.749  26.213  1.00 15.24           C  
ANISOU  870  CD2 LEU A  96     2398   1535   1858   -374    -20   -213       C  
ATOM    871  N   SER A  97      -2.609 -10.010  25.170  1.00 10.68           N  
ANISOU  871  N   SER A  97     1287   1254   1518   -198     36     96       N  
ATOM    872  CA  SER A  97      -3.012 -11.352  25.637  1.00 11.56           C  
ANISOU  872  CA  SER A  97     1249   1412   1730   -332     15    331       C  
ATOM    873  C   SER A  97      -1.857 -12.093  26.302  1.00 11.52           C  
ANISOU  873  C   SER A  97     1401   1296   1682   -400     16    307       C  
ATOM    874  O   SER A  97      -1.997 -12.671  27.388  1.00 13.50           O  
ANISOU  874  O   SER A  97     1606   1647   1876   -297     78    646       O  
ATOM    875  CB  SER A  97      -3.509 -12.180  24.408  1.00 15.93           C  
ANISOU  875  CB  SER A  97     1973   1524   2556   -766   -750    262       C  
ATOM    876  OG ASER A  97      -3.961 -13.390  24.882  0.70 18.25           O  
ANISOU  876  OG ASER A  97     2690   1561   2683   -655   -184    252       O  
ATOM    877  OG BSER A  97      -4.787 -11.629  24.025  0.30 15.28           O  
ANISOU  877  OG BSER A  97     1850   1881   2076   -761   -390    178       O  
ATOM    878  N   ASP A  98      -0.679 -12.038  25.654  1.00 10.41           N  
ANISOU  878  N   ASP A  98     1312   1013   1632   -195     53     58       N  
ATOM    879  CA  ASP A  98       0.505 -12.704  26.283  1.00 10.61           C  
ANISOU  879  CA  ASP A  98     1424   1080   1529   -218    138    193       C  
ATOM    880  C   ASP A  98       0.925 -12.034  27.584  1.00 10.32           C  
ANISOU  880  C   ASP A  98     1454   1105   1362   -126    185    242       C  
ATOM    881  O   ASP A  98       1.293 -12.748  28.551  1.00 11.57           O  
ANISOU  881  O   ASP A  98     1781   1138   1476    -17    165    381       O  
ATOM    882  CB  ASP A  98       1.656 -12.690  25.266  1.00 10.75           C  
ANISOU  882  CB  ASP A  98     1427   1111   1547   -172    262     13       C  
ATOM    883  CG  ASP A  98       1.507 -13.651  24.128  1.00 12.36           C  
ANISOU  883  CG  ASP A  98     1780   1121   1794   -290    292     -9       C  
ATOM    884  OD1 ASP A  98       0.576 -14.514  24.089  1.00 16.50           O  
ANISOU  884  OD1 ASP A  98     2323   1479   2469   -777    532   -321       O  
ATOM    885  OD2 ASP A  98       2.322 -13.572  23.179  1.00 14.79           O  
ANISOU  885  OD2 ASP A  98     2289   1376   1953   -453    667   -366       O  
ATOM    886  N   LEU A  99       0.975 -10.711  27.608  1.00 10.11           N  
ANISOU  886  N   LEU A  99     1443    956   1441    -69     78    150       N  
ATOM    887  CA  LEU A  99       1.397  -9.997  28.864  1.00 10.58           C  
ANISOU  887  CA  LEU A  99     1567   1216   1237   -102    110    148       C  
ATOM    888  C   LEU A  99       0.294 -10.016  29.920  1.00 11.11           C  
ANISOU  888  C   LEU A  99     1499   1442   1282     92    106    277       C  
ATOM    889  O   LEU A  99       0.595  -9.672  31.063  1.00 13.10           O  
ANISOU  889  O   LEU A  99     1745   1943   1290    156     24    221       O  
ATOM    890  CB  LEU A  99       1.758  -8.539  28.503  1.00 10.39           C  
ANISOU  890  CB  LEU A  99     1511   1098   1338    -54     51    117       C  
ATOM    891  CG  LEU A  99       3.077  -8.414  27.724  1.00 10.06           C  
ANISOU  891  CG  LEU A  99     1593   1103   1129   -112      4    132       C  
ATOM    892  CD1 LEU A  99       3.256  -6.941  27.284  1.00 12.56           C  
ANISOU  892  CD1 LEU A  99     1986   1161   1627   -273    -77    202       C  
ATOM    893  CD2 LEU A  99       4.293  -8.864  28.503  1.00 12.11           C  
ANISOU  893  CD2 LEU A  99     1516   1471   1617   -136   -154    145       C  
ATOM    894  N   LYS A 100      -0.948 -10.407  29.542  1.00 11.57           N  
ANISOU  894  N   LYS A 100     1464   1357   1575    -49    216    181       N  
ATOM    895  CA  LYS A 100      -2.119 -10.493  30.443  1.00 12.56           C  
ANISOU  895  CA  LYS A 100     1659   1483   1630    -99    333    321       C  
ATOM    896  C   LYS A 100      -2.478  -9.109  31.007  1.00 12.68           C  
ANISOU  896  C   LYS A 100     1720   1550   1549     51    390    246       C  
ATOM    897  O   LYS A 100      -2.816  -8.960  32.181  1.00 16.63           O  
ANISOU  897  O   LYS A 100     2858   1873   1588    349    775    440       O  
ATOM    898  CB  LYS A 100      -1.901 -11.552  31.528  1.00 15.38           C  
ANISOU  898  CB  LYS A 100     2642   1536   1667   -199    251    322       C  
ATOM    899  CG  LYS A 100      -1.817 -12.969  30.891  1.00 16.05           C  
ANISOU  899  CG  LYS A 100     2441   1381   2275   -387    122    321       C  
ATOM    900  CD  LYS A 100      -1.226 -13.981  31.769  1.00 16.79           C  
ANISOU  900  CD  LYS A 100     2024   1896   2459    263    333    200       C  
ATOM    901  CE  LYS A 100       0.279 -13.870  31.734  1.00 14.98           C  
ANISOU  901  CE  LYS A 100     2066   1838   1788   -391    289   -283       C  
ATOM    902  NZ  LYS A 100       0.918 -14.604  30.576  1.00 14.57           N  
ANISOU  902  NZ  LYS A 100     2451   1448   1635    292    348    193       N  
ATOM    903  N   LEU A 101      -2.446  -8.121  30.105  1.00 11.10           N  
ANISOU  903  N   LEU A 101     1422   1398   1398    -91    125    181       N  
ATOM    904  CA  LEU A 101      -2.748  -6.741  30.470  1.00 11.46           C  
ANISOU  904  CA  LEU A 101     1405   1455   1496      3     98    114       C  
ATOM    905  C   LEU A 101      -3.947  -6.260  29.650  1.00 11.03           C  
ANISOU  905  C   LEU A 101     1306   1575   1309   -106    210    248       C  
ATOM    906  O   LEU A 101      -4.224  -6.829  28.565  1.00 14.16           O  
ANISOU  906  O   LEU A 101     1735   2110   1534     84    -38   -113       O  
ATOM    907  CB  LEU A 101      -1.538  -5.827  30.146  1.00 12.40           C  
ANISOU  907  CB  LEU A 101     1392   1474   1844   -105    -27    136       C  
ATOM    908  CG  LEU A 101      -0.266  -6.166  30.957  1.00 14.11           C  
ANISOU  908  CG  LEU A 101     1517   1521   2324     71   -285    -78       C  
ATOM    909  CD1 LEU A 101       0.888  -5.328  30.509  1.00 17.80           C  
ANISOU  909  CD1 LEU A 101     1495   1655   3615   -110    -85   -367       C  
ATOM    910  CD2 LEU A 101      -0.524  -5.995  32.468  1.00 18.15           C  
ANISOU  910  CD2 LEU A 101     2289   2414   2192    151   -707   -151       C  
ATOM    911  N   ASP A 102      -4.580  -5.200  30.136  1.00 11.50           N  
ANISOU  911  N   ASP A 102     1179   1610   1581     -8    254    200       N  
ATOM    912  CA  ASP A 102      -5.675  -4.620  29.314  1.00 12.60           C  
ANISOU  912  CA  ASP A 102     1002   1840   1947   -195     59    386       C  
ATOM    913  C   ASP A 102      -5.248  -3.341  28.626  1.00 11.22           C  
ANISOU  913  C   ASP A 102     1187   1579   1499   -147     38    104       C  
ATOM    914  O   ASP A 102      -5.980  -2.816  27.788  1.00 13.81           O  
ANISOU  914  O   ASP A 102     1210   2090   1948   -270   -336    339       O  
ATOM    915  CB  ASP A 102      -7.002  -4.425  30.054  1.00 16.31           C  
ANISOU  915  CB  ASP A 102     1344   2561   2294     76    457    483       C  
ATOM    916  CG AASP A 102      -6.970  -3.742  31.345  0.68 15.27           C  
ANISOU  916  CG AASP A 102     1029   2466   2306    462    178    510       C  
ATOM    917  CG BASP A 102      -7.326  -5.277  31.253  0.32 21.84           C  
ANISOU  917  CG BASP A 102     2014   3161   3125   -215   1241    879       C  
ATOM    918  OD1AASP A 102      -8.027  -3.883  32.052  0.68 18.97           O  
ANISOU  918  OD1AASP A 102     1565   3135   2509     33    697    230       O  
ATOM    919  OD1BASP A 102      -7.513  -6.464  30.981  0.32 32.08           O  
ANISOU  919  OD1BASP A 102     4421   3596   4171  -1919    686   1006       O  
ATOM    920  OD2AASP A 102      -5.983  -3.081  31.637  0.68 16.30           O  
ANISOU  920  OD2AASP A 102     1300   2726   2169     55    451    409       O  
ATOM    921  OD2BASP A 102      -7.345  -4.796  32.402  0.32 24.84           O  
ANISOU  921  OD2BASP A 102     2922   3871   2646   -257    873   1296       O  
ATOM    922  N   TYR A 103      -4.024  -2.821  28.901  1.00 10.13           N  
ANISOU  922  N   TYR A 103     1070   1481   1295   -131    105     20       N  
ATOM    923  CA  TYR A 103      -3.477  -1.708  28.118  1.00  9.48           C  
ANISOU  923  CA  TYR A 103      990   1344   1268     -5     44    125       C  
ATOM    924  C   TYR A 103      -1.955  -1.773  28.262  1.00  8.23           C  
ANISOU  924  C   TYR A 103      988   1127   1013     38      5    -13       C  
ATOM    925  O   TYR A 103      -1.419  -2.329  29.235  1.00  9.27           O  
ANISOU  925  O   TYR A 103     1204   1335    981    -31      8     85       O  
ATOM    926  CB  TYR A 103      -4.016  -0.326  28.568  1.00 10.58           C  
ANISOU  926  CB  TYR A 103     1174   1426   1418    181     -7     17       C  
ATOM    927  CG  TYR A 103      -3.552   0.094  29.972  1.00 10.36           C  
ANISOU  927  CG  TYR A 103     1211   1405   1321    173    242     66       C  
ATOM    928  CD1 TYR A 103      -2.405   0.854  30.161  1.00 10.61           C  
ANISOU  928  CD1 TYR A 103     1286   1465   1282     68    135   -137       C  
ATOM    929  CD2 TYR A 103      -4.278  -0.268  31.096  1.00 12.27           C  
ANISOU  929  CD2 TYR A 103     1453   1723   1487     94    409    -72       C  
ATOM    930  CE1 TYR A 103      -1.966   1.258  31.414  1.00 11.49           C  
ANISOU  930  CE1 TYR A 103     1579   1614   1174    244    170   -103       C  
ATOM    931  CE2 TYR A 103      -3.845   0.132  32.387  1.00 12.93           C  
ANISOU  931  CE2 TYR A 103     1795   1800   1317     53    274     54       C  
ATOM    932  CZ  TYR A 103      -2.691   0.873  32.510  1.00 12.05           C  
ANISOU  932  CZ  TYR A 103     1760   1481   1336    155    288    -53       C  
ATOM    933  OH  TYR A 103      -2.296   1.242  33.787  1.00 14.31           O  
ANISOU  933  OH  TYR A 103     2342   1898   1197    -33    243    -78       O  
ATOM    934  N   LEU A 104      -1.266  -1.165  27.285  1.00  8.49           N  
ANISOU  934  N   LEU A 104     1025   1201    999    -12     20     50       N  
ATOM    935  CA  LEU A 104       0.153  -0.903  27.368  1.00  7.96           C  
ANISOU  935  CA  LEU A 104      938   1092    994    -68     11    -72       C  
ATOM    936  C   LEU A 104       0.386   0.564  27.691  1.00  7.58           C  
ANISOU  936  C   LEU A 104     1043   1011    826    105     61    -42       C  
ATOM    937  O   LEU A 104      -0.332   1.444  27.217  1.00  9.12           O  
ANISOU  937  O   LEU A 104     1126   1130   1208    138   -157      9       O  
ATOM    938  CB  LEU A 104       0.869  -1.181  26.028  1.00  9.08           C  
ANISOU  938  CB  LEU A 104     1364   1033   1051     12    226    -76       C  
ATOM    939  CG  LEU A 104       0.854  -2.661  25.626  1.00 10.73           C  
ANISOU  939  CG  LEU A 104     1692   1091   1295     87    242   -114       C  
ATOM    940  CD1 LEU A 104       1.376  -2.776  24.195  1.00 13.78           C  
ANISOU  940  CD1 LEU A 104     2431   1608   1195    528    209   -282       C  
ATOM    941  CD2 LEU A 104       1.708  -3.501  26.520  1.00 20.72           C  
ANISOU  941  CD2 LEU A 104     4615   1721   1538   1317   -116    171       C  
ATOM    942  N   ASP A 105       1.464   0.858  28.443  1.00  7.37           N  
ANISOU  942  N   ASP A 105      939   1076    784    -22     65      1       N  
ATOM    943  CA  ASP A 105       1.815   2.250  28.672  1.00  7.62           C  
ANISOU  943  CA  ASP A 105     1191   1006    697     39     17    -67       C  
ATOM    944  C   ASP A 105       2.445   2.898  27.442  1.00  7.56           C  
ANISOU  944  C   ASP A 105     1094   1009    769     59     94   -111       C  
ATOM    945  O   ASP A 105       2.276   4.118  27.206  1.00  9.37           O  
ANISOU  945  O   ASP A 105     1564   1031    966    266    246      0       O  
ATOM    946  CB  ASP A 105       2.804   2.350  29.872  1.00  8.13           C  
ANISOU  946  CB  ASP A 105     1155   1254    681     17     17    -81       C  
ATOM    947  CG  ASP A 105       2.072   1.859  31.106  1.00  7.97           C  
ANISOU  947  CG  ASP A 105     1191   1116    721    103     88    -82       C  
ATOM    948  OD1 ASP A 105       1.339   2.684  31.718  1.00 10.11           O  
ANISOU  948  OD1 ASP A 105     1477   1426    940    329    239   -103       O  
ATOM    949  OD2 ASP A 105       2.180   0.660  31.424  1.00  8.70           O  
ANISOU  949  OD2 ASP A 105     1161   1202    941     60    135    -19       O  
ATOM    950  N   LEU A 106       3.176   2.123  26.640  1.00  7.48           N  
ANISOU  950  N   LEU A 106     1119   1023    699     63     94    -39       N  
ATOM    951  CA  LEU A 106       3.851   2.661  25.434  1.00  7.19           C  
ANISOU  951  CA  LEU A 106     1054    979    699     59     80    -63       C  
ATOM    952  C   LEU A 106       3.969   1.529  24.449  1.00  6.88           C  
ANISOU  952  C   LEU A 106      939    946    729     80     77     12       C  
ATOM    953  O   LEU A 106       4.376   0.417  24.788  1.00  8.24           O  
ANISOU  953  O   LEU A 106     1385    947    798    201     37     48       O  
ATOM    954  CB  LEU A 106       5.221   3.186  25.860  1.00  8.27           C  
ANISOU  954  CB  LEU A 106     1199   1053    888   -114    121    -43       C  
ATOM    955  CG  LEU A 106       6.161   3.748  24.744  1.00  8.27           C  
ANISOU  955  CG  LEU A 106     1126   1126    892    -74     40     38       C  
ATOM    956  CD1 LEU A 106       5.538   5.003  24.082  1.00 10.15           C  
ANISOU  956  CD1 LEU A 106     1437   1142   1278     14    177    206       C  
ATOM    957  CD2 LEU A 106       7.524   4.053  25.346  1.00  9.97           C  
ANISOU  957  CD2 LEU A 106     1246   1251   1293   -290     22     45       C  
ATOM    958  N   TYR A 107       3.625   1.846  23.177  1.00  7.10           N  
ANISOU  958  N   TYR A 107     1056    910    734    108     90    -41       N  
ATOM    959  CA  TYR A 107       3.749   0.846  22.095  1.00  6.68           C  
ANISOU  959  CA  TYR A 107     1005    863    672     14     43    -62       C  
ATOM    960  C   TYR A 107       4.550   1.521  20.988  1.00  6.51           C  
ANISOU  960  C   TYR A 107     1017    754    703      1    -34   -101       C  
ATOM    961  O   TYR A 107       4.223   2.624  20.535  1.00  7.90           O  
ANISOU  961  O   TYR A 107     1150    874    975    184    102    120       O  
ATOM    962  CB  TYR A 107       2.373   0.393  21.618  1.00  7.71           C  
ANISOU  962  CB  TYR A 107     1052    926    952    -25     74   -110       C  
ATOM    963  CG  TYR A 107       2.332  -0.844  20.782  1.00  7.35           C  
ANISOU  963  CG  TYR A 107     1009    932    852    -21     34      1       C  
ATOM    964  CD1 TYR A 107       2.946  -2.015  21.212  1.00  7.81           C  
ANISOU  964  CD1 TYR A 107     1133    937    898     31     10    -69       C  
ATOM    965  CD2 TYR A 107       1.623  -0.883  19.585  1.00  8.96           C  
ANISOU  965  CD2 TYR A 107     1272   1160    974    -48   -122     -7       C  
ATOM    966  CE1 TYR A 107       2.885  -3.196  20.462  1.00  8.38           C  
ANISOU  966  CE1 TYR A 107     1193    987   1003    -40     17   -122       C  
ATOM    967  CE2 TYR A 107       1.537  -2.066  18.848  1.00  9.30           C  
ANISOU  967  CE2 TYR A 107     1427   1204    903   -116   -113    -38       C  
ATOM    968  CZ  TYR A 107       2.177  -3.211  19.269  1.00  8.51           C  
ANISOU  968  CZ  TYR A 107     1196   1134    905   -125     11   -131       C  
ATOM    969  OH  TYR A 107       2.037  -4.377  18.522  1.00 10.40           O  
ANISOU  969  OH  TYR A 107     1495   1352   1106    -86    -52   -338       O  
ATOM    970  N   LEU A 108       5.628   0.860  20.559  1.00  6.68           N  
ANISOU  970  N   LEU A 108     1030    780    728     67     53    -40       N  
ATOM    971  CA  LEU A 108       6.580   1.426  19.586  1.00  6.56           C  
ANISOU  971  CA  LEU A 108     1038    868    588     37     81     39       C  
ATOM    972  C   LEU A 108       6.494   0.722  18.254  1.00  6.62           C  
ANISOU  972  C   LEU A 108     1022    733    759    112     58     22       C  
ATOM    973  O   LEU A 108       6.356  -0.505  18.192  1.00  8.56           O  
ANISOU  973  O   LEU A 108     1693    785    773    -73     67    -28       O  
ATOM    974  CB  LEU A 108       8.034   1.254  20.096  1.00  7.48           C  
ANISOU  974  CB  LEU A 108     1109    970    762    105    -40    -79       C  
ATOM    975  CG  LEU A 108       8.319   1.841  21.485  1.00  7.86           C  
ANISOU  975  CG  LEU A 108     1211    994    784    137    -67      0       C  
ATOM    976  CD1 LEU A 108       9.781   1.532  21.883  1.00 10.57           C  
ANISOU  976  CD1 LEU A 108     1227   1574   1214    199   -286   -175       C  
ATOM    977  CD2 LEU A 108       8.037   3.336  21.572  1.00  9.63           C  
ANISOU  977  CD2 LEU A 108     1705    929   1024     43    -62   -169       C  
ATOM    978  N   ILE A 109       6.685   1.466  17.158  1.00  6.97           N  
ANISOU  978  N   ILE A 109     1163    837    646     60     43     55       N  
ATOM    979  CA  ILE A 109       7.042   0.822  15.886  1.00  6.98           C  
ANISOU  979  CA  ILE A 109     1143    885    624    168     34     10       C  
ATOM    980  C   ILE A 109       8.501   0.333  16.023  1.00  6.69           C  
ANISOU  980  C   ILE A 109     1160    740    641      0     -4    -35       C  
ATOM    981  O   ILE A 109       9.398   1.147  16.222  1.00  8.32           O  
ANISOU  981  O   ILE A 109     1178    836   1149     40    -56    -92       O  
ATOM    982  CB  ILE A 109       6.896   1.774  14.683  1.00  7.64           C  
ANISOU  982  CB  ILE A 109     1245    973    684    161     57     64       C  
ATOM    983  CG1 ILE A 109       5.479   2.320  14.584  1.00  8.98           C  
ANISOU  983  CG1 ILE A 109     1379   1165    868    371    -27    105       C  
ATOM    984  CG2 ILE A 109       7.275   0.997  13.427  1.00  9.76           C  
ANISOU  984  CG2 ILE A 109     1727   1249    732    373    113    -39       C  
ATOM    985  CD1 ILE A 109       5.294   3.317  13.409  1.00 10.95           C  
ANISOU  985  CD1 ILE A 109     1815   1318   1027    465   -102    205       C  
ATOM    986  N   HIS A 110       8.729  -0.980  15.974  1.00  6.74           N  
ANISOU  986  N   HIS A 110     1145    788    627     94      4     -5       N  
ATOM    987  CA  HIS A 110      10.030  -1.537  16.390  1.00  6.59           C  
ANISOU  987  CA  HIS A 110     1124    750    630     33     21     74       C  
ATOM    988  C   HIS A 110      11.169  -1.098  15.465  1.00  6.33           C  
ANISOU  988  C   HIS A 110     1142    689    576     53     -3    -27       C  
ATOM    989  O   HIS A 110      12.263  -0.779  15.948  1.00  7.07           O  
ANISOU  989  O   HIS A 110     1136    806    745     35    -14     20       O  
ATOM    990  CB  HIS A 110       9.876  -3.078  16.445  1.00  7.09           C  
ANISOU  990  CB  HIS A 110     1206    749    738     12    -40     63       C  
ATOM    991  CG  HIS A 110      10.893  -3.777  17.316  1.00  6.54           C  
ANISOU  991  CG  HIS A 110     1106    722    658     -5     45     -8       C  
ATOM    992  ND1 HIS A 110      10.576  -4.976  17.927  1.00  7.35           N  
ANISOU  992  ND1 HIS A 110     1355    763    674     -5     41     34       N  
ATOM    993  CD2 HIS A 110      12.166  -3.434  17.631  1.00  7.47           C  
ANISOU  993  CD2 HIS A 110     1229    917    694      1    -66     50       C  
ATOM    994  CE1 HIS A 110      11.645  -5.338  18.598  1.00  7.63           C  
ANISOU  994  CE1 HIS A 110     1260    864    777     80    -21    -16       C  
ATOM    995  NE2 HIS A 110      12.635  -4.438  18.445  1.00  8.00           N  
ANISOU  995  NE2 HIS A 110     1386    851    801     44    -68    129       N  
ATOM    996  N   TRP A 111      10.901  -1.106  14.161  1.00  7.10           N  
ANISOU  996  N   TRP A 111     1232    871    593     87     67     59       N  
ATOM    997  CA  TRP A 111      11.854  -0.631  13.142  1.00  6.97           C  
ANISOU  997  CA  TRP A 111     1119    872    659     66    125     78       C  
ATOM    998  C   TRP A 111      11.046   0.061  12.077  1.00  7.12           C  
ANISOU  998  C   TRP A 111     1286    801    620      1     51     -1       C  
ATOM    999  O   TRP A 111       9.865  -0.259  11.835  1.00  8.24           O  
ANISOU  999  O   TRP A 111     1279   1108    745    -71    -34    136       O  
ATOM   1000  CB  TRP A 111      12.616  -1.836  12.456  1.00  7.98           C  
ANISOU 1000  CB  TRP A 111     1347    918    766    135     85    -33       C  
ATOM   1001  CG  TRP A 111      13.567  -2.515  13.403  1.00  7.74           C  
ANISOU 1001  CG  TRP A 111     1265    864    812    139    107     -1       C  
ATOM   1002  CD1 TRP A 111      13.280  -3.478  14.327  1.00  8.96           C  
ANISOU 1002  CD1 TRP A 111     1380   1047    977    218    177    178       C  
ATOM   1003  CD2 TRP A 111      14.970  -2.239  13.520  1.00  8.11           C  
ANISOU 1003  CD2 TRP A 111     1369    971    740    126     92    -83       C  
ATOM   1004  NE1 TRP A 111      14.415  -3.836  15.037  1.00  9.72           N  
ANISOU 1004  NE1 TRP A 111     1514   1150   1029    260    206    148       N  
ATOM   1005  CE2 TRP A 111      15.477  -3.082  14.556  1.00  8.58           C  
ANISOU 1005  CE2 TRP A 111     1368   1017    875    330     27    -43       C  
ATOM   1006  CE3 TRP A 111      15.859  -1.364  12.855  1.00  8.67           C  
ANISOU 1006  CE3 TRP A 111     1277   1037    979    102    167    -77       C  
ATOM   1007  CZ2 TRP A 111      16.808  -3.053  14.945  1.00  9.82           C  
ANISOU 1007  CZ2 TRP A 111     1438   1231   1061    397    -16   -233       C  
ATOM   1008  CZ3 TRP A 111      17.186  -1.358  13.239  1.00 10.46           C  
ANISOU 1008  CZ3 TRP A 111     1365   1246   1365     87     57   -153       C  
ATOM   1009  CH2 TRP A 111      17.669  -2.194  14.272  1.00 10.90           C  
ANISOU 1009  CH2 TRP A 111     1404   1239   1499    246    -49   -307       C  
ATOM   1010  N   PRO A 112      11.672   0.997  11.318  1.00  7.60           N  
ANISOU 1010  N   PRO A 112     1269    907    710     48     31     41       N  
ATOM   1011  CA  PRO A 112      10.898   1.699  10.268  1.00  8.08           C  
ANISOU 1011  CA  PRO A 112     1479    887    705     61    -38    150       C  
ATOM   1012  C   PRO A 112      10.584   0.844   9.051  1.00  8.88           C  
ANISOU 1012  C   PRO A 112     1602   1079    694    208    -52     84       C  
ATOM   1013  O   PRO A 112       9.740   1.202   8.261  1.00 13.58           O  
ANISOU 1013  O   PRO A 112     2409   1679   1071    653   -646    -60       O  
ATOM   1014  CB  PRO A 112      11.833   2.883   9.893  1.00  9.83           C  
ANISOU 1014  CB  PRO A 112     1639   1147    948    -34     29    257       C  
ATOM   1015  CG  PRO A 112      13.200   2.455  10.295  1.00 10.13           C  
ANISOU 1015  CG  PRO A 112     1514   1266   1069    -99     84    402       C  
ATOM   1016  CD  PRO A 112      13.007   1.578  11.543  1.00  8.63           C  
ANISOU 1016  CD  PRO A 112     1384   1044    853   -118     51    164       C  
ATOM   1017  N   THR A 113      11.239  -0.307   8.911  1.00  9.17           N  
ANISOU 1017  N   THR A 113     1721   1063    699    133    -57    -38       N  
ATOM   1018  CA  THR A 113      11.105  -1.196   7.761  1.00  9.01           C  
ANISOU 1018  CA  THR A 113     1728   1050    646    105    -99    -85       C  
ATOM   1019  C   THR A 113       9.944  -2.165   7.876  1.00  9.24           C  
ANISOU 1019  C   THR A 113     1702   1101    709     60    -76     22       C  
ATOM   1020  O   THR A 113       9.888  -2.981   8.827  1.00 11.78           O  
ANISOU 1020  O   THR A 113     1928   1465   1082   -230   -375    402       O  
ATOM   1021  CB  THR A 113      12.407  -2.021   7.645  1.00  9.56           C  
ANISOU 1021  CB  THR A 113     1723   1182    726    172     56    100       C  
ATOM   1022  OG1 THR A 113      12.668  -2.662   8.925  1.00  9.98           O  
ANISOU 1022  OG1 THR A 113     1687   1274    832    204    -34     92       O  
ATOM   1023  CG2 THR A 113      13.601  -1.214   7.332  1.00 11.25           C  
ANISOU 1023  CG2 THR A 113     1882   1342   1050     77    115    180       C  
ATOM   1024  N   GLY A 114       8.998  -2.143   6.932  1.00  9.26           N  
ANISOU 1024  N   GLY A 114     1626   1131    763    156   -112    -88       N  
ATOM   1025  CA  GLY A 114       7.969  -3.164   6.869  1.00  9.57           C  
ANISOU 1025  CA  GLY A 114     1525   1087   1026    134   -104   -249       C  
ATOM   1026  C   GLY A 114       8.400  -4.350   6.024  1.00  8.57           C  
ANISOU 1026  C   GLY A 114     1595   1060    600    240   -103    -60       C  
ATOM   1027  O   GLY A 114       9.038  -4.177   4.959  1.00 10.00           O  
ANISOU 1027  O   GLY A 114     1909   1133    759    100      7    -34       O  
ATOM   1028  N   PHE A 115       8.111  -5.538   6.504  1.00  9.00           N  
ANISOU 1028  N   PHE A 115     1667   1009    743    281   -152    -43       N  
ATOM   1029  CA  PHE A 115       8.417  -6.787   5.794  1.00  9.47           C  
ANISOU 1029  CA  PHE A 115     1752    984    863    260   -117    -83       C  
ATOM   1030  C   PHE A 115       7.117  -7.477   5.377  1.00  9.00           C  
ANISOU 1030  C   PHE A 115     1713   1008    700    206   -149    -47       C  
ATOM   1031  O   PHE A 115       6.067  -7.274   5.968  1.00 10.58           O  
ANISOU 1031  O   PHE A 115     1806   1224    991    221   -122   -250       O  
ATOM   1032  CB  PHE A 115       9.179  -7.758   6.719  1.00 10.13           C  
ANISOU 1032  CB  PHE A 115     1739   1035   1077    258   -232     74       C  
ATOM   1033  CG  PHE A 115      10.496  -7.310   7.303  1.00  9.81           C  
ANISOU 1033  CG  PHE A 115     1829   1063    837    366    -22   -108       C  
ATOM   1034  CD1 PHE A 115      11.223  -6.223   6.859  1.00 10.42           C  
ANISOU 1034  CD1 PHE A 115     1725   1146   1087    234      9   -147       C  
ATOM   1035  CD2 PHE A 115      11.028  -8.049   8.395  1.00 10.83           C  
ANISOU 1035  CD2 PHE A 115     1934   1442    738    537   -165   -141       C  
ATOM   1036  CE1 PHE A 115      12.425  -5.836   7.432  1.00 11.68           C  
ANISOU 1036  CE1 PHE A 115     1771   1413   1256    321    -40   -211       C  
ATOM   1037  CE2 PHE A 115      12.193  -7.686   8.993  1.00 11.84           C  
ANISOU 1037  CE2 PHE A 115     1961   1608    929    493   -118   -251       C  
ATOM   1038  CZ  PHE A 115      12.902  -6.580   8.540  1.00 12.58           C  
ANISOU 1038  CZ  PHE A 115     1888   1794   1098    363   -141   -381       C  
ATOM   1039  N   LYS A 116       7.253  -8.364   4.377  1.00 10.51           N  
ANISOU 1039  N   LYS A 116     1922   1214    857    221   -208   -203       N  
ATOM   1040  CA  LYS A 116       6.114  -9.176   3.916  1.00 11.38           C  
ANISOU 1040  CA  LYS A 116     2065   1231   1028    225   -300   -346       C  
ATOM   1041  C   LYS A 116       5.420  -9.878   5.086  1.00 11.17           C  
ANISOU 1041  C   LYS A 116     1772   1204   1268    201   -304   -292       C  
ATOM   1042  O   LYS A 116       6.125 -10.554   5.853  1.00 12.27           O  
ANISOU 1042  O   LYS A 116     1781   1526   1354    186   -296      0       O  
ATOM   1043  CB  LYS A 116       6.647 -10.272   2.964  1.00 15.82           C  
ANISOU 1043  CB  LYS A 116     2759   1871   1383   -100    -27   -821       C  
ATOM   1044  CG  LYS A 116       5.537 -11.152   2.385  1.00 20.06           C  
ANISOU 1044  CG  LYS A 116     3194   2658   1770   -318    -98  -1347       C  
ATOM   1045  CD  LYS A 116       6.160 -12.315   1.575  1.00 27.30           C  
ANISOU 1045  CD  LYS A 116     5479   2137   2757   -710    759  -1570       C  
ATOM   1046  CE  LYS A 116       5.344 -13.558   1.634  1.00 34.04           C  
ANISOU 1046  CE  LYS A 116     6601   2392   3941   -982   1961  -1055       C  
ATOM   1047  NZ ALYS A 116       6.188 -14.748   1.351  0.45 35.51           N  
ANISOU 1047  NZ ALYS A 116     7832   1914   3744   -810   2567   -490       N  
ATOM   1048  NZ BLYS A 116       4.811 -14.146   2.851  0.55 27.29           N  
ANISOU 1048  NZ BLYS A 116     2883   4291   3196   -556    234   -301       N  
ATOM   1049  N   PRO A 117       4.080  -9.788   5.222  1.00 12.16           N  
ANISOU 1049  N   PRO A 117     1715   1429   1477    217   -496   -396       N  
ATOM   1050  CA  PRO A 117       3.423 -10.491   6.317  1.00 13.63           C  
ANISOU 1050  CA  PRO A 117     1709   1636   1833    147   -178   -360       C  
ATOM   1051  C   PRO A 117       3.474 -11.987   6.152  1.00 13.81           C  
ANISOU 1051  C   PRO A 117     1853   1557   1835     -8   -356   -448       C  
ATOM   1052  O   PRO A 117       3.563 -12.540   5.030  1.00 16.99           O  
ANISOU 1052  O   PRO A 117     2497   1730   2228     81   -575   -697       O  
ATOM   1053  CB  PRO A 117       1.962  -9.994   6.294  1.00 16.84           C  
ANISOU 1053  CB  PRO A 117     1722   2156   2518    400   -234    -45       C  
ATOM   1054  CG  PRO A 117       2.025  -8.824   5.500  1.00 28.41           C  
ANISOU 1054  CG  PRO A 117     2170   4379   4247   1209    683   2100       C  
ATOM   1055  CD  PRO A 117       3.196  -8.868   4.499  1.00 16.41           C  
ANISOU 1055  CD  PRO A 117     1882   2208   2144    693   -334     59       C  
ATOM   1056  N   GLY A 118       3.394 -12.686   7.243  1.00 16.03           N  
ANISOU 1056  N   GLY A 118     2074   1724   2294     31   -548   -186       N  
ATOM   1057  CA  GLY A 118       3.490 -14.145   7.224  1.00 17.27           C  
ANISOU 1057  CA  GLY A 118     2518   1620   2424   -259   -935   -206       C  
ATOM   1058  C   GLY A 118       3.989 -14.644   8.561  1.00 17.78           C  
ANISOU 1058  C   GLY A 118     2402   1898   2456   -284   -901    -33       C  
ATOM   1059  O   GLY A 118       4.107 -13.904   9.524  1.00 21.10           O  
ANISOU 1059  O   GLY A 118     3180   2580   2258    -21   -708   -270       O  
ATOM   1060  N   LYS A 119       4.317 -15.913   8.630  1.00 18.27           N  
ANISOU 1060  N   LYS A 119     2323   1911   2706   -390   -750    229       N  
ATOM   1061  CA  LYS A 119       4.737 -16.566   9.855  1.00 20.48           C  
ANISOU 1061  CA  LYS A 119     2069   2678   3036   -493   -769    845       C  
ATOM   1062  C   LYS A 119       6.188 -16.281  10.235  1.00 16.59           C  
ANISOU 1062  C   LYS A 119     1931   2136   2237    -77   -392    156       C  
ATOM   1063  O   LYS A 119       6.574 -16.347  11.401  1.00 20.10           O  
ANISOU 1063  O   LYS A 119     2098   3413   2125    -59   -299    548       O  
ATOM   1064  CB  LYS A 119       4.542 -18.085   9.788  1.00 31.15           C  
ANISOU 1064  CB  LYS A 119     3766   2790   5281  -1378  -2211   1702       C  
ATOM   1065  CG ALYS A 119       3.102 -18.545   9.649  0.46 32.28           C  
ANISOU 1065  CG ALYS A 119     3333   2804   6126  -1108  -1027   1509       C  
ATOM   1066  CG BLYS A 119       5.025 -18.816  11.020  0.54 41.43           C  
ANISOU 1066  CG BLYS A 119     5734   4008   6000   -396  -1851   2749       C  
ATOM   1067  CD ALYS A 119       2.109 -17.438   9.948  0.46 40.34           C  
ANISOU 1067  CD ALYS A 119     4490   3767   7072   -479   -554    467       C  
ATOM   1068  CD BLYS A 119       4.136 -19.982  11.388  0.54 44.28           C  
ANISOU 1068  CD BLYS A 119     6530   5123   5171   -910   -575   2799       C  
ATOM   1069  CE ALYS A 119       1.930 -17.215  11.446  0.46 44.17           C  
ANISOU 1069  CE ALYS A 119     5810   3897   7078   -810  -1320   -300       C  
ATOM   1070  CE BLYS A 119       3.134 -19.583  12.462  0.54 48.17           C  
ANISOU 1070  CE BLYS A 119     6269   6726   5307   -549  -1110   1598       C  
ATOM   1071  NZ ALYS A 119       2.625 -15.978  11.888  0.46 41.52           N  
ANISOU 1071  NZ ALYS A 119     5427   3563   6787  -1182  -2711   1609       N  
ATOM   1072  NZ BLYS A 119       2.417 -20.780  12.962  0.54 46.78           N  
ANISOU 1072  NZ BLYS A 119     6248   6617   4911   1568    276   3457       N  
ATOM   1073  N  AGLU A 120       6.983 -16.010   9.199  0.52 14.58           N  
ANISOU 1073  N  AGLU A 120     2102   1610   1830   -281   -484   -325       N  
ATOM   1074  N  BGLU A 120       6.991 -15.902   9.228  0.47 13.66           N  
ANISOU 1074  N  BGLU A 120     2001   1269   1920    -30   -520     32       N  
ATOM   1075  CA AGLU A 120       8.407 -15.805   9.483  0.52 13.68           C  
ANISOU 1075  CA AGLU A 120     2012   1415   1772   -254   -404   -205       C  
ATOM   1076  CA BGLU A 120       8.432 -15.682   9.324  0.47 11.29           C  
ANISOU 1076  CA BGLU A 120     1883   1011   1395    311   -311   -312       C  
ATOM   1077  C  AGLU A 120       8.608 -14.346   9.878  0.52 11.48           C  
ANISOU 1077  C  AGLU A 120     1805   1287   1269   -117   -334     15       C  
ATOM   1078  C  BGLU A 120       8.730 -14.239   9.755  0.47 10.27           C  
ANISOU 1078  C  BGLU A 120     1722    921   1258    316   -307   -184       C  
ATOM   1079  O  AGLU A 120       8.007 -13.440   9.274  0.52 13.00           O  
ANISOU 1079  O  AGLU A 120     1905   1471   1562    -12   -542     38       O  
ATOM   1080  O  BGLU A 120       8.346 -13.269   9.074  0.47 10.75           O  
ANISOU 1080  O  BGLU A 120     1920   1010   1156    202   -327    -72       O  
ATOM   1081  CB AGLU A 120       9.220 -16.125   8.238  0.52 15.20           C  
ANISOU 1081  CB AGLU A 120     2417   1424   1933    276   -256   -202       C  
ATOM   1082  CB BGLU A 120       9.156 -15.891   7.999  0.47 14.57           C  
ANISOU 1082  CB BGLU A 120     2816   1318   1401    149      6   -431       C  
ATOM   1083  CG AGLU A 120       9.082 -17.572   7.784  0.52 20.95           C  
ANISOU 1083  CG AGLU A 120     3498   1764   2698   -274   -316   -811       C  
ATOM   1084  CG BGLU A 120       9.359 -17.284   7.458  0.47 20.74           C  
ANISOU 1084  CG BGLU A 120     3593   1694   2593    375    137  -1166       C  
ATOM   1085  CD AGLU A 120       9.976 -17.810   6.586  0.52 26.05           C  
ANISOU 1085  CD AGLU A 120     4262   2516   3120   -378     38  -1678       C  
ATOM   1086  CD BGLU A 120      10.412 -18.070   8.207  0.47 29.57           C  
ANISOU 1086  CD BGLU A 120     4921   1808   4506   1180   -546   -968       C  
ATOM   1087  OE1AGLU A 120      10.511 -18.915   6.437  0.52 39.63           O  
ANISOU 1087  OE1AGLU A 120     4671   4584   5803   1805   -443  -2254       O  
ATOM   1088  OE1BGLU A 120      10.058 -19.219   8.548  0.47 46.07           O  
ANISOU 1088  OE1BGLU A 120     5983   3705   7818    820    440   2159       O  
ATOM   1089  OE2AGLU A 120      10.148 -16.885   5.794  0.52 40.42           O  
ANISOU 1089  OE2AGLU A 120     8589   3674   3097  -1859   1620  -1576       O  
ATOM   1090  OE2BGLU A 120      11.551 -17.602   8.477  0.47 37.92           O  
ANISOU 1090  OE2BGLU A 120     6633   3403   4371    356  -3428   -527       O  
ATOM   1091  N   PHE A 121       9.451 -14.140  10.881  1.00 10.01           N  
ANISOU 1091  N   PHE A 121     1627   1156   1022     68   -139   -112       N  
ATOM   1092  CA  PHE A 121       9.799 -12.774  11.305  1.00  9.36           C  
ANISOU 1092  CA  PHE A 121     1768   1030    760    175    -47    -36       C  
ATOM   1093  C   PHE A 121      10.736 -12.057  10.345  1.00  9.04           C  
ANISOU 1093  C   PHE A 121     1630   1037    766    217   -156    -67       C  
ATOM   1094  O   PHE A 121      10.705 -10.812  10.274  1.00  9.77           O  
ANISOU 1094  O   PHE A 121     1871   1002    838    216      7    -56       O  
ATOM   1095  CB  PHE A 121      10.473 -12.820  12.692  1.00 10.30           C  
ANISOU 1095  CB  PHE A 121     1949   1223    741    101   -104    -27       C  
ATOM   1096  CG  PHE A 121       9.539 -13.227  13.819  1.00 10.63           C  
ANISOU 1096  CG  PHE A 121     2166   1027    846     93     54   -121       C  
ATOM   1097  CD1 PHE A 121       8.167 -12.967  13.820  1.00 15.45           C  
ANISOU 1097  CD1 PHE A 121     2249   2089   1532    224    454    355       C  
ATOM   1098  CD2 PHE A 121      10.081 -13.849  14.953  1.00 14.00           C  
ANISOU 1098  CD2 PHE A 121     3049   1398    871    290     67     48       C  
ATOM   1099  CE1 PHE A 121       7.334 -13.245  14.891  1.00 17.50           C  
ANISOU 1099  CE1 PHE A 121     2790   2027   1831    345    890    266       C  
ATOM   1100  CE2 PHE A 121       9.234 -14.160  16.037  1.00 17.16           C  
ANISOU 1100  CE2 PHE A 121     3533   1820   1166     -7    236    360       C  
ATOM   1101  CZ  PHE A 121       7.880 -13.856  15.991  1.00 17.85           C  
ANISOU 1101  CZ  PHE A 121     3401   1973   1407   -311    637     87       C  
ATOM   1102  N   PHE A 122      11.574 -12.819   9.625  1.00  9.30           N  
ANISOU 1102  N   PHE A 122     1672   1090    773    292    -55    -34       N  
ATOM   1103  CA  PHE A 122      12.519 -12.259   8.648  1.00  9.96           C  
ANISOU 1103  CA  PHE A 122     1763   1193    829    365     19    -31       C  
ATOM   1104  C   PHE A 122      12.320 -13.031   7.338  1.00 10.86           C  
ANISOU 1104  C   PHE A 122     2222   1046    857    452     27     20       C  
ATOM   1105  O   PHE A 122      13.079 -13.954   7.045  1.00 14.06           O  
ANISOU 1105  O   PHE A 122     2842   1448   1054    945    -89    -99       O  
ATOM   1106  CB  PHE A 122      13.980 -12.378   9.115  1.00 11.99           C  
ANISOU 1106  CB  PHE A 122     1695   1532   1330    308    122   -186       C  
ATOM   1107  CG  PHE A 122      14.320 -11.457  10.282  1.00 12.05           C  
ANISOU 1107  CG  PHE A 122     1653   1372   1553    408   -150   -179       C  
ATOM   1108  CD1 PHE A 122      14.197 -11.872  11.571  1.00 13.28           C  
ANISOU 1108  CD1 PHE A 122     1990   1646   1407    529   -225   -275       C  
ATOM   1109  CD2 PHE A 122      14.790 -10.175  10.036  1.00 14.39           C  
ANISOU 1109  CD2 PHE A 122     1568   1487   2413    191    -55   -235       C  
ATOM   1110  CE1 PHE A 122      14.501 -11.058  12.681  1.00 15.32           C  
ANISOU 1110  CE1 PHE A 122     2076   1859   1886    534   -622   -559       C  
ATOM   1111  CE2 PHE A 122      15.126  -9.350  11.103  1.00 16.79           C  
ANISOU 1111  CE2 PHE A 122     1841   1702   2836    164   -353   -520       C  
ATOM   1112  CZ  PHE A 122      14.998  -9.803  12.429  1.00 16.45           C  
ANISOU 1112  CZ  PHE A 122     1838   1768   2643    544   -423   -678       C  
ATOM   1113  N   PRO A 123      11.333 -12.660   6.535  1.00 11.35           N  
ANISOU 1113  N   PRO A 123     2351   1202    762    441    -35    -95       N  
ATOM   1114  CA  PRO A 123      11.099 -13.371   5.241  1.00 11.56           C  
ANISOU 1114  CA  PRO A 123     2399   1189    804    207     63   -196       C  
ATOM   1115  C   PRO A 123      12.218 -12.998   4.311  1.00 11.94           C  
ANISOU 1115  C   PRO A 123     2569   1101    866    407     85    -51       C  
ATOM   1116  O   PRO A 123      12.462 -11.800   4.066  1.00 13.93           O  
ANISOU 1116  O   PRO A 123     2707   1323   1264    383    450     56       O  
ATOM   1117  CB  PRO A 123       9.730 -12.847   4.787  1.00 12.96           C  
ANISOU 1117  CB  PRO A 123     2494   1409   1020    224   -225   -174       C  
ATOM   1118  CG  PRO A 123       9.632 -11.460   5.395  1.00 12.32           C  
ANISOU 1118  CG  PRO A 123     2331   1413    936    379   -224   -134       C  
ATOM   1119  CD  PRO A 123      10.343 -11.576   6.749  1.00 11.65           C  
ANISOU 1119  CD  PRO A 123     2015   1355   1055    536   -207   -268       C  
ATOM   1120  N   LEU A 124      12.926 -13.968   3.754  1.00 13.94           N  
ANISOU 1120  N   LEU A 124     2787   1453   1057    574    405     41       N  
ATOM   1121  CA  LEU A 124      14.028 -13.701   2.877  1.00 13.97           C  
ANISOU 1121  CA  LEU A 124     2526   1724   1060    501    286    180       C  
ATOM   1122  C   LEU A 124      13.760 -14.243   1.447  1.00 14.53           C  
ANISOU 1122  C   LEU A 124     3285   1143   1091    581    327    113       C  
ATOM   1123  O   LEU A 124      13.028 -15.247   1.267  1.00 19.40           O  
ANISOU 1123  O   LEU A 124     4327   1411   1634    -52    989   -374       O  
ATOM   1124  CB  LEU A 124      15.329 -14.434   3.337  1.00 18.92           C  
ANISOU 1124  CB  LEU A 124     3061   2692   1434   1319    257    404       C  
ATOM   1125  CG  LEU A 124      15.790 -14.093   4.755  1.00 19.71           C  
ANISOU 1125  CG  LEU A 124     2790   3286   1414   1207    209    630       C  
ATOM   1126  CD1 LEU A 124      17.077 -14.891   5.058  1.00 31.23           C  
ANISOU 1126  CD1 LEU A 124     3295   6218   2355   2273    138   1688       C  
ATOM   1127  CD2 LEU A 124      16.048 -12.620   4.968  1.00 24.00           C  
ANISOU 1127  CD2 LEU A 124     2945   3837   2336   -320   -860    521       C  
ATOM   1128  N   ASP A 125      14.335 -13.567   0.473  1.00 14.18           N  
ANISOU 1128  N   ASP A 125     3076   1296   1016    591    278     41       N  
ATOM   1129  CA  ASP A 125      14.264 -14.098  -0.921  1.00 15.67           C  
ANISOU 1129  CA  ASP A 125     3595   1324   1036    740    425    -65       C  
ATOM   1130  C   ASP A 125      15.442 -15.013  -1.169  1.00 19.29           C  
ANISOU 1130  C   ASP A 125     4124   1796   1409   1268    217   -279       C  
ATOM   1131  O   ASP A 125      16.217 -15.308  -0.253  1.00 22.27           O  
ANISOU 1131  O   ASP A 125     4530   2237   1694   1755    267     30       O  
ATOM   1132  CB  ASP A 125      14.169 -12.929  -1.903  1.00 13.75           C  
ANISOU 1132  CB  ASP A 125     2599   1519   1106    188    -24    220       C  
ATOM   1133  CG  ASP A 125      15.357 -12.063  -2.048  1.00 13.59           C  
ANISOU 1133  CG  ASP A 125     2231   1880   1051    400    214    -75       C  
ATOM   1134  OD1 ASP A 125      16.504 -12.464  -1.674  1.00 15.77           O  
ANISOU 1134  OD1 ASP A 125     2348   2226   1419    465    220     31       O  
ATOM   1135  OD2 ASP A 125      15.205 -10.888  -2.578  1.00 14.60           O  
ANISOU 1135  OD2 ASP A 125     2452   1903   1192     17     93    241       O  
ATOM   1136  N   GLU A 126      15.572 -15.508  -2.381  1.00 23.14           N  
ANISOU 1136  N   GLU A 126     4015   2882   1896   1075    416  -1249       N  
ATOM   1137  CA  GLU A 126      16.434 -16.661  -2.564  1.00 27.28           C  
ANISOU 1137  CA  GLU A 126     3757   3131   3476    974    263  -2057       C  
ATOM   1138  C   GLU A 126      17.873 -16.220  -2.463  1.00 25.15           C  
ANISOU 1138  C   GLU A 126     3778   2805   2971    892    720  -1029       C  
ATOM   1139  O   GLU A 126      18.742 -17.092  -2.354  1.00 33.27           O  
ANISOU 1139  O   GLU A 126     3677   2954   6008   1119    990  -1590       O  
ATOM   1140  CB  GLU A 126      16.131 -17.313  -3.928  0.50 32.92           C  
ANISOU 1140  CB  GLU A 126     4210   4530   3768   1136    765  -3049       C  
ATOM   1141  CG  GLU A 126      15.182 -18.477  -3.732  0.50 38.23           C  
ANISOU 1141  CG  GLU A 126     5630   3629   5267    857   -886  -2727       C  
ATOM   1142  CD  GLU A 126      15.860 -19.732  -3.211  0.50 42.71           C  
ANISOU 1142  CD  GLU A 126     6531   4323   5376   1167  -2396  -2744       C  
ATOM   1143  OE1 GLU A 126      17.087 -19.720  -2.982  0.50 48.59           O  
ANISOU 1143  OE1 GLU A 126     6541   5541   6378   1162  -2483  -2224       O  
ATOM   1144  OE2 GLU A 126      15.147 -20.736  -3.031  0.50 47.84           O  
ANISOU 1144  OE2 GLU A 126     6699   4449   7029   1298  -3007  -1044       O  
ATOM   1145  N   SER A 127      18.178 -14.965  -2.533  1.00 22.65           N  
ANISOU 1145  N   SER A 127     4000   2886   1721    791    926   -277       N  
ATOM   1146  CA  SER A 127      19.503 -14.442  -2.378  1.00 26.37           C  
ANISOU 1146  CA  SER A 127     4297   3748   1975     96   1486   -388       C  
ATOM   1147  C   SER A 127      19.775 -13.842  -1.019  1.00 21.55           C  
ANISOU 1147  C   SER A 127     3079   3635   1473   1267    423    531       C  
ATOM   1148  O   SER A 127      20.869 -13.277  -0.808  1.00 29.16           O  
ANISOU 1148  O   SER A 127     3332   5060   2687    750    659   -488       O  
ATOM   1149  CB  SER A 127      19.619 -13.334  -3.428  1.00 32.27           C  
ANISOU 1149  CB  SER A 127     4907   6064   1293  -1097    617    480       C  
ATOM   1150  OG  SER A 127      19.631 -14.184  -4.639  1.00 42.97           O  
ANISOU 1150  OG  SER A 127     9466   4618   2243  -1420    638    330       O  
ATOM   1151  N   GLY A 128      18.815 -13.963  -0.087  1.00 18.97           N  
ANISOU 1151  N   GLY A 128     3710   2256   1244   1322    691    166       N  
ATOM   1152  CA  GLY A 128      19.218 -13.539   1.307  1.00 22.60           C  
ANISOU 1152  CA  GLY A 128     4571   2699   1317   2034    100    170       C  
ATOM   1153  C   GLY A 128      18.769 -12.120   1.660  1.00 17.23           C  
ANISOU 1153  C   GLY A 128     2964   2540   1042   1318    309    100       C  
ATOM   1154  O   GLY A 128      19.113 -11.673   2.754  1.00 21.96           O  
ANISOU 1154  O   GLY A 128     3686   3174   1485   1286    -68   -199       O  
ATOM   1155  N   ASN A 129      18.082 -11.408   0.774  1.00 15.56           N  
ANISOU 1155  N   ASN A 129     2486   2141   1287   1023    395    208       N  
ATOM   1156  CA  ASN A 129      17.545 -10.093   1.055  1.00 14.05           C  
ANISOU 1156  CA  ASN A 129     2060   1780   1497    531    211    137       C  
ATOM   1157  C   ASN A 129      16.213 -10.218   1.748  1.00 12.48           C  
ANISOU 1157  C   ASN A 129     2164   1414   1164    394    225    -43       C  
ATOM   1158  O   ASN A 129      15.384 -11.064   1.388  1.00 14.31           O  
ANISOU 1158  O   ASN A 129     2321   1815   1299    280    236   -288       O  
ATOM   1159  CB  ASN A 129      17.298  -9.347  -0.255  1.00 16.63           C  
ANISOU 1159  CB  ASN A 129     2674   2041   1603    627    489    555       C  
ATOM   1160  CG  ASN A 129      18.540  -9.338  -1.134  1.00 16.10           C  
ANISOU 1160  CG  ASN A 129     2385   2213   1521    329    187    142       C  
ATOM   1161  OD1 ASN A 129      19.563  -8.798  -0.690  1.00 20.94           O  
ANISOU 1161  OD1 ASN A 129     2764   2920   2272   -187    -24   -157       O  
ATOM   1162  ND2 ASN A 129      18.487  -9.958  -2.337  1.00 20.00           N  
ANISOU 1162  ND2 ASN A 129     3344   3076   1178    -23    213    121       N  
ATOM   1163  N   VAL A 130      15.917  -9.321   2.725  1.00 13.08           N  
ANISOU 1163  N   VAL A 130     2179   1579   1213    518    260    -99       N  
ATOM   1164  CA  VAL A 130      14.579  -9.339   3.290  1.00 12.12           C  
ANISOU 1164  CA  VAL A 130     2002   1626    976    384     71   -311       C  
ATOM   1165  C   VAL A 130      13.529  -8.940   2.247  1.00 11.57           C  
ANISOU 1165  C   VAL A 130     2010   1337   1051    423    270    -62       C  
ATOM   1166  O   VAL A 130      13.807  -8.078   1.365  1.00 14.85           O  
ANISOU 1166  O   VAL A 130     2199   1794   1651    222    132    397       O  
ATOM   1167  CB  VAL A 130      14.517  -8.395   4.529  1.00 14.34           C  
ANISOU 1167  CB  VAL A 130     2542   1587   1321    283    325   -499       C  
ATOM   1168  CG1 VAL A 130      14.463  -6.910   4.184  1.00 17.83           C  
ANISOU 1168  CG1 VAL A 130     3276   1599   1899    350     22   -422       C  
ATOM   1169  CG2 VAL A 130      13.345  -8.781   5.413  1.00 16.46           C  
ANISOU 1169  CG2 VAL A 130     2442   2531   1280    213    388   -528       C  
ATOM   1170  N   VAL A 131      12.361  -9.523   2.326  1.00 11.16           N  
ANISOU 1170  N   VAL A 131     1951   1309    980    348     77    -88       N  
ATOM   1171  CA  VAL A 131      11.284  -9.197   1.384  1.00 10.98           C  
ANISOU 1171  CA  VAL A 131     2156   1177    840    331     -8    -29       C  
ATOM   1172  C   VAL A 131      10.496  -8.049   1.972  1.00 10.28           C  
ANISOU 1172  C   VAL A 131     2068   1237    600    316    128    -10       C  
ATOM   1173  O   VAL A 131       9.853  -8.226   3.028  1.00 11.20           O  
ANISOU 1173  O   VAL A 131     2253   1266    737    242    117     -7       O  
ATOM   1174  CB  VAL A 131      10.400 -10.418   1.122  1.00 11.52           C  
ANISOU 1174  CB  VAL A 131     2144   1180   1054    297    -67   -130       C  
ATOM   1175  CG1 VAL A 131       9.353  -9.990   0.083  1.00 13.55           C  
ANISOU 1175  CG1 VAL A 131     2512   1701    935    317   -285   -106       C  
ATOM   1176  CG2 VAL A 131      11.180 -11.581   0.556  1.00 16.63           C  
ANISOU 1176  CG2 VAL A 131     3062   1523   1733    665   -247   -613       C  
ATOM   1177  N   PRO A 132      10.492  -6.835   1.377  1.00 10.47           N  
ANISOU 1177  N   PRO A 132     2068   1235    674    393    164    -24       N  
ATOM   1178  CA  PRO A 132       9.754  -5.720   1.945  1.00 10.06           C  
ANISOU 1178  CA  PRO A 132     2043   1080    701    287     57    -54       C  
ATOM   1179  C   PRO A 132       8.254  -5.856   1.726  1.00 10.75           C  
ANISOU 1179  C   PRO A 132     2134   1328    622    403   -161    -96       C  
ATOM   1180  O   PRO A 132       7.794  -6.567   0.865  1.00 13.89           O  
ANISOU 1180  O   PRO A 132     2343   1890   1045    321   -256   -556       O  
ATOM   1181  CB  PRO A 132      10.304  -4.464   1.182  1.00 13.30           C  
ANISOU 1181  CB  PRO A 132     2758   1302    993    246    435    101       C  
ATOM   1182  CG  PRO A 132      11.136  -5.004   0.142  1.00 19.40           C  
ANISOU 1182  CG  PRO A 132     3855   1345   2172    454   1623    295       C  
ATOM   1183  CD  PRO A 132      11.218  -6.476   0.134  1.00 12.10           C  
ANISOU 1183  CD  PRO A 132     2553   1345    698    417    249    128       C  
ATOM   1184  N  ASER A 133       7.482  -5.107   2.517  0.41 11.28           N  
ANISOU 1184  N  ASER A 133     1932   1640    716    576   -279   -149       N  
ATOM   1185  N  BSER A 133       7.555  -5.058   2.536  0.60 10.88           N  
ANISOU 1185  N  BSER A 133     1859   1269   1005    345    -89   -140       N  
ATOM   1186  CA ASER A 133       6.110  -4.632   2.433  0.41 12.85           C  
ANISOU 1186  CA ASER A 133     1769   1962   1150    411   -235    516       C  
ATOM   1187  CA BSER A 133       6.180  -4.813   2.113  0.60 10.57           C  
ANISOU 1187  CA BSER A 133     1963   1332    722    296   -254   -107       C  
ATOM   1188  C  ASER A 133       6.013  -3.265   1.767  0.41 11.82           C  
ANISOU 1188  C  ASER A 133     2103   1385   1002    388   -512   -111       C  
ATOM   1189  C  BSER A 133       6.061  -3.414   1.545  0.60 10.71           C  
ANISOU 1189  C  BSER A 133     2132   1284    654    420   -141   -269       C  
ATOM   1190  O  ASER A 133       6.867  -2.407   1.968  0.41 13.71           O  
ANISOU 1190  O  ASER A 133     1773   2027   1409     58   -155      3       O  
ATOM   1191  O  BSER A 133       6.900  -2.537   1.747  0.60 13.27           O  
ANISOU 1191  O  BSER A 133     2340   1249   1452    332   -623   -100       O  
ATOM   1192  CB ASER A 133       5.434  -4.478   3.813  0.41 17.58           C  
ANISOU 1192  CB ASER A 133     1916   3193   1571    636    244    627       C  
ATOM   1193  CB BSER A 133       5.242  -5.025   3.309  0.60 10.97           C  
ANISOU 1193  CB BSER A 133     1822   1525    822    362   -240   -143       C  
ATOM   1194  OG ASER A 133       4.344  -3.555   3.880  0.41 20.77           O  
ANISOU 1194  OG ASER A 133     2953   2454   2483    841    882    773       O  
ATOM   1195  OG BSER A 133       5.582  -4.058   4.344  0.60 11.03           O  
ANISOU 1195  OG BSER A 133     1875   1448    870    340    -37   -233       O  
ATOM   1196  N  AASP A 134       4.948  -3.048   0.970  0.41 12.21           N  
ANISOU 1196  N  AASP A 134     1970   1324   1345    504   -506     36       N  
ATOM   1197  N  BASP A 134       4.957  -3.244   0.788  0.60 10.76           N  
ANISOU 1197  N  BASP A 134     1920   1485    683    444      1    -40       N  
ATOM   1198  CA AASP A 134       4.788  -1.731   0.321  0.41 12.82           C  
ANISOU 1198  CA AASP A 134     2651   1508    711    744   -151     25       C  
ATOM   1199  CA BASP A 134       4.667  -1.934   0.195  0.60 12.85           C  
ANISOU 1199  CA BASP A 134     2425   1703    754    647    -29     10       C  
ATOM   1200  C  AASP A 134       4.107  -0.705   1.225  0.41 11.53           C  
ANISOU 1200  C  AASP A 134     2318   1223    841    291    -59    -73       C  
ATOM   1201  C  BASP A 134       3.867  -1.096   1.188  0.60 13.92           C  
ANISOU 1201  C  BASP A 134     2529   1721   1038    836   -339   -221       C  
ATOM   1202  O  AASP A 134       3.901   0.411   0.741  0.41 13.25           O  
ANISOU 1202  O  AASP A 134     2815   1333    888    526    142     75       O  
ATOM   1203  O  BASP A 134       2.766  -0.642   0.878  0.60 24.62           O  
ANISOU 1203  O  BASP A 134     2913   4171   2269   1955   -996  -1580       O  
ATOM   1204  CB AASP A 134       3.992  -1.882  -0.972  0.41 14.32           C  
ANISOU 1204  CB AASP A 134     2784   1754    901   1148   -375   -273       C  
ATOM   1205  CB BASP A 134       3.841  -2.141  -1.068  0.60 16.45           C  
ANISOU 1205  CB BASP A 134     3300   2074    875    702   -471    -51       C  
ATOM   1206  CG AASP A 134       2.624  -2.501  -0.966  0.41 16.82           C  
ANISOU 1206  CG AASP A 134     3401   1729   1262    436   -673   -198       C  
ATOM   1207  CG BASP A 134       3.686  -0.829  -1.803  0.60 20.77           C  
ANISOU 1207  CG BASP A 134     4252   2327   1312   1078   -611    269       C  
ATOM   1208  OD1AASP A 134       2.042  -2.664   0.137  0.41 21.30           O  
ANISOU 1208  OD1AASP A 134     2176   4380   1537    753   -473   -762       O  
ATOM   1209  OD1BASP A 134       4.581   0.039  -1.845  0.60 32.95           O  
ANISOU 1209  OD1BASP A 134     6841   3300   2378   -685   -741   1225       O  
ATOM   1210  OD2AASP A 134       2.086  -2.796  -2.100  0.41 20.69           O  
ANISOU 1210  OD2AASP A 134     3634   2787   1442    382  -1043     47       O  
ATOM   1211  OD2BASP A 134       2.630  -0.702  -2.471  0.60 34.90           O  
ANISOU 1211  OD2BASP A 134     6481   3646   3132   1847  -2863   -155       O  
ATOM   1212  N  ATHR A 135       3.735  -1.041   2.449  0.41 12.16           N  
ANISOU 1212  N  ATHR A 135     2524   1345    753    734   -163     39       N  
ATOM   1213  N  BTHR A 135       4.400  -0.934   2.367  0.60 11.82           N  
ANISOU 1213  N  BTHR A 135     1880   1690    922    454     31   -292       N  
ATOM   1214  CA ATHR A 135       3.015  -0.094   3.293  0.41 12.94           C  
ANISOU 1214  CA ATHR A 135     2605   1497    813    620     -9    -58       C  
ATOM   1215  CA BTHR A 135       3.871  -0.094   3.405  0.60 11.31           C  
ANISOU 1215  CA BTHR A 135     2075   1342    881    416     90    -93       C  
ATOM   1216  C  ATHR A 135       3.921   1.009   3.770  0.41 14.61           C  
ANISOU 1216  C  ATHR A 135     2731   1621   1199    627     32   -300       C  
ATOM   1217  C  BTHR A 135       4.786   1.108   3.587  0.60 11.96           C  
ANISOU 1217  C  BTHR A 135     2178   1337   1030    437    222   -107       C  
ATOM   1218  O  ATHR A 135       5.034   0.767   4.274  0.41 21.92           O  
ANISOU 1218  O  ATHR A 135     3244   2738   2346    640   -951  -1078       O  
ATOM   1219  O  BTHR A 135       5.990   1.073   3.305  0.60 15.87           O  
ANISOU 1219  O  BTHR A 135     2073   2108   1850    151     72   -685       O  
ATOM   1220  CB ATHR A 135       2.408  -0.841   4.507  0.41 19.01           C  
ANISOU 1220  CB ATHR A 135     3738   2593    892    -70    399    -56       C  
ATOM   1221  CB BTHR A 135       3.758  -0.900   4.744  0.60 13.82           C  
ANISOU 1221  CB BTHR A 135     2754   1526    969    207    350    -81       C  
ATOM   1222  OG1ATHR A 135       1.382  -1.733   4.040  0.41 22.74           O  
ANISOU 1222  OG1ATHR A 135     4381   2350   1907   -543    482     19       O  
ATOM   1223  OG1BTHR A 135       5.056  -1.444   5.055  0.60 15.60           O  
ANISOU 1223  OG1BTHR A 135     3222   1482   1224      5   -775     49       O  
ATOM   1224  CG2ATHR A 135       1.741   0.115   5.497  0.41 16.32           C  
ANISOU 1224  CG2ATHR A 135     2505   2554   1142     68    263    142       C  
ATOM   1225  CG2BTHR A 135       2.779  -2.045   4.603  0.60 14.28           C  
ANISOU 1225  CG2BTHR A 135     2583   1523   1318    299    341    133       C  
ATOM   1226  N  AASN A 136       3.562   2.295   3.713  0.41 17.18           N  
ANISOU 1226  N  AASN A 136     3361   1425   1742    447   1501      9       N  
ATOM   1227  N  BASN A 136       4.281   2.191   4.127  0.60 19.13           N  
ANISOU 1227  N  BASN A 136     3016   1166   3087    665    440   -388       N  
ATOM   1228  CA AASN A 136       4.627   3.163   4.295  0.41 18.56           C  
ANISOU 1228  CA AASN A 136     3893   1506   1653    252   1516   -188       C  
ATOM   1229  CA BASN A 136       5.161   3.372   4.365  0.60 19.88           C  
ANISOU 1229  CA BASN A 136     4223   1134   2195      0   1022    -19       C  
ATOM   1230  C  AASN A 136       4.532   3.492   5.763  0.41 16.93           C  
ANISOU 1230  C  AASN A 136     3295   1691   1447    673   1525     61       C  
ATOM   1231  C  BASN A 136       4.817   3.829   5.769  0.60 19.80           C  
ANISOU 1231  C  BASN A 136     4559    971   1992    377    887    191       C  
ATOM   1232  O  AASN A 136       3.627   3.115   6.504  0.41 22.05           O  
ANISOU 1232  O  AASN A 136     5033   1579   1766   -320   1908    558       O  
ATOM   1233  O  BASN A 136       3.743   3.528   6.285  0.60 22.63           O  
ANISOU 1233  O  BASN A 136     5127   1086   2384    111   1458   -211       O  
ATOM   1234  CB AASN A 136       4.614   4.499   3.532  0.41 17.19           C  
ANISOU 1234  CB AASN A 136     3908   1527   1098    186   1019   -386       C  
ATOM   1235  CB BASN A 136       5.023   4.394   3.254  0.60 20.81           C  
ANISOU 1235  CB BASN A 136     3786   2050   2072    544    809    276       C  
ATOM   1236  CG AASN A 136       3.165   4.938   3.672  0.41 18.05           C  
ANISOU 1236  CG AASN A 136     3626   1890   1343   -104   1086    815       C  
ATOM   1237  CG BASN A 136       3.979   5.484   3.465  0.60 23.63           C  
ANISOU 1237  CG BASN A 136     4501   3501    975   1653    755    257       C  
ATOM   1238  OD1AASN A 136       2.997   5.600   4.668  0.41 16.59           O  
ANISOU 1238  OD1AASN A 136     2447   2758   1098    825    680    827       O  
ATOM   1239  OD1BASN A 136       4.077   6.393   4.315  0.60 30.37           O  
ANISOU 1239  OD1BASN A 136     7377   2757   1405   1952   1325    385       O  
ATOM   1240  ND2AASN A 136       2.305   4.553   2.768  0.41 28.03           N  
ANISOU 1240  ND2AASN A 136     3661   3443   3547   -363    911  -1456       N  
ATOM   1241  ND2BASN A 136       2.968   5.427   2.612  0.60 35.39           N  
ANISOU 1241  ND2BASN A 136     2515   6930   4000    796    761     18       N  
ATOM   1242  N  AILE A 137       5.487   4.272   6.227  0.41 15.21           N  
ANISOU 1242  N  AILE A 137     2983   1709   1086   1056    835    697       N  
ATOM   1243  N  BILE A 137       5.737   4.550   6.383  0.60 20.06           N  
ANISOU 1243  N  BILE A 137     3699   2029   1892   1313    254     50       N  
ATOM   1244  CA AILE A 137       5.627   4.676   7.620  0.41 17.16           C  
ANISOU 1244  CA AILE A 137     2989   2277   1256   1249    724    393       C  
ATOM   1245  CA BILE A 137       5.661   4.727   7.835  0.60 18.99           C  
ANISOU 1245  CA BILE A 137     2588   3012   1615   1243    313    747       C  
ATOM   1246  C  AILE A 137       4.397   5.464   8.101  0.41 15.27           C  
ANISOU 1246  C  AILE A 137     2536   2435    829   1109    301    290       C  
ATOM   1247  C  BILE A 137       4.443   5.580   8.212  0.60 17.07           C  
ANISOU 1247  C  BILE A 137     2597   2599   1292   1074     -6    357       C  
ATOM   1248  O  AILE A 137       3.876   5.168   9.181  0.41 17.26           O  
ANISOU 1248  O  AILE A 137     2827   2711   1021    968    614    317       O  
ATOM   1249  O  BILE A 137       3.923   5.450   9.324  0.60 17.36           O  
ANISOU 1249  O  BILE A 137     2752   2560   1282   1385     85    389       O  
ATOM   1250  CB AILE A 137       6.905   5.524   7.839  0.41 21.37           C  
ANISOU 1250  CB AILE A 137     2591   4131   1396    959    625    139       C  
ATOM   1251  CB BILE A 137       6.977   5.329   8.372  0.60 21.80           C  
ANISOU 1251  CB BILE A 137     2553   3427   2302   1239    447   -237       C  
ATOM   1252  CG1AILE A 137       8.215   4.732   7.786  0.41 22.57           C  
ANISOU 1252  CG1AILE A 137     2958   3986   1633   1217    814    585       C  
ATOM   1253  CG1BILE A 137       7.472   6.535   7.584  0.60 23.84           C  
ANISOU 1253  CG1BILE A 137     3115   3263   2680    678   -286   -161       C  
ATOM   1254  CG2AILE A 137       6.850   6.258   9.181  0.41 19.87           C  
ANISOU 1254  CG2AILE A 137     2306   3924   1319    874    348    264       C  
ATOM   1255  CG2BILE A 137       8.133   4.340   8.457  0.60 23.28           C  
ANISOU 1255  CG2BILE A 137     2609   3605   2631   1351   -100   -257       C  
ATOM   1256  CD1AILE A 137       9.476   5.540   7.960  0.41 25.68           C  
ANISOU 1256  CD1AILE A 137     2622   4937   2198   1225    152   1236       C  
ATOM   1257  CD1BILE A 137       8.697   7.163   8.286  0.60 26.86           C  
ANISOU 1257  CD1BILE A 137     2558   4637   3009    555   -179     79       C  
ATOM   1258  N   LEU A 138       3.944   6.427   7.295  1.00 14.80           N  
ANISOU 1258  N   LEU A 138     2578   1877   1168    896    187    123       N  
ATOM   1259  CA  LEU A 138       2.794   7.275   7.677  1.00 13.99           C  
ANISOU 1259  CA  LEU A 138     2572   1498   1247    715    208      7       C  
ATOM   1260  C   LEU A 138       1.505   6.508   7.832  1.00 13.72           C  
ANISOU 1260  C   LEU A 138     2469   1697   1049    730    -92    218       C  
ATOM   1261  O   LEU A 138       0.699   6.813   8.751  1.00 15.42           O  
ANISOU 1261  O   LEU A 138     2390   2098   1372    595     48     68       O  
ATOM   1262  CB  LEU A 138       2.613   8.420   6.616  1.00 16.91           C  
ANISOU 1262  CB  LEU A 138     2967   1737   1723    846    446    441       C  
ATOM   1263  CG ALEU A 138       3.864   9.314   6.472  0.90 23.17           C  
ANISOU 1263  CG ALEU A 138     4179   2118   2505   -206    -47    536       C  
ATOM   1264  CG BLEU A 138       3.702   9.491   6.806  0.10 19.30           C  
ANISOU 1264  CG BLEU A 138     3322   1826   2186    568    744    388       C  
ATOM   1265  CD1ALEU A 138       3.520  10.417   5.469  0.90 23.70           C  
ANISOU 1265  CD1ALEU A 138     3927   2031   3047    182    537    753       C  
ATOM   1266  CD1BLEU A 138       4.158   9.495   8.258  0.10 12.99           C  
ANISOU 1266  CD1BLEU A 138     2254    701   1979    163   1246    579       C  
ATOM   1267  CD2ALEU A 138       4.335   9.906   7.778  0.90 24.29           C  
ANISOU 1267  CD2ALEU A 138     3881   2789   2559    -94    581   -170       C  
ATOM   1268  CD2BLEU A 138       4.879   9.271   5.873  0.10 17.75           C  
ANISOU 1268  CD2BLEU A 138     3637   1416   1691    157    771    -34       C  
ATOM   1269  N   ASP A 139       1.261   5.488   6.992  1.00 15.32           N  
ANISOU 1269  N   ASP A 139     2711   1906   1203    615   -345     45       N  
ATOM   1270  CA  ASP A 139       0.024   4.717   7.179  1.00 15.32           C  
ANISOU 1270  CA  ASP A 139     2503   2140   1179    681   -487    -78       C  
ATOM   1271  C   ASP A 139       0.129   3.840   8.427  1.00 14.27           C  
ANISOU 1271  C   ASP A 139     2261   1973   1185    523   -460   -132       C  
ATOM   1272  O   ASP A 139      -0.853   3.682   9.153  1.00 15.28           O  
ANISOU 1272  O   ASP A 139     2399   2003   1405    570   -421    -33       O  
ATOM   1273  CB  ASP A 139      -0.320   3.846   5.979  1.00 17.46           C  
ANISOU 1273  CB  ASP A 139     2964   2400   1271    511   -536   -222       C  
ATOM   1274  CG  ASP A 139      -0.788   4.687   4.797  1.00 21.49           C  
ANISOU 1274  CG  ASP A 139     3628   3033   1504    875  -1041   -246       C  
ATOM   1275  OD1 ASP A 139      -1.394   5.772   5.011  1.00 29.31           O  
ANISOU 1275  OD1 ASP A 139     5894   3204   2038   1770   -875    277       O  
ATOM   1276  OD2 ASP A 139      -0.572   4.221   3.679  1.00 31.38           O  
ANISOU 1276  OD2 ASP A 139     4949   5593   1380   2404   -702   -253       O  
ATOM   1277  N   THR A 140       1.321   3.285   8.727  1.00 13.67           N  
ANISOU 1277  N   THR A 140     2418   1803    974    674   -257    -77       N  
ATOM   1278  CA  THR A 140       1.450   2.524   9.962  1.00 11.95           C  
ANISOU 1278  CA  THR A 140     2068   1511    961    539   -182   -212       C  
ATOM   1279  C   THR A 140       1.245   3.464  11.157  1.00 11.35           C  
ANISOU 1279  C   THR A 140     2018   1318    977    481   -240    -79       C  
ATOM   1280  O   THR A 140       0.606   3.062  12.141  1.00 11.78           O  
ANISOU 1280  O   THR A 140     2022   1372   1080    485   -127    -74       O  
ATOM   1281  CB  THR A 140       2.857   1.894  10.017  1.00 12.60           C  
ANISOU 1281  CB  THR A 140     2302   1316   1170    631   -145   -131       C  
ATOM   1282  OG1 THR A 140       3.055   1.130   8.817  1.00 13.86           O  
ANISOU 1282  OG1 THR A 140     2404   1616   1245    494     34   -289       O  
ATOM   1283  CG2 THR A 140       3.026   0.991  11.242  1.00 12.60           C  
ANISOU 1283  CG2 THR A 140     2109   1364   1313    459   -266    -23       C  
ATOM   1284  N   TRP A 141       1.755   4.709  11.100  1.00 11.38           N  
ANISOU 1284  N   TRP A 141     2084   1312    928    536   -103    -73       N  
ATOM   1285  CA  TRP A 141       1.538   5.652  12.206  1.00 10.18           C  
ANISOU 1285  CA  TRP A 141     1686   1119   1062    357     -5    -78       C  
ATOM   1286  C   TRP A 141       0.037   5.903  12.440  1.00 10.23           C  
ANISOU 1286  C   TRP A 141     1786   1134    966    376    -25     52       C  
ATOM   1287  O   TRP A 141      -0.416   5.931  13.567  1.00 10.59           O  
ANISOU 1287  O   TRP A 141     1685   1323   1014    318     41     -4       O  
ATOM   1288  CB  TRP A 141       2.304   6.962  11.964  1.00 11.09           C  
ANISOU 1288  CB  TRP A 141     1929   1235   1051    291     54     35       C  
ATOM   1289  CG  TRP A 141       2.242   7.808  13.206  1.00  9.98           C  
ANISOU 1289  CG  TRP A 141     1695   1097    998    332     16     79       C  
ATOM   1290  CD1 TRP A 141       1.513   8.947  13.448  1.00 10.79           C  
ANISOU 1290  CD1 TRP A 141     1659   1287   1155    380    -11     19       C  
ATOM   1291  CD2 TRP A 141       2.961   7.532  14.413  1.00  9.58           C  
ANISOU 1291  CD2 TRP A 141     1512   1155    972    315    140    158       C  
ATOM   1292  NE1 TRP A 141       1.722   9.385  14.733  1.00 10.38           N  
ANISOU 1292  NE1 TRP A 141     1575   1189   1179    416    -15     42       N  
ATOM   1293  CE2 TRP A 141       2.617   8.508  15.344  1.00  9.37           C  
ANISOU 1293  CE2 TRP A 141     1533    980   1048    249     75    154       C  
ATOM   1294  CE3 TRP A 141       3.852   6.484  14.816  1.00 10.56           C  
ANISOU 1294  CE3 TRP A 141     1217   1353   1444    397    -20     23       C  
ATOM   1295  CZ2 TRP A 141       3.140   8.527  16.648  1.00 10.10           C  
ANISOU 1295  CZ2 TRP A 141     1454   1243   1141    111    -93     53       C  
ATOM   1296  CZ3 TRP A 141       4.331   6.517  16.097  1.00 11.06           C  
ANISOU 1296  CZ3 TRP A 141     1379   1250   1574    248   -214    145       C  
ATOM   1297  CH2 TRP A 141       3.994   7.513  17.001  1.00 11.09           C  
ANISOU 1297  CH2 TRP A 141     1466   1379   1371    166   -160    129       C  
ATOM   1298  N   ALA A 142      -0.733   6.091  11.355  1.00 12.10           N  
ANISOU 1298  N   ALA A 142     2002   1449   1148    518   -213    153       N  
ATOM   1299  CA  ALA A 142      -2.147   6.329  11.544  1.00 12.92           C  
ANISOU 1299  CA  ALA A 142     1970   1576   1362    538   -317    293       C  
ATOM   1300  C   ALA A 142      -2.826   5.143  12.226  1.00 11.99           C  
ANISOU 1300  C   ALA A 142     1884   1440   1232    621   -194     40       C  
ATOM   1301  O   ALA A 142      -3.715   5.321  13.045  1.00 12.97           O  
ANISOU 1301  O   ALA A 142     1765   1605   1556    490   -185    -29       O  
ATOM   1302  CB  ALA A 142      -2.838   6.582  10.158  1.00 17.41           C  
ANISOU 1302  CB  ALA A 142     2516   2438   1661    384   -691    631       C  
ATOM   1303  N   ALA A 143      -2.402   3.918  11.921  1.00 11.92           N  
ANISOU 1303  N   ALA A 143     1879   1422   1230    426   -367    -59       N  
ATOM   1304  CA  ALA A 143      -2.938   2.746  12.609  1.00 11.95           C  
ANISOU 1304  CA  ALA A 143     1828   1371   1341    262   -365   -133       C  
ATOM   1305  C   ALA A 143      -2.536   2.720  14.095  1.00 11.13           C  
ANISOU 1305  C   ALA A 143     1707   1254   1266    184   -207    -66       C  
ATOM   1306  O   ALA A 143      -3.326   2.260  14.957  1.00 13.16           O  
ANISOU 1306  O   ALA A 143     1672   1702   1626      5   -231     80       O  
ATOM   1307  CB  ALA A 143      -2.479   1.437  11.932  1.00 14.48           C  
ANISOU 1307  CB  ALA A 143     2687   1449   1367    393   -364   -272       C  
ATOM   1308  N   MET A 144      -1.330   3.168  14.411  1.00 10.58           N  
ANISOU 1308  N   MET A 144     1559   1203   1257    266   -283    -61       N  
ATOM   1309  CA  MET A 144      -0.912   3.282  15.804  1.00  9.84           C  
ANISOU 1309  CA  MET A 144     1342   1291   1107    335   -124     99       C  
ATOM   1310  C   MET A 144      -1.784   4.291  16.575  1.00  9.26           C  
ANISOU 1310  C   MET A 144     1250   1134   1133    153   -121     83       C  
ATOM   1311  O   MET A 144      -2.125   4.102  17.729  1.00  9.97           O  
ANISOU 1311  O   MET A 144     1223   1430   1136    238    -34    197       O  
ATOM   1312  CB  MET A 144       0.570   3.683  15.876  1.00 10.16           C  
ANISOU 1312  CB  MET A 144     1266   1265   1328    220    -42     42       C  
ATOM   1313  CG  MET A 144       1.528   2.621  15.315  1.00 11.56           C  
ANISOU 1313  CG  MET A 144     1582   1642   1169    576     30    146       C  
ATOM   1314  SD  MET A 144       1.784   1.180  16.358  1.00 11.48           S  
ANISOU 1314  SD  MET A 144     1636   1418   1307    461   -192    -49       S  
ATOM   1315  CE  MET A 144       2.897   1.836  17.581  1.00 11.57           C  
ANISOU 1315  CE  MET A 144     1524   1667   1203    158   -173    156       C  
ATOM   1316  N   GLU A 145      -2.089   5.433  15.894  1.00  9.85           N  
ANISOU 1316  N   GLU A 145     1440   1118   1185    347    -69     52       N  
ATOM   1317  CA  GLU A 145      -2.918   6.446  16.533  1.00 10.20           C  
ANISOU 1317  CA  GLU A 145     1481   1129   1266    353    -26    109       C  
ATOM   1318  C   GLU A 145      -4.288   5.881  16.915  1.00  9.89           C  
ANISOU 1318  C   GLU A 145     1414   1194   1152    375    -56     66       C  
ATOM   1319  O   GLU A 145      -4.843   6.225  17.964  1.00 11.13           O  
ANISOU 1319  O   GLU A 145     1514   1416   1300    356     43    -66       O  
ATOM   1320  CB  GLU A 145      -3.100   7.657  15.601  1.00 10.62           C  
ANISOU 1320  CB  GLU A 145     1580   1226   1231    332    -54    185       C  
ATOM   1321  CG  GLU A 145      -1.779   8.448  15.446  1.00 10.62           C  
ANISOU 1321  CG  GLU A 145     1599   1185   1249    303    -93    249       C  
ATOM   1322  CD  GLU A 145      -1.932   9.605  14.461  1.00 10.42           C  
ANISOU 1322  CD  GLU A 145     1659   1088   1213    421    -65     94       C  
ATOM   1323  OE1 GLU A 145      -2.659   9.428  13.448  1.00 13.35           O  
ANISOU 1323  OE1 GLU A 145     2287   1441   1343    217   -453    193       O  
ATOM   1324  OE2 GLU A 145      -1.319  10.663  14.702  1.00 11.34           O  
ANISOU 1324  OE2 GLU A 145     1901   1044   1363    400   -104     42       O  
ATOM   1325  N   GLU A 146      -4.851   5.010  16.074  1.00 10.52           N  
ANISOU 1325  N   GLU A 146     1341   1438   1217    304   -131     48       N  
ATOM   1326  CA  GLU A 146      -6.141   4.402  16.388  1.00 10.94           C  
ANISOU 1326  CA  GLU A 146     1340   1536   1282    216   -190     31       C  
ATOM   1327  C   GLU A 146      -6.086   3.582  17.672  1.00 10.46           C  
ANISOU 1327  C   GLU A 146     1182   1587   1207    154   -171    -57       C  
ATOM   1328  O   GLU A 146      -7.098   3.516  18.399  1.00 12.33           O  
ANISOU 1328  O   GLU A 146     1173   1989   1522    151    -76    122       O  
ATOM   1329  CB  GLU A 146      -6.582   3.533  15.235  1.00 14.66           C  
ANISOU 1329  CB  GLU A 146     1716   2649   1203   -125   -335   -206       C  
ATOM   1330  CG AGLU A 146      -6.987   4.329  14.008  0.38 15.61           C  
ANISOU 1330  CG AGLU A 146     2195   2313   1424   -151   -529   -164       C  
ATOM   1331  CG BGLU A 146      -7.933   2.841  15.404  0.62 22.22           C  
ANISOU 1331  CG BGLU A 146     1917   4617   1910   -927   -295   -879       C  
ATOM   1332  CD AGLU A 146      -8.445   4.749  14.002  0.38 27.69           C  
ANISOU 1332  CD AGLU A 146     2724   4468   3328   1087   -601    685       C  
ATOM   1333  OE1AGLU A 146      -8.960   4.977  12.875  0.38 31.74           O  
ANISOU 1333  OE1AGLU A 146     2083   5843   4133   -981  -1188   2145       O  
ATOM   1334  OE2AGLU A 146      -9.075   4.850  15.082  0.38 31.82           O  
ANISOU 1334  OE2AGLU A 146     1420   6761   3908    230   -540    -69       O  
ATOM   1335  N   LEU A 147      -4.935   2.956  17.973  1.00 10.19           N  
ANISOU 1335  N   LEU A 147     1333   1364   1175    259   -179     -2       N  
ATOM   1336  CA  LEU A 147      -4.851   2.205  19.239  1.00 10.17           C  
ANISOU 1336  CA  LEU A 147     1384   1337   1143    262   -110    -32       C  
ATOM   1337  C   LEU A 147      -4.997   3.102  20.451  1.00  9.64           C  
ANISOU 1337  C   LEU A 147     1138   1368   1157    309     12     40       C  
ATOM   1338  O   LEU A 147      -5.519   2.665  21.490  1.00 11.76           O  
ANISOU 1338  O   LEU A 147     1555   1633   1280    206    233    141       O  
ATOM   1339  CB  LEU A 147      -3.472   1.484  19.304  1.00 10.12           C  
ANISOU 1339  CB  LEU A 147     1394   1309   1143    383     28    -23       C  
ATOM   1340  CG  LEU A 147      -3.154   0.546  18.151  1.00 12.06           C  
ANISOU 1340  CG  LEU A 147     1716   1535   1332    464    -37   -110       C  
ATOM   1341  CD1 LEU A 147      -1.722  -0.015  18.350  1.00 15.03           C  
ANISOU 1341  CD1 LEU A 147     2225   2140   1345   1160    178    236       C  
ATOM   1342  CD2 LEU A 147      -4.189  -0.563  18.049  1.00 18.11           C  
ANISOU 1342  CD2 LEU A 147     2914   1723   2247   -167    182   -637       C  
ATOM   1343  N   VAL A 148      -4.480   4.334  20.373  1.00  9.94           N  
ANISOU 1343  N   VAL A 148     1313   1257   1207    290    -56    -55       N  
ATOM   1344  CA  VAL A 148      -4.670   5.311  21.492  1.00 10.28           C  
ANISOU 1344  CA  VAL A 148     1234   1419   1255    352      9   -175       C  
ATOM   1345  C   VAL A 148      -6.157   5.630  21.630  1.00 11.21           C  
ANISOU 1345  C   VAL A 148     1347   1623   1289    454      6    -33       C  
ATOM   1346  O   VAL A 148      -6.705   5.609  22.728  1.00 12.91           O  
ANISOU 1346  O   VAL A 148     1322   2289   1292    535     37   -166       O  
ATOM   1347  CB  VAL A 148      -3.845   6.577  21.224  1.00 11.51           C  
ANISOU 1347  CB  VAL A 148     1491   1395   1488    309    -76   -279       C  
ATOM   1348  CG1 VAL A 148      -4.092   7.615  22.357  1.00 14.20           C  
ANISOU 1348  CG1 VAL A 148     1955   1721   1718    246     -6   -564       C  
ATOM   1349  CG2 VAL A 148      -2.344   6.275  21.094  1.00 13.04           C  
ANISOU 1349  CG2 VAL A 148     1287   1837   1832    270    -54   -202       C  
ATOM   1350  N   ASP A 149      -6.828   5.883  20.499  1.00 11.88           N  
ANISOU 1350  N   ASP A 149     1361   1745   1406    658   -195   -110       N  
ATOM   1351  CA  ASP A 149      -8.255   6.258  20.570  1.00 13.03           C  
ANISOU 1351  CA  ASP A 149     1367   2003   1583    570    -60     30       C  
ATOM   1352  C   ASP A 149      -9.132   5.118  21.015  1.00 12.81           C  
ANISOU 1352  C   ASP A 149     1478   2182   1208    662     33    300       C  
ATOM   1353  O   ASP A 149     -10.253   5.369  21.488  1.00 16.52           O  
ANISOU 1353  O   ASP A 149     1727   2630   1918    859    525    561       O  
ATOM   1354  CB  ASP A 149      -8.694   6.749  19.167  1.00 13.65           C  
ANISOU 1354  CB  ASP A 149     1367   1900   1917    252   -216    519       C  
ATOM   1355  CG  ASP A 149      -8.120   8.156  18.949  1.00 16.74           C  
ANISOU 1355  CG  ASP A 149     1905   1559   2896    610     10    397       C  
ATOM   1356  OD1 ASP A 149      -7.893   8.948  19.859  1.00 22.87           O  
ANISOU 1356  OD1 ASP A 149     2601   1919   4168    223     -1   -325       O  
ATOM   1357  OD2 ASP A 149      -7.891   8.511  17.808  1.00 23.04           O  
ANISOU 1357  OD2 ASP A 149     3035   2095   3625    514    753   1133       O  
ATOM   1358  N   GLU A 150      -8.691   3.880  20.854  1.00 12.69           N  
ANISOU 1358  N   GLU A 150     1097   2061   1664    333     23    138       N  
ATOM   1359  CA  GLU A 150      -9.478   2.720  21.300  1.00 14.00           C  
ANISOU 1359  CA  GLU A 150     1402   2234   1684    166    -10    236       C  
ATOM   1360  C   GLU A 150      -9.127   2.318  22.734  1.00 14.07           C  
ANISOU 1360  C   GLU A 150     1272   2331   1743    435    214    383       C  
ATOM   1361  O   GLU A 150      -9.729   1.395  23.245  1.00 18.14           O  
ANISOU 1361  O   GLU A 150     1667   3093   2134     58    358    704       O  
ATOM   1362  CB AGLU A 150      -9.363   1.551  20.335  0.35 15.73           C  
ANISOU 1362  CB AGLU A 150     1488   2314   2174     97   -228   -110       C  
ATOM   1363  CB BGLU A 150      -9.196   1.552  20.380  0.65 15.76           C  
ANISOU 1363  CB BGLU A 150     1871   2132   1984     25    273    123       C  
ATOM   1364  CG AGLU A 150     -10.128   1.834  19.022  0.35 17.44           C  
ANISOU 1364  CG AGLU A 150     1970   2609   2046   -636   -301     88       C  
ATOM   1365  CG BGLU A 150      -9.740   1.810  18.958  0.65 22.06           C  
ANISOU 1365  CG BGLU A 150     2427   4073   1880  -1065      1   -165       C  
ATOM   1366  CD AGLU A 150      -9.939   0.675  18.059  0.35 22.22           C  
ANISOU 1366  CD AGLU A 150     1709   3962   2773  -1165   -113  -1083       C  
ATOM   1367  CD BGLU A 150      -9.378   0.647  18.053  0.65 27.99           C  
ANISOU 1367  CD BGLU A 150     4063   4531   2040   -271   -270   -380       C  
ATOM   1368  OE1AGLU A 150      -9.793   0.953  16.846  0.35 35.83           O  
ANISOU 1368  OE1AGLU A 150     5276   5715   2625   -754     58  -1188       O  
ATOM   1369  OE1BGLU A 150      -8.256   0.092  18.162  0.65 40.04           O  
ANISOU 1369  OE1BGLU A 150     5211   3567   6437    488  -1887  -1535       O  
ATOM   1370  OE2AGLU A 150      -9.912  -0.471  18.553  0.35 23.60           O  
ANISOU 1370  OE2AGLU A 150     2316   3543   3106    819   -516  -1650       O  
ATOM   1371  OE2BGLU A 150     -10.245   0.299  17.232  0.65 35.52           O  
ANISOU 1371  OE2BGLU A 150     4042   4877   4574   -959   -543  -1881       O  
ATOM   1372  N   GLY A 151      -8.111   2.968  23.365  1.00 13.70           N  
ANISOU 1372  N   GLY A 151     1204   2372   1630    701     70    158       N  
ATOM   1373  CA  GLY A 151      -7.816   2.685  24.753  1.00 15.38           C  
ANISOU 1373  CA  GLY A 151     1586   2684   1575    879    195    154       C  
ATOM   1374  C   GLY A 151      -6.876   1.505  24.963  1.00 12.63           C  
ANISOU 1374  C   GLY A 151     1526   1988   1285    414    208    270       C  
ATOM   1375  O   GLY A 151      -6.625   1.143  26.097  1.00 16.35           O  
ANISOU 1375  O   GLY A 151     2265   2544   1404    856    315    296       O  
ATOM   1376  N   LEU A 152      -6.292   0.947  23.900  1.00 10.81           N  
ANISOU 1376  N   LEU A 152     1085   1563   1460    122     11    125       N  
ATOM   1377  CA  LEU A 152      -5.366  -0.218  24.063  1.00 10.44           C  
ANISOU 1377  CA  LEU A 152     1053   1581   1331    136     -5    118       C  
ATOM   1378  C   LEU A 152      -3.993   0.221  24.533  1.00  9.25           C  
ANISOU 1378  C   LEU A 152     1160   1244   1111     81     83    111       C  
ATOM   1379  O   LEU A 152      -3.264  -0.598  25.158  1.00 10.37           O  
ANISOU 1379  O   LEU A 152     1277   1374   1290     95   -129    175       O  
ATOM   1380  CB  LEU A 152      -5.246  -0.960  22.745  1.00 11.27           C  
ANISOU 1380  CB  LEU A 152     1304   1458   1519    -92   -142     28       C  
ATOM   1381  CG ALEU A 152      -6.311  -2.006  22.381  0.53 14.12           C  
ANISOU 1381  CG ALEU A 152     1358   2252   1755   -388   -198   -170       C  
ATOM   1382  CG BLEU A 152      -6.605  -1.508  22.237  0.47 14.43           C  
ANISOU 1382  CG BLEU A 152     1392   2308   1784   -291   -402    143       C  
ATOM   1383  CD1ALEU A 152      -7.603  -1.305  22.048  0.53 18.45           C  
ANISOU 1383  CD1ALEU A 152     1373   2604   3033   -146   -229   -479       C  
ATOM   1384  CD1BLEU A 152      -6.418  -2.034  20.829  0.47 18.82           C  
ANISOU 1384  CD1BLEU A 152     2102   2795   2253   -198   -587   -608       C  
ATOM   1385  CD2ALEU A 152      -5.798  -2.889  21.250  0.53 15.76           C  
ANISOU 1385  CD2ALEU A 152     2491   1383   2114    130   -401   -130       C  
ATOM   1386  CD2BLEU A 152      -7.134  -2.567  23.193  0.47 20.29           C  
ANISOU 1386  CD2BLEU A 152     1790   3010   2911  -1114   -830    866       C  
ATOM   1387  N   VAL A 153      -3.576   1.433  24.190  1.00  9.29           N  
ANISOU 1387  N   VAL A 153     1178   1234   1116     78      2      1       N  
ATOM   1388  CA  VAL A 153      -2.230   1.923  24.550  1.00  9.12           C  
ANISOU 1388  CA  VAL A 153     1096   1109   1260    115    -14   -186       C  
ATOM   1389  C   VAL A 153      -2.388   3.341  24.996  1.00  9.35           C  
ANISOU 1389  C   VAL A 153     1184   1152   1218    169     -2    -63       C  
ATOM   1390  O   VAL A 153      -3.221   4.094  24.483  1.00 11.90           O  
ANISOU 1390  O   VAL A 153     1435   1471   1617    447   -289   -181       O  
ATOM   1391  CB  VAL A 153      -1.235   1.785  23.374  1.00 10.39           C  
ANISOU 1391  CB  VAL A 153     1342   1278   1329     38    227   -111       C  
ATOM   1392  CG1 VAL A 153      -1.238   0.355  22.819  1.00 10.99           C  
ANISOU 1392  CG1 VAL A 153     1309   1399   1469     62    195   -304       C  
ATOM   1393  CG2 VAL A 153      -1.460   2.798  22.312  1.00 13.62           C  
ANISOU 1393  CG2 VAL A 153     2000   1691   1484     99    250     98       C  
ATOM   1394  N   LYS A 154      -1.548   3.775  25.968  1.00  9.26           N  
ANISOU 1394  N   LYS A 154     1173   1227   1118    154     89   -144       N  
ATOM   1395  CA  LYS A 154      -1.610   5.158  26.450  1.00  9.65           C  
ANISOU 1395  CA  LYS A 154     1296   1229   1140    137    146   -168       C  
ATOM   1396  C   LYS A 154      -0.721   6.121  25.655  1.00  9.17           C  
ANISOU 1396  C   LYS A 154     1229   1124   1132    306    138    -91       C  
ATOM   1397  O   LYS A 154      -1.021   7.321  25.647  1.00 12.96           O  
ANISOU 1397  O   LYS A 154     1734   1202   1987    331    564   -126       O  
ATOM   1398  CB  LYS A 154      -1.197   5.229  27.936  1.00 11.17           C  
ANISOU 1398  CB  LYS A 154     1721   1498   1025    180    188   -125       C  
ATOM   1399  CG ALYS A 154      -2.391   4.609  28.724  0.53 13.53           C  
ANISOU 1399  CG ALYS A 154     1818   2203   1119    -36     58    314       C  
ATOM   1400  CG BLYS A 154      -1.910   4.408  28.989  0.47 12.76           C  
ANISOU 1400  CG BLYS A 154     1666   2057   1127     25    330    -90       C  
ATOM   1401  CD ALYS A 154      -2.141   4.816  30.205  0.53 17.23           C  
ANISOU 1401  CD ALYS A 154     2968   2537   1042   -442    549   -282       C  
ATOM   1402  CD BLYS A 154      -3.336   4.855  29.161  0.47 16.55           C  
ANISOU 1402  CD BLYS A 154     1710   2630   1949    260    339    297       C  
ATOM   1403  CE ALYS A 154      -3.119   5.970  30.579  0.53 31.13           C  
ANISOU 1403  CE ALYS A 154     6772   2540   2515   1377   -339   -893       C  
ATOM   1404  CE BLYS A 154      -3.862   4.291  30.501  0.47 17.64           C  
ANISOU 1404  CE BLYS A 154     1753   2690   2260    779    845    393       C  
ATOM   1405  NZ ALYS A 154      -2.392   7.253  30.366  0.53 42.07           N  
ANISOU 1405  NZ ALYS A 154     8040   2824   5122    479  -1485  -1050       N  
ATOM   1406  NZ BLYS A 154      -5.362   4.290  30.450  0.47 27.48           N  
ANISOU 1406  NZ BLYS A 154     1765   6264   2413    120    734    -79       N  
ATOM   1407  N   ALA A 155       0.332   5.638  25.053  1.00 10.02           N  
ANISOU 1407  N   ALA A 155     1394   1266   1145    289    286    -19       N  
ATOM   1408  CA  ALA A 155       1.272   6.465  24.284  1.00 10.20           C  
ANISOU 1408  CA  ALA A 155     1394   1227   1254     96    367   -182       C  
ATOM   1409  C   ALA A 155       1.821   5.589  23.188  1.00  8.38           C  
ANISOU 1409  C   ALA A 155     1186    996   1003    229    112     16       C  
ATOM   1410  O   ALA A 155       1.950   4.367  23.332  1.00  9.24           O  
ANISOU 1410  O   ALA A 155     1449   1109    953    278    211     50       O  
ATOM   1411  CB  ALA A 155       2.414   6.964  25.175  1.00 13.51           C  
ANISOU 1411  CB  ALA A 155     1911   1807   1414   -306    314   -536       C  
ATOM   1412  N   ILE A 156       2.244   6.237  22.090  1.00  8.47           N  
ANISOU 1412  N   ILE A 156     1160   1003   1054    196    161    -30       N  
ATOM   1413  CA  ILE A 156       2.880   5.566  20.977  1.00  7.93           C  
ANISOU 1413  CA  ILE A 156     1129    985    899    167     59    -43       C  
ATOM   1414  C   ILE A 156       4.207   6.242  20.666  1.00  7.25           C  
ANISOU 1414  C   ILE A 156     1090    780    886    188    -16     18       C  
ATOM   1415  O   ILE A 156       4.433   7.433  20.925  1.00  9.16           O  
ANISOU 1415  O   ILE A 156     1272    924   1283    144    152   -178       O  
ATOM   1416  CB  ILE A 156       1.939   5.516  19.733  1.00  8.45           C  
ANISOU 1416  CB  ILE A 156     1061    995   1153    122    -82    107       C  
ATOM   1417  CG1 ILE A 156       1.350   6.902  19.394  1.00 10.04           C  
ANISOU 1417  CG1 ILE A 156     1325   1111   1378    313   -152    214       C  
ATOM   1418  CG2 ILE A 156       0.858   4.455  20.005  1.00  9.22           C  
ANISOU 1418  CG2 ILE A 156     1153   1153   1198     25    -14     72       C  
ATOM   1419  CD1 ILE A 156       0.534   6.872  18.102  1.00 12.49           C  
ANISOU 1419  CD1 ILE A 156     1497   1540   1707    203   -506    384       C  
ATOM   1420  N   GLY A 157       5.121   5.466  20.077  1.00  7.61           N  
ANISOU 1420  N   GLY A 157     1053    849    989    152     97      0       N  
ATOM   1421  CA  GLY A 157       6.408   5.991  19.694  1.00  7.66           C  
ANISOU 1421  CA  GLY A 157     1061    890    957     83     74    -98       C  
ATOM   1422  C   GLY A 157       7.078   5.112  18.629  1.00  6.85           C  
ANISOU 1422  C   GLY A 157     1049    769    783     51    -57     90       C  
ATOM   1423  O   GLY A 157       6.428   4.293  17.993  1.00  7.30           O  
ANISOU 1423  O   GLY A 157     1045    800    930     74    -16    -49       O  
ATOM   1424  N   ILE A 158       8.382   5.363  18.484  1.00  7.08           N  
ANISOU 1424  N   ILE A 158     1043    857    791    120     53     56       N  
ATOM   1425  CA  ILE A 158       9.152   4.790  17.383  1.00  7.04           C  
ANISOU 1425  CA  ILE A 158     1081    863    731    131     39     58       C  
ATOM   1426  C   ILE A 158      10.484   4.245  17.940  1.00  6.46           C  
ANISOU 1426  C   ILE A 158     1046    654    755    -23     27     30       C  
ATOM   1427  O   ILE A 158      10.887   4.560  19.065  1.00  7.15           O  
ANISOU 1427  O   ILE A 158     1105    840    773    133    -32    -58       O  
ATOM   1428  CB  ILE A 158       9.349   5.840  16.261  1.00  8.12           C  
ANISOU 1428  CB  ILE A 158     1186   1003    894    148     21    240       C  
ATOM   1429  CG1 ILE A 158      10.088   7.074  16.799  1.00 11.15           C  
ANISOU 1429  CG1 ILE A 158     1756   1109   1372   -255   -173    440       C  
ATOM   1430  CG2 ILE A 158       8.006   6.169  15.617  1.00  9.83           C  
ANISOU 1430  CG2 ILE A 158     1409   1387    941    255   -170    185       C  
ATOM   1431  CD1AILE A 158      10.175   8.293  15.895  0.69 10.43           C  
ANISOU 1431  CD1AILE A 158     1816    942   1205   -126    451    182       C  
ATOM   1432  CD1BILE A 158       9.521   8.065  17.654  0.31 30.00           C  
ANISOU 1432  CD1BILE A 158     3618   2654   5128    130   -460  -2287       C  
ATOM   1433  N   SER A 159      11.153   3.452  17.119  1.00  6.98           N  
ANISOU 1433  N   SER A 159     1042    833    778    142     13    -58       N  
ATOM   1434  CA  SER A 159      12.430   2.863  17.511  1.00  6.62           C  
ANISOU 1434  CA  SER A 159     1059    759    697    119     58     47       C  
ATOM   1435  C   SER A 159      13.249   2.678  16.242  1.00  6.35           C  
ANISOU 1435  C   SER A 159     1103    707    600     39     13     83       C  
ATOM   1436  O   SER A 159      12.762   2.290  15.201  1.00  7.37           O  
ANISOU 1436  O   SER A 159     1191    964    645      8     15     56       O  
ATOM   1437  CB  SER A 159      12.185   1.561  18.232  1.00  7.60           C  
ANISOU 1437  CB  SER A 159     1104    943    840    118    134    148       C  
ATOM   1438  OG  SER A 159      13.419   0.976  18.695  1.00  9.20           O  
ANISOU 1438  OG  SER A 159     1414   1028   1052    268    118    271       O  
ATOM   1439  N   ASN A 160      14.563   3.054  16.359  1.00  6.98           N  
ANISOU 1439  N   ASN A 160     1099    816    739     42     85     80       N  
ATOM   1440  CA  ASN A 160      15.504   2.916  15.235  1.00  7.08           C  
ANISOU 1440  CA  ASN A 160     1086    886    718     41     99     81       C  
ATOM   1441  C   ASN A 160      15.126   3.826  14.055  1.00  7.83           C  
ANISOU 1441  C   ASN A 160     1308    824    842     44    144    181       C  
ATOM   1442  O   ASN A 160      15.426   3.503  12.905  1.00 10.46           O  
ANISOU 1442  O   ASN A 160     1896   1246    832    413    329    279       O  
ATOM   1443  CB  ASN A 160      15.632   1.475  14.744  1.00  7.56           C  
ANISOU 1443  CB  ASN A 160     1299    856    717    151    121     98       C  
ATOM   1444  CG  ASN A 160      16.070   0.560  15.857  1.00  6.78           C  
ANISOU 1444  CG  ASN A 160     1034    829    711    106     40    -45       C  
ATOM   1445  OD1 ASN A 160      17.192   0.706  16.369  1.00  8.37           O  
ANISOU 1445  OD1 ASN A 160     1219   1008    953     29    -23    171       O  
ATOM   1446  ND2 ASN A 160      15.202  -0.358  16.261  1.00  7.47           N  
ANISOU 1446  ND2 ASN A 160     1257    860    722     12     99     55       N  
ATOM   1447  N   PHE A 161      14.462   4.962  14.338  1.00  8.02           N  
ANISOU 1447  N   PHE A 161     1341    759    947     37     65    223       N  
ATOM   1448  CA  PHE A 161      14.171   5.935  13.265  1.00  8.16           C  
ANISOU 1448  CA  PHE A 161     1376    814    910     51     71    316       C  
ATOM   1449  C   PHE A 161      15.285   6.984  13.226  1.00  8.55           C  
ANISOU 1449  C   PHE A 161     1331    933    985      0      8    278       C  
ATOM   1450  O   PHE A 161      15.728   7.504  14.262  1.00 10.09           O  
ANISOU 1450  O   PHE A 161     1585   1192   1058   -224    116    151       O  
ATOM   1451  CB  PHE A 161      12.840   6.649  13.511  1.00  9.23           C  
ANISOU 1451  CB  PHE A 161     1363    872   1274     98     78    252       C  
ATOM   1452  CG  PHE A 161      11.605   5.888  13.120  1.00  8.60           C  
ANISOU 1452  CG  PHE A 161     1303   1110    856    110     92    180       C  
ATOM   1453  CD1 PHE A 161      11.405   4.561  13.442  1.00  8.38           C  
ANISOU 1453  CD1 PHE A 161     1300   1005    878     19     97     90       C  
ATOM   1454  CD2 PHE A 161      10.564   6.549  12.424  1.00 10.54           C  
ANISOU 1454  CD2 PHE A 161     1469   1440   1095    208    -13    325       C  
ATOM   1455  CE1 PHE A 161      10.242   3.870  13.097  1.00  9.71           C  
ANISOU 1455  CE1 PHE A 161     1375   1342    970     -7     84   -158       C  
ATOM   1456  CE2 PHE A 161       9.433   5.826  12.074  1.00 11.97           C  
ANISOU 1456  CE2 PHE A 161     1480   1801   1268     84    -94    264       C  
ATOM   1457  CZ  PHE A 161       9.241   4.532  12.409  1.00 10.88           C  
ANISOU 1457  CZ  PHE A 161     1372   1660   1102      2      2   -102       C  
ATOM   1458  N   ASN A 162      15.765   7.268  11.997  1.00  9.35           N  
ANISOU 1458  N   ASN A 162     1485   1041   1028    -31    167    355       N  
ATOM   1459  CA  ASN A 162      16.704   8.350  11.806  1.00  9.27           C  
ANISOU 1459  CA  ASN A 162     1375    963   1184   -111    183    294       C  
ATOM   1460  C   ASN A 162      15.990   9.700  11.787  1.00  9.61           C  
ANISOU 1460  C   ASN A 162     1397   1084   1170    -77    195    293       C  
ATOM   1461  O   ASN A 162      14.764   9.785  11.817  1.00 10.46           O  
ANISOU 1461  O   ASN A 162     1486   1118   1371    -14    195    406       O  
ATOM   1462  CB  ASN A 162      17.588   8.092  10.553  1.00 10.58           C  
ANISOU 1462  CB  ASN A 162     1291   1500   1227    -12    240    281       C  
ATOM   1463  CG  ASN A 162      16.865   8.250   9.213  1.00 10.86           C  
ANISOU 1463  CG  ASN A 162     1594   1340   1192     28    243    393       C  
ATOM   1464  OD1 ASN A 162      16.020   9.127   9.070  1.00 12.43           O  
ANISOU 1464  OD1 ASN A 162     1842   1586   1296    292    157    389       O  
ATOM   1465  ND2 ASN A 162      17.254   7.455   8.224  1.00 12.05           N  
ANISOU 1465  ND2 ASN A 162     1861   1466   1252    -25    278    223       N  
ATOM   1466  N  AHIS A 163      16.743  10.818  11.735  0.83 11.25           N  
ANISOU 1466  N  AHIS A 163     1660    997   1617   -115     66    377       N  
ATOM   1467  N  BHIS A 163      16.792  10.771  11.709  0.17 10.36           N  
ANISOU 1467  N  BHIS A 163     1662   1004   1271   -135    288    497       N  
ATOM   1468  CA AHIS A 163      16.010  12.103  11.975  0.83 11.02           C  
ANISOU 1468  CA AHIS A 163     1652    966   1568   -108   -112    239       C  
ATOM   1469  CA BHIS A 163      16.230  12.125  11.741  0.17 10.09           C  
ANISOU 1469  CA BHIS A 163     1409   1060   1367   -168    364    333       C  
ATOM   1470  C  AHIS A 163      15.097  12.448  10.809  0.83 10.49           C  
ANISOU 1470  C  AHIS A 163     1347   1188   1452   -182    155    471       C  
ATOM   1471  C  BHIS A 163      15.339  12.392  10.534  0.17 11.27           C  
ANISOU 1471  C  BHIS A 163     1681    997   1603    151    157    170       C  
ATOM   1472  O  AHIS A 163      14.111  13.120  11.045  0.83 12.06           O  
ANISOU 1472  O  AHIS A 163     1547   1373   1664     41    167    431       O  
ATOM   1473  O  BHIS A 163      14.378  13.153  10.656  0.17 14.09           O  
ANISOU 1473  O  BHIS A 163     1920   1586   1848    535    300    322       O  
ATOM   1474  CB AHIS A 163      16.997  13.252  12.295  0.83 12.69           C  
ANISOU 1474  CB AHIS A 163     1826   1195   1800   -380    -22    326       C  
ATOM   1475  CB BHIS A 163      17.331  13.185  11.828  0.17 12.27           C  
ANISOU 1475  CB BHIS A 163     1435   1001   2228   -228     46   1076       C  
ATOM   1476  CG AHIS A 163      17.579  13.941  11.133  0.83 14.35           C  
ANISOU 1476  CG AHIS A 163     1702   1595   2154   -249     -7    803       C  
ATOM   1477  CG BHIS A 163      17.788  13.794  10.552  0.17 14.22           C  
ANISOU 1477  CG BHIS A 163     2002   1219   2181   -443     12   1049       C  
ATOM   1478  ND1AHIS A 163      18.581  13.404  10.307  0.83 15.63           N  
ANISOU 1478  ND1AHIS A 163     1992   1937   2011   -337    189    743       N  
ATOM   1479  ND1BHIS A 163      18.847  13.240   9.856  0.17 15.36           N  
ANISOU 1479  ND1BHIS A 163     1989   1962   1886   -392     48   1043       N  
ATOM   1480  CD2AHIS A 163      17.375  15.228  10.704  0.83 19.02           C  
ANISOU 1480  CD2AHIS A 163     2357   1813   3055    -86     68   1212       C  
ATOM   1481  CD2BHIS A 163      17.418  14.882   9.830  0.17 17.54           C  
ANISOU 1481  CD2BHIS A 163     2487   1726   2453   -299    192   1524       C  
ATOM   1482  CE1AHIS A 163      18.909  14.335   9.392  0.83 19.27           C  
ANISOU 1482  CE1AHIS A 163     2354   2355   2611   -509    281   1209       C  
ATOM   1483  CE1BHIS A 163      19.098  13.947   8.759  0.17 17.45           C  
ANISOU 1483  CE1BHIS A 163     2353   2138   2140   -436     74   1299       C  
ATOM   1484  NE2AHIS A 163      18.187  15.427   9.613  0.83 21.49           N  
ANISOU 1484  NE2AHIS A 163     3067   2207   2892   -290    214   1428       N  
ATOM   1485  NE2BHIS A 163      18.232  14.950   8.722  0.17 18.72           N  
ANISOU 1485  NE2BHIS A 163     2461   1872   2779   -554    402   1539       N  
ATOM   1486  N  ALEU A 164      15.415  12.024   9.561  0.83 11.25           N  
ANISOU 1486  N  ALEU A 164     1640   1209   1424    -19    128    478       N  
ATOM   1487  N  BLEU A 164      15.634  11.794   9.380  0.17 10.85           N  
ANISOU 1487  N  BLEU A 164     1731   1012   1379    -85    265    336       N  
ATOM   1488  CA ALEU A 164      14.499  12.301   8.454  0.83 11.32           C  
ANISOU 1488  CA ALEU A 164     1772   1264   1263     34    211    489       C  
ATOM   1489  CA BLEU A 164      14.751  12.029   8.235  0.17 11.87           C  
ANISOU 1489  CA BLEU A 164     1829   1042   1637    -66     48    323       C  
ATOM   1490  C  ALEU A 164      13.232  11.485   8.598  0.83 11.40           C  
ANISOU 1490  C  ALEU A 164     1610   1399   1324    131    161    457       C  
ATOM   1491  C  BLEU A 164      13.369  11.426   8.487  0.17 11.47           C  
ANISOU 1491  C  BLEU A 164     1723   1311   1324    100    209    454       C  
ATOM   1492  O  ALEU A 164      12.141  11.955   8.186  0.83 12.74           O  
ANISOU 1492  O  ALEU A 164     1688   1650   1502    315    202    534       O  
ATOM   1493  O  BLEU A 164      12.364  12.010   8.067  0.17 16.11           O  
ANISOU 1493  O  BLEU A 164     1895   1445   2780   -348   -613   1014       O  
ATOM   1494  CB ALEU A 164      15.196  11.956   7.088  0.83 13.46           C  
ANISOU 1494  CB ALEU A 164     1957   1707   1449    202    421    410       C  
ATOM   1495  CB BLEU A 164      15.355  11.451   6.954  0.17 12.75           C  
ANISOU 1495  CB BLEU A 164     1594   1910   1341    -27    141    585       C  
ATOM   1496  CG ALEU A 164      16.427  12.794   6.753  0.83 18.80           C  
ANISOU 1496  CG ALEU A 164     2034   3097   2011      4    532   1019       C  
ATOM   1497  CG BLEU A 164      14.514  11.429   5.686  0.17 19.43           C  
ANISOU 1497  CG BLEU A 164     2705   3030   1648   -189   -434    367       C  
ATOM   1498  CD1ALEU A 164      17.029  12.358   5.416  0.83 27.26           C  
ANISOU 1498  CD1ALEU A 164     2866   5430   2061    497   1086   1416       C  
ATOM   1499  CD1BLEU A 164      15.355  11.708   4.444  0.17 21.26           C  
ANISOU 1499  CD1BLEU A 164     4657   2100   1319   1630    333    431       C  
ATOM   1500  CD2ALEU A 164      16.115  14.293   6.698  0.83 25.73           C  
ANISOU 1500  CD2ALEU A 164     4010   2594   3173   -970     51   1463       C  
ATOM   1501  CD2BLEU A 164      13.809  10.080   5.510  0.17 26.58           C  
ANISOU 1501  CD2BLEU A 164     1896   3409   4793    -89  -1619    -61       C  
ATOM   1502  N   GLN A 165      13.320  10.277   9.137  1.00 10.96           N  
ANISOU 1502  N   GLN A 165     1802   1122   1240     -6    110    324       N  
ATOM   1503  CA  GLN A 165      12.104   9.484   9.366  1.00 10.92           C  
ANISOU 1503  CA  GLN A 165     1559   1261   1330     51    145    289       C  
ATOM   1504  C   GLN A 165      11.257  10.055  10.500  1.00 11.05           C  
ANISOU 1504  C   GLN A 165     1655   1174   1368     96     57    172       C  
ATOM   1505  O   GLN A 165      10.009  10.021  10.435  1.00 12.64           O  
ANISOU 1505  O   GLN A 165     1608   1661   1535     -3     12     37       O  
ATOM   1506  CB  GLN A 165      12.533   8.034   9.664  1.00 10.93           C  
ANISOU 1506  CB  GLN A 165     1730   1168   1255    108    232    157       C  
ATOM   1507  CG  GLN A 165      13.198   7.384   8.445  1.00 11.65           C  
ANISOU 1507  CG  GLN A 165     1993   1328   1104    190    155    205       C  
ATOM   1508  CD  GLN A 165      13.834   6.051   8.756  1.00 10.13           C  
ANISOU 1508  CD  GLN A 165     1610   1112   1126    -78     62    248       C  
ATOM   1509  OE1 GLN A 165      14.388   5.799   9.836  1.00 11.45           O  
ANISOU 1509  OE1 GLN A 165     1922   1260   1167     16    -51    228       O  
ATOM   1510  NE2 GLN A 165      13.788   5.136   7.769  1.00 12.50           N  
ANISOU 1510  NE2 GLN A 165     2151   1409   1189     47    118     67       N  
ATOM   1511  N   VAL A 166      11.931  10.543  11.551  1.00 10.62           N  
ANISOU 1511  N   VAL A 166     1618   1128   1289      3     85    150       N  
ATOM   1512  CA  VAL A 166      11.149  11.290  12.582  1.00 10.96           C  
ANISOU 1512  CA  VAL A 166     1520   1270   1373      8    210    155       C  
ATOM   1513  C   VAL A 166      10.469  12.494  11.949  1.00 11.98           C  
ANISOU 1513  C   VAL A 166     1755   1350   1448    134    237    216       C  
ATOM   1514  O   VAL A 166       9.264  12.735  12.197  1.00 13.36           O  
ANISOU 1514  O   VAL A 166     1856   1617   1603    334    290    257       O  
ATOM   1515  CB  VAL A 166      12.056  11.714  13.727  1.00 11.99           C  
ANISOU 1515  CB  VAL A 166     1998   1344   1215     25     83    195       C  
ATOM   1516  CG1 VAL A 166      11.273  12.514  14.783  1.00 14.97           C  
ANISOU 1516  CG1 VAL A 166     2375   1859   1454    274    150    -40       C  
ATOM   1517  CG2 VAL A 166      12.787  10.522  14.391  1.00 12.82           C  
ANISOU 1517  CG2 VAL A 166     1933   1446   1493      5     76    303       C  
ATOM   1518  N   GLU A 167      11.194  13.241  11.127  1.00 12.48           N  
ANISOU 1518  N   GLU A 167     1821   1267   1656    154    161    322       N  
ATOM   1519  CA  GLU A 167      10.623  14.463  10.494  1.00 14.31           C  
ANISOU 1519  CA  GLU A 167     2094   1433   1910    227    114    452       C  
ATOM   1520  C   GLU A 167       9.396  14.106   9.653  1.00 13.45           C  
ANISOU 1520  C   GLU A 167     1989   1503   1617    420    298    434       C  
ATOM   1521  O   GLU A 167       8.452  14.848   9.610  1.00 14.95           O  
ANISOU 1521  O   GLU A 167     1942   1701   2038    434    178    433       O  
ATOM   1522  CB  GLU A 167      11.746  15.163   9.724  1.00 16.79           C  
ANISOU 1522  CB  GLU A 167     2236   1813   2330    234    361    887       C  
ATOM   1523  CG AGLU A 167      11.302  16.465   9.122  0.69 25.32           C  
ANISOU 1523  CG AGLU A 167     3353   2209   4057    237   -105   1757       C  
ATOM   1524  CG BGLU A 167      11.490  16.560   9.233  0.31 22.73           C  
ANISOU 1524  CG BGLU A 167     3274   1569   3792    -17    332   1012       C  
ATOM   1525  CD AGLU A 167      12.351  17.016   8.192  0.69 29.30           C  
ANISOU 1525  CD AGLU A 167     3747   2518   4868    242    227   2451       C  
ATOM   1526  CD BGLU A 167      11.347  17.557  10.359  0.31 25.77           C  
ANISOU 1526  CD BGLU A 167     3573   1848   4369    201   -288    462       C  
ATOM   1527  OE1AGLU A 167      13.031  16.397   7.367  0.69 41.14           O  
ANISOU 1527  OE1AGLU A 167     4173   3368   8091     80   2299   1991       O  
ATOM   1528  OE1BGLU A 167      10.433  18.386  10.257  0.31 28.04           O  
ANISOU 1528  OE1BGLU A 167     5106   2845   2702   1422   -803    478       O  
ATOM   1529  OE2AGLU A 167      12.426  18.252   8.277  0.69 42.21           O  
ANISOU 1529  OE2AGLU A 167     6714   2832   6492  -1619   1022   1013       O  
ATOM   1530  OE2BGLU A 167      12.073  17.557  11.372  0.31 32.38           O  
ANISOU 1530  OE2BGLU A 167     4281   1502   6522   1314  -2000   -860       O  
ATOM   1531  N   MET A 168       9.465  12.950   8.927  1.00 13.19           N  
ANISOU 1531  N   MET A 168     1807   1824   1380    330    230    291       N  
ATOM   1532  CA  MET A 168       8.330  12.553   8.123  1.00 14.90           C  
ANISOU 1532  CA  MET A 168     1787   2522   1351    430    172    163       C  
ATOM   1533  C   MET A 168       7.062  12.378   8.972  1.00 13.43           C  
ANISOU 1533  C   MET A 168     1863   1827   1414    339    188    278       C  
ATOM   1534  O   MET A 168       5.972  12.818   8.545  1.00 16.84           O  
ANISOU 1534  O   MET A 168     1798   2788   1814    352    101    579       O  
ATOM   1535  CB  MET A 168       8.655  11.227   7.402  1.00 18.34           C  
ANISOU 1535  CB  MET A 168     2231   3227   1511    526      2   -613       C  
ATOM   1536  CG AMET A 168       9.694  11.253   6.315  0.33 20.38           C  
ANISOU 1536  CG AMET A 168     2651   3509   1582   1064    239    -87       C  
ATOM   1537  CG BMET A 168       9.580  11.559   6.234  0.33 22.30           C  
ANISOU 1537  CG BMET A 168     2348   4220   1907    815    396   -512       C  
ATOM   1538  CG CMET A 168       7.555  10.603   6.601  0.33 19.79           C  
ANISOU 1538  CG CMET A 168     2206   3880   1433    636   -107   -759       C  
ATOM   1539  SD AMET A 168      10.026   9.580   5.666  0.33 27.62           S  
ANISOU 1539  SD AMET A 168     3823   4278   2392    915    656  -1292       S  
ATOM   1540  SD BMET A 168       8.853  12.582   4.950  0.33 48.28           S  
ANISOU 1540  SD BMET A 168     7766   6492   4089   1818    818   2564       S  
ATOM   1541  SD CMET A 168       8.081   9.119   5.724  0.33 39.85           S  
ANISOU 1541  SD CMET A 168     5539   4420   5184    961  -1179  -2859       S  
ATOM   1542  CE AMET A 168      11.727   9.807   5.153  0.33 49.31           C  
ANISOU 1542  CE AMET A 168     1530  11789   5416   2970  -1243  -4082       C  
ATOM   1543  CE BMET A 168       7.467  11.598   4.389  0.33 90.79           C  
ANISOU 1543  CE BMET A 168     4815  20000   9682   6754  -4457 -10000       C  
ATOM   1544  N   ILE A 169       7.170  11.769  10.141  1.00 12.59           N  
ANISOU 1544  N   ILE A 169     1856   1639   1290     67     63     98       N  
ATOM   1545  CA  ILE A 169       5.993  11.687  11.018  1.00 12.67           C  
ANISOU 1545  CA  ILE A 169     1885   1631   1299     71    149     96       C  
ATOM   1546  C   ILE A 169       5.557  13.052  11.516  1.00 12.42           C  
ANISOU 1546  C   ILE A 169     1731   1659   1331    138    120    140       C  
ATOM   1547  O   ILE A 169       4.368  13.393  11.506  1.00 14.23           O  
ANISOU 1547  O   ILE A 169     1601   2239   1568    212    174    196       O  
ATOM   1548  CB  ILE A 169       6.264  10.712  12.203  1.00 13.62           C  
ANISOU 1548  CB  ILE A 169     2091   1708   1377    176    182    102       C  
ATOM   1549  CG1 ILE A 169       6.471   9.313  11.672  1.00 17.22           C  
ANISOU 1549  CG1 ILE A 169     3248   1691   1602    293    459    189       C  
ATOM   1550  CG2 ILE A 169       5.119  10.766  13.211  1.00 15.97           C  
ANISOU 1550  CG2 ILE A 169     2340   2256   1471    -50    418     70       C  
ATOM   1551  CD1 ILE A 169       6.918   8.403  12.723  1.00 25.53           C  
ANISOU 1551  CD1 ILE A 169     4137   2643   2922   1545    972   1077       C  
ATOM   1552  N   LEU A 170       6.540  13.870  11.959  1.00 12.76           N  
ANISOU 1552  N   LEU A 170     1793   1418   1637    150     99    161       N  
ATOM   1553  CA  LEU A 170       6.163  15.177  12.488  1.00 13.64           C  
ANISOU 1553  CA  LEU A 170     1958   1485   1738    286    113    169       C  
ATOM   1554  C   LEU A 170       5.448  16.047  11.440  1.00 15.07           C  
ANISOU 1554  C   LEU A 170     2076   1721   1931    560    223    364       C  
ATOM   1555  O   LEU A 170       4.657  16.894  11.809  1.00 18.05           O  
ANISOU 1555  O   LEU A 170     2343   2079   2436    868    243    250       O  
ATOM   1556  CB  LEU A 170       7.389  15.923  13.082  1.00 14.35           C  
ANISOU 1556  CB  LEU A 170     2120   1419   1911     34    110    152       C  
ATOM   1557  CG  LEU A 170       8.020  15.212  14.319  1.00 15.38           C  
ANISOU 1557  CG  LEU A 170     2074   1773   1998    -91    -77    262       C  
ATOM   1558  CD1 LEU A 170       9.276  15.967  14.798  1.00 18.64           C  
ANISOU 1558  CD1 LEU A 170     2607   1827   2648   -215   -441   -175       C  
ATOM   1559  CD2 LEU A 170       6.996  15.055  15.459  1.00 19.02           C  
ANISOU 1559  CD2 LEU A 170     2849   2385   1991    167    220    434       C  
ATOM   1560  N   ASN A 171       5.777  15.850  10.146  1.00 15.07           N  
ANISOU 1560  N   ASN A 171     1996   1846   1883    393    201    583       N  
ATOM   1561  CA  ASN A 171       5.165  16.589   9.067  1.00 18.58           C  
ANISOU 1561  CA  ASN A 171     2321   2587   2152    685    269    889       C  
ATOM   1562  C   ASN A 171       3.950  15.857   8.471  1.00 18.80           C  
ANISOU 1562  C   ASN A 171     2085   2957   2102    946     33    712       C  
ATOM   1563  O   ASN A 171       3.483  16.310   7.406  1.00 27.59           O  
ANISOU 1563  O   ASN A 171     2783   5415   2287    825   -120   1713       O  
ATOM   1564  CB  ASN A 171       6.225  16.861   7.970  1.00 21.87           C  
ANISOU 1564  CB  ASN A 171     2786   2873   2651    637    702   1553       C  
ATOM   1565  CG  ASN A 171       7.315  17.796   8.369  1.00 29.46           C  
ANISOU 1565  CG  ASN A 171     3947   2711   4536   -227    968   1556       C  
ATOM   1566  OD1 ASN A 171       7.377  18.533   9.351  1.00 47.27           O  
ANISOU 1566  OD1 ASN A 171     7270   4690   6001  -2779   1880    -96       O  
ATOM   1567  ND2 ASN A 171       8.356  17.849   7.494  1.00 35.96           N  
ANISOU 1567  ND2 ASN A 171     3349   4401   5914   -202   1116   1879       N  
ATOM   1568  N   LYS A 172       3.453  14.766   9.076  1.00 17.65           N  
ANISOU 1568  N   LYS A 172     2219   2901   1588    583    136    226       N  
ATOM   1569  CA  LYS A 172       2.357  13.964   8.488  1.00 18.36           C  
ANISOU 1569  CA  LYS A 172     2520   2822   1635    740   -151   -130       C  
ATOM   1570  C   LYS A 172       1.092  14.769   8.357  1.00 20.19           C  
ANISOU 1570  C   LYS A 172     2481   3714   1478    959     57    476       C  
ATOM   1571  O   LYS A 172       0.682  15.354   9.400  1.00 17.85           O  
ANISOU 1571  O   LYS A 172     2271   2848   1665    973     25    510       O  
ATOM   1572  CB  LYS A 172       2.024  12.740   9.332  1.00 17.88           C  
ANISOU 1572  CB  LYS A 172     2045   2987   1760    491   -248    -54       C  
ATOM   1573  CG  LYS A 172       0.834  11.945   8.790  1.00 18.68           C  
ANISOU 1573  CG  LYS A 172     2172   3338   1589    396    -78   -301       C  
ATOM   1574  CD  LYS A 172       0.513  10.737   9.647  1.00 20.21           C  
ANISOU 1574  CD  LYS A 172     2205   3229   2246    296    169   -128       C  
ATOM   1575  CE  LYS A 172      -0.659   9.872   9.053  1.00 21.63           C  
ANISOU 1575  CE  LYS A 172     2478   2585   3157    703   -317   -357       C  
ATOM   1576  NZ  LYS A 172      -1.898  10.726   9.004  1.00 19.37           N  
ANISOU 1576  NZ  LYS A 172     2688   2228   2445    653   -673    -88       N  
ATOM   1577  N  APRO A 173       0.398  14.658   7.204  0.59 16.32           N  
ANISOU 1577  N  APRO A 173     2535   2021   1644    585     74    323       N  
ATOM   1578  N  BPRO A 173       0.498  15.048   7.189  0.41 22.04           N  
ANISOU 1578  N  BPRO A 173     2851   3853   1671    780   -312    220       N  
ATOM   1579  CA APRO A 173      -0.922  15.344   7.144  0.59 15.63           C  
ANISOU 1579  CA APRO A 173     2260   2165   1513    299    -45    218       C  
ATOM   1580  CA BPRO A 173      -0.705  15.906   7.154  0.41 20.72           C  
ANISOU 1580  CA BPRO A 173     2904   3375   1596    671   -124    834       C  
ATOM   1581  C  APRO A 173      -1.873  14.743   8.168  0.59 12.65           C  
ANISOU 1581  C  APRO A 173     2262   1508   1036    441   -370    109       C  
ATOM   1582  C  BPRO A 173      -1.831  15.178   7.880  0.41 20.55           C  
ANISOU 1582  C  BPRO A 173     3157   2750   1902    200    254   -407       C  
ATOM   1583  O  APRO A 173      -2.051  13.536   8.215  0.59 14.68           O  
ANISOU 1583  O  APRO A 173     2643   1395   1541    616     32      2       O  
ATOM   1584  O  BPRO A 173      -2.152  14.065   7.413  0.41 30.65           O  
ANISOU 1584  O  BPRO A 173     4121   3434   4092   -190    529  -1620       O  
ATOM   1585  CB APRO A 173      -1.438  15.023   5.729  0.59 16.23           C  
ANISOU 1585  CB APRO A 173     3114   1774   1278    407   -157    425       C  
ATOM   1586  CB BPRO A 173      -1.030  16.024   5.673  0.41 23.97           C  
ANISOU 1586  CB BPRO A 173     3840   3663   1603   1094   -339    403       C  
ATOM   1587  CG APRO A 173      -0.194  14.716   4.940  0.59 20.35           C  
ANISOU 1587  CG APRO A 173     3684   2463   1585    905    102    268       C  
ATOM   1588  CG BPRO A 173       0.128  15.482   4.897  0.41 20.03           C  
ANISOU 1588  CG BPRO A 173     3681   2227   1702    267    -33    496       C  
ATOM   1589  CD APRO A 173       0.699  13.969   5.941  0.59 20.34           C  
ANISOU 1589  CD APRO A 173     3114   3204   1411    914    429    415       C  
ATOM   1590  CD BPRO A 173       0.916  14.634   5.853  0.41 19.80           C  
ANISOU 1590  CD BPRO A 173     2810   3200   1512    180   -107    485       C  
ATOM   1591  N  AGLY A 174      -2.482  15.667   8.945  0.59 13.62           N  
ANISOU 1591  N  AGLY A 174     2458   1447   1272    570   -133     98       N  
ATOM   1592  N  BGLY A 174      -2.331  15.829   8.940  0.41 16.14           N  
ANISOU 1592  N  BGLY A 174     2507   2288   1338   1035   -276    281       N  
ATOM   1593  CA AGLY A 174      -3.459  15.162   9.886  0.59 14.37           C  
ANISOU 1593  CA AGLY A 174     2380   1750   1329    706   -122    220       C  
ATOM   1594  CA BGLY A 174      -3.346  15.260   9.792  0.41 14.87           C  
ANISOU 1594  CA BGLY A 174     2499   1705   1447    878   -271     16       C  
ATOM   1595  C  AGLY A 174      -2.870  14.464  11.083  0.59 13.06           C  
ANISOU 1595  C  AGLY A 174     2201   1435   1326    433   -212    107       C  
ATOM   1596  C  BGLY A 174      -2.885  14.621  11.080  0.41 12.76           C  
ANISOU 1596  C  BGLY A 174     2142   1222   1484    703   -215    -41       C  
ATOM   1597  O  AGLY A 174      -3.568  13.714  11.778  0.59 14.64           O  
ANISOU 1597  O  AGLY A 174     2535   1296   1731    251   -328    293       O  
ATOM   1598  O  BGLY A 174      -3.710  14.051  11.817  0.41 12.68           O  
ANISOU 1598  O  BGLY A 174     2011   1147   1661    688   -311     23       O  
ATOM   1599  N   LEU A 175      -1.602  14.702  11.422  1.00 12.45           N  
ANISOU 1599  N   LEU A 175     2121   1332   1278    719    -97     50       N  
ATOM   1600  CA  LEU A 175      -1.013  14.090  12.622  1.00 11.25           C  
ANISOU 1600  CA  LEU A 175     1820   1278   1178    571     77     94       C  
ATOM   1601  C   LEU A 175      -1.836  14.380  13.851  1.00 10.26           C  
ANISOU 1601  C   LEU A 175     1602   1089   1206    584    -25     79       C  
ATOM   1602  O   LEU A 175      -2.131  15.536  14.168  1.00 11.52           O  
ANISOU 1602  O   LEU A 175     1868   1087   1423    540    109     83       O  
ATOM   1603  CB  LEU A 175       0.379  14.689  12.822  1.00 11.49           C  
ANISOU 1603  CB  LEU A 175     1866   1224   1275    438    129    217       C  
ATOM   1604  CG  LEU A 175       1.175  14.083  13.991  1.00 12.39           C  
ANISOU 1604  CG  LEU A 175     1638   1550   1521    438     21    235       C  
ATOM   1605  CD1 LEU A 175       1.496  12.623  13.709  1.00 15.25           C  
ANISOU 1605  CD1 LEU A 175     2201   1629   1965    817     31    494       C  
ATOM   1606  CD2 LEU A 175       2.441  14.932  14.223  1.00 16.34           C  
ANISOU 1606  CD2 LEU A 175     1737   2456   2014    -31     15    515       C  
ATOM   1607  N   LYS A 176      -2.179  13.334  14.591  1.00 10.43           N  
ANISOU 1607  N   LYS A 176     1657   1161   1145    437    -48    132       N  
ATOM   1608  CA  LYS A 176      -3.041  13.458  15.776  1.00 10.64           C  
ANISOU 1608  CA  LYS A 176     1488   1335   1220    474    -26     41       C  
ATOM   1609  C   LYS A 176      -2.219  13.336  17.079  1.00 10.38           C  
ANISOU 1609  C   LYS A 176     1530   1191   1224    567    105    -54       C  
ATOM   1610  O   LYS A 176      -2.423  14.112  17.996  1.00 12.70           O  
ANISOU 1610  O   LYS A 176     2053   1495   1276    863   -160   -182       O  
ATOM   1611  CB  LYS A 176      -4.166  12.407  15.728  1.00 12.52           C  
ANISOU 1611  CB  LYS A 176     1583   1564   1611    284    -25     37       C  
ATOM   1612  CG ALYS A 176      -5.294  12.668  16.698  0.24 14.99           C  
ANISOU 1612  CG ALYS A 176     1828   1898   1971    161    325    200       C  
ATOM   1613  CG BLYS A 176      -5.229  12.638  16.791  0.76 15.81           C  
ANISOU 1613  CG BLYS A 176     1870   1994   2142    124    369    -43       C  
ATOM   1614  CD ALYS A 176      -6.512  11.793  16.357  0.24 17.74           C  
ANISOU 1614  CD ALYS A 176     1700   1974   3066    149     99    450       C  
ATOM   1615  CD BLYS A 176      -6.427  11.680  16.577  0.76 17.32           C  
ANISOU 1615  CD BLYS A 176     1684   1807   3089    234     40    345       C  
ATOM   1616  CE ALYS A 176      -7.708  12.385  17.122  0.24 18.84           C  
ANISOU 1616  CE ALYS A 176     1753   2498   2909   -103    114    -66       C  
ATOM   1617  CE BLYS A 176      -7.588  12.023  17.536  0.76 16.94           C  
ANISOU 1617  CE BLYS A 176     1658   1604   3175    250     48    348       C  
ATOM   1618  NZ ALYS A 176      -7.213  12.837  18.454  0.24 25.71           N  
ANISOU 1618  NZ ALYS A 176     3715   3301   2753  -1891    537   -169       N  
ATOM   1619  NZ BLYS A 176      -8.717  11.091  17.209  0.76 16.96           N  
ANISOU 1619  NZ BLYS A 176     1700   1568   3177    254    -18    393       N  
ATOM   1620  N   TYR A 177      -1.332  12.346  17.147  1.00 10.30           N  
ANISOU 1620  N   TYR A 177     1557   1201   1157    549   -156    -26       N  
ATOM   1621  CA  TYR A 177      -0.475  12.153  18.321  1.00 11.46           C  
ANISOU 1621  CA  TYR A 177     1651   1520   1183    630    -87     90       C  
ATOM   1622  C   TYR A 177       0.963  12.126  17.857  1.00 10.71           C  
ANISOU 1622  C   TYR A 177     1579   1316   1173    541   -124    -83       C  
ATOM   1623  O   TYR A 177       1.355  11.353  16.991  1.00 12.49           O  
ANISOU 1623  O   TYR A 177     1658   1561   1528    477    -39   -302       O  
ATOM   1624  CB  TYR A 177      -0.818  10.816  19.049  1.00 12.28           C  
ANISOU 1624  CB  TYR A 177     1794   1525   1346    573     -6    229       C  
ATOM   1625  CG  TYR A 177      -2.256  10.769  19.461  1.00 11.66           C  
ANISOU 1625  CG  TYR A 177     1819   1481   1130    610    -39    172       C  
ATOM   1626  CD1 TYR A 177      -2.777  11.688  20.399  1.00 14.99           C  
ANISOU 1626  CD1 TYR A 177     1914   2034   1747    357    302   -322       C  
ATOM   1627  CD2 TYR A 177      -3.172   9.870  18.911  1.00 12.72           C  
ANISOU 1627  CD2 TYR A 177     1995   1377   1462    387     36    214       C  
ATOM   1628  CE1 TYR A 177      -4.106  11.666  20.779  1.00 16.01           C  
ANISOU 1628  CE1 TYR A 177     1978   1971   2134    260    381   -368       C  
ATOM   1629  CE2 TYR A 177      -4.506   9.847  19.286  1.00 13.41           C  
ANISOU 1629  CE2 TYR A 177     1918   1662   1516    421     26    167       C  
ATOM   1630  CZ  TYR A 177      -4.977  10.760  20.210  1.00 14.18           C  
ANISOU 1630  CZ  TYR A 177     1859   1735   1792    379     49    -33       C  
ATOM   1631  OH  TYR A 177      -6.308  10.796  20.633  1.00 17.86           O  
ANISOU 1631  OH  TYR A 177     1971   2180   2636    387    447     79       O  
ATOM   1632  N   LYS A 178       1.795  12.985  18.463  1.00 11.61           N  
ANISOU 1632  N   LYS A 178     1756   1270   1385    564   -135    -30       N  
ATOM   1633  CA  LYS A 178       3.227  12.987  18.195  1.00 11.90           C  
ANISOU 1633  CA  LYS A 178     1662   1307   1552    314   -228     74       C  
ATOM   1634  C   LYS A 178       3.885  11.777  18.825  1.00  9.64           C  
ANISOU 1634  C   LYS A 178     1432   1139   1092    189   -123     42       C  
ATOM   1635  O   LYS A 178       3.441  11.305  19.884  1.00 11.58           O  
ANISOU 1635  O   LYS A 178     1563   1560   1276    410     -1    119       O  
ATOM   1636  CB  LYS A 178       3.909  14.248  18.792  1.00 15.60           C  
ANISOU 1636  CB  LYS A 178     2626   1188   2112    294   -639     12       C  
ATOM   1637  CG  LYS A 178       3.687  15.464  17.936  1.00 20.70           C  
ANISOU 1637  CG  LYS A 178     3205   1413   3246    257   -255    481       C  
ATOM   1638  CD  LYS A 178       4.213  16.652  18.682  1.00 30.03           C  
ANISOU 1638  CD  LYS A 178     4570   1442   5397   -206   -631     33       C  
ATOM   1639  CE  LYS A 178       5.691  16.636  19.016  1.00 41.87           C  
ANISOU 1639  CE  LYS A 178     4943   4068   6896  -1211  -1546   -244       C  
ATOM   1640  NZ  LYS A 178       5.969  18.002  19.636  1.00 54.40           N  
ANISOU 1640  NZ  LYS A 178     8447   6418   5803  -3827   -493  -1794       N  
ATOM   1641  N   PRO A 179       4.956  11.233  18.265  1.00 10.10           N  
ANISOU 1641  N   PRO A 179     1530   1204   1104    171   -110     73       N  
ATOM   1642  CA  PRO A 179       5.690  10.143  18.932  1.00  9.70           C  
ANISOU 1642  CA  PRO A 179     1457   1118   1111    288   -130     -1       C  
ATOM   1643  C   PRO A 179       6.204  10.645  20.271  1.00  9.10           C  
ANISOU 1643  C   PRO A 179     1262    980   1217    159   -124     26       C  
ATOM   1644  O   PRO A 179       6.780  11.733  20.400  1.00 11.59           O  
ANISOU 1644  O   PRO A 179     1814   1094   1494    -84   -151     88       O  
ATOM   1645  CB  PRO A 179       6.816   9.842  18.008  1.00 12.33           C  
ANISOU 1645  CB  PRO A 179     1788   1591   1305    400    197      4       C  
ATOM   1646  CG  PRO A 179       6.645  10.618  16.779  1.00 20.86           C  
ANISOU 1646  CG  PRO A 179     2290   3506   2130   1501    846   1345       C  
ATOM   1647  CD  PRO A 179       5.541  11.585  16.939  1.00 13.01           C  
ANISOU 1647  CD  PRO A 179     2016   1545   1383    336    364    317       C  
ATOM   1648  N   ALA A 180       5.999   9.794  21.312  1.00  8.83           N  
ANISOU 1648  N   ALA A 180     1265    992   1098    284    -99     23       N  
ATOM   1649  CA  ALA A 180       6.422  10.198  22.659  1.00  9.17           C  
ANISOU 1649  CA  ALA A 180     1247   1099   1139    244   -105   -112       C  
ATOM   1650  C   ALA A 180       7.912   9.894  22.908  1.00  8.28           C  
ANISOU 1650  C   ALA A 180     1254    820   1073    224   -128    -94       C  
ATOM   1651  O   ALA A 180       8.555  10.567  23.723  1.00  9.40           O  
ANISOU 1651  O   ALA A 180     1312    964   1297    188   -116   -224       O  
ATOM   1652  CB  ALA A 180       5.570   9.438  23.682  1.00 10.79           C  
ANISOU 1652  CB  ALA A 180     1271   1656   1171    266     72    -10       C  
ATOM   1653  N   VAL A 181       8.411   8.830  22.274  1.00  7.80           N  
ANISOU 1653  N   VAL A 181     1121    826   1015    183     18    -28       N  
ATOM   1654  CA  VAL A 181       9.727   8.237  22.504  1.00  7.67           C  
ANISOU 1654  CA  VAL A 181     1111    831    974    280    -83     19       C  
ATOM   1655  C   VAL A 181      10.322   7.801  21.193  1.00  7.36           C  
ANISOU 1655  C   VAL A 181     1173    731    891    152   -108    -72       C  
ATOM   1656  O   VAL A 181       9.572   7.308  20.322  1.00  8.28           O  
ANISOU 1656  O   VAL A 181     1141    997   1007    127    -49   -191       O  
ATOM   1657  CB  VAL A 181       9.577   7.038  23.456  1.00  8.61           C  
ANISOU 1657  CB  VAL A 181     1481    841    950    217     18     53       C  
ATOM   1658  CG1 VAL A 181      10.847   6.173  23.514  1.00 11.76           C  
ANISOU 1658  CG1 VAL A 181     1539   1184   1744    385    205    612       C  
ATOM   1659  CG2 VAL A 181       9.155   7.484  24.868  1.00 11.01           C  
ANISOU 1659  CG2 VAL A 181     2056   1175    952    -17    137    -82       C  
ATOM   1660  N   ASN A 182      11.654   7.920  21.061  1.00  7.26           N  
ANISOU 1660  N   ASN A 182     1040    753    967    117    -60      0       N  
ATOM   1661  CA  ASN A 182      12.454   7.198  20.040  1.00  7.07           C  
ANISOU 1661  CA  ASN A 182     1164    701    823    123     -1     63       C  
ATOM   1662  C   ASN A 182      13.472   6.365  20.812  1.00  6.87           C  
ANISOU 1662  C   ASN A 182     1094    647    868     70     68    -41       C  
ATOM   1663  O   ASN A 182      14.303   6.918  21.534  1.00  8.62           O  
ANISOU 1663  O   ASN A 182     1336    683   1258     32   -349    -14       O  
ATOM   1664  CB  ASN A 182      13.114   8.179  19.080  1.00  8.07           C  
ANISOU 1664  CB  ASN A 182     1283    754   1031     -1     29    124       C  
ATOM   1665  CG  ASN A 182      13.754   7.492  17.851  1.00  8.07           C  
ANISOU 1665  CG  ASN A 182     1340    781    946     65     33    141       C  
ATOM   1666  OD1 ASN A 182      13.526   6.328  17.574  1.00  8.84           O  
ANISOU 1666  OD1 ASN A 182     1400    857   1102    -10    180     37       O  
ATOM   1667  ND2 ASN A 182      14.527   8.263  17.103  1.00 10.35           N  
ANISOU 1667  ND2 ASN A 182     1596   1014   1322   -122    302    271       N  
ATOM   1668  N   GLN A 183      13.368   5.029  20.663  1.00  6.50           N  
ANISOU 1668  N   GLN A 183     1012    647    812     36      0     56       N  
ATOM   1669  CA  GLN A 183      14.286   4.110  21.332  1.00  6.31           C  
ANISOU 1669  CA  GLN A 183     1019    650    729     85     66     42       C  
ATOM   1670  C   GLN A 183      15.403   3.718  20.348  1.00  6.11           C  
ANISOU 1670  C   GLN A 183     1012    636    674     40     22     68       C  
ATOM   1671  O   GLN A 183      15.110   3.165  19.274  1.00  7.12           O  
ANISOU 1671  O   GLN A 183     1067    891    748     -3     15   -111       O  
ATOM   1672  CB  GLN A 183      13.508   2.893  21.838  1.00  6.54           C  
ANISOU 1672  CB  GLN A 183      919    715    850     11     62     79       C  
ATOM   1673  CG  GLN A 183      14.406   1.902  22.544  1.00  7.65           C  
ANISOU 1673  CG  GLN A 183     1112    796    999     57     23    183       C  
ATOM   1674  CD  GLN A 183      13.759   0.620  23.040  1.00  6.32           C  
ANISOU 1674  CD  GLN A 183     1058    730    614     97    -13     24       C  
ATOM   1675  OE1 GLN A 183      14.232  -0.483  22.716  1.00  7.57           O  
ANISOU 1675  OE1 GLN A 183     1300    754    824     75     92     13       O  
ATOM   1676  NE2 GLN A 183      12.700   0.720  23.854  1.00  7.24           N  
ANISOU 1676  NE2 GLN A 183     1102    911    738     34     97     16       N  
ATOM   1677  N   ILE A 184      16.638   4.037  20.705  1.00  6.27           N  
ANISOU 1677  N   ILE A 184      900    720    764     -8     34     16       N  
ATOM   1678  CA  ILE A 184      17.790   3.886  19.779  1.00  6.94           C  
ANISOU 1678  CA  ILE A 184      984    842    810     39    125     75       C  
ATOM   1679  C   ILE A 184      18.970   3.308  20.531  1.00  6.35           C  
ANISOU 1679  C   ILE A 184      970    813    630    -70     14    -19       C  
ATOM   1680  O   ILE A 184      19.087   3.441  21.768  1.00  7.48           O  
ANISOU 1680  O   ILE A 184     1111    927    805     29     33     10       O  
ATOM   1681  CB  ILE A 184      18.188   5.236  19.152  1.00  8.07           C  
ANISOU 1681  CB  ILE A 184     1184    913    968     28     92    241       C  
ATOM   1682  CG1 ILE A 184      18.594   6.272  20.219  1.00 11.68           C  
ANISOU 1682  CG1 ILE A 184     2143    891   1403   -371    382    -40       C  
ATOM   1683  CG2 ILE A 184      17.072   5.701  18.193  1.00 12.61           C  
ANISOU 1683  CG2 ILE A 184     1311   1766   1716    -24   -119   1003       C  
ATOM   1684  CD1 ILE A 184      19.126   7.581  19.636  1.00 14.19           C  
ANISOU 1684  CD1 ILE A 184     2370   1128   1892   -422    505    113       C  
ATOM   1685  N   GLU A 185      19.913   2.717  19.798  1.00  6.92           N  
ANISOU 1685  N   GLU A 185      931    882    815     11     26     18       N  
ATOM   1686  CA  GLU A 185      21.150   2.202  20.394  1.00  6.93           C  
ANISOU 1686  CA  GLU A 185      964    792    876     -2     41    -30       C  
ATOM   1687  C   GLU A 185      21.986   3.382  20.870  1.00  6.85           C  
ANISOU 1687  C   GLU A 185      968    771    862    -66     44     84       C  
ATOM   1688  O   GLU A 185      22.167   4.361  20.138  1.00  8.58           O  
ANISOU 1688  O   GLU A 185     1317    959    986   -203    -56    134       O  
ATOM   1689  CB  GLU A 185      21.936   1.432  19.335  1.00  7.41           C  
ANISOU 1689  CB  GLU A 185     1001    944    872     53     84    -15       C  
ATOM   1690  CG  GLU A 185      23.148   0.719  19.913  1.00  8.28           C  
ANISOU 1690  CG  GLU A 185     1070   1028   1049    175    -27   -128       C  
ATOM   1691  CD  GLU A 185      23.900  -0.127  18.883  1.00  8.37           C  
ANISOU 1691  CD  GLU A 185     1178    880   1123    141    -62   -108       C  
ATOM   1692  OE1 GLU A 185      23.272  -0.625  17.916  1.00  9.71           O  
ANISOU 1692  OE1 GLU A 185     1248   1188   1252    183   -133   -369       O  
ATOM   1693  OE2 GLU A 185      25.123  -0.337  19.090  1.00 10.19           O  
ANISOU 1693  OE2 GLU A 185     1175   1234   1462    194    -67   -414       O  
ATOM   1694  N   CYS A 186      22.524   3.308  22.086  1.00  7.00           N  
ANISOU 1694  N   CYS A 186      972    855    835    -52    -23    -41       N  
ATOM   1695  CA  CYS A 186      23.367   4.431  22.570  1.00  7.57           C  
ANISOU 1695  CA  CYS A 186     1134    743   1000    -72    -20    -11       C  
ATOM   1696  C   CYS A 186      24.234   3.940  23.706  1.00  7.12           C  
ANISOU 1696  C   CYS A 186     1037    817    851   -117     54   -106       C  
ATOM   1697  O   CYS A 186      23.737   3.363  24.666  1.00  8.09           O  
ANISOU 1697  O   CYS A 186     1142   1028    904   -148      5     80       O  
ATOM   1698  CB  CYS A 186      22.448   5.561  23.005  1.00  9.02           C  
ANISOU 1698  CB  CYS A 186     1364    802   1262     -3     52    -95       C  
ATOM   1699  SG  CYS A 186      23.341   7.057  23.501  1.00 13.02           S  
ANISOU 1699  SG  CYS A 186     1909    982   2055    -98   -153   -317       S  
ATOM   1700  N   HIS A 187      25.523   4.239  23.610  1.00  8.04           N  
ANISOU 1700  N   HIS A 187     1031   1045    979    -59     38     22       N  
ATOM   1701  CA  HIS A 187      26.559   3.817  24.577  1.00  8.02           C  
ANISOU 1701  CA  HIS A 187      991   1051   1004    -71      6     96       C  
ATOM   1702  C   HIS A 187      27.809   4.629  24.250  1.00  8.05           C  
ANISOU 1702  C   HIS A 187     1061   1109    890    -62     53      8       C  
ATOM   1703  O   HIS A 187      27.858   5.358  23.256  1.00  8.88           O  
ANISOU 1703  O   HIS A 187     1159   1157   1058   -115     61     85       O  
ATOM   1704  CB  HIS A 187      26.768   2.282  24.552  1.00  8.65           C  
ANISOU 1704  CB  HIS A 187     1158   1067   1061    -71     81     78       C  
ATOM   1705  CG  HIS A 187      26.962   1.724  23.189  1.00  8.14           C  
ANISOU 1705  CG  HIS A 187     1040   1013   1038   -100    -30    135       C  
ATOM   1706  ND1 HIS A 187      28.082   1.998  22.417  1.00  9.10           N  
ANISOU 1706  ND1 HIS A 187     1179   1254   1024   -129     55      3       N  
ATOM   1707  CD2 HIS A 187      26.082   0.996  22.447  1.00  9.07           C  
ANISOU 1707  CD2 HIS A 187     1281    993   1170   -120      7    -45       C  
ATOM   1708  CE1 HIS A 187      27.873   1.400  21.237  1.00  9.15           C  
ANISOU 1708  CE1 HIS A 187     1240   1037   1200    -65    -31    -18       C  
ATOM   1709  NE2 HIS A 187      26.681   0.780  21.226  1.00  9.14           N  
ANISOU 1709  NE2 HIS A 187     1210    968   1296    -52     17    -98       N  
ATOM   1710  N   PRO A 188      28.893   4.526  25.058  1.00  8.44           N  
ANISOU 1710  N   PRO A 188     1082   1222    903   -177     -5     31       N  
ATOM   1711  CA  PRO A 188      30.065   5.370  24.751  1.00  9.01           C  
ANISOU 1711  CA  PRO A 188     1047   1314   1063   -241     19    -69       C  
ATOM   1712  C   PRO A 188      30.719   5.126  23.389  1.00  8.64           C  
ANISOU 1712  C   PRO A 188     1122   1157   1004   -135     85    -70       C  
ATOM   1713  O   PRO A 188      31.492   6.010  22.994  1.00 10.76           O  
ANISOU 1713  O   PRO A 188     1397   1313   1377   -415    290   -153       O  
ATOM   1714  CB  PRO A 188      31.039   5.058  25.889  1.00 10.02           C  
ANISOU 1714  CB  PRO A 188     1112   1622   1074   -148    -97      7       C  
ATOM   1715  CG  PRO A 188      30.106   4.711  27.053  1.00 10.35           C  
ANISOU 1715  CG  PRO A 188     1329   1518   1085   -322    -87     13       C  
ATOM   1716  CD  PRO A 188      28.973   3.898  26.385  1.00  9.65           C  
ANISOU 1716  CD  PRO A 188     1235   1441    989   -206    -72     46       C  
ATOM   1717  N   TYR A 189      30.493   3.967  22.736  1.00  8.60           N  
ANISOU 1717  N   TYR A 189     1063   1086   1117    -82     24    -48       N  
ATOM   1718  CA  TYR A 189      31.065   3.796  21.406  1.00  8.72           C  
ANISOU 1718  CA  TYR A 189     1086   1166   1061    -68     97   -170       C  
ATOM   1719  C   TYR A 189      30.148   4.257  20.277  1.00  8.41           C  
ANISOU 1719  C   TYR A 189     1081    997   1117   -159    172    -91       C  
ATOM   1720  O   TYR A 189      30.582   4.250  19.098  1.00 10.09           O  
ANISOU 1720  O   TYR A 189     1326   1354   1154    -88    181    -94       O  
ATOM   1721  CB  TYR A 189      31.527   2.334  21.181  1.00 10.08           C  
ANISOU 1721  CB  TYR A 189     1289   1190   1349     62     23   -174       C  
ATOM   1722  CG  TYR A 189      32.635   1.839  22.099  1.00  9.30           C  
ANISOU 1722  CG  TYR A 189     1136   1227   1170     16    131   -173       C  
ATOM   1723  CD1 TYR A 189      33.481   2.698  22.823  1.00 10.05           C  
ANISOU 1723  CD1 TYR A 189     1204   1315   1299    -73     19    -48       C  
ATOM   1724  CD2 TYR A 189      32.796   0.481  22.255  1.00 11.14           C  
ANISOU 1724  CD2 TYR A 189     1485   1260   1488    171     -8   -205       C  
ATOM   1725  CE1 TYR A 189      34.461   2.159  23.664  1.00 11.14           C  
ANISOU 1725  CE1 TYR A 189     1106   1438   1690    -53    -48     -2       C  
ATOM   1726  CE2 TYR A 189      33.771  -0.074  23.088  1.00 13.02           C  
ANISOU 1726  CE2 TYR A 189     1507   1485   1955    339   -317   -399       C  
ATOM   1727  CZ  TYR A 189      34.616   0.801  23.809  1.00 11.52           C  
ANISOU 1727  CZ  TYR A 189     1326   1452   1601     69    -55     38       C  
ATOM   1728  OH  TYR A 189      35.565   0.225  24.605  1.00 15.06           O  
ANISOU 1728  OH  TYR A 189     1785   1835   2104    319   -537   -128       O  
ATOM   1729  N   LEU A 190      28.934   4.653  20.595  1.00  8.77           N  
ANISOU 1729  N   LEU A 190     1150   1101   1080    -81    -10     16       N  
ATOM   1730  CA  LEU A 190      27.916   5.151  19.634  1.00  8.32           C  
ANISOU 1730  CA  LEU A 190     1122    945   1094    -84     39      9       C  
ATOM   1731  C   LEU A 190      27.073   6.192  20.389  1.00  7.96           C  
ANISOU 1731  C   LEU A 190     1161    975    888   -143     32     67       C  
ATOM   1732  O   LEU A 190      25.989   5.903  20.904  1.00  8.98           O  
ANISOU 1732  O   LEU A 190     1203   1081   1126   -139    110    112       O  
ATOM   1733  CB  LEU A 190      27.048   4.000  19.126  1.00  8.79           C  
ANISOU 1733  CB  LEU A 190     1296    929   1114    -33    -72    -39       C  
ATOM   1734  CG  LEU A 190      26.086   4.415  18.013  1.00 10.10           C  
ANISOU 1734  CG  LEU A 190     1401   1247   1190   -150   -192    -33       C  
ATOM   1735  CD1 LEU A 190      26.777   4.559  16.648  1.00 13.73           C  
ANISOU 1735  CD1 LEU A 190     1860   2201   1156   -389   -109    219       C  
ATOM   1736  CD2 LEU A 190      24.968   3.350  17.881  1.00 12.23           C  
ANISOU 1736  CD2 LEU A 190     1372   1482   1791   -261   -112   -204       C  
ATOM   1737  N  ATHR A 191      27.708   7.377  20.489  0.47  8.02           N  
ANISOU 1737  N  ATHR A 191     1175    919    955    -85   -206   -124       N  
ATOM   1738  N  BTHR A 191      27.552   7.430  20.529  0.53  8.96           N  
ANISOU 1738  N  BTHR A 191     1197    934   1274   -110    386     63       N  
ATOM   1739  CA ATHR A 191      27.188   8.395  21.426  0.47  7.97           C  
ANISOU 1739  CA ATHR A 191     1126   1012    892   -196    264     90       C  
ATOM   1740  CA BTHR A 191      26.969   8.375  21.515  0.53  9.38           C  
ANISOU 1740  CA BTHR A 191     1249   1026   1290    -40      7   -141       C  
ATOM   1741  C  ATHR A 191      25.955   9.104  20.872  0.47  7.44           C  
ANISOU 1741  C  ATHR A 191     1085    718   1022   -325    224    -59       C  
ATOM   1742  C  BTHR A 191      25.780   9.160  20.987  0.53 10.45           C  
ANISOU 1742  C  BTHR A 191     1329   1392   1250    201    225    167       C  
ATOM   1743  O  ATHR A 191      25.262   9.702  21.701  0.47 10.43           O  
ANISOU 1743  O  ATHR A 191     1789   1038   1135    306    216     56       O  
ATOM   1744  O  BTHR A 191      25.054   9.778  21.779  0.53 10.36           O  
ANISOU 1744  O  BTHR A 191     1141   1338   1460   -101    266     13       O  
ATOM   1745  CB ATHR A 191      28.322   9.367  21.813  0.47  7.92           C  
ANISOU 1745  CB ATHR A 191     1068    905   1035     -2    183   -205       C  
ATOM   1746  CB BTHR A 191      28.021   9.410  21.993  0.53 10.77           C  
ANISOU 1746  CB BTHR A 191     1567   1194   1331   -465    135    155       C  
ATOM   1747  OG1ATHR A 191      28.933   9.830  20.584  0.47 10.24           O  
ANISOU 1747  OG1ATHR A 191     1385    997   1508   -229    413    204       O  
ATOM   1748  OG1BTHR A 191      28.598   9.952  20.779  0.53 12.45           O  
ANISOU 1748  OG1BTHR A 191     1968   1553   1210   -611    513   -370       O  
ATOM   1749  CG2ATHR A 191      29.371   8.639  22.661  0.47 12.94           C  
ANISOU 1749  CG2ATHR A 191     1011   2122   1782   -197     13    709       C  
ATOM   1750  CG2BTHR A 191      29.082   8.700  22.815  0.53 11.27           C  
ANISOU 1750  CG2BTHR A 191     1685   1054   1543   -271   -325   -609       C  
ATOM   1751  N  AGLN A 192      25.715   9.115  19.558  0.47  9.18           N  
ANISOU 1751  N  AGLN A 192     1394   1059   1034   -166    -11    127       N  
ATOM   1752  N  BGLN A 192      25.604   9.221  19.659  0.53 10.15           N  
ANISOU 1752  N  BGLN A 192     1411   1156   1290     10     17     94       N  
ATOM   1753  CA AGLN A 192      24.470   9.591  18.942  0.47 11.38           C  
ANISOU 1753  CA AGLN A 192     1530    977   1817    -42   -283    148       C  
ATOM   1754  CA BGLN A 192      24.341   9.710  19.096  0.53  9.64           C  
ANISOU 1754  CA BGLN A 192     1335   1054   1273    -45    161    269       C  
ATOM   1755  C  AGLN A 192      24.129  11.037  19.269  0.47 10.57           C  
ANISOU 1755  C  AGLN A 192     1575    993   1450   -119    -12    127       C  
ATOM   1756  C  BGLN A 192      24.061  11.169  19.396  0.53  9.63           C  
ANISOU 1756  C  BGLN A 192     1361    971   1325   -128    328    325       C  
ATOM   1757  O  AGLN A 192      22.957  11.428  19.382  0.47 11.58           O  
ANISOU 1757  O  AGLN A 192     1655   1138   1608    -66     96   -122       O  
ATOM   1758  O  BGLN A 192      22.901  11.558  19.581  0.53 10.63           O  
ANISOU 1758  O  BGLN A 192     1326    913   1801    -40    103    518       O  
ATOM   1759  CB AGLN A 192      23.312   8.675  19.385  0.47 13.32           C  
ANISOU 1759  CB AGLN A 192     1439    986   2636    -55   -157      6       C  
ATOM   1760  CB BGLN A 192      23.155   8.855  19.608  0.53 10.25           C  
ANISOU 1760  CB BGLN A 192     1546   1004   1345   -206    194    203       C  
ATOM   1761  CG AGLN A 192      23.493   7.203  18.965  0.47 15.32           C  
ANISOU 1761  CG AGLN A 192     1957   1263   2601   -427   -197   -629       C  
ATOM   1762  CG BGLN A 192      23.218   7.379  19.196  0.53 10.19           C  
ANISOU 1762  CG BGLN A 192     1537   1015   1320     31   -227    298       C  
ATOM   1763  CD AGLN A 192      22.763   6.915  17.672  0.47 12.10           C  
ANISOU 1763  CD AGLN A 192     1812    838   1949    122   -157    388       C  
ATOM   1764  CD BGLN A 192      22.522   7.138  17.875  0.53 10.69           C  
ANISOU 1764  CD BGLN A 192     1518   1331   1211   -277    -83    279       C  
ATOM   1765  OE1AGLN A 192      22.679   7.716  16.740  0.47 22.85           O  
ANISOU 1765  OE1AGLN A 192     3423   2304   2953   -577    552   1802       O  
ATOM   1766  OE1BGLN A 192      22.510   7.967  16.967  0.53 13.51           O  
ANISOU 1766  OE1BGLN A 192     2683   1107   1343   -389   -621    286       O  
ATOM   1767  NE2AGLN A 192      22.186   5.724  17.588  0.47  8.69           N  
ANISOU 1767  NE2AGLN A 192     1574    785    944    120    -45     -3       N  
ATOM   1768  NE2BGLN A 192      21.898   5.961  17.751  0.53  9.51           N  
ANISOU 1768  NE2BGLN A 192     1199    996   1417     20    247     13       N  
ATOM   1769  N  AGLU A 193      25.143  11.906  19.403  0.47 10.77           N  
ANISOU 1769  N  AGLU A 193     1791    878   1424   -175   -201    346       N  
ATOM   1770  N  BGLU A 193      25.063  12.056  19.425  0.53 11.51           N  
ANISOU 1770  N  BGLU A 193     1593   1117   1664   -332    279    283       N  
ATOM   1771  CA AGLU A 193      24.845  13.291  19.805  0.47 11.40           C  
ANISOU 1771  CA AGLU A 193     1607    983   1741   -196   -482    173       C  
ATOM   1772  CA BGLU A 193      24.783  13.417  19.905  0.53 12.25           C  
ANISOU 1772  CA BGLU A 193     1747    949   1957   -283     50    429       C  
ATOM   1773  C  AGLU A 193      23.907  13.986  18.831  0.47  9.75           C  
ANISOU 1773  C  AGLU A 193     1626    663   1417   -272   -110    268       C  
ATOM   1774  C  BGLU A 193      23.756  14.151  19.045  0.53 12.34           C  
ANISOU 1774  C  BGLU A 193     1705   1095   1888   -393     12    397       C  
ATOM   1775  O  AGLU A 193      23.017  14.773  19.273  0.47 11.75           O  
ANISOU 1775  O  AGLU A 193     1968    803   1694    103     61    486       O  
ATOM   1776  O  BGLU A 193      22.820  14.764  19.601  0.53 14.67           O  
ANISOU 1776  O  BGLU A 193     1655   1633   2285    -89    -50    172       O  
ATOM   1777  CB AGLU A 193      26.190  14.047  19.939  0.47 14.10           C  
ANISOU 1777  CB AGLU A 193     1675   1247   2434   -384   -363    121       C  
ATOM   1778  CB BGLU A 193      26.070  14.278  19.918  0.53 14.25           C  
ANISOU 1778  CB BGLU A 193     1807   1380   2226   -549   -122    332       C  
ATOM   1779  CG AGLU A 193      27.131  13.436  20.971  0.47 13.90           C  
ANISOU 1779  CG AGLU A 193     1338   1375   2568   -253   -422   -103       C  
ATOM   1780  CG BGLU A 193      26.971  14.066  21.126  0.53 17.08           C  
ANISOU 1780  CG BGLU A 193     2474   1627   2386   -482   -504     38       C  
ATOM   1781  CD AGLU A 193      28.073  14.437  21.620  0.47 13.75           C  
ANISOU 1781  CD AGLU A 193     1915   1243   2065   -563   -253    120       C  
ATOM   1782  CD BGLU A 193      28.109  13.132  20.817  0.53 14.45           C  
ANISOU 1782  CD BGLU A 193     2144   1313   2032   -703   -552    529       C  
ATOM   1783  OE1AGLU A 193      27.580  15.492  22.070  0.47 18.93           O  
ANISOU 1783  OE1AGLU A 193     2719   1348   3126   -415   -320   -233       O  
ATOM   1784  OE1BGLU A 193      27.906  12.154  20.070  0.53 16.39           O  
ANISOU 1784  OE1BGLU A 193     2050   1840   2337   -380   -404     20       O  
ATOM   1785  OE2AGLU A 193      29.294  14.204  21.738  0.47 13.86           O  
ANISOU 1785  OE2AGLU A 193     1714   1642   1911  -1047   -206      7       O  
ATOM   1786  OE2BGLU A 193      29.206  13.284  21.397  0.53 19.12           O  
ANISOU 1786  OE2BGLU A 193     1937   2645   2683  -1313   -475    672       O  
ATOM   1787  N  ALYS A 194      24.029  13.754  17.526  0.47 10.43           N  
ANISOU 1787  N  ALYS A 194     1728    836   1402   -292   -275    214       N  
ATOM   1788  N  BLYS A 194      23.950  14.095  17.725  0.53 13.07           N  
ANISOU 1788  N  BLYS A 194     1770   1323   1872   -462     52    592       N  
ATOM   1789  CA ALYS A 194      23.200  14.476  16.559  0.47 11.19           C  
ANISOU 1789  CA ALYS A 194     1747   1007   1498   -330   -209    437       C  
ATOM   1790  CA BLYS A 194      23.068  14.862  16.843  0.53 13.60           C  
ANISOU 1790  CA BLYS A 194     1891   1221   2055   -490   -131    592       C  
ATOM   1791  C  ALYS A 194      21.743  14.047  16.607  0.47 10.34           C  
ANISOU 1791  C  ALYS A 194     1737    823   1370   -271   -292    113       C  
ATOM   1792  C  BLYS A 194      21.642  14.350  16.923  0.53 11.62           C  
ANISOU 1792  C  BLYS A 194     1904   1003   1508   -390   -132    361       C  
ATOM   1793  O  ALYS A 194      20.842  14.913  16.658  0.47 11.83           O  
ANISOU 1793  O  ALYS A 194     1803   1076   1615   -121   -166    492       O  
ATOM   1794  O  BLYS A 194      20.679  15.150  16.982  0.53 13.49           O  
ANISOU 1794  O  BLYS A 194     1979   1003   2146   -325    181    374       O  
ATOM   1795  CB ALYS A 194      23.779  14.271  15.138  0.47 15.32           C  
ANISOU 1795  CB ALYS A 194     2179   2276   1366  -1042    -99    402       C  
ATOM   1796  CB BLYS A 194      23.645  14.732  15.415  0.53 16.59           C  
ANISOU 1796  CB BLYS A 194     2091   2086   2126   -495     71   1079       C  
ATOM   1797  CG ALYS A 194      25.177  14.845  14.855  0.47 20.43           C  
ANISOU 1797  CG ALYS A 194     2133   3518   2113  -1093    201    254       C  
ATOM   1798  CG BLYS A 194      24.948  15.492  15.124  0.53 21.69           C  
ANISOU 1798  CG BLYS A 194     2450   3398   2394  -1178   -120   1483       C  
ATOM   1799  CD ALYS A 194      25.549  14.872  13.371  0.47 25.97           C  
ANISOU 1799  CD ALYS A 194     2568   5017   2282   -725    640    805       C  
ATOM   1800  CD BLYS A 194      25.438  15.228  13.688  0.53 25.64           C  
ANISOU 1800  CD BLYS A 194     2668   4451   2624  -1077    301   1453       C  
ATOM   1801  CE ALYS A 194      26.891  15.519  13.082  0.47 30.68           C  
ANISOU 1801  CE ALYS A 194     3186   5723   2747  -1432    445   1714       C  
ATOM   1802  CE BLYS A 194      26.598  16.131  13.307  0.53 28.71           C  
ANISOU 1802  CE BLYS A 194     3001   5278   2631  -1634    236   1397       C  
ATOM   1803  NZ ALYS A 194      26.823  16.754  12.250  0.47 40.04           N  
ANISOU 1803  NZ ALYS A 194     5440   6078   3697  -1804     74   2309       N  
ATOM   1804  NZ BLYS A 194      27.017  15.978  11.881  0.53 35.66           N  
ANISOU 1804  NZ BLYS A 194     2386   8146   3018  -1962    680    713       N  
ATOM   1805  N  ALEU A 195      21.450  12.750  16.619  0.47  9.84           N  
ANISOU 1805  N  ALEU A 195     1883    894    963   -413     58     60       N  
ATOM   1806  N  BLEU A 195      21.451  13.030  16.967  0.53 10.83           N  
ANISOU 1806  N  BLEU A 195     1551   1031   1534   -351    -85    154       N  
ATOM   1807  CA ALEU A 195      20.028  12.310  16.618  0.47 11.13           C  
ANISOU 1807  CA ALEU A 195     1893   1141   1193   -501    214   -267       C  
ATOM   1808  CA BLEU A 195      20.064  12.500  16.976  0.53  9.45           C  
ANISOU 1808  CA BLEU A 195     1551    883   1156   -243    -85    258       C  
ATOM   1809  C  ALEU A 195      19.414  12.653  17.954  0.47  8.41           C  
ANISOU 1809  C  ALEU A 195     1601    477   1118   -193    -20    133       C  
ATOM   1810  C  BLEU A 195      19.407  12.793  18.318  0.53 10.14           C  
ANISOU 1810  C  BLEU A 195     1496   1141   1214   -165   -154    212       C  
ATOM   1811  O  ALEU A 195      18.216  12.951  18.034  0.47 11.20           O  
ANISOU 1811  O  ALEU A 195     1639   1346   1270     12    -27     94       O  
ATOM   1812  O  BLEU A 195      18.209  13.090  18.315  0.53  9.75           O  
ANISOU 1812  O  BLEU A 195     1567    834   1303    -89   -137     23       O  
ATOM   1813  CB ALEU A 195      19.971  10.801  16.326  0.47  8.98           C  
ANISOU 1813  CB ALEU A 195     1561    918    931   -169   -149    -12       C  
ATOM   1814  CB BLEU A 195      20.079  10.995  16.662  0.53 10.98           C  
ANISOU 1814  CB BLEU A 195     1718   1017   1439   -492     79     77       C  
ATOM   1815  CG ALEU A 195      18.560  10.169  16.260  0.47  9.48           C  
ANISOU 1815  CG ALEU A 195     1620   1030    953   -274     14     37       C  
ATOM   1816  CG BLEU A 195      18.679  10.345  16.622  0.53 11.15           C  
ANISOU 1816  CG BLEU A 195     1876   1170   1192   -538   -220    -29       C  
ATOM   1817  CD1ALEU A 195      17.698  10.928  15.233  0.47 12.42           C  
ANISOU 1817  CD1ALEU A 195     1944   1372   1403    141   -641   -422       C  
ATOM   1818  CD1BLEU A 195      17.763  11.084  15.637  0.53 12.90           C  
ANISOU 1818  CD1BLEU A 195     1772   1994   1136   -424     97    450       C  
ATOM   1819  CD2ALEU A 195      18.654   8.682  15.918  0.47 10.78           C  
ANISOU 1819  CD2ALEU A 195     1928   1086   1083   -260    -56   -222       C  
ATOM   1820  CD2BLEU A 195      18.878   8.873  16.259  0.53 12.38           C  
ANISOU 1820  CD2BLEU A 195     1948   1247   1508   -706    149   -268       C  
ATOM   1821  N  AILE A 196      20.166  12.584  19.065  0.47  9.78           N  
ANISOU 1821  N  AILE A 196     1736    955   1026   -131     -3      1       N  
ATOM   1822  N  BILE A 196      20.171  12.631  19.397  0.53  9.50           N  
ANISOU 1822  N  BILE A 196     1563    927   1118   -206    -65    336       N  
ATOM   1823  CA AILE A 196      19.606  12.904  20.391  0.47  9.05           C  
ANISOU 1823  CA AILE A 196     1561    811   1067    -49    -26    197       C  
ATOM   1824  CA BILE A 196      19.554  12.923  20.724  0.53 10.72           C  
ANISOU 1824  CA BILE A 196     1873   1025   1174    -15      6    283       C  
ATOM   1825  C  AILE A 196      19.206  14.366  20.482  0.47  9.17           C  
ANISOU 1825  C  AILE A 196     1483    855   1146     17   -170    101       C  
ATOM   1826  C  BILE A 196      19.170  14.386  20.843  0.53 11.02           C  
ANISOU 1826  C  BILE A 196     1754    996   1437    -61   -161    219       C  
ATOM   1827  O  AILE A 196      18.099  14.663  20.913  0.47  9.32           O  
ANISOU 1827  O  AILE A 196     1504    968   1069     37   -218    126       O  
ATOM   1828  O  BILE A 196      18.119  14.745  21.352  0.53 12.81           O  
ANISOU 1828  O  BILE A 196     1989   1212   1666    114    -22    177       O  
ATOM   1829  CB AILE A 196      20.591  12.496  21.494  0.47  9.92           C  
ANISOU 1829  CB AILE A 196     1678   1126    965    140    123    394       C  
ATOM   1830  CB BILE A 196      20.483  12.486  21.850  0.53  9.81           C  
ANISOU 1830  CB BILE A 196     1574   1040   1116   -109     88    315       C  
ATOM   1831  CG1AILE A 196      20.634  10.972  21.582  0.47 10.63           C  
ANISOU 1831  CG1AILE A 196     1352   1190   1498    105    155    604       C  
ATOM   1832  CG1BILE A 196      20.561  10.966  21.949  0.53 12.31           C  
ANISOU 1832  CG1BILE A 196     1735   1077   1864    119    263    536       C  
ATOM   1833  CG2AILE A 196      20.201  13.122  22.833  0.47 11.54           C  
ANISOU 1833  CG2AILE A 196     1738   1666    983     73     71    287       C  
ATOM   1834  CG2BILE A 196      19.997  13.082  23.188  0.53 15.02           C  
ANISOU 1834  CG2BILE A 196     2753   1887   1068    463    146    190       C  
ATOM   1835  CD1AILE A 196      21.694  10.458  22.558  0.47 12.98           C  
ANISOU 1835  CD1AILE A 196     2348   1698    887    716     21    396       C  
ATOM   1836  CD1BILE A 196      21.633  10.451  22.907  0.53 16.04           C  
ANISOU 1836  CD1BILE A 196     1773   1917   2404    352    287   1154       C  
ATOM   1837  N  AGLN A 197      20.102  15.271  20.055  0.47 10.46           N  
ANISOU 1837  N  AGLN A 197     1695    780   1499   -146   -187     87       N  
ATOM   1838  N  BGLN A 197      20.033  15.304  20.354  0.53 12.71           N  
ANISOU 1838  N  BGLN A 197     1829   1050   1951   -247   -383    331       N  
ATOM   1839  CA AGLN A 197      19.775  16.714  20.093  0.47 11.90           C  
ANISOU 1839  CA AGLN A 197     1528    867   2126    -88   -269    192       C  
ATOM   1840  CA BGLN A 197      19.630  16.725  20.451  0.53 13.40           C  
ANISOU 1840  CA BGLN A 197     2016   1092   1983   -230   -305    509       C  
ATOM   1841  C  AGLN A 197      18.523  17.014  19.286  0.47 12.37           C  
ANISOU 1841  C  AGLN A 197     1550    977   2173    -93   -279    230       C  
ATOM   1842  C  BGLN A 197      18.479  17.009  19.482  0.53 13.71           C  
ANISOU 1842  C  BGLN A 197     2221    754   2235   -245   -477    454       C  
ATOM   1843  O  AGLN A 197      17.634  17.759  19.694  0.47 13.62           O  
ANISOU 1843  O  AGLN A 197     2020    805   2348    301   -294    448       O  
ATOM   1844  O  BGLN A 197      17.615  17.796  19.882  0.53 16.70           O  
ANISOU 1844  O  BGLN A 197     1954   1128   3263   -249   -692   -158       O  
ATOM   1845  CB AGLN A 197      20.971  17.536  19.597  0.47 11.57           C  
ANISOU 1845  CB AGLN A 197     1648    833   1917   -242   -370    166       C  
ATOM   1846  CB BGLN A 197      20.808  17.669  20.193  0.53 17.77           C  
ANISOU 1846  CB BGLN A 197     2666   1346   2741   -849   -740    711       C  
ATOM   1847  CG AGLN A 197      20.742  19.053  19.641  0.47 14.14           C  
ANISOU 1847  CG AGLN A 197     2463    868   2041   -299   -416    234       C  
ATOM   1848  CG BGLN A 197      20.555  19.083  20.765  0.53 22.81           C  
ANISOU 1848  CG BGLN A 197     4369   1466   2830  -1056   -673    408       C  
ATOM   1849  CD AGLN A 197      20.521  19.661  21.016  0.47 18.19           C  
ANISOU 1849  CD AGLN A 197     3919    849   2145   -235   -719    -42       C  
ATOM   1850  CD BGLN A 197      19.795  19.994  19.807  0.53 24.18           C  
ANISOU 1850  CD BGLN A 197     4213   2072   2901    649   -164   -157       C  
ATOM   1851  OE1AGLN A 197      20.866  19.142  22.067  0.47 20.24           O  
ANISOU 1851  OE1AGLN A 197     4356   1282   2051   -563   -632    144       O  
ATOM   1852  OE1BGLN A 197      19.194  21.016  20.212  0.53 29.12           O  
ANISOU 1852  OE1BGLN A 197     3784   1849   5433    -79   1235   -400       O  
ATOM   1853  NE2AGLN A 197      19.919  20.858  21.009  0.47 22.40           N  
ANISOU 1853  NE2AGLN A 197     3950   1710   2850    567  -1500   -778       N  
ATOM   1854  NE2BGLN A 197      19.807  19.587  18.530  0.53 22.72           N  
ANISOU 1854  NE2BGLN A 197     4194   1844   2595   -922   -278    295       N  
ATOM   1855  N  ATYR A 198      18.386  16.383  18.108  0.47 12.45           N  
ANISOU 1855  N  ATYR A 198     1798   1267   1667     72   -199    568       N  
ATOM   1856  N  BTYR A 198      18.472  16.392  18.287  0.53 13.31           N  
ANISOU 1856  N  BTYR A 198     1993    811   2253   -538   -590    428       N  
ATOM   1857  CA ATYR A 198      17.210  16.610  17.287  0.47 12.75           C  
ANISOU 1857  CA ATYR A 198     1898   1148   1799     21   -266    625       C  
ATOM   1858  CA BTYR A 198      17.353  16.510  17.373  0.53 12.82           C  
ANISOU 1858  CA BTYR A 198     1864    933   2074   -301   -351    648       C  
ATOM   1859  C  ATYR A 198      15.933  16.117  17.937  0.47 10.48           C  
ANISOU 1859  C  ATYR A 198     1838    695   1448    -17   -393    224       C  
ATOM   1860  C  BTYR A 198      16.092  16.183  18.159  0.53 11.98           C  
ANISOU 1860  C  BTYR A 198     1906    902   1743   -178   -421    443       C  
ATOM   1861  O  ATYR A 198      14.917  16.828  17.999  0.47 11.70           O  
ANISOU 1861  O  ATYR A 198     1785    738   1922     -5   -450    397       O  
ATOM   1862  O  BTYR A 198      15.124  16.953  18.253  0.53 13.83           O  
ANISOU 1862  O  BTYR A 198     1783   1042   2431   -217   -399    510       O  
ATOM   1863  CB ATYR A 198      17.424  15.905  15.918  0.47 12.44           C  
ANISOU 1863  CB ATYR A 198     2109    987   1631   -161   -187    694       C  
ATOM   1864  CB BTYR A 198      17.570  15.622  16.096  0.53 14.28           C  
ANISOU 1864  CB BTYR A 198     1890   1698   1837   -219   -366    482       C  
ATOM   1865  CG ATYR A 198      16.220  16.083  15.025  0.47 14.11           C  
ANISOU 1865  CG ATYR A 198     2155   1455   1752   -422   -282   1063       C  
ATOM   1866  CG BTYR A 198      16.298  15.691  15.259  0.53 13.67           C  
ANISOU 1866  CG BTYR A 198     1954   1143   2096   -189   -512    784       C  
ATOM   1867  CD1ATYR A 198      16.057  17.276  14.313  0.47 20.38           C  
ANISOU 1867  CD1ATYR A 198     3169   2128   2445   -764   -897   1845       C  
ATOM   1868  CD1BTYR A 198      15.956  16.682  14.377  0.53 17.07           C  
ANISOU 1868  CD1BTYR A 198     2373   1767   2347   -411   -506   1324       C  
ATOM   1869  CD2ATYR A 198      15.236  15.112  14.913  0.47 15.02           C  
ANISOU 1869  CD2ATYR A 198     2652   1189   1866   -353   -673    586       C  
ATOM   1870  CD2BTYR A 198      15.351  14.673  15.392  0.53 12.86           C  
ANISOU 1870  CD2BTYR A 198     2096   1282   1508   -329   -245    509       C  
ATOM   1871  CE1ATYR A 198      14.930  17.426  13.505  0.47 24.40           C  
ANISOU 1871  CE1ATYR A 198     3573   2199   3498   -533  -1468   1860       C  
ATOM   1872  CE1BTYR A 198      14.767  16.688  13.646  0.53 19.02           C  
ANISOU 1872  CE1BTYR A 198     3395   1450   2381   -217  -1394    775       C  
ATOM   1873  CE2ATYR A 198      14.131  15.276  14.127  0.47 15.46           C  
ANISOU 1873  CE2ATYR A 198     2490   1264   2121      0   -685    208       C  
ATOM   1874  CE2BTYR A 198      14.164  14.660  14.718  0.53 13.73           C  
ANISOU 1874  CE2BTYR A 198     2070   1464   1682   -261   -256     73       C  
ATOM   1875  CZ ATYR A 198      13.982  16.450  13.418  0.47 19.30           C  
ANISOU 1875  CZ ATYR A 198     3484   1760   2091   -154  -1275    594       C  
ATOM   1876  CZ BTYR A 198      13.867  15.678  13.833  0.53 16.73           C  
ANISOU 1876  CZ BTYR A 198     2228   1778   2352    159   -747    250       C  
ATOM   1877  OH ATYR A 198      12.878  16.609  12.615  0.47 27.95           O  
ANISOU 1877  OH ATYR A 198     3462   2834   4322     30  -1976   1366       O  
ATOM   1878  OH BTYR A 198      12.672  15.630  13.158  0.53 20.52           O  
ANISOU 1878  OH BTYR A 198     2417   2597   2785    583  -1061   -593       O  
ATOM   1879  N  ACYS A 199      15.891  14.878  18.416  0.47  9.68           N  
ANISOU 1879  N  ACYS A 199     1739    601   1336     91    -78    -43       N  
ATOM   1880  N  BCYS A 199      16.033  14.976  18.733  0.53 10.88           N  
ANISOU 1880  N  BCYS A 199     1860    892   1381   -391   -396    341       N  
ATOM   1881  CA ACYS A 199      14.698  14.363  19.066  0.47 10.77           C  
ANISOU 1881  CA ACYS A 199     2064    739   1288   -128   -100     73       C  
ATOM   1882  CA BCYS A 199      14.828  14.486  19.385  0.53 10.73           C  
ANISOU 1882  CA BCYS A 199     1719    769   1588   -108   -241    110       C  
ATOM   1883  C  ACYS A 199      14.369  15.203  20.287  0.47  9.40           C  
ANISOU 1883  C  ACYS A 199     1924    512   1136     37    -31    336       C  
ATOM   1884  C  BCYS A 199      14.399  15.312  20.567  0.53 12.55           C  
ANISOU 1884  C  BCYS A 199     1727   1049   1993    265   -368   -268       C  
ATOM   1885  O  ACYS A 199      13.203  15.596  20.520  0.47 12.52           O  
ANISOU 1885  O  ACYS A 199     2119    658   1981    352   -143     82       O  
ATOM   1886  O  BCYS A 199      13.221  15.712  20.722  0.53 12.32           O  
ANISOU 1886  O  BCYS A 199     1567   1094   2020     34     22    322       O  
ATOM   1887  CB ACYS A 199      14.904  12.909  19.478  0.47  9.20           C  
ANISOU 1887  CB ACYS A 199     1489    744   1261     56   -309     35       C  
ATOM   1888  CB BCYS A 199      15.075  13.043  19.836  0.53 11.27           C  
ANISOU 1888  CB BCYS A 199     2069    750   1463    -42    179    196       C  
ATOM   1889  SG ACYS A 199      14.913  11.779  18.051  0.47 12.09           S  
ANISOU 1889  SG ACYS A 199     2065    954   1576    -18   -125   -195       S  
ATOM   1890  SG BCYS A 199      14.984  11.883  18.441  0.53 12.72           S  
ANISOU 1890  SG BCYS A 199     2003    893   1939   -297    122    -93       S  
ATOM   1891  N  AGLN A 200      15.383  15.527  21.083  0.47 11.64           N  
ANISOU 1891  N  AGLN A 200     2141    985   1298     90   -142   -147       N  
ATOM   1892  N  BGLN A 200      15.319  15.626  21.451  0.53 11.33           N  
ANISOU 1892  N  BGLN A 200     1785    844   1676    143   -294    -37       N  
ATOM   1893  CA AGLN A 200      15.080  16.320  22.297  0.47 12.26           C  
ANISOU 1893  CA AGLN A 200     2048   1363   1249    141     30   -156       C  
ATOM   1894  CA BGLN A 200      14.958  16.365  22.659  0.53 12.35           C  
ANISOU 1894  CA BGLN A 200     1883   1216   1594    419   -213    -56       C  
ATOM   1895  C  AGLN A 200      14.556  17.678  21.917  0.47 12.31           C  
ANISOU 1895  C  AGLN A 200     1837   1185   1655     91   -212   -401       C  
ATOM   1896  C  BGLN A 200      14.462  17.752  22.320  0.53 13.23           C  
ANISOU 1896  C  BGLN A 200     2168   1040   1820    316   -290   -207       C  
ATOM   1897  O  AGLN A 200      13.699  18.276  22.559  0.47 16.14           O  
ANISOU 1897  O  AGLN A 200     2121   2081   1931    561   -265   -594       O  
ATOM   1898  O  BGLN A 200      13.558  18.249  23.000  0.53 15.17           O  
ANISOU 1898  O  BGLN A 200     2208   1032   2524    356    -69   -165       O  
ATOM   1899  CB AGLN A 200      16.330  16.438  23.203  0.47 13.24           C  
ANISOU 1899  CB AGLN A 200     2395   1464   1173    427   -171   -324       C  
ATOM   1900  CB BGLN A 200      16.174  16.463  23.619  0.53 12.91           C  
ANISOU 1900  CB BGLN A 200     2100   1134   1670    103   -347   -128       C  
ATOM   1901  CG AGLN A 200      16.694  15.028  23.777  0.47 14.28           C  
ANISOU 1901  CG AGLN A 200     2260   1654   1512   -236   -246    342       C  
ATOM   1902  CG BGLN A 200      16.505  15.043  24.184  0.53 12.20           C  
ANISOU 1902  CG BGLN A 200     2024   1161   1452    135   -291    -32       C  
ATOM   1903  CD AGLN A 200      17.800  15.122  24.807  0.47 14.51           C  
ANISOU 1903  CD AGLN A 200     2440   1757   1316    296   -203     11       C  
ATOM   1904  CD BGLN A 200      17.690  15.015  25.142  0.53 12.24           C  
ANISOU 1904  CD BGLN A 200     1854   1350   1447   -209   -188    145       C  
ATOM   1905  OE1AGLN A 200      17.845  14.257  25.696  0.47 26.05           O  
ANISOU 1905  OE1AGLN A 200     4492   3450   1957   -363   -956   1155       O  
ATOM   1906  OE1BGLN A 200      17.776  14.057  25.967  0.53 12.34           O  
ANISOU 1906  OE1BGLN A 200     1932   1057   1700    211    -85     86       O  
ATOM   1907  NE2AGLN A 200      18.711  16.050  24.732  0.47 14.55           N  
ANISOU 1907  NE2AGLN A 200     1728   2408   1393    313   -328   -150       N  
ATOM   1908  NE2BGLN A 200      18.616  15.934  25.052  0.53 13.68           N  
ANISOU 1908  NE2BGLN A 200     1869   1200   2128   -183   -183    174       N  
ATOM   1909  N  ASER A 201      15.046  18.292  20.829  0.47 13.32           N  
ANISOU 1909  N  ASER A 201     2304    820   1938    -41   -215   -265       N  
ATOM   1910  N  BSER A 201      15.009  18.404  21.294  0.53 13.75           N  
ANISOU 1910  N  BSER A 201     2185    931   2109    176   -354    -74       N  
ATOM   1911  CA ASER A 201      14.525  19.611  20.430  0.47 16.28           C  
ANISOU 1911  CA ASER A 201     2327   1004   2856    -60   -272    -34       C  
ATOM   1912  CA BSER A 201      14.555  19.716  20.835  0.53 16.59           C  
ANISOU 1912  CA BSER A 201     2362    858   3082     69   -306     68       C  
ATOM   1913  C  ASER A 201      13.050  19.593  20.038  0.47 16.73           C  
ANISOU 1913  C  ASER A 201     2474    809   3073    -23   -436    156       C  
ATOM   1914  C  BSER A 201      13.106  19.681  20.340  0.53 16.42           C  
ANISOU 1914  C  BSER A 201     2485    818   2935    204   -450    362       C  
ATOM   1915  O  ASER A 201      12.391  20.646  19.989  0.47 18.13           O  
ANISOU 1915  O  ASER A 201     2534    794   3560     28   -279    423       O  
ATOM   1916  O  BSER A 201      12.418  20.698  20.434  0.53 23.47           O  
ANISOU 1916  O  BSER A 201     3127   1394   4397    836  -1029   -441       O  
ATOM   1917  CB ASER A 201      15.402  20.160  19.272  0.47 17.29           C  
ANISOU 1917  CB ASER A 201     2756    921   2892     41   -105    139       C  
ATOM   1918  CB BSER A 201      15.463  20.241  19.691  0.53 19.14           C  
ANISOU 1918  CB BSER A 201     2802    893   3578    -92   -144    438       C  
ATOM   1919  OG ASER A 201      15.241  19.358  18.099  0.47 24.38           O  
ANISOU 1919  OG ASER A 201     3203   3205   2857    688   -352   -663       O  
ATOM   1920  OG BSER A 201      15.130  19.729  18.393  0.53 18.10           O  
ANISOU 1920  OG BSER A 201     2923    678   3276    121    203    622       O  
ATOM   1921  N  ALYS A 202      12.508  18.402  19.739  0.47 15.24           N  
ANISOU 1921  N  ALYS A 202     2182    826   2783    -22   -484    411       N  
ATOM   1922  N  BLYS A 202      12.654  18.541  19.809  0.53 16.47           N  
ANISOU 1922  N  BLYS A 202     2353   1061   2843    142   -591    264       N  
ATOM   1923  CA ALYS A 202      11.113  18.268  19.361  0.47 15.43           C  
ANISOU 1923  CA ALYS A 202     2059   1157   2648     41   -366    425       C  
ATOM   1924  CA BLYS A 202      11.337  18.289  19.267  0.53 16.00           C  
ANISOU 1924  CA BLYS A 202     2142   1215   2723    315   -470    362       C  
ATOM   1925  C  ALYS A 202      10.278  17.704  20.510  0.47 15.72           C  
ANISOU 1925  C  ALYS A 202     2370    912   2690   -202   -347    415       C  
ATOM   1926  C  BLYS A 202      10.366  17.811  20.350  0.53 16.16           C  
ANISOU 1926  C  BLYS A 202     2249   1028   2862    496   -282    392       C  
ATOM   1927  O  ALYS A 202       9.104  17.374  20.246  0.47 16.70           O  
ANISOU 1927  O  ALYS A 202     1979   1310   3058    265   -339    847       O  
ATOM   1928  O  BLYS A 202       9.203  17.603  19.954  0.53 21.37           O  
ANISOU 1928  O  BLYS A 202     2426   2702   2989   -266   -255   -109       O  
ATOM   1929  CB ALYS A 202      10.991  17.368  18.122  0.47 15.51           C  
ANISOU 1929  CB ALYS A 202     2123   1256   2516    338   -671    473       C  
ATOM   1930  CB BLYS A 202      11.414  17.225  18.158  0.53 17.88           C  
ANISOU 1930  CB BLYS A 202     1695   1970   3128   -126   -230   -224       C  
ATOM   1931  CG ALYS A 202      11.768  17.882  16.912  0.47 16.99           C  
ANISOU 1931  CG ALYS A 202     2097   1728   2630    261   -484    353       C  
ATOM   1932  CG BLYS A 202      12.193  17.644  16.926  0.53 19.84           C  
ANISOU 1932  CG BLYS A 202     1921   2314   3303    371     71   -102       C  
ATOM   1933  CD ALYS A 202      11.153  19.164  16.376  0.47 20.98           C  
ANISOU 1933  CD ALYS A 202     3288   1787   2898    327      5    866       C  
ATOM   1934  CD BLYS A 202      11.777  18.965  16.324  0.53 22.05           C  
ANISOU 1934  CD BLYS A 202     2781   2271   3324    198     87     43       C  
ATOM   1935  CE ALYS A 202      11.873  19.605  15.100  0.47 22.88           C  
ANISOU 1935  CE ALYS A 202     3649   2425   2619     49     -4    633       C  
ATOM   1936  CE BLYS A 202      12.580  19.188  15.045  0.53 23.04           C  
ANISOU 1936  CE BLYS A 202     2633   2948   3171    537      6    125       C  
ATOM   1937  NZ ALYS A 202      11.176  20.792  14.527  0.47 31.85           N  
ANISOU 1937  NZ ALYS A 202     5730   2937   3433   -449  -1731   1662       N  
ATOM   1938  NZ BLYS A 202      12.327  20.504  14.426  0.53 28.51           N  
ANISOU 1938  NZ BLYS A 202     3378   3428   4028   -219   -530   1053       N  
ATOM   1939  N  AGLY A 203      10.824  17.578  21.715  0.47 14.26           N  
ANISOU 1939  N  AGLY A 203     2179    662   2578    329   -172    229       N  
ATOM   1940  N  BGLY A 203      10.796  17.646  21.593  0.53 16.33           N  
ANISOU 1940  N  BGLY A 203     2438   1064   2701    341   -174     95       N  
ATOM   1941  CA AGLY A 203      10.088  17.074  22.863  0.47 15.47           C  
ANISOU 1941  CA AGLY A 203     2460    882   2535    292    111      2       C  
ATOM   1942  CA BGLY A 203       9.953  17.132  22.663  0.53 16.26           C  
ANISOU 1942  CA BGLY A 203     2518   1038   2624    439    -18    -94       C  
ATOM   1943  C  AGLY A 203       9.897  15.557  22.894  0.47 12.80           C  
ANISOU 1943  C  AGLY A 203     1939    934   1993    125     66     11       C  
ATOM   1944  C  BGLY A 203       9.756  15.616  22.659  0.53 13.73           C  
ANISOU 1944  C  BGLY A 203     1783   1097   2338    348   -187   -123       C  
ATOM   1945  O  AGLY A 203       9.062  15.082  23.675  0.47 16.23           O  
ANISOU 1945  O  AGLY A 203     1824   1307   3036    410    460    365       O  
ATOM   1946  O  BGLY A 203       8.760  15.147  23.215  0.53 16.52           O  
ANISOU 1946  O  BGLY A 203     2085   1278   2914    237    295   -544       O  
ATOM   1947  N   ILE A 204      10.663  14.848  22.070  1.00 11.72           N  
ANISOU 1947  N   ILE A 204     1865    906   1684    335   -269     29       N  
ATOM   1948  CA  ILE A 204      10.631  13.403  22.023  1.00 10.54           C  
ANISOU 1948  CA  ILE A 204     1673    853   1480    148   -251    124       C  
ATOM   1949  C   ILE A 204      11.666  12.882  22.987  1.00 10.35           C  
ANISOU 1949  C   ILE A 204     1394    894   1646    101   -133    142       C  
ATOM   1950  O   ILE A 204      12.834  13.240  22.924  1.00 14.65           O  
ANISOU 1950  O   ILE A 204     1570   1690   2307   -122   -357    827       O  
ATOM   1951  CB  ILE A 204      10.909  12.917  20.569  1.00 10.89           C  
ANISOU 1951  CB  ILE A 204     1619    939   1579    220   -109    111       C  
ATOM   1952  CG1 ILE A 204       9.826  13.479  19.603  1.00 12.92           C  
ANISOU 1952  CG1 ILE A 204     2024   1412   1473    170   -366    169       C  
ATOM   1953  CG2 ILE A 204      10.930  11.396  20.529  1.00 12.59           C  
ANISOU 1953  CG2 ILE A 204     2082    923   1780    121    -68    -15       C  
ATOM   1954  CD1 ILE A 204      10.161  13.260  18.137  1.00 17.24           C  
ANISOU 1954  CD1 ILE A 204     2808   2313   1428     77   -120    444       C  
ATOM   1955  N   VAL A 205      11.232  12.031  23.932  1.00  9.45           N  
ANISOU 1955  N   VAL A 205     1536    802   1251    270   -153    -88       N  
ATOM   1956  CA  VAL A 205      12.167  11.411  24.874  1.00  9.24           C  
ANISOU 1956  CA  VAL A 205     1446    816   1251    240    -66    -15       C  
ATOM   1957  C   VAL A 205      12.932  10.281  24.210  1.00  8.51           C  
ANISOU 1957  C   VAL A 205     1324    806   1103     42   -160    -88       C  
ATOM   1958  O   VAL A 205      12.376   9.502  23.423  1.00 10.49           O  
ANISOU 1958  O   VAL A 205     1285   1097   1605     84   -213   -433       O  
ATOM   1959  CB  VAL A 205      11.358  10.894  26.108  1.00 10.70           C  
ANISOU 1959  CB  VAL A 205     1677   1156   1233    258     22    -60       C  
ATOM   1960  CG1 VAL A 205      12.131   9.949  27.013  1.00 12.46           C  
ANISOU 1960  CG1 VAL A 205     1749   1537   1449    209   -121    277       C  
ATOM   1961  CG2 VAL A 205      10.825  12.121  26.878  1.00 13.11           C  
ANISOU 1961  CG2 VAL A 205     1947   1432   1603    248    238   -401       C  
ATOM   1962  N   VAL A 206      14.229  10.201  24.486  1.00  8.42           N  
ANISOU 1962  N   VAL A 206     1333    676   1191     86   -231    -57       N  
ATOM   1963  CA  VAL A 206      15.078   9.144  23.925  1.00  7.99           C  
ANISOU 1963  CA  VAL A 206     1288    655   1092     -3    -32     98       C  
ATOM   1964  C   VAL A 206      15.315   8.082  24.973  1.00  7.37           C  
ANISOU 1964  C   VAL A 206     1114    719    969     20    -92    -26       C  
ATOM   1965  O   VAL A 206      15.673   8.364  26.114  1.00  8.71           O  
ANISOU 1965  O   VAL A 206     1477    808   1025     23   -207    -92       O  
ATOM   1966  CB  VAL A 206      16.390   9.740  23.382  1.00  9.70           C  
ANISOU 1966  CB  VAL A 206     1443    792   1451   -105     76    146       C  
ATOM   1967  CG1 VAL A 206      17.346   8.629  22.929  1.00 11.37           C  
ANISOU 1967  CG1 VAL A 206     1508   1052   1761    -86    405    -98       C  
ATOM   1968  CG2 VAL A 206      16.055  10.731  22.231  1.00 13.56           C  
ANISOU 1968  CG2 VAL A 206     1912   1606   1632   -171    117    723       C  
ATOM   1969  N   THR A 207      15.110   6.820  24.549  1.00  7.34           N  
ANISOU 1969  N   THR A 207     1167    652    970     70    -79    -13       N  
ATOM   1970  CA  THR A 207      15.528   5.652  25.364  1.00  7.16           C  
ANISOU 1970  CA  THR A 207     1132    686    905    107    -60     37       C  
ATOM   1971  C   THR A 207      16.770   5.030  24.705  1.00  7.14           C  
ANISOU 1971  C   THR A 207     1201    757    756     32     -2     19       C  
ATOM   1972  O   THR A 207      16.745   4.743  23.501  1.00  9.19           O  
ANISOU 1972  O   THR A 207     1332   1362    797    260     20   -174       O  
ATOM   1973  CB  THR A 207      14.401   4.608  25.412  1.00  7.34           C  
ANISOU 1973  CB  THR A 207     1178    669    941     71     32    -16       C  
ATOM   1974  OG1 THR A 207      13.246   5.199  26.006  1.00  8.35           O  
ANISOU 1974  OG1 THR A 207     1085    945   1143     12     96    -72       O  
ATOM   1975  CG2 THR A 207      14.831   3.392  26.239  1.00  8.83           C  
ANISOU 1975  CG2 THR A 207     1515    811   1030     49    -37    181       C  
ATOM   1976  N   ALA A 208      17.797   4.827  25.512  1.00  7.03           N  
ANISOU 1976  N   ALA A 208     1119    714    837     91      1     -8       N  
ATOM   1977  CA  ALA A 208      19.051   4.182  25.102  1.00  7.01           C  
ANISOU 1977  CA  ALA A 208      981    750    932     59     90    -33       C  
ATOM   1978  C   ALA A 208      18.945   2.675  25.314  1.00  6.63           C  
ANISOU 1978  C   ALA A 208     1058    727    736     -5     15     53       C  
ATOM   1979  O   ALA A 208      18.797   2.207  26.454  1.00  8.62           O  
ANISOU 1979  O   ALA A 208     1709    843    724    -85     93    -69       O  
ATOM   1980  CB  ALA A 208      20.196   4.726  25.952  1.00  8.45           C  
ANISOU 1980  CB  ALA A 208     1157    914   1140    -77    -20    -73       C  
ATOM   1981  N   TYR A 209      19.061   1.937  24.215  1.00  6.91           N  
ANISOU 1981  N   TYR A 209     1236    712    677     51     14     -7       N  
ATOM   1982  CA  TYR A 209      19.156   0.469  24.280  1.00  6.83           C  
ANISOU 1982  CA  TYR A 209     1158    627    809      7     27     13       C  
ATOM   1983  C   TYR A 209      20.617   0.013  24.122  1.00  6.92           C  
ANISOU 1983  C   TYR A 209     1117    690    824    -40      4    -39       C  
ATOM   1984  O   TYR A 209      21.495   0.764  23.679  1.00  7.58           O  
ANISOU 1984  O   TYR A 209     1137    767    976    -51     46     73       O  
ATOM   1985  CB  TYR A 209      18.203  -0.161  23.322  1.00  7.60           C  
ANISOU 1985  CB  TYR A 209     1198    869    819    -36     58    -54       C  
ATOM   1986  CG  TYR A 209      18.449  -0.248  21.848  1.00  6.87           C  
ANISOU 1986  CG  TYR A 209     1102    675    835    -13     64    -21       C  
ATOM   1987  CD1 TYR A 209      19.519  -0.970  21.288  1.00  7.04           C  
ANISOU 1987  CD1 TYR A 209     1132    730    814      0     33    -17       C  
ATOM   1988  CD2 TYR A 209      17.552   0.299  20.933  1.00  7.21           C  
ANISOU 1988  CD2 TYR A 209     1057    719    965     11     44    -18       C  
ATOM   1989  CE1 TYR A 209      19.713  -1.098  19.939  1.00  7.40           C  
ANISOU 1989  CE1 TYR A 209     1154    806    853     11     29      9       C  
ATOM   1990  CE2 TYR A 209      17.673   0.120  19.554  1.00  7.13           C  
ANISOU 1990  CE2 TYR A 209     1057    752    900     14     75     12       C  
ATOM   1991  CZ  TYR A 209      18.756  -0.585  19.054  1.00  6.99           C  
ANISOU 1991  CZ  TYR A 209     1168    715    774    -43     64     61       C  
ATOM   1992  OH  TYR A 209      18.897  -0.861  17.728  1.00  8.38           O  
ANISOU 1992  OH  TYR A 209     1304   1052    828     91    115     34       O  
ATOM   1993  N   SER A 210      20.846  -1.253  24.478  1.00  7.05           N  
ANISOU 1993  N   SER A 210     1146    667    864     52    -27     40       N  
ATOM   1994  CA  SER A 210      22.184  -1.872  24.493  1.00  7.63           C  
ANISOU 1994  CA  SER A 210     1184    837    879     76     10    -45       C  
ATOM   1995  C   SER A 210      23.190  -0.974  25.203  1.00  7.15           C  
ANISOU 1995  C   SER A 210     1046    814    857     74    122     56       C  
ATOM   1996  O   SER A 210      24.307  -0.756  24.698  1.00  8.48           O  
ANISOU 1996  O   SER A 210     1162   1066    995     13    128      4       O  
ATOM   1997  CB  SER A 210      22.666  -2.256  23.079  1.00  8.56           C  
ANISOU 1997  CB  SER A 210     1365    947    942     68     29   -153       C  
ATOM   1998  OG  SER A 210      21.732  -3.120  22.450  1.00  9.00           O  
ANISOU 1998  OG  SER A 210     1559    938    921    142    -87   -110       O  
ATOM   1999  N   PRO A 211      22.891  -0.465  26.405  1.00  7.45           N  
ANISOU 1999  N   PRO A 211     1073    817    941     13     51    -12       N  
ATOM   2000  CA  PRO A 211      23.813   0.488  27.067  1.00  7.99           C  
ANISOU 2000  CA  PRO A 211     1164    798   1076     38     49   -150       C  
ATOM   2001  C   PRO A 211      25.124  -0.162  27.524  1.00  7.62           C  
ANISOU 2001  C   PRO A 211     1109    814    971    -30    108   -170       C  
ATOM   2002  O   PRO A 211      26.087   0.589  27.767  1.00  9.12           O  
ANISOU 2002  O   PRO A 211     1214    922   1329   -124    -37   -165       O  
ATOM   2003  CB  PRO A 211      22.990   0.971  28.287  1.00  8.90           C  
ANISOU 2003  CB  PRO A 211     1248   1026   1109    -12    181   -158       C  
ATOM   2004  CG  PRO A 211      22.140  -0.247  28.624  1.00  8.81           C  
ANISOU 2004  CG  PRO A 211     1326   1057    964    -22     80    -90       C  
ATOM   2005  CD  PRO A 211      21.701  -0.760  27.245  1.00  8.06           C  
ANISOU 2005  CD  PRO A 211     1133   1065    864     -7    161    -42       C  
ATOM   2006  N   LEU A 212      25.156  -1.490  27.630  1.00  7.94           N  
ANISOU 2006  N   LEU A 212     1067    801   1149     43    -25    -72       N  
ATOM   2007  CA  LEU A 212      26.382  -2.204  28.020  1.00  8.86           C  
ANISOU 2007  CA  LEU A 212     1093    990   1283     90   -130    -49       C  
ATOM   2008  C   LEU A 212      27.096  -2.757  26.779  1.00  9.61           C  
ANISOU 2008  C   LEU A 212     1166    922   1564     38     81   -154       C  
ATOM   2009  O   LEU A 212      28.080  -3.487  26.917  1.00 12.58           O  
ANISOU 2009  O   LEU A 212     1206   1316   2259    341     33   -108       O  
ATOM   2010  CB  LEU A 212      26.095  -3.309  29.009  1.00  9.67           C  
ANISOU 2010  CB  LEU A 212     1260   1044   1372      2   -220     20       C  
ATOM   2011  CG  LEU A 212      25.227  -2.910  30.207  1.00 11.36           C  
ANISOU 2011  CG  LEU A 212     1846   1249   1222   -170    -33    -26       C  
ATOM   2012  CD1 LEU A 212      24.939  -4.159  31.108  1.00 14.92           C  
ANISOU 2012  CD1 LEU A 212     2736   1498   1436   -176     38    285       C  
ATOM   2013  CD2 LEU A 212      25.833  -1.779  31.005  1.00 15.23           C  
ANISOU 2013  CD2 LEU A 212     2789   1464   1535   -256     28   -341       C  
ATOM   2014  N   GLY A 213      26.588  -2.424  25.570  1.00  9.23           N  
ANISOU 2014  N   GLY A 213     1168   1041   1300    -48    161   -151       N  
ATOM   2015  CA  GLY A 213      27.210  -2.947  24.327  1.00 11.42           C  
ANISOU 2015  CA  GLY A 213     1523   1166   1651   -153    519   -442       C  
ATOM   2016  C   GLY A 213      26.711  -4.344  23.977  1.00 11.32           C  
ANISOU 2016  C   GLY A 213     1393   1158   1749   -139    606   -369       C  
ATOM   2017  O   GLY A 213      27.315  -4.973  23.112  1.00 14.48           O  
ANISOU 2017  O   GLY A 213     1808   1466   2229   -265    966   -796       O  
ATOM   2018  N   SER A 214      25.644  -4.843  24.607  1.00  9.69           N  
ANISOU 2018  N   SER A 214     1238    902   1544    -18    341   -172       N  
ATOM   2019  CA  SER A 214      25.026  -6.123  24.196  1.00  9.77           C  
ANISOU 2019  CA  SER A 214     1323    868   1520     35    313   -335       C  
ATOM   2020  C   SER A 214      26.057  -7.238  24.081  1.00 10.67           C  
ANISOU 2020  C   SER A 214     1275    978   1802     49    359   -327       C  
ATOM   2021  O   SER A 214      26.166  -7.876  23.013  1.00 11.70           O  
ANISOU 2021  O   SER A 214     1549   1088   1809    196    427   -381       O  
ATOM   2022  CB  SER A 214      24.225  -5.965  22.917  1.00 10.37           C  
ANISOU 2022  CB  SER A 214     1359   1046   1533      1    321   -267       C  
ATOM   2023  OG  SER A 214      23.285  -7.043  22.742  1.00 11.42           O  
ANISOU 2023  OG  SER A 214     1350   1158   1832      6    178   -431       O  
ATOM   2024  N   PRO A 215      26.796  -7.567  25.155  1.00 11.97           N  
ANISOU 2024  N   PRO A 215     1283   1167   2097    152    114   -484       N  
ATOM   2025  CA  PRO A 215      27.836  -8.623  25.023  1.00 14.76           C  
ANISOU 2025  CA  PRO A 215     1474   1319   2815    296   -322   -568       C  
ATOM   2026  C   PRO A 215      27.270 -10.005  24.708  1.00 12.99           C  
ANISOU 2026  C   PRO A 215     1371   1195   2367    353     61   -314       C  
ATOM   2027  O   PRO A 215      28.046 -10.838  24.204  1.00 16.74           O  
ANISOU 2027  O   PRO A 215     1804   1374   3181    441    489   -485       O  
ATOM   2028  CB  PRO A 215      28.567  -8.592  26.353  1.00 18.09           C  
ANISOU 2028  CB  PRO A 215     1932   2103   2836    591   -492   -778       C  
ATOM   2029  CG  PRO A 215      27.720  -7.816  27.301  1.00 16.06           C  
ANISOU 2029  CG  PRO A 215     1616   2010   2477    509   -216   -134       C  
ATOM   2030  CD  PRO A 215      26.919  -6.868  26.425  1.00 12.05           C  
ANISOU 2030  CD  PRO A 215     1445   1329   1806     11    102   -122       C  
ATOM   2031  N   ASP A 216      26.012 -10.255  24.923  1.00 11.80           N  
ANISOU 2031  N   ASP A 216     1410   1159   1916    231    -48   -280       N  
ATOM   2032  CA  ASP A 216      25.354 -11.530  24.615  1.00 11.09           C  
ANISOU 2032  CA  ASP A 216     1637   1097   1481    155     89   -212       C  
ATOM   2033  C   ASP A 216      24.669 -11.528  23.276  1.00 10.69           C  
ANISOU 2033  C   ASP A 216     1571   1078   1414    250    171   -239       C  
ATOM   2034  O   ASP A 216      24.024 -12.519  22.915  1.00 12.56           O  
ANISOU 2034  O   ASP A 216     1860   1284   1628     34     95   -230       O  
ATOM   2035  CB  ASP A 216      24.405 -11.953  25.750  1.00 11.66           C  
ANISOU 2035  CB  ASP A 216     1523   1497   1411    331     95    -97       C  
ATOM   2036  CG  ASP A 216      23.278 -10.927  25.985  1.00 12.93           C  
ANISOU 2036  CG  ASP A 216     1553   2121   1238    453    -41   -480       C  
ATOM   2037  OD1 ASP A 216      23.428  -9.726  25.677  1.00 14.66           O  
ANISOU 2037  OD1 ASP A 216     1896   2046   1629    976    -83   -355       O  
ATOM   2038  OD2 ASP A 216      22.224 -11.394  26.549  1.00 16.53           O  
ANISOU 2038  OD2 ASP A 216     1482   3416   1383    264     97   -425       O  
ATOM   2039  N  AARG A 217      24.774 -10.483  22.443  0.57 11.48           N  
ANISOU 2039  N  AARG A 217     1753   1083   1526    410    169   -229       N  
ATOM   2040  N  BARG A 217      24.959 -10.507  22.422  0.43 12.09           N  
ANISOU 2040  N  BARG A 217     1818   1421   1354     75    423   -176       N  
ATOM   2041  CA AARG A 217      24.211 -10.479  21.109  0.57 11.32           C  
ANISOU 2041  CA AARG A 217     1891   1187   1222    230    312   -198       C  
ATOM   2042  CA BARG A 217      24.304 -10.537  21.106  0.43 12.12           C  
ANISOU 2042  CA BARG A 217     1998   1241   1368    259    172   -232       C  
ATOM   2043  C  AARG A 217      24.700 -11.718  20.352  0.57 11.57           C  
ANISOU 2043  C  AARG A 217     1587   1200   1611     37    356   -351       C  
ATOM   2044  C  BARG A 217      24.808 -11.755  20.308  0.43 12.03           C  
ANISOU 2044  C  BARG A 217     1837   1093   1640    257     11   -280       C  
ATOM   2045  O  AARG A 217      25.862 -12.166  20.472  0.57 12.78           O  
ANISOU 2045  O  AARG A 217     1902   1281   1673    319    128   -432       O  
ATOM   2046  O  BARG A 217      26.037 -12.045  20.397  0.43 14.15           O  
ANISOU 2046  O  BARG A 217     1694   1840   1841    177    395   -410       O  
ATOM   2047  CB AARG A 217      24.635  -9.199  20.389  0.57 13.58           C  
ANISOU 2047  CB AARG A 217     2246   1213   1701     34    346   -104       C  
ATOM   2048  CB BARG A 217      24.473  -9.253  20.306  0.43 13.63           C  
ANISOU 2048  CB BARG A 217     2625   1102   1451    417    461   -322       C  
ATOM   2049  CG AARG A 217      26.161  -9.127  20.119  0.57 13.30           C  
ANISOU 2049  CG AARG A 217     2446   1075   1533     65    936   -447       C  
ATOM   2050  CG BARG A 217      25.817  -8.976  19.660  0.43 17.73           C  
ANISOU 2050  CG BARG A 217     2923   1575   2240     30    752     42       C  
ATOM   2051  CD AARG A 217      26.551  -7.686  19.785  0.57 14.56           C  
ANISOU 2051  CD AARG A 217     2448   1362   1720    -50    812    -75       C  
ATOM   2052  CD BARG A 217      25.955  -7.508  19.221  0.43 15.53           C  
ANISOU 2052  CD BARG A 217     2343   1388   2171    331    575   -230       C  
ATOM   2053  NE AARG A 217      27.975  -7.615  19.457  0.57 16.38           N  
ANISOU 2053  NE AARG A 217     2429   1733   2061   -186    668    -83       N  
ATOM   2054  NE BARG A 217      27.364  -7.275  18.862  0.43 14.85           N  
ANISOU 2054  NE BARG A 217     2359   1724   1559    215    380    142       N  
ATOM   2055  CZ AARG A 217      28.966  -7.541  20.320  0.57 15.52           C  
ANISOU 2055  CZ AARG A 217     2309   1919   1670   -249    998   -163       C  
ATOM   2056  CZ BARG A 217      28.457  -7.223  19.623  0.43 14.89           C  
ANISOU 2056  CZ BARG A 217     2341   1941   1376    259    471   -382       C  
ATOM   2057  NH1AARG A 217      28.674  -7.501  21.614  0.57 18.90           N  
ANISOU 2057  NH1AARG A 217     2600   2758   1824   -367   1013   -949       N  
ATOM   2058  NH1BARG A 217      29.666  -7.006  19.068  0.43 18.29           N  
ANISOU 2058  NH1BARG A 217     2315   2616   2020    274    444    528       N  
ATOM   2059  NH2AARG A 217      30.263  -7.490  19.940  0.57 16.77           N  
ANISOU 2059  NH2AARG A 217     2239   1786   2348   -287   1031   -571       N  
ATOM   2060  NH2BARG A 217      28.468  -7.367  20.946  0.43 19.27           N  
ANISOU 2060  NH2BARG A 217     3157   2802   1365   -767    240   -326       N  
ATOM   2061  N   PRO A 218      23.880 -12.399  19.563  1.00 13.33           N  
ANISOU 2061  N   PRO A 218     1984   1401   1681    161     68   -411       N  
ATOM   2062  CA  PRO A 218      24.323 -13.695  18.976  1.00 15.13           C  
ANISOU 2062  CA  PRO A 218     2530   1233   1984    -34    290   -507       C  
ATOM   2063  C   PRO A 218      25.432 -13.585  17.941  1.00 15.48           C  
ANISOU 2063  C   PRO A 218     2884   1239   1757    396    404   -390       C  
ATOM   2064  O   PRO A 218      26.070 -14.594  17.625  1.00 19.78           O  
ANISOU 2064  O   PRO A 218     3359   1612   2544    801    434   -369       O  
ATOM   2065  CB  PRO A 218      23.048 -14.200  18.323  1.00 23.21           C  
ANISOU 2065  CB  PRO A 218     2984   2293   3539   -339   -185  -1308       C  
ATOM   2066  CG  PRO A 218      21.934 -13.355  18.740  1.00 23.58           C  
ANISOU 2066  CG  PRO A 218     2836   2435   3689    235  -1241  -1060       C  
ATOM   2067  CD  PRO A 218      22.451 -12.078  19.367  1.00 16.18           C  
ANISOU 2067  CD  PRO A 218     1854   2298   1995     74      1   -633       C  
ATOM   2068  N   TRP A 219      25.620 -12.438  17.354  1.00 15.08           N  
ANISOU 2068  N   TRP A 219     2556   1323   1853    156    447   -409       N  
ATOM   2069  CA  TRP A 219      26.587 -12.272  16.257  1.00 15.23           C  
ANISOU 2069  CA  TRP A 219     2418   1634   1734    462    389   -344       C  
ATOM   2070  C   TRP A 219      27.898 -11.674  16.804  1.00 15.77           C  
ANISOU 2070  C   TRP A 219     2176   1914   1902    568    423   -419       C  
ATOM   2071  O   TRP A 219      28.752 -11.285  15.978  1.00 19.50           O  
ANISOU 2071  O   TRP A 219     2390   2710   2311    364    706   -349       O  
ATOM   2072  CB  TRP A 219      26.025 -11.440  15.121  1.00 15.71           C  
ANISOU 2072  CB  TRP A 219     2522   1643   1805    532    227   -438       C  
ATOM   2073  CG  TRP A 219      25.403 -10.133  15.602  1.00 14.77           C  
ANISOU 2073  CG  TRP A 219     2185   1487   1941    338    313   -335       C  
ATOM   2074  CD1 TRP A 219      26.045  -8.954  15.860  1.00 15.92           C  
ANISOU 2074  CD1 TRP A 219     1987   1618   2446    268    272   -495       C  
ATOM   2075  CD2 TRP A 219      24.024  -9.893  15.875  1.00 14.46           C  
ANISOU 2075  CD2 TRP A 219     2166   1322   2006    198    459    -28       C  
ATOM   2076  NE1 TRP A 219      25.151  -7.992  16.270  1.00 16.20           N  
ANISOU 2076  NE1 TRP A 219     1995   1591   2571    294     11   -577       N  
ATOM   2077  CE2 TRP A 219      23.895  -8.561  16.290  1.00 13.39           C  
ANISOU 2077  CE2 TRP A 219     2030   1407   1648    340    194    -92       C  
ATOM   2078  CE3 TRP A 219      22.865 -10.719  15.797  1.00 16.47           C  
ANISOU 2078  CE3 TRP A 219     2325   1767   2165    -95    299      0       C  
ATOM   2079  CZ2 TRP A 219      22.655  -7.998  16.629  1.00 13.97           C  
ANISOU 2079  CZ2 TRP A 219     2008   1660   1640    373    374    137       C  
ATOM   2080  CZ3 TRP A 219      21.639 -10.164  16.138  1.00 17.03           C  
ANISOU 2080  CZ3 TRP A 219     2144   1998   2327     16     20     80       C  
ATOM   2081  CH2 TRP A 219      21.565  -8.807  16.547  1.00 15.14           C  
ANISOU 2081  CH2 TRP A 219     2070   1984   1699    190     38    214       C  
ATOM   2082  N   ALA A 220      28.097 -11.611  18.111  1.00 16.63           N  
ANISOU 2082  N   ALA A 220     2422   1927   1971    353    166   -511       N  
ATOM   2083  CA  ALA A 220      29.377 -11.129  18.706  1.00 17.93           C  
ANISOU 2083  CA  ALA A 220     2126   2132   2554    383    217   -679       C  
ATOM   2084  C   ALA A 220      30.528 -12.007  18.216  1.00 21.70           C  
ANISOU 2084  C   ALA A 220     2400   2137   3710    466    448   -867       C  
ATOM   2085  O   ALA A 220      30.379 -13.213  18.070  1.00 24.73           O  
ANISOU 2085  O   ALA A 220     3074   2052   4270    644    456   -715       O  
ATOM   2086  CB  ALA A 220      29.345 -11.225  20.233  1.00 21.79           C  
ANISOU 2086  CB  ALA A 220     2430   3332   2517   -294   -180   -910       C  
ATOM   2087  N   LYS A 221      31.679 -11.352  18.015  1.00 23.45           N  
ANISOU 2087  N   LYS A 221     2252   2601   4056    563    786   -610       N  
ATOM   2088  CA  LYS A 221      32.899 -12.014  17.560  1.00 28.02           C  
ANISOU 2088  CA  LYS A 221     2580   3648   4417   1094    843   -759       C  
ATOM   2089  C   LYS A 221      33.964 -11.817  18.650  1.00 27.71           C  
ANISOU 2089  C   LYS A 221     2350   3086   5094    917    642   -668       C  
ATOM   2090  O   LYS A 221      33.901 -10.777  19.324  1.00 32.27           O  
ANISOU 2090  O   LYS A 221     2741   3728   5794   1008    295  -1351       O  
ATOM   2091  CB  LYS A 221      33.376 -11.403  16.242  1.00 35.69           C  
ANISOU 2091  CB  LYS A 221     3134   5768   4660   1471   1584   -392       C  
ATOM   2092  CG  LYS A 221      32.506 -11.732  15.048  1.00 42.14           C  
ANISOU 2092  CG  LYS A 221     3334   8231   4445   2055   1217    103       C  
ATOM   2093  CD  LYS A 221      33.202 -11.365  13.769  1.00 50.92           C  
ANISOU 2093  CD  LYS A 221     6541   8116   4691   1892   1847    901       C  
ATOM   2094  CE  LYS A 221      32.931  -9.943  13.309  1.00 61.60           C  
ANISOU 2094  CE  LYS A 221     8573   8611   6220   2704   1219   1491       C  
ATOM   2095  NZ  LYS A 221      33.761  -9.554  12.119  1.00 69.87           N  
ANISOU 2095  NZ  LYS A 221    11316   8257   6973   4613   2595   3032       N  
ATOM   2096  N   PRO A 222      34.891 -12.713  18.922  1.00 32.33           N  
ANISOU 2096  N   PRO A 222     2360   3608   6316   1186    265   -841       N  
ATOM   2097  CA  PRO A 222      35.916 -12.498  19.990  1.00 36.72           C  
ANISOU 2097  CA  PRO A 222     2216   4519   7218   1149    -92   -968       C  
ATOM   2098  C   PRO A 222      36.745 -11.220  19.813  1.00 38.38           C  
ANISOU 2098  C   PRO A 222     2558   4521   7503    959   -224  -1053       C  
ATOM   2099  O   PRO A 222      37.218 -10.585  20.782  1.00 37.83           O  
ANISOU 2099  O   PRO A 222     2646   4710   7019    748    -89   -677       O  
ATOM   2100  CB  PRO A 222      36.801 -13.741  19.913  1.00 39.39           C  
ANISOU 2100  CB  PRO A 222     4099   4704   6164   2042   -214    606       C  
ATOM   2101  CG  PRO A 222      35.998 -14.774  19.191  1.00 40.65           C  
ANISOU 2101  CG  PRO A 222     4666   3991   6790   2058    770   -100       C  
ATOM   2102  CD  PRO A 222      35.015 -14.060  18.296  1.00 37.42           C  
ANISOU 2102  CD  PRO A 222     3009   4081   7130   1925    355  -1492       C  
ATOM   2103  N   GLU A 223      36.961 -10.767  18.566  1.00 37.23           N  
ANISOU 2103  N   GLU A 223     2445   4626   7074    245   1023  -2283       N  
ATOM   2104  CA  GLU A 223      37.725  -9.541  18.337  1.00 42.53           C  
ANISOU 2104  CA  GLU A 223     2826   5127   8208    -60   2535  -2639       C  
ATOM   2105  C   GLU A 223      36.983  -8.219  18.502  1.00 41.01           C  
ANISOU 2105  C   GLU A 223     2767   4655   8158   -334   2050  -2344       C  
ATOM   2106  O   GLU A 223      37.579  -7.122  18.413  1.00 47.28           O  
ANISOU 2106  O   GLU A 223     3209   5124   9632  -1149   2865  -4427       O  
ATOM   2107  CB  GLU A 223      38.309  -9.497  16.916  1.00 49.80           C  
ANISOU 2107  CB  GLU A 223     4355   6226   8342  -1395   3080  -3552       C  
ATOM   2108  CG  GLU A 223      37.271  -9.715  15.833  1.00 55.24           C  
ANISOU 2108  CG  GLU A 223     6225   6481   8282  -2402   2305  -3070       C  
ATOM   2109  CD  GLU A 223      37.079 -11.156  15.414  1.00 52.53           C  
ANISOU 2109  CD  GLU A 223     7095   6209   6654  -1494   2280  -2864       C  
ATOM   2110  OE1 GLU A 223      36.880 -11.388  14.204  1.00 67.12           O  
ANISOU 2110  OE1 GLU A 223     9650   8872   6981  -3554   1753  -3393       O  
ATOM   2111  OE2 GLU A 223      37.089 -12.068  16.261  1.00 51.06           O  
ANISOU 2111  OE2 GLU A 223     4709   6381   8312    662   2881  -1974       O  
ATOM   2112  N   ASP A 224      35.674  -8.279  18.722  1.00 34.60           N  
ANISOU 2112  N   ASP A 224     2741   4087   6317   -244   1880  -2438       N  
ATOM   2113  CA  ASP A 224      34.919  -7.082  18.943  1.00 31.16           C  
ANISOU 2113  CA  ASP A 224     3030   3947   4864   -122   1325  -2234       C  
ATOM   2114  C   ASP A 224      35.279  -6.311  20.219  1.00 30.17           C  
ANISOU 2114  C   ASP A 224     3471   3625   4365    688    488  -1585       C  
ATOM   2115  O   ASP A 224      35.684  -6.838  21.246  1.00 32.61           O  
ANISOU 2115  O   ASP A 224     2768   4660   4963    898    645   -771       O  
ATOM   2116  CB  ASP A 224      33.411  -7.461  19.009  1.00 24.68           C  
ANISOU 2116  CB  ASP A 224     2848   3476   3053    126   1338   -565       C  
ATOM   2117  CG  ASP A 224      32.845  -7.812  17.655  1.00 25.43           C  
ANISOU 2117  CG  ASP A 224     3389   3003   3270   -233   1301   -918       C  
ATOM   2118  OD1 ASP A 224      33.444  -7.534  16.602  1.00 33.18           O  
ANISOU 2118  OD1 ASP A 224     4911   4561   3134  -1109   1298   -555       O  
ATOM   2119  OD2 ASP A 224      31.740  -8.392  17.604  1.00 28.69           O  
ANISOU 2119  OD2 ASP A 224     3409   3571   3922   -225   1166  -1194       O  
ATOM   2120  N   PRO A 225      35.113  -4.982  20.197  1.00 27.02           N  
ANISOU 2120  N   PRO A 225     3274   3327   3666   -375   1602  -1304       N  
ATOM   2121  CA  PRO A 225      35.334  -4.188  21.406  1.00 30.07           C  
ANISOU 2121  CA  PRO A 225     3891   3823   3713   -276   1773  -1587       C  
ATOM   2122  C   PRO A 225      34.347  -4.595  22.493  1.00 22.72           C  
ANISOU 2122  C   PRO A 225     2400   3351   2881    160    466   -976       C  
ATOM   2123  O   PRO A 225      33.240  -5.086  22.263  1.00 23.53           O  
ANISOU 2123  O   PRO A 225     2383   3738   2819    260     13   -835       O  
ATOM   2124  CB  PRO A 225      35.037  -2.765  20.924  1.00 34.95           C  
ANISOU 2124  CB  PRO A 225     5483   3266   4532  -1221   2505  -1455       C  
ATOM   2125  CG  PRO A 225      35.094  -2.791  19.429  1.00 37.03           C  
ANISOU 2125  CG  PRO A 225     6334   3253   4484   -801    442  -1329       C  
ATOM   2126  CD  PRO A 225      34.722  -4.201  19.031  1.00 33.09           C  
ANISOU 2126  CD  PRO A 225     5189   3282   4100  -1208    914   -864       C  
ATOM   2127  N   SER A 226      34.779  -4.358  23.723  1.00 24.45           N  
ANISOU 2127  N   SER A 226     2076   4045   3168    205    250  -1282       N  
ATOM   2128  CA  SER A 226      33.994  -4.600  24.945  1.00 20.79           C  
ANISOU 2128  CA  SER A 226     2222   2988   2691    553   -125   -841       C  
ATOM   2129  C   SER A 226      33.961  -3.384  25.845  1.00 18.19           C  
ANISOU 2129  C   SER A 226     1527   2528   2855    314    -70   -637       C  
ATOM   2130  O   SER A 226      35.022  -3.065  26.459  1.00 20.45           O  
ANISOU 2130  O   SER A 226     1497   3165   3110    497   -315   -795       O  
ATOM   2131  CB  SER A 226      34.633  -5.789  25.692  1.00 26.07           C  
ANISOU 2131  CB  SER A 226     2773   2788   4346    973   -213   -797       C  
ATOM   2132  OG  SER A 226      34.110  -5.888  27.029  1.00 29.56           O  
ANISOU 2132  OG  SER A 226     2936   3829   4469    165   -374    900       O  
ATOM   2133  N   LEU A 227      32.805  -2.755  26.017  1.00 15.38           N  
ANISOU 2133  N   LEU A 227     1345   2094   2404    160   -121   -123       N  
ATOM   2134  CA  LEU A 227      32.711  -1.643  26.930  1.00 14.35           C  
ANISOU 2134  CA  LEU A 227     1423   1580   2449    142   -189     26       C  
ATOM   2135  C   LEU A 227      32.973  -2.024  28.352  1.00 14.06           C  
ANISOU 2135  C   LEU A 227     1594   1289   2459    212   -223    -18       C  
ATOM   2136  O   LEU A 227      33.577  -1.251  29.081  1.00 15.76           O  
ANISOU 2136  O   LEU A 227     1820   1618   2552    -98   -342     67       O  
ATOM   2137  CB  LEU A 227      31.236  -1.074  26.892  1.00 14.11           C  
ANISOU 2137  CB  LEU A 227     1305   1777   2278     58    153    411       C  
ATOM   2138  CG  LEU A 227      30.957  -0.249  25.656  1.00 12.68           C  
ANISOU 2138  CG  LEU A 227     1380   1365   2074    -31   -107    -40       C  
ATOM   2139  CD1 LEU A 227      29.476  -0.126  25.501  1.00 14.65           C  
ANISOU 2139  CD1 LEU A 227     1501   1559   2505     26   -355     94       C  
ATOM   2140  CD2 LEU A 227      31.619   1.121  25.769  1.00 13.86           C  
ANISOU 2140  CD2 LEU A 227     1696   1340   2230   -118    319   -144       C  
ATOM   2141  N   LEU A 228      32.480  -3.186  28.799  1.00 14.32           N  
ANISOU 2141  N   LEU A 228     1458   1536   2447     59     -9     76       N  
ATOM   2142  CA  LEU A 228      32.656  -3.563  30.201  1.00 15.85           C  
ANISOU 2142  CA  LEU A 228     1681   1932   2408   -203   -197    173       C  
ATOM   2143  C   LEU A 228      34.105  -3.762  30.615  1.00 18.41           C  
ANISOU 2143  C   LEU A 228     1874   2587   2535   -409   -367    450       C  
ATOM   2144  O   LEU A 228      34.405  -3.630  31.793  1.00 22.14           O  
ANISOU 2144  O   LEU A 228     2617   3167   2628   -397   -882    394       O  
ATOM   2145  CB  LEU A 228      31.818  -4.841  30.453  1.00 17.66           C  
ANISOU 2145  CB  LEU A 228     1910   2036   2762   -373    -19    328       C  
ATOM   2146  CG  LEU A 228      30.316  -4.605  30.533  1.00 17.14           C  
ANISOU 2146  CG  LEU A 228     1851   2364   2298   -504    -22     17       C  
ATOM   2147  CD1 LEU A 228      29.628  -6.006  30.546  1.00 24.07           C  
ANISOU 2147  CD1 LEU A 228     2860   3221   3066  -1628    -54    337       C  
ATOM   2148  CD2 LEU A 228      29.874  -3.803  31.704  1.00 23.10           C  
ANISOU 2148  CD2 LEU A 228     3086   3269   2423    214    298    -33       C  
ATOM   2149  N   GLU A 229      34.947  -4.038  29.607  1.00 16.10           N  
ANISOU 2149  N   GLU A 229     1651   1300   3167    -15   -239    262       N  
ATOM   2150  CA  GLU A 229      36.382  -4.247  29.873  1.00 18.97           C  
ANISOU 2150  CA  GLU A 229     1768   1349   4091      3   -754    239       C  
ATOM   2151  C   GLU A 229      37.291  -3.119  29.412  1.00 16.48           C  
ANISOU 2151  C   GLU A 229     1582   1300   3379     59   -650    -36       C  
ATOM   2152  O   GLU A 229      38.491  -3.255  29.486  1.00 19.77           O  
ANISOU 2152  O   GLU A 229     1615   1773   4122     59   -750    134       O  
ATOM   2153  CB AGLU A 229      36.766  -5.596  29.282  0.74 22.51           C  
ANISOU 2153  CB AGLU A 229     1749   1354   5448    114   -628      9       C  
ATOM   2154  CB BGLU A 229      36.787  -5.504  29.089  0.26 22.37           C  
ANISOU 2154  CB BGLU A 229     1673   1239   5588    148   -757    -98       C  
ATOM   2155  CG AGLU A 229      35.926  -6.750  29.901  0.74 26.21           C  
ANISOU 2155  CG AGLU A 229     2160   1327   6472    152   -537    537       C  
ATOM   2156  CG BGLU A 229      36.573  -6.862  29.744  0.26 28.51           C  
ANISOU 2156  CG BGLU A 229     3489   1327   6017   -270   -410    -40       C  
ATOM   2157  CD AGLU A 229      36.246  -7.926  29.009  0.74 33.78           C  
ANISOU 2157  CD AGLU A 229     3879   1547   7410   -231   -489   -138       C  
ATOM   2158  CD BGLU A 229      37.745  -7.155  30.676  0.26 29.00           C  
ANISOU 2158  CD BGLU A 229     4761   1770   4489    710   -255    127       C  
ATOM   2159  OE1AGLU A 229      35.356  -8.593  28.449  0.74 55.81           O  
ANISOU 2159  OE1AGLU A 229     7204   2722  11280    501  -4703  -1373       O  
ATOM   2160  OE1BGLU A 229      37.748  -6.490  31.735  0.26 29.82           O  
ANISOU 2160  OE1BGLU A 229     6090   1820   3420    596    552    930       O  
ATOM   2161  OE2AGLU A 229      37.477  -8.123  28.903  0.74 45.61           O  
ANISOU 2161  OE2AGLU A 229     4647   6703   5980   2676   -886  -1699       O  
ATOM   2162  OE2BGLU A 229      38.632  -7.980  30.370  0.26 38.54           O  
ANISOU 2162  OE2BGLU A 229     6747   2231   5667   2334  -1674   -620       O  
ATOM   2163  N   ASP A 230      36.697  -2.001  28.954  1.00 14.21           N  
ANISOU 2163  N   ASP A 230     1618   1182   2601     13   -385   -145       N  
ATOM   2164  CA  ASP A 230      37.574  -0.881  28.528  1.00 12.96           C  
ANISOU 2164  CA  ASP A 230     1377   1474   2073     84   -309    -37       C  
ATOM   2165  C   ASP A 230      38.283  -0.318  29.699  1.00 11.94           C  
ANISOU 2165  C   ASP A 230     1190   1246   2101    172   -165   -235       C  
ATOM   2166  O   ASP A 230      37.649   0.101  30.675  1.00 12.68           O  
ANISOU 2166  O   ASP A 230     1296   1522   2000    148   -221   -151       O  
ATOM   2167  CB  ASP A 230      36.626   0.163  27.852  1.00 12.66           C  
ANISOU 2167  CB  ASP A 230     1440   1330   2039     76   -344   -172       C  
ATOM   2168  CG  ASP A 230      37.378   1.316  27.238  1.00 13.10           C  
ANISOU 2168  CG  ASP A 230     1624   1366   1986    106   -346   -185       C  
ATOM   2169  OD1 ASP A 230      38.337   1.842  27.858  1.00 16.06           O  
ANISOU 2169  OD1 ASP A 230     1855   1594   2651   -201   -748     84       O  
ATOM   2170  OD2 ASP A 230      36.982   1.775  26.134  1.00 14.93           O  
ANISOU 2170  OD2 ASP A 230     1759   1770   2142   -160   -443    124       O  
ATOM   2171  N   PRO A 231      39.644  -0.300  29.731  1.00 12.84           N  
ANISOU 2171  N   PRO A 231     1242   1409   2226    121   -176   -239       N  
ATOM   2172  CA  PRO A 231      40.353   0.150  30.944  1.00 13.60           C  
ANISOU 2172  CA  PRO A 231     1272   1513   2382    149   -447    -82       C  
ATOM   2173  C   PRO A 231      40.091   1.589  31.281  1.00 11.99           C  
ANISOU 2173  C   PRO A 231     1145   1520   1891    -21   -243    -28       C  
ATOM   2174  O   PRO A 231      40.188   1.990  32.462  1.00 14.54           O  
ANISOU 2174  O   PRO A 231     1561   2009   1953     82   -426   -218       O  
ATOM   2175  CB  PRO A 231      41.865  -0.060  30.650  1.00 16.88           C  
ANISOU 2175  CB  PRO A 231     1324   2138   2952    410   -360   -366       C  
ATOM   2176  CG  PRO A 231      41.897  -0.100  29.181  1.00 18.18           C  
ANISOU 2176  CG  PRO A 231     1133   2902   2871    152   -140    -25       C  
ATOM   2177  CD  PRO A 231      40.583  -0.704  28.659  1.00 14.59           C  
ANISOU 2177  CD  PRO A 231     1327   1658   2558    215     32   -215       C  
ATOM   2178  N   ARG A 232      39.728   2.400  30.293  1.00 11.91           N  
ANISOU 2178  N   ARG A 232     1278   1364   1883     72   -156    -57       N  
ATOM   2179  CA  ARG A 232      39.428   3.814  30.604  1.00 12.25           C  
ANISOU 2179  CA  ARG A 232     1253   1466   1936     83    -47    -83       C  
ATOM   2180  C   ARG A 232      38.130   3.959  31.388  1.00 12.03           C  
ANISOU 2180  C   ARG A 232     1236   1541   1793     25    -85   -279       C  
ATOM   2181  O   ARG A 232      37.994   4.822  32.264  1.00 14.64           O  
ANISOU 2181  O   ARG A 232     1559   1890   2115   -121     79   -506       O  
ATOM   2182  CB  ARG A 232      39.337   4.614  29.282  1.00 12.64           C  
ANISOU 2182  CB  ARG A 232     1447   1396   1958    154     78    -33       C  
ATOM   2183  CG  ARG A 232      40.621   4.523  28.461  1.00 12.99           C  
ANISOU 2183  CG  ARG A 232     1378   1599   1960     57     81    -84       C  
ATOM   2184  CD  ARG A 232      40.455   5.071  27.052  1.00 13.63           C  
ANISOU 2184  CD  ARG A 232     1631   1581   1966    -29     66    -86       C  
ATOM   2185  NE  ARG A 232      39.431   4.259  26.344  1.00 14.26           N  
ANISOU 2185  NE  ARG A 232     1728   1757   1932    228    -64   -264       N  
ATOM   2186  CZ  ARG A 232      39.054   4.545  25.111  1.00 13.32           C  
ANISOU 2186  CZ  ARG A 232     1662   1474   1923    259     14   -137       C  
ATOM   2187  NH1 ARG A 232      39.632   5.558  24.415  1.00 14.76           N  
ANISOU 2187  NH1 ARG A 232     1829   1527   2254    232    528   -145       N  
ATOM   2188  NH2 ARG A 232      38.123   3.800  24.547  1.00 15.15           N  
ANISOU 2188  NH2 ARG A 232     1722   1763   2271    175   -190   -241       N  
ATOM   2189  N   ILE A 233      37.138   3.152  31.037  1.00 11.74           N  
ANISOU 2189  N   ILE A 233     1160   1587   1715     80   -111    -88       N  
ATOM   2190  CA  ILE A 233      35.846   3.176  31.767  1.00 11.97           C  
ANISOU 2190  CA  ILE A 233     1194   1653   1703     88    -88   -187       C  
ATOM   2191  C   ILE A 233      36.001   2.549  33.126  1.00 12.61           C  
ANISOU 2191  C   ILE A 233     1466   1646   1680    -21   -114   -186       C  
ATOM   2192  O   ILE A 233      35.449   3.008  34.117  1.00 14.27           O  
ANISOU 2192  O   ILE A 233     1569   2112   1742     31   -109   -384       O  
ATOM   2193  CB  ILE A 233      34.756   2.538  30.874  1.00 13.11           C  
ANISOU 2193  CB  ILE A 233     1170   1969   1843    252   -170   -127       C  
ATOM   2194  CG1 ILE A 233      34.692   3.255  29.528  1.00 12.98           C  
ANISOU 2194  CG1 ILE A 233     1493   1722   1718     -5   -191   -114       C  
ATOM   2195  CG2 ILE A 233      33.412   2.622  31.623  1.00 16.44           C  
ANISOU 2195  CG2 ILE A 233     1172   3038   2038   -133    -11   -208       C  
ATOM   2196  CD1 ILE A 233      33.678   2.736  28.531  1.00 16.07           C  
ANISOU 2196  CD1 ILE A 233     1483   2585   2038    -13   -358   -229       C  
ATOM   2197  N   LYS A 234      36.817   1.448  33.220  1.00 13.41           N  
ANISOU 2197  N   LYS A 234     1665   1707   1724     68    -81     24       N  
ATOM   2198  CA  LYS A 234      37.139   0.847  34.514  1.00 15.02           C  
ANISOU 2198  CA  LYS A 234     2084   1719   1902    106   -296     76       C  
ATOM   2199  C   LYS A 234      37.743   1.900  35.446  1.00 14.55           C  
ANISOU 2199  C   LYS A 234     1825   1909   1795    119   -338    159       C  
ATOM   2200  O   LYS A 234      37.450   1.909  36.656  1.00 17.51           O  
ANISOU 2200  O   LYS A 234     2235   2649   1769     76   -199     96       O  
ATOM   2201  CB  LYS A 234      38.127  -0.301  34.323  1.00 18.50           C  
ANISOU 2201  CB  LYS A 234     2862   1779   2387    420   -526    139       C  
ATOM   2202  CG ALYS A 234      37.519  -1.563  33.682  0.50 16.56           C  
ANISOU 2202  CG ALYS A 234     3002   1631   1659    242    170    249       C  
ATOM   2203  CD ALYS A 234      38.622  -2.627  33.599  0.50 25.17           C  
ANISOU 2203  CD ALYS A 234     4213   1852   3500    938    610    349       C  
ATOM   2204  CE ALYS A 234      38.104  -4.040  33.400  0.50 34.56           C  
ANISOU 2204  CE ALYS A 234     5571   1749   5810    888   -327    410       C  
ATOM   2205  NZ ALYS A 234      39.277  -4.970  33.269  0.50 35.82           N  
ANISOU 2205  NZ ALYS A 234     6503   2093   5016   1855  -2600   -182       N  
ATOM   2206  N   ALA A 235      38.594   2.792  34.915  1.00 14.50           N  
ANISOU 2206  N   ALA A 235     1541   1981   1988     36   -309    -49       N  
ATOM   2207  CA  ALA A 235      39.228   3.780  35.810  1.00 16.69           C  
ANISOU 2207  CA  ALA A 235     1536   2512   2294    -69   -229   -382       C  
ATOM   2208  C   ALA A 235      38.227   4.807  36.347  1.00 14.46           C  
ANISOU 2208  C   ALA A 235     1625   1923   1948   -213   -488   -166       C  
ATOM   2209  O   ALA A 235      38.322   5.218  37.501  1.00 17.67           O  
ANISOU 2209  O   ALA A 235     1889   2806   2019    -70   -523   -533       O  
ATOM   2210  CB  ALA A 235      40.337   4.487  35.035  1.00 20.25           C  
ANISOU 2210  CB  ALA A 235     1795   3335   2565   -712   -105   -465       C  
ATOM   2211  N   ILE A 236      37.216   5.192  35.532  1.00 14.19           N  
ANISOU 2211  N   ILE A 236     1636   1905   1850   -180   -364   -168       N  
ATOM   2212  CA  ILE A 236      36.176   6.105  36.007  1.00 14.45           C  
ANISOU 2212  CA  ILE A 236     1545   2210   1733   -140   -258     -6       C  
ATOM   2213  C   ILE A 236      35.337   5.405  37.070  1.00 13.28           C  
ANISOU 2213  C   ILE A 236     1623   1875   1547   -156   -412    -88       C  
ATOM   2214  O   ILE A 236      35.000   6.018  38.105  1.00 15.69           O  
ANISOU 2214  O   ILE A 236     2104   2167   1691   -272   -234   -249       O  
ATOM   2215  CB  ILE A 236      35.334   6.613  34.837  1.00 14.28           C  
ANISOU 2215  CB  ILE A 236     1814   1898   1715    -10   -211     24       C  
ATOM   2216  CG1 ILE A 236      36.198   7.525  33.928  1.00 17.47           C  
ANISOU 2216  CG1 ILE A 236     2091   2551   1994    -32     61    345       C  
ATOM   2217  CG2 ILE A 236      34.070   7.335  35.304  1.00 14.96           C  
ANISOU 2217  CG2 ILE A 236     1881   1971   1831    160   -138   -252       C  
ATOM   2218  CD1 ILE A 236      35.422   7.887  32.636  1.00 21.86           C  
ANISOU 2218  CD1 ILE A 236     3228   2823   2255   -142   -343    666       C  
ATOM   2219  N   ALA A 237      34.999   4.150  36.838  1.00 12.92           N  
ANISOU 2219  N   ALA A 237     1502   1970   1439   -124   -258   -119       N  
ATOM   2220  CA  ALA A 237      34.254   3.367  37.829  1.00 14.33           C  
ANISOU 2220  CA  ALA A 237     1770   2155   1518   -391   -403    -47       C  
ATOM   2221  C   ALA A 237      35.014   3.324  39.173  1.00 15.00           C  
ANISOU 2221  C   ALA A 237     1954   2205   1539   -202   -538    -30       C  
ATOM   2222  O   ALA A 237      34.432   3.491  40.263  1.00 16.71           O  
ANISOU 2222  O   ALA A 237     2230   2499   1620   -566   -373   -241       O  
ATOM   2223  CB  ALA A 237      33.969   1.990  37.285  1.00 15.16           C  
ANISOU 2223  CB  ALA A 237     2033   2191   1537   -513   -238    -68       C  
ATOM   2224  N   ALA A 238      36.308   3.037  39.099  1.00 16.30           N  
ANISOU 2224  N   ALA A 238     1882   2463   1849   -165   -568    226       N  
ATOM   2225  CA  ALA A 238      37.102   2.842  40.354  1.00 17.64           C  
ANISOU 2225  CA  ALA A 238     2122   2983   1597   -191   -610    213       C  
ATOM   2226  C   ALA A 238      37.120   4.143  41.159  1.00 18.82           C  
ANISOU 2226  C   ALA A 238     2100   3269   1782     15   -818     -4       C  
ATOM   2227  O   ALA A 238      37.022   4.133  42.380  1.00 22.18           O  
ANISOU 2227  O   ALA A 238     2600   4185   1641    142   -761   -171       O  
ATOM   2228  CB  ALA A 238      38.495   2.349  39.981  1.00 20.98           C  
ANISOU 2228  CB  ALA A 238     2387   3453   2132    543   -702    317       C  
ATOM   2229  N   LYS A 239      37.212   5.290  40.460  1.00 19.84           N  
ANISOU 2229  N   LYS A 239     2445   2993   2102   -210  -1010   -201       N  
ATOM   2230  CA  LYS A 239      37.256   6.617  41.134  1.00 21.05           C  
ANISOU 2230  CA  LYS A 239     2386   3300   2312   -804   -503   -528       C  
ATOM   2231  C   LYS A 239      35.973   6.842  41.930  1.00 20.69           C  
ANISOU 2231  C   LYS A 239     2498   3293   2070   -879   -656   -716       C  
ATOM   2232  O   LYS A 239      35.987   7.452  42.961  1.00 23.67           O  
ANISOU 2232  O   LYS A 239     2698   3700   2594   -765   -417  -1160       O  
ATOM   2233  CB  LYS A 239      37.513   7.702  40.093  1.00 27.44           C  
ANISOU 2233  CB  LYS A 239     4001   3415   3009  -1847   -151   -421       C  
ATOM   2234  CG  LYS A 239      37.403   9.158  40.509  1.00 35.65           C  
ANISOU 2234  CG  LYS A 239     5731   3362   4454   -477    611     30       C  
ATOM   2235  CD  LYS A 239      37.715  10.014  39.298  1.00 44.01           C  
ANISOU 2235  CD  LYS A 239     6102   4395   6226    858    196   2187       C  
ATOM   2236  CE  LYS A 239      36.491  10.415  38.476  1.00 40.28           C  
ANISOU 2236  CE  LYS A 239     4412   5202   5690    721   1216   1263       C  
ATOM   2237  NZ ALYS A 239      37.049  11.323  37.439  0.67 38.60           N  
ANISOU 2237  NZ ALYS A 239     4902   6570   3192  -1408  -1252    888       N  
ATOM   2238  NZ BLYS A 239      36.366   9.769  37.146  0.33 30.31           N  
ANISOU 2238  NZ BLYS A 239     2786   2388   6342    924   1359   1198       N  
ATOM   2239  N   HIS A 240      34.841   6.311  41.407  1.00 18.05           N  
ANISOU 2239  N   HIS A 240     2097   2697   2063   -417   -614   -328       N  
ATOM   2240  CA  HIS A 240      33.561   6.482  42.076  1.00 17.76           C  
ANISOU 2240  CA  HIS A 240     2324   2728   1695   -161   -560   -151       C  
ATOM   2241  C   HIS A 240      33.181   5.295  42.983  1.00 17.85           C  
ANISOU 2241  C   HIS A 240     2398   2857   1527   -325   -661   -171       C  
ATOM   2242  O   HIS A 240      32.097   5.257  43.603  1.00 21.24           O  
ANISOU 2242  O   HIS A 240     2899   3268   1903   -392    -66   -413       O  
ATOM   2243  CB  HIS A 240      32.436   6.716  41.038  1.00 18.26           C  
ANISOU 2243  CB  HIS A 240     2134   2743   2060   -386   -656    104       C  
ATOM   2244  CG  HIS A 240      32.555   8.011  40.287  1.00 17.69           C  
ANISOU 2244  CG  HIS A 240     2295   2429   1997   -376   -632    -84       C  
ATOM   2245  ND1 HIS A 240      32.071   9.172  40.904  1.00 19.27           N  
ANISOU 2245  ND1 HIS A 240     2412   2790   2121    -97   -338   -136       N  
ATOM   2246  CD2 HIS A 240      33.088   8.383  39.123  1.00 17.47           C  
ANISOU 2246  CD2 HIS A 240     2440   2280   1919   -145   -566   -179       C  
ATOM   2247  CE1 HIS A 240      32.311  10.195  40.061  1.00 19.39           C  
ANISOU 2247  CE1 HIS A 240     2508   2592   2269     54   -330   -193       C  
ATOM   2248  NE2 HIS A 240      32.920   9.744  38.979  1.00 17.10           N  
ANISOU 2248  NE2 HIS A 240     2252   2254   1991   -160   -512   -128       N  
ATOM   2249  N  AASN A 241      34.027   4.251  43.049  0.54 19.83           N  
ANISOU 2249  N  AASN A 241     2472   3023   2041   -271   -791    296       N  
ATOM   2250  N  BASN A 241      34.036   4.269  43.127  0.46 18.26           N  
ANISOU 2250  N  BASN A 241     2569   2839   1531   -338  -1083    -87       N  
ATOM   2251  CA AASN A 241      33.793   3.013  43.834  0.54 19.47           C  
ANISOU 2251  CA AASN A 241     2993   2927   1478   -417  -1019      1       C  
ATOM   2252  CA BASN A 241      33.683   3.059  43.894  0.46 19.24           C  
ANISOU 2252  CA BASN A 241     2776   3029   1506   -388   -978     19       C  
ATOM   2253  C  AASN A 241      32.530   2.259  43.390  0.54 18.11           C  
ANISOU 2253  C  AASN A 241     2298   3065   1517   -191   -684    402       C  
ATOM   2254  C  BASN A 241      32.369   2.428  43.400  0.46 16.86           C  
ANISOU 2254  C  BASN A 241     2206   2773   1427    -21   -625    160       C  
ATOM   2255  O  AASN A 241      31.792   1.669  44.216  0.54 23.07           O  
ANISOU 2255  O  AASN A 241     2827   4087   1853   -357   -538    981       O  
ATOM   2256  O  BASN A 241      31.462   2.095  44.196  0.46 17.04           O  
ANISOU 2256  O  BASN A 241     2513   2673   1289    161   -491    298       O  
ATOM   2257  CB AASN A 241      33.784   3.356  45.336  0.54 27.20           C  
ANISOU 2257  CB AASN A 241     4566   4352   1417    -48  -1360     21       C  
ATOM   2258  CB BASN A 241      33.578   3.341  45.396  0.46 24.08           C  
ANISOU 2258  CB BASN A 241     3728   3947   1474   -549   -982     34       C  
ATOM   2259  CG AASN A 241      35.220   3.670  45.751  0.54 30.17           C  
ANISOU 2259  CG AASN A 241     5204   4460   1801   -900  -1873   -231       C  
ATOM   2260  CG BASN A 241      33.804   2.057  46.171  0.46 28.77           C  
ANISOU 2260  CG BASN A 241     4484   4658   1787   -546  -1392    667       C  
ATOM   2261  OD1AASN A 241      35.615   4.810  45.930  0.54 42.21           O  
ANISOU 2261  OD1AASN A 241     8274   4876   2890  -2084  -2738    159       O  
ATOM   2262  OD1BASN A 241      34.432   1.115  45.672  0.46 39.71           O  
ANISOU 2262  OD1BASN A 241     6336   5678   3072   1661   -502   1987       O  
ATOM   2263  ND2AASN A 241      35.977   2.589  45.846  0.54 33.26           N  
ANISOU 2263  ND2AASN A 241     4294   5508   2836   -522  -1818    302       N  
ATOM   2264  ND2BASN A 241      33.319   2.045  47.408  0.46 37.08           N  
ANISOU 2264  ND2BASN A 241     6862   5587   1641  -1025  -1126    660       N  
ATOM   2265  N   LYS A 242      32.264   2.280  42.084  1.00 15.33           N  
ANISOU 2265  N   LYS A 242     1912   2477   1436   -257   -464    -26       N  
ATOM   2266  CA  LYS A 242      31.121   1.673  41.429  1.00 14.01           C  
ANISOU 2266  CA  LYS A 242     1845   1991   1488   -162   -470    136       C  
ATOM   2267  C   LYS A 242      31.658   0.680  40.410  1.00 13.89           C  
ANISOU 2267  C   LYS A 242     1659   2122   1498   -215   -409    193       C  
ATOM   2268  O   LYS A 242      32.851   0.643  40.085  1.00 16.86           O  
ANISOU 2268  O   LYS A 242     1628   2808   1970   -397   -296   -122       O  
ATOM   2269  CB  LYS A 242      30.272   2.734  40.732  1.00 14.52           C  
ANISOU 2269  CB  LYS A 242     2144   1888   1484   -229   -429    180       C  
ATOM   2270  CG  LYS A 242      29.503   3.625  41.704  1.00 17.14           C  
ANISOU 2270  CG  LYS A 242     2232   2366   1915    185   -234    153       C  
ATOM   2271  CD  LYS A 242      28.301   2.854  42.313  0.70 20.40           C  
ANISOU 2271  CD  LYS A 242     3179   2200   2372    442    551    871       C  
ATOM   2272  CE  LYS A 242      27.367   3.602  43.195  0.70 19.76           C  
ANISOU 2272  CE  LYS A 242     2365   2589   2551   -161    118     -3       C  
ATOM   2273  NZ  LYS A 242      26.167   2.838  43.714  0.70 18.06           N  
ANISOU 2273  NZ  LYS A 242     2556   2991   1314   -538   -378    237       N  
ATOM   2274  N   THR A 243      30.767  -0.200  39.893  1.00 13.71           N  
ANISOU 2274  N   THR A 243     1838   1892   1477   -257   -519    291       N  
ATOM   2275  CA  THR A 243      31.205  -1.085  38.830  1.00 14.35           C  
ANISOU 2275  CA  THR A 243     1936   1758   1756    -63   -661    251       C  
ATOM   2276  C   THR A 243      31.146  -0.389  37.466  1.00 12.41           C  
ANISOU 2276  C   THR A 243     1550   1610   1557    -28   -493     95       C  
ATOM   2277  O   THR A 243      30.501   0.646  37.288  1.00 11.99           O  
ANISOU 2277  O   THR A 243     1643   1408   1507     -5   -360     55       O  
ATOM   2278  CB  THR A 243      30.332  -2.356  38.767  1.00 15.17           C  
ANISOU 2278  CB  THR A 243     1941   1747   2077   -153   -778    538       C  
ATOM   2279  OG1 THR A 243      29.011  -1.991  38.308  1.00 14.31           O  
ANISOU 2279  OG1 THR A 243     1810   1807   1820   -132   -526    327       O  
ATOM   2280  CG2 THR A 243      30.230  -3.096  40.118  1.00 20.00           C  
ANISOU 2280  CG2 THR A 243     2774   2600   2223   -493  -1084    943       C  
ATOM   2281  N   THR A 244      31.838  -1.016  36.479  1.00 13.68           N  
ANISOU 2281  N   THR A 244     1722   1628   1846    174   -514    -48       N  
ATOM   2282  CA  THR A 244      31.758  -0.453  35.137  1.00 12.44           C  
ANISOU 2282  CA  THR A 244     1463   1563   1701     68   -228   -163       C  
ATOM   2283  C   THR A 244      30.326  -0.423  34.606  1.00 10.94           C  
ANISOU 2283  C   THR A 244     1376   1206   1575     55    -91     21       C  
ATOM   2284  O   THR A 244      29.917   0.559  33.969  1.00 11.31           O  
ANISOU 2284  O   THR A 244     1476   1247   1573     52    -35     76       O  
ATOM   2285  CB  THR A 244      32.700  -1.203  34.180  1.00 14.90           C  
ANISOU 2285  CB  THR A 244     1325   1884   2451     87   -102   -586       C  
ATOM   2286  OG1ATHR A 244      32.354  -2.528  33.960  0.23 10.10           O  
ANISOU 2286  OG1ATHR A 244      829   1539   1467    234   -226      9       O  
ATOM   2287  OG1BTHR A 244      34.039  -1.070  34.733  0.77 30.64           O  
ANISOU 2287  OG1BTHR A 244     1571   5205   4864   1013   -823  -2377       O  
ATOM   2288  CG2ATHR A 244      34.113  -1.253  34.785  0.23 20.31           C  
ANISOU 2288  CG2ATHR A 244     1517   2839   3362    269   -566  -2114       C  
ATOM   2289  CG2BTHR A 244      32.813  -0.653  32.814  0.77 21.16           C  
ANISOU 2289  CG2BTHR A 244     2803   2415   2823    147   1075   -169       C  
ATOM   2290  N   ALA A 245      29.545  -1.486  34.875  1.00 11.00           N  
ANISOU 2290  N   ALA A 245     1535   1255   1392    -43   -213     26       N  
ATOM   2291  CA  ALA A 245      28.121  -1.447  34.426  1.00 10.93           C  
ANISOU 2291  CA  ALA A 245     1523   1273   1359   -102   -242    -23       C  
ATOM   2292  C   ALA A 245      27.384  -0.285  35.041  1.00  9.77           C  
ANISOU 2292  C   ALA A 245     1448   1169   1095   -116   -234    191       C  
ATOM   2293  O   ALA A 245      26.552   0.356  34.377  1.00 10.22           O  
ANISOU 2293  O   ALA A 245     1465   1288   1130   -102   -268    186       O  
ATOM   2294  CB  ALA A 245      27.481  -2.795  34.778  1.00 12.10           C  
ANISOU 2294  CB  ALA A 245     1797   1250   1549   -203   -188    -52       C  
ATOM   2295  N   GLN A 246      27.606   0.002  36.340  1.00 10.48           N  
ANISOU 2295  N   GLN A 246     1564   1255   1164    -23   -315     62       N  
ATOM   2296  CA  GLN A 246      26.903   1.110  36.962  1.00  9.99           C  
ANISOU 2296  CA  GLN A 246     1444   1332   1020   -127   -253     75       C  
ATOM   2297  C   GLN A 246      27.263   2.445  36.331  1.00  9.67           C  
ANISOU 2297  C   GLN A 246     1394   1317    964    -33   -167     51       C  
ATOM   2298  O   GLN A 246      26.377   3.312  36.147  1.00 10.30           O  
ANISOU 2298  O   GLN A 246     1272   1405   1234      5    -45    136       O  
ATOM   2299  CB  GLN A 246      27.205   1.130  38.477  1.00 10.70           C  
ANISOU 2299  CB  GLN A 246     1480   1543   1043   -131   -255    190       C  
ATOM   2300  CG  GLN A 246      26.459  -0.046  39.177  1.00 12.28           C  
ANISOU 2300  CG  GLN A 246     1734   1794   1138   -263   -318    376       C  
ATOM   2301  CD  GLN A 246      26.933  -0.230  40.599  1.00 11.95           C  
ANISOU 2301  CD  GLN A 246     1711   1705   1126   -136   -265    197       C  
ATOM   2302  OE1 GLN A 246      28.098  -0.015  40.970  1.00 14.38           O  
ANISOU 2302  OE1 GLN A 246     1765   2385   1314   -395   -467    317       O  
ATOM   2303  NE2 GLN A 246      25.994  -0.674  41.431  1.00 13.21           N  
ANISOU 2303  NE2 GLN A 246     1787   2105   1126   -179   -121    154       N  
ATOM   2304  N   VAL A 247      28.543   2.661  35.949  1.00  9.89           N  
ANISOU 2304  N   VAL A 247     1334   1243   1180   -112   -210     50       N  
ATOM   2305  CA  VAL A 247      28.899   3.890  35.219  1.00  9.98           C  
ANISOU 2305  CA  VAL A 247     1365   1200   1226   -143   -208     74       C  
ATOM   2306  C   VAL A 247      28.195   3.916  33.858  1.00  8.92           C  
ANISOU 2306  C   VAL A 247     1164   1096   1129   -111    -23      2       C  
ATOM   2307  O   VAL A 247      27.739   5.001  33.441  1.00 10.00           O  
ANISOU 2307  O   VAL A 247     1343   1082   1376    -48   -117     35       O  
ATOM   2308  CB  VAL A 247      30.418   3.975  35.066  1.00 11.48           C  
ANISOU 2308  CB  VAL A 247     1317   1533   1512   -294   -307    148       C  
ATOM   2309  CG1 VAL A 247      30.858   5.028  34.053  1.00 12.75           C  
ANISOU 2309  CG1 VAL A 247     1518   1609   1717   -239      5    102       C  
ATOM   2310  CG2 VAL A 247      31.084   4.240  36.441  1.00 16.35           C  
ANISOU 2310  CG2 VAL A 247     2007   2441   1762   -697   -723    251       C  
ATOM   2311  N   LEU A 248      28.156   2.794  33.145  1.00  9.09           N  
ANISOU 2311  N   LEU A 248     1267   1079   1109   -102   -144    -15       N  
ATOM   2312  CA  LEU A 248      27.536   2.763  31.824  1.00  8.75           C  
ANISOU 2312  CA  LEU A 248     1236   1049   1040     38    -11    -10       C  
ATOM   2313  C   LEU A 248      26.022   3.023  31.892  1.00  8.17           C  
ANISOU 2313  C   LEU A 248     1254    930    919     -4    -50    -10       C  
ATOM   2314  O   LEU A 248      25.451   3.490  30.904  1.00  9.86           O  
ANISOU 2314  O   LEU A 248     1403   1404    941    276     87    150       O  
ATOM   2315  CB  LEU A 248      27.827   1.416  31.141  1.00  9.72           C  
ANISOU 2315  CB  LEU A 248     1284   1137   1273     16     88   -143       C  
ATOM   2316  CG  LEU A 248      29.297   1.224  30.751  1.00 10.24           C  
ANISOU 2316  CG  LEU A 248     1196   1369   1327    140    121     31       C  
ATOM   2317  CD1 LEU A 248      29.576  -0.238  30.353  1.00 13.66           C  
ANISOU 2317  CD1 LEU A 248     1577   1594   2018    221    579   -195       C  
ATOM   2318  CD2 LEU A 248      29.651   2.134  29.593  1.00 14.89           C  
ANISOU 2318  CD2 LEU A 248     1642   2129   1885    233    502    567       C  
ATOM   2319  N   ILE A 249      25.376   2.711  33.009  1.00  8.56           N  
ANISOU 2319  N   ILE A 249     1164   1145    942    -54    -24     -2       N  
ATOM   2320  CA  ILE A 249      23.944   2.981  33.179  1.00  8.31           C  
ANISOU 2320  CA  ILE A 249     1150   1124    884    -80      2     57       C  
ATOM   2321  C   ILE A 249      23.718   4.423  33.601  1.00  8.36           C  
ANISOU 2321  C   ILE A 249     1195   1141    840    -32    -30     66       C  
ATOM   2322  O   ILE A 249      22.796   5.092  33.129  1.00  9.72           O  
ANISOU 2322  O   ILE A 249     1289   1291   1112     70    -22     19       O  
ATOM   2323  CB  ILE A 249      23.350   1.935  34.164  1.00  9.19           C  
ANISOU 2323  CB  ILE A 249     1279   1223    991    -99     10     89       C  
ATOM   2324  CG1 ILE A 249      23.378   0.552  33.529  1.00 10.50           C  
ANISOU 2324  CG1 ILE A 249     1527   1067   1396   -162   -183     80       C  
ATOM   2325  CG2 ILE A 249      21.941   2.356  34.622  1.00 10.80           C  
ANISOU 2325  CG2 ILE A 249     1182   1591   1330    -36    163    221       C  
ATOM   2326  CD1 ILE A 249      23.211  -0.582  34.550  1.00 12.11           C  
ANISOU 2326  CD1 ILE A 249     1670   1416   1516   -299   -212    390       C  
ATOM   2327  N   ARG A 250      24.573   4.959  34.492  1.00  8.73           N  
ANISOU 2327  N   ARG A 250     1253   1009   1055   -167    -28    -30       N  
ATOM   2328  CA  ARG A 250      24.409   6.324  34.939  1.00  9.48           C  
ANISOU 2328  CA  ARG A 250     1463   1199    938    -54    -58    -64       C  
ATOM   2329  C   ARG A 250      24.684   7.341  33.806  1.00  8.97           C  
ANISOU 2329  C   ARG A 250     1475    963    971    -42    -38    -63       C  
ATOM   2330  O   ARG A 250      24.059   8.410  33.777  1.00 10.08           O  
ANISOU 2330  O   ARG A 250     1466   1213   1152    123    -26    -57       O  
ATOM   2331  CB  ARG A 250      25.412   6.570  36.118  1.00  9.98           C  
ANISOU 2331  CB  ARG A 250     1491   1260   1039   -121   -225   -160       C  
ATOM   2332  CG  ARG A 250      25.314   7.970  36.745  1.00 11.09           C  
ANISOU 2332  CG  ARG A 250     1787   1242   1185   -204    -26   -200       C  
ATOM   2333  CD  ARG A 250      24.059   8.169  37.546  1.00 13.01           C  
ANISOU 2333  CD  ARG A 250     2399   1226   1319   -189    380   -236       C  
ATOM   2334  NE  ARG A 250      23.898   9.579  37.881  1.00 12.39           N  
ANISOU 2334  NE  ARG A 250     2016   1331   1359   -109    -21   -287       N  
ATOM   2335  CZ  ARG A 250      23.023  10.050  38.773  1.00 15.42           C  
ANISOU 2335  CZ  ARG A 250     2277   1310   2273   -124    612   -296       C  
ATOM   2336  NH1 ARG A 250      22.237   9.242  39.488  1.00 16.63           N  
ANISOU 2336  NH1 ARG A 250     2164   1555   2599    -77    752     14       N  
ATOM   2337  NH2 ARG A 250      22.970  11.361  38.957  1.00 17.17           N  
ANISOU 2337  NH2 ARG A 250     2904   1257   2361    158    630    -34       N  
ATOM   2338  N   PHE A 251      25.592   7.019  32.896  1.00  8.89           N  
ANISOU 2338  N   PHE A 251     1261   1110   1007   -145    -31    -66       N  
ATOM   2339  CA  PHE A 251      25.972   7.916  31.789  1.00  8.71           C  
ANISOU 2339  CA  PHE A 251     1230    969   1109    -96     14     13       C  
ATOM   2340  C   PHE A 251      24.757   8.421  30.999  1.00  8.21           C  
ANISOU 2340  C   PHE A 251     1237    794   1088   -159     29    -54       C  
ATOM   2341  O   PHE A 251      24.530   9.641  30.910  1.00  8.96           O  
ANISOU 2341  O   PHE A 251     1339    827   1239   -135    -82    -64       O  
ATOM   2342  CB  PHE A 251      27.050   7.185  30.966  1.00  9.76           C  
ANISOU 2342  CB  PHE A 251     1328   1178   1204     -4    161    -23       C  
ATOM   2343  CG  PHE A 251      27.439   7.871  29.658  1.00  9.20           C  
ANISOU 2343  CG  PHE A 251     1059   1070   1365    -36    104     62       C  
ATOM   2344  CD1 PHE A 251      27.857   9.178  29.610  1.00 11.38           C  
ANISOU 2344  CD1 PHE A 251     1404   1215   1706   -233    196     93       C  
ATOM   2345  CD2 PHE A 251      27.420   7.132  28.476  1.00 10.84           C  
ANISOU 2345  CD2 PHE A 251     1361   1563   1195    -75    249   -108       C  
ATOM   2346  CE1 PHE A 251      28.297   9.735  28.427  1.00 12.91           C  
ANISOU 2346  CE1 PHE A 251     1660   1329   1916   -162    370    333       C  
ATOM   2347  CE2 PHE A 251      27.846   7.687  27.302  1.00 13.59           C  
ANISOU 2347  CE2 PHE A 251     2005   1691   1467    -56    444     87       C  
ATOM   2348  CZ  PHE A 251      28.296   9.018  27.280  1.00 14.04           C  
ANISOU 2348  CZ  PHE A 251     1881   1664   1792     52    539    281       C  
ATOM   2349  N   PRO A 252      23.905   7.541  30.422  1.00  8.06           N  
ANISOU 2349  N   PRO A 252     1270    834    959    -40    -22    -71       N  
ATOM   2350  CA  PRO A 252      22.735   8.047  29.703  1.00  8.23           C  
ANISOU 2350  CA  PRO A 252     1301    840    987    -80    -44   -111       C  
ATOM   2351  C   PRO A 252      21.767   8.770  30.608  1.00  7.84           C  
ANISOU 2351  C   PRO A 252     1231    712   1034   -144   -115   -144       C  
ATOM   2352  O   PRO A 252      21.097   9.721  30.157  1.00  8.92           O  
ANISOU 2352  O   PRO A 252     1305    862   1223    -61    -41   -140       O  
ATOM   2353  CB  PRO A 252      22.093   6.766  29.086  1.00  9.00           C  
ANISOU 2353  CB  PRO A 252     1551    821   1046   -169   -116   -114       C  
ATOM   2354  CG  PRO A 252      22.660   5.610  29.893  1.00  8.97           C  
ANISOU 2354  CG  PRO A 252     1400    917   1091   -150    -60    -73       C  
ATOM   2355  CD  PRO A 252      24.078   6.065  30.252  1.00  8.54           C  
ANISOU 2355  CD  PRO A 252     1385    674   1187   -133      4   -110       C  
ATOM   2356  N   MET A 253      21.619   8.340  31.878  1.00  8.29           N  
ANISOU 2356  N   MET A 253     1179    926   1044   -138     99   -129       N  
ATOM   2357  CA  MET A 253      20.678   9.042  32.748  1.00  9.11           C  
ANISOU 2357  CA  MET A 253     1434    891   1135   -152    195   -179       C  
ATOM   2358  C   MET A 253      21.020  10.521  32.850  1.00  8.98           C  
ANISOU 2358  C   MET A 253     1384    924   1103    -54    132   -152       C  
ATOM   2359  O   MET A 253      20.140  11.386  32.896  1.00 10.53           O  
ANISOU 2359  O   MET A 253     1416   1037   1549    -44    115   -179       O  
ATOM   2360  CB  MET A 253      20.727   8.425  34.183  1.00 10.64           C  
ANISOU 2360  CB  MET A 253     1725   1103   1216    -73    319    -50       C  
ATOM   2361  CG  MET A 253      20.204   6.993  34.189  1.00 11.51           C  
ANISOU 2361  CG  MET A 253     1666   1245   1464   -201    383     71       C  
ATOM   2362  SD  MET A 253      20.553   6.164  35.796  1.00 16.53           S  
ANISOU 2362  SD  MET A 253     2582   1903   1795   -203    462    422       S  
ATOM   2363  CE  MET A 253      19.541   7.073  36.931  1.00 25.47           C  
ANISOU 2363  CE  MET A 253     4830   3299   1549   1361    634    344       C  
ATOM   2364  N   GLN A 254      22.333  10.851  32.914  1.00  8.94           N  
ANISOU 2364  N   GLN A 254     1409    871   1117   -186    -36   -203       N  
ATOM   2365  CA  GLN A 254      22.728  12.278  33.038  1.00  9.90           C  
ANISOU 2365  CA  GLN A 254     1555   1000   1205   -222   -188   -228       C  
ATOM   2366  C   GLN A 254      22.648  13.049  31.745  1.00 10.46           C  
ANISOU 2366  C   GLN A 254     1775    971   1229   -249    -77   -135       C  
ATOM   2367  O   GLN A 254      22.820  14.276  31.760  1.00 15.21           O  
ANISOU 2367  O   GLN A 254     3199    959   1620   -454   -529   -229       O  
ATOM   2368  CB  GLN A 254      24.147  12.370  33.636  1.00 10.97           C  
ANISOU 2368  CB  GLN A 254     1633   1264   1270   -418   -200    -83       C  
ATOM   2369  CG  GLN A 254      24.107  11.986  35.124  1.00 12.27           C  
ANISOU 2369  CG  GLN A 254     1707   1756   1197   -469   -259     49       C  
ATOM   2370  CD  GLN A 254      25.402  12.217  35.868  1.00 10.80           C  
ANISOU 2370  CD  GLN A 254     1566   1266   1274   -226    -88   -117       C  
ATOM   2371  OE1 GLN A 254      25.734  11.456  36.779  1.00 12.75           O  
ANISOU 2371  OE1 GLN A 254     1868   1470   1506   -458   -320    129       O  
ATOM   2372  NE2 GLN A 254      26.175  13.260  35.546  1.00 12.62           N  
ANISOU 2372  NE2 GLN A 254     1848   1395   1551   -447    -24    -43       N  
ATOM   2373  N   ARG A 255      22.309  12.398  30.635  1.00  9.77           N  
ANISOU 2373  N   ARG A 255     1595    930   1186   -248    -57   -135       N  
ATOM   2374  CA  ARG A 255      21.997  13.036  29.357  1.00  9.64           C  
ANISOU 2374  CA  ARG A 255     1636    886   1142   -148     20    -93       C  
ATOM   2375  C   ARG A 255      20.485  13.182  29.190  1.00  9.66           C  
ANISOU 2375  C   ARG A 255     1584    775   1313   -190    -91    -75       C  
ATOM   2376  O   ARG A 255      20.018  13.523  28.083  1.00 11.64           O  
ANISOU 2376  O   ARG A 255     1851   1180   1392     50     34     74       O  
ATOM   2377  CB  ARG A 255      22.602  12.229  28.175  1.00 10.47           C  
ANISOU 2377  CB  ARG A 255     1450   1280   1247   -328     41   -271       C  
ATOM   2378  CG  ARG A 255      24.112  12.065  28.316  1.00 11.43           C  
ANISOU 2378  CG  ARG A 255     1474   1545   1324   -186    -17   -155       C  
ATOM   2379  CD  ARG A 255      24.689  11.183  27.197  1.00 11.65           C  
ANISOU 2379  CD  ARG A 255     1619   1556   1252    -65     84    -34       C  
ATOM   2380  NE  ARG A 255      24.620  11.855  25.901  1.00 11.05           N  
ANISOU 2380  NE  ARG A 255     1616   1275   1307   -209    267    -67       N  
ATOM   2381  CZ  ARG A 255      24.775  11.259  24.737  1.00 10.18           C  
ANISOU 2381  CZ  ARG A 255     1490   1146   1233   -150    146    -34       C  
ATOM   2382  NH1 ARG A 255      24.941   9.927  24.667  1.00 11.36           N  
ANISOU 2382  NH1 ARG A 255     1877   1194   1244   -177    157     17       N  
ATOM   2383  NH2 ARG A 255      24.782  11.973  23.604  1.00 13.12           N  
ANISOU 2383  NH2 ARG A 255     2349   1316   1320    -85    327    209       N  
ATOM   2384  N  AASN A 256      19.726  12.935  30.263  0.53  9.81           N  
ANISOU 2384  N  AASN A 256     1484    951   1292     66    -67    -81       N  
ATOM   2385  N  BASN A 256      19.710  12.931  30.255  0.47 10.36           N  
ANISOU 2385  N  BASN A 256     1624    997   1318   -393    -20   -163       N  
ATOM   2386  CA AASN A 256      18.253  12.983  30.197  0.53 10.31           C  
ANISOU 2386  CA AASN A 256     1561   1012   1343    158    -22   -169       C  
ATOM   2387  CA BASN A 256      18.232  13.020  30.252  0.47 11.35           C  
ANISOU 2387  CA BASN A 256     1691   1080   1542   -228     17   -215       C  
ATOM   2388  C  AASN A 256      17.706  11.954  29.238  0.53 10.03           C  
ANISOU 2388  C  AASN A 256     1619   1085   1107     22   -152    -14       C  
ATOM   2389  C  BASN A 256      17.609  11.919  29.410  0.47  9.19           C  
ANISOU 2389  C  BASN A 256     1241   1147   1102    -96    150   -159       C  
ATOM   2390  O  AASN A 256      16.752  12.265  28.495  0.53 12.70           O  
ANISOU 2390  O  AASN A 256     1661   1838   1325    483   -227   -334       O  
ATOM   2391  O  BASN A 256      16.488  12.101  28.878  0.47 10.51           O  
ANISOU 2391  O  BASN A 256     1501   1237   1257     89    -43   -252       O  
ATOM   2392  CB AASN A 256      17.662  14.351  29.833  0.53 12.76           C  
ANISOU 2392  CB AASN A 256     1769   1098   1983    369    149   -143       C  
ATOM   2393  CB BASN A 256      17.746  14.425  29.870  0.47 16.35           C  
ANISOU 2393  CB BASN A 256     2737   1155   2322    463     49   -597       C  
ATOM   2394  CG AASN A 256      18.157  15.338  30.868  0.53 17.16           C  
ANISOU 2394  CG AASN A 256     3038   1079   2401    442     69   -471       C  
ATOM   2395  CG BASN A 256      16.357  14.720  30.386  0.47 21.43           C  
ANISOU 2395  CG BASN A 256     2512   1464   4167    354    326    285       C  
ATOM   2396  OD1AASN A 256      17.977  15.101  32.058  0.53 22.30           O  
ANISOU 2396  OD1AASN A 256     4540   1639   2292    277    269   -893       O  
ATOM   2397  OD1BASN A 256      15.921  14.347  31.482  0.47 28.32           O  
ANISOU 2397  OD1BASN A 256     3478   3141   4141  -1190   1210   -866       O  
ATOM   2398  ND2AASN A 256      18.756  16.394  30.374  0.53 25.58           N  
ANISOU 2398  ND2AASN A 256     4625   1604   3491   -773    753   -900       N  
ATOM   2399  ND2BASN A 256      15.570  15.403  29.541  0.47 39.90           N  
ANISOU 2399  ND2BASN A 256     3250   3839   8073    913  -1157   1763       N  
ATOM   2400  N   LEU A 257      18.297  10.769  29.268  1.00  9.22           N  
ANISOU 2400  N   LEU A 257     1447    913   1145   -141    -63    -49       N  
ATOM   2401  CA  LEU A 257      17.786   9.610  28.547  1.00  8.87           C  
ANISOU 2401  CA  LEU A 257     1245    929   1195   -190    -37     -3       C  
ATOM   2402  C   LEU A 257      17.209   8.604  29.532  1.00  8.79           C  
ANISOU 2402  C   LEU A 257     1316    948   1077   -144   -135     53       C  
ATOM   2403  O   LEU A 257      17.571   8.523  30.718  1.00 13.43           O  
ANISOU 2403  O   LEU A 257     2333   1601   1168   -822   -517    243       O  
ATOM   2404  CB  LEU A 257      18.895   8.898  27.736  1.00  9.37           C  
ANISOU 2404  CB  LEU A 257     1349   1055   1157   -152    -58    -59       C  
ATOM   2405  CG  LEU A 257      19.800   9.848  26.932  1.00 10.38           C  
ANISOU 2405  CG  LEU A 257     1483   1317   1143   -101     38    128       C  
ATOM   2406  CD1 LEU A 257      20.923   9.036  26.212  1.00 12.38           C  
ANISOU 2406  CD1 LEU A 257     1683   1496   1525    155    233    285       C  
ATOM   2407  CD2 LEU A 257      19.073  10.725  25.959  1.00 12.77           C  
ANISOU 2407  CD2 LEU A 257     1999   1427   1426    167      4    310       C  
ATOM   2408  N   VAL A 258      16.288   7.791  29.022  1.00  7.57           N  
ANISOU 2408  N   VAL A 258     1211    709    955    -14    -39    -58       N  
ATOM   2409  CA  VAL A 258      15.840   6.550  29.686  1.00  7.44           C  
ANISOU 2409  CA  VAL A 258     1236    603    987     21    -39    -15       C  
ATOM   2410  C   VAL A 258      16.803   5.451  29.269  1.00  6.89           C  
ANISOU 2410  C   VAL A 258     1129    733    758    -36     38   -134       C  
ATOM   2411  O   VAL A 258      17.305   5.462  28.165  1.00  8.98           O  
ANISOU 2411  O   VAL A 258     1611   1017    783    209    118    -30       O  
ATOM   2412  CB  VAL A 258      14.384   6.285  29.232  1.00  8.19           C  
ANISOU 2412  CB  VAL A 258     1134    917   1063     -9    -43     -6       C  
ATOM   2413  CG1 VAL A 258      13.812   4.969  29.776  1.00  9.37           C  
ANISOU 2413  CG1 VAL A 258     1245    997   1316   -225     79      8       C  
ATOM   2414  CG2 VAL A 258      13.463   7.444  29.614  1.00 10.41           C  
ANISOU 2414  CG2 VAL A 258     1415   1171   1370    273    133     89       C  
ATOM   2415  N   VAL A 259      17.039   4.476  30.163  1.00  7.20           N  
ANISOU 2415  N   VAL A 259     1232    633    871     99     19    -70       N  
ATOM   2416  CA  VAL A 259      18.016   3.424  29.858  1.00  7.09           C  
ANISOU 2416  CA  VAL A 259     1169    607    920     -6     66    -24       C  
ATOM   2417  C   VAL A 259      17.439   2.066  30.326  1.00  6.40           C  
ANISOU 2417  C   VAL A 259     1000    701    730     52     14    -94       C  
ATOM   2418  O   VAL A 259      16.819   1.974  31.381  1.00  7.61           O  
ANISOU 2418  O   VAL A 259     1308    718    863    -60    155   -114       O  
ATOM   2419  CB  VAL A 259      19.383   3.744  30.465  1.00  8.60           C  
ANISOU 2419  CB  VAL A 259     1175    738   1354    -34    -53   -164       C  
ATOM   2420  CG1 VAL A 259      19.353   3.847  31.964  1.00 10.97           C  
ANISOU 2420  CG1 VAL A 259     1359   1592   1216   -199   -123    -92       C  
ATOM   2421  CG2 VAL A 259      20.454   2.743  29.973  1.00 10.66           C  
ANISOU 2421  CG2 VAL A 259     1111   1016   1925     26    118    -38       C  
ATOM   2422  N   ILE A 260      17.682   1.021  29.500  1.00  6.76           N  
ANISOU 2422  N   ILE A 260     1087    659    824     37    -16    -83       N  
ATOM   2423  CA  ILE A 260      17.036  -0.279  29.702  1.00  6.33           C  
ANISOU 2423  CA  ILE A 260     1013    617    774    -72    -66    -93       C  
ATOM   2424  C   ILE A 260      18.008  -1.448  29.636  1.00  6.57           C  
ANISOU 2424  C   ILE A 260     1159    690    646     46     -3    -96       C  
ATOM   2425  O   ILE A 260      17.914  -2.335  28.789  1.00  8.28           O  
ANISOU 2425  O   ILE A 260     1388    869    887    202   -174   -221       O  
ATOM   2426  CB  ILE A 260      15.844  -0.464  28.698  1.00  6.77           C  
ANISOU 2426  CB  ILE A 260     1003    827    744     72    -29    -15       C  
ATOM   2427  CG1 ILE A 260      16.255  -0.199  27.251  1.00  7.18           C  
ANISOU 2427  CG1 ILE A 260     1060    942    727    -88    -55    -35       C  
ATOM   2428  CG2 ILE A 260      14.671   0.424  29.152  1.00  8.48           C  
ANISOU 2428  CG2 ILE A 260     1058   1139   1026    194    -38   -133       C  
ATOM   2429  CD1 ILE A 260      15.166  -0.623  26.248  1.00  8.60           C  
ANISOU 2429  CD1 ILE A 260     1202   1248    816     20   -133   -152       C  
ATOM   2430  N   PRO A 261      18.947  -1.546  30.599  1.00  6.72           N  
ANISOU 2430  N   PRO A 261     1112    665    778     52    -63    -49       N  
ATOM   2431  CA  PRO A 261      19.891  -2.688  30.613  1.00  7.04           C  
ANISOU 2431  CA  PRO A 261     1009    706    959     72    -83     43       C  
ATOM   2432  C   PRO A 261      19.148  -3.993  30.802  1.00  6.49           C  
ANISOU 2432  C   PRO A 261     1042    711    714     18    -28     33       C  
ATOM   2433  O   PRO A 261      18.182  -4.098  31.593  1.00  7.58           O  
ANISOU 2433  O   PRO A 261     1190    773    915    -13     85    -56       O  
ATOM   2434  CB  PRO A 261      20.783  -2.377  31.820  1.00  8.41           C  
ANISOU 2434  CB  PRO A 261     1244    947   1006     29   -258    -78       C  
ATOM   2435  CG  PRO A 261      19.885  -1.553  32.754  1.00  9.58           C  
ANISOU 2435  CG  PRO A 261     1507   1064   1070    242   -371   -138       C  
ATOM   2436  CD  PRO A 261      19.067  -0.714  31.810  1.00  7.81           C  
ANISOU 2436  CD  PRO A 261     1244    923    801     68   -147   -147       C  
ATOM   2437  N   LYS A 262      19.633  -5.039  30.130  1.00  6.84           N  
ANISOU 2437  N   LYS A 262     1096    699    802     88     18     67       N  
ATOM   2438  CA  LYS A 262      19.084  -6.393  30.271  1.00  6.87           C  
ANISOU 2438  CA  LYS A 262     1200    609    801     49    -61     38       C  
ATOM   2439  C   LYS A 262      19.987  -7.218  31.196  1.00  6.98           C  
ANISOU 2439  C   LYS A 262     1145    740    765     71    -65    -28       C  
ATOM   2440  O   LYS A 262      21.202  -7.269  31.061  1.00  7.88           O  
ANISOU 2440  O   LYS A 262     1113    962    920    123    -59     75       O  
ATOM   2441  CB  LYS A 262      19.007  -7.057  28.889  1.00  7.65           C  
ANISOU 2441  CB  LYS A 262     1381    745    782     78   -132     -8       C  
ATOM   2442  CG  LYS A 262      18.633  -8.550  28.854  1.00  8.20           C  
ANISOU 2442  CG  LYS A 262     1354    689   1073     53    -77    -54       C  
ATOM   2443  CD  LYS A 262      19.853  -9.468  28.871  1.00  8.34           C  
ANISOU 2443  CD  LYS A 262     1358    759   1051    152     50    -48       C  
ATOM   2444  CE  LYS A 262      19.484 -10.949  28.849  1.00  9.26           C  
ANISOU 2444  CE  LYS A 262     1556    706   1256     90     27    -47       C  
ATOM   2445  NZ  LYS A 262      20.705 -11.803  28.925  1.00  9.75           N  
ANISOU 2445  NZ  LYS A 262     1602    844   1259    179     46      9       N  
ATOM   2446  N   SER A 263      19.316  -7.989  32.094  1.00  7.74           N  
ANISOU 2446  N   SER A 263     1362    739    840    139     91     84       N  
ATOM   2447  CA  SER A 263      20.001  -9.070  32.812  1.00  8.03           C  
ANISOU 2447  CA  SER A 263     1418    780    854    147    -94    189       C  
ATOM   2448  C   SER A 263      18.943 -10.104  33.208  1.00  8.17           C  
ANISOU 2448  C   SER A 263     1466    846    790     77    -60     43       C  
ATOM   2449  O   SER A 263      17.784  -9.756  33.491  1.00  9.26           O  
ANISOU 2449  O   SER A 263     1450    910   1159     82     53     90       O  
ATOM   2450  CB  SER A 263      20.718  -8.560  34.062  1.00  8.78           C  
ANISOU 2450  CB  SER A 263     1591    826    917     29   -138    111       C  
ATOM   2451  OG  SER A 263      21.421  -9.611  34.726  1.00  9.60           O  
ANISOU 2451  OG  SER A 263     1648   1014    987     51   -202    263       O  
ATOM   2452  N   VAL A 264      19.408 -11.361  33.266  1.00  9.06           N  
ANISOU 2452  N   VAL A 264     1751    717    975     71    -71    123       N  
ATOM   2453  CA  VAL A 264      18.617 -12.435  33.921  1.00 10.10           C  
ANISOU 2453  CA  VAL A 264     1872    853   1112   -165   -155    123       C  
ATOM   2454  C   VAL A 264      19.308 -12.887  35.220  1.00 10.57           C  
ANISOU 2454  C   VAL A 264     2073    934   1008    -38    -67    243       C  
ATOM   2455  O   VAL A 264      18.841 -13.859  35.837  1.00 14.58           O  
ANISOU 2455  O   VAL A 264     2665   1350   1525   -469   -164    532       O  
ATOM   2456  CB  VAL A 264      18.373 -13.644  33.022  1.00 12.65           C  
ANISOU 2456  CB  VAL A 264     2605    945   1257   -176   -245     25       C  
ATOM   2457  CG1 VAL A 264      17.369 -13.241  31.945  1.00 16.48           C  
ANISOU 2457  CG1 VAL A 264     3357   1412   1493   -642   -831    281       C  
ATOM   2458  CG2 VAL A 264      19.671 -14.259  32.496  1.00 16.46           C  
ANISOU 2458  CG2 VAL A 264     3273   1083   1897     70    438   -209       C  
ATOM   2459  N   THR A 265      20.355 -12.210  35.665  1.00 10.28           N  
ANISOU 2459  N   THR A 265     2025    925    954     77   -147    126       N  
ATOM   2460  CA  THR A 265      21.132 -12.641  36.837  1.00 10.33           C  
ANISOU 2460  CA  THR A 265     1973    969    984    152    -80    186       C  
ATOM   2461  C   THR A 265      20.663 -11.811  38.027  1.00  9.82           C  
ANISOU 2461  C   THR A 265     1822    949    961     30   -102    177       C  
ATOM   2462  O   THR A 265      20.851 -10.595  38.021  1.00 10.38           O  
ANISOU 2462  O   THR A 265     1931    910   1101    155    -53    168       O  
ATOM   2463  CB  THR A 265      22.623 -12.379  36.596  1.00 10.89           C  
ANISOU 2463  CB  THR A 265     1931   1192   1016    289    -98    128       C  
ATOM   2464  OG1 THR A 265      23.028 -13.087  35.399  1.00 12.49           O  
ANISOU 2464  OG1 THR A 265     2323   1221   1202    539    169    167       O  
ATOM   2465  CG2 THR A 265      23.489 -12.836  37.757  1.00 13.45           C  
ANISOU 2465  CG2 THR A 265     2186   1642   1281    431   -281    356       C  
ATOM   2466  N   PRO A 266      20.075 -12.420  39.070  1.00 11.32           N  
ANISOU 2466  N   PRO A 266     2184    995   1123     79     40    193       N  
ATOM   2467  CA  PRO A 266      19.558 -11.595  40.173  1.00 11.85           C  
ANISOU 2467  CA  PRO A 266     2179   1343    981     13     60    207       C  
ATOM   2468  C   PRO A 266      20.509 -10.596  40.769  1.00 11.27           C  
ANISOU 2468  C   PRO A 266     2209   1248    826    217    -58    223       C  
ATOM   2469  O   PRO A 266      20.089  -9.466  41.054  1.00 11.99           O  
ANISOU 2469  O   PRO A 266     2249   1227   1082    211    -29    142       O  
ATOM   2470  CB  PRO A 266      19.119 -12.695  41.207  1.00 15.48           C  
ANISOU 2470  CB  PRO A 266     2979   1489   1413   -163    421    381       C  
ATOM   2471  CG  PRO A 266      18.710 -13.837  40.349  1.00 19.53           C  
ANISOU 2471  CG  PRO A 266     4142   1484   1794   -509   1101     70       C  
ATOM   2472  CD  PRO A 266      19.706 -13.855  39.188  1.00 14.97           C  
ANISOU 2472  CD  PRO A 266     2916   1152   1621   -261    501    318       C  
ATOM   2473  N  AGLU A 267      21.771 -11.009  41.002  0.56 12.30           N  
ANISOU 2473  N  AGLU A 267     2303   1380    991    309   -284    124       N  
ATOM   2474  N  BGLU A 267      21.773 -10.940  41.012  0.44 11.82           N  
ANISOU 2474  N  BGLU A 267     2201   1208   1083    172   -230    363       N  
ATOM   2475  CA AGLU A 267      22.729 -10.057  41.608  0.56 13.91           C  
ANISOU 2475  CA AGLU A 267     2467   1617   1203    155   -534    309       C  
ATOM   2476  CA BGLU A 267      22.732 -10.007  41.628  0.44 13.33           C  
ANISOU 2476  CA BGLU A 267     2379   1450   1235     77   -311    240       C  
ATOM   2477  C  AGLU A 267      22.869  -8.857  40.712  0.56 11.64           C  
ANISOU 2477  C  AGLU A 267     1995   1389   1038    274   -535     84       C  
ATOM   2478  C  BGLU A 267      23.057  -8.857  40.718  0.44 10.90           C  
ANISOU 2478  C  BGLU A 267     1609   1381   1151    122   -334    123       C  
ATOM   2479  O  AGLU A 267      22.878  -7.720  41.200  0.56 13.18           O  
ANISOU 2479  O  AGLU A 267     2156   1451   1399    418   -434    -59       O  
ATOM   2480  O  BGLU A 267      23.388  -7.753  41.178  0.44 10.40           O  
ANISOU 2480  O  BGLU A 267     1433   1412   1105    153   -403    122       O  
ATOM   2481  CB AGLU A 267      24.121 -10.730  41.833  0.56 18.60           C  
ANISOU 2481  CB AGLU A 267     2810   2092   2167    364  -1151    928       C  
ATOM   2482  CB BGLU A 267      24.011 -10.827  41.922  0.44 17.13           C  
ANISOU 2482  CB BGLU A 267     2708   1806   1992    132  -1044    640       C  
ATOM   2483  CG AGLU A 267      25.065  -9.751  42.514  0.56 25.90           C  
ANISOU 2483  CG AGLU A 267     2664   3004   4173     92  -1395    365       C  
ATOM   2484  CG BGLU A 267      23.876 -11.872  42.994  0.44 20.69           C  
ANISOU 2484  CG BGLU A 267     4057   2129   1676    343   -949    655       C  
ATOM   2485  CD AGLU A 267      26.239  -9.108  41.851  0.56 33.18           C  
ANISOU 2485  CD AGLU A 267     2804   3004   6798    111   -477    346       C  
ATOM   2486  CD BGLU A 267      23.413 -13.236  42.528  0.44 27.49           C  
ANISOU 2486  CD BGLU A 267     5723   2030   2691   -317   -527    844       C  
ATOM   2487  OE1AGLU A 267      27.265  -9.801  41.589  0.56 41.60           O  
ANISOU 2487  OE1AGLU A 267     4385   3615   7807    906   1355    372       O  
ATOM   2488  OE1BGLU A 267      23.204 -13.514  41.331  0.44 22.87           O  
ANISOU 2488  OE1BGLU A 267     3370   1912   3407    947  -1485    -95       O  
ATOM   2489  OE2AGLU A 267      26.273  -7.870  41.600  0.56 33.44           O  
ANISOU 2489  OE2AGLU A 267     3949   3522   5236    733     64   1547       O  
ATOM   2490  OE2BGLU A 267      23.252 -14.121  43.407  0.44 45.75           O  
ANISOU 2490  OE2BGLU A 267     8833   3443   5106  -1697  -2985   2989       O  
ATOM   2491  N   ARG A 268      23.021  -9.071  39.381  1.00 10.44           N  
ANISOU 2491  N   ARG A 268     1599   1225   1141    212   -145    181       N  
ATOM   2492  CA  ARG A 268      23.234  -7.963  38.449  1.00  9.93           C  
ANISOU 2492  CA  ARG A 268     1467   1114   1191    198   -164    112       C  
ATOM   2493  C   ARG A 268      22.000  -7.080  38.294  1.00  8.91           C  
ANISOU 2493  C   ARG A 268     1403    988    994     79   -134      3       C  
ATOM   2494  O   ARG A 268      22.116  -5.862  38.155  1.00  9.91           O  
ANISOU 2494  O   ARG A 268     1474    979   1313     58   -180      3       O  
ATOM   2495  CB  ARG A 268      23.653  -8.507  37.069  1.00 10.40           C  
ANISOU 2495  CB  ARG A 268     1671   1190   1092    283    -54     46       C  
ATOM   2496  CG  ARG A 268      25.037  -9.117  37.087  1.00 11.20           C  
ANISOU 2496  CG  ARG A 268     1659   1339   1259    437   -175     35       C  
ATOM   2497  CD  ARG A 268      25.293  -9.818  35.721  1.00 11.40           C  
ANISOU 2497  CD  ARG A 268     1678   1318   1335    434    -44    107       C  
ATOM   2498  NE  ARG A 268      26.653 -10.285  35.637  1.00 13.49           N  
ANISOU 2498  NE  ARG A 268     1823   1536   1768    434     91    -39       N  
ATOM   2499  CZ  ARG A 268      27.107 -11.011  34.638  1.00 15.01           C  
ANISOU 2499  CZ  ARG A 268     1781   1849   2072    617    -15   -300       C  
ATOM   2500  NH1 ARG A 268      26.269 -11.329  33.635  1.00 15.92           N  
ANISOU 2500  NH1 ARG A 268     2271   1788   1991    335   -148   -171       N  
ATOM   2501  NH2 ARG A 268      28.369 -11.384  34.623  1.00 21.17           N  
ANISOU 2501  NH2 ARG A 268     1808   3118   3116   1092    111   -267       N  
ATOM   2502  N   ILE A 269      20.816  -7.690  38.332  1.00  9.23           N  
ANISOU 2502  N   ILE A 269     1354   1023   1131    128   -178     34       N  
ATOM   2503  CA  ILE A 269      19.578  -6.881  38.326  1.00  8.86           C  
ANISOU 2503  CA  ILE A 269     1383    929   1056    115    -78    -44       C  
ATOM   2504  C   ILE A 269      19.586  -5.909  39.465  1.00  8.97           C  
ANISOU 2504  C   ILE A 269     1346   1041   1022    102   -143     -8       C  
ATOM   2505  O   ILE A 269      19.283  -4.707  39.300  1.00  9.63           O  
ANISOU 2505  O   ILE A 269     1452   1047   1160    174    -82   -104       O  
ATOM   2506  CB  ILE A 269      18.366  -7.851  38.355  1.00  8.92           C  
ANISOU 2506  CB  ILE A 269     1385   1008    998     25    -41      6       C  
ATOM   2507  CG1 ILE A 269      18.290  -8.635  37.041  1.00  9.78           C  
ANISOU 2507  CG1 ILE A 269     1498   1265    954    -83    -49    -54       C  
ATOM   2508  CG2 ILE A 269      17.072  -7.103  38.636  1.00 11.38           C  
ANISOU 2508  CG2 ILE A 269     1494   1344   1485     57     39   -249       C  
ATOM   2509  CD1 ILE A 269      17.285  -9.819  37.105  1.00 12.18           C  
ANISOU 2509  CD1 ILE A 269     1792   1330   1504   -323     40   -213       C  
ATOM   2510  N   ALA A 270      19.994  -6.384  40.664  1.00 10.35           N  
ANISOU 2510  N   ALA A 270     1706   1276    951     41   -210    -65       N  
ATOM   2511  CA  ALA A 270      20.077  -5.473  41.814  1.00 11.31           C  
ANISOU 2511  CA  ALA A 270     2021   1358    919    -35    -91    -14       C  
ATOM   2512  C   ALA A 270      21.210  -4.455  41.664  1.00 11.28           C  
ANISOU 2512  C   ALA A 270     1827   1398   1058      8   -408   -138       C  
ATOM   2513  O   ALA A 270      21.004  -3.269  41.964  1.00 13.26           O  
ANISOU 2513  O   ALA A 270     2189   1387   1464    -13   -358   -276       O  
ATOM   2514  CB  ALA A 270      20.257  -6.360  43.067  1.00 16.24           C  
ANISOU 2514  CB  ALA A 270     3319   1919    933   -132   -322    190       C  
ATOM   2515  N  AGLU A 271      22.396  -4.867  41.216  0.66 11.47           N  
ANISOU 2515  N  AGLU A 271     1683   1455   1219     12   -469     69       N  
ATOM   2516  N  BGLU A 271      22.398  -4.852  41.230  0.34 11.71           N  
ANISOU 2516  N  BGLU A 271     1713   1377   1359     15   -481     75       N  
ATOM   2517  CA AGLU A 271      23.518  -3.938  40.974  0.66 12.20           C  
ANISOU 2517  CA AGLU A 271     1773   1495   1368    -55   -339     40       C  
ATOM   2518  CA BGLU A 271      23.505  -3.881  41.087  0.34 12.53           C  
ANISOU 2518  CA BGLU A 271     1711   1236   1815     26   -640     78       C  
ATOM   2519  C  AGLU A 271      23.102  -2.789  40.087  0.66 10.71           C  
ANISOU 2519  C  AGLU A 271     1371   1238   1460     16   -351   -195       C  
ATOM   2520  C  BGLU A 271      23.164  -2.821  40.056  0.34 11.17           C  
ANISOU 2520  C  BGLU A 271     1610   1322   1312     22   -289    -93       C  
ATOM   2521  O  AGLU A 271      23.395  -1.633  40.390  0.66 14.06           O  
ANISOU 2521  O  AGLU A 271     1741   1249   2354   -119   -474   -361       O  
ATOM   2522  O  BGLU A 271      23.559  -1.659  40.233  0.34  9.05           O  
ANISOU 2522  O  BGLU A 271     1412   1249    777    157   -220    -54       O  
ATOM   2523  CB AGLU A 271      24.685  -4.721  40.286  0.66 12.58           C  
ANISOU 2523  CB AGLU A 271     1586   1363   1830     39   -432    153       C  
ATOM   2524  CB BGLU A 271      24.771  -4.678  40.730  0.34 16.44           C  
ANISOU 2524  CB BGLU A 271     1679   2218   2350    336   -367    433       C  
ATOM   2525  CG AGLU A 271      25.880  -3.896  39.843  0.66 13.24           C  
ANISOU 2525  CG AGLU A 271     1743   1468   1819    105    -67    -24       C  
ATOM   2526  CG BGLU A 271      26.029  -3.923  40.368  0.34 17.98           C  
ANISOU 2526  CG BGLU A 271     1909   2399   2525    140   -218    330       C  
ATOM   2527  CD AGLU A 271      27.095  -4.752  39.490  0.66 14.70           C  
ANISOU 2527  CD AGLU A 271     1840   1641   2102    362    -14    283       C  
ATOM   2528  CD BGLU A 271      26.839  -4.624  39.280  0.34 13.96           C  
ANISOU 2528  CD BGLU A 271     1647   1882   1776   -239   -603    492       C  
ATOM   2529  OE1AGLU A 271      27.465  -5.652  40.262  0.66 17.22           O  
ANISOU 2529  OE1AGLU A 271     1870   2205   2469    321   -361    729       O  
ATOM   2530  OE1BGLU A 271      27.079  -3.935  38.265  0.34 21.31           O  
ANISOU 2530  OE1BGLU A 271     3902   2834   1361  -1708   -868    393       O  
ATOM   2531  OE2AGLU A 271      27.630  -4.412  38.413  0.66 11.74           O  
ANISOU 2531  OE2AGLU A 271     1340   1516   1605    130   -373   -128       O  
ATOM   2532  OE2BGLU A 271      27.186  -5.814  39.456  0.34 21.76           O  
ANISOU 2532  OE2BGLU A 271     3346   2336   2587    875  -1081    199       O  
ATOM   2533  N   ASN A 272      22.452  -3.166  38.978  1.00 10.24           N  
ANISOU 2533  N   ASN A 272     1496   1193   1203     71   -189   -134       N  
ATOM   2534  CA  ASN A 272      22.126  -2.197  37.937  1.00  9.97           C  
ANISOU 2534  CA  ASN A 272     1542   1121   1125    -68    -24    -58       C  
ATOM   2535  C   ASN A 272      21.137  -1.134  38.398  1.00  9.63           C  
ANISOU 2535  C   ASN A 272     1458   1083   1116    -81    -24   -123       C  
ATOM   2536  O   ASN A 272      21.053  -0.075  37.783  1.00 11.80           O  
ANISOU 2536  O   ASN A 272     1920   1136   1428     91    185     86       O  
ATOM   2537  CB  ASN A 272      21.570  -2.937  36.713  1.00  9.84           C  
ANISOU 2537  CB  ASN A 272     1497   1206   1035      2    -53   -139       C  
ATOM   2538  CG  ASN A 272      22.617  -3.769  35.983  1.00  9.94           C  
ANISOU 2538  CG  ASN A 272     1478   1193   1107    -40     70      3       C  
ATOM   2539  OD1 ASN A 272      23.813  -3.715  36.267  1.00 11.45           O  
ANISOU 2539  OD1 ASN A 272     1498   1401   1451     34    -28   -220       O  
ATOM   2540  ND2 ASN A 272      22.154  -4.536  34.987  1.00 10.62           N  
ANISOU 2540  ND2 ASN A 272     1578   1328   1129     42     -3   -154       N  
ATOM   2541  N   PHE A 273      20.397  -1.426  39.480  1.00  9.97           N  
ANISOU 2541  N   PHE A 273     1521   1094   1175     18      1    -67       N  
ATOM   2542  CA  PHE A 273      19.449  -0.445  40.032  1.00  9.79           C  
ANISOU 2542  CA  PHE A 273     1470   1007   1242    -77     81   -112       C  
ATOM   2543  C   PHE A 273      20.103   0.533  40.962  1.00  9.75           C  
ANISOU 2543  C   PHE A 273     1648   1008   1050    -63     42    -26       C  
ATOM   2544  O   PHE A 273      19.528   1.563  41.288  1.00 11.78           O  
ANISOU 2544  O   PHE A 273     1753   1150   1574    -48    189   -249       O  
ATOM   2545  CB  PHE A 273      18.291  -1.213  40.761  1.00 12.21           C  
ANISOU 2545  CB  PHE A 273     1574   1089   1975   -136    352   -160       C  
ATOM   2546  CG  PHE A 273      17.019  -0.353  40.874  1.00 12.90           C  
ANISOU 2546  CG  PHE A 273     1565    984   2354   -235    385   -201       C  
ATOM   2547  CD1 PHE A 273      16.206  -0.120  39.768  1.00 18.07           C  
ANISOU 2547  CD1 PHE A 273     1831   1424   3609   -110   -535   -350       C  
ATOM   2548  CD2 PHE A 273      16.691   0.161  42.103  1.00 18.32           C  
ANISOU 2548  CD2 PHE A 273     2516   1686   2761   -266   1298   -379       C  
ATOM   2549  CE1 PHE A 273      15.040   0.679  39.854  1.00 22.75           C  
ANISOU 2549  CE1 PHE A 273     1769   1448   5428    -62   -511   -576       C  
ATOM   2550  CE2 PHE A 273      15.550   0.969  42.238  1.00 22.67           C  
ANISOU 2550  CE2 PHE A 273     2656   1677   4280   -256   1940   -249       C  
ATOM   2551  CZ  PHE A 273      14.762   1.205  41.102  1.00 25.93           C  
ANISOU 2551  CZ  PHE A 273     2257   1690   5907   -207    852   -458       C  
ATOM   2552  N   LYS A 274      21.303   0.222  41.469  1.00 10.31           N  
ANISOU 2552  N   LYS A 274     1723   1269    925   -148    -54    -37       N  
ATOM   2553  CA  LYS A 274      21.966   1.047  42.492  1.00 11.61           C  
ANISOU 2553  CA  LYS A 274     2070   1336   1005   -122   -123   -163       C  
ATOM   2554  C   LYS A 274      22.817   2.127  41.823  1.00 11.50           C  
ANISOU 2554  C   LYS A 274     1849   1431   1090   -255    -51   -160       C  
ATOM   2555  O   LYS A 274      24.049   2.157  41.955  1.00 15.02           O  
ANISOU 2555  O   LYS A 274     1930   2061   1716   -269   -301   -126       O  
ATOM   2556  CB  LYS A 274      22.806   0.128  43.394  1.00 14.49           C  
ANISOU 2556  CB  LYS A 274     2516   1982   1006   -125   -409    157       C  
ATOM   2557  CG  LYS A 274      21.942  -0.818  44.217  1.00 19.48           C  
ANISOU 2557  CG  LYS A 274     3892   1964   1545   -809   -545    360       C  
ATOM   2558  CD  LYS A 274      22.800  -1.588  45.228  1.00 30.49           C  
ANISOU 2558  CD  LYS A 274     5771   3487   2328    784     -3   1482       C  
ATOM   2559  CE  LYS A 274      21.945  -2.719  45.749  1.00 38.16           C  
ANISOU 2559  CE  LYS A 274     7761   3488   3249    774   1273   1851       C  
ATOM   2560  NZ  LYS A 274      22.698  -3.771  46.475  0.50 43.23           N  
ANISOU 2560  NZ  LYS A 274    10031   4015   2382   2118   2008   1925       N  
ATOM   2561  N   VAL A 275      22.102   3.026  41.133  1.00 11.08           N  
ANISOU 2561  N   VAL A 275     1793   1292   1125   -344     29   -120       N  
ATOM   2562  CA  VAL A 275      22.727   4.071  40.303  1.00 11.74           C  
ANISOU 2562  CA  VAL A 275     1998   1228   1233   -356    117   -158       C  
ATOM   2563  C   VAL A 275      22.165   5.417  40.619  1.00 12.81           C  
ANISOU 2563  C   VAL A 275     2069   1360   1439   -262    286   -170       C  
ATOM   2564  O   VAL A 275      22.451   6.400  39.881  1.00 16.52           O  
ANISOU 2564  O   VAL A 275     3200   1299   1776   -243    781    -68       O  
ATOM   2565  CB  VAL A 275      22.580   3.787  38.800  1.00 12.68           C  
ANISOU 2565  CB  VAL A 275     2001   1598   1220   -119    216   -142       C  
ATOM   2566  CG1 VAL A 275      23.419   2.529  38.432  1.00 14.37           C  
ANISOU 2566  CG1 VAL A 275     2141   1721   1597     33    144   -418       C  
ATOM   2567  CG2 VAL A 275      21.143   3.561  38.362  1.00 13.57           C  
ANISOU 2567  CG2 VAL A 275     2125   1692   1340     18   -206    -19       C  
ATOM   2568  N   PHE A 276      21.423   5.556  41.736  1.00 13.32           N  
ANISOU 2568  N   PHE A 276     2191   1438   1430   -267    402   -272       N  
ATOM   2569  CA  PHE A 276      20.824   6.840  42.065  1.00 15.29           C  
ANISOU 2569  CA  PHE A 276     2220   1568   2021    -66    249   -470       C  
ATOM   2570  C   PHE A 276      21.549   7.578  43.180  1.00 17.84           C  
ANISOU 2570  C   PHE A 276     2870   1787   2121   -426    372   -725       C  
ATOM   2571  O   PHE A 276      21.136   8.612  43.670  1.00 29.56           O  
ANISOU 2571  O   PHE A 276     3789   2804   4639     -2   -269  -2243       O  
ATOM   2572  CB  PHE A 276      19.316   6.670  42.438  1.00 16.28           C  
ANISOU 2572  CB  PHE A 276     2420   2033   1733   -239    703   -549       C  
ATOM   2573  CG  PHE A 276      18.425   6.146  41.291  1.00 15.29           C  
ANISOU 2573  CG  PHE A 276     1965   1989   1855     29    434   -122       C  
ATOM   2574  CD1 PHE A 276      17.808   7.022  40.407  1.00 22.04           C  
ANISOU 2574  CD1 PHE A 276     2599   3191   2585    535    411    563       C  
ATOM   2575  CD2 PHE A 276      18.240   4.781  41.142  1.00 17.38           C  
ANISOU 2575  CD2 PHE A 276     2006   2137   2461   -203    273   -607       C  
ATOM   2576  CE1 PHE A 276      17.006   6.562  39.358  1.00 26.67           C  
ANISOU 2576  CE1 PHE A 276     3221   4924   1987    292    177    928       C  
ATOM   2577  CE2 PHE A 276      17.439   4.311  40.081  1.00 21.87           C  
ANISOU 2577  CE2 PHE A 276     2274   3387   2647   -216    210  -1105       C  
ATOM   2578  CZ  PHE A 276      16.858   5.192  39.197  1.00 29.67           C  
ANISOU 2578  CZ  PHE A 276     3908   5278   2086    392   -202   -700       C  
ATOM   2579  N   ASP A 277      22.660   7.055  43.652  1.00 17.43           N  
ANISOU 2579  N   ASP A 277     2745   2213   1664   -807    280   -513       N  
ATOM   2580  CA  ASP A 277      23.397   7.583  44.790  1.00 20.28           C  
ANISOU 2580  CA  ASP A 277     3500   2964   1241  -1517    392   -516       C  
ATOM   2581  C   ASP A 277      24.795   8.060  44.451  1.00 18.32           C  
ANISOU 2581  C   ASP A 277     3292   2361   1308  -1135    170   -292       C  
ATOM   2582  O   ASP A 277      25.587   8.271  45.349  1.00 23.87           O  
ANISOU 2582  O   ASP A 277     3822   3902   1347  -1847    228   -675       O  
ATOM   2583  CB  ASP A 277      23.467   6.449  45.839  1.00 25.19           C  
ANISOU 2583  CB  ASP A 277     4084   3778   1708  -1929    139    174       C  
ATOM   2584  CG  ASP A 277      24.260   5.215  45.503  1.00 29.79           C  
ANISOU 2584  CG  ASP A 277     5365   3232   2721  -1668   -380    474       C  
ATOM   2585  OD1 ASP A 277      24.735   5.062  44.366  1.00 29.32           O  
ANISOU 2585  OD1 ASP A 277     4929   3216   2996   -109   -322    541       O  
ATOM   2586  OD2 ASP A 277      24.403   4.313  46.385  1.00 38.66           O  
ANISOU 2586  OD2 ASP A 277     5857   4824   4010  -1258   -215   1926       O  
ATOM   2587  N   PHE A 278      25.119   8.289  43.188  1.00 16.89           N  
ANISOU 2587  N   PHE A 278     2801   2284   1334   -878    362   -474       N  
ATOM   2588  CA  PHE A 278      26.364   8.933  42.799  1.00 15.74           C  
ANISOU 2588  CA  PHE A 278     2514   2088   1379   -683     15   -172       C  
ATOM   2589  C   PHE A 278      26.113   9.750  41.549  1.00 14.10           C  
ANISOU 2589  C   PHE A 278     2153   1913   1290   -509      8   -314       C  
ATOM   2590  O   PHE A 278      25.062   9.614  40.880  1.00 17.22           O  
ANISOU 2590  O   PHE A 278     2219   2360   1965   -527   -259   -223       O  
ATOM   2591  CB  PHE A 278      27.469   7.872  42.635  1.00 16.83           C  
ANISOU 2591  CB  PHE A 278     2653   2459   1281   -332   -444   -219       C  
ATOM   2592  CG  PHE A 278      27.443   7.129  41.300  1.00 15.09           C  
ANISOU 2592  CG  PHE A 278     2383   2046   1304   -478   -177    -98       C  
ATOM   2593  CD1 PHE A 278      26.468   6.201  41.028  1.00 16.17           C  
ANISOU 2593  CD1 PHE A 278     2084   2195   1866   -216   -331   -413       C  
ATOM   2594  CD2 PHE A 278      28.426   7.361  40.334  1.00 16.14           C  
ANISOU 2594  CD2 PHE A 278     2397   2168   1569    -61    -30     74       C  
ATOM   2595  CE1 PHE A 278      26.509   5.491  39.808  1.00 18.04           C  
ANISOU 2595  CE1 PHE A 278     2134   2638   2084   -238   -215   -766       C  
ATOM   2596  CE2 PHE A 278      28.464   6.651  39.129  1.00 16.59           C  
ANISOU 2596  CE2 PHE A 278     2493   2308   1502     52    -50     42       C  
ATOM   2597  CZ  PHE A 278      27.494   5.685  38.868  1.00 16.88           C  
ANISOU 2597  CZ  PHE A 278     2115   2680   1619    289   -527   -103       C  
ATOM   2598  N   GLU A 279      27.077  10.608  41.225  1.00 14.37           N  
ANISOU 2598  N   GLU A 279     2220   1932   1307   -588    176   -316       N  
ATOM   2599  CA  GLU A 279      26.997  11.447  40.029  1.00 15.31           C  
ANISOU 2599  CA  GLU A 279     2177   2374   1264   -428    119    -95       C  
ATOM   2600  C   GLU A 279      28.343  11.438  39.310  1.00 13.61           C  
ANISOU 2600  C   GLU A 279     1931   2114   1128   -371    -46   -127       C  
ATOM   2601  O   GLU A 279      29.387  11.529  39.948  1.00 18.55           O  
ANISOU 2601  O   GLU A 279     2176   3677   1193   -566   -191   -213       O  
ATOM   2602  CB  GLU A 279      26.701  12.915  40.470  1.00 23.26           C  
ANISOU 2602  CB  GLU A 279     3829   2630   2379    803    997    230       C  
ATOM   2603  CG  GLU A 279      26.386  13.917  39.400  1.00 39.29           C  
ANISOU 2603  CG  GLU A 279     7478   3085   4364    912    434   1214       C  
ATOM   2604  CD  GLU A 279      25.529  15.100  39.828  1.00 51.64           C  
ANISOU 2604  CD  GLU A 279     8045   3316   8259   1933     94   1467       C  
ATOM   2605  OE1 GLU A 279      25.246  15.238  41.037  1.00 54.35           O  
ANISOU 2605  OE1 GLU A 279     7588   3335   9726   1236   2530   -169       O  
ATOM   2606  OE2 GLU A 279      25.161  15.879  38.916  1.00 64.43           O  
ANISOU 2606  OE2 GLU A 279     8840   3942  11699    900  -3262   2534       O  
ATOM   2607  N   LEU A 280      28.312  11.339  38.012  1.00 11.85           N  
ANISOU 2607  N   LEU A 280     1809   1504   1191   -405    -65   -126       N  
ATOM   2608  CA  LEU A 280      29.499  11.586  37.172  1.00 10.99           C  
ANISOU 2608  CA  LEU A 280     1637   1402   1138   -333    -24    -77       C  
ATOM   2609  C   LEU A 280      29.689  13.070  37.006  1.00 11.07           C  
ANISOU 2609  C   LEU A 280     1610   1311   1283   -299   -107   -333       C  
ATOM   2610  O   LEU A 280      28.739  13.850  36.847  1.00 13.38           O  
ANISOU 2610  O   LEU A 280     1697   1302   2084   -301   -161   -306       O  
ATOM   2611  CB  LEU A 280      29.245  10.936  35.802  1.00 11.67           C  
ANISOU 2611  CB  LEU A 280     1969   1171   1296   -281    -20   -290       C  
ATOM   2612  CG  LEU A 280      29.073   9.400  35.851  1.00 11.96           C  
ANISOU 2612  CG  LEU A 280     1915   1237   1392   -232    -52   -110       C  
ATOM   2613  CD1 LEU A 280      28.566   8.885  34.500  1.00 13.99           C  
ANISOU 2613  CD1 LEU A 280     2295   1403   1617   -507   -173   -394       C  
ATOM   2614  CD2 LEU A 280      30.370   8.701  36.247  1.00 17.16           C  
ANISOU 2614  CD2 LEU A 280     2282   1459   2777    147   -518   -224       C  
ATOM   2615  N   SER A 281      30.960  13.529  37.075  1.00 11.21           N  
ANISOU 2615  N   SER A 281     1708   1369   1184   -451    -28   -201       N  
ATOM   2616  CA  SER A 281      31.200  14.957  36.908  1.00 11.62           C  
ANISOU 2616  CA  SER A 281     1843   1356   1216   -493   -128   -262       C  
ATOM   2617  C   SER A 281      31.012  15.386  35.431  1.00 10.36           C  
ANISOU 2617  C   SER A 281     1552   1099   1284   -351    -31   -262       C  
ATOM   2618  O   SER A 281      30.978  14.554  34.541  1.00 11.32           O  
ANISOU 2618  O   SER A 281     1867   1194   1240   -382   -134   -298       O  
ATOM   2619  CB  SER A 281      32.650  15.267  37.372  1.00 12.53           C  
ANISOU 2619  CB  SER A 281     1674   1601   1486   -438   -151   -372       C  
ATOM   2620  OG  SER A 281      33.547  14.651  36.426  1.00 12.86           O  
ANISOU 2620  OG  SER A 281     1779   1784   1322   -453   -122   -303       O  
ATOM   2621  N   SER A 282      30.936  16.695  35.184  1.00 12.24           N  
ANISOU 2621  N   SER A 282     1885   1072   1695   -217    125   -209       N  
ATOM   2622  CA  SER A 282      30.901  17.191  33.803  1.00 12.37           C  
ANISOU 2622  CA  SER A 282     1792   1186   1721      7     -1     16       C  
ATOM   2623  C   SER A 282      32.136  16.698  33.038  1.00 10.79           C  
ANISOU 2623  C   SER A 282     1669    940   1490   -221    -79   -183       C  
ATOM   2624  O   SER A 282      32.031  16.325  31.876  1.00 12.00           O  
ANISOU 2624  O   SER A 282     1837   1192   1532   -174   -314   -174       O  
ATOM   2625  CB  SER A 282      30.852  18.728  33.851  1.00 15.91           C  
ANISOU 2625  CB  SER A 282     2865   1279   1902    330    511     44       C  
ATOM   2626  OG ASER A 282      31.924  19.257  34.580  0.33 22.15           O  
ANISOU 2626  OG ASER A 282     4256   1363   2795   -116   -126   -872       O  
ATOM   2627  OG BSER A 282      29.514  19.125  34.113  0.33 32.14           O  
ANISOU 2627  OG BSER A 282     3734   3079   5398   1852    954    -36       O  
ATOM   2628  OG CSER A 282      30.978  19.285  32.589  0.33 12.14           O  
ANISOU 2628  OG CSER A 282     2214    751   1648    462    282    -67       O  
ATOM   2629  N   GLN A 283      33.307  16.723  33.692  1.00 10.83           N  
ANISOU 2629  N   GLN A 283     1605   1002   1509   -211    -51   -175       N  
ATOM   2630  CA  GLN A 283      34.516  16.251  33.044  1.00 11.13           C  
ANISOU 2630  CA  GLN A 283     1524   1053   1652   -264   -187   -311       C  
ATOM   2631  C   GLN A 283      34.423  14.783  32.684  1.00 10.24           C  
ANISOU 2631  C   GLN A 283     1419   1130   1342   -213   -143   -214       C  
ATOM   2632  O   GLN A 283      34.810  14.351  31.600  1.00 11.58           O  
ANISOU 2632  O   GLN A 283     1680   1351   1368   -175    -59   -276       O  
ATOM   2633  CB  GLN A 283      35.640  16.543  34.080  1.00 12.77           C  
ANISOU 2633  CB  GLN A 283     1572   1427   1855   -283   -227   -467       C  
ATOM   2634  CG  GLN A 283      37.034  16.235  33.496  1.00 12.44           C  
ANISOU 2634  CG  GLN A 283     1635   1548   1542    -98   -212   -347       C  
ATOM   2635  CD  GLN A 283      38.127  16.695  34.461  1.00 12.45           C  
ANISOU 2635  CD  GLN A 283     1706   1450   1576   -270   -171   -286       C  
ATOM   2636  OE1 GLN A 283      39.365  16.622  34.118  1.00 18.07           O  
ANISOU 2636  OE1 GLN A 283     1552   2717   2594   -121      1   -252       O  
ATOM   2637  NE2 GLN A 283      37.778  17.177  35.580  1.00 11.93           N  
ANISOU 2637  NE2 GLN A 283     1741   1413   1379   -467   -189   -190       N  
ATOM   2638  N   ASP A 284      33.915  13.935  33.617  1.00 10.51           N  
ANISOU 2638  N   ASP A 284     1626   1035   1331   -181   -213   -189       N  
ATOM   2639  CA  ASP A 284      33.681  12.521  33.291  1.00 10.81           C  
ANISOU 2639  CA  ASP A 284     1759    999   1348   -144   -296   -112       C  
ATOM   2640  C   ASP A 284      32.754  12.347  32.105  1.00  9.44           C  
ANISOU 2640  C   ASP A 284     1391   1028   1167   -254    -44   -101       C  
ATOM   2641  O   ASP A 284      32.971  11.458  31.260  1.00 10.64           O  
ANISOU 2641  O   ASP A 284     1609   1077   1357   -142    -80   -206       O  
ATOM   2642  CB  ASP A 284      33.001  11.798  34.512  1.00 14.28           C  
ANISOU 2642  CB  ASP A 284     2808   1207   1412   -465   -548    170       C  
ATOM   2643  CG  ASP A 284      33.769  11.565  35.790  1.00 14.53           C  
ANISOU 2643  CG  ASP A 284     2153   1891   1477   -134   -148    147       C  
ATOM   2644  OD1 ASP A 284      35.025  11.427  35.749  1.00 18.00           O  
ANISOU 2644  OD1 ASP A 284     1849   2426   2563    202   -341   -260       O  
ATOM   2645  OD2 ASP A 284      33.082  11.450  36.854  1.00 16.72           O  
ANISOU 2645  OD2 ASP A 284     2541   2230   1582   -169     29    103       O  
ATOM   2646  N   MET A 285      31.663  13.142  32.088  1.00  9.38           N  
ANISOU 2646  N   MET A 285     1357   1070   1136   -277    -80    -97       N  
ATOM   2647  CA  MET A 285      30.685  13.022  30.967  1.00  9.15           C  
ANISOU 2647  CA  MET A 285     1396    975   1106   -213    -47   -116       C  
ATOM   2648  C   MET A 285      31.338  13.353  29.649  1.00  9.03           C  
ANISOU 2648  C   MET A 285     1282   1033   1117   -191    -53   -173       C  
ATOM   2649  O   MET A 285      31.155  12.612  28.668  1.00 10.13           O  
ANISOU 2649  O   MET A 285     1440   1236   1174   -198    -50   -194       O  
ATOM   2650  CB  MET A 285      29.520  13.937  31.250  1.00  9.94           C  
ANISOU 2650  CB  MET A 285     1356   1140   1280   -137     83   -144       C  
ATOM   2651  CG  MET A 285      28.621  13.513  32.424  1.00 11.07           C  
ANISOU 2651  CG  MET A 285     1527   1495   1182   -428     54   -202       C  
ATOM   2652  SD  MET A 285      27.734  11.967  32.186  1.00 11.48           S  
ANISOU 2652  SD  MET A 285     1573   1339   1448   -322    -28    -42       S  
ATOM   2653  CE  MET A 285      26.649  12.445  30.863  1.00 13.52           C  
ANISOU 2653  CE  MET A 285     1850   1500   1787   -436   -542    -73       C  
ATOM   2654  N   THR A 286      32.095  14.459  29.582  1.00  9.36           N  
ANISOU 2654  N   THR A 286     1351   1036   1170   -233     -5    -33       N  
ATOM   2655  CA  THR A 286      32.751  14.841  28.333  1.00  9.68           C  
ANISOU 2655  CA  THR A 286     1432   1028   1219   -122     26    -24       C  
ATOM   2656  C   THR A 286      33.784  13.778  27.936  1.00  9.51           C  
ANISOU 2656  C   THR A 286     1305   1110   1200   -268    -10    -55       C  
ATOM   2657  O   THR A 286      33.922  13.467  26.750  1.00 10.90           O  
ANISOU 2657  O   THR A 286     1618   1304   1220   -135     57   -164       O  
ATOM   2658  CB  THR A 286      33.372  16.244  28.526  1.00 11.10           C  
ANISOU 2658  CB  THR A 286     1640   1019   1557   -152    186    146       C  
ATOM   2659  OG1 THR A 286      32.290  17.163  28.740  1.00 13.30           O  
ANISOU 2659  OG1 THR A 286     1948   1152   1955     95    199    -68       O  
ATOM   2660  CG2 THR A 286      34.186  16.656  27.288  1.00 13.03           C  
ANISOU 2660  CG2 THR A 286     2206   1308   1435   -364    313    123       C  
ATOM   2661  N   THR A 287      34.483  13.218  28.917  1.00  9.60           N  
ANISOU 2661  N   THR A 287     1314    981   1352   -185    -60    -46       N  
ATOM   2662  CA  THR A 287      35.468  12.171  28.620  1.00 10.16           C  
ANISOU 2662  CA  THR A 287     1317   1099   1444   -175    -25   -175       C  
ATOM   2663  C   THR A 287      34.755  10.930  28.035  1.00 10.13           C  
ANISOU 2663  C   THR A 287     1395   1071   1383   -159     60   -174       C  
ATOM   2664  O   THR A 287      35.205  10.366  27.044  1.00 10.90           O  
ANISOU 2664  O   THR A 287     1389   1234   1519   -143    121   -254       O  
ATOM   2665  CB  THR A 287      36.246  11.820  29.888  1.00 11.19           C  
ANISOU 2665  CB  THR A 287     1509   1069   1673    -93   -197   -122       C  
ATOM   2666  OG1 THR A 287      36.948  13.018  30.302  1.00 13.81           O  
ANISOU 2666  OG1 THR A 287     1793   1538   1916   -423   -472   -146       O  
ATOM   2667  CG2 THR A 287      37.247  10.700  29.650  1.00 14.24           C  
ANISOU 2667  CG2 THR A 287     1667   1706   2036    310   -219   -194       C  
ATOM   2668  N   LEU A 288      33.647  10.484  28.662  1.00  9.91           N  
ANISOU 2668  N   LEU A 288     1438   1056   1273   -257     26   -105       N  
ATOM   2669  CA  LEU A 288      32.938   9.308  28.109  1.00  9.85           C  
ANISOU 2669  CA  LEU A 288     1455    999   1290   -276     -7    -94       C  
ATOM   2670  C   LEU A 288      32.428   9.581  26.698  1.00  9.62           C  
ANISOU 2670  C   LEU A 288     1379    995   1282   -250    124   -179       C  
ATOM   2671  O   LEU A 288      32.458   8.702  25.832  1.00 10.85           O  
ANISOU 2671  O   LEU A 288     1623   1139   1359   -187     88   -283       O  
ATOM   2672  CB  LEU A 288      31.785   8.923  29.048  1.00 10.55           C  
ANISOU 2672  CB  LEU A 288     1476   1182   1351   -270    -20     14       C  
ATOM   2673  CG  LEU A 288      32.232   8.217  30.305  1.00 11.06           C  
ANISOU 2673  CG  LEU A 288     1560   1163   1479   -182     30    127       C  
ATOM   2674  CD1 LEU A 288      31.145   8.273  31.402  1.00 13.41           C  
ANISOU 2674  CD1 LEU A 288     1746   1773   1575     -2    186    180       C  
ATOM   2675  CD2 LEU A 288      32.615   6.765  30.043  1.00 15.93           C  
ANISOU 2675  CD2 LEU A 288     2507   1312   2234    297    366    249       C  
ATOM   2676  N   LEU A 289      31.934  10.813  26.440  1.00  9.55           N  
ANISOU 2676  N   LEU A 289     1270   1151   1208   -147    -26   -161       N  
ATOM   2677  CA  LEU A 289      31.503  11.152  25.094  1.00 10.23           C  
ANISOU 2677  CA  LEU A 289     1370   1228   1288   -105     65    -64       C  
ATOM   2678  C   LEU A 289      32.622  11.055  24.074  1.00 10.15           C  
ANISOU 2678  C   LEU A 289     1361   1325   1172    -98     12   -127       C  
ATOM   2679  O   LEU A 289      32.417  10.711  22.918  1.00 12.26           O  
ANISOU 2679  O   LEU A 289     1516   1863   1280   -199     80   -267       O  
ATOM   2680  CB  LEU A 289      30.866  12.556  25.048  1.00 10.03           C  
ANISOU 2680  CB  LEU A 289     1448   1214   1147   -170    130    -46       C  
ATOM   2681  CG  LEU A 289      29.500  12.674  25.710  1.00 10.58           C  
ANISOU 2681  CG  LEU A 289     1428   1247   1344    -42     88   -202       C  
ATOM   2682  CD1 LEU A 289      29.148  14.172  25.928  1.00 15.58           C  
ANISOU 2682  CD1 LEU A 289     1974   1485   2460    247    152   -430       C  
ATOM   2683  CD2 LEU A 289      28.417  12.004  24.854  1.00 12.75           C  
ANISOU 2683  CD2 LEU A 289     1432   1707   1707   -136    -54   -143       C  
ATOM   2684  N   SER A 290      33.867  11.309  24.526  1.00 10.20           N  
ANISOU 2684  N   SER A 290     1302   1166   1408   -163     84    -44       N  
ATOM   2685  CA  SER A 290      35.018  11.287  23.606  1.00 10.62           C  
ANISOU 2685  CA  SER A 290     1403   1175   1458   -322    181    -38       C  
ATOM   2686  C   SER A 290      35.362   9.895  23.102  1.00 10.33           C  
ANISOU 2686  C   SER A 290     1319   1237   1368   -180    143    -68       C  
ATOM   2687  O   SER A 290      36.175   9.775  22.173  1.00 12.92           O  
ANISOU 2687  O   SER A 290     1655   1535   1720   -343    459   -145       O  
ATOM   2688  CB  SER A 290      36.249  11.921  24.257  1.00 11.99           C  
ANISOU 2688  CB  SER A 290     1339   1431   1786   -403     93      0       C  
ATOM   2689  OG  SER A 290      36.926  11.004  25.127  1.00 13.38           O  
ANISOU 2689  OG  SER A 290     1464   1831   1787   -394    -45     53       O  
ATOM   2690  N   TYR A 291      34.762   8.852  23.695  1.00 10.92           N  
ANISOU 2690  N   TYR A 291     1456   1115   1578   -209    252   -206       N  
ATOM   2691  CA  TYR A 291      35.090   7.459  23.323  1.00 10.72           C  
ANISOU 2691  CA  TYR A 291     1559   1114   1400    -31    187   -167       C  
ATOM   2692  C   TYR A 291      34.278   7.003  22.098  1.00 10.39           C  
ANISOU 2692  C   TYR A 291     1258   1131   1558   -175    233   -220       C  
ATOM   2693  O   TYR A 291      34.482   5.890  21.616  1.00 11.74           O  
ANISOU 2693  O   TYR A 291     1541   1236   1682   -128    187   -268       O  
ATOM   2694  CB  TYR A 291      34.890   6.510  24.491  1.00 11.60           C  
ANISOU 2694  CB  TYR A 291     1598   1301   1510    -88     94    -80       C  
ATOM   2695  CG  TYR A 291      35.794   6.823  25.666  1.00 11.52           C  
ANISOU 2695  CG  TYR A 291     1490   1263   1624    173     87   -131       C  
ATOM   2696  CD1 TYR A 291      36.975   7.537  25.563  1.00 13.68           C  
ANISOU 2696  CD1 TYR A 291     1588   1544   2066     -3   -204   -251       C  
ATOM   2697  CD2 TYR A 291      35.411   6.404  26.955  1.00 14.16           C  
ANISOU 2697  CD2 TYR A 291     2126   1693   1562    223     -5     -5       C  
ATOM   2698  CE1 TYR A 291      37.754   7.821  26.671  1.00 15.24           C  
ANISOU 2698  CE1 TYR A 291     1920   1601   2271    232   -481   -293       C  
ATOM   2699  CE2 TYR A 291      36.205   6.698  28.077  1.00 16.10           C  
ANISOU 2699  CE2 TYR A 291     2483   1879   1756    409   -269    -30       C  
ATOM   2700  CZ  TYR A 291      37.375   7.398  27.917  1.00 15.69           C  
ANISOU 2700  CZ  TYR A 291     2423   1435   2102    447   -534   -415       C  
ATOM   2701  OH  TYR A 291      38.117   7.651  29.040  1.00 19.85           O  
ANISOU 2701  OH  TYR A 291     3319   1827   2396    775  -1141   -600       O  
ATOM   2702  N   ASN A 292      33.422   7.884  21.527  1.00 10.56           N  
ANISOU 2702  N   ASN A 292     1278   1195   1541   -297    136    -89       N  
ATOM   2703  CA  ASN A 292      32.622   7.506  20.382  1.00 10.60           C  
ANISOU 2703  CA  ASN A 292     1348   1234   1445   -217    283   -186       C  
ATOM   2704  C   ASN A 292      33.489   6.970  19.237  1.00 11.06           C  
ANISOU 2704  C   ASN A 292     1361   1370   1474   -239    306    -20       C  
ATOM   2705  O   ASN A 292      34.512   7.555  18.909  1.00 13.52           O  
ANISOU 2705  O   ASN A 292     1510   1786   1841   -420    596   -120       O  
ATOM   2706  CB  ASN A 292      31.860   8.736  19.864  1.00 11.41           C  
ANISOU 2706  CB  ASN A 292     1240   1360   1734   -274    193     32       C  
ATOM   2707  CG  ASN A 292      30.955   8.368  18.700  1.00 11.49           C  
ANISOU 2707  CG  ASN A 292     1585   1298   1481   -358    287     22       C  
ATOM   2708  OD1 ASN A 292      30.145   7.447  18.777  1.00 11.60           O  
ANISOU 2708  OD1 ASN A 292     1483   1281   1645   -345    225    -50       O  
ATOM   2709  ND2 ASN A 292      31.051   9.044  17.593  1.00 18.81           N  
ANISOU 2709  ND2 ASN A 292     2880   2271   1997  -1282   -399    780       N  
ATOM   2710  N  AARG A 293      32.992   5.871  18.652  0.35 10.45           N  
ANISOU 2710  N  AARG A 293     1175   1422   1373     20    288   -268       N  
ATOM   2711  N  BARG A 293      33.042   5.863  18.625  0.65 11.88           N  
ANISOU 2711  N  BARG A 293     1524   1594   1397   -221    256   -307       N  
ATOM   2712  CA AARG A 293      33.552   5.095  17.543  0.35 13.50           C  
ANISOU 2712  CA AARG A 293     1586   2278   1265    163    581   -340       C  
ATOM   2713  CA BARG A 293      33.777   5.324  17.462  0.65 14.33           C  
ANISOU 2713  CA BARG A 293     1496   2200   1750   -101    418   -565       C  
ATOM   2714  C  AARG A 293      32.609   4.880  16.379  0.35 14.01           C  
ANISOU 2714  C  AARG A 293     1928   1914   1482   -361    458   -526       C  
ATOM   2715  C  BARG A 293      32.757   5.003  16.367  0.65 14.36           C  
ANISOU 2715  C  BARG A 293     1549   2471   1437   -586    655   -475       C  
ATOM   2716  O  AARG A 293      32.987   4.442  15.288  0.35 19.95           O  
ANISOU 2716  O  AARG A 293     2530   3558   1493  -1270    933   -926       O  
ATOM   2717  O  BARG A 293      33.061   4.300  15.410  0.65 17.46           O  
ANISOU 2717  O  BARG A 293     2423   2761   1449   -293    598   -542       O  
ATOM   2718  CB AARG A 293      33.975   3.690  18.072  0.35 16.04           C  
ANISOU 2718  CB AARG A 293     2657   2137   1300    739    654   -899       C  
ATOM   2719  CB BARG A 293      34.543   4.039  17.706  0.65 18.90           C  
ANISOU 2719  CB BARG A 293     2554   2691   1936    681    747   -376       C  
ATOM   2720  CG AARG A 293      34.798   3.917  19.356  0.35 20.63           C  
ANISOU 2720  CG AARG A 293     2704   2335   2798    388   -655   -199       C  
ATOM   2721  CG BARG A 293      34.915   3.548  19.028  0.65 22.46           C  
ANISOU 2721  CG BARG A 293     3963   2610   1962   1019    729   -452       C  
ATOM   2722  CD AARG A 293      36.173   4.409  18.911  0.35 26.15           C  
ANISOU 2722  CD AARG A 293     3148   3969   2818    -20    -98   -118       C  
ATOM   2723  CD BARG A 293      35.377   2.113  19.203  0.65 21.10           C  
ANISOU 2723  CD BARG A 293     3170   2605   2241    835    917   -139       C  
ATOM   2724  NE AARG A 293      36.693   3.486  17.903  0.35 33.62           N  
ANISOU 2724  NE AARG A 293     3385   5756   3632    823    -72   -933       N  
ATOM   2725  NE BARG A 293      36.215   2.058  20.416  0.65 18.50           N  
ANISOU 2725  NE BARG A 293     2727   1923   2379    113   1025   -357       N  
ATOM   2726  CZ AARG A 293      37.602   3.769  16.986  0.35 34.82           C  
ANISOU 2726  CZ AARG A 293     2206   7525   3498   1719   -493   -560       C  
ATOM   2727  CZ BARG A 293      36.906   1.047  20.807  0.65 16.83           C  
ANISOU 2727  CZ BARG A 293     1318   2478   2598    -43    569   -652       C  
ATOM   2728  NH1AARG A 293      37.951   2.807  16.144  0.35 43.56           N  
ANISOU 2728  NH1AARG A 293     2463   8764   5324   2594     85  -1525       N  
ATOM   2729  NH1BARG A 293      36.957  -0.098  20.071  0.65 19.65           N  
ANISOU 2729  NH1BARG A 293     2236   1935   3296    131    110   -557       N  
ATOM   2730  NH2AARG A 293      38.136   4.984  16.925  0.35 36.49           N  
ANISOU 2730  NH2AARG A 293     3888   7582   2393   1503    618    833       N  
ATOM   2731  NH2BARG A 293      37.586   1.110  21.919  0.65 22.31           N  
ANISOU 2731  NH2BARG A 293     1377   4268   2833   -754    314   -694       N  
ATOM   2732  N  AASN A 294      31.311   5.179  16.539  0.40 13.48           N  
ANISOU 2732  N  AASN A 294     1826   1754   1541   -396    161    -81       N  
ATOM   2733  N  BASN A 294      31.510   5.499  16.507  0.61 11.02           N  
ANISOU 2733  N  BASN A 294     1670   1317   1200   -477    194    182       N  
ATOM   2734  CA AASN A 294      30.332   4.848  15.486  0.40 15.16           C  
ANISOU 2734  CA AASN A 294     2264   2230   1267   -820    131    228       C  
ATOM   2735  CA BASN A 294      30.433   5.183  15.563  0.61 14.17           C  
ANISOU 2735  CA BASN A 294     2235   1756   1394   -392   -143     81       C  
ATOM   2736  C  AASN A 294      30.224   3.331  15.301  0.40 16.51           C  
ANISOU 2736  C  AASN A 294     2534   2280   1459   -784    -90   -145       C  
ATOM   2737  C  BASN A 294      30.332   3.666  15.335  0.61 13.76           C  
ANISOU 2737  C  BASN A 294     2076   1893   1258   -692    306   -258       C  
ATOM   2738  O  AASN A 294      30.029   2.816  14.183  0.40 21.30           O  
ANISOU 2738  O  AASN A 294     3774   3067   1253  -1247    719   -417       O  
ATOM   2739  O  BASN A 294      30.159   3.218  14.172  0.61 18.55           O  
ANISOU 2739  O  BASN A 294     2689   2754   1607   -242   -298   -686       O  
ATOM   2740  CB AASN A 294      30.677   5.543  14.164  0.40 19.68           C  
ANISOU 2740  CB AASN A 294     3280   2811   1389   -429    490    466       C  
ATOM   2741  CB BASN A 294      30.638   5.891  14.216  0.61 18.90           C  
ANISOU 2741  CB BASN A 294     3456   2240   1483   -419   -506    392       C  
ATOM   2742  CG AASN A 294      30.374   7.030  14.253  0.40 21.87           C  
ANISOU 2742  CG AASN A 294     3909   2749   1652   -345     74    757       C  
ATOM   2743  CG BASN A 294      30.746   7.389  14.486  0.61 20.76           C  
ANISOU 2743  CG BASN A 294     3906   2255   1728  -1152    -18    450       C  
ATOM   2744  OD1AASN A 294      29.565   7.460  15.081  0.40 27.52           O  
ANISOU 2744  OD1AASN A 294     4374   2622   3461   -259    901    240       O  
ATOM   2745  OD1BASN A 294      29.879   7.941  15.174  0.61 21.32           O  
ANISOU 2745  OD1BASN A 294     3454   2301   2344   -504   -836     -4       O  
ATOM   2746  ND2AASN A 294      31.025   7.791  13.406  0.40 28.06           N  
ANISOU 2746  ND2AASN A 294     3744   3113   3805  -1532    485    794       N  
ATOM   2747  ND2BASN A 294      31.799   7.953  13.983  0.61 29.11           N  
ANISOU 2747  ND2BASN A 294     4556   4414   2092  -2589    -12     81       N  
ATOM   2748  N  ATRP A 295      30.338   2.624  16.426  0.40 11.88           N  
ANISOU 2748  N  ATRP A 295     1613   1583   1317   -294    350   -470       N  
ATOM   2749  N  BTRP A 295      30.414   2.923  16.457  0.61 13.38           N  
ANISOU 2749  N  BTRP A 295     1938   1517   1627   -534    123   -107       N  
ATOM   2750  CA ATRP A 295      30.218   1.160  16.430  0.40 12.67           C  
ANISOU 2750  CA ATRP A 295     1657   1531   1626   -194    458   -818       C  
ATOM   2751  CA BTRP A 295      30.404   1.464  16.423  0.61 13.62           C  
ANISOU 2751  CA BTRP A 295     1601   1555   2018   -387    -28   -439       C  
ATOM   2752  C  ATRP A 295      28.798   0.751  16.835  0.40 11.92           C  
ANISOU 2752  C  ATRP A 295     1669   1519   1340   -154    373   -340       C  
ATOM   2753  C  BTRP A 295      29.013   0.957  16.788  0.61 10.46           C  
ANISOU 2753  C  BTRP A 295     1486   1042   1445    -39      5   -248       C  
ATOM   2754  O  ATRP A 295      28.355   1.137  17.931  0.40 12.25           O  
ANISOU 2754  O  ATRP A 295     2102   1039   1515   -468    733   -330       O  
ATOM   2755  O  BTRP A 295      28.609   1.019  17.968  0.61 13.35           O  
ANISOU 2755  O  BTRP A 295     1699   2071   1301    -37   -186   -311       O  
ATOM   2756  CB ATRP A 295      31.234   0.532  17.391  0.40 16.79           C  
ANISOU 2756  CB ATRP A 295     1783   1692   2906     43     64   -460       C  
ATOM   2757  CB BTRP A 295      31.437   0.891  17.412  0.61 17.08           C  
ANISOU 2757  CB BTRP A 295     1734   1773   2983    -20   -550   -601       C  
ATOM   2758  CG ATRP A 295      31.124  -0.955  17.561  0.40 17.71           C  
ANISOU 2758  CG ATRP A 295     1553   1736   3441     18    278   -417       C  
ATOM   2759  CG BTRP A 295      31.548  -0.590  17.268  0.61 19.11           C  
ANISOU 2759  CG BTRP A 295     2104   1858   3301    232   -224   -553       C  
ATOM   2760  CD1ATRP A 295      31.464  -1.940  16.680  0.40 22.26           C  
ANISOU 2760  CD1ATRP A 295     3082   1652   3724    131    433   -463       C  
ATOM   2761  CD1BTRP A 295      31.922  -1.332  16.195  0.61 24.48           C  
ANISOU 2761  CD1BTRP A 295     3831   1868   3602    316    -55   -715       C  
ATOM   2762  CD2ATRP A 295      30.631  -1.651  18.724  0.40 19.04           C  
ANISOU 2762  CD2ATRP A 295     1570   1985   3678    -92    218   -141       C  
ATOM   2763  CD2BTRP A 295      31.256  -1.504  18.331  0.61 19.72           C  
ANISOU 2763  CD2BTRP A 295     1537   2057   3898    -50    -80   -266       C  
ATOM   2764  NE1ATRP A 295      31.208  -3.174  17.206  0.40 26.03           N  
ANISOU 2764  NE1ATRP A 295     3773   1718   4400     69    665   -300       N  
ATOM   2765  NE1BTRP A 295      31.865  -2.656  16.550  0.61 25.37           N  
ANISOU 2765  NE1BTRP A 295     3528   1826   4284    314    -21   -506       N  
ATOM   2766  CE2ATRP A 295      30.695  -3.036  18.467  0.40 24.34           C  
ANISOU 2766  CE2ATRP A 295     2580   1883   4784    466    987    146       C  
ATOM   2767  CE2BTRP A 295      31.464  -2.806  17.855  0.61 25.03           C  
ANISOU 2767  CE2BTRP A 295     2768   1996   4745    334    306   -158       C  
ATOM   2768  CE3ATRP A 295      30.124  -1.251  19.964  0.40 19.16           C  
ANISOU 2768  CE3ATRP A 295     1956   2237   3088    405   -221    271       C  
ATOM   2769  CE3BTRP A 295      30.838  -1.336  19.646  0.61 22.35           C  
ANISOU 2769  CE3BTRP A 295     2616   2629   3249   -246   -729    -85       C  
ATOM   2770  CZ2ATRP A 295      30.301  -4.041  19.359  0.40 26.51           C  
ANISOU 2770  CZ2ATRP A 295     2884   2125   5062    138    758    349       C  
ATOM   2771  CZ2BTRP A 295      31.279  -3.976  18.596  0.61 27.29           C  
ANISOU 2771  CZ2BTRP A 295     2826   2228   5316    372    752    147       C  
ATOM   2772  CZ3ATRP A 295      29.725  -2.228  20.870  0.40 23.38           C  
ANISOU 2772  CZ3ATRP A 295     3201   2509   3174   -465   -414    291       C  
ATOM   2773  CZ3BTRP A 295      30.668  -2.504  20.363  0.61 25.19           C  
ANISOU 2773  CZ3BTRP A 295     3362   2610   3600   -221   -893    109       C  
ATOM   2774  CH2ATRP A 295      29.814  -3.603  20.567  0.40 27.90           C  
ANISOU 2774  CH2ATRP A 295     4074   2437   4088    -10     70    563       C  
ATOM   2775  CH2BTRP A 295      30.873  -3.811  19.898  0.61 28.22           C  
ANISOU 2775  CH2BTRP A 295     2882   2707   5135    112    580    115       C  
ATOM   2776  N  AARG A 296      28.082   0.020  16.006  0.40 13.10           N  
ANISOU 2776  N  AARG A 296     1538   1718   1722   -134    437   -661       N  
ATOM   2777  N  BARG A 296      28.287   0.483  15.786  0.61 12.28           N  
ANISOU 2777  N  BARG A 296     1362   1915   1387   -222     89   -384       N  
ATOM   2778  CA AARG A 296      26.712  -0.408  16.252  0.40 11.54           C  
ANISOU 2778  CA AARG A 296     1387   1507   1491    119    198   -237       C  
ATOM   2779  CA BARG A 296      26.894   0.072  15.917  0.61 10.68           C  
ANISOU 2779  CA BARG A 296     1445   1327   1287    -97    -32   -318       C  
ATOM   2780  C  AARG A 296      26.669  -1.914  16.509  0.40 11.25           C  
ANISOU 2780  C  AARG A 296     1394   1414   1465    137    -22   -518       C  
ATOM   2781  C  BARG A 296      26.773  -1.441  15.972  0.61 10.93           C  
ANISOU 2781  C  BARG A 296     1518   1279   1358     69    132   -331       C  
ATOM   2782  O  AARG A 296      27.227  -2.700  15.744  0.40 16.99           O  
ANISOU 2782  O  AARG A 296     2362   1971   2124   1012    318   -563       O  
ATOM   2783  O  BARG A 296      27.264  -2.129  15.069  0.61 13.22           O  
ANISOU 2783  O  BARG A 296     1934   1620   1470    327    209   -521       O  
ATOM   2784  CB AARG A 296      25.758  -0.121  15.082  0.40 15.06           C  
ANISOU 2784  CB AARG A 296     1959   2036   1726     -4   -118    128       C  
ATOM   2785  CB BARG A 296      26.133   0.703  14.731  0.61 11.71           C  
ANISOU 2785  CB BARG A 296     1330   1612   1506   -174    163    168       C  
ATOM   2786  CG AARG A 296      25.363   1.329  14.879  0.40 16.16           C  
ANISOU 2786  CG AARG A 296     1822   2235   2082    422   -184     79       C  
ATOM   2787  CG BARG A 296      24.669   0.315  14.759  0.61 10.55           C  
ANISOU 2787  CG BARG A 296     1303   1315   1391   -149     46    -15       C  
ATOM   2788  CD AARG A 296      24.399   1.383  13.679  0.40 12.78           C  
ANISOU 2788  CD AARG A 296     1767   1626   1464    113    225    -35       C  
ATOM   2789  CD BARG A 296      23.900   0.800  13.526  0.61 11.60           C  
ANISOU 2789  CD BARG A 296     1822   1347   1240   -163   -207   -125       C  
ATOM   2790  NE AARG A 296      24.291   2.796  13.293  0.40 12.78           N  
ANISOU 2790  NE AARG A 296     1706   1661   1491     12    215     44       N  
ATOM   2791  NE BARG A 296      24.078   2.233  13.262  0.61 12.06           N  
ANISOU 2791  NE BARG A 296     1698   1433   1453    -59    -12     47       N  
ATOM   2792  CZ AARG A 296      23.425   3.630  13.862  0.40 12.24           C  
ANISOU 2792  CZ AARG A 296     1298   1449   1903    -61    192    317       C  
ATOM   2793  CZ BARG A 296      23.400   3.197  13.840  0.61 11.75           C  
ANISOU 2793  CZ BARG A 296     1715   1343   1404    -80    -86     95       C  
ATOM   2794  NH1AARG A 296      22.619   3.215  14.835  0.40 11.90           N  
ANISOU 2794  NH1AARG A 296     1715   1644   1164    192    145    204       N  
ATOM   2795  NH1BARG A 296      22.495   2.932  14.773  0.61 11.84           N  
ANISOU 2795  NH1BARG A 296     1301   1783   1414    -75   -181   -107       N  
ATOM   2796  NH2AARG A 296      23.388   4.897  13.448  0.40 15.46           N  
ANISOU 2796  NH2AARG A 296     1741   1479   2656   -169     34    594       N  
ATOM   2797  NH2BARG A 296      23.665   4.466  13.472  0.61 17.16           N  
ANISOU 2797  NH2BARG A 296     2719   1337   2464    -98      2    341       N  
ATOM   2798  N  AVAL A 297      25.992  -2.341  17.546  0.40 11.82           N  
ANISOU 2798  N  AVAL A 297     1619   1447   1427    228   -186   -119       N  
ATOM   2799  N  BVAL A 297      26.133  -1.994  16.996  0.61  9.91           N  
ANISOU 2799  N  BVAL A 297     1231   1159   1377    131     73   -304       N  
ATOM   2800  CA AVAL A 297      25.590  -3.683  17.855  0.40 12.96           C  
ANISOU 2800  CA AVAL A 297     2001   1265   1659    374   -319    -80       C  
ATOM   2801  CA BVAL A 297      26.008  -3.448  17.158  0.61 10.76           C  
ANISOU 2801  CA BVAL A 297     1538   1055   1496    305   -128   -259       C  
ATOM   2802  C  AVAL A 297      24.490  -4.194  16.932  0.40 12.46           C  
ANISOU 2802  C  AVAL A 297     2264   1141   1329    214   -234   -126       C  
ATOM   2803  C  BVAL A 297      24.670  -3.961  16.611  0.61  9.68           C  
ANISOU 2803  C  BVAL A 297     1506    762   1411    224     -9     -5       C  
ATOM   2804  O  AVAL A 297      24.511  -5.350  16.553  0.40 15.15           O  
ANISOU 2804  O  AVAL A 297     2238   1175   2344    119      3   -291       O  
ATOM   2805  O  BVAL A 297      24.666  -5.114  16.157  0.61 12.38           O  
ANISOU 2805  O  BVAL A 297     1770    961   1974    255     28   -325       O  
ATOM   2806  CB AVAL A 297      24.964  -3.803  19.274  0.40 16.73           C  
ANISOU 2806  CB AVAL A 297     3079   1985   1292   -257   -610    304       C  
ATOM   2807  CB BVAL A 297      26.261  -3.975  18.601  0.61 14.79           C  
ANISOU 2807  CB BVAL A 297     1867   1612   2140    330   -635    281       C  
ATOM   2808  CG1AVAL A 297      24.333  -5.179  19.462  0.40 18.68           C  
ANISOU 2808  CG1AVAL A 297     3314   2074   1708   -429    -42   -112       C  
ATOM   2809  CG1BVAL A 297      27.628  -3.449  19.099  0.61 19.82           C  
ANISOU 2809  CG1BVAL A 297     2364   2387   2780    -61  -1287    583       C  
ATOM   2810  CG2AVAL A 297      25.991  -3.526  20.345  0.40 20.45           C  
ANISOU 2810  CG2AVAL A 297     3429   2454   1887    -24   -988   -381       C  
ATOM   2811  CG2BVAL A 297      25.169  -3.633  19.599  0.61 16.55           C  
ANISOU 2811  CG2BVAL A 297     2921   1927   1440   -330   -186    206       C  
ATOM   2812  N  ACYS A 298      23.623  -3.211  16.679  0.40 11.67           N  
ANISOU 2812  N  ACYS A 298     1855   1137   1442     -4   -419   -221       N  
ATOM   2813  N  BCYS A 298      23.567  -3.192  16.561  0.61  8.66           N  
ANISOU 2813  N  BCYS A 298     1328   1050    912    252     87   -127       N  
ATOM   2814  CA ACYS A 298      22.338  -3.499  16.083  0.40 11.75           C  
ANISOU 2814  CA ACYS A 298     1834   1243   1388   -244   -163   -288       C  
ATOM   2815  CA BCYS A 298      22.300  -3.756  16.025  0.61  8.79           C  
ANISOU 2815  CA BCYS A 298     1261   1019   1061     66    375    -43       C  
ATOM   2816  C  ACYS A 298      22.163  -3.021  14.669  0.40 12.21           C  
ANISOU 2816  C  ACYS A 298     1658   1470   1510    -27   -405   -206       C  
ATOM   2817  C  BCYS A 298      22.037  -3.168  14.656  0.61  8.64           C  
ANISOU 2817  C  BCYS A 298     1323    944   1016     43     98   -308       C  
ATOM   2818  O  ACYS A 298      21.967  -1.825  14.423  0.40 18.04           O  
ANISOU 2818  O  ACYS A 298     2870   1807   2176    846   -152    167       O  
ATOM   2819  O  BCYS A 298      21.516  -2.025  14.523  0.61  9.33           O  
ANISOU 2819  O  BCYS A 298     1539   1132    875    230    -36   -215       O  
ATOM   2820  CB ACYS A 298      21.272  -2.804  16.985  0.40 15.87           C  
ANISOU 2820  CB ACYS A 298     2037   2063   1931     54    329     34       C  
ATOM   2821  CB BCYS A 298      21.115  -3.401  16.952  0.61  9.40           C  
ANISOU 2821  CB BCYS A 298     1538    663   1371    -80    656     44       C  
ATOM   2822  SG ACYS A 298      20.486  -4.195  17.797  0.40 26.91           S  
ANISOU 2822  SG ACYS A 298     3792   1694   4738   -626   2496   -882       S  
ATOM   2823  SG BCYS A 298      21.112  -4.324  18.481  0.61 11.28           S  
ANISOU 2823  SG BCYS A 298     1918   1157   1210    128    531    134       S  
ATOM   2824  N  AALA A 299      22.223  -4.002  13.794  0.40 12.59           N  
ANISOU 2824  N  AALA A 299     1690   1827   1264   -554     54   -269       N  
ATOM   2825  N  BALA A 299      22.413  -3.873  13.604  0.61 10.98           N  
ANISOU 2825  N  BALA A 299     1638   1518   1015    327    122   -386       N  
ATOM   2826  CA AALA A 299      21.906  -3.831  12.391  0.40 11.71           C  
ANISOU 2826  CA AALA A 299     1916   1203   1332     76     97    -59       C  
ATOM   2827  CA BALA A 299      22.200  -3.514  12.188  0.61 13.11           C  
ANISOU 2827  CA BALA A 299     1964   1951   1065    551   -228   -329       C  
ATOM   2828  C  AALA A 299      21.968  -5.208  11.742  0.40 10.33           C  
ANISOU 2828  C  AALA A 299     1740   1130   1053   -190    336     37       C  
ATOM   2829  C  BALA A 299      22.406  -4.675  11.235  0.61 14.42           C  
ANISOU 2829  C  BALA A 299     1873   2363   1241    761   -244   -754       C  
ATOM   2830  O  AALA A 299      22.516  -6.151  12.250  0.40 12.11           O  
ANISOU 2830  O  AALA A 299     2575   1078    950     39   -103   -385       O  
ATOM   2831  O  BALA A 299      23.561  -4.998  10.918  0.61 28.85           O  
ANISOU 2831  O  BALA A 299     1823   4132   5009    502     21  -2916       O  
ATOM   2832  CB AALA A 299      22.882  -2.931  11.682  0.40 14.11           C  
ANISOU 2832  CB AALA A 299     2765   1241   1356   -506    363   -402       C  
ATOM   2833  CB BALA A 299      23.175  -2.389  11.864  0.61 17.51           C  
ANISOU 2833  CB BALA A 299     3282   1875   1497    361    365    133       C  
ATOM   2834  N   LEU A 300      21.468  -5.293  10.568  1.00 14.39           N  
ANISOU 2834  N   LEU A 300     2002   1914   1552    262   -234   -345       N  
ATOM   2835  CA  LEU A 300      21.538  -6.562   9.826  1.00 14.29           C  
ANISOU 2835  CA  LEU A 300     2206   1712   1513     95     48   -290       C  
ATOM   2836  C   LEU A 300      21.791  -6.287   8.364  1.00 15.41           C  
ANISOU 2836  C   LEU A 300     2006   2419   1431    302   -139   -255       C  
ATOM   2837  O   LEU A 300      21.075  -5.511   7.726  1.00 16.47           O  
ANISOU 2837  O   LEU A 300     2506   2260   1490    436     -8   -263       O  
ATOM   2838  CB  LEU A 300      20.178  -7.196   9.965  1.00 19.70           C  
ANISOU 2838  CB  LEU A 300     2649   2249   2588   -612   -344    633       C  
ATOM   2839  CG ALEU A 300      19.988  -8.108  11.154  0.43 14.62           C  
ANISOU 2839  CG ALEU A 300     2121   2095   1338    153    182   -224       C  
ATOM   2840  CG BLEU A 300      19.816  -8.636   9.747  0.57 20.28           C  
ANISOU 2840  CG BLEU A 300     2505   2275   2924   -316    485   -150       C  
ATOM   2841  CD1ALEU A 300      18.589  -8.750  11.067  0.43 17.58           C  
ANISOU 2841  CD1ALEU A 300     2311   3217   1151   -465    388     54       C  
ATOM   2842  CD1BLEU A 300      20.812  -9.584  10.439  0.57 26.40           C  
ANISOU 2842  CD1BLEU A 300     2647   2198   5184   -318    347    609       C  
ATOM   2843  CD2ALEU A 300      21.006  -9.218  11.364  0.43 16.94           C  
ANISOU 2843  CD2ALEU A 300     2461   1681   2295    202   1090    247       C  
ATOM   2844  CD2BLEU A 300      18.399  -8.941  10.223  0.57 19.37           C  
ANISOU 2844  CD2BLEU A 300     2502   2764   2094   -717    -71    953       C  
ATOM   2845  N   LEU A 301      22.746  -7.015   7.803  1.00 16.54           N  
ANISOU 2845  N   LEU A 301     2233   2402   1647    328     62   -341       N  
ATOM   2846  CA  LEU A 301      23.075  -6.858   6.401  1.00 18.03           C  
ANISOU 2846  CA  LEU A 301     2177   2984   1689    527    104   -234       C  
ATOM   2847  C   LEU A 301      21.914  -7.180   5.491  1.00 15.59           C  
ANISOU 2847  C   LEU A 301     2091   2379   1454    569    297   -200       C  
ATOM   2848  O   LEU A 301      21.785  -6.546   4.418  1.00 17.11           O  
ANISOU 2848  O   LEU A 301     2361   2570   1570    498    300     47       O  
ATOM   2849  CB  LEU A 301      24.256  -7.814   6.048  1.00 22.50           C  
ANISOU 2849  CB  LEU A 301     2296   3720   2532   1082    265   -379       C  
ATOM   2850  CG  LEU A 301      24.749  -7.791   4.615  1.00 32.39           C  
ANISOU 2850  CG  LEU A 301     3609   5751   2947   1895   1031    -42       C  
ATOM   2851  CD1 LEU A 301      25.135  -6.403   4.141  1.00 57.60           C  
ANISOU 2851  CD1 LEU A 301     7125   7776   6983   2125   2759   3779       C  
ATOM   2852  CD2 LEU A 301      25.914  -8.794   4.517  1.00 48.11           C  
ANISOU 2852  CD2 LEU A 301     4167   6743   7368   2367   2729  -1044       C  
ATOM   2853  N   SER A 302      21.107  -8.178   5.841  1.00 15.52           N  
ANISOU 2853  N   SER A 302     2213   2327   1359    499    314   -248       N  
ATOM   2854  CA  SER A 302      20.004  -8.592   4.970  1.00 15.10           C  
ANISOU 2854  CA  SER A 302     2269   2056   1414    544    283   -376       C  
ATOM   2855  C   SER A 302      18.963  -7.479   4.768  1.00 13.36           C  
ANISOU 2855  C   SER A 302     2191   1809   1076    369    231   -155       C  
ATOM   2856  O   SER A 302      18.104  -7.619   3.912  1.00 16.71           O  
ANISOU 2856  O   SER A 302     2723   2214   1413    474   -121   -236       O  
ATOM   2857  CB  SER A 302      19.320  -9.820   5.586  1.00 16.37           C  
ANISOU 2857  CB  SER A 302     2800   1751   1668    497    188   -301       C  
ATOM   2858  OG  SER A 302      18.825  -9.448   6.886  1.00 19.09           O  
ANISOU 2858  OG  SER A 302     3580   2134   1541    194    431    -22       O  
ATOM   2859  N   CYS A 303      18.971  -6.418   5.607  1.00 14.08           N  
ANISOU 2859  N   CYS A 303     2100   1838   1410    351    293   -168       N  
ATOM   2860  CA  CYS A 303      17.993  -5.339   5.534  1.00 13.55           C  
ANISOU 2860  CA  CYS A 303     1929   1789   1429    361    327   -211       C  
ATOM   2861  C   CYS A 303      18.525  -4.080   4.862  1.00 13.31           C  
ANISOU 2861  C   CYS A 303     1945   1822   1291    154    217   -231       C  
ATOM   2862  O   CYS A 303      17.769  -3.083   4.704  1.00 14.10           O  
ANISOU 2862  O   CYS A 303     2030   1929   1399    230     29   -181       O  
ATOM   2863  CB  CYS A 303      17.548  -4.978   6.974  1.00 15.02           C  
ANISOU 2863  CB  CYS A 303     2382   1895   1431    178    467   -149       C  
ATOM   2864  SG  CYS A 303      16.672  -6.338   7.773  1.00 18.38           S  
ANISOU 2864  SG  CYS A 303     2772   2189   2022    262    952    -51       S  
ATOM   2865  N   THR A 304      19.792  -4.083   4.408  1.00 14.17           N  
ANISOU 2865  N   THR A 304     1975   1878   1531    122    203   -261       N  
ATOM   2866  CA  THR A 304      20.375  -2.828   3.919  1.00 14.22           C  
ANISOU 2866  CA  THR A 304     2035   1911   1455   -154    101   -361       C  
ATOM   2867  C   THR A 304      19.861  -2.376   2.593  1.00 15.10           C  
ANISOU 2867  C   THR A 304     2212   2246   1280   -236     63   -283       C  
ATOM   2868  O   THR A 304      20.112  -1.197   2.272  1.00 19.87           O  
ANISOU 2868  O   THR A 304     3433   2381   1736   -493   -233    -54       O  
ATOM   2869  CB  THR A 304      21.913  -2.939   3.845  1.00 17.61           C  
ANISOU 2869  CB  THR A 304     2070   2854   1768     58    148   -192       C  
ATOM   2870  OG1 THR A 304      22.254  -4.061   3.003  1.00 20.03           O  
ANISOU 2870  OG1 THR A 304     2217   3220   2175     22    542   -450       O  
ATOM   2871  CG2 THR A 304      22.534  -3.129   5.240  1.00 17.78           C  
ANISOU 2871  CG2 THR A 304     2061   2775   1919    178     50     -8       C  
ATOM   2872  N   SER A 305      19.119  -3.150   1.814  1.00 15.92           N  
ANISOU 2872  N   SER A 305     2042   2656   1350   -153    234   -542       N  
ATOM   2873  CA  SER A 305      18.554  -2.642   0.544  1.00 18.40           C  
ANISOU 2873  CA  SER A 305     2196   3766   1029   -313    175   -484       C  
ATOM   2874  C   SER A 305      17.096  -2.226   0.729  1.00 16.18           C  
ANISOU 2874  C   SER A 305     2125   3007   1015   -357    195   -183       C  
ATOM   2875  O   SER A 305      16.470  -1.819  -0.242  1.00 22.76           O  
ANISOU 2875  O   SER A 305     2632   5117    897    172    319    288       O  
ATOM   2876  CB  SER A 305      18.637  -3.682  -0.555  1.00 20.65           C  
ANISOU 2876  CB  SER A 305     2736   3683   1427    107    336   -621       C  
ATOM   2877  OG  SER A 305      19.940  -3.785  -1.027  1.00 28.53           O  
ANISOU 2877  OG  SER A 305     2816   5431   2592    737    366  -1150       O  
ATOM   2878  N   HIS A 306      16.548  -2.345   1.951  1.00 15.05           N  
ANISOU 2878  N   HIS A 306     2270   2543    907     39    287   -158       N  
ATOM   2879  CA  HIS A 306      15.175  -1.922   2.159  1.00 14.74           C  
ANISOU 2879  CA  HIS A 306     2305   2304    990     50    269    219       C  
ATOM   2880  C   HIS A 306      15.094  -0.401   1.979  1.00 14.16           C  
ANISOU 2880  C   HIS A 306     2243   2333    805    -70    181     58       C  
ATOM   2881  O   HIS A 306      16.008   0.286   2.488  1.00 14.63           O  
ANISOU 2881  O   HIS A 306     2171   2416    973   -106    215    -29       O  
ATOM   2882  CB  HIS A 306      14.734  -2.394   3.578  1.00 14.54           C  
ANISOU 2882  CB  HIS A 306     2143   2522    859    190    280    245       C  
ATOM   2883  CG  HIS A 306      13.251  -2.204   3.814  1.00 12.96           C  
ANISOU 2883  CG  HIS A 306     2222   1985    715     15    211     40       C  
ATOM   2884  ND1 HIS A 306      12.604  -0.954   3.833  1.00 12.60           N  
ANISOU 2884  ND1 HIS A 306     2054   1844    890    -64     70    154       N  
ATOM   2885  CD2 HIS A 306      12.324  -3.176   4.056  1.00 13.84           C  
ANISOU 2885  CD2 HIS A 306     2394   1937    926    -73    243    173       C  
ATOM   2886  CE1 HIS A 306      11.332  -1.198   4.044  1.00 12.79           C  
ANISOU 2886  CE1 HIS A 306     2084   1871    904   -296    183    137       C  
ATOM   2887  NE2 HIS A 306      11.127  -2.508   4.193  1.00 12.92           N  
ANISOU 2887  NE2 HIS A 306     2288   1759    860   -129    108    -43       N  
ATOM   2888  N   LYS A 307      14.053   0.126   1.311  1.00 15.16           N  
ANISOU 2888  N   LYS A 307     2536   2461    765    -28      8    320       N  
ATOM   2889  CA  LYS A 307      13.916   1.530   1.095  1.00 17.82           C  
ANISOU 2889  CA  LYS A 307     3414   2485    871     27    -65    560       C  
ATOM   2890  C   LYS A 307      13.969   2.338   2.399  1.00 14.88           C  
ANISOU 2890  C   LYS A 307     2424   2224   1006   -124     15    546       C  
ATOM   2891  O   LYS A 307      14.422   3.526   2.378  1.00 18.66           O  
ANISOU 2891  O   LYS A 307     3380   2289   1422   -378    175    661       O  
ATOM   2892  CB  LYS A 307      12.603   1.850   0.361  1.00 20.62           C  
ANISOU 2892  CB  LYS A 307     3692   2936   1208     12   -605    645       C  
ATOM   2893  CG  LYS A 307      11.307   1.683   1.159  1.00 29.99           C  
ANISOU 2893  CG  LYS A 307     3399   5923   2072   -555   -791   1175       C  
ATOM   2894  CD  LYS A 307      10.101   1.802   0.198  1.00 39.15           C  
ANISOU 2894  CD  LYS A 307     3703   7715   3458    550  -1273   1803       C  
ATOM   2895  CE  LYS A 307       9.158   2.657   1.044  1.00 43.17           C  
ANISOU 2895  CE  LYS A 307     4535   6812   5056    929    243   3099       C  
ATOM   2896  NZ  LYS A 307       8.344   1.792   1.926  1.00 32.66           N  
ANISOU 2896  NZ  LYS A 307     3680   5381   3346   -613  -1302   1318       N  
ATOM   2897  N   ASP A 308      13.556   1.779   3.507  1.00 13.24           N  
ANISOU 2897  N   ASP A 308     2213   1921    899     70     26    431       N  
ATOM   2898  CA  ASP A 308      13.433   2.507   4.778  1.00 12.87           C  
ANISOU 2898  CA  ASP A 308     2082   1767   1041    100      4    343       C  
ATOM   2899  C   ASP A 308      14.529   2.077   5.779  1.00 11.12           C  
ANISOU 2899  C   ASP A 308     1916   1374    933     42    148    166       C  
ATOM   2900  O   ASP A 308      14.455   2.352   6.948  1.00 11.63           O  
ANISOU 2900  O   ASP A 308     1995   1437    985     81    145    104       O  
ATOM   2901  CB  ASP A 308      12.034   2.314   5.371  1.00 13.40           C  
ANISOU 2901  CB  ASP A 308     1918   1914   1258    188     94    385       C  
ATOM   2902  CG  ASP A 308      10.956   2.879   4.434  1.00 18.11           C  
ANISOU 2902  CG  ASP A 308     2359   2542   1982     17   -577    555       C  
ATOM   2903  OD1 ASP A 308      11.166   3.995   3.888  1.00 23.84           O  
ANISOU 2903  OD1 ASP A 308     3888   2157   3015    186  -1282    763       O  
ATOM   2904  OD2 ASP A 308       9.915   2.194   4.228  1.00 20.91           O  
ANISOU 2904  OD2 ASP A 308     1832   3798   2313   -129   -134    786       O  
ATOM   2905  N   TYR A 309      15.568   1.375   5.290  1.00 11.50           N  
ANISOU 2905  N   TYR A 309     1814   1582    972    -34     81    115       N  
ATOM   2906  CA  TYR A 309      16.683   1.051   6.172  1.00 11.13           C  
ANISOU 2906  CA  TYR A 309     1709   1533    986    -93     87    -69       C  
ATOM   2907  C   TYR A 309      17.216   2.323   6.813  1.00 11.16           C  
ANISOU 2907  C   TYR A 309     1836   1501    905   -169    169    176       C  
ATOM   2908  O   TYR A 309      17.484   3.292   6.091  1.00 13.20           O  
ANISOU 2908  O   TYR A 309     2217   1703   1097   -320    153    301       O  
ATOM   2909  CB  TYR A 309      17.813   0.416   5.343  1.00 12.82           C  
ANISOU 2909  CB  TYR A 309     1862   2060    950    143    164    -30       C  
ATOM   2910  CG  TYR A 309      18.969   0.003   6.193  1.00 11.82           C  
ANISOU 2910  CG  TYR A 309     1752   1783    955     91    265   -102       C  
ATOM   2911  CD1 TYR A 309      18.946  -1.092   7.064  1.00 13.50           C  
ANISOU 2911  CD1 TYR A 309     2261   1935    933    208    279     63       C  
ATOM   2912  CD2 TYR A 309      20.183   0.720   6.116  1.00 13.17           C  
ANISOU 2912  CD2 TYR A 309     1882   1898   1225    -41    137   -206       C  
ATOM   2913  CE1 TYR A 309      20.069  -1.425   7.811  1.00 15.01           C  
ANISOU 2913  CE1 TYR A 309     2397   2227   1079    265    203     49       C  
ATOM   2914  CE2 TYR A 309      21.317   0.361   6.845  1.00 15.09           C  
ANISOU 2914  CE2 TYR A 309     1928   2499   1306   -133    102   -185       C  
ATOM   2915  CZ  TYR A 309      21.226  -0.724   7.693  1.00 15.93           C  
ANISOU 2915  CZ  TYR A 309     2194   2445   1414    437     25   -122       C  
ATOM   2916  OH  TYR A 309      22.321  -1.121   8.461  1.00 20.75           O  
ANISOU 2916  OH  TYR A 309     2461   3755   1666    830   -230   -143       O  
ATOM   2917  N   PRO A 310      17.385   2.385   8.150  1.00 10.02           N  
ANISOU 2917  N   PRO A 310     1615   1302    891     16     69    121       N  
ATOM   2918  CA  PRO A 310      17.601   3.670   8.790  1.00 10.21           C  
ANISOU 2918  CA  PRO A 310     1535   1342   1002    -32    147    141       C  
ATOM   2919  C   PRO A 310      19.040   4.184   8.817  1.00 10.59           C  
ANISOU 2919  C   PRO A 310     1625   1310   1089    -35    228    104       C  
ATOM   2920  O   PRO A 310      19.237   5.356   9.132  1.00 12.60           O  
ANISOU 2920  O   PRO A 310     1687   1468   1634   -141    157     22       O  
ATOM   2921  CB  PRO A 310      17.059   3.503  10.237  1.00 10.82           C  
ANISOU 2921  CB  PRO A 310     1682   1426   1002   -121    282      4       C  
ATOM   2922  CG  PRO A 310      17.256   1.997  10.469  1.00 11.39           C  
ANISOU 2922  CG  PRO A 310     1941   1521    865   -129    107    147       C  
ATOM   2923  CD  PRO A 310      16.934   1.352   9.113  1.00 10.44           C  
ANISOU 2923  CD  PRO A 310     1808   1363    796   -171    231    156       C  
ATOM   2924  N   PHE A 311      20.025   3.324   8.585  1.00 10.84           N  
ANISOU 2924  N   PHE A 311     1496   1525   1098     32    302    183       N  
ATOM   2925  CA  PHE A 311      21.393   3.673   8.942  1.00 12.00           C  
ANISOU 2925  CA  PHE A 311     1602   1667   1289   -197    215    285       C  
ATOM   2926  C   PHE A 311      22.284   4.037   7.747  1.00 13.49           C  
ANISOU 2926  C   PHE A 311     1612   2035   1480    -45    419    198       C  
ATOM   2927  O   PHE A 311      23.496   4.114   7.961  1.00 19.89           O  
ANISOU 2927  O   PHE A 311     1588   3396   2572   -296    376    987       O  
ATOM   2928  CB  PHE A 311      22.034   2.536   9.768  1.00 13.02           C  
ANISOU 2928  CB  PHE A 311     1547   1970   1431     -8    245    357       C  
ATOM   2929  CG  PHE A 311      21.203   2.134  10.983  1.00 11.74           C  
ANISOU 2929  CG  PHE A 311     1455   1877   1129   -103     14    270       C  
ATOM   2930  CD1 PHE A 311      20.553   3.091  11.789  1.00 12.84           C  
ANISOU 2930  CD1 PHE A 311     1732   2039   1106   -131     46    -43       C  
ATOM   2931  CD2 PHE A 311      21.087   0.794  11.313  1.00 13.05           C  
ANISOU 2931  CD2 PHE A 311     1631   1880   1448    -20     -2    418       C  
ATOM   2932  CE1 PHE A 311      19.805   2.665  12.915  1.00 13.06           C  
ANISOU 2932  CE1 PHE A 311     1944   1945   1075   -374    -49     32       C  
ATOM   2933  CE2 PHE A 311      20.326   0.379  12.415  1.00 12.58           C  
ANISOU 2933  CE2 PHE A 311     1433   1939   1408     52     72    368       C  
ATOM   2934  CZ  PHE A 311      19.696   1.329  13.213  1.00 12.40           C  
ANISOU 2934  CZ  PHE A 311     1661   1956   1095   -151   -218    158       C  
ATOM   2935  N   HIS A 312      21.738   4.323   6.587  1.00 14.41           N  
ANISOU 2935  N   HIS A 312     2145   1965   1365   -248    445    286       N  
ATOM   2936  CA  HIS A 312      22.566   4.937   5.554  1.00 16.95           C  
ANISOU 2936  CA  HIS A 312     2612   2278   1550   -333    758    190       C  
ATOM   2937  C   HIS A 312      22.776   6.442   5.865  1.00 19.36           C  
ANISOU 2937  C   HIS A 312     2996   2288   2070   -731   1258    115       C  
ATOM   2938  O   HIS A 312      23.822   6.963   5.520  1.00 23.23           O  
ANISOU 2938  O   HIS A 312     2874   3060   2892   -855    933    537       O  
ATOM   2939  CB  HIS A 312      21.921   4.809   4.165  1.00 21.66           C  
ANISOU 2939  CB  HIS A 312     3456   3335   1440  -1084    753    250       C  
ATOM   2940  CG  HIS A 312      21.744   3.409   3.695  1.00 24.80           C  
ANISOU 2940  CG  HIS A 312     4422   3514   1487  -1618   1059     -6       C  
ATOM   2941  ND1 HIS A 312      22.760   2.493   3.765  1.00 31.01           N  
ANISOU 2941  ND1 HIS A 312     4939   3458   3383  -1245   1899   -660       N  
ATOM   2942  CD2 HIS A 312      20.672   2.794   3.123  1.00 30.63           C  
ANISOU 2942  CD2 HIS A 312     5333   4674   1631  -2369    995   -505       C  
ATOM   2943  CE1 HIS A 312      22.295   1.344   3.271  1.00 36.76           C  
ANISOU 2943  CE1 HIS A 312     6860   3998   3110  -1593   2350  -1353       C  
ATOM   2944  NE2 HIS A 312      21.039   1.490   2.876  1.00 35.44           N  
ANISOU 2944  NE2 HIS A 312     7172   4525   1770  -2790   1674   -891       N  
ATOM   2945  N   GLU A 313      21.761   7.094   6.377  1.00 17.70           N  
ANISOU 2945  N   GLU A 313     2778   1980   1968   -400    569    278       N  
ATOM   2946  CA  GLU A 313      21.824   8.515   6.663  1.00 17.60           C  
ANISOU 2946  CA  GLU A 313     2640   2225   1824   -468    479    176       C  
ATOM   2947  C   GLU A 313      22.838   8.738   7.775  1.00 18.49           C  
ANISOU 2947  C   GLU A 313     2722   2512   1789   -632    606    164       C  
ATOM   2948  O   GLU A 313      23.032   7.914   8.673  1.00 19.95           O  
ANISOU 2948  O   GLU A 313     2346   3058   2178     49    486    475       O  
ATOM   2949  CB  GLU A 313      20.444   9.040   7.075  1.00 22.13           C  
ANISOU 2949  CB  GLU A 313     3006   2558   2845    389    555    734       C  
ATOM   2950  CG  GLU A 313      19.455   9.106   5.933  1.00 31.75           C  
ANISOU 2950  CG  GLU A 313     3602   4210   4253    650   -410   1718       C  
ATOM   2951  CD  GLU A 313      19.893  10.143   4.912  1.00 35.94           C  
ANISOU 2951  CD  GLU A 313     3951   5097   4607    456   -741   2486       C  
ATOM   2952  OE1 GLU A 313      20.508  11.150   5.286  1.00 34.92           O  
ANISOU 2952  OE1 GLU A 313     3963   5025   4280    363    514   2084       O  
ATOM   2953  OE2 GLU A 313      19.651   9.896   3.732  1.00 42.89           O  
ANISOU 2953  OE2 GLU A 313     6066   5686   4545   -343   -416   2289       O  
ATOM   2954  N   GLU A 314      23.475   9.893   7.813  1.00 20.95           N  
ANISOU 2954  N   GLU A 314     2172   2835   2953   -897    885   -277       N  
ATOM   2955  CA  GLU A 314      24.411  10.189   8.882  1.00 21.91           C  
ANISOU 2955  CA  GLU A 314     2451   2954   2919   -888    858   -284       C  
ATOM   2956  C   GLU A 314      23.794  10.090  10.264  1.00 20.73           C  
ANISOU 2956  C   GLU A 314     1674   3344   2857   -273    456    640       C  
ATOM   2957  O   GLU A 314      24.382   9.598  11.216  1.00 23.07           O  
ANISOU 2957  O   GLU A 314     1837   4001   2926    171    -77    -55       O  
ATOM   2958  CB  GLU A 314      25.011  11.603   8.736  1.00 25.96           C  
ANISOU 2958  CB  GLU A 314     3162   3323   3378  -1664   1061   -366       C  
ATOM   2959  CG  GLU A 314      26.083  11.791   9.840  0.72 34.04           C  
ANISOU 2959  CG  GLU A 314     3626   5015   4291  -2679    419    195       C  
ATOM   2960  CD  GLU A 314      26.502  13.231   9.984  0.72 40.23           C  
ANISOU 2960  CD  GLU A 314     5070   5432   4784  -3478   -670    302       C  
ATOM   2961  OE1 GLU A 314      26.245  14.006   9.043  0.72 54.22           O  
ANISOU 2961  OE1 GLU A 314     9432   6121   5049  -5537   -951   1416       O  
ATOM   2962  OE2 GLU A 314      27.077  13.636  11.025  0.72 46.28           O  
ANISOU 2962  OE2 GLU A 314     5981   7376   4228  -4465    142   -366       O  
ATOM   2963  N   PHE A 315      22.579  10.589  10.471  1.00 16.20           N  
ANISOU 2963  N   PHE A 315     1825   2288   2042   -448    218    321       N  
ATOM   2964  CA  PHE A 315      21.828  10.468  11.731  1.00 14.88           C  
ANISOU 2964  CA  PHE A 315     1730   1975   1949   -440    127    423       C  
ATOM   2965  C   PHE A 315      20.337  10.632  11.444  1.00 13.28           C  
ANISOU 2965  C   PHE A 315     1794   1591   1663   -297     25    424       C  
ATOM   2966  O   PHE A 315      19.949  11.049  10.333  1.00 17.02           O  
ANISOU 2966  O   PHE A 315     2363   2225   1880   -384    -96    558       O  
ATOM   2967  CB  PHE A 315      22.253  11.543  12.734  1.00 15.72           C  
ANISOU 2967  CB  PHE A 315     1779   2171   2024   -391    -45    354       C  
ATOM   2968  CG  PHE A 315      21.786  12.959  12.445  1.00 16.41           C  
ANISOU 2968  CG  PHE A 315     2279   1937   2018   -508    186    206       C  
ATOM   2969  CD1 PHE A 315      22.381  13.745  11.469  1.00 20.40           C  
ANISOU 2969  CD1 PHE A 315     2889   2269   2592   -625    444    562       C  
ATOM   2970  CD2 PHE A 315      20.726  13.498  13.183  1.00 17.21           C  
ANISOU 2970  CD2 PHE A 315     2427   2203   1910   -255    -21    -84       C  
ATOM   2971  CE1 PHE A 315      21.946  15.042  11.189  1.00 23.86           C  
ANISOU 2971  CE1 PHE A 315     3959   1989   3120   -888    321    498       C  
ATOM   2972  CE2 PHE A 315      20.264  14.818  12.934  1.00 19.37           C  
ANISOU 2972  CE2 PHE A 315     2317   2085   2957   -304   -394   -224       C  
ATOM   2973  CZ  PHE A 315      20.902  15.599  11.941  1.00 23.10           C  
ANISOU 2973  CZ  PHE A 315     2991   1902   3886   -683   -392    182       C  
ATOM   2974  OXT PHE A 315      19.536  10.321  12.368  1.00 14.22           O  
ANISOU 2974  OXT PHE A 315     1614   1838   1951   -326     51    441       O  
TER    2975      PHE A 315                                                      
HETATM 2976  PA  NDP A 318      22.751  -4.797  27.225  1.00  6.97           P  
ANISOU 2976  PA  NDP A 318     1025    774    851     82     -8    -15       P  
HETATM 2977  O1A NDP A 318      23.667  -3.768  26.685  1.00  8.21           O  
ANISOU 2977  O1A NDP A 318     1102    897   1121     67     57     62       O  
HETATM 2978  O2A NDP A 318      21.711  -4.434  28.192  1.00  8.29           O  
ANISOU 2978  O2A NDP A 318     1237    941    972    175    131     44       O  
HETATM 2979  O5B NDP A 318      23.678  -5.997  27.722  1.00  7.65           O  
ANISOU 2979  O5B NDP A 318     1037    831   1039    153     22     62       O  
HETATM 2980  C5B NDP A 318      23.103  -7.220  28.254  1.00  8.23           C  
ANISOU 2980  C5B NDP A 318     1259    752   1117    140    -10    125       C  
HETATM 2981  C4B NDP A 318      24.243  -8.121  28.651  1.00  8.04           C  
ANISOU 2981  C4B NDP A 318     1240    892    924    157    -56     21       C  
HETATM 2982  O4B NDP A 318      24.998  -7.527  29.736  1.00  9.20           O  
ANISOU 2982  O4B NDP A 318     1425   1069   1000     58   -135    114       O  
HETATM 2983  C3B NDP A 318      23.846  -9.509  29.083  1.00  8.63           C  
ANISOU 2983  C3B NDP A 318     1383    893   1003    186     92     83       C  
HETATM 2984  O3B NDP A 318      24.818 -10.442  28.607  1.00 10.03           O  
ANISOU 2984  O3B NDP A 318     1617   1021   1173    371    124    -17       O  
HETATM 2985  C2B NDP A 318      23.936  -9.412  30.625  1.00  8.73           C  
ANISOU 2985  C2B NDP A 318     1476    861    981    245     -8    126       C  
HETATM 2986  O2B NDP A 318      24.221 -10.673  31.240  1.00  9.84           O  
ANISOU 2986  O2B NDP A 318     1526   1075   1138    421      1    228       O  
HETATM 2987  C1B NDP A 318      25.084  -8.447  30.820  1.00  8.96           C  
ANISOU 2987  C1B NDP A 318     1358   1100    949    281    -40     88       C  
HETATM 2988  N9A NDP A 318      25.056  -7.676  32.055  1.00  9.12           N  
ANISOU 2988  N9A NDP A 318     1279   1169   1015    266    -91     23       N  
HETATM 2989  C8A NDP A 318      23.965  -7.006  32.580  1.00  9.20           C  
ANISOU 2989  C8A NDP A 318     1296   1245    957    110     20    -76       C  
HETATM 2990  N7A NDP A 318      24.231  -6.374  33.695  1.00  9.76           N  
ANISOU 2990  N7A NDP A 318     1327   1297   1083    175   -104    -63       N  
HETATM 2991  C5A NDP A 318      25.571  -6.645  33.932  1.00  9.11           C  
ANISOU 2991  C5A NDP A 318     1268   1065   1128    121   -155     98       C  
HETATM 2992  C6A NDP A 318      26.394  -6.263  34.987  1.00  9.90           C  
ANISOU 2992  C6A NDP A 318     1445   1142   1176     22   -158     80       C  
HETATM 2993  N6A NDP A 318      26.008  -5.517  36.043  1.00 10.89           N  
ANISOU 2993  N6A NDP A 318     1557   1297   1283     20   -169    -73       N  
HETATM 2994  N1A NDP A 318      27.680  -6.729  34.935  1.00 11.90           N  
ANISOU 2994  N1A NDP A 318     1451   1426   1645    183   -420   -109       N  
HETATM 2995  C2A NDP A 318      28.086  -7.488  33.906  1.00 12.25           C  
ANISOU 2995  C2A NDP A 318     1427   1472   1756    265   -369   -216       C  
HETATM 2996  N3A NDP A 318      27.364  -7.890  32.849  1.00 11.15           N  
ANISOU 2996  N3A NDP A 318     1413   1339   1484    321   -229     10       N  
HETATM 2997  C4A NDP A 318      26.083  -7.426  32.915  1.00  9.04           C  
ANISOU 2997  C4A NDP A 318     1349    937   1149    210   -154     48       C  
HETATM 2998  O3  NDP A 318      22.086  -5.510  25.928  1.00  9.17           O  
ANISOU 2998  O3  NDP A 318     1142   1097   1247    215   -288   -328       O  
HETATM 2999  PN  NDP A 318      20.730  -5.572  25.111  1.00  6.92           P  
ANISOU 2999  PN  NDP A 318     1042    769    819     37     13    -29       P  
HETATM 3000  O1N NDP A 318      19.893  -6.692  25.594  1.00  7.86           O  
ANISOU 3000  O1N NDP A 318     1092    731   1165    100     87     17       O  
HETATM 3001  O2N NDP A 318      21.115  -5.564  23.673  1.00  8.64           O  
ANISOU 3001  O2N NDP A 318     1441    961    881     38    188    -44       O  
HETATM 3002  O5D NDP A 318      20.006  -4.166  25.345  1.00  6.65           O  
ANISOU 3002  O5D NDP A 318     1028    733    767    -16     74     31       O  
HETATM 3003  C5D NDP A 318      19.129  -3.906  26.480  1.00  6.68           C  
ANISOU 3003  C5D NDP A 318      960    845    734     52     48    -63       C  
HETATM 3004  C4D NDP A 318      17.669  -4.018  26.056  1.00  6.26           C  
ANISOU 3004  C4D NDP A 318     1084    579    715    -21    -64     79       C  
HETATM 3005  O4D NDP A 318      17.361  -2.987  25.075  1.00  6.49           O  
ANISOU 3005  O4D NDP A 318     1152    623    690    -35    -22     24       O  
HETATM 3006  C3D NDP A 318      17.222  -5.277  25.349  1.00  6.26           C  
ANISOU 3006  C3D NDP A 318      999    640    741    -20    -53     71       C  
HETATM 3007  O3D NDP A 318      17.139  -6.408  26.205  1.00  6.43           O  
ANISOU 3007  O3D NDP A 318     1070    637    737    -20      3     69       O  
HETATM 3008  C2D NDP A 318      15.896  -4.834  24.736  1.00  6.43           C  
ANISOU 3008  C2D NDP A 318     1015    740    686     28     37    109       C  
HETATM 3009  O2D NDP A 318      14.929  -4.769  25.808  1.00  7.16           O  
ANISOU 3009  O2D NDP A 318     1018    983    722     45     88     92       O  
HETATM 3010  C1D NDP A 318      16.283  -3.415  24.270  1.00  6.41           C  
ANISOU 3010  C1D NDP A 318     1113    763    561     13     -3    -25       C  
HETATM 3011  N1N NDP A 318      16.746  -3.397  22.833  1.00  6.12           N  
ANISOU 3011  N1N NDP A 318     1054    622    651     14     27     67       N  
HETATM 3012  C2N NDP A 318      15.875  -2.882  21.904  1.00  6.43           C  
ANISOU 3012  C2N NDP A 318     1148    597    697    -77    -60     64       C  
HETATM 3013  C3N NDP A 318      16.255  -2.839  20.569  1.00  6.56           C  
ANISOU 3013  C3N NDP A 318     1259    601    632     -9      3      9       C  
HETATM 3014  C7N NDP A 318      15.378  -2.183  19.531  1.00  6.87           C  
ANISOU 3014  C7N NDP A 318     1238    700    670    -52     14     33       C  
HETATM 3015  O7N NDP A 318      15.618  -2.402  18.339  1.00  8.34           O  
ANISOU 3015  O7N NDP A 318     1545    944    682     42    -46     77       O  
HETATM 3016  N7N NDP A 318      14.431  -1.374  19.973  1.00  7.76           N  
ANISOU 3016  N7N NDP A 318     1235    820    894     62    -39    130       N  
HETATM 3017  C4N NDP A 318      17.473  -3.397  20.185  1.00  7.23           C  
ANISOU 3017  C4N NDP A 318     1247    696    804     12     78     21       C  
HETATM 3018  C5N NDP A 318      18.362  -3.896  21.143  1.00  7.13           C  
ANISOU 3018  C5N NDP A 318     1176    812    721     32    122    103       C  
HETATM 3019  C6N NDP A 318      17.973  -3.879  22.467  1.00  6.86           C  
ANISOU 3019  C6N NDP A 318     1039    698    870     50    124     22       C  
HETATM 3020  P2B NDP A 318      23.128 -11.577  32.023  1.00  9.78           P  
ANISOU 3020  P2B NDP A 318     1702    952   1063    322     35    155       P  
HETATM 3021  O1X NDP A 318      21.799 -11.307  31.391  1.00  9.64           O  
ANISOU 3021  O1X NDP A 318     1576    942   1145    302      7     41       O  
HETATM 3022  O2X NDP A 318      23.675 -12.969  31.806  1.00 12.15           O  
ANISOU 3022  O2X NDP A 318     2060    958   1600    597     49    140       O  
HETATM 3023  O3X NDP A 318      23.216 -11.169  33.463  1.00 11.12           O  
ANISOU 3023  O3X NDP A 318     2003   1233    988    378     40    129       O  
HETATM 3024  C2  3NA A 320      16.321  -9.526  17.344  1.00 14.54           C  
ANISOU 3024  C2  3NA A 320     2273   1363   1889   -151   -431    459       C  
HETATM 3025  C3  3NA A 320      17.895  -9.560  14.896  1.00 14.81           C  
ANISOU 3025  C3  3NA A 320     3019   1429   1177    191   -531   -181       C  
HETATM 3026  C4  3NA A 320      17.129  -8.455  16.942  1.00 10.64           C  
ANISOU 3026  C4  3NA A 320     1651   1140   1254    221   -254    123       C  
HETATM 3027  C5  3NA A 320      16.276 -10.657  16.509  1.00 18.31           C  
ANISOU 3027  C5  3NA A 320     3377   1552   2027   -502   -713    287       C  
HETATM 3028  C6  3NA A 320      17.136 -10.674  15.280  1.00 17.13           C  
ANISOU 3028  C6  3NA A 320     3127   1491   1890     17   -952     96       C  
HETATM 3029  C7  3NA A 320      17.816  -8.425  15.769  1.00 10.99           C  
ANISOU 3029  C7  3NA A 320     1833   1245   1096    300   -242    -56       C  
HETATM 3030  C11 3NA A 320      18.474  -7.124  15.672  1.00 10.90           C  
ANISOU 3030  C11 3NA A 320     1944   1283    915    242     75    -48       C  
HETATM 3031  C13 3NA A 320      18.342  -5.943  13.493  1.00  9.72           C  
ANISOU 3031  C13 3NA A 320     1432   1353    907    261    116   -157       C  
HETATM 3032  S14 3NA A 320      16.648  -6.347  13.418  1.00 10.29           S  
ANISOU 3032  S14 3NA A 320     1509   1357   1042    121     89    -31       S  
HETATM 3033  N15 3NA A 320      17.313  -7.239  17.563  1.00  9.53           N  
ANISOU 3033  N15 3NA A 320     1551   1085    986    301     58     37       N  
HETATM 3034  C16 3NA A 320      18.125  -6.466  16.815  1.00  9.77           C  
ANISOU 3034  C16 3NA A 320     1481   1204   1029    210    100      5       C  
HETATM 3035  C17 3NA A 320      19.285  -6.600  14.509  1.00 11.61           C  
ANISOU 3035  C17 3NA A 320     1642   1815    952    317     69     53       C  
HETATM 3036  F19 3NA A 320      14.162  -5.547  11.662  1.00 12.38           F  
ANISOU 3036  F19 3NA A 320     1600   1823   1280    -27    -56    -60       F  
HETATM 3037  C20 3NA A 320      16.653  -6.814  18.786  1.00 11.54           C  
ANISOU 3037  C20 3NA A 320     1739   1402   1244    474    292    247       C  
HETATM 3038  F22 3NA A 320      18.897  -3.092  10.527  1.00 14.36           F  
ANISOU 3038  F22 3NA A 320     1769   2205   1483   -156    209    356       F  
HETATM 3039  F23 3NA A 320      16.653  -2.418   9.172  1.00 14.71           F  
ANISOU 3039  F23 3NA A 320     2283   1995   1310    233     76    369       F  
HETATM 3040  C24 3NA A 320      17.675  -4.651  11.835  1.00 10.07           C  
ANISOU 3040  C24 3NA A 320     1590   1300    935    182     79    -90       C  
HETATM 3041  C25 3NA A 320      15.365  -3.973  10.359  1.00 10.92           C  
ANISOU 3041  C25 3NA A 320     1812   1399    936    176    138   -152       C  
HETATM 3042  C26 3NA A 320      17.739  -3.709  10.822  1.00 11.49           C  
ANISOU 3042  C26 3NA A 320     1733   1593   1038      2    176     68       C  
HETATM 3043  C27 3NA A 320      16.468  -5.279  12.098  1.00  9.35           C  
ANISOU 3043  C27 3NA A 320     1527   1157    869    167     90   -218       C  
HETATM 3044  C28 3NA A 320      15.322  -4.935  11.360  1.00 10.01           C  
ANISOU 3044  C28 3NA A 320     1552   1332    919    220     44   -162       C  
HETATM 3045  C29 3NA A 320      16.584  -3.387  10.133  1.00 11.45           C  
ANISOU 3045  C29 3NA A 320     1819   1543    989    214    189    174       C  
HETATM 3046  C32 3NA A 320      15.424  -5.876  18.505  1.00  8.09           C  
ANISOU 3046  C32 3NA A 320     1362    917    794    102     12     14       C  
HETATM 3047  O33 3NA A 320      14.938  -5.386  19.469  1.00  9.59           O  
ANISOU 3047  O33 3NA A 320     1394   1145   1106     67     -1    189       O  
HETATM 3048  O34 3NA A 320      15.145  -5.612  17.280  1.00 11.46           O  
ANISOU 3048  O34 3NA A 320     1709   1502   1142    296     59    229       O  
HETATM 3049  N36 3NA A 320      18.750  -5.058  12.635  1.00 10.45           N  
ANISOU 3049  N36 3NA A 320     1499   1569    903    136    135   -110       N  
HETATM 3050  O   HOH A2001      13.565   4.858  37.277  1.00 15.91           O  
ANISOU 3050  O   HOH A2001     2477   1815   1753    377     59   -277       O  
HETATM 3051  O   HOH A2002      10.451  15.346  33.331  1.00 27.88           O  
ANISOU 3051  O   HOH A2002     3967   1932   4694   -245  -1419   -738       O  
HETATM 3052  O   HOH A2003       7.480  12.774  25.031  1.00 19.06           O  
ANISOU 3052  O   HOH A2003     4071   1403   1767   1142     -6   -329       O  
HETATM 3053  O  BHOH A2004       2.439  11.714  22.269  0.57 18.96           O  
ANISOU 3053  O  BHOH A2004     2527   2952   1726   -203    491   -507       O  
HETATM 3054  O   HOH A2005       1.784   9.147  22.144  1.00 22.30           O  
ANISOU 3054  O   HOH A2005     3126   1533   3815    898   -453   -443       O  
HETATM 3055  O   HOH A2006       1.991   6.502  28.889  1.00 13.28           O  
ANISOU 3055  O   HOH A2006     2202   1278   1564    247    -88   -250       O  
HETATM 3056  O   HOH A2007       1.459   5.445  31.506  1.00 14.02           O  
ANISOU 3056  O   HOH A2007     2159   1514   1655    156    236   -143       O  
HETATM 3057  O   HOH A2008       0.220   2.414  34.129  1.00 14.05           O  
ANISOU 3057  O   HOH A2008     1928   2051   1358    202    408    -50       O  
HETATM 3058  O   HOH A2009       3.156   3.966  35.395  1.00 18.18           O  
ANISOU 3058  O   HOH A2009     2639   1732   2536     -2    344     94       O  
HETATM 3059  O   HOH A2010       2.943   6.306  33.803  1.00 17.67           O  
ANISOU 3059  O   HOH A2010     2694   2121   1900     90    -25   -373       O  
HETATM 3060  O   HOH A2011       8.734   3.273  43.005  1.00 49.93           O  
ANISOU 3060  O   HOH A2011     3411   6447   9111    233     59  -4423       O  
HETATM 3061  O   HOH A2012      12.021   1.419  37.159  1.00 14.19           O  
ANISOU 3061  O   HOH A2012     2114   1483   1793   -152    632    369       O  
HETATM 3062  O   HOH A2013      15.598  -9.839  31.521  1.00 10.44           O  
ANISOU 3062  O   HOH A2013     1823    977   1166     23    -15    -76       O  
HETATM 3063  O   HOH A2014       9.583  -9.298  25.871  1.00  8.88           O  
ANISOU 3063  O   HOH A2014     1438    868   1068     -1    -93     15       O  
HETATM 3064  O   HOH A2015      14.745 -12.990  22.813  1.00 15.43           O  
ANISOU 3064  O   HOH A2015     1707   1671   2485   -165   -313   -461       O  
HETATM 3065  O   HOH A2016      16.518 -15.230  36.277  1.00 25.14           O  
ANISOU 3065  O   HOH A2016     2626   4164   2762    321   -202    359       O  
HETATM 3066  O   HOH A2017       9.554  -2.862  45.112  1.00 22.12           O  
ANISOU 3066  O   HOH A2017     4789   2194   1423   1269    789     98       O  
HETATM 3067  O   HOH A2018      11.166   2.056  42.554  1.00 33.49           O  
ANISOU 3067  O   HOH A2018     4613   3112   4998    959   -133  -2423       O  
HETATM 3068  O   HOH A2019      11.403   0.960  26.928  1.00  9.40           O  
ANISOU 3068  O   HOH A2019     1674    938    959     42    165     69       O  
HETATM 3069  O   HOH A2020      11.377   3.020  25.161  1.00  9.13           O  
ANISOU 3069  O   HOH A2020     1351    968   1151     98     86    -32       O  
HETATM 3070  O   HOH A2021       8.327  -6.862  18.126  1.00  8.78           O  
ANISOU 3070  O   HOH A2021     1446   1019    870    -59    -67   -121       O  
HETATM 3071  O   HOH A2022       4.300  -7.357  16.925  1.00 12.31           O  
ANISOU 3071  O   HOH A2022     1912   1316   1451   -144    420    152       O  
HETATM 3072  O  AHOH A2023       3.570  -6.423  19.535  0.70  9.01           O  
ANISOU 3072  O  AHOH A2023     1469    766   1190     -7    308     20       O  
HETATM 3073  O  BHOH A2023       5.121  -6.867  20.391  0.30 26.19           O  
ANISOU 3073  O  BHOH A2023     3077   2960   3915   -736   1151    -31       O  
HETATM 3074  O   HOH A2024       6.622 -14.446  19.685  1.00 21.60           O  
ANISOU 3074  O   HOH A2024     2666   2105   3437   -208   -813    375       O  
HETATM 3075  O   HOH A2025       6.398 -13.277  22.815  1.00 15.78           O  
ANISOU 3075  O   HOH A2025     2440   2258   1300    582   -250   -498       O  
HETATM 3076  O   HOH A2026       3.971 -11.780  22.052  1.00 13.41           O  
ANISOU 3076  O   HOH A2026     2404   1489   1201   -658     57   -300       O  
HETATM 3077  O   HOH A2028       1.036 -15.326  37.192  1.00 18.76           O  
ANISOU 3077  O   HOH A2028     2684   2169   2274   -534     69   -217       O  
HETATM 3078  O   HOH A2029      -0.304 -15.621  34.836  1.00 13.71           O  
ANISOU 3078  O   HOH A2029     2070   1337   1803   -400     55    -47       O  
HETATM 3079  O   HOH A2030      -2.987 -14.948  34.755  1.00 19.82           O  
ANISOU 3079  O   HOH A2030     2368   2266   2895   -426    105    134       O  
HETATM 3080  O   HOH A2031      -4.118 -16.226  37.067  1.00 23.73           O  
ANISOU 3080  O   HOH A2031     3006   3289   2722  -1453    867   -908       O  
HETATM 3081  O  BHOH A2032      -0.448 -15.059  39.445  0.60 16.85           O  
ANISOU 3081  O  BHOH A2032     2725   1785   1894   -926    303   -295       O  
HETATM 3082  O  BHOH A2033      -3.094 -14.397  38.991  0.60 28.86           O  
ANISOU 3082  O  BHOH A2033     4547   3374   3044   -335   1263    134       O  
HETATM 3083  O   HOH A2034      -1.793  -5.170  42.924  1.00 29.91           O  
ANISOU 3083  O   HOH A2034     3228   3644   4493    159   1157  -1623       O  
HETATM 3084  O   HOH A2035      -3.365  -3.368  40.197  1.00 25.88           O  
ANISOU 3084  O   HOH A2035     2811   3941   3080   -687    882    840       O  
HETATM 3085  O   HOH A2036       2.876  -7.588  49.148  1.00 29.83           O  
ANISOU 3085  O   HOH A2036     4618   4582   2134   -842   -860    904       O  
HETATM 3086  O   HOH A2037      -3.529  -5.166  34.792  1.00 40.29           O  
ANISOU 3086  O   HOH A2037     5965   5310   4033  -2742   -276   1420       O  
HETATM 3087  O   HOH A2038      -3.382  -3.685  32.452  1.00 16.75           O  
ANISOU 3087  O   HOH A2038     1779   2571   2016   -188   -170   -546       O  
HETATM 3088  O   HOH A2039       8.517  -2.831  13.169  1.00  8.38           O  
ANISOU 3088  O   HOH A2039     1401   1028    756    -60    -73    -10       O  
HETATM 3089  O   HOH A2040       6.021   0.558   6.988  1.00 22.39           O  
ANISOU 3089  O   HOH A2040     3402   2558   2549   -751  -1427   1225       O  
HETATM 3090  O   HOH A2041       4.459  -5.134   6.860  1.00 15.58           O  
ANISOU 3090  O   HOH A2041     2413   1869   1639    805   -455   -448       O  
HETATM 3091  O   HOH A2042       2.541 -10.947   9.633  1.00 18.65           O  
ANISOU 3091  O   HOH A2042     2676   2221   2187   -541    266   -540       O  
HETATM 3092  O   HOH A2043       5.173 -12.422  11.538  1.00 23.33           O  
ANISOU 3092  O   HOH A2043     5154   1541   2170   -531     23    101       O  
HETATM 3093  O   HOH A2044       6.674 -13.196   6.831  1.00 13.84           O  
ANISOU 3093  O   HOH A2044     2078   1676   1503    149   -449   -171       O  
HETATM 3094  O   HOH A2045      -4.165  -3.350   5.658  1.00 34.23           O  
ANISOU 3094  O   HOH A2045     4080   6651   2277   -484   -507   -397       O  
HETATM 3095  O   HOH A2046      -1.441  -0.765   4.902  1.00 41.79           O  
ANISOU 3095  O   HOH A2046     4800   8489   2590   1838    471   2533       O  
HETATM 3096  O   HOH A2047      -5.199  -2.165  12.789  1.00 17.56           O  
ANISOU 3096  O   HOH A2047     1885   2892   1895    401   -326    308       O  
HETATM 3097  O   HOH A2048      -5.177   0.246  14.202  1.00 21.66           O  
ANISOU 3097  O   HOH A2048     2499   2535   3196   -107    329  -1055       O  
HETATM 3098  O   HOH A2049      -5.672  -6.585  13.053  1.00 24.98           O  
ANISOU 3098  O   HOH A2049     2660   4986   1847  -1031   -732   -216       O  
HETATM 3099  O   HOH A2050      -2.266  -8.998  13.108  1.00 22.62           O  
ANISOU 3099  O   HOH A2050     3607   2657   2331   -577   -252   -373       O  
HETATM 3100  O  AHOH A2051      -4.594 -10.948  17.987  0.50 23.33           O  
ANISOU 3100  O  AHOH A2051     2553   2760   3550  -1499   -441   -165       O  
HETATM 3101  O   HOH A2052       2.369  -9.256  17.863  1.00 18.24           O  
ANISOU 3101  O   HOH A2052     1831   1996   3105    238     71    228       O  
HETATM 3102  O   HOH A2053      -5.084  -9.819  28.548  1.00 30.78           O  
ANISOU 3102  O   HOH A2053     2971   4095   4629  -1456   -182    171       O  
HETATM 3103  O   HOH A2054      -0.257 -17.137  31.083  1.00 17.60           O  
ANISOU 3103  O   HOH A2054     2859   1735   2095   -178    382     88       O  
HETATM 3104  O   HOH A2055      -4.483 -14.765  32.476  1.00 40.40           O  
ANISOU 3104  O   HOH A2055     2985   6741   5624  -1082   -337   3361       O  
HETATM 3105  O   HOH A2057      14.361 -15.277  11.803  1.00 19.84           O  
ANISOU 3105  O   HOH A2057     2840   1774   2924    283   -189   1012       O  
HETATM 3106  O   HOH A2058      12.235 -15.686  10.174  1.00 16.59           O  
ANISOU 3106  O   HOH A2058     2494   1510   2299    432   -258    323       O  
HETATM 3107  O   HOH A2059      -6.069   3.032  28.054  1.00 26.84           O  
ANISOU 3107  O   HOH A2059     3357   3700   3142   -849     61   -788       O  
HETATM 3108  O   HOH A2060      19.498   2.176  16.856  1.00  8.68           O  
ANISOU 3108  O   HOH A2060     1360   1081    856     33     47     -2       O  
HETATM 3109  O   HOH A2061      21.613   0.468  16.019  1.00 10.21           O  
ANISOU 3109  O   HOH A2061     1385   1291   1202    231     94    -99       O  
HETATM 3110  O   HOH A2062      20.221   4.623  15.813  1.00 11.10           O  
ANISOU 3110  O   HOH A2062     1566   1316   1333   -113    -71     17       O  
HETATM 3111  O   HOH A2063      18.305   5.803  14.177  1.00 15.22           O  
ANISOU 3111  O   HOH A2063     1855   1592   2337    103   -382    379       O  
HETATM 3112  O   HOH A2064      20.069   7.643  12.859  1.00 15.70           O  
ANISOU 3112  O   HOH A2064     1995   2228   1743    -20     70    450       O  
HETATM 3113  O   HOH A2065      22.337   7.041  14.319  1.00 16.75           O  
ANISOU 3113  O   HOH A2065     2438   1988   1938   -223     86    220       O  
HETATM 3114  O   HOH A2066      21.164   6.953  10.507  1.00 21.14           O  
ANISOU 3114  O   HOH A2066     3197   2603   2234  -1187    791   -508       O  
HETATM 3115  O   HOH A2067      23.375  10.677  16.067  1.00 16.57           O  
ANISOU 3115  O   HOH A2067     2359   2184   1753    149   -163    488       O  
HETATM 3116  O   HOH A2068      26.169  12.395  16.180  1.00 24.61           O  
ANISOU 3116  O   HOH A2068     2742   4309   2302    326    510    386       O  
HETATM 3117  O   HOH A2069      24.649   7.889  26.815  1.00 15.16           O  
ANISOU 3117  O   HOH A2069     2226   1595   1937     45    295    418       O  
HETATM 3118  O   HOH A2070      24.167   5.032  26.914  1.00 11.81           O  
ANISOU 3118  O   HOH A2070     1833   1521   1135    371    -64   -226       O  
HETATM 3119  O   HOH A2071      26.043   3.376  28.212  1.00  9.46           O  
ANISOU 3119  O   HOH A2071     1475    989   1129    -90     30    -22       O  
HETATM 3120  O   HOH A2072      31.073  12.060  20.957  1.00 33.02           O  
ANISOU 3120  O   HOH A2072     8540   2054   1953   1530   -517     99       O  
HETATM 3121  O   HOH A2073      27.867  11.142  18.021  1.00 24.66           O  
ANISOU 3121  O   HOH A2073     3177   2325   3868   -209   -747    490       O  
HETATM 3122  O   HOH A2074      27.394   8.381  17.388  1.00 21.62           O  
ANISOU 3122  O   HOH A2074     3432   2837   1946    229    875    -81       O  
HETATM 3123  O   HOH A2075      20.910  17.754  15.891  1.00 27.59           O  
ANISOU 3123  O   HOH A2075     5069   1777   3638  -1147   -962    939       O  
HETATM 3124  O   HOH A2076      15.300  12.328  26.284  1.00 13.21           O  
ANISOU 3124  O   HOH A2076     2039   1289   1693    -72   -477   -195       O  
HETATM 3125  O   HOH A2077      23.864 -15.356  27.927  1.00 37.13           O  
ANISOU 3125  O   HOH A2077     4560   3846   5700    791    867  -2306       O  
HETATM 3126  O   HOH A2078      30.472  -4.698  26.481  1.00 29.13           O  
ANISOU 3126  O   HOH A2078     1679   2423   6967    350    648  -1098       O  
HETATM 3127  O   HOH A2079      30.651  -4.149  35.607  1.00 25.03           O  
ANISOU 3127  O   HOH A2079     4861   2025   2624    885   -534    239       O  
HETATM 3128  O   HOH A2080      17.391  10.718  32.671  1.00 16.59           O  
ANISOU 3128  O   HOH A2080     2139   1790   2373   -148    339   -450       O  
HETATM 3129  O   HOH A2082      25.780  15.672  33.838  1.00 32.56           O  
ANISOU 3129  O   HOH A2082     5333   1959   5081    459   -561   1027       O  
HETATM 3130  O   HOH A2083      19.214  -4.692  34.553  1.00 13.07           O  
ANISOU 3130  O   HOH A2083     1572   1971   1422     58    105     37       O  
HETATM 3131  O   HOH A2084      28.506  -9.530  37.779  1.00 36.60           O  
ANISOU 3131  O   HOH A2084     3288   6157   4462    104  -1826   -930       O  
HETATM 3132  O   HOH A2085      29.382  -6.041  36.999  1.00 28.25           O  
ANISOU 3132  O   HOH A2085     2241   5337   3154    686  -1130   -914       O  
HETATM 3133  O   HOH A2086      18.589   2.438  43.862  1.00 20.75           O  
ANISOU 3133  O   HOH A2086     3310   2411   2162   -556    708   -641       O  
HETATM 3134  O   HOH A2087      20.874   4.035  44.242  1.00 19.42           O  
ANISOU 3134  O   HOH A2087     3519   2224   1635   -681    257    -33       O  
HETATM 3135  O   HOH A2088      28.897  11.203  43.503  1.00 31.02           O  
ANISOU 3135  O   HOH A2088     4811   3517   3459   -534  -1471   -602       O  
HETATM 3136  O   HOH A2089      31.190  18.676  37.382  1.00 25.08           O  
ANISOU 3136  O   HOH A2089     3388   2584   3557    -52   -107  -1709       O  
HETATM 3137  O   HOH A2090      33.827  14.710  24.233  1.00 17.63           O  
ANISOU 3137  O   HOH A2090     2849   2149   1701   -547    284     98       O  
HETATM 3138  O   HOH A2091      36.901   4.497  21.901  1.00 14.41           O  
ANISOU 3138  O   HOH A2091     1694   1951   1829    127    260     -1       O  
HETATM 3139  O   HOH A2092      38.425   7.795  21.782  1.00 38.93           O  
ANISOU 3139  O   HOH A2092     3506   5780   5507   2127   1135    -11       O  
HETATM 3140  O   HOH A2093      24.145  -5.789  13.794  1.00 58.13           O  
ANISOU 3140  O   HOH A2093    10193   7132   4762    310   -884   1877       O  
HETATM 3141  O   HOH A2094      18.285   1.265   1.445  1.00 30.72           O  
ANISOU 3141  O   HOH A2094     3157   5001   3515  -1328    132    904       O  
HETATM 3142  O   HOH A2095      19.107   5.539   5.926  1.00 18.16           O  
ANISOU 3142  O   HOH A2095     2583   2310   2007   -525    -30    548       O  
HETATM 3143  O   HOH A2097       8.339  14.786  26.691  1.00 31.42           O  
ANISOU 3143  O   HOH A2097     5027   3252   3661    966   -317   -460       O  
HETATM 3144  O   HOH A2098      19.223  17.175  27.468  1.00 40.57           O  
ANISOU 3144  O   HOH A2098     6719   3864   4831   -857  -1719    960       O  
HETATM 3145  O   HOH A2099       0.832  14.501  20.701  1.00 26.77           O  
ANISOU 3145  O   HOH A2099     2779   4358   3033   1022   -641  -2099       O  
HETATM 3146  O   HOH A2100       2.149   8.893  35.047  1.00 29.59           O  
ANISOU 3146  O   HOH A2100     3885   3626   3734    224   1766    516       O  
HETATM 3147  O   HOH A2101      11.659   3.130  39.148  1.00 29.33           O  
ANISOU 3147  O   HOH A2101     3943   5148   2052    274    243   -654       O  
HETATM 3148  O   HOH A2102       9.203   4.494  39.155  1.00 35.90           O  
ANISOU 3148  O   HOH A2102     4545   4939   4157    122    -92   -671       O  
HETATM 3149  O   HOH A2103      20.159 -14.525  28.704  1.00 21.91           O  
ANISOU 3149  O   HOH A2103     3560   1229   3534   -233   -217   -346       O  
HETATM 3150  O   HOH A2104      20.917 -16.691  29.946  1.00 31.08           O  
ANISOU 3150  O   HOH A2104     5428   2433   3948   1227   1623    590       O  
HETATM 3151  O   HOH A2105      10.561 -18.420  33.407  1.00 37.60           O  
ANISOU 3151  O   HOH A2105     6605   5036   2646   1994   1566    -96       O  
HETATM 3152  O   HOH A2106      11.906 -18.039  35.569  1.00 20.13           O  
ANISOU 3152  O   HOH A2106     3320   1354   2976    288    195   -529       O  
HETATM 3153  O   HOH A2107       6.752 -18.773  33.142  1.00 25.50           O  
ANISOU 3153  O   HOH A2107     4437   2253   3001  -1200   -169   -347       O  
HETATM 3154  O   HOH A2108       9.090 -13.590  44.014  1.00 21.96           O  
ANISOU 3154  O   HOH A2108     2829   2235   3280    717   -631   -258       O  
HETATM 3155  O   HOH A2109       2.766 -19.145  41.607  1.00 54.53           O  
ANISOU 3155  O   HOH A2109     5851   9134   5734   -175    858   1069       O  
HETATM 3156  O   HOH A2110       7.061 -14.350  46.574  1.00 50.27           O  
ANISOU 3156  O   HOH A2110     5837   6650   6615  -1516   -174  -2884       O  
HETATM 3157  O   HOH A2111      19.005  -2.805  44.149  1.00 34.95           O  
ANISOU 3157  O   HOH A2111     6717   3800   2764   -946    756   -240       O  
HETATM 3158  O   HOH A2112      13.294  -5.997  48.320  1.00 21.28           O  
ANISOU 3158  O   HOH A2112     2832   2952   2301   -633   -552   1013       O  
HETATM 3159  O   HOH A2113      18.301   0.118  45.591  1.00 37.80           O  
ANISOU 3159  O   HOH A2113     4593   6242   3529  -2355   -359   1722       O  
HETATM 3160  O   HOH A2114       6.107   2.187  42.742  1.00 39.73           O  
ANISOU 3160  O   HOH A2114     5601   5402   4091   2492    825  -2352       O  
HETATM 3161  O   HOH A2115       1.130 -11.380  16.455  1.00 23.18           O  
ANISOU 3161  O   HOH A2115     3404   2828   2577   -203    641   -323       O  
HETATM 3162  O   HOH A2116      -1.121 -10.864  15.119  1.00 35.08           O  
ANISOU 3162  O   HOH A2116     5950   2815   4562   -437   1233   -485       O  
HETATM 3163  O   HOH A2117      12.650 -14.286  17.219  1.00 21.00           O  
ANISOU 3163  O   HOH A2117     3122   2769   2087   1295    448   -312       O  
HETATM 3164  O   HOH A2118       8.364 -20.369  25.395  1.00 28.09           O  
ANISOU 3164  O   HOH A2118     4109   2985   3578    -76    323   -579       O  
HETATM 3165  O   HOH A2119      12.532 -16.487  23.959  1.00 26.70           O  
ANISOU 3165  O   HOH A2119     3146   4378   2622   1043    439   1202       O  
HETATM 3166  O   HOH A2120       5.666 -15.661  24.673  1.00 23.57           O  
ANISOU 3166  O   HOH A2120     4286   2300   2368  -1504   1296  -1084       O  
HETATM 3167  O   HOH A2121       6.747 -17.612  25.014  1.00 22.71           O  
ANISOU 3167  O   HOH A2121     2998   3180   2450  -1446    685  -1514       O  
HETATM 3168  O   HOH A2122       4.073 -19.074  24.169  1.00 63.31           O  
ANISOU 3168  O   HOH A2122     7492   8041   8522     29  -2974  -3556       O  
HETATM 3169  O   HOH A2123       4.900 -19.874  26.883  1.00 23.07           O  
ANISOU 3169  O   HOH A2123     2222   1892   4653   -339    102   -360       O  
HETATM 3170  O  AHOH A2124      -1.410 -15.386  28.178  0.50 22.25           O  
ANISOU 3170  O  AHOH A2124     3609   2437   2407    375    132    872       O  
HETATM 3171  O   HOH A2125      -1.788 -15.318  25.083  1.00 30.64           O  
ANISOU 3171  O   HOH A2125     3404   2867   5372  -1528   1075   -533       O  
HETATM 3172  O   HOH A2126       5.374  -0.842  45.429  1.00 40.14           O  
ANISOU 3172  O   HOH A2126     5196   4947   5107   -311   2262  -1573       O  
HETATM 3173  O   HOH A2127       6.706  -2.473  46.547  1.00 27.38           O  
ANISOU 3173  O   HOH A2127     3443   4312   2649      3    -26    257       O  
HETATM 3174  O   HOH A2128       6.596 -15.392   5.313  1.00 31.87           O  
ANISOU 3174  O   HOH A2128     3662   3010   5436    393  -1424  -2014       O  
HETATM 3175  O   HOH A2129       3.620 -17.449   6.524  1.00 44.66           O  
ANISOU 3175  O   HOH A2129     7371   3211   6389   -658  -1034    -36       O  
HETATM 3176  O   HOH A2130      11.995 -18.788  10.393  1.00 33.55           O  
ANISOU 3176  O   HOH A2130     2449   6266   4032   -282  -1358    407       O  
HETATM 3177  O   HOH A2131      14.633 -15.947   8.020  1.00 33.57           O  
ANISOU 3177  O   HOH A2131     6437   3527   2790   3372    745   1030       O  
HETATM 3178  O   HOH A2133       8.039  -1.161   4.181  1.00 20.77           O  
ANISOU 3178  O   HOH A2133     2956   2487   2448    353   -316    418       O  
HETATM 3179  O   HOH A2134      12.526   6.062   5.271  1.00 23.86           O  
ANISOU 3179  O   HOH A2134     4848   2291   1929    669   -835    228       O  
HETATM 3180  O  AHOH A2135      -5.241   9.092  13.013  0.50 28.53           O  
ANISOU 3180  O  AHOH A2135     1930   5075   3836    356  -1350    262       O  
HETATM 3181  O   HOH A2136      -2.697  11.202  11.473  1.00 19.50           O  
ANISOU 3181  O   HOH A2136     4063   1747   1599    428     50    299       O  
HETATM 3182  O  AHOH A2137      -7.673  -0.398  15.201  0.50 33.14           O  
ANISOU 3182  O  AHOH A2137     5517   2953   4122   -205    827    605       O  
HETATM 3183  O   HOH A2138      -8.156   7.125  24.638  1.00 28.26           O  
ANISOU 3183  O   HOH A2138     3318   3640   3779   -604    865    -91       O  
HETATM 3184  O   HOH A2139      -9.677   9.036  28.573  1.00 31.91           O  
ANISOU 3184  O   HOH A2139     2608   4336   5179    -79   -821  -1741       O  
HETATM 3185  O   HOH A2140      -5.496   5.321  25.574  1.00 27.51           O  
ANISOU 3185  O   HOH A2140     2521   4469   3461   1729   -112   -975       O  
HETATM 3186  O   HOH A2141       9.442  19.722  12.407  1.00 58.58           O  
ANISOU 3186  O   HOH A2141     7461   6403   8393   1347  -2182   1134       O  
HETATM 3187  O   HOH A2142       5.574  13.751   5.916  1.00 29.35           O  
ANISOU 3187  O   HOH A2142     4689   4058   2406    118   -308   1114       O  
HETATM 3188  O   HOH A2143       4.693  17.971  14.342  1.00 36.38           O  
ANISOU 3188  O   HOH A2143     2756   6067   5000    799    411  -2308       O  
HETATM 3189  O   HOH A2144      23.272  15.240  22.386  1.00 37.46           O  
ANISOU 3189  O   HOH A2144     3664   5461   5110   -118   -258  -2594       O  
HETATM 3190  O   HOH A2145      25.251  14.922  23.494  1.00 33.69           O  
ANISOU 3190  O   HOH A2145     5794   2950   4055    851    969    770       O  
HETATM 3191  O   HOH A2146      24.705  14.680  26.087  1.00 32.54           O  
ANISOU 3191  O   HOH A2146     7159   1599   3607    500   1746     51       O  
HETATM 3192  O   HOH A2147      28.850  -9.578  31.082  1.00 25.18           O  
ANISOU 3192  O   HOH A2147     2704   3168   3696   1163   -265  -1676       O  
HETATM 3193  O  AHOH A2148      31.218  -8.748  28.703  0.50 39.28           O  
ANISOU 3193  O  AHOH A2148     4318   6168   4439    209  -2018    643       O  
HETATM 3194  O   HOH A2149      24.137 -13.000  29.107  1.00 27.33           O  
ANISOU 3194  O   HOH A2149     6451   1524   2411   -911   1696   -363       O  
HETATM 3195  O  AHOH A2150      20.258 -15.017  22.468  0.50 35.27           O  
ANISOU 3195  O  AHOH A2150     4137   5139   4125    -77    911   -414       O  
HETATM 3196  O   HOH A2151      34.457 -10.366  27.301  1.00 41.27           O  
ANISOU 3196  O   HOH A2151     4070   3154   8456   1082    761    254       O  
HETATM 3197  O   HOH A2152      40.810   5.450  38.895  1.00 34.52           O  
ANISOU 3197  O   HOH A2152     3255   5154   4708   -949  -1857     83       O  
HETATM 3198  O   HOH A2153      30.953   9.259  43.485  1.00 35.82           O  
ANISOU 3198  O   HOH A2153     3786   6318   3507    107    803  -1705       O  
HETATM 3199  O   HOH A2154      18.839  -9.914  43.740  1.00 25.04           O  
ANISOU 3199  O   HOH A2154     3994   3394   2126   -339   1042   -134       O  
HETATM 3200  O   HOH A2155      24.132  -7.189  43.694  1.00 32.36           O  
ANISOU 3200  O   HOH A2155     5466   4252   2577    665  -1593   -657       O  
HETATM 3201  O   HOH A2156      36.818  11.998  34.184  1.00 43.22           O  
ANISOU 3201  O   HOH A2156     5065   6199   5159   -390  -1976   1829       O  
HETATM 3202  O   HOH A2157      39.419   7.202  31.977  1.00 34.97           O  
ANISOU 3202  O   HOH A2157     4846   2909   5531  -1811   2363  -1220       O  
HETATM 3203  O   HOH A2158      29.439  -0.114  13.125  1.00 35.02           O  
ANISOU 3203  O   HOH A2158     4153   6699   2455     92    286  -1378       O  
HETATM 3204  O   HOH A2160      17.640 -12.228  11.212  1.00 24.04           O  
ANISOU 3204  O   HOH A2160     2819   2244   4073    254   -222    363       O  
HETATM 3205  O   HOH A2161      18.626 -11.785   8.337  1.00 41.49           O  
ANISOU 3205  O   HOH A2161     8217   4175   3371    656    211    989       O  
HETATM 3206  O   HOH A2162      18.696   6.822   3.639  1.00 41.97           O  
ANISOU 3206  O   HOH A2162     5544   5160   5244   -743  -1412   2625       O  
HETATM 3207  O   HOH A2163      27.872   3.669  12.521  1.00 44.40           O  
ANISOU 3207  O   HOH A2163     5855   5795   5221  -1806   -686   -963       O  
HETATM 3208  O   HOH A2165      24.480   5.785  10.821  1.00 42.65           O  
ANISOU 3208  O   HOH A2165     5997   5839   4369  -1350     -2   2084       O  
HETATM 3209  O   HOH A2166      26.938 -12.698  31.306  1.00 33.54           O  
ANISOU 3209  O   HOH A2166     4164   5539   3040   2515     95  -1497       O  
HETATM 3210  O   HOH A2167      27.448 -11.068  29.397  1.00 30.29           O  
ANISOU 3210  O   HOH A2167     2987   3685   4837    976    -67   -900       O  
HETATM 3211  O   HOH A2168      25.124 -14.772  33.272  1.00 33.01           O  
ANISOU 3211  O   HOH A2168     3969   2947   5628   1147   -623    612       O  
HETATM 3212  O   HOH A2169      23.407 -15.482  31.932  1.00 47.29           O  
ANISOU 3212  O   HOH A2169     7156   3686   7125   -571   2449  -1667       O  
HETATM 3213  O   HOH A2170      29.048 -14.432  33.654  1.00 55.32           O  
ANISOU 3213  O   HOH A2170     4246   6882   9893   3141  -1398  -3628       O  
HETATM 3214  O   HOH A2171      25.330 -14.872  35.525  1.00 45.30           O  
ANISOU 3214  O   HOH A2171     8141   4342   4730   3782    358    866       O  
HETATM 3215  O   HOH A2172       3.934 -20.463  36.230  1.00 40.23           O  
ANISOU 3215  O   HOH A2172     3842   4691   6752   1496   -336    731       O  
HETATM 3216  O   HOH A2173      15.796  12.639  33.670  1.00 41.87           O  
ANISOU 3216  O   HOH A2173     3084   4510   8313    363    562  -2204       O  
HETATM 3217  O   HOH A2174       6.480  16.704  21.699  1.00 36.59           O  
ANISOU 3217  O   HOH A2174     4673   5049   4183   -338   -267   -571       O  
HETATM 3218  O   HOH A2175      -0.918   9.619  23.616  1.00 34.97           O  
ANISOU 3218  O   HOH A2175     3817   3236   6233   -546   -868    -35       O  
HETATM 3219  O   HOH A2176       3.595  16.587  29.080  1.00 38.61           O  
ANISOU 3219  O   HOH A2176     6904   2408   5359   1677   -188   -901       O  
HETATM 3220  O   HOH A2177      18.195  10.984  42.073  1.00 51.22           O  
ANISOU 3220  O   HOH A2177     6263   6018   7181   2034   1809   -223       O  
HETATM 3221  O   HOH A2178      12.660 -23.424  28.405  1.00 22.44           O  
ANISOU 3221  O   HOH A2178     2359   2490   3676    393    -23   -198       O  
HETATM 3222  O   HOH A2179      14.422 -21.313  28.594  1.00 25.14           O  
ANISOU 3222  O   HOH A2179     4550   1449   3552   -371   1466   -593       O  
HETATM 3223  O   HOH A2180       4.083 -14.636  15.709  1.00 24.80           O  
ANISOU 3223  O   HOH A2180     3968   2704   2749  -1100     22  -1051       O  
HETATM 3224  O   HOH A2181      14.283 -13.629  15.069  1.00 42.21           O  
ANISOU 3224  O   HOH A2181     5182   4145   6711   -104   1880    504       O  
HETATM 3225  O   HOH A2182       0.189  -9.480  33.691  1.00 30.31           O  
ANISOU 3225  O   HOH A2182     5654   2846   3016   -187  -1326    265       O  
HETATM 3226  O   HOH A2183      -5.012  -9.567  12.592  1.00 37.96           O  
ANISOU 3226  O   HOH A2183     5182   4833   4409  -1373  -1243   -850       O  
HETATM 3227  O   HOH A2184      -3.625 -14.796  28.269  1.00 47.58           O  
ANISOU 3227  O   HOH A2184     5858   6904   5314  -2737    474    933       O  
HETATM 3228  O   HOH A2185      -6.942  -8.738  30.362  1.00 52.96           O  
ANISOU 3228  O   HOH A2185     6863   6148   7110   -340   1102   -870       O  
HETATM 3229  O   HOH A2186      12.540 -16.797   4.489  1.00 31.00           O  
ANISOU 3229  O   HOH A2186     6663   2162   2954    -32    269    321       O  
HETATM 3230  O   HOH A2187       7.839   4.745   4.460  1.00 25.46           O  
ANISOU 3230  O   HOH A2187     3044   4503   2127   1065    469    486       O  
HETATM 3231  O   HOH A2188      -3.231   8.625  26.740  1.00 40.49           O  
ANISOU 3231  O   HOH A2188     3920   4337   7129   1711   2452   -247       O  
HETATM 3232  O   HOH A2189      -7.934   6.124  31.828  1.00 41.52           O  
ANISOU 3232  O   HOH A2189     2863   6271   6642  -1498    398  -1046       O  
HETATM 3233  O   HOH A2190       9.172  15.701   6.053  1.00 41.03           O  
ANISOU 3233  O   HOH A2190     5967   5950   3673   -240    815   1736       O  
HETATM 3234  O   HOH A2191      11.976  13.964   6.112  1.00 31.04           O  
ANISOU 3234  O   HOH A2191     4781   3826   3187     56   -507   1979       O  
HETATM 3235  O   HOH A2192      37.725  -3.583  26.358  1.00 42.45           O  
ANISOU 3235  O   HOH A2192     3765   6386   5977   -612   1055  -1492       O  
HETATM 3236  O   HOH A2193      29.368  12.849  18.334  1.00 53.26           O  
ANISOU 3236  O   HOH A2193     7013   4894   8330  -2453   1226  -1877       O  
HETATM 3237  O   HOH A2194      42.020   0.899  34.215  1.00 39.14           O  
ANISOU 3237  O   HOH A2194     4895   5233   4743   2215  -2848   -919       O  
HETATM 3238  O   HOH A2195      29.117  -1.164  43.302  1.00 30.54           O  
ANISOU 3238  O   HOH A2195     3730   5571   2301     -8   -915   1223       O  
HETATM 3239  O   HOH A2196      27.265   0.522  45.073  1.00 57.80           O  
ANISOU 3239  O   HOH A2196     8096   8154   5712   2138    340   4629       O  
HETATM 3240  O   HOH A2197      29.117   2.286  46.208  1.00 52.45           O  
ANISOU 3240  O   HOH A2197     7642   8655   3633   -887    651    320       O  
HETATM 3241  O   HOH A2198      26.723  -2.287  43.996  1.00 55.00           O  
ANISOU 3241  O   HOH A2198     8166   7892   4841   -510    269   3574       O  
HETATM 3242  O   HOH A2199      23.347  14.108  37.869  1.00 37.23           O  
ANISOU 3242  O   HOH A2199     6724   2383   5040    -54   1573   -550       O  
HETATM 3243  O   HOH A2200      39.488  11.458  26.073  1.00 38.75           O  
ANISOU 3243  O   HOH A2200     3838   5988   4900  -1696   -562   1058       O  
HETATM 3244  O   HOH A2201      37.385   6.786  19.744  1.00 29.68           O  
ANISOU 3244  O   HOH A2201     2229   4092   4954    -64    455    344       O  
HETATM 3245  O   HOH A2202      20.345  12.411   2.759  1.00 55.97           O  
ANISOU 3245  O   HOH A2202     6119   7606   7542  -1445   1548   3554       O  
HETATM 3246  O   HOH A2203      14.641 -15.296  24.691  1.00 31.48           O  
ANISOU 3246  O   HOH A2203     7094   2413   2453     46    163   -269       O  
HETATM 3247  O   HOH A2204      16.582 -14.899  21.466  1.00 33.27           O  
ANISOU 3247  O   HOH A2204     2736   5957   3948   -983     93  -1784       O  
HETATM 3248  O   HOH A2205      14.901   5.327  42.298  1.00 40.28           O  
ANISOU 3248  O   HOH A2205     4212   6964   4130   1064    171   -237       O  
HETATM 3249  O   HOH A2206       3.558 -15.944  22.823  1.00 47.20           O  
ANISOU 3249  O   HOH A2206     5270   5241   7422   1693  -3977  -3656       O  
HETATM 3250  O   HOH A2207       5.783 -16.116  21.056  1.00 52.82           O  
ANISOU 3250  O   HOH A2207     5686   6339   8042    -94    678  -2093       O  
HETATM 3251  O   HOH A2208      31.788  -6.846  26.946  1.00 34.61           O  
ANISOU 3251  O   HOH A2208     2536   5217   5397    259   -298   1089       O  
HETATM 3252  O   HOH A2209      27.543  -8.616  12.276  1.00 55.93           O  
ANISOU 3252  O   HOH A2209     8619   8389   4243   2352     80   1482       O  
HETATM 3253  O   HOH A2210      28.286  -4.839  14.920  1.00 48.51           O  
ANISOU 3253  O   HOH A2210     6694   5402   6338   3285   1686  -1497       O  
HETATM 3254  O   HOH A2211      28.806  -7.127  16.726  1.00 32.28           O  
ANISOU 3254  O   HOH A2211     4126   4511   3628  -1526   1763  -1323       O  
HETATM 3255  O   HOH A2212      15.979   7.895   5.605  1.00 29.66           O  
ANISOU 3255  O   HOH A2212     4039   4929   2301   -860  -1117    917       O  
HETATM 3256  O   HOH A2213       1.092 -14.416  16.815  1.00 42.93           O  
ANISOU 3256  O   HOH A2213     6129   5788   4395  -1526    731  -1271       O  
HETATM 3257  O   HOH A2214      21.297  17.272  23.607  1.00 50.80           O  
ANISOU 3257  O   HOH A2214     5829   8548   4927    715   -495  -3104       O  
HETATM 3258  O   HOH A2215      21.283  14.953  25.823  1.00 35.62           O  
ANISOU 3258  O   HOH A2215     5326   4369   3840   -218  -1209    439       O  
HETATM 3259  O   HOH A2216      27.505 -13.981  21.525  1.00 56.44           O  
ANISOU 3259  O   HOH A2216     6641   6359   8445   2984  -1696   2195       O  
HETATM 3260  O   HOH A2217      24.359 -17.209  20.205  1.00 52.34           O  
ANISOU 3260  O   HOH A2217     9237   3945   6705    761  -2071    872       O  
HETATM 3261  O   HOH A2218      42.564   3.301  38.119  1.00 48.89           O  
ANISOU 3261  O   HOH A2218     4631   8875   5072   1641   -742  -1940       O  
HETATM 3262  O   HOH A2220      27.002   8.006  14.631  1.00 43.29           O  
ANISOU 3262  O   HOH A2220     7028   6684   2737  -1459  -1437    421       O  
HETATM 3263  O   HOH A2221      27.107 -14.497  36.903  1.00 50.40           O  
ANISOU 3263  O   HOH A2221     6458   5365   7328  -1539    729  -2166       O  
HETATM 3264  O   HOH A2222      27.225  -5.830  42.668  1.00 45.17           O  
ANISOU 3264  O   HOH A2222     5817   7933   3413   2780    -14   2062       O  
HETATM 3265  O   HOH A2223      31.882  -1.276  43.583  1.00 42.88           O  
ANISOU 3265  O   HOH A2223     4934   6103   5257    842   -451   1560       O  
HETATM 3266  O   HOH A2224      22.601  13.564  41.728  1.00 72.04           O  
ANISOU 3266  O   HOH A2224     8094   9771   9508   3210   3608  -1392       O  
HETATM 3267  O   HOH A2225      22.610  16.172  38.878  1.00 52.41           O  
ANISOU 3267  O   HOH A2225     6393   6823   6696   1499     76    944       O  
HETATM 3268  O   HOH A2226      20.968  18.946   5.691  1.00 54.47           O  
ANISOU 3268  O   HOH A2226     6513   7062   7124  -1060   1398    -14       O  
HETATM 3269  O   HOH A2227      20.185  10.314  41.186  1.00 44.53           O  
ANISOU 3269  O   HOH A2227     6333   4491   6096    846   2647    239       O  
HETATM 3270  O   HOH A2228      14.363  12.676  35.655  1.00 47.65           O  
ANISOU 3270  O   HOH A2228     5721   6779   5605   1284    894  -1556       O  
HETATM 3271  O   HOH A2229      -0.079  15.441  24.273  1.00 50.01           O  
ANISOU 3271  O   HOH A2229     7865   4757   6378   1529  -2559   -459       O  
HETATM 3272  O   HOH A2230      -0.865   8.753  33.538  1.00 48.95           O  
ANISOU 3272  O   HOH A2230     5030   5876   7693   -914   2520  -2738       O  
HETATM 3273  O   HOH A2231      -0.723   4.956  34.928  1.00 31.86           O  
ANISOU 3273  O   HOH A2231     5122   3391   3593   1185   1356    182       O  
HETATM 3274  O   HOH A2232      15.359 -14.305  17.399  1.00 21.63           O  
ANISOU 3274  O   HOH A2232     3413   1771   3034    125    876   -216       O  
HETATM 3275  O   HOH A2233      21.750 -14.143  26.211  1.00 33.35           O  
ANISOU 3275  O   HOH A2233     3549   3676   5448    865   1041    539       O  
HETATM 3276  O   HOH A2234      22.407 -14.719  23.221  1.00 47.84           O  
ANISOU 3276  O   HOH A2234     8047   2208   7921  -1655   1003    344       O  
HETATM 3277  O   HOH A2235      11.153 -15.334  43.529  1.00 26.64           O  
ANISOU 3277  O   HOH A2235     3951   3603   2568    777   -421  -1037       O  
HETATM 3278  O   HOH A2236      15.534  -5.557  49.857  1.00 24.16           O  
ANISOU 3278  O   HOH A2236     3248   2948   2983   -630   -455    408       O  
HETATM 3279  O   HOH A2237      11.822  -2.246  46.462  1.00 41.09           O  
ANISOU 3279  O   HOH A2237     3938   8243   3433   -133    219  -2932       O  
HETATM 3280  O   HOH A2238      12.920  -0.340  45.861  1.00 53.45           O  
ANISOU 3280  O   HOH A2238     9133   8322   2856    502   1226  -2669       O  
HETATM 3281  O   HOH A2239       9.861  -1.506  48.187  1.00 20.15           O  
ANISOU 3281  O   HOH A2239     3371   2467   1816    144    221   -288       O  
HETATM 3282  O   HOH A2240       6.956  -1.040  48.530  1.00 31.20           O  
ANISOU 3282  O   HOH A2240     3662   3805   4388   -130    533   1262       O  
HETATM 3283  O   HOH A2241       3.801 -15.009  20.742  1.00 57.91           O  
ANISOU 3283  O   HOH A2241     7920   4525   9559    587     -9  -1084       O  
HETATM 3284  O   HOH A2242       2.319 -14.988  43.363  1.00 42.92           O  
ANISOU 3284  O   HOH A2242     8245   5109   2954  -2738    875    384       O  
HETATM 3285  O   HOH A2243      -4.350   1.713  35.670  1.00 49.97           O  
ANISOU 3285  O   HOH A2243     7848   7686   3453   -285   1659    323       O  
HETATM 3286  O   HOH A2244       6.602   2.117   9.909  1.00 58.43           O  
ANISOU 3286  O   HOH A2244     8457   9872   3872    469   -356  -1819       O  
HETATM 3287  O   HOH A2245       0.060 -12.090   9.432  1.00 36.58           O  
ANISOU 3287  O   HOH A2245     3293   3732   6873   -989    935  -1055       O  
HETATM 3288  O   HOH A2246       9.741 -15.312   2.116  1.00 44.04           O  
ANISOU 3288  O   HOH A2246     5671   5406   5656  -1098   -114  -2231       O  
HETATM 3289  O   HOH A2247      21.785 -11.060  -1.171  1.00 59.44           O  
ANISOU 3289  O   HOH A2247     6754   6806   9025   3032   1847   -333       O  
HETATM 3290  O   HOH A2248      19.919  -7.478   1.153  1.00 55.50           O  
ANISOU 3290  O   HOH A2248     7907   8043   5137    -69   3389    842       O  
HETATM 3291  O   HOH A2251      -2.068  12.045  24.625  1.00 61.25           O  
ANISOU 3291  O   HOH A2251     8817   8575   5879    435    707    615       O  
HETATM 3292  O   HOH A2252      24.393   8.776  13.854  1.00 41.52           O  
ANISOU 3292  O   HOH A2252     3849   4726   7201  -1590   -141   2287       O  
HETATM 3293  O   HOH A2253      13.953  14.694  26.618  1.00 35.73           O  
ANISOU 3293  O   HOH A2253     3811   2063   7700    961   1879    614       O  
HETATM 3294  O   HOH A2254      10.353  21.368  21.632  1.00 47.88           O  
ANISOU 3294  O   HOH A2254     6022   6504   5666   1026  -1485  -1788       O  
HETATM 3295  O   HOH A2255      30.791 -10.379  23.666  1.00 42.76           O  
ANISOU 3295  O   HOH A2255     2494   7134   6620  -1437    970  -2433       O  
HETATM 3296  O   HOH A2256      32.676 -11.053  21.685  1.00 46.69           O  
ANISOU 3296  O   HOH A2256     3650   7634   6454   -918    652    534       O  
HETATM 3297  O   HOH A2257      40.024  -0.866  25.029  1.00 36.73           O  
ANISOU 3297  O   HOH A2257     5993   3899   4062   -325    144    672       O  
HETATM 3298  O   HOH A2258      42.035  -3.718  26.374  1.00 40.70           O  
ANISOU 3298  O   HOH A2258     2943   9351   3171  -1706   -969  -1263       O  
HETATM 3299  O   HOH A2259      43.769  -7.516  26.883  1.00 40.08           O  
ANISOU 3299  O   HOH A2259     5396   6155   3678   -245   -643   -473       O  
HETATM 3300  O   HOH A2260      37.069  -0.711  38.251  1.00 33.62           O  
ANISOU 3300  O   HOH A2260     4640   2801   5333    133    972    182       O  
HETATM 3301  O   HOH A2261      31.952  -6.320  34.324  1.00 51.11           O  
ANISOU 3301  O   HOH A2261     5268   6927   7223    654   2091    636       O  
HETATM 3302  O   HOH A2262      19.522 -17.706  39.259  1.00 48.29           O  
ANISOU 3302  O   HOH A2262     6660   3692   7996   1549    -83   -500       O  
HETATM 3303  O   HOH A2263      30.451  20.831  28.811  1.00 27.40           O  
ANISOU 3303  O   HOH A2263     6203   1631   2578    -61   -293    698       O  
HETATM 3304  O   HOH A2264      39.239   9.747  24.236  1.00 42.32           O  
ANISOU 3304  O   HOH A2264     3746   5891   6441    -43    134   2020       O  
HETATM 3305  O   HOH A2265      14.540 -19.224  36.786  1.00 43.33           O  
ANISOU 3305  O   HOH A2265     6631   4100   5734   1246  -1721   -656       O  
HETATM 3306  O   HOH A2266      15.825 -22.083  35.900  1.00 55.17           O  
ANISOU 3306  O   HOH A2266     7183   7908   5871   2519  -1051  -2165       O  
HETATM 3307  O   HOH A2267      21.372 -22.067  34.194  1.00 51.50           O  
ANISOU 3307  O   HOH A2267     7914   7282   4372   1064   -214   -397       O  
HETATM 3308  O   HOH A2268      14.661   1.613  -3.116  1.00 45.77           O  
ANISOU 3308  O   HOH A2268     7574   5690   4127  -1505     92    658       O  
HETATM 3309  O   HOH A2269      17.329  -0.172  -2.289  1.00 31.20           O  
ANISOU 3309  O   HOH A2269     6164   3509   2181  -1346      1   -183       O  
HETATM 3310  O   HOH A2270      21.894  -0.199   0.201  1.00 50.08           O  
ANISOU 3310  O   HOH A2270     5627   8509   4891  -1625   -337  -1124       O  
HETATM 3311  O   HOH A2271      18.459   4.069  -3.417  1.00 33.54           O  
ANISOU 3311  O   HOH A2271     4350   4359   4035    540   1970    113       O  
HETATM 3312  O   HOH A2272      14.407 -12.300  19.681  1.00 33.72           O  
ANISOU 3312  O   HOH A2272     4135   4755   3922   -293    208   -934       O  
HETATM 3313  O   HOH A2273      20.212 -17.314  10.392  1.00 40.03           O  
ANISOU 3313  O   HOH A2273     5369   3811   6030    389  -1313   1188       O  
HETATM 3314  O   HOH A2274      19.849 -12.286  12.858  1.00 37.98           O  
ANISOU 3314  O   HOH A2274     4926   3962   5542  -1004    -55    246       O  
HETATM 3315  O   HOH A2275      16.047 -16.727  23.584  1.00 36.43           O  
ANISOU 3315  O   HOH A2275     4428   5849   3563   -571    -43   -990       O  
HETATM 3316  O   HOH A2276      18.714 -16.436  24.648  1.00 32.58           O  
ANISOU 3316  O   HOH A2276     5882   2750   3748   1391    573   -651       O  
HETATM 3317  O   HOH A2277       8.465 -21.343  28.915  1.00 30.04           O  
ANISOU 3317  O   HOH A2277     3019   2984   5410   -479   1009    939       O  
HETATM 3318  O   HOH A2278      -4.697  -7.951  33.749  1.00 56.68           O  
ANISOU 3318  O   HOH A2278     6276   7809   7453   1001   3861   -387       O  
HETATM 3319  O   HOH A2279      -5.532   0.062  37.398  1.00 66.94           O  
ANISOU 3319  O   HOH A2279     7487   9557   8389   2710  -1007   2335       O  
HETATM 3320  O   HOH A2280      -4.681 -12.541  19.632  1.00 57.47           O  
ANISOU 3320  O   HOH A2280     6330   6920   8585  -1822   -390   2812       O  
HETATM 3321  O   HOH A2281      -5.920  -8.846  23.896  1.00 29.60           O  
ANISOU 3321  O   HOH A2281     2404   4825   4018    -41   1006    298       O  
HETATM 3322  O   HOH A2282       0.853   2.573   2.321  1.00 51.05           O  
ANISOU 3322  O   HOH A2282     6539   5365   7493   2179     55  -1239       O  
HETATM 3323  O   HOH A2283      -3.407   6.218   6.504  1.00 47.44           O  
ANISOU 3323  O   HOH A2283     7192   6545   4290   3045  -1713   -559       O  
HETATM 3324  O   HOH A2284      -2.702   1.414   3.565  1.00 61.47           O  
ANISOU 3324  O   HOH A2284     7951   8867   6537   -116   1606   1524       O  
HETATM 3325  O   HOH A2285       3.411  13.781   4.139  1.00 53.44           O  
ANISOU 3325  O   HOH A2285     4973   8045   7286   2197   -420   2882       O  
HETATM 3326  O   HOH A2286      -6.722  10.808  12.192  1.00 50.22           O  
ANISOU 3326  O   HOH A2286     6525   4761   7795   1023  -2512    961       O  
HETATM 3327  O   HOH A2287      -8.052  14.617   9.395  1.00 47.45           O  
ANISOU 3327  O   HOH A2287     6087   5033   6907    412  -1017  -1288       O  
HETATM 3328  O   HOH A2288      31.175  -3.344  23.705  1.00 45.68           O  
ANISOU 3328  O   HOH A2288     5763   5923   5669    887  -2308  -1160       O  
HETATM 3329  O   HOH A2289      43.226   3.395  32.192  1.00 52.58           O  
ANISOU 3329  O   HOH A2289     4975   6397   8605   -924    812  -1274       O  
HETATM 3330  O   HOH A2290      28.826  -7.775  39.659  1.00 54.92           O  
ANISOU 3330  O   HOH A2290     7470   6817   6578   2598    674   -836       O  
HETATM 3331  O   HOH A2291      25.853  16.235  30.798  1.00 54.60           O  
ANISOU 3331  O   HOH A2291    10142   4121   6483   2016   2202   2420       O  
HETATM 3332  O   HOH A2292      24.676   0.196   7.779  1.00 39.07           O  
ANISOU 3332  O   HOH A2292     2143   6817   5883    449    374  -1206       O  
HETATM 3333  O   HOH A2293      10.503   5.286   1.695  1.00 42.96           O  
ANISOU 3333  O   HOH A2293     5930   6898   3492   1276   -566   1831       O  
HETATM 3334  O   HOH A2294      16.415   4.590   3.960  1.00 46.10           O  
ANISOU 3334  O   HOH A2294     6592   4981   5942  -3193  -3247   3491       O  
HETATM 3335  O   HOH A2295      10.246  15.696  29.472  1.00 38.37           O  
ANISOU 3335  O   HOH A2295     5641   3886   5050  -2425  -1204   1052       O  
HETATM 3336  O   HOH A2296      10.237  16.212  26.196  1.00 49.56           O  
ANISOU 3336  O   HOH A2296     6483   6984   5363   -742   2125    636       O  
HETATM 3337  O   HOH A2297      10.377 -22.383  29.914  1.00 55.13           O  
ANISOU 3337  O   HOH A2297     4289   8922   7736    797    452  -3415       O  
HETATM 3338  O   HOH A2298      12.210 -22.504  34.632  1.00 50.96           O  
ANISOU 3338  O   HOH A2298     8389   5481   5492  -2481    271   2726       O  
HETATM 3339  O   HOH A2299       7.433 -23.528  32.791  1.00 50.76           O  
ANISOU 3339  O   HOH A2299     4370   5860   9056   1086   -610     52       O  
HETATM 3340  O   HOH A2300       6.024 -20.060  35.392  1.00 55.66           O  
ANISOU 3340  O   HOH A2300     8905   4816   7426  -1275   2258   2936       O  
HETATM 3341  O   HOH A2301      16.102 -22.507  33.048  1.00 45.65           O  
ANISOU 3341  O   HOH A2301     7600   3701   6045    740   2017   -419       O  
HETATM 3342  O   HOH A2304       9.517 -19.909  21.213  1.00 34.99           O  
ANISOU 3342  O   HOH A2304     4058   4281   4957    508    330   -315       O  
HETATM 3343  O   HOH A2305       4.886 -15.931  13.668  1.00 35.37           O  
ANISOU 3343  O   HOH A2305     3375   4699   5364   -389    490  -1756       O  
HETATM 3344  O   HOH A2306      -1.780 -11.264  11.694  1.00 37.60           O  
ANISOU 3344  O   HOH A2306     5461   4006   4819   -396    -59     59       O  
HETATM 3345  O   HOH A2307      -7.851  -3.037  12.458  1.00 35.75           O  
ANISOU 3345  O   HOH A2307     2760   6956   3868   -308   -590    324       O  
HETATM 3346  O  BHOH A2309      -3.595 -12.158  16.768  0.50 42.18           O  
ANISOU 3346  O  BHOH A2309     4243   6076   5707  -2373    209   2177       O  
HETATM 3347  O   HOH A2310      -4.690 -12.696  28.682  1.00 40.85           O  
ANISOU 3347  O   HOH A2310     5402   6420   3699  -1288   -175   1357       O  
HETATM 3348  O   HOH A2311      -5.490 -13.095  30.803  1.00 37.67           O  
ANISOU 3348  O   HOH A2311     3315   6390   4607   -889    706   1002       O  
HETATM 3349  O   HOH A2312      -3.203 -16.704  30.270  1.00 35.93           O  
ANISOU 3349  O   HOH A2312     4326   5461   3866  -1122   -484   -952       O  
HETATM 3350  O  AHOH A2313       1.976 -12.412   2.766  0.50 30.67           O  
ANISOU 3350  O  AHOH A2313     3433   4216   4004     82  -1730  -1064       O  
HETATM 3351  O  AHOH A2314      -1.555 -11.611   6.863  0.50 34.15           O  
ANISOU 3351  O  AHOH A2314     3894   5069   4012   -412    555  -1412       O  
HETATM 3352  O  BHOH A2315      -1.817  -9.893   5.458  0.50 34.17           O  
ANISOU 3352  O  BHOH A2315     3495   4574   4915   -664  -1092   -964       O  
HETATM 3353  O   HOH A2316       8.446 -16.348   4.352  1.00 49.68           O  
ANISOU 3353  O   HOH A2316     6396   4196   8285    713    551  -2502       O  
HETATM 3354  O   HOH A2317       5.878 -16.234  17.636  1.00 41.58           O  
ANISOU 3354  O   HOH A2317     6135   4834   4830  -1414  -1039   -170       O  
HETATM 3355  O   HOH A2318       7.578 -17.926  16.291  1.00 34.51           O  
ANISOU 3355  O   HOH A2318     5927   3934   3252     59    953    930       O  
HETATM 3356  O   HOH A2319      -7.185   7.811  15.367  1.00 44.49           O  
ANISOU 3356  O   HOH A2319     6892   3939   6072   2277   -114   -189       O  
HETATM 3357  O  AHOH A2320      -6.015   6.928  13.083  0.50 27.97           O  
ANISOU 3357  O  AHOH A2320     3493   3575   3559   1894   -835   -390       O  
HETATM 3358  O   HOH A2321      -3.646   8.999   7.629  1.00 37.54           O  
ANISOU 3358  O   HOH A2321     5409   3748   5106    -64  -1934    727       O  
HETATM 3359  O  AHOH A2324      12.640  19.749  11.843  0.50 39.13           O  
ANISOU 3359  O  AHOH A2324     4144   6651   4073   2244   -938   1339       O  
HETATM 3360  O   HOH A2327      16.450  20.268  23.996  1.00 42.39           O  
ANISOU 3360  O   HOH A2327     4335   4851   6919  -1387  -1425   -413       O  
HETATM 3361  O   HOH A2328      30.364  -8.829  15.603  1.00 39.51           O  
ANISOU 3361  O   HOH A2328     5483   3574   5953    579    126   -650       O  
HETATM 3362  O   HOH A2329      31.676 -10.814  26.095  1.00 51.90           O  
ANISOU 3362  O   HOH A2329     8080   6090   5551   2124  -1061    960       O  
HETATM 3363  O   HOH A2330      37.348  -1.706  24.578  1.00 43.90           O  
ANISOU 3363  O   HOH A2330     3943   6265   6471   1429   1226    -98       O  
HETATM 3364  O   HOH A2331      38.618  13.947  36.374  1.00 51.41           O  
ANISOU 3364  O   HOH A2331     7548   4143   7841   1562   1555   2321       O  
HETATM 3365  O   HOH A2332      38.829   9.846  33.264  1.00 39.80           O  
ANISOU 3365  O   HOH A2332     3987   5296   5841  -1367   -842    287       O  
HETATM 3366  O   HOH A2333      39.186   8.405  36.023  1.00 51.99           O  
ANISOU 3366  O   HOH A2333     5332   7602   6819  -1289   -701    799       O  
HETATM 3367  O   HOH A2334      35.262  -0.262  40.610  1.00 52.14           O  
ANISOU 3367  O   HOH A2334     3113   6882   9814    994   -985   3673       O  
HETATM 3368  O   HOH A2335      33.518  -3.377  37.356  1.00 33.56           O  
ANISOU 3368  O   HOH A2335     3867   4151   4733   1831   -401    834       O  
HETATM 3369  O   HOH A2336      23.419  16.180  34.854  1.00 60.35           O  
ANISOU 3369  O   HOH A2336     8064   7021   7844   1494   1156    723       O  
HETATM 3370  O   HOH A2337      26.762  19.943  33.713  1.00 52.95           O  
ANISOU 3370  O   HOH A2337     7708   4129   8283   -571  -3578    512       O  
HETATM 3371  O  AHOH A2339      30.080   7.021  44.717  0.50 35.73           O  
ANISOU 3371  O  AHOH A2339     2783   5575   5216    866   -970  -1148       O  
HETATM 3372  O   HOH A2340      38.179  11.282  21.256  1.00 42.01           O  
ANISOU 3372  O   HOH A2340     6558   4581   4824  -1755   1552    855       O  
HETATM 3373  O   HOH A2341      31.661  -7.600  14.154  1.00 48.82           O  
ANISOU 3373  O   HOH A2341     7296   5578   5675    893   1973   -357       O  
HETATM 3374  O   HOH A2342      22.077   5.865  -1.757  1.00 44.70           O  
ANISOU 3374  O   HOH A2342     7006   6671   3305  -2328    547  -1603       O  
HETATM 3375  O  AHOH A2343       0.537  11.551  22.739  0.50 21.52           O  
ANISOU 3375  O  AHOH A2343     2599   3279   2300   -306    105   -550       O  
HETATM 3376  O   HOH A2344      14.559  18.232  25.653  1.00 58.52           O  
ANISOU 3376  O   HOH A2344     9160   6829   6246   1232   2748    151       O  
HETATM 3377  O   HOH A2345      18.665  18.802  24.584  1.00 49.10           O  
ANISOU 3377  O   HOH A2345     6749   3928   7980  -2163  -1848   2167       O  
HETATM 3378  O   HOH A2346      -5.970   7.718  26.385  1.00 60.06           O  
ANISOU 3378  O   HOH A2346     4377   9383   9059   -819   2403   -678       O  
HETATM 3379  O   HOH A2348      -1.007   6.485  32.322  1.00 31.17           O  
ANISOU 3379  O   HOH A2348     2787   4250   4807    690   1340   -268       O  
HETATM 3380  O   HOH A2349      23.092 -16.360  37.150  1.00 48.11           O  
ANISOU 3380  O   HOH A2349     9081   2536   6663   -460   -205  -1248       O  
HETATM 3381  O   HOH A2350      30.090 -14.878  36.168  1.00 46.82           O  
ANISOU 3381  O   HOH A2350     7115   4485   6189    819   -437  -2207       O  
HETATM 3382  O   HOH A2351      25.991 -15.553  38.603  1.00 46.34           O  
ANISOU 3382  O   HOH A2351     5696   4834   7076    826   1991  -1088       O  
HETATM 3383  O   HOH A2352      12.814   4.163  41.994  1.00 53.44           O  
ANISOU 3383  O   HOH A2352     8723   4836   6746   1243   1136  -1382       O  
HETATM 3384  O   HOH A2353       5.280 -18.199  13.727  1.00 47.53           O  
ANISOU 3384  O   HOH A2353     4422   5339   8297   -442   1730  -1157       O  
HETATM 3385  O   HOH A2355      -6.374  -2.052  33.655  1.00 47.54           O  
ANISOU 3385  O   HOH A2355     7106   6800   4158  -2144   1674    577       O  
HETATM 3386  O   HOH A2356      30.798  13.918  40.718  1.00 45.61           O  
ANISOU 3386  O   HOH A2356     5068   7416   4843  -3162    -57  -2697       O  
HETATM 3387  O   HOH A2357      30.445  16.156  40.326  1.00 53.77           O  
ANISOU 3387  O   HOH A2357     7363   8193   4875  -2285   1906  -3552       O  
HETATM 3388  O   HOH A2358      18.671 -16.582  35.833  1.00 42.66           O  
ANISOU 3388  O   HOH A2358     7680   2650   5881    247    157    397       O  
HETATM 3389  O   HOH A2359      10.461  11.472  39.332  1.00 49.28           O  
ANISOU 3389  O   HOH A2359     7827   6025   4871   2771    -40  -2338       O  
HETATM 3390  O   HOH A2360      15.852 -15.602  42.652  1.00 61.77           O  
ANISOU 3390  O   HOH A2360     8313   5354   9801   3436   -916  -1674       O  
HETATM 3391  O   HOH A2361      17.864 -17.632  41.956  1.00 63.88           O  
ANISOU 3391  O   HOH A2361     7013   9328   7929   1777   1288    993       O  
HETATM 3392  O   HOH A2362      -4.831 -15.142  41.758  1.00 62.12           O  
ANISOU 3392  O   HOH A2362     7272   9176   7154  -1967  -1723  -2751       O  
HETATM 3393  O   HOH A2363      -5.500  -3.757  36.557  1.00 54.49           O  
ANISOU 3393  O   HOH A2363     5495   7700   7509  -1744    551  -1088       O  
HETATM 3394  O   HOH A2364       3.563   5.893  41.053  1.00 52.57           O  
ANISOU 3394  O   HOH A2364     5432   6592   7951   -715   1724   1542       O  
HETATM 3395  O   HOH A2365       7.425   6.481  41.385  1.00 53.45           O  
ANISOU 3395  O   HOH A2365     8580   6309   5418  -1027  -3037    364       O  
HETATM 3396  O   HOH A2366       8.496   1.032   5.881  1.00 31.42           O  
ANISOU 3396  O   HOH A2366     3977   5824   2139  -1977  -1042   1794       O  
HETATM 3397  O   HOH A2367       0.852 -14.729   9.740  1.00 46.13           O  
ANISOU 3397  O   HOH A2367     4580   6482   6467    289    906     27       O  
HETATM 3398  O   HOH A2368      -0.189 -16.059   7.721  1.00 58.10           O  
ANISOU 3398  O   HOH A2368     5432   8836   7806   -771  -2362    754       O  
HETATM 3399  O   HOH A2369       7.497   9.088   1.784  1.00 60.59           O  
ANISOU 3399  O   HOH A2369     7847   6256   8916   2104  -1372    151       O  
HETATM 3400  O   HOH A2370      -9.415   8.909  22.439  1.00 41.76           O  
ANISOU 3400  O   HOH A2370     6451   3927   5487   1402   1738    720       O  
HETATM 3401  O   HOH A2371      -6.447  10.381  23.684  1.00 49.79           O  
ANISOU 3401  O   HOH A2371     5971   7513   5436   2816   2405    738       O  
HETATM 3402  O   HOH A2372     -11.122  -1.729  21.857  1.00 51.37           O  
ANISOU 3402  O   HOH A2372     5592   6439   7488  -1201    307   2612       O  
HETATM 3403  O   HOH A2373      -6.781  -6.967  22.908  1.00 59.68           O  
ANISOU 3403  O   HOH A2373     4893   8148   9634   -279   -361   -215       O  
HETATM 3404  O   HOH A2374      24.913  18.294  12.753  1.00 46.11           O  
ANISOU 3404  O   HOH A2374     6110   6948   4461  -1682    504  -1192       O  
HETATM 3405  O   HOH A2375      39.891  -4.455  27.169  1.00 43.24           O  
ANISOU 3405  O   HOH A2375     4580   4421   7430   -729   1103   -773       O  
HETATM 3406  O   HOH A2376      37.437   1.803  43.986  1.00 48.16           O  
ANISOU 3406  O   HOH A2376     8325   5152   4821    786  -1843   1589       O  
HETATM 3407  O   HOH A2377      35.703   0.306  43.928  1.00 62.43           O  
ANISOU 3407  O   HOH A2377     7809   6764   9147   1958   -299    784       O  
HETATM 3408  O   HOH A2378      23.179  11.300  42.343  1.00 48.92           O  
ANISOU 3408  O   HOH A2378     6083   6437   6068   1131   -169     98       O  
HETATM 3409  O   HOH A2381      15.691   4.860   0.151  1.00 44.34           O  
ANISOU 3409  O   HOH A2381     7565   4837   4445   1402    395    468       O  
HETATM 3410  O   HOH A2382      21.563  12.944   7.891  1.00 47.38           O  
ANISOU 3410  O   HOH A2382     3523   9342   5138   -852    694  -1729       O  
HETATM 3411  O   HOH A2383      23.398  11.512   5.615  1.00 49.00           O  
ANISOU 3411  O   HOH A2383     6161   5034   7423    721  -1290  -1610       O  
HETATM 3412  O   HOH A2384      21.022   9.991   1.793  1.00 55.05           O  
ANISOU 3412  O   HOH A2384     6484   9242   5192   -731   1469   -318       O  
HETATM 3413  O  AHOH A2385      23.190   7.411  11.838  0.50 41.48           O  
ANISOU 3413  O  AHOH A2385     4865   4857   6038     71    569     74       O  
HETATM 3414  O   HOH A2386      26.153   2.751  11.167  1.00 36.97           O  
ANISOU 3414  O   HOH A2386     3726   6831   3491   -584   1459    392       O  
HETATM 3415  O   HOH A2387      27.428   5.823  13.194  1.00 48.36           O  
ANISOU 3415  O   HOH A2387     7684   6788   3901   -341   1881    358       O  
HETATM 3416  O   HOH A2388      27.424  16.624  35.111  1.00 41.49           O  
ANISOU 3416  O   HOH A2388     4673   6388   4703  -1198   -179    614       O  
HETATM 3417  O  AHOH A2389      22.519 -13.760  41.095  0.56 17.67           O  
ANISOU 3417  O  AHOH A2389     3125   1873   1718    804   -199    491       O  
HETATM 3418  O   HOH A2390      26.384  -7.406  44.105  1.00 62.36           O  
ANISOU 3418  O   HOH A2390     7436   8034   8224   -263  -1660   -484       O  
HETATM 3419  O  BHOH A2391      39.937  -4.969  31.279  0.50 24.99           O  
ANISOU 3419  O  BHOH A2391     1415   3822   4260   -138   -388   1229       O  
HETATM 3420  O   HOH A2392      29.060 -14.778  16.539  1.00 47.41           O  
ANISOU 3420  O   HOH A2392     6940   3347   7726   1996    435   1035       O  
HETATM 3421  O   HOH A2393       7.679  18.836  18.041  1.00 42.52           O  
ANISOU 3421  O   HOH A2393     4349   4506   7300   -391  -2364   1492       O  
HETATM 3422  O   HOH A2394       1.037  -3.999   1.709  1.00 54.45           O  
ANISOU 3422  O   HOH A2394     9404   7567   3718   -197    344  -2175       O  
HETATM 3423  O   HOH A2398       7.312 -16.741  19.331  1.00 44.68           O  
ANISOU 3423  O   HOH A2398     6188   5991   4797   1294   -886   -495       O  
HETATM 3424  O   HOH A2399       9.913 -18.899  23.303  1.00 37.00           O  
ANISOU 3424  O   HOH A2399     7823   2203   4033   1973  -1044   -405       O  
HETATM 3425  O   HOH A2400      24.583  -8.433   9.614  1.00 31.12           O  
ANISOU 3425  O   HOH A2400     4167   5149   2507   2022      5    335       O  
HETATM 3426  O   HOH A2401      22.079 -10.495   7.563  1.00 31.68           O  
ANISOU 3426  O   HOH A2401     4692   3945   3401   1258    263     16       O  
HETATM 3427  O   HOH A2402      -1.588  15.501  20.515  1.00 43.83           O  
ANISOU 3427  O   HOH A2402     3184   8590   4881   2486   -502   1260       O  
HETATM 3428  O   HOH A2403      22.963   2.577  45.918  1.00 35.70           O  
ANISOU 3428  O   HOH A2403     7090   3439   3037      5    605   -646       O  
HETATM 3429  O   HOH A2404      26.672  15.257  28.699  1.00 37.11           O  
ANISOU 3429  O   HOH A2404     4464   4945   4691  -1193   -263   1356       O  
HETATM 3430  O   HOH A2405      23.923  -3.569   8.212  1.00 40.61           O  
ANISOU 3430  O   HOH A2405     7098   4342   3990    226   -729    303       O  
HETATM 3431  O   HOH A2406      20.616 -13.212   4.509  1.00 34.98           O  
ANISOU 3431  O   HOH A2406     5656   4373   3260   2311  -1500   -703       O  
HETATM 3432  O  AHOH A2407       8.607 -20.528  31.908  0.50 32.00           O  
ANISOU 3432  O  AHOH A2407     4850   3361   3949    693   -752   1214       O  
HETATM 3433  O  AHOH A2410      24.323  -8.723  12.472  0.50 26.52           O  
ANISOU 3433  O  AHOH A2410     3042   4547   2486    906     22   1183       O  
HETATM 3434  O  AHOH A2411      16.479 -21.543  30.510  0.50 27.37           O  
ANISOU 3434  O  AHOH A2411     3567   1381   5450    300    106   -355       O  
HETATM 3435  O   HOH A2413      29.500  17.336  29.825  1.00 40.12           O  
ANISOU 3435  O   HOH A2413     3759   3388   8096    569    752   2497       O  
HETATM 3436  O  AHOH A2415      -5.104 -10.997  14.548  0.50 32.45           O  
ANISOU 3436  O  AHOH A2415     4159   3974   4196    252  -1007  -1348       O  
HETATM 3437  O   HOH A2416      14.280 -23.548  31.503  1.00 51.25           O  
ANISOU 3437  O   HOH A2416     8069   5173   6232   3638    247   -410       O  
HETATM 3438  O   HOH A2417      29.401 -16.424  40.291  1.00 49.77           O  
ANISOU 3438  O   HOH A2417     8387   4425   6097   1113    922  -3514       O  
HETATM 3439  O   HOH A2418       1.635 -10.506   1.531  1.00 45.43           O  
ANISOU 3439  O   HOH A2418     5804   8709   2748  -3638     99   1283       O  
HETATM 3440  O  AHOH A2422      24.577 -15.919  22.285  0.50 29.90           O  
ANISOU 3440  O  AHOH A2422     3404   4486   3471     -9   -227    964       O  
HETATM 3441  O  AHOH A2423       6.489  14.129  21.702  0.43 17.02           O  
ANISOU 3441  O  AHOH A2423     2305   1936   2226     73    -69   -284       O  
HETATM 3442  O  BHOH A2424      26.632  -8.417  39.912  0.44 27.81           O  
ANISOU 3442  O  BHOH A2424     3219   2839   4508   -304    331     14       O  
HETATM 3443  O  BHOH A2425      25.439 -13.838  40.704  0.44 27.19           O  
ANISOU 3443  O  BHOH A2425     3417   3012   3903   1550  -1386   -657       O  
HETATM 3444  O  AHOH A2426      14.221  14.896  32.822  0.53 44.18           O  
ANISOU 3444  O  AHOH A2426     5835   4781   6171   -757  -1803  -1546       O  
HETATM 3445  O   HOH A2427      19.214  -1.830  -2.570  1.00 35.14           O  
ANISOU 3445  O   HOH A2427     4841   3858   4653   -627  -2388    150       O  
HETATM 3446  O  AHOH A2428      16.632 -18.394  25.093  0.50 21.13           O  
ANISOU 3446  O  AHOH A2428     3358   2290   2379    869    129   -722       O  
HETATM 3447  O  AHOH A2429      25.390 -17.164  18.159  0.50 41.27           O  
ANISOU 3447  O  AHOH A2429     7034   1105   7541    975   1461   -456       O  
CONECT 2976 2977 2978 2979 2998                                                 
CONECT 2977 2976                                                                
CONECT 2978 2976                                                                
CONECT 2979 2976 2980                                                           
CONECT 2980 2979 2981                                                           
CONECT 2981 2980 2982 2983                                                      
CONECT 2982 2981 2987                                                           
CONECT 2983 2981 2984 2985                                                      
CONECT 2984 2983                                                                
CONECT 2985 2983 2986 2987                                                      
CONECT 2986 2985 3020                                                           
CONECT 2987 2982 2985 2988                                                      
CONECT 2988 2987 2989 2997                                                      
CONECT 2989 2988 2990                                                           
CONECT 2990 2989 2991                                                           
CONECT 2991 2990 2992 2997                                                      
CONECT 2992 2991 2993 2994                                                      
CONECT 2993 2992                                                                
CONECT 2994 2992 2995                                                           
CONECT 2995 2994 2996                                                           
CONECT 2996 2995 2997                                                           
CONECT 2997 2988 2991 2996                                                      
CONECT 2998 2976 2999                                                           
CONECT 2999 2998 3000 3001 3002                                                 
CONECT 3000 2999                                                                
CONECT 3001 2999                                                                
CONECT 3002 2999 3003                                                           
CONECT 3003 3002 3004                                                           
CONECT 3004 3003 3005 3006                                                      
CONECT 3005 3004 3010                                                           
CONECT 3006 3004 3007 3008                                                      
CONECT 3007 3006                                                                
CONECT 3008 3006 3009 3010                                                      
CONECT 3009 3008                                                                
CONECT 3010 3005 3008 3011                                                      
CONECT 3011 3010 3012 3019                                                      
CONECT 3012 3011 3013                                                           
CONECT 3013 3012 3014 3017                                                      
CONECT 3014 3013 3015 3016                                                      
CONECT 3015 3014                                                                
CONECT 3016 3014                                                                
CONECT 3017 3013 3018                                                           
CONECT 3018 3017 3019                                                           
CONECT 3019 3011 3018                                                           
CONECT 3020 2986 3021 3022 3023                                                 
CONECT 3021 3020                                                                
CONECT 3022 3020                                                                
CONECT 3023 3020                                                                
CONECT 3024 3026 3027                                                           
CONECT 3025 3028 3029                                                           
CONECT 3026 3024 3029 3033                                                      
CONECT 3027 3024 3028                                                           
CONECT 3028 3025 3027                                                           
CONECT 3029 3025 3026 3030                                                      
CONECT 3030 3029 3034 3035                                                      
CONECT 3031 3032 3035 3049                                                      
CONECT 3032 3031 3043                                                           
CONECT 3033 3026 3034 3037                                                      
CONECT 3034 3030 3033                                                           
CONECT 3035 3030 3031                                                           
CONECT 3036 3044                                                                
CONECT 3037 3033 3046                                                           
CONECT 3038 3042                                                                
CONECT 3039 3045                                                                
CONECT 3040 3042 3043 3049                                                      
CONECT 3041 3044 3045                                                           
CONECT 3042 3038 3040 3045                                                      
CONECT 3043 3032 3040 3044                                                      
CONECT 3044 3036 3041 3043                                                      
CONECT 3045 3039 3041 3042                                                      
CONECT 3046 3037 3047 3048                                                      
CONECT 3047 3046                                                                
CONECT 3048 3046                                                                
CONECT 3049 3031 3040                                                           
MASTER      274    0    2   16   10    0   13    6 3446    1   74   25          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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.