CNRS Nantes University US2B US2B
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***  5MNE_1  ***

elNémo ID: 240918111408862086

Job options:

ID        	=	 240918111408862086
JOBID     	=	 5MNE_1
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 5MNE_1

HEADER    HYDROLASE                               13-DEC-16   5MNE              
TITLE     CATIONIC TRYPSIN IN ITS APO FORM (DEUTERATED SAMPLE AT 100 K)         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CATIONIC TRYPSIN;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BETA-TRYPSIN;                                               
COMPND   5 EC: 3.4.21.4                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    HYDROGEN BONDING, PROTONATION, PROTEIN-LIGAND INTERACTION, HYDROLASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHIEBEL,A.HEINE,G.KLEBE                                            
REVDAT   3   17-JAN-24 5MNE    1       REMARK                                   
REVDAT   2   12-SEP-18 5MNE    1       JRNL                                     
REVDAT   1   17-JAN-18 5MNE    0                                                
JRNL        AUTH   J.SCHIEBEL,R.GASPARI,T.WULSDORF,K.NGO,C.SOHN,T.E.SCHRADER,   
JRNL        AUTH 2 A.CAVALLI,A.OSTERMANN,A.HEINE,G.KLEBE                        
JRNL        TITL   INTRIGUING ROLE OF WATER IN PROTEIN-LIGAND BINDING STUDIED   
JRNL        TITL 2 BY NEUTRON CRYSTALLOGRAPHY ON TRYPSIN COMPLEXES.             
JRNL        REF    NAT COMMUN                    V.   9  3559 2018              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30177695                                                     
JRNL        DOI    10.1038/S41467-018-05769-2                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155)                                 
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.75                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 110662                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.107                           
REMARK   3   R VALUE            (WORKING SET) : 0.106                           
REMARK   3   FREE R VALUE                     : 0.125                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5532                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 24.7559 -  3.1287    0.97     3735   198  0.1209 0.1395        
REMARK   3     2  3.1287 -  2.4841    0.99     3624   191  0.1228 0.1399        
REMARK   3     3  2.4841 -  2.1703    0.98     3574   187  0.1101 0.1231        
REMARK   3     4  2.1703 -  1.9720    1.00     3622   190  0.1029 0.1284        
REMARK   3     5  1.9720 -  1.8307    0.99     3596   189  0.1017 0.1253        
REMARK   3     6  1.8307 -  1.7228    0.99     3598   188  0.0992 0.1112        
REMARK   3     7  1.7228 -  1.6365    0.99     3573   189  0.0890 0.1019        
REMARK   3     8  1.6365 -  1.5653    0.99     3557   187  0.0835 0.0986        
REMARK   3     9  1.5653 -  1.5050    0.99     3565   188  0.0818 0.0997        
REMARK   3    10  1.5050 -  1.4531    0.99     3524   185  0.0794 0.0830        
REMARK   3    11  1.4531 -  1.4077    0.99     3541   186  0.0821 0.1089        
REMARK   3    12  1.4077 -  1.3674    0.97     3470   182  0.0875 0.1052        
REMARK   3    13  1.3674 -  1.3314    0.97     3463   182  0.0874 0.1176        
REMARK   3    14  1.3314 -  1.2990    0.98     3527   186  0.0910 0.1170        
REMARK   3    15  1.2990 -  1.2694    0.98     3447   182  0.0914 0.1156        
REMARK   3    16  1.2694 -  1.2424    0.98     3530   186  0.0886 0.1136        
REMARK   3    17  1.2424 -  1.2176    0.98     3489   183  0.0925 0.1216        
REMARK   3    18  1.2176 -  1.1946    0.98     3514   185  0.0941 0.1078        
REMARK   3    19  1.1946 -  1.1733    0.98     3484   184  0.0909 0.1036        
REMARK   3    20  1.1733 -  1.1534    0.98     3492   184  0.0913 0.1058        
REMARK   3    21  1.1534 -  1.1348    0.98     3491   183  0.0898 0.1105        
REMARK   3    22  1.1348 -  1.1173    0.98     3491   184  0.0946 0.1180        
REMARK   3    23  1.1173 -  1.1009    0.98     3475   183  0.1006 0.1272        
REMARK   3    24  1.1009 -  1.0854    0.98     3460   182  0.1151 0.1444        
REMARK   3    25  1.0854 -  1.0707    0.98     3482   183  0.1238 0.1575        
REMARK   3    26  1.0707 -  1.0568    0.97     3451   182  0.1334 0.1513        
REMARK   3    27  1.0568 -  1.0436    0.97     3420   180  0.1458 0.1651        
REMARK   3    28  1.0436 -  1.0310    0.97     3451   182  0.1570 0.1833        
REMARK   3    29  1.0310 -  1.0190    0.95     3393   179  0.1742 0.2017        
REMARK   3    30  1.0190 -  1.0076    0.88     3091   162  0.2063 0.2141        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.060            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 9.570            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           1916                                  
REMARK   3   ANGLE     :  1.156           2645                                  
REMARK   3   CHIRALITY :  0.098            286                                  
REMARK   3   PLANARITY :  0.009            352                                  
REMARK   3   DIHEDRAL  : 13.097            712                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5MNE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-DEC-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200002701.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7069                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 110736                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.008                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.322                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 6.607                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 26.3400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.65                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4I8H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M HEPES PH   
REMARK 280  7.5, 18-20% (W/V) PEG 8000, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 290K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       27.33450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.43050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       29.14500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.43050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.33450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       29.14500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 720 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 9120 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 145    CD   CE   NZ                                        
REMARK 470     LYS A 222    CE   NZ                                             
REMARK 470     LYS A 239    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  71      -82.50   -117.72                                   
REMARK 500    ASP A 153      -53.47     74.30                                   
REMARK 500    SER A 214      -66.25   -120.44                                   
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 A 724        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A 725        DISTANCE =  6.70 ANGSTROMS                       
REMARK 525    HOH A 726        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH A 727        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH A 728        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH A 729        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH A 730        DISTANCE =  9.23 ANGSTROMS                       
REMARK 525    HOH A 731        DISTANCE = 10.94 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 ASN A  72   O    90.9                                              
REMARK 620 3 VAL A  75   O   165.9  81.2                                        
REMARK 620 4 GLU A  80   OE2 102.9 159.6  87.9                                  
REMARK 620 5 HOH A 413   O    86.3  89.4 105.2  76.8                            
REMARK 620 6 HOH A 529   O    80.4 102.6  89.8  94.5 162.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 305                 
DBREF  5MNE A   16   245  UNP    P00760   TRY1_BOVIN      24    246             
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER          
SEQRES   7 A  223  ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS          
SEQRES   8 A  223  SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER          
SEQRES   9 A  223  LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER          
SEQRES  11 A  223  TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA          
SEQRES  18 A  223  SER ASN                                                      
HET     CA  A 301       1                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HET    SO4  A 305       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   7  HOH   *331(H2 O)                                                    
HELIX    1 AA1 ALA A   55  TYR A   59  5                                   5    
HELIX    2 AA2 SER A  164  TYR A  172  1                                   9    
HELIX    3 AA3 TYR A  234  ASN A  245  1                                  12    
SHEET    1 AA1 7 TYR A  20  THR A  21  0                                        
SHEET    2 AA1 7 LYS A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3 AA1 7 GLN A 135  GLY A 140 -1  N  ILE A 138   O  LEU A 158           
SHEET    4 AA1 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5 AA1 7 LYS A 204  TRP A 215 -1  O  LYS A 204   N  CYS A 201           
SHEET    6 AA1 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7 AA1 7 MET A 180  ALA A 183 -1  N  PHE A 181   O  TYR A 228           
SHEET    1 AA2 7 GLN A  30  ASN A  34  0                                        
SHEET    2 AA2 7 HIS A  40  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3 AA2 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4 AA2 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5 AA2 7 GLN A  81  VAL A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    6 AA2 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    7 AA2 7 GLN A  30  ASN A  34 -1  N  SER A  32   O  ARG A  66           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.06  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.06  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.04  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.05  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.04  
LINK         OE1 GLU A  70                CA    CA A 301     1555   1555  2.26  
LINK         O   ASN A  72                CA    CA A 301     1555   1555  2.34  
LINK         O   VAL A  75                CA    CA A 301     1555   1555  2.28  
LINK         OE2 GLU A  80                CA    CA A 301     1555   1555  2.33  
LINK        CA    CA A 301                 O   HOH A 413     1555   1555  2.39  
LINK        CA    CA A 301                 O   HOH A 529     1555   1555  2.35  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
SITE     2 AC1  6 HOH A 413  HOH A 529                                          
SITE     1 AC2  6 LYS A 169  PRO A 173  GLY A 174  HOH A 441                    
SITE     2 AC2  6 HOH A 518  HOH A 536                                          
SITE     1 AC3  6 HIS A  57  GLN A 192  GLY A 193  SER A 195                    
SITE     2 AC3  6 HOH A 402  HOH A 495                                          
SITE     1 AC4  6 LYS A  87  LYS A 107  THR A 149  TYR A 151                    
SITE     2 AC4  6 HOH A 403  HOH A 412                                          
SITE     1 AC5  7 PRO A 124  THR A 125  SER A 127  SER A 147                    
SITE     2 AC5  7 GLY A 148  LYS A 204  HOH A 408                               
CRYST1   54.669   58.290   66.861  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018292  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017156  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014956        0.00000                         
ATOM      1  N   ILE A  16      -8.078 -19.521 -13.407  1.00  7.95           N  
ANISOU    1  N   ILE A  16      965    904   1151    -66    -79    -27       N  
ATOM      2  CA  ILE A  16      -8.055 -20.420 -14.577  1.00  8.34           C  
ANISOU    2  CA  ILE A  16     1042    988   1140    -18     -1    -87       C  
ATOM      3  C   ILE A  16      -9.328 -20.169 -15.371  1.00  8.18           C  
ANISOU    3  C   ILE A  16     1004    935   1170     12    -43    -23       C  
ATOM      4  O   ILE A  16     -10.415 -20.292 -14.814  1.00  9.04           O  
ANISOU    4  O   ILE A  16     1057   1134   1245     44    -42    -56       O  
ATOM      5  CB  ILE A  16      -7.984 -21.897 -14.151  1.00  8.24           C  
ANISOU    5  CB  ILE A  16     1043    987   1099     14     10     12       C  
ATOM      6  CG1 ILE A  16      -6.779 -22.219 -13.249  1.00  8.55           C  
ANISOU    6  CG1 ILE A  16     1082    968   1197     12    -59    -79       C  
ATOM      7  CG2 ILE A  16      -8.054 -22.822 -15.367  1.00  9.46           C  
ANISOU    7  CG2 ILE A  16     1352   1051   1193    -23    -68    -94       C  
ATOM      8  CD1 ILE A  16      -5.428 -22.254 -13.930  1.00  9.27           C  
ANISOU    8  CD1 ILE A  16     1144   1021   1356    146     17     38       C  
ATOM      9  H1  ILE A  16      -8.454 -19.983 -12.655  1.00  9.54           H  
ATOM     10  H2  ILE A  16      -7.153 -19.329 -13.234  1.00  9.54           H  
ATOM     11  HA  ILE A  16      -7.290 -20.216 -15.136  1.00 10.01           H  
ATOM     12  HB  ILE A  16      -8.779 -22.072 -13.623  1.00  9.88           H  
ATOM     13 HG12 ILE A  16      -6.734 -21.547 -12.550  1.00 10.26           H  
ATOM     14 HG13 ILE A  16      -6.923 -23.091 -12.848  1.00 10.26           H  
ATOM     15 HG21 ILE A  16      -8.007 -23.743 -15.066  1.00 11.35           H  
ATOM     16 HG22 ILE A  16      -8.891 -22.668 -15.832  1.00 11.35           H  
ATOM     17 HG23 ILE A  16      -7.307 -22.627 -15.955  1.00 11.35           H  
ATOM     18 HD12 ILE A  16      -5.348 -23.081 -14.430  1.00 11.12           H  
ATOM     19  N   VAL A  17      -9.180 -19.823 -16.642  1.00  8.84           N  
ANISOU   19  N   VAL A  17     1031   1148   1180     -7   -137     57       N  
ATOM     20  CA  VAL A  17     -10.301 -19.610 -17.558  1.00  8.96           C  
ANISOU   20  CA  VAL A  17     1107   1059   1238      9   -217    -50       C  
ATOM     21  C   VAL A  17     -10.434 -20.847 -18.438  1.00  9.06           C  
ANISOU   21  C   VAL A  17     1113   1092   1237     40   -143     96       C  
ATOM     22  O   VAL A  17      -9.444 -21.330 -19.013  1.00  9.52           O  
ANISOU   22  O   VAL A  17     1214   1164   1240      7   -159    -26       O  
ATOM     23  CB  VAL A  17     -10.052 -18.370 -18.434  1.00  9.61           C  
ANISOU   23  CB  VAL A  17     1266   1188   1197     29   -135     97       C  
ATOM     24  CG1 VAL A  17     -11.199 -18.201 -19.441  1.00 10.94           C  
ANISOU   24  CG1 VAL A  17     1339   1377   1442    112   -251     94       C  
ATOM     25  CG2 VAL A  17      -9.904 -17.117 -17.600  1.00 11.63           C  
ANISOU   25  CG2 VAL A  17     1765   1294   1359     52   -124    -17       C  
ATOM     26  H   VAL A  17      -8.414 -19.701 -17.013  1.00 10.61           H  
ATOM     27  HB  VAL A  17      -9.231 -18.496 -18.934  1.00 11.53           H  
ATOM     28 HG12 VAL A  17     -11.244 -18.990 -20.004  1.00 13.13           H  
ATOM     29 HG13 VAL A  17     -12.032 -18.092 -18.956  1.00 13.13           H  
ATOM     30  N   GLY A  18     -11.652 -21.368 -18.552  1.00  9.17           N  
ANISOU   30  N   GLY A  18     1054   1143   1287      6   -157    -26       N  
ATOM     31  CA  GLY A  18     -11.906 -22.478 -19.450  1.00  9.99           C  
ANISOU   31  CA  GLY A  18     1395   1078   1322     11   -196    118       C  
ATOM     32  C   GLY A  18     -11.456 -23.822 -18.931  1.00  9.79           C  
ANISOU   32  C   GLY A  18     1281   1159   1279    -27    -98     20       C  
ATOM     33  O   GLY A  18     -11.308 -24.759 -19.727  1.00 11.12           O  
ANISOU   33  O   GLY A  18     1532   1213   1480    -49   -182    142       O  
ATOM     34  H   GLY A  18     -12.344 -21.094 -18.121  1.00 11.00           H  
ATOM     35  HA3 GLY A  18     -11.485 -22.313 -20.308  1.00 11.98           H  
ATOM     36  N   GLY A  19     -11.207 -23.934 -17.622  1.00  9.90           N  
ANISOU   36  N   GLY A  19     1194   1165   1401    -57   -172    261       N  
ATOM     37  CA  GLY A  19     -10.796 -25.164 -16.989  1.00 10.19           C  
ANISOU   37  CA  GLY A  19     1166   1266   1440     25    -22    169       C  
ATOM     38  C   GLY A  19     -11.948 -25.904 -16.355  1.00  9.57           C  
ANISOU   38  C   GLY A  19     1096   1120   1420    -89   -193    100       C  
ATOM     39  O   GLY A  19     -13.111 -25.763 -16.757  1.00 11.50           O  
ANISOU   39  O   GLY A  19     1240   1510   1621   -127   -340    366       O  
ATOM     40  HA2 GLY A  19     -10.367 -25.744 -17.637  1.00 12.22           H  
ATOM     41  N   TYR A  20     -11.623 -26.728 -15.358  1.00  8.56           N  
ANISOU   41  N   TYR A  20     1083   1047   1122   -149    -89     -1       N  
ATOM     42  CA  TYR A  20     -12.562 -27.614 -14.709  1.00  9.17           C  
ANISOU   42  CA  TYR A  20     1131   1158   1196   -203    -82    -37       C  
ATOM     43  C   TYR A  20     -12.237 -27.655 -13.218  1.00  8.74           C  
ANISOU   43  C   TYR A  20     1072   1034   1214   -143   -118    -55       C  
ATOM     44  O   TYR A  20     -11.117 -27.352 -12.791  1.00  8.71           O  
ANISOU   44  O   TYR A  20     1039   1111   1160   -209    -91   -110       O  
ATOM     45  CB  TYR A  20     -12.575 -29.032 -15.340  1.00  9.66           C  
ANISOU   45  CB  TYR A  20     1239   1241   1189   -399   -102    -92       C  
ATOM     46  CG  TYR A  20     -11.255 -29.741 -15.253  1.00  9.13           C  
ANISOU   46  CG  TYR A  20     1220   1107   1142   -245    -79   -262       C  
ATOM     47  CD1 TYR A  20     -10.236 -29.496 -16.181  1.00  9.55           C  
ANISOU   47  CD1 TYR A  20     1278   1117   1234   -314    -24   -292       C  
ATOM     48  CD2 TYR A  20     -11.011 -30.678 -14.260  1.00  9.43           C  
ANISOU   48  CD2 TYR A  20     1261   1091   1232   -194    -79   -258       C  
ATOM     49  CE1 TYR A  20      -9.025 -30.140 -16.106  1.00 10.11           C  
ANISOU   49  CE1 TYR A  20     1421   1153   1266   -125    -59   -345       C  
ATOM     50  CE2 TYR A  20      -9.768 -31.322 -14.175  1.00  9.52           C  
ANISOU   50  CE2 TYR A  20     1378   1116   1123    -96   -108   -319       C  
ATOM     51  CZ  TYR A  20      -8.787 -31.036 -15.108  1.00  9.51           C  
ANISOU   51  CZ  TYR A  20     1124   1169   1322   -103    -99   -477       C  
ATOM     52  OH  TYR A  20      -7.547 -31.634 -15.069  1.00 11.49           O  
ANISOU   52  OH  TYR A  20     1391   1396   1577    -96   -156   -401       O  
ATOM     53  HB2 TYR A  20     -13.237 -29.575 -14.883  1.00 11.59           H  
ATOM     54  HD2 TYR A  20     -11.668 -30.858 -13.626  1.00 11.32           H  
ATOM     55  HE2 TYR A  20      -9.606 -31.940 -13.499  1.00 11.42           H  
ATOM     56  HH  TYR A  20      -7.504 -32.165 -14.420  1.00 13.79           H  
ATOM     57  N   THR A  21     -13.217 -28.049 -12.414  1.00  9.39           N  
ANISOU   57  N   THR A  21     1075   1282   1212   -208   -101    -18       N  
ATOM     58  CA  THR A  21     -12.979 -28.226 -10.986  1.00  8.92           C  
ANISOU   58  CA  THR A  21     1121   1030   1239   -143   -124     43       C  
ATOM     59  C   THR A  21     -12.083 -29.434 -10.775  1.00  9.30           C  
ANISOU   59  C   THR A  21     1346   1166   1022   -304    -41   -139       C  
ATOM     60  O   THR A  21     -12.422 -30.545 -11.178  1.00 10.33           O  
ANISOU   60  O   THR A  21     1518   1147   1262   -322   -192   -154       O  
ATOM     61  CB  THR A  21     -14.329 -28.412 -10.292  1.00 10.08           C  
ANISOU   61  CB  THR A  21     1205   1285   1339   -213   -131     69       C  
ATOM     62  OG1 THR A  21     -15.034 -27.175 -10.454  1.00 12.00           O  
ANISOU   62  OG1 THR A  21     1173   1779   1609    -16     42    -52       O  
ATOM     63  CG2 THR A  21     -14.178 -28.712  -8.797  1.00 11.19           C  
ANISOU   63  CG2 THR A  21     1406   1571   1275   -202     57      0       C  
ATOM     64  HA  THR A  21     -12.542 -27.441 -10.621  1.00 10.71           H  
ATOM     65 HG22 THR A  21     -13.716 -29.556  -8.674  1.00 13.43           H  
ATOM     66  N   CYS A  22     -10.925 -29.225 -10.153  1.00  8.74           N  
ANISOU   66  N   CYS A  22     1248   1016   1055   -143   -141    -83       N  
ATOM     67  CA  CYS A  22      -9.947 -30.308 -10.023  1.00  9.40           C  
ANISOU   67  CA  CYS A  22     1423    999   1151   -127    -28     -5       C  
ATOM     68  C   CYS A  22     -10.521 -31.487  -9.248  1.00  9.53           C  
ANISOU   68  C   CYS A  22     1426    894   1302   -149   -206   -168       C  
ATOM     69  O   CYS A  22     -10.287 -32.644  -9.598  1.00 10.90           O  
ANISOU   69  O   CYS A  22     1758   1003   1382   -127   -109   -166       O  
ATOM     70  CB  CYS A  22      -8.690 -29.819  -9.268  1.00  9.10           C  
ANISOU   70  CB  CYS A  22     1264   1045   1149     64    -37     15       C  
ATOM     71  SG  CYS A  22      -7.815 -28.418  -9.966  1.00  8.61           S  
ANISOU   71  SG  CYS A  22     1320    885   1065   -116    -60    -75       S  
ATOM     72  H   CYS A  22     -10.682 -28.478  -9.802  1.00 10.48           H  
ATOM     73  HB2 CYS A  22      -8.955 -29.570  -8.369  1.00 10.92           H  
ATOM     74  HB3 CYS A  22      -8.060 -30.555  -9.223  1.00 10.92           H  
ATOM     75  N   GLY A  23     -11.207 -31.191  -8.148  1.00  9.08           N  
ANISOU   75  N   GLY A  23     1361    891   1198   -189    -14    -49       N  
ATOM     76  CA  GLY A  23     -11.566 -32.154  -7.124  1.00  9.88           C  
ANISOU   76  CA  GLY A  23     1442    953   1358   -296    -21    -48       C  
ATOM     77  C   GLY A  23     -10.690 -31.940  -5.900  1.00  8.99           C  
ANISOU   77  C   GLY A  23     1368    824   1225   -227    -75    -28       C  
ATOM     78  O   GLY A  23      -9.487 -31.675  -5.988  1.00  9.26           O  
ANISOU   78  O   GLY A  23     1300    997   1223   -238    -41    -44       O  
ATOM     79  H   GLY A  23     -11.486 -30.398  -7.970  1.00 10.90           H  
ATOM     80  HA2 GLY A  23     -12.496 -32.040  -6.872  1.00 11.85           H  
ATOM     81  HA3 GLY A  23     -11.435 -33.056  -7.454  1.00 11.85           H  
ATOM     82  N   ALA A  24     -11.296 -32.060  -4.729  1.00  9.71           N  
ANISOU   82  N   ALA A  24     1421   1043   1225   -304      6    -20       N  
ATOM     83  CA  ALA A  24     -10.621 -31.703  -3.492  1.00  9.47           C  
ANISOU   83  CA  ALA A  24     1336    997   1263   -210     69    -58       C  
ATOM     84  C   ALA A  24      -9.353 -32.526  -3.294  1.00  8.82           C  
ANISOU   84  C   ALA A  24     1408    846   1097   -179     65     25       C  
ATOM     85  O   ALA A  24      -9.377 -33.759  -3.259  1.00 10.17           O  
ANISOU   85  O   ALA A  24     1658    895   1312   -341    -11     77       O  
ATOM     86  CB  ALA A  24     -11.577 -31.902  -2.305  1.00 11.23           C  
ANISOU   86  CB  ALA A  24     1400   1559   1310   -248    196    -59       C  
ATOM     87  HA  ALA A  24     -10.371 -30.767  -3.525  1.00 11.36           H  
ATOM     88  N   ASN A  25      -8.248 -31.825  -3.091  1.00  8.80           N  
ANISOU   88  N   ASN A  25     1397    793   1155   -108     56    -82       N  
ATOM     89  CA  ASN A  25      -6.966 -32.425  -2.729  1.00  9.61           C  
ANISOU   89  CA  ASN A  25     1442    950   1259     25   -199     -2       C  
ATOM     90  C   ASN A  25      -6.403 -33.350  -3.791  1.00  9.53           C  
ANISOU   90  C   ASN A  25     1460    760   1401     39    -74   -124       C  
ATOM     91  O   ASN A  25      -5.531 -34.156  -3.488  1.00 12.26           O  
ANISOU   91  O   ASN A  25     1905   1171   1581    353   -237   -124       O  
ATOM     92  CB  ASN A  25      -6.997 -33.104  -1.359  1.00 10.83           C  
ANISOU   92  CB  ASN A  25     1777    916   1422   -142   -131   -136       C  
ATOM     93  CG  ASN A  25      -7.589 -32.213  -0.309  1.00 10.69           C  
ANISOU   93  CG  ASN A  25     1648   1065   1349   -252   -168     74       C  
ATOM     94  OD1 ASN A  25      -8.673 -32.498   0.203  1.00 12.77           O  
ANISOU   94  OD1 ASN A  25     2021   1303   1530   -514     84    -89       O  
ATOM     95  ND2 ASN A  25      -6.924 -31.109  -0.023  1.00 10.28           N  
ANISOU   95  ND2 ASN A  25     1497   1084   1323   -216    -73   -105       N  
ATOM     96  H   ASN A  25      -8.212 -30.968  -3.160  1.00 10.56           H  
ATOM     97  HB2 ASN A  25      -7.542 -33.904  -1.415  1.00 13.00           H  
ATOM     98  N   THR A  26      -6.831 -33.191  -5.037  1.00  8.76           N  
ANISOU   98  N   THR A  26     1290    757   1283    -34    -10    -96       N  
ATOM     99  CA  THR A  26      -6.307 -33.981  -6.144  1.00  9.37           C  
ANISOU   99  CA  THR A  26     1407    742   1412    -45    -19   -186       C  
ATOM    100  C   THR A  26      -5.011 -33.414  -6.717  1.00  9.10           C  
ANISOU  100  C   THR A  26     1332    857   1268   -147    -12   -170       C  
ATOM    101  O   THR A  26      -4.366 -34.088  -7.531  1.00 10.45           O  
ANISOU  101  O   THR A  26     1485    972   1514    -41    236   -351       O  
ATOM    102  CB  THR A  26      -7.341 -34.101  -7.266  1.00 10.29           C  
ANISOU  102  CB  THR A  26     1510    935   1466   -203    -22   -241       C  
ATOM    103  OG1 THR A  26      -7.630 -32.815  -7.812  1.00 10.46           O  
ANISOU  103  OG1 THR A  26     1507   1098   1369   -201    -94    -65       O  
ATOM    104  CG2 THR A  26      -8.628 -34.800  -6.805  1.00 11.33           C  
ANISOU  104  CG2 THR A  26     1366   1172   1765   -265    -91   -355       C  
ATOM    105  H   THR A  26      -7.434 -32.624  -5.271  1.00 10.51           H  
ATOM    106  HA  THR A  26      -6.118 -34.876  -5.822  1.00 11.25           H  
ATOM    107  HB  THR A  26      -6.958 -34.647  -7.970  1.00 12.35           H  
ATOM    108  N   VAL A  27      -4.610 -32.225  -6.278  1.00  8.38           N  
ANISOU  108  N   VAL A  27     1179    729   1275    -86     16   -132       N  
ATOM    109  CA  VAL A  27      -3.386 -31.544  -6.694  1.00  8.37           C  
ANISOU  109  CA  VAL A  27     1176    801   1204    -31     53   -149       C  
ATOM    110  C   VAL A  27      -2.618 -31.269  -5.401  1.00  7.78           C  
ANISOU  110  C   VAL A  27      970    705   1282    -27     47   -143       C  
ATOM    111  O   VAL A  27      -2.622 -30.143  -4.888  1.00  8.04           O  
ANISOU  111  O   VAL A  27     1072    778   1204     18    -53   -107       O  
ATOM    112  CB  VAL A  27      -3.686 -30.275  -7.503  1.00  8.27           C  
ANISOU  112  CB  VAL A  27     1197    791   1155    -34     64    -12       C  
ATOM    113  CG1 VAL A  27      -2.406 -29.715  -8.081  1.00  9.18           C  
ANISOU  113  CG1 VAL A  27     1367    841   1281     50     92    -94       C  
ATOM    114  CG2 VAL A  27      -4.679 -30.533  -8.620  1.00  9.61           C  
ANISOU  114  CG2 VAL A  27     1344   1009   1298    -12     26    -67       C  
ATOM    115  H   VAL A  27      -5.058 -31.767  -5.704  1.00 10.05           H  
ATOM    116  HA  VAL A  27      -2.856 -32.141  -7.245  1.00 10.04           H  
ATOM    117  HB  VAL A  27      -4.066 -29.606  -6.912  1.00  9.93           H  
ATOM    118 HG12 VAL A  27      -1.800 -29.498  -7.355  1.00 11.02           H  
ATOM    119 HG13 VAL A  27      -2.004 -30.380  -8.661  1.00 11.02           H  
ATOM    120 HG22 VAL A  27      -4.312 -31.199  -9.222  1.00 11.53           H  
ATOM    121 HG23 VAL A  27      -5.510 -30.854  -8.236  1.00 11.53           H  
ATOM    122  N   PRO A  28      -1.982 -32.289  -4.818  1.00  8.03           N  
ANISOU  122  N   PRO A  28     1106    729   1218     34     16     18       N  
ATOM    123  CA  PRO A  28      -1.611 -32.195  -3.392  1.00  8.50           C  
ANISOU  123  CA  PRO A  28     1061    863   1306    -63     53     87       C  
ATOM    124  C   PRO A  28      -0.409 -31.307  -3.116  1.00  7.93           C  
ANISOU  124  C   PRO A  28     1102    706   1206     79     15     -7       C  
ATOM    125  O   PRO A  28      -0.145 -30.982  -1.953  1.00  8.12           O  
ANISOU  125  O   PRO A  28     1140    696   1250     30     19     45       O  
ATOM    126  CB  PRO A  28      -1.340 -33.662  -3.013  1.00  9.12           C  
ANISOU  126  CB  PRO A  28     1294    748   1424   -118    -37    123       C  
ATOM    127  CG  PRO A  28      -0.931 -34.301  -4.321  1.00  9.77           C  
ANISOU  127  CG  PRO A  28     1473    704   1534    -78    -61     53       C  
ATOM    128  CD  PRO A  28      -1.831 -33.672  -5.338  1.00  9.39           C  
ANISOU  128  CD  PRO A  28     1405    638   1525    -78     21    -42       C  
ATOM    129  HA  PRO A  28      -2.366 -31.871  -2.876  1.00 10.20           H  
ATOM    130  HB3 PRO A  28      -2.163 -34.062  -2.691  1.00 10.95           H  
ATOM    131  HG3 PRO A  28      -1.100 -35.255  -4.273  1.00 11.72           H  
ATOM    132  HD2 PRO A  28      -1.407 -33.664  -6.210  1.00 11.27           H  
ATOM    133  HD3 PRO A  28      -2.689 -34.124  -5.359  1.00 11.27           H  
ATOM    134  N   TYR A  29       0.304 -30.906  -4.158  1.00  7.76           N  
ANISOU  134  N   TYR A  29     1080    695   1174      8    -56    -26       N  
ATOM    135  CA  TYR A  29       1.424 -29.980  -4.091  1.00  7.36           C  
ANISOU  135  CA  TYR A  29      952    647   1199     20    -45     32       C  
ATOM    136  C   TYR A  29       1.004 -28.522  -4.257  1.00  7.18           C  
ANISOU  136  C   TYR A  29      977    625   1126    -69     45     -3       C  
ATOM    137  O   TYR A  29       1.833 -27.632  -4.088  1.00  7.54           O  
ANISOU  137  O   TYR A  29      951    681   1233    -21    -10     77       O  
ATOM    138  CB  TYR A  29       2.475 -30.359  -5.163  1.00  7.97           C  
ANISOU  138  CB  TYR A  29      992    785   1251     66      9      3       C  
ATOM    139  CG  TYR A  29       1.864 -30.492  -6.544  1.00  7.82           C  
ANISOU  139  CG  TYR A  29     1049    737   1187     93     85    -61       C  
ATOM    140  CD1 TYR A  29       1.658 -29.395  -7.353  1.00  7.75           C  
ANISOU  140  CD1 TYR A  29     1155    630   1158    -23     71    -50       C  
ATOM    141  CD2 TYR A  29       1.459 -31.729  -7.013  1.00  8.39           C  
ANISOU  141  CD2 TYR A  29     1180    683   1326     -1     18    -39       C  
ATOM    142  CE1 TYR A  29       1.056 -29.515  -8.592  1.00  7.99           C  
ANISOU  142  CE1 TYR A  29     1187    692   1157     26     37    -72       C  
ATOM    143  CE2 TYR A  29       0.842 -31.869  -8.250  1.00  8.87           C  
ANISOU  143  CE2 TYR A  29     1215    711   1446    -44     57   -208       C  
ATOM    144  CZ  TYR A  29       0.636 -30.756  -9.039  1.00  8.14           C  
ANISOU  144  CZ  TYR A  29     1144    742   1206     33     97    -53       C  
ATOM    145  OH  TYR A  29       0.003 -30.912 -10.262  1.00  8.79           O  
ANISOU  145  OH  TYR A  29     1289    877   1172    -40    -66   -165       O  
ATOM    146  H   TYR A  29       0.146 -31.173  -4.960  1.00  9.31           H  
ATOM    147  HA  TYR A  29       1.845 -30.067  -3.221  1.00  8.84           H  
ATOM    148  HB2 TYR A  29       3.155 -29.668  -5.199  1.00  9.56           H  
ATOM    149  HB3 TYR A  29       2.877 -31.210  -4.928  1.00  9.56           H  
ATOM    150  HD1 TYR A  29       1.916 -28.554  -7.052  1.00  9.30           H  
ATOM    151  HD2 TYR A  29       1.574 -32.479  -6.474  1.00 10.07           H  
ATOM    152  HE1 TYR A  29       0.915 -28.759  -9.116  1.00  9.59           H  
ATOM    153  HE2 TYR A  29       0.566 -32.708  -8.543  1.00 10.65           H  
ATOM    154  N   GLN A  30      -0.251 -28.261  -4.625  1.00  7.09           N  
ANISOU  154  N   GLN A  30      883    687   1123      1    -32    -50       N  
ATOM    155  CA  GLN A  30      -0.712 -26.894  -4.799  1.00  7.32           C  
ANISOU  155  CA  GLN A  30      892    766   1123     31     37    -53       C  
ATOM    156  C   GLN A  30      -0.875 -26.204  -3.460  1.00  6.92           C  
ANISOU  156  C   GLN A  30      873    684   1072     47     45      1       C  
ATOM    157  O   GLN A  30      -1.590 -26.721  -2.586  1.00  7.79           O  
ANISOU  157  O   GLN A  30     1103    719   1137    -14    134     -6       O  
ATOM    158  CB  GLN A  30      -2.060 -26.890  -5.532  1.00  7.91           C  
ANISOU  158  CB  GLN A  30     1106    782   1117    -31    -45    -93       C  
ATOM    159  CG  GLN A  30      -2.727 -25.516  -5.607  1.00  7.50           C  
ANISOU  159  CG  GLN A  30      891    860   1099     14    -54    -59       C  
ATOM    160  CD  GLN A  30      -2.254 -24.650  -6.757  1.00  7.22           C  
ANISOU  160  CD  GLN A  30      886    813   1043     46    -34   -134       C  
ATOM    161  OE1 GLN A  30      -2.300 -25.069  -7.911  1.00  8.61           O  
ANISOU  161  OE1 GLN A  30     1209   1003   1058   -104    -15   -128       O  
ATOM    162  NE2 GLN A  30      -1.856 -23.420  -6.464  1.00  8.04           N  
ANISOU  162  NE2 GLN A  30     1100    845   1111     -3     35    -22       N  
ATOM    163  H   GLN A  30      -0.849 -28.859  -4.778  1.00  8.50           H  
ATOM    164  HA  GLN A  30      -0.068 -26.397  -5.329  1.00  8.78           H  
ATOM    165  HB2 GLN A  30      -1.921 -27.201  -6.441  1.00  9.49           H  
ATOM    166  HB3 GLN A  30      -2.667 -27.489  -5.070  1.00  9.49           H  
ATOM    167  HG2 GLN A  30      -3.684 -25.641  -5.706  1.00  9.00           H  
ATOM    168  HG3 GLN A  30      -2.544 -25.038  -4.783  1.00  9.00           H  
ATOM    169 HE22 GLN A  30      -1.581 -22.897  -7.088  1.00  9.65           H  
ATOM    170  N  AVAL A  31      -0.251 -25.039  -3.289  0.63  7.25           N  
ANISOU  170  N  AVAL A  31      909    790   1055     73     98    -13       N  
ATOM    171  N  BVAL A  31      -0.328 -24.988  -3.396  0.37  6.91           N  
ANISOU  171  N  BVAL A  31      926    523   1176   -272    -13   -239       N  
ATOM    172  CA AVAL A  31      -0.480 -24.243  -2.089  0.63  7.41           C  
ANISOU  172  CA AVAL A  31     1050    765    999     89     40    -77       C  
ATOM    173  CA BVAL A  31      -0.344 -24.114  -2.238  0.37  7.32           C  
ANISOU  173  CA BVAL A  31      815    698   1267   -104     -6   -126       C  
ATOM    174  C  AVAL A  31      -1.099 -22.904  -2.486  0.63  6.84           C  
ANISOU  174  C  AVAL A  31      872    715   1014    -40      8    -37       C  
ATOM    175  C  BVAL A  31      -1.190 -22.891  -2.557  0.37  6.43           C  
ANISOU  175  C  BVAL A  31      664    732   1046    -66   -134   -246       C  
ATOM    176  O  AVAL A  31      -0.963 -22.428  -3.623  0.63  7.00           O  
ANISOU  176  O  AVAL A  31      827    860    973    -80     59     14       O  
ATOM    177  O  BVAL A  31      -1.255 -22.447  -3.713  0.37  6.46           O  
ANISOU  177  O  BVAL A  31      676    747   1033    -30    -43   -281       O  
ATOM    178  CB AVAL A  31       0.787 -24.044  -1.212  0.63  7.58           C  
ANISOU  178  CB AVAL A  31      951    888   1043    -20    -80    -48       C  
ATOM    179  CB BVAL A  31       1.113 -23.669  -1.999  0.37  7.80           C  
ANISOU  179  CB BVAL A  31      949    670   1345   -179    -73   -126       C  
ATOM    180  CG1AVAL A  31       1.457 -25.389  -0.888  0.63  9.34           C  
ANISOU  180  CG1AVAL A  31     1188   1069   1291    130   -135    -10       C  
ATOM    181  CG1BVAL A  31       1.198 -22.714  -0.835  0.37 10.74           C  
ANISOU  181  CG1BVAL A  31     1273   1252   1555    -32   -319    -94       C  
ATOM    182  CG2AVAL A  31       1.749 -23.075  -1.869  0.63  8.94           C  
ANISOU  182  CG2AVAL A  31      961   1319   1118   -250      7     26       C  
ATOM    183  CG2BVAL A  31       2.011 -24.879  -1.817  0.37  8.03           C  
ANISOU  183  CG2BVAL A  31      969    957   1126    155   -250   -101       C  
ATOM    184  H  AVAL A  31       0.304 -24.692  -3.847  0.63  8.70           H  
ATOM    185  H  BVAL A  31       0.084 -24.633  -4.063  0.37  8.29           H  
ATOM    186  HA AVAL A  31      -1.132 -24.708  -1.542  0.63  8.89           H  
ATOM    187  HA BVAL A  31      -0.691 -24.571  -1.455  0.37  8.78           H  
ATOM    188  N   SER A  32      -1.795 -22.312  -1.516  1.00  6.89           N  
ANISOU  188  N   SER A  32      925    675   1017     56     51    -65       N  
ATOM    189  CA  SER A  32      -2.289 -20.949  -1.564  1.00  7.19           C  
ANISOU  189  CA  SER A  32      963    815    953     48    -11      9       C  
ATOM    190  C   SER A  32      -1.419 -20.089  -0.656  1.00  6.96           C  
ANISOU  190  C   SER A  32      979    746    918    145     82     13       C  
ATOM    191  O   SER A  32      -1.196 -20.451   0.501  1.00  8.26           O  
ANISOU  191  O   SER A  32     1269    867   1004    -23    -22     -7       O  
ATOM    192  CB  SER A  32      -3.747 -20.878  -1.092  1.00  7.54           C  
ANISOU  192  CB  SER A  32     1116    856    892    102     42    -44       C  
ATOM    193  OG  SER A  32      -4.166 -19.534  -0.894  1.00  7.94           O  
ANISOU  193  OG  SER A  32     1079    866   1074    141    105    -32       O  
ATOM    194  H  ASER A  32      -2.002 -22.710  -0.782  0.63  8.27           H  
ATOM    195  H  BSER A  32      -1.931 -22.701  -0.761  0.37  8.27           H  
ATOM    196  HA  SER A  32      -2.233 -20.608  -2.471  1.00  8.63           H  
ATOM    197  HB2 SER A  32      -4.314 -21.287  -1.764  1.00  9.04           H  
ATOM    198  HB3 SER A  32      -3.829 -21.358  -0.254  1.00  9.04           H  
ATOM    199  HG  SER A  32      -4.102 -19.105  -1.613  1.00  9.53           H  
ATOM    200  N   LEU A  33      -0.923 -18.979  -1.185  1.00  6.87           N  
ANISOU  200  N   LEU A  33      910    771    931     27     28    -11       N  
ATOM    201  CA  LEU A  33      -0.210 -17.993  -0.389  1.00  7.09           C  
ANISOU  201  CA  LEU A  33      935    774    984     80     16    -64       C  
ATOM    202  C   LEU A  33      -1.222 -16.975   0.114  1.00  7.26           C  
ANISOU  202  C   LEU A  33      895    810   1054     39    -49     21       C  
ATOM    203  O   LEU A  33      -1.979 -16.409  -0.687  1.00  7.54           O  
ANISOU  203  O   LEU A  33      982    805   1080     94     88    -82       O  
ATOM    204  CB  LEU A  33       0.899 -17.313  -1.190  1.00  7.45           C  
ANISOU  204  CB  LEU A  33      877    937   1018    -35     58   -106       C  
ATOM    205  CG  LEU A  33       1.925 -18.248  -1.825  1.00  8.25           C  
ANISOU  205  CG  LEU A  33      887   1090   1157     55     66   -217       C  
ATOM    206  CD1 LEU A  33       3.002 -17.419  -2.531  1.00  9.66           C  
ANISOU  206  CD1 LEU A  33      890   1495   1287     42    164    -81       C  
ATOM    207  CD2 LEU A  33       2.539 -19.191  -0.836  1.00  8.95           C  
ANISOU  207  CD2 LEU A  33      925    967   1510    135      6    -76       C  
ATOM    208  H   LEU A  33      -0.988 -18.771  -2.017  1.00  8.25           H  
ATOM    209  HA  LEU A  33       0.192 -18.429   0.378  1.00  8.51           H  
ATOM    210  HB2 LEU A  33       0.490 -16.802  -1.906  1.00  8.94           H  
ATOM    211  HB3 LEU A  33       1.380 -16.713  -0.599  1.00  8.94           H  
ATOM    212  HG  LEU A  33       1.479 -18.782  -2.500  1.00  9.90           H  
ATOM    213  N   ASN A  34      -1.245 -16.757   1.436  1.00  7.63           N  
ANISOU  213  N   ASN A  34      969    886   1042     51     83   -111       N  
ATOM    214  CA  ASN A  34      -2.283 -15.958   2.078  1.00  7.42           C  
ANISOU  214  CA  ASN A  34      947    818   1054     43    131   -101       C  
ATOM    215  C   ASN A  34      -1.645 -14.847   2.897  1.00  7.69           C  
ANISOU  215  C   ASN A  34      963    921   1039      5    134    -68       C  
ATOM    216  O   ASN A  34      -0.747 -15.086   3.709  1.00  8.61           O  
ANISOU  216  O   ASN A  34     1127    939   1205     52    -45   -199       O  
ATOM    217  CB  ASN A  34      -3.119 -16.880   2.975  1.00  7.80           C  
ANISOU  217  CB  ASN A  34     1007    855   1101    -20     76    -91       C  
ATOM    218  CG  ASN A  34      -4.288 -16.167   3.625  1.00  8.04           C  
ANISOU  218  CG  ASN A  34     1106    803   1145    -96    202    -83       C  
ATOM    219  OD1 ASN A  34      -4.114 -15.376   4.554  1.00  8.67           O  
ANISOU  219  OD1 ASN A  34     1159    950   1184    -86    254   -170       O  
ATOM    220  ND2 ASN A  34      -5.482 -16.454   3.152  1.00  8.27           N  
ANISOU  220  ND2 ASN A  34     1098    922   1124     25    239    -57       N  
ATOM    221  HA  ASN A  34      -2.861 -15.563   1.406  1.00  8.90           H  
ATOM    222  HB2 ASN A  34      -3.472 -17.607   2.438  1.00  9.36           H  
ATOM    223  HB3 ASN A  34      -2.554 -17.232   3.679  1.00  9.36           H  
ATOM    224 HD21 ASN A  34      -6.179 -16.077   3.487  1.00  9.93           H  
ATOM    225 HD22 ASN A  34      -5.566 -17.019   2.509  1.00  9.93           H  
ATOM    226  N   SER A  37      -2.120 -13.619   2.695  1.00  8.06           N  
ANISOU  226  N   SER A  37      964    847   1253      8    101    -58       N  
ATOM    227  CA  SER A  37      -1.705 -12.466   3.500  1.00  8.96           C  
ANISOU  227  CA  SER A  37     1047    915   1441    -15    146   -199       C  
ATOM    228  C   SER A  37      -2.933 -11.746   4.046  1.00  8.82           C  
ANISOU  228  C   SER A  37     1201    775   1374    -21    189   -194       C  
ATOM    229  O   SER A  37      -3.047 -10.524   3.979  1.00 10.97           O  
ANISOU  229  O   SER A  37     1307   1025   1835     71    426   -186       O  
ATOM    230  CB  SER A  37      -0.835 -11.518   2.690  1.00 10.07           C  
ANISOU  230  CB  SER A  37     1068    991   1768     38    186    -85       C  
ATOM    231  OG  SER A  37      -1.548 -10.978   1.593  1.00 10.85           O  
ANISOU  231  OG  SER A  37     1294   1038   1788     44    444     14       O  
ATOM    232  H   SER A  37      -2.696 -13.424   2.087  1.00  9.68           H  
ATOM    233  HA  SER A  37      -1.183 -12.780   4.254  1.00 10.75           H  
ATOM    234  HB3 SER A  37      -0.064 -12.004   2.357  1.00 12.09           H  
ATOM    235  N   GLY A  38      -3.874 -12.511   4.568  1.00  9.00           N  
ANISOU  235  N   GLY A  38     1162    918   1341     12    145   -173       N  
ATOM    236  CA  GLY A  38      -5.214 -12.042   4.904  1.00  9.87           C  
ANISOU  236  CA  GLY A  38     1113   1191   1445     70    205   -337       C  
ATOM    237  C   GLY A  38      -6.270 -12.514   3.932  1.00  9.06           C  
ANISOU  237  C   GLY A  38     1132    915   1394    121    319    -89       C  
ATOM    238  O   GLY A  38      -7.470 -12.388   4.197  1.00  9.10           O  
ANISOU  238  O   GLY A  38     1219    995   1242     32    331   -153       O  
ATOM    239  H   GLY A  38      -3.758 -13.344   4.746  1.00 10.80           H  
ATOM    240  N   TYR A  39      -5.831 -13.039   2.796  1.00  9.05           N  
ANISOU  240  N   TYR A  39     1060   1073   1306    151    309   -154       N  
ATOM    241  CA  TYR A  39      -6.613 -13.419   1.633  1.00  8.64           C  
ANISOU  241  CA  TYR A  39     1009   1032   1242    194    130    -84       C  
ATOM    242  C   TYR A  39      -5.647 -14.175   0.720  1.00  8.36           C  
ANISOU  242  C   TYR A  39     1008    968   1200    215    166    -14       C  
ATOM    243  O   TYR A  39      -4.422 -13.948   0.758  1.00  8.18           O  
ANISOU  243  O   TYR A  39      954    980   1173    116    165   -134       O  
ATOM    244  CB  TYR A  39      -7.184 -12.183   0.877  1.00 10.08           C  
ANISOU  244  CB  TYR A  39     1030   1436   1362    313    292    -80       C  
ATOM    245  CG  TYR A  39      -6.137 -11.108   0.739  1.00 10.32           C  
ANISOU  245  CG  TYR A  39     1422   1192   1309    410    124   -112       C  
ATOM    246  CD1 TYR A  39      -5.244 -11.101  -0.311  1.00  9.82           C  
ANISOU  246  CD1 TYR A  39     1311    896   1524    108    194   -173       C  
ATOM    247  CD2 TYR A  39      -6.001 -10.115   1.713  1.00 13.59           C  
ANISOU  247  CD2 TYR A  39     2412   1112   1641    710   -136   -133       C  
ATOM    248  CE1 TYR A  39      -4.233 -10.172  -0.372  1.00 11.87           C  
ANISOU  248  CE1 TYR A  39     1340   1054   2115    147   -123   -153       C  
ATOM    249  CE2 TYR A  39      -5.006  -9.182   1.644  1.00 16.05           C  
ANISOU  249  CE2 TYR A  39     2789   1153   2159    526   -784   -316       C  
ATOM    250  CZ  TYR A  39      -4.107  -9.222   0.610  1.00 14.90           C  
ANISOU  250  CZ  TYR A  39     2037   1010   2616     77   -904    -89       C  
ATOM    251  OH  TYR A  39      -3.077  -8.319   0.517  1.00 18.89           O  
ANISOU  251  OH  TYR A  39     2277   1170   3731   -121  -1268    -92       O  
ATOM    252  H   TYR A  39      -4.995 -13.197   2.671  1.00 10.86           H  
ATOM    253  HA  TYR A  39      -7.341 -14.006   1.890  1.00 10.37           H  
ATOM    254  HB2 TYR A  39      -7.467 -12.452  -0.011  1.00 12.09           H  
ATOM    255  HB3 TYR A  39      -7.933 -11.819   1.374  1.00 12.09           H  
ATOM    256  HD1 TYR A  39      -5.294 -11.767  -0.959  1.00 11.78           H  
ATOM    257  N   HIS A  40      -6.206 -15.043  -0.127  1.00  8.65           N  
ANISOU  257  N   HIS A  40     1057   1031   1198    164     87   -173       N  
ATOM    258  CA  HIS A  40      -5.401 -15.669  -1.178  1.00  8.02           C  
ANISOU  258  CA  HIS A  40      990    967   1089    174     55    -92       C  
ATOM    259  C   HIS A  40      -4.882 -14.620  -2.144  1.00  7.74           C  
ANISOU  259  C   HIS A  40     1082    787   1074    155     31    -59       C  
ATOM    260  O   HIS A  40      -5.661 -13.815  -2.630  1.00  8.66           O  
ANISOU  260  O   HIS A  40     1105    879   1306    168     14     22       O  
ATOM    261  CB  HIS A  40      -6.289 -16.653  -1.953  1.00  8.34           C  
ANISOU  261  CB  HIS A  40     1019    917   1233    100     97    -19       C  
ATOM    262  CG  HIS A  40      -5.654 -17.148  -3.204  1.00  7.84           C  
ANISOU  262  CG  HIS A  40     1022    915   1041    -22     26     -9       C  
ATOM    263  ND1 HIS A  40      -4.749 -18.186  -3.223  1.00  7.79           N  
ANISOU  263  ND1 HIS A  40      919    871   1169     21     16    -60       N  
ATOM    264  CD2 HIS A  40      -5.724 -16.647  -4.461  1.00  9.09           C  
ANISOU  264  CD2 HIS A  40     1284    962   1209     88   -112    -45       C  
ATOM    265  CE1 HIS A  40      -4.320 -18.315  -4.470  1.00  7.91           C  
ANISOU  265  CE1 HIS A  40      979    937   1090    -61     59    -73       C  
ATOM    266  NE2 HIS A  40      -4.895 -17.398  -5.235  1.00  8.70           N  
ANISOU  266  NE2 HIS A  40     1261    990   1057   -155     27   -156       N  
ATOM    267  HA  HIS A  40      -4.652 -16.149  -0.790  1.00  9.62           H  
ATOM    268  HB2 HIS A  40      -6.477 -17.420  -1.389  1.00 10.01           H  
ATOM    269  HB3 HIS A  40      -7.117 -16.209  -2.194  1.00 10.01           H  
ATOM    270  HD2 HIS A  40      -6.247 -15.932  -4.743  1.00 10.91           H  
ATOM    271  HE1 HIS A  40      -3.719 -18.960  -4.766  1.00  9.49           H  
ATOM    272  HE2 HIS A  40      -4.776 -17.303  -6.081  1.00 10.45           H  
ATOM    273  N   PHE A  41      -3.581 -14.660  -2.453  1.00  7.98           N  
ANISOU  273  N   PHE A  41      954    870   1208     95    221     -4       N  
ATOM    274  CA  PHE A  41      -3.071 -13.743  -3.467  1.00  8.57           C  
ANISOU  274  CA  PHE A  41     1179    746   1331    189    222      4       C  
ATOM    275  C   PHE A  41      -2.197 -14.391  -4.536  1.00  8.47           C  
ANISOU  275  C   PHE A  41     1202    845   1172    214    186     82       C  
ATOM    276  O   PHE A  41      -1.879 -13.740  -5.536  1.00 10.79           O  
ANISOU  276  O   PHE A  41     1668   1041   1392    296    356    171       O  
ATOM    277  CB  PHE A  41      -2.298 -12.572  -2.837  1.00 10.19           C  
ANISOU  277  CB  PHE A  41     1343    981   1549    147    442   -143       C  
ATOM    278  CG  PHE A  41      -1.017 -12.964  -2.191  1.00  9.12           C  
ANISOU  278  CG  PHE A  41     1187    849   1428   -191    370   -240       C  
ATOM    279  CD1 PHE A  41      -0.966 -13.337  -0.846  1.00  9.70           C  
ANISOU  279  CD1 PHE A  41     1183   1044   1457   -173    296   -239       C  
ATOM    280  CD2 PHE A  41       0.185 -12.960  -2.927  1.00 10.20           C  
ANISOU  280  CD2 PHE A  41     1294   1027   1556   -194    354   -427       C  
ATOM    281  CE1 PHE A  41       0.218 -13.738  -0.263  1.00 11.25           C  
ANISOU  281  CE1 PHE A  41     1351   1298   1627   -387    407   -349       C  
ATOM    282  CE2 PHE A  41       1.368 -13.359  -2.323  1.00 10.83           C  
ANISOU  282  CE2 PHE A  41     1303   1248   1561   -333    420   -516       C  
ATOM    283  CZ  PHE A  41       1.398 -13.737  -0.998  1.00 10.97           C  
ANISOU  283  CZ  PHE A  41     1278   1138   1754   -252    324   -466       C  
ATOM    284  HA  PHE A  41      -3.835 -13.359  -3.926  1.00 10.28           H  
ATOM    285  HB3 PHE A  41      -2.856 -12.150  -2.165  1.00 12.23           H  
ATOM    286  HZ  PHE A  41       2.200 -13.990  -0.600  1.00 13.17           H  
ATOM    287  N   CYS A  42      -1.762 -15.618  -4.361  1.00  7.30           N  
ANISOU  287  N   CYS A  42     1024    747   1002     75    136    -27       N  
ATOM    288  CA  CYS A  42      -0.907 -16.276  -5.351  1.00  7.13           C  
ANISOU  288  CA  CYS A  42      980    780    951      5     33   -110       C  
ATOM    289  C   CYS A  42      -0.918 -17.759  -5.042  1.00  6.69           C  
ANISOU  289  C   CYS A  42      788    816    938     40     21     14       C  
ATOM    290  O   CYS A  42      -1.204 -18.173  -3.915  1.00  7.85           O  
ANISOU  290  O   CYS A  42     1034    917   1030     20     80    -24       O  
ATOM    291  CB  CYS A  42       0.564 -15.785  -5.311  1.00  8.50           C  
ANISOU  291  CB  CYS A  42     1040    863   1327    -58    197   -251       C  
ATOM    292  SG  CYS A  42       0.961 -14.354  -6.324  1.00  8.51           S  
ANISOU  292  SG  CYS A  42     1116    981   1138   -119    130   -122       S  
ATOM    293  H   CYS A  42      -1.942 -16.104  -3.675  1.00  8.76           H  
ATOM    294  HA  CYS A  42      -1.263 -16.135  -6.242  1.00  8.56           H  
ATOM    295  HB2 CYS A  42       0.783 -15.557  -4.393  1.00 10.20           H  
ATOM    296  HB3 CYS A  42       1.135 -16.512  -5.605  1.00 10.20           H  
ATOM    297  N   GLY A  43      -0.563 -18.559  -6.043  1.00  6.96           N  
ANISOU  297  N   GLY A  43      895    736   1012     17     33    -32       N  
ATOM    298  CA  GLY A  43      -0.285 -19.958  -5.834  1.00  7.17           C  
ANISOU  298  CA  GLY A  43      912    733   1080     11     89    -24       C  
ATOM    299  C   GLY A  43       1.195 -20.216  -5.561  1.00  6.50           C  
ANISOU  299  C   GLY A  43      808    735    924     18     24    -57       C  
ATOM    300  O   GLY A  43       2.039 -19.323  -5.584  1.00  7.00           O  
ANISOU  300  O   GLY A  43      886    746   1029     -8     -3    -40       O  
ATOM    301  HA2 GLY A  43      -0.807 -20.292  -5.088  1.00  8.61           H  
ATOM    302  N   GLY A  44       1.488 -21.492  -5.339  1.00  7.13           N  
ANISOU  302  N   GLY A  44      861    679   1170    -13    -15     11       N  
ATOM    303  CA  GLY A  44       2.843 -21.988  -5.182  1.00  6.74           C  
ANISOU  303  CA  GLY A  44      822    692   1048     33     26    -82       C  
ATOM    304  C   GLY A  44       2.800 -23.502  -5.228  1.00  6.82           C  
ANISOU  304  C   GLY A  44      890    719    984    -31     29    -46       C  
ATOM    305  O   GLY A  44       1.724 -24.105  -5.278  1.00  7.27           O  
ANISOU  305  O   GLY A  44      902    725   1135    -43     35    -34       O  
ATOM    306  H   GLY A  44       0.893 -22.110  -5.273  1.00  8.56           H  
ATOM    307  HA2 GLY A  44       3.407 -21.661  -5.901  1.00  8.09           H  
ATOM    308  HA3 GLY A  44       3.210 -21.703  -4.331  1.00  8.09           H  
ATOM    309  N   SER A  45       3.982 -24.110  -5.183  1.00  6.67           N  
ANISOU  309  N   SER A  45      790    685   1059     11    -61     -9       N  
ATOM    310  CA  SER A  45       4.134 -25.559  -5.270  1.00  7.25           C  
ANISOU  310  CA  SER A  45      985    688   1080     31    -38    -91       C  
ATOM    311  C   SER A  45       5.049 -26.040  -4.147  1.00  7.07           C  
ANISOU  311  C   SER A  45      886    642   1160      0    -48      3       C  
ATOM    312  O   SER A  45       6.154 -25.511  -3.968  1.00  7.91           O  
ANISOU  312  O   SER A  45      925    806   1274    -54   -143    155       O  
ATOM    313  CB  SER A  45       4.753 -25.955  -6.605  1.00  8.02           C  
ANISOU  313  CB  SER A  45     1103    756   1186    137   -104    -72       C  
ATOM    314  OG  SER A  45       3.968 -25.540  -7.688  1.00  8.62           O  
ANISOU  314  OG  SER A  45     1169    945   1159     42   -144    -89       O  
ATOM    315  H   SER A  45       4.730 -23.693  -5.101  1.00  8.00           H  
ATOM    316  HB2 SER A  45       5.629 -25.544  -6.677  1.00  9.62           H  
ATOM    317  HB3 SER A  45       4.841 -26.921  -6.634  1.00  9.62           H  
ATOM    318  HG  SER A  45       3.885 -24.704  -7.679  1.00 10.34           H  
ATOM    319  N   LEU A  46       4.602 -27.037  -3.413  1.00  7.46           N  
ANISOU  319  N   LEU A  46      981    688   1165     -3    -48     47       N  
ATOM    320  CA  LEU A  46       5.403 -27.643  -2.353  1.00  7.51           C  
ANISOU  320  CA  LEU A  46     1041    639   1172      1    -58     53       C  
ATOM    321  C   LEU A  46       6.434 -28.562  -2.986  1.00  7.92           C  
ANISOU  321  C   LEU A  46     1194    663   1151    -51   -133    131       C  
ATOM    322  O   LEU A  46       6.065 -29.486  -3.702  1.00  8.94           O  
ANISOU  322  O   LEU A  46     1208    799   1391     48   -108      2       O  
ATOM    323  CB  LEU A  46       4.487 -28.445  -1.433  1.00  8.66           C  
ANISOU  323  CB  LEU A  46     1201    823   1267     18    -28    124       C  
ATOM    324  CG  LEU A  46       5.120 -28.974  -0.145  1.00  9.09           C  
ANISOU  324  CG  LEU A  46     1468    804   1183    -55      5    205       C  
ATOM    325  CD1 LEU A  46       5.522 -27.827   0.782  1.00  9.68           C  
ANISOU  325  CD1 LEU A  46     1312   1149   1217    -21    -86    191       C  
ATOM    326  CD2 LEU A  46       4.136 -29.924   0.543  1.00 11.86           C  
ANISOU  326  CD2 LEU A  46     2207   1035   1263   -308     61     80       C  
ATOM    327  H   LEU A  46       3.824 -27.393  -3.505  1.00  8.95           H  
ATOM    328  HA  LEU A  46       5.857 -26.957  -1.838  1.00  9.01           H  
ATOM    329  HB2 LEU A  46       3.741 -27.880  -1.177  1.00 10.39           H  
ATOM    330  HB3 LEU A  46       4.154 -29.211  -1.927  1.00 10.39           H  
ATOM    331 HD11 LEU A  46       5.920 -28.195   1.586  1.00 11.62           H  
ATOM    332 HD13 LEU A  46       4.731 -27.313   1.008  1.00 11.62           H  
ATOM    333 HD23 LEU A  46       3.938 -30.661  -0.055  1.00 14.23           H  
ATOM    334  N   ILE A  47       7.718 -28.320  -2.735  1.00  8.68           N  
ANISOU  334  N   ILE A  47     1118    869   1310      6    -35    103       N  
ATOM    335  CA  ILE A  47       8.773 -29.124  -3.344  1.00 10.02           C  
ANISOU  335  CA  ILE A  47     1112   1055   1640    225    144    132       C  
ATOM    336  C   ILE A  47       9.517 -30.017  -2.346  1.00 10.12           C  
ANISOU  336  C   ILE A  47     1172    944   1729    257     22    339       C  
ATOM    337  O   ILE A  47      10.213 -30.942  -2.768  1.00 11.48           O  
ANISOU  337  O   ILE A  47     1427   1066   1869    352   -131    112       O  
ATOM    338  CB  ILE A  47       9.733 -28.301  -4.225  1.00 10.45           C  
ANISOU  338  CB  ILE A  47     1296   1164   1509     80    -47    122       C  
ATOM    339  CG1 ILE A  47      10.429 -27.245  -3.395  1.00 10.81           C  
ANISOU  339  CG1 ILE A  47     1131   1377   1598     -6    -78    178       C  
ATOM    340  CG2 ILE A  47       9.023 -27.743  -5.462  1.00 10.89           C  
ANISOU  340  CG2 ILE A  47     1362   1296   1481     10    -43     67       C  
ATOM    341  CD1 ILE A  47      11.695 -26.733  -4.059  1.00 13.60           C  
ANISOU  341  CD1 ILE A  47     1262   1802   2104   -353     10    135       C  
ATOM    342  H   ILE A  47       8.004 -27.696  -2.216  1.00 10.41           H  
ATOM    343 HG12 ILE A  47       9.828 -26.493  -3.271  1.00 12.97           H  
ATOM    344 HG13 ILE A  47      10.671 -27.624  -2.536  1.00 12.97           H  
ATOM    345 HG21 ILE A  47       9.683 -27.349  -6.054  1.00 13.07           H  
ATOM    346 HG22 ILE A  47       8.562 -28.466  -5.915  1.00 13.07           H  
ATOM    347  N  AASN A  48       9.326 -29.806  -1.053  0.47 10.62           N  
ANISOU  347  N  AASN A  48     1275   1086   1675    151   -109    400       N  
ATOM    348  N  BASN A  48       9.382 -29.777  -1.052  0.53 10.75           N  
ANISOU  348  N  BASN A  48     1430   1019   1638    331     52    223       N  
ATOM    349  CA AASN A  48       9.730 -30.734  -0.002  0.47 11.02           C  
ANISOU  349  CA AASN A  48     1236   1153   1798    167   -247    414       C  
ATOM    350  CA BASN A  48       9.769 -30.717  -0.001  0.53 10.88           C  
ANISOU  350  CA BASN A  48     1341    950   1843    164     47    302       C  
ATOM    351  C  AASN A  48       8.980 -30.293   1.249  0.47 11.02           C  
ANISOU  351  C  AASN A  48     1194   1151   1842    150   -340    315       C  
ATOM    352  C  BASN A  48       8.973 -30.307   1.237  0.53 10.89           C  
ANISOU  352  C  BASN A  48     1375    983   1778     54     81    335       C  
ATOM    353  O  AASN A  48       8.185 -29.352   1.196  0.47 12.16           O  
ANISOU  353  O  AASN A  48     1262   1451   1905    417   -414    337       O  
ATOM    354  O  BASN A  48       8.137 -29.404   1.158  0.53 11.94           O  
ANISOU  354  O  BASN A  48     1570   1285   1682    129    405    407       O  
ATOM    355  CB AASN A  48      11.252 -30.788   0.163  0.47 11.69           C  
ANISOU  355  CB AASN A  48     1387   1158   1897    224   -286    308       C  
ATOM    356  CB BASN A  48      11.299 -30.846   0.159  0.53 11.45           C  
ANISOU  356  CB BASN A  48     1371    879   2100    191    -38    134       C  
ATOM    357  CG AASN A  48      11.836 -29.456   0.512  0.47 11.57           C  
ANISOU  357  CG AASN A  48     1334   1182   1880    199     88    294       C  
ATOM    358  CG BASN A  48      11.951 -29.610   0.742  0.53 11.15           C  
ANISOU  358  CG BASN A  48     1217    877   2145     67    391    130       C  
ATOM    359  OD1AASN A  48      11.485 -28.862   1.535  0.47 12.77           O  
ANISOU  359  OD1AASN A  48     1459   1481   1912    143    258    118       O  
ATOM    360  OD1BASN A  48      11.297 -28.797   1.388  0.53  9.71           O  
ANISOU  360  OD1BASN A  48     1003    890   1797     55    -46    220       O  
ATOM    361  ND2AASN A  48      12.739 -28.970  -0.326  0.47 12.10           N  
ANISOU  361  ND2AASN A  48     1494   1141   1962    143    143    323       N  
ATOM    362  ND2BASN A  48      13.262 -29.483   0.544  0.53 13.95           N  
ANISOU  362  ND2BASN A  48     1395   1357   2546   -147    585    -81       N  
ATOM    363  H  AASN A  48       8.946 -29.099  -0.745  0.47 12.75           H  
ATOM    364  H  BASN A  48       9.055 -29.045  -0.741  0.53 12.91           H  
ATOM    365  N   SER A  49       9.218 -30.956   2.379  1.00 11.55           N  
ANISOU  365  N   SER A  49     1484   1068   1838     -8    -58    540       N  
ATOM    366  CA  SER A  49       8.394 -30.668   3.542  1.00 12.98           C  
ANISOU  366  CA  SER A  49     1841   1218   1874    -91    109    527       C  
ATOM    367  C   SER A  49       8.537 -29.247   4.055  1.00 11.89           C  
ANISOU  367  C   SER A  49     1530   1287   1700     21     98    584       C  
ATOM    368  O   SER A  49       7.668 -28.800   4.816  1.00 13.58           O  
ANISOU  368  O   SER A  49     1666   1480   2015     33    434    561       O  
ATOM    369  CB  SER A  49       8.708 -31.646   4.676  1.00 15.08           C  
ANISOU  369  CB  SER A  49     2387   1352   1990      6    257    774       C  
ATOM    370  OG  SER A  49      10.013 -31.425   5.154  1.00 15.90           O  
ANISOU  370  OG  SER A  49     2377   1494   2169    430    -47    680       O  
ATOM    371  H  ASER A  49       9.826 -31.553   2.494  0.47 13.86           H  
ATOM    372  H  BSER A  49       9.833 -31.545   2.499  0.53 13.86           H  
ATOM    373  HB2 SER A  49       8.078 -31.503   5.399  1.00 18.09           H  
ATOM    374  N  AGLN A  50       9.570 -28.519   3.649  0.61 10.89           N  
ANISOU  374  N  AGLN A  50     1588   1035   1515    387     11    411       N  
ATOM    375  N  BGLN A  50       9.637 -28.547   3.700  0.39 10.93           N  
ANISOU  375  N  BGLN A  50     1303   1123   1725    -78    104    541       N  
ATOM    376  CA AGLN A  50       9.767 -27.207   4.239  0.61 10.16           C  
ANISOU  376  CA AGLN A  50     1531   1112   1217    228    -73    252       C  
ATOM    377  CA BGLN A  50       9.972 -27.232   4.248  0.39 10.88           C  
ANISOU  377  CA BGLN A  50     1319   1255   1559     59     89    515       C  
ATOM    378  C  AGLN A  50       9.995 -26.087   3.232  0.61  8.19           C  
ANISOU  378  C  AGLN A  50      896   1006   1211     76    -43    200       C  
ATOM    379  C  BGLN A  50       9.907 -26.077   3.246  0.39  8.62           C  
ANISOU  379  C  BGLN A  50      836   1116   1323     67    -78    251       C  
ATOM    380  O  AGLN A  50      10.337 -24.972   3.648  0.61  8.17           O  
ANISOU  380  O  AGLN A  50      870   1024   1210    100    -21    216       O  
ATOM    381  O  BGLN A  50       9.960 -24.919   3.677  0.39  8.33           O  
ANISOU  381  O  BGLN A  50      747   1199   1217    111     24     84       O  
ATOM    382  CB AGLN A  50      10.888 -27.281   5.283  0.61 11.55           C  
ANISOU  382  CB AGLN A  50     1911   1508    969    360   -167    158       C  
ATOM    383  CB BGLN A  50      11.388 -27.256   4.883  0.39 12.82           C  
ANISOU  383  CB BGLN A  50     1903   1445   1524    205   -209    691       C  
ATOM    384  CG AGLN A  50      10.743 -26.235   6.308  0.61 13.33           C  
ANISOU  384  CG AGLN A  50     2011   1849   1206    307   -425    312       C  
ATOM    385  CG BGLN A  50      11.495 -28.010   6.213  0.39 14.38           C  
ANISOU  385  CG BGLN A  50     1894   1751   1819    354   -197    726       C  
ATOM    386  CD AGLN A  50      11.487 -26.554   7.581  0.61 13.11           C  
ANISOU  386  CD AGLN A  50     1978   1550   1453    439   -399    544       C  
ATOM    387  CD BGLN A  50      12.881 -27.935   6.830  0.39 15.55           C  
ANISOU  387  CD BGLN A  50     1729   2268   1912    508   -239    606       C  
ATOM    388  OE1AGLN A  50      12.146 -27.605   7.717  0.61 15.46           O  
ANISOU  388  OE1AGLN A  50     2588   1639   1649    232   -754    359       O  
ATOM    389  OE1BGLN A  50      13.806 -28.659   6.430  0.39 18.49           O  
ANISOU  389  OE1BGLN A  50     1916   2976   2134    975   -198    435       O  
ATOM    390  NE2AGLN A  50      11.398 -25.636   8.541  0.61 14.55           N  
ANISOU  390  NE2AGLN A  50     2184   1808   1536    453   -421    368       N  
ATOM    391  NE2BGLN A  50      13.034 -27.053   7.807  0.39 15.62           N  
ANISOU  391  NE2BGLN A  50     1823   2209   1903    295   -390    651       N  
ATOM    392  HA AGLN A  50       8.956 -26.981   4.721  0.61 12.19           H  
ATOM    393  HA BGLN A  50       9.342 -27.031   4.958  0.39 13.05           H  
ATOM    394  N   TRP A  51       9.777 -26.344   1.945  1.00  8.37           N  
ANISOU  394  N   TRP A  51     1032    959   1187    -15   -110    179       N  
ATOM    395  CA  TRP A  51      10.024 -25.329   0.925  1.00  7.79           C  
ANISOU  395  CA  TRP A  51      925    852   1181     42    -82    184       C  
ATOM    396  C   TRP A  51       8.941 -25.327  -0.142  1.00  7.66           C  
ANISOU  396  C   TRP A  51      946    807   1159    -48   -120    117       C  
ATOM    397  O   TRP A  51       8.498 -26.384  -0.619  1.00  8.18           O  
ANISOU  397  O   TRP A  51     1000    797   1310     26   -173    121       O  
ATOM    398  CB  TRP A  51      11.375 -25.561   0.241  1.00  8.13           C  
ANISOU  398  CB  TRP A  51     1026    928   1134    -36   -138    105       C  
ATOM    399  CG  TRP A  51      12.565 -25.259   1.103  1.00  8.31           C  
ANISOU  399  CG  TRP A  51      920   1026   1212     28    -54    213       C  
ATOM    400  CD1 TRP A  51      13.218 -26.109   1.961  1.00  9.29           C  
ANISOU  400  CD1 TRP A  51     1017   1153   1359    -37    -64    199       C  
ATOM    401  CD2 TRP A  51      13.246 -23.999   1.190  1.00  8.30           C  
ANISOU  401  CD2 TRP A  51      920   1172   1062     19    -85    151       C  
ATOM    402  NE1 TRP A  51      14.272 -25.457   2.550  1.00  9.10           N  
ANISOU  402  NE1 TRP A  51      949   1264   1245     23   -127    153       N  
ATOM    403  CE2 TRP A  51      14.315 -24.169   2.084  1.00  8.78           C  
ANISOU  403  CE2 TRP A  51      992   1200   1145    -31    -35    167       C  
ATOM    404  CE3 TRP A  51      13.074 -22.748   0.582  1.00  9.01           C  
ANISOU  404  CE3 TRP A  51     1067   1207   1149    -93   -108    159       C  
ATOM    405  CZ2 TRP A  51      15.215 -23.133   2.370  1.00  9.70           C  
ANISOU  405  CZ2 TRP A  51     1088   1369   1228   -126   -116    135       C  
ATOM    406  CZ3 TRP A  51      13.949 -21.735   0.868  1.00 10.75           C  
ANISOU  406  CZ3 TRP A  51     1257   1521   1307   -336   -263    125       C  
ATOM    407  CH2 TRP A  51      15.014 -21.928   1.749  1.00 10.53           C  
ANISOU  407  CH2 TRP A  51     1276   1454   1273   -334   -234    106       C  
ATOM    408  H  ATRP A  51       9.488 -27.094   1.637  0.61 10.04           H  
ATOM    409  H  BTRP A  51       9.546 -27.110   1.628  0.39 10.04           H  
ATOM    410  HA  TRP A  51      10.041 -24.454   1.343  1.00  9.34           H  
ATOM    411  HB2 TRP A  51      11.432 -26.492  -0.025  1.00  9.76           H  
ATOM    412  HB3 TRP A  51      11.427 -24.993  -0.543  1.00  9.76           H  
ATOM    413  HD1 TRP A  51      12.989 -26.999   2.108  1.00 11.15           H  
ATOM    414  HE3 TRP A  51      12.391 -22.618  -0.037  1.00 10.81           H  
ATOM    415  HZ2 TRP A  51      15.905 -23.250   2.982  1.00 11.64           H  
ATOM    416  HH2 TRP A  51      15.577 -21.214   1.946  1.00 12.64           H  
ATOM    417  N   VAL A  52       8.582 -24.109  -0.541  1.00  7.56           N  
ANISOU  417  N   VAL A  52      900    708   1265     39   -142     63       N  
ATOM    418  CA  VAL A  52       7.640 -23.824  -1.612  1.00  7.19           C  
ANISOU  418  CA  VAL A  52      894    693   1145      3    -82     16       C  
ATOM    419  C   VAL A  52       8.329 -23.013  -2.699  1.00  7.34           C  
ANISOU  419  C   VAL A  52      881    690   1218     25    -79     77       C  
ATOM    420  O   VAL A  52       9.115 -22.111  -2.400  1.00  8.30           O  
ANISOU  420  O   VAL A  52      990    872   1292   -137    -34     68       O  
ATOM    421  CB  VAL A  52       6.447 -23.044  -1.019  1.00  7.91           C  
ANISOU  421  CB  VAL A  52      976    856   1172    101    -35     95       C  
ATOM    422  CG1 VAL A  52       5.564 -22.396  -2.087  1.00  8.18           C  
ANISOU  422  CG1 VAL A  52      953    831   1322    190    -31    -23       C  
ATOM    423  CG2 VAL A  52       5.613 -23.985  -0.138  1.00  9.29           C  
ANISOU  423  CG2 VAL A  52      998   1157   1374    143     69    186       C  
ATOM    424  H   VAL A  52       8.892 -23.393  -0.181  1.00  9.07           H  
ATOM    425  HA  VAL A  52       7.315 -24.653  -1.996  1.00  8.63           H  
ATOM    426 HG11 VAL A  52       4.837 -21.924  -1.652  1.00  9.81           H  
ATOM    427 HG12 VAL A  52       6.100 -21.774  -2.604  1.00  9.81           H  
ATOM    428 HG13 VAL A  52       5.210 -23.089  -2.666  1.00  9.81           H  
ATOM    429 HG21 VAL A  52       4.864 -23.492   0.231  1.00 11.15           H  
ATOM    430 HG23 VAL A  52       6.172 -24.325   0.578  1.00 11.15           H  
ATOM    431  N  AVAL A  53       8.009 -23.338  -3.974  0.54  7.54           N  
ANISOU  431  N  AVAL A  53      921    923   1021    370    -40    143       N  
ATOM    432  N  BVAL A  53       7.983 -23.267  -3.942  0.46  7.35           N  
ANISOU  432  N  BVAL A  53      871    761   1161   -242   -106    -17       N  
ATOM    433  CA AVAL A  53       8.382 -22.557  -5.162  0.54  7.36           C  
ANISOU  433  CA AVAL A  53     1003    698   1094     29    -18    264       C  
ATOM    434  CA BVAL A  53       8.470 -22.433  -5.016  0.46  7.69           C  
ANISOU  434  CA BVAL A  53      862    768   1291    -53     68    101       C  
ATOM    435  C  AVAL A  53       7.185 -21.699  -5.570  0.54  6.37           C  
ANISOU  435  C  AVAL A  53      941    722    756    117     33    118       C  
ATOM    436  C  BVAL A  53       7.283 -21.731  -5.666  0.46  7.51           C  
ANISOU  436  C  BVAL A  53      878    901   1075    -96     -5     -7       C  
ATOM    437  O  AVAL A  53       6.046 -22.190  -5.645  0.54  6.11           O  
ANISOU  437  O  AVAL A  53      848    544    928    -51    123    -10       O  
ATOM    438  O  BVAL A  53       6.242 -22.350  -5.943  0.46  6.99           O  
ANISOU  438  O  BVAL A  53      791    854   1013     72    -32    -50       O  
ATOM    439  CB AVAL A  53       8.826 -23.471  -6.334  0.54  8.06           C  
ANISOU  439  CB AVAL A  53      942    850   1269     66    143    146       C  
ATOM    440  CB BVAL A  53       9.340 -23.229  -5.998  0.46  8.21           C  
ANISOU  440  CB BVAL A  53      892    849   1379     56    -45    -19       C  
ATOM    441  CG1AVAL A  53       8.914 -22.712  -7.702  0.54  8.85           C  
ANISOU  441  CG1AVAL A  53     1304    909   1149    110      5     50       C  
ATOM    442  CG1BVAL A  53       8.491 -24.157  -6.809  0.46  8.55           C  
ANISOU  442  CG1BVAL A  53     1102    904   1242     38   -126   -103       C  
ATOM    443  CG2AVAL A  53      10.138 -24.173  -6.013  0.54  9.48           C  
ANISOU  443  CG2AVAL A  53     1159   1230   1212    343     81     74       C  
ATOM    444  CG2BVAL A  53      10.166 -22.279  -6.854  0.46  8.60           C  
ANISOU  444  CG2BVAL A  53     1106    886   1277    -74    124     81       C  
ATOM    445  HA AVAL A  53       9.119 -21.966  -4.940  0.54  8.83           H  
ATOM    446  HA BVAL A  53       9.034 -21.743  -4.632  0.46  9.23           H  
ATOM    447  HB AVAL A  53       8.155 -24.164  -6.441  0.54  9.67           H  
ATOM    448 HG12BVAL A  53       8.043 -24.777  -6.213  0.46 10.26           H  
ATOM    449  N   SER A  54       7.442 -20.428  -5.872  1.00  6.80           N  
ANISOU  449  N   SER A  54      859    691   1035    -42    -72     60       N  
ATOM    450  CA  SER A  54       6.408 -19.564  -6.426  1.00  6.49           C  
ANISOU  450  CA  SER A  54      866    647    954    -21    -95    -29       C  
ATOM    451  C   SER A  54       7.073 -18.590  -7.395  1.00  6.47           C  
ANISOU  451  C   SER A  54      847    714    895     -7   -106    -82       C  
ATOM    452  O   SER A  54       8.235 -18.764  -7.787  1.00  6.75           O  
ANISOU  452  O   SER A  54      816    803    947     -4    -43    -16       O  
ATOM    453  CB  SER A  54       5.667 -18.874  -5.270  1.00  6.60           C  
ANISOU  453  CB  SER A  54      855    751    903     -5    -44     69       C  
ATOM    454  OG  SER A  54       4.555 -18.115  -5.716  1.00  7.14           O  
ANISOU  454  OG  SER A  54      945    784    984     79    -20    -19       O  
ATOM    455  H  ASER A  54       8.204 -20.045  -5.765  0.54  8.17           H  
ATOM    456  H  BSER A  54       8.169 -20.007  -5.690  0.46  8.17           H  
ATOM    457  HA  SER A  54       5.770 -20.101  -6.922  1.00  7.79           H  
ATOM    458  HB2 SER A  54       5.352 -19.554  -4.654  1.00  7.92           H  
ATOM    459  HB3 SER A  54       6.285 -18.281  -4.815  1.00  7.92           H  
ATOM    460  N   ALA A  55       6.308 -17.579  -7.832  1.00  6.63           N  
ANISOU  460  N   ALA A  55      807    712   1000     53    -54    -54       N  
ATOM    461  CA  ALA A  55       6.820 -16.535  -8.714  1.00  6.41           C  
ANISOU  461  CA  ALA A  55      876    704    855    -14     38      9       C  
ATOM    462  C   ALA A  55       7.410 -15.406  -7.874  1.00  6.69           C  
ANISOU  462  C   ALA A  55      896    684    963      3     17     51       C  
ATOM    463  O   ALA A  55       6.846 -15.028  -6.847  1.00  7.72           O  
ANISOU  463  O   ALA A  55     1082    853    999   -159    145   -146       O  
ATOM    464  CB  ALA A  55       5.703 -15.981  -9.595  1.00  7.22           C  
ANISOU  464  CB  ALA A  55     1009    777    957      0     -5     56       C  
ATOM    465  H   ALA A  55       5.480 -17.480  -7.625  1.00  7.96           H  
ATOM    466  HA  ALA A  55       7.516 -16.898  -9.283  1.00  7.69           H  
ATOM    467  HB1 ALA A  55       6.068 -15.291 -10.171  1.00  8.66           H  
ATOM    468  HB3 ALA A  55       5.010 -15.607  -9.029  1.00  8.66           H  
ATOM    469  N   ALA A  56       8.531 -14.827  -8.326  1.00  6.47           N  
ANISOU  469  N   ALA A  56      873    668    916    -47      3      2       N  
ATOM    470  CA  ALA A  56       9.076 -13.648  -7.670  1.00  6.56           C  
ANISOU  470  CA  ALA A  56      863    717    911    -23    -67     46       C  
ATOM    471  C   ALA A  56       8.102 -12.483  -7.645  1.00  7.05           C  
ANISOU  471  C   ALA A  56      912    829    937   -128     53    -50       C  
ATOM    472  O   ALA A  56       8.122 -11.686  -6.695  1.00  7.65           O  
ANISOU  472  O   ALA A  56     1008    864   1035    -83     99   -139       O  
ATOM    473  CB  ALA A  56      10.373 -13.218  -8.356  1.00  7.44           C  
ANISOU  473  CB  ALA A  56      831    897   1099    -38    -17     41       C  
ATOM    474  H   ALA A  56       8.985 -15.099  -9.003  1.00  7.76           H  
ATOM    475  HA  ALA A  56       9.288 -13.874  -6.751  1.00  7.87           H  
ATOM    476  HB3 ALA A  56      10.186 -13.013  -9.285  1.00  8.93           H  
ATOM    477  N   HIS A  57       7.253 -12.357  -8.665  1.00  7.11           N  
ANISOU  477  N   HIS A  57      954    797    950    105     -4    -84       N  
ATOM    478  CA  HIS A  57       6.337 -11.230  -8.659  1.00  8.66           C  
ANISOU  478  CA  HIS A  57     1170    966   1154    175     -9    -68       C  
ATOM    479  C   HIS A  57       5.246 -11.374  -7.589  1.00  8.80           C  
ANISOU  479  C   HIS A  57     1057   1096   1192    221    -92   -267       C  
ATOM    480  O   HIS A  57       4.535 -10.406  -7.323  1.00 10.67           O  
ANISOU  480  O   HIS A  57     1246   1315   1495    474     31   -246       O  
ATOM    481  CB  HIS A  57       5.798 -10.924 -10.067  1.00  9.02           C  
ANISOU  481  CB  HIS A  57     1146    975   1309     65    -57     22       C  
ATOM    482  CG  HIS A  57       4.626 -11.737 -10.475  1.00  9.18           C  
ANISOU  482  CG  HIS A  57     1065   1179   1245     45      3     19       C  
ATOM    483  ND1 HIS A  57       4.708 -12.829 -11.315  1.00  9.19           N  
ANISOU  483  ND1 HIS A  57     1079   1279   1135    -11    -61   -112       N  
ATOM    484  CD2 HIS A  57       3.317 -11.583 -10.171  1.00 11.03           C  
ANISOU  484  CD2 HIS A  57      992   1704   1493     49    -35   -161       C  
ATOM    485  CE1 HIS A  57       3.481 -13.285 -11.537  1.00 11.02           C  
ANISOU  485  CE1 HIS A  57     1307   1549   1332   -117   -106   -254       C  
ATOM    486  NE2 HIS A  57       2.624 -12.556 -10.840  1.00 11.79           N  
ANISOU  486  NE2 HIS A  57     1182   1991   1309     18     -5   -275       N  
ATOM    487  H   HIS A  57       7.191 -12.886  -9.340  1.00  8.53           H  
ATOM    488  HE1 HIS A  57       3.265 -14.027 -12.055  1.00 13.23           H  
ATOM    489  N   CYS A  58       5.166 -12.537  -6.933  1.00  8.27           N  
ANISOU  489  N   CYS A  58      872   1080   1190      8    103   -297       N  
ATOM    490  CA  CYS A  58       4.308 -12.770  -5.778  1.00  9.67           C  
ANISOU  490  CA  CYS A  58      984   1380   1312   -210    174   -403       C  
ATOM    491  C   CYS A  58       4.955 -12.364  -4.455  1.00 10.55           C  
ANISOU  491  C   CYS A  58     1244   1606   1157   -440    334   -453       C  
ATOM    492  O   CYS A  58       4.310 -12.476  -3.419  1.00 14.53           O  
ANISOU  492  O   CYS A  58     1545   2579   1398  -1000    402   -689       O  
ATOM    493  CB  CYS A  58       3.927 -14.256  -5.698  1.00  9.96           C  
ANISOU  493  CB  CYS A  58     1078   1449   1257   -202    148   -283       C  
ATOM    494  SG  CYS A  58       2.838 -14.826  -7.022  1.00  9.68           S  
ANISOU  494  SG  CYS A  58     1096   1367   1214   -200    103   -346       S  
ATOM    495  H   CYS A  58       5.623 -13.231  -7.153  1.00  9.92           H  
ATOM    496  HA  CYS A  58       3.492 -12.256  -5.882  1.00 11.61           H  
ATOM    497  HB2 CYS A  58       4.735 -14.791  -5.724  1.00 11.95           H  
ATOM    498  N   TYR A  59       6.196 -11.914  -4.453  1.00  8.66           N  
ANISOU  498  N   TYR A  59     1009   1161   1122   -250    154   -226       N  
ATOM    499  CA  TYR A  59       6.855 -11.552  -3.206  1.00  8.45           C  
ANISOU  499  CA  TYR A  59     1010   1064   1136   -170     71   -249       C  
ATOM    500  C   TYR A  59       6.047 -10.503  -2.431  1.00  9.02           C  
ANISOU  500  C   TYR A  59     1076   1195   1155   -255    102   -257       C  
ATOM    501  O   TYR A  59       5.618  -9.480  -2.976  1.00  9.99           O  
ANISOU  501  O   TYR A  59     1132   1237   1428    -76    115   -252       O  
ATOM    502  CB  TYR A  59       8.284 -11.007  -3.493  1.00  9.24           C  
ANISOU  502  CB  TYR A  59      999   1368   1143   -133     59   -336       C  
ATOM    503  CG  TYR A  59       8.845 -10.319  -2.272  1.00 10.42           C  
ANISOU  503  CG  TYR A  59      996   1653   1310   -213    255   -224       C  
ATOM    504  CD1 TYR A  59       9.340 -11.016  -1.178  1.00 11.99           C  
ANISOU  504  CD1 TYR A  59     1254   1960   1343   -359    -59    -20       C  
ATOM    505  CD2 TYR A  59       8.734  -8.948  -2.156  1.00 12.20           C  
ANISOU  505  CD2 TYR A  59     1538   1602   1497   -501    200   -433       C  
ATOM    506  CE1 TYR A  59       9.726 -10.338   0.029  1.00 12.52           C  
ANISOU  506  CE1 TYR A  59     1368   2111   1277   -597    -31   -389       C  
ATOM    507  CE2 TYR A  59       9.094  -8.278  -0.980  1.00 14.34           C  
ANISOU  507  CE2 TYR A  59     1719   1983   1749   -833    307   -650       C  
ATOM    508  CZ  TYR A  59       9.586  -8.983   0.080  1.00 15.09           C  
ANISOU  508  CZ  TYR A  59     1701   2428   1603   -995    232   -609       C  
ATOM    509  OH  TYR A  59       9.908  -8.296   1.219  1.00 18.82           O  
ANISOU  509  OH  TYR A  59     2355   3029   1766  -1315    238   -862       O  
ATOM    510  H   TYR A  59       6.681 -11.808  -5.156  1.00 10.40           H  
ATOM    511  HA  TYR A  59       6.938 -12.341  -2.649  1.00 10.14           H  
ATOM    512  HD1 TYR A  59       9.394 -11.944  -1.216  1.00 14.39           H  
ATOM    513  HD2 TYR A  59       8.362  -8.464  -2.857  1.00 14.64           H  
ATOM    514  N   LYS A  60       5.946 -10.725  -1.133  1.00  9.78           N  
ANISOU  514  N   LYS A  60     1180   1399   1136   -176    233   -324       N  
ATOM    515  CA  LYS A  60       5.536  -9.710  -0.161  1.00 12.36           C  
ANISOU  515  CA  LYS A  60     1471   1813   1412   -312    320   -569       C  
ATOM    516  C   LYS A  60       5.929 -10.246   1.203  1.00 12.85           C  
ANISOU  516  C   LYS A  60     1735   1883   1266   -687    372   -504       C  
ATOM    517  O   LYS A  60       6.302 -11.410   1.343  1.00 13.14           O  
ANISOU  517  O   LYS A  60     1843   1933   1215   -411     24   -301       O  
ATOM    518  CB  LYS A  60       4.043  -9.404  -0.239  1.00 13.47           C  
ANISOU  518  CB  LYS A  60     1680   1545   1892   -354    542   -502       C  
ATOM    519  CG  LYS A  60       3.258 -10.621   0.075  1.00 13.03           C  
ANISOU  519  CG  LYS A  60     1758   1203   1991   -140    534   -495       C  
ATOM    520  CD  LYS A  60       1.823 -10.356   0.366  1.00 15.08           C  
ANISOU  520  CD  LYS A  60     1602   1625   2503   -206    568   -219       C  
ATOM    521  CE  LYS A  60       1.107  -9.888  -0.841  1.00 14.24           C  
ANISOU  521  CE  LYS A  60     1604   1584   2222   -607    561   -302       C  
ATOM    522  NZ  LYS A  60      -0.337  -9.400  -0.507  1.00 16.05           N  
ANISOU  522  NZ  LYS A  60     1599   1945   2553   -560    338    307       N  
ATOM    523  H   LYS A  60       6.116 -11.486  -0.770  1.00 11.73           H  
ATOM    524  HG2 LYS A  60       3.303 -11.230  -0.679  1.00 15.64           H  
ATOM    525  HZ3 LYS A  60      -0.305  -8.725   0.072  1.00 19.26           H  
ATOM    526  N  ASER A  61       5.855  -9.371   2.202  0.62 14.91           N  
ANISOU  526  N  ASER A  61     2380   2109   1175  -1078    487   -562       N  
ATOM    527  N  BSER A  61       5.868  -9.384   2.211  0.38 16.07           N  
ANISOU  527  N  BSER A  61     2469   2249   1386   -857    284   -797       N  
ATOM    528  CA ASER A  61       5.979  -9.807   3.589  0.62 16.97           C  
ANISOU  528  CA ASER A  61     2864   2299   1286  -1450    609   -504       C  
ATOM    529  CA BSER A  61       6.036  -9.865   3.577  0.38 19.34           C  
ANISOU  529  CA BSER A  61     3195   2528   1627   -993    300   -888       C  
ATOM    530  C  ASER A  61       4.659 -10.400   4.096  0.62 15.27           C  
ANISOU  530  C  ASER A  61     2618   1824   1359  -1147    664   -580       C  
ATOM    531  C  BSER A  61       4.687 -10.299   4.155  0.38 18.82           C  
ANISOU  531  C  BSER A  61     3338   2209   1605   -890    577   -814       C  
ATOM    532  O  ASER A  61       3.595 -10.262   3.481  0.62 15.85           O  
ANISOU  532  O  ASER A  61     2609   1716   1698   -899    884   -757       O  
ATOM    533  O  BSER A  61       3.623  -9.955   3.634  0.38 21.56           O  
ANISOU  533  O  BSER A  61     3780   2356   2057   -743    602   -737       O  
ATOM    534  CB ASER A  61       6.394  -8.640   4.481  0.62 20.62           C  
ANISOU  534  CB ASER A  61     3493   2658   1683  -1678    798   -531       C  
ATOM    535  CB BSER A  61       6.713  -8.808   4.457  0.38 22.33           C  
ANISOU  535  CB BSER A  61     3646   2856   1984  -1096    176  -1067       C  
ATOM    536  OG ASER A  61       5.428  -7.617   4.413  0.62 23.17           O  
ANISOU  536  OG ASER A  61     3868   2832   2105  -1669    889   -909       O  
ATOM    537  OG BSER A  61       6.419  -7.500   4.003  0.38 23.69           O  
ANISOU  537  OG BSER A  61     3832   2811   2359  -1156    267  -1203       O  
ATOM    538  N   GLY A  62       4.743 -11.080   5.230  1.00 17.22           N  
ANISOU  538  N   GLY A  62     3055   1869   1617  -1031    705   -668       N  
ATOM    539  CA  GLY A  62       3.532 -11.516   5.897  1.00 17.22           C  
ANISOU  539  CA  GLY A  62     2857   2005   1680  -1057    608   -551       C  
ATOM    540  C   GLY A  62       2.839 -12.691   5.241  1.00 14.30           C  
ANISOU  540  C   GLY A  62     2096   1682   1654   -776    588   -474       C  
ATOM    541  O   GLY A  62       1.591 -12.774   5.292  1.00 16.25           O  
ANISOU  541  O   GLY A  62     2249   1706   2218   -467    726   -462       O  
ATOM    542  N   ILE A  63       3.605 -13.630   4.670  1.00 11.33           N  
ANISOU  542  N   ILE A  63     1668   1314   1325   -442    144   -203       N  
ATOM    543  CA  ILE A  63       3.026 -14.769   3.967  1.00 10.16           C  
ANISOU  543  CA  ILE A  63     1339   1083   1438   -260     20   -121       C  
ATOM    544  C   ILE A  63       2.752 -15.921   4.932  1.00  9.24           C  
ANISOU  544  C   ILE A  63     1113   1045   1353   -143   -116   -145       C  
ATOM    545  O   ILE A  63       3.649 -16.385   5.662  1.00 10.39           O  
ANISOU  545  O   ILE A  63     1072   1377   1497   -172   -147     94       O  
ATOM    546  CB  ILE A  63       3.925 -15.239   2.812  1.00 10.32           C  
ANISOU  546  CB  ILE A  63     1411   1133   1377   -179     95   -141       C  
ATOM    547  CG1 ILE A  63       4.105 -14.108   1.802  1.00 12.48           C  
ANISOU  547  CG1 ILE A  63     2042   1266   1434   -181    208   -314       C  
ATOM    548  CG2 ILE A  63       3.344 -16.475   2.152  1.00 11.91           C  
ANISOU  548  CG2 ILE A  63     1675   1269   1582   -173    -76   -326       C  
ATOM    549  CD1 ILE A  63       5.029 -14.447   0.636  1.00 14.65           C  
ANISOU  549  CD1 ILE A  63     2213   1755   1596   -110    327   -163       C  
ATOM    550  H   ILE A  63       4.465 -13.624   4.679  1.00 13.60           H  
ATOM    551  HA  ILE A  63       2.176 -14.498   3.586  1.00 12.19           H  
ATOM    552 HG13 ILE A  63       4.469 -13.333   2.258  1.00 14.97           H  
ATOM    553 HG23 ILE A  63       2.463 -16.264   1.804  1.00 14.30           H  
ATOM    554  N   GLN A  64       1.520 -16.429   4.869  1.00  8.73           N  
ANISOU  554  N   GLN A  64     1043    950   1325      7   -124   -130       N  
ATOM    555  CA  GLN A  64       1.157 -17.720   5.426  1.00  8.24           C  
ANISOU  555  CA  GLN A  64      953    946   1234     39    -81    -53       C  
ATOM    556  C   GLN A  64       0.914 -18.688   4.282  1.00  8.03           C  
ANISOU  556  C   GLN A  64      902   1001   1148    -26   -104    -67       C  
ATOM    557  O   GLN A  64       0.131 -18.392   3.373  1.00  9.34           O  
ANISOU  557  O   GLN A  64     1229    976   1345    178   -275    -83       O  
ATOM    558  CB  GLN A  64      -0.082 -17.606   6.322  1.00  8.83           C  
ANISOU  558  CB  GLN A  64     1100    973   1282     34     -5   -155       C  
ATOM    559  CG  GLN A  64      -0.399 -18.915   7.050  1.00  9.51           C  
ANISOU  559  CG  GLN A  64     1150   1177   1287      3    -87    -69       C  
ATOM    560  CD  GLN A  64      -1.694 -18.815   7.821  1.00  9.97           C  
ANISOU  560  CD  GLN A  64     1121   1313   1352   -114     67   -231       C  
ATOM    561  OE1 GLN A  64      -2.750 -18.603   7.237  1.00 11.20           O  
ANISOU  561  OE1 GLN A  64     1067   1705   1485    -31     81   -381       O  
ATOM    562  NE2 GLN A  64      -1.627 -18.956   9.137  1.00 12.25           N  
ANISOU  562  NE2 GLN A  64     1611   1649   1394    -61    230   -172       N  
ATOM    563  H   GLN A  64       0.859 -16.026   4.495  1.00 10.48           H  
ATOM    564  HA  GLN A  64       1.891 -18.058   5.962  1.00  9.89           H  
ATOM    565  HB2 GLN A  64       0.072 -16.920   6.990  1.00 10.59           H  
ATOM    566  HB3 GLN A  64      -0.848 -17.373   5.775  1.00 10.59           H  
ATOM    567  HG3 GLN A  64       0.312 -19.105   7.682  1.00 11.41           H  
ATOM    568  N   VAL A  65       1.587 -19.814   4.311  1.00  7.42           N  
ANISOU  568  N   VAL A  65      841    920   1058      4    -68    -29       N  
ATOM    569  CA  VAL A  65       1.407 -20.848   3.311  1.00  7.44           C  
ANISOU  569  CA  VAL A  65      927    919    980    -62    -15    -31       C  
ATOM    570  C   VAL A  65       0.263 -21.745   3.750  1.00  7.29           C  
ANISOU  570  C   VAL A  65      847    994    930     24     35     29       C  
ATOM    571  O   VAL A  65       0.238 -22.236   4.878  1.00  8.54           O  
ANISOU  571  O   VAL A  65      988   1261    997   -114    -54    119       O  
ATOM    572  CB  VAL A  65       2.702 -21.648   3.119  1.00  8.62           C  
ANISOU  572  CB  VAL A  65     1008   1026   1243     74    101    -66       C  
ATOM    573  CG1 VAL A  65       2.476 -22.775   2.137  1.00 11.31           C  
ANISOU  573  CG1 VAL A  65     1081   1288   1926    -47    350   -411       C  
ATOM    574  CG2 VAL A  65       3.812 -20.728   2.613  1.00 10.13           C  
ANISOU  574  CG2 VAL A  65      966   1195   1687    -59    165     -6       C  
ATOM    575  H   VAL A  65       2.168 -20.012   4.913  1.00  8.91           H  
ATOM    576  HA  VAL A  65       1.170 -20.440   2.464  1.00  8.92           H  
ATOM    577  HB  VAL A  65       2.978 -22.028   3.967  1.00 10.35           H  
ATOM    578 HG22 VAL A  65       3.541 -20.343   1.765  1.00 12.15           H  
ATOM    579 HG23 VAL A  65       3.960 -20.024   3.264  1.00 12.15           H  
ATOM    580  N   ARG A  66      -0.698 -21.961   2.856  1.00  7.07           N  
ANISOU  580  N   ARG A  66      898    878    911      2     29     19       N  
ATOM    581  CA  ARG A  66      -1.868 -22.792   3.141  1.00  7.06           C  
ANISOU  581  CA  ARG A  66      868    856    956    -29     48      3       C  
ATOM    582  C   ARG A  66      -1.813 -24.017   2.247  1.00  6.91           C  
ANISOU  582  C   ARG A  66      840    864    922     -6     84     27       C  
ATOM    583  O   ARG A  66      -1.967 -23.920   1.017  1.00  7.28           O  
ANISOU  583  O   ARG A  66     1068    741    958     30      1      1       O  
ATOM    584  CB  ARG A  66      -3.159 -21.998   3.007  1.00  7.15           C  
ANISOU  584  CB  ARG A  66      865    842   1010     59     20    -60       C  
ATOM    585  CG  ARG A  66      -3.202 -20.838   3.996  1.00  7.30           C  
ANISOU  585  CG  ARG A  66      863    932    978     38     74    -58       C  
ATOM    586  CD  ARG A  66      -4.584 -20.179   4.065  1.00  7.58           C  
ANISOU  586  CD  ARG A  66      932    868   1080     58     78    -53       C  
ATOM    587  NE  ARG A  66      -4.637 -19.350   5.251  1.00  7.84           N  
ANISOU  587  NE  ARG A  66      816   1018   1143     30    115   -110       N  
ATOM    588  CZ  ARG A  66      -5.756 -19.001   5.875  1.00  8.53           C  
ANISOU  588  CZ  ARG A  66      925   1214   1103      6     69   -134       C  
ATOM    589  NH1 ARG A  66      -6.946 -19.194   5.310  1.00  9.27           N  
ANISOU  589  NH1 ARG A  66     1049   1227   1248     23    140   -157       N  
ATOM    590  NH2 ARG A  66      -5.667 -18.400   7.052  1.00 10.43           N  
ANISOU  590  NH2 ARG A  66     1062   1639   1263     59    144   -373       N  
ATOM    591  H   ARG A  66      -0.697 -21.632   2.061  1.00  8.49           H  
ATOM    592  HA  ARG A  66      -1.810 -23.100   4.059  1.00  8.47           H  
ATOM    593  HB2 ARG A  66      -3.211 -21.630   2.111  1.00  8.58           H  
ATOM    594  HG2 ARG A  66      -2.984 -21.169   4.882  1.00  8.76           H  
ATOM    595  HD2 ARG A  66      -4.699 -19.604   3.292  1.00  9.10           H  
ATOM    596  HE  ARG A  66      -3.893 -19.064   5.574  1.00  9.40           H  
ATOM    597 HH11 ARG A  66      -7.004 -19.624   4.567  1.00 11.13           H  
ATOM    598 HH21 ARG A  66      -4.895 -18.229   7.390  1.00 12.52           H  
ATOM    599  N  ALEU A  67      -1.578 -25.160   2.872  0.53  8.03           N  
ANISOU  599  N  ALEU A  67     1183    897    971   -344    128    101       N  
ATOM    600  N  BLEU A  67      -1.527 -25.162   2.871  0.47  6.71           N  
ANISOU  600  N  BLEU A  67      878    752    920    365   -136    -57       N  
ATOM    601  CA ALEU A  67      -1.475 -26.451   2.221  0.53  8.57           C  
ANISOU  601  CA ALEU A  67     1175    909   1173   -108    -78     53       C  
ATOM    602  CA BLEU A  67      -1.441 -26.473   2.248  0.47  6.53           C  
ANISOU  602  CA BLEU A  67      955    633    893    180      5     99       C  
ATOM    603  C  ALEU A  67      -2.756 -27.235   2.464  0.53  8.06           C  
ANISOU  603  C  ALEU A  67     1038    833   1190     80   -111    -81       C  
ATOM    604  C  BLEU A  67      -2.750 -27.222   2.457  0.47  6.91           C  
ANISOU  604  C  BLEU A  67      975    671    982    -91     89    142       C  
ATOM    605  O  ALEU A  67      -3.508 -26.962   3.401  0.53  8.88           O  
ANISOU  605  O  ALEU A  67     1198    958   1217    237    -41   -193       O  
ATOM    606  O  BLEU A  67      -3.507 -26.926   3.382  0.47  7.87           O  
ANISOU  606  O  BLEU A  67     1004   1043    941   -247     92    113       O  
ATOM    607  CB ALEU A  67      -0.282 -27.235   2.777  0.53  9.47           C  
ANISOU  607  CB ALEU A  67     1281   1050   1266   -211    -66     49       C  
ATOM    608  CB BLEU A  67      -0.305 -27.284   2.880  0.47  6.87           C  
ANISOU  608  CB BLEU A  67      856    871    886    311     30     81       C  
ATOM    609  CG ALEU A  67       1.055 -26.482   2.771  0.53  9.00           C  
ANISOU  609  CG ALEU A  67     1041   1070   1307    -39   -140     29       C  
ATOM    610  CG BLEU A  67       1.046 -26.561   2.939  0.47  7.97           C  
ANISOU  610  CG BLEU A  67      976    861   1191    175     -9    121       C  
ATOM    611  CD1ALEU A  67       1.390 -25.922   4.145  0.53 10.52           C  
ANISOU  611  CD1ALEU A  67     1193   1402   1404   -159   -136   -108       C  
ATOM    612  CD1BLEU A  67       2.070 -27.459   3.638  0.47  9.96           C  
ANISOU  612  CD1BLEU A  67     1086   1118   1580    335   -156    169       C  
ATOM    613  CD2ALEU A  67       2.164 -27.398   2.268  0.53  9.71           C  
ANISOU  613  CD2ALEU A  67     1042   1182   1465    147     62    166       C  
ATOM    614  CD2BLEU A  67       1.542 -26.153   1.544  0.47  9.69           C  
ANISOU  614  CD2BLEU A  67     1163   1086   1434     66   -121    289       C  
ATOM    615  H  ALEU A  67      -1.469 -25.211   3.724  0.53  9.64           H  
ATOM    616  H  BLEU A  67      -1.368 -25.197   3.715  0.47  8.05           H  
ATOM    617  HA ALEU A  67      -1.356 -26.331   1.266  0.53 10.28           H  
ATOM    618  HA BLEU A  67      -1.276 -26.380   1.296  0.47  7.84           H  
ATOM    619  HB2ALEU A  67      -0.475 -27.479   3.695  0.53 11.36           H  
ATOM    620  HB2BLEU A  67      -0.556 -27.511   3.789  0.47  8.25           H  
ATOM    621  HB3ALEU A  67      -0.166 -28.038   2.245  0.53 11.36           H  
ATOM    622  HB3BLEU A  67      -0.180 -28.096   2.364  0.47  8.25           H  
ATOM    623  N   GLY A  69      -3.008 -28.224   1.605  1.00  7.91           N  
ANISOU  623  N   GLY A  69     1023    791   1193     27      5     87       N  
ATOM    624  CA  GLY A  69      -4.181 -29.054   1.797  1.00  8.23           C  
ANISOU  624  CA  GLY A  69     1082    890   1155    -46     17     37       C  
ATOM    625  C   GLY A  69      -5.501 -28.372   1.525  1.00  7.73           C  
ANISOU  625  C   GLY A  69      993    826   1117   -118     32    -37       C  
ATOM    626  O   GLY A  69      -6.549 -28.862   1.965  1.00  8.58           O  
ANISOU  626  O   GLY A  69     1057    891   1313    -88     29     74       O  
ATOM    627  HA3 GLY A  69      -4.190 -29.411   2.699  1.00  9.88           H  
ATOM    628  N   GLU A  70      -5.484 -27.281   0.773  1.00  7.53           N  
ANISOU  628  N   GLU A  70      935    821   1104    -25     51    -25       N  
ATOM    629  CA  GLU A  70      -6.682 -26.512   0.490  1.00  7.73           C  
ANISOU  629  CA  GLU A  70      978    803   1155    -28     77    -38       C  
ATOM    630  C   GLU A  70      -7.460 -27.044  -0.697  1.00  7.42           C  
ANISOU  630  C   GLU A  70      883    807   1129    -45    -20    -45       C  
ATOM    631  O   GLU A  70      -6.889 -27.401  -1.726  1.00  7.93           O  
ANISOU  631  O   GLU A  70      999    933   1082      7     14   -120       O  
ATOM    632  CB  GLU A  70      -6.344 -25.055   0.181  1.00  7.38           C  
ANISOU  632  CB  GLU A  70      873    857   1074      6      1      0       C  
ATOM    633  CG  GLU A  70      -5.917 -24.224   1.371  1.00  7.79           C  
ANISOU  633  CG  GLU A  70      913    944   1104    -29     32    -18       C  
ATOM    634  CD  GLU A  70      -7.065 -23.782   2.244  1.00  7.58           C  
ANISOU  634  CD  GLU A  70      975    788   1118    -60    -40   -100       C  
ATOM    635  OE1 GLU A  70      -8.157 -24.392   2.119  1.00  8.40           O  
ANISOU  635  OE1 GLU A  70     1030    994   1169    -32     71   -143       O  
ATOM    636  OE2 GLU A  70      -6.893 -22.831   3.021  1.00  8.55           O  
ANISOU  636  OE2 GLU A  70      971   1073   1203    -48     55   -109       O  
ATOM    637  H   GLU A  70      -4.774 -26.961   0.408  1.00  9.03           H  
ATOM    638  HA  GLU A  70      -7.263 -26.530   1.267  1.00  9.28           H  
ATOM    639  HB2 GLU A  70      -5.618 -25.038  -0.462  1.00  8.86           H  
ATOM    640  HB3 GLU A  70      -7.127 -24.632  -0.204  1.00  8.86           H  
ATOM    641  HG2 GLU A  70      -5.312 -24.749   1.918  1.00  9.35           H  
ATOM    642  HG3 GLU A  70      -5.464 -23.428   1.051  1.00  9.35           H  
ATOM    643  N   ASP A  71      -8.791 -27.002  -0.571  1.00  7.89           N  
ANISOU  643  N   ASP A  71     1056    934   1007    -98     55    -49       N  
ATOM    644  CA  ASP A  71      -9.694 -27.009  -1.730  1.00  7.94           C  
ANISOU  644  CA  ASP A  71      948    992   1077    -99      7   -102       C  
ATOM    645  C   ASP A  71     -10.471 -25.702  -1.715  1.00  7.70           C  
ANISOU  645  C   ASP A  71      968    864   1093    -74    117    -16       C  
ATOM    646  O   ASP A  71     -10.076 -24.753  -2.381  1.00  8.98           O  
ANISOU  646  O   ASP A  71     1103    983   1325     56    199     42       O  
ATOM    647  CB  ASP A  71     -10.586 -28.244  -1.837  1.00  8.40           C  
ANISOU  647  CB  ASP A  71     1099    918   1175   -115     40    -10       C  
ATOM    648  CG  ASP A  71     -11.291 -28.298  -3.181  1.00  8.35           C  
ANISOU  648  CG  ASP A  71     1119   1015   1038   -221      4      1       C  
ATOM    649  OD1 ASP A  71     -10.601 -28.028  -4.208  1.00  8.89           O  
ANISOU  649  OD1 ASP A  71     1159   1082   1136    -91    -54   -136       O  
ATOM    650  OD2 ASP A  71     -12.507 -28.566  -3.217  1.00 10.16           O  
ANISOU  650  OD2 ASP A  71     1058   1578   1224   -247     38    -66       O  
ATOM    651  H   ASP A  71      -9.201 -26.969   0.184  1.00  9.47           H  
ATOM    652  HA  ASP A  71      -9.144 -26.997  -2.530  1.00  9.53           H  
ATOM    653  HB2 ASP A  71     -10.042 -29.042  -1.746  1.00 10.08           H  
ATOM    654  HB3 ASP A  71     -11.260 -28.214  -1.140  1.00 10.08           H  
ATOM    655  N   ASN A  72     -11.550 -25.602  -0.938  1.00  7.90           N  
ANISOU  655  N   ASN A  72      982    925   1097    -33     52    -23       N  
ATOM    656  CA  ASN A  72     -12.242 -24.333  -0.796  1.00  7.92           C  
ANISOU  656  CA  ASN A  72      899   1053   1057     18     23    -75       C  
ATOM    657  C   ASN A  72     -11.422 -23.422   0.123  1.00  7.56           C  
ANISOU  657  C   ASN A  72      903   1023    947     76     18   -102       C  
ATOM    658  O   ASN A  72     -11.261 -23.720   1.316  1.00  8.00           O  
ANISOU  658  O   ASN A  72      967   1011   1064     -6     13    -59       O  
ATOM    659  CB  ASN A  72     -13.641 -24.557  -0.230  1.00  9.10           C  
ANISOU  659  CB  ASN A  72      923   1383   1150    -65     48   -158       C  
ATOM    660  CG  ASN A  72     -14.491 -23.307  -0.327  1.00  9.41           C  
ANISOU  660  CG  ASN A  72      988   1471   1117     74   -112   -353       C  
ATOM    661  OD1 ASN A  72     -14.041 -22.218  -0.017  1.00  9.81           O  
ANISOU  661  OD1 ASN A  72      926   1479   1320    179   -130   -433       O  
ATOM    662  ND2 ASN A  72     -15.743 -23.469  -0.756  1.00 12.06           N  
ANISOU  662  ND2 ASN A  72     1001   1957   1622     76   -129   -654       N  
ATOM    663  H   ASN A  72     -11.895 -26.250  -0.490  1.00  9.49           H  
ATOM    664  HA  ASN A  72     -12.323 -23.907  -1.664  1.00  9.50           H  
ATOM    665  HB2 ASN A  72     -14.080 -25.262  -0.732  1.00 10.92           H  
ATOM    666  HB3 ASN A  72     -13.572 -24.805   0.705  1.00 10.92           H  
ATOM    667  N   ILE A  73     -10.918 -22.317  -0.407  1.00  7.66           N  
ANISOU  667  N   ILE A  73      981    930   1002     14     12    -28       N  
ATOM    668  CA  ILE A  73     -10.059 -21.422   0.368  1.00  7.72           C  
ANISOU  668  CA  ILE A  73      962    921   1051     90     -9    -91       C  
ATOM    669  C   ILE A  73     -10.828 -20.564   1.366  1.00  7.72           C  
ANISOU  669  C   ILE A  73     1010    922   1002     20      0    -20       C  
ATOM    670  O   ILE A  73     -10.202 -19.842   2.153  1.00  8.30           O  
ANISOU  670  O   ILE A  73      981   1080   1094     -7     29   -114       O  
ATOM    671  CB  ILE A  73      -9.151 -20.569  -0.545  1.00  8.08           C  
ANISOU  671  CB  ILE A  73     1085    923   1062     25    122    -33       C  
ATOM    672  CG1 ILE A  73      -9.952 -19.856  -1.642  1.00  9.34           C  
ANISOU  672  CG1 ILE A  73     1319   1094   1137    -77    129      9       C  
ATOM    673  CG2 ILE A  73      -8.018 -21.432  -1.082  1.00  9.04           C  
ANISOU  673  CG2 ILE A  73     1080   1189   1164     43    133   -127       C  
ATOM    674  CD1 ILE A  73      -9.198 -18.741  -2.309  1.00 11.15           C  
ANISOU  674  CD1 ILE A  73     1400   1534   1303   -212    116    142       C  
ATOM    675  H   ILE A  73     -11.057 -22.059  -1.216  1.00  9.20           H  
ATOM    676  HA  ILE A  73      -9.465 -21.980   0.894  1.00  9.27           H  
ATOM    677  HB  ILE A  73      -8.750 -19.881   0.010  1.00  9.69           H  
ATOM    678 HG12 ILE A  73     -10.192 -20.502  -2.325  1.00 11.21           H  
ATOM    679 HG13 ILE A  73     -10.755 -19.479  -1.249  1.00 11.21           H  
ATOM    680 HG21 ILE A  73      -7.452 -20.890  -1.654  1.00 10.84           H  
ATOM    681 HG22 ILE A  73      -7.502 -21.776  -0.336  1.00 10.84           H  
ATOM    682 HG23 ILE A  73      -8.395 -22.167  -1.590  1.00 10.84           H  
ATOM    683  N   ASN A  74     -12.173 -20.626   1.346  1.00  7.51           N  
ANISOU  683  N   ASN A  74      861    972   1020     89     25   -129       N  
ATOM    684  CA  ASN A  74     -13.020 -19.881   2.266  1.00  8.16           C  
ANISOU  684  CA  ASN A  74     1062    964   1075    104     23    -71       C  
ATOM    685  C   ASN A  74     -13.705 -20.737   3.321  1.00  8.47           C  
ANISOU  685  C   ASN A  74     1088   1097   1032     61     32   -107       C  
ATOM    686  O   ASN A  74     -14.482 -20.189   4.109  1.00  9.31           O  
ANISOU  686  O   ASN A  74     1195   1135   1208     47    224   -154       O  
ATOM    687  CB  ASN A  74     -14.064 -19.087   1.490  1.00  8.53           C  
ANISOU  687  CB  ASN A  74     1053   1112   1078    177     -6    -83       C  
ATOM    688  CG  ASN A  74     -13.534 -17.796   0.952  1.00  9.43           C  
ANISOU  688  CG  ASN A  74     1458   1119   1006    418    -52   -171       C  
ATOM    689  OD1 ASN A  74     -12.734 -17.095   1.608  1.00  9.06           O  
ANISOU  689  OD1 ASN A  74     1320   1050   1072    229     31    -71       O  
ATOM    690  ND2 ASN A  74     -13.995 -17.430  -0.237  1.00 12.84           N  
ANISOU  690  ND2 ASN A  74     2300   1348   1231    383   -310   -122       N  
ATOM    691  H   ASN A  74     -12.618 -21.108   0.790  1.00  9.01           H  
ATOM    692  HA  ASN A  74     -12.464 -19.241   2.736  1.00  9.79           H  
ATOM    693  HB2 ASN A  74     -14.372 -19.619   0.740  1.00 10.24           H  
ATOM    694  HB3 ASN A  74     -14.807 -18.883   2.079  1.00 10.24           H  
ATOM    695  N   VAL A  75     -13.428 -22.040   3.357  1.00  7.82           N  
ANISOU  695  N   VAL A  75      979    952   1039     43    148    -37       N  
ATOM    696  CA  VAL A  75     -14.073 -22.963   4.282  1.00  8.48           C  
ANISOU  696  CA  VAL A  75     1058    997   1167    -29    124    -81       C  
ATOM    697  C   VAL A  75     -13.000 -23.876   4.845  1.00  8.04           C  
ANISOU  697  C   VAL A  75     1032   1009   1015    -21     95    -14       C  
ATOM    698  O   VAL A  75     -12.220 -24.442   4.073  1.00  8.46           O  
ANISOU  698  O   VAL A  75     1027   1102   1086     12    145    -38       O  
ATOM    699  CB  VAL A  75     -15.177 -23.798   3.590  1.00  8.99           C  
ANISOU  699  CB  VAL A  75     1088   1161   1166   -151    138    -32       C  
ATOM    700  CG1 VAL A  75     -15.822 -24.759   4.584  1.00  9.98           C  
ANISOU  700  CG1 VAL A  75     1100   1253   1437   -321     41    -87       C  
ATOM    701  CG2 VAL A  75     -16.207 -22.898   2.967  1.00  9.73           C  
ANISOU  701  CG2 VAL A  75      979   1321   1399    -58    -42     -7       C  
ATOM    702  H   VAL A  75     -12.855 -22.419   2.841  1.00  9.38           H  
ATOM    703  HA  VAL A  75     -14.472 -22.467   5.013  1.00 10.18           H  
ATOM    704  HB  VAL A  75     -14.775 -24.326   2.882  1.00 10.79           H  
ATOM    705 HG11 VAL A  75     -16.509 -25.270   4.129  1.00 11.97           H  
ATOM    706 HG12 VAL A  75     -15.142 -25.356   4.934  1.00 11.97           H  
ATOM    707 HG21 VAL A  75     -16.886 -23.444   2.541  1.00 11.68           H  
ATOM    708 HG22 VAL A  75     -16.608 -22.351   3.660  1.00 11.68           H  
ATOM    709 HG23 VAL A  75     -15.775 -22.333   2.308  1.00 11.68           H  
ATOM    710  N   VAL A  76     -12.973 -24.071   6.158  1.00  8.73           N  
ANISOU  710  N   VAL A  76     1065   1114   1136     13    104    -93       N  
ATOM    711  CA  VAL A  76     -12.080 -25.056   6.764  1.00  8.77           C  
ANISOU  711  CA  VAL A  76     1059   1132   1140    -16     81    -31       C  
ATOM    712  C   VAL A  76     -12.745 -26.419   6.591  1.00  9.65           C  
ANISOU  712  C   VAL A  76     1214   1204   1251    -25     81    102       C  
ATOM    713  O   VAL A  76     -13.791 -26.684   7.187  1.00 11.27           O  
ANISOU  713  O   VAL A  76     1221   1403   1657   -138    416     71       O  
ATOM    714  CB  VAL A  76     -11.802 -24.741   8.246  1.00 10.30           C  
ANISOU  714  CB  VAL A  76     1309   1498   1105     33     -8    -36       C  
ATOM    715  CG1 VAL A  76     -10.968 -25.837   8.878  1.00 11.55           C  
ANISOU  715  CG1 VAL A  76     1516   1631   1243    179    -50     86       C  
ATOM    716  CG2 VAL A  76     -11.107 -23.391   8.362  1.00 10.27           C  
ANISOU  716  CG2 VAL A  76     1206   1552   1144     57    -18   -111       C  
ATOM    717  H   VAL A  76     -13.463 -23.645   6.722  1.00 10.47           H  
ATOM    718  HA  VAL A  76     -11.235 -25.063   6.287  1.00 10.52           H  
ATOM    719 HG13 VAL A  76     -10.125 -25.906   8.404  1.00 13.87           H  
ATOM    720 HG21 VAL A  76     -10.937 -23.203   9.298  1.00 12.32           H  
ATOM    721 HG22 VAL A  76     -10.269 -23.425   7.873  1.00 12.32           H  
ATOM    722 HG23 VAL A  76     -11.682 -22.707   7.986  1.00 12.32           H  
ATOM    723  N   GLU A  77     -12.145 -27.265   5.745  1.00  8.67           N  
ANISOU  723  N   GLU A  77     1107   1027   1161   -224     41      4       N  
ATOM    724  CA  GLU A  77     -12.702 -28.548   5.342  1.00 10.03           C  
ANISOU  724  CA  GLU A  77     1262   1149   1401   -251     64    142       C  
ATOM    725  C   GLU A  77     -12.038 -29.751   5.997  1.00 11.43           C  
ANISOU  725  C   GLU A  77     1419   1290   1635   -310     61    206       C  
ATOM    726  O   GLU A  77     -12.591 -30.849   5.929  1.00 14.31           O  
ANISOU  726  O   GLU A  77     2033   1238   2165   -520   -295    309       O  
ATOM    727  CB  GLU A  77     -12.696 -28.685   3.811  1.00 10.15           C  
ANISOU  727  CB  GLU A  77     1275   1220   1363   -253     67   -106       C  
ATOM    728  CG  GLU A  77     -13.576 -27.638   3.137  1.00  9.75           C  
ANISOU  728  CG  GLU A  77     1076   1384   1245   -257      1     71       C  
ATOM    729  CD  GLU A  77     -13.569 -27.732   1.628  1.00 11.39           C  
ANISOU  729  CD  GLU A  77     1054   1833   1439   -569      9   -105       C  
ATOM    730  OE1 GLU A  77     -12.498 -27.559   0.999  1.00  9.81           O  
ANISOU  730  OE1 GLU A  77     1174   1385   1167   -248     55     23       O  
ATOM    731  OE2 GLU A  77     -14.646 -27.929   1.050  1.00 16.47           O  
ANISOU  731  OE2 GLU A  77     1361   3354   1544   -733    174   -178       O  
ATOM    732  H   GLU A  77     -11.383 -27.103   5.380  1.00 10.41           H  
ATOM    733  HG3 GLU A  77     -13.261 -26.755   3.384  1.00 11.70           H  
ATOM    734  N   GLY A  78     -10.874 -29.579   6.619  1.00 10.56           N  
ANISOU  734  N   GLY A  78     1359   1218   1435   -120    157    184       N  
ATOM    735  CA  GLY A  78     -10.303 -30.611   7.469  1.00 11.67           C  
ANISOU  735  CA  GLY A  78     1433   1362   1640     50    237    356       C  
ATOM    736  C   GLY A  78      -8.967 -31.163   7.041  1.00 11.12           C  
ANISOU  736  C   GLY A  78     1548   1180   1497    -32     24    344       C  
ATOM    737  O   GLY A  78      -8.398 -31.973   7.787  1.00 14.97           O  
ANISOU  737  O   GLY A  78     2083   1848   1757    391    365    745       O  
ATOM    738  N   ASN A  79      -8.430 -30.778   5.883  1.00  9.41           N  
ANISOU  738  N   ASN A  79     1278   1020   1275    -64     -7    195       N  
ATOM    739  CA  ASN A  79      -7.129 -31.276   5.445  1.00  9.72           C  
ANISOU  739  CA  ASN A  79     1346   1021   1328    -88    -10    177       C  
ATOM    740  C   ASN A  79      -6.076 -30.177   5.369  1.00  9.82           C  
ANISOU  740  C   ASN A  79     1219   1171   1340     51     91    199       C  
ATOM    741  O   ASN A  79      -4.950 -30.441   4.926  1.00 10.60           O  
ANISOU  741  O   ASN A  79     1411   1181   1434    103    126    260       O  
ATOM    742  CB  ASN A  79      -7.258 -32.036   4.129  1.00 11.12           C  
ANISOU  742  CB  ASN A  79     1612   1160   1454    -41      8    -17       C  
ATOM    743  CG  ASN A  79      -8.039 -33.300   4.305  1.00 13.55           C  
ANISOU  743  CG  ASN A  79     2366   1209   1573   -286    -15    129       C  
ATOM    744  OD1 ASN A  79      -7.562 -34.234   4.960  1.00 17.09           O  
ANISOU  744  OD1 ASN A  79     3189   1270   2035   -330   -403    219       O  
ATOM    745  ND2 ASN A  79      -9.245 -33.347   3.762  1.00 14.77           N  
ANISOU  745  ND2 ASN A  79     2278   1449   1885   -508     52     62       N  
ATOM    746  H   ASN A  79      -8.800 -30.229   5.334  1.00 11.29           H  
ATOM    747  HA  ASN A  79      -6.818 -31.913   6.107  1.00 11.67           H  
ATOM    748  HB2 ASN A  79      -7.720 -31.480   3.482  1.00 13.35           H  
ATOM    749  HB3 ASN A  79      -6.374 -32.267   3.804  1.00 13.35           H  
ATOM    750  N   GLU A  80      -6.396 -28.962   5.804  1.00  8.88           N  
ANISOU  750  N   GLU A  80     1087   1020   1265    -90     54    113       N  
ATOM    751  CA  GLU A  80      -5.472 -27.849   5.720  1.00  9.40           C  
ANISOU  751  CA  GLU A  80     1123   1029   1418    -58    -63    268       C  
ATOM    752  C   GLU A  80      -4.317 -27.978   6.700  1.00  9.26           C  
ANISOU  752  C   GLU A  80     1242   1087   1190   -130    -96    148       C  
ATOM    753  O   GLU A  80      -4.447 -28.508   7.803  1.00 10.29           O  
ANISOU  753  O   GLU A  80     1233   1491   1185   -162      3    332       O  
ATOM    754  CB  GLU A  80      -6.185 -26.540   6.041  1.00 10.28           C  
ANISOU  754  CB  GLU A  80     1158   1001   1747   -229   -211    249       C  
ATOM    755  CG  GLU A  80      -7.324 -26.180   5.091  1.00 10.24           C  
ANISOU  755  CG  GLU A  80     1057   1073   1762   -105   -253    499       C  
ATOM    756  CD  GLU A  80      -8.703 -26.686   5.480  1.00  8.60           C  
ANISOU  756  CD  GLU A  80     1064   1020   1183   -100    -43    107       C  
ATOM    757  OE1 GLU A  80      -8.836 -27.544   6.389  1.00  9.06           O  
ANISOU  757  OE1 GLU A  80     1137   1067   1237    -74     -3    126       O  
ATOM    758  OE2 GLU A  80      -9.661 -26.209   4.823  1.00  8.54           O  
ANISOU  758  OE2 GLU A  80     1033   1013   1199    -36     26     34       O  
ATOM    759  H   GLU A  80      -7.153 -28.759   6.157  1.00 10.65           H  
ATOM    760  HB2 GLU A  80      -6.557 -26.602   6.934  1.00 12.34           H  
ATOM    761  HB3 GLU A  80      -5.536 -25.819   6.008  1.00 12.34           H  
ATOM    762  HG2 GLU A  80      -7.372 -25.214   5.007  1.00 12.29           H  
ATOM    763  N   GLN A  81      -3.191 -27.397   6.297  1.00  9.08           N  
ANISOU  763  N   GLN A  81     1113   1136   1200    -67    -14    231       N  
ATOM    764  CA  GLN A  81      -2.096 -27.055   7.186  1.00  8.99           C  
ANISOU  764  CA  GLN A  81     1150   1171   1093    -64    -38    154       C  
ATOM    765  C   GLN A  81      -1.712 -25.618   6.869  1.00  8.58           C  
ANISOU  765  C   GLN A  81     1032   1176   1051   -104    -56     93       C  
ATOM    766  O   GLN A  81      -1.433 -25.291   5.712  1.00  9.59           O  
ANISOU  766  O   GLN A  81     1448   1197   1000   -134     18    102       O  
ATOM    767  CB  GLN A  81      -0.892 -27.972   6.978  1.00  9.83           C  
ANISOU  767  CB  GLN A  81     1235   1214   1287    -39    -78    309       C  
ATOM    768  CG  GLN A  81      -1.171 -29.418   7.368  1.00 11.02           C  
ANISOU  768  CG  GLN A  81     1311   1354   1522    -18    -53    276       C  
ATOM    769  CD  GLN A  81      -0.016 -30.338   7.053  1.00 11.45           C  
ANISOU  769  CD  GLN A  81     1327   1367   1657    -10    123    336       C  
ATOM    770  OE1 GLN A  81       1.127 -30.056   7.416  1.00 12.13           O  
ANISOU  770  OE1 GLN A  81     1251   1411   1944     70    -33    281       O  
ATOM    771  NE2 GLN A  81      -0.304 -31.444   6.381  1.00 12.32           N  
ANISOU  771  NE2 GLN A  81     1389   1588   1704     92   -126    137       N  
ATOM    772  H   GLN A  81      -3.038 -27.184   5.478  1.00 10.89           H  
ATOM    773  HA  GLN A  81      -2.384 -27.112   8.110  1.00 10.78           H  
ATOM    774  HB3 GLN A  81      -0.154 -27.652   7.522  1.00 11.80           H  
ATOM    775  HG3 GLN A  81      -1.947 -29.733   6.879  1.00 13.22           H  
ATOM    776 HE21 GLN A  81      -1.116 -31.608   6.151  1.00 14.78           H  
ATOM    777  N   PHE A  82      -1.739 -24.751   7.874  1.00  9.00           N  
ANISOU  777  N   PHE A  82     1095   1248   1077   -173     29    126       N  
ATOM    778  CA  PHE A  82      -1.398 -23.338   7.736  1.00  9.17           C  
ANISOU  778  CA  PHE A  82     1156   1240   1088   -127     77    137       C  
ATOM    779  C   PHE A  82      -0.049 -23.128   8.429  1.00  9.11           C  
ANISOU  779  C   PHE A  82     1123   1365    974   -240    -53    140       C  
ATOM    780  O   PHE A  82       0.063 -23.363   9.631  1.00 11.39           O  
ANISOU  780  O   PHE A  82     1219   2044   1064   -345    -26    171       O  
ATOM    781  CB  PHE A  82      -2.436 -22.452   8.418  1.00 10.12           C  
ANISOU  781  CB  PHE A  82     1245   1299   1302    -66     37     45       C  
ATOM    782  CG  PHE A  82      -3.823 -22.452   7.814  1.00 10.09           C  
ANISOU  782  CG  PHE A  82     1216   1224   1392    -92     84    105       C  
ATOM    783  CD1 PHE A  82      -4.145 -23.066   6.610  1.00  9.33           C  
ANISOU  783  CD1 PHE A  82     1108   1113   1323   -147     -4    179       C  
ATOM    784  CD2 PHE A  82      -4.831 -21.735   8.471  1.00 12.07           C  
ANISOU  784  CD2 PHE A  82     1127   1745   1714    115    162     -3       C  
ATOM    785  CE1 PHE A  82      -5.453 -23.012   6.098  1.00  9.78           C  
ANISOU  785  CE1 PHE A  82     1120   1088   1506   -157     24    379       C  
ATOM    786  CE2 PHE A  82      -6.108 -21.670   7.963  1.00 13.39           C  
ANISOU  786  CE2 PHE A  82     1299   1896   1894      5    185     74       C  
ATOM    787  CZ  PHE A  82      -6.427 -22.315   6.788  1.00 12.17           C  
ANISOU  787  CZ  PHE A  82     1243   1658   1723    -74     -8     67       C  
ATOM    788  H   PHE A  82      -1.960 -24.966   8.677  1.00 10.80           H  
ATOM    789  HA  PHE A  82      -1.325 -23.093   6.800  1.00 11.01           H  
ATOM    790  HD1 PHE A  82      -3.493 -23.546   6.151  1.00 11.20           H  
ATOM    791  HZ  PHE A  82      -7.292 -22.267   6.450  1.00 14.61           H  
ATOM    792  N   ILE A  83       0.967 -22.701   7.678  1.00  9.02           N  
ANISOU  792  N   ILE A  83     1071   1311   1047   -104    -16    129       N  
ATOM    793  CA  ILE A  83       2.328 -22.566   8.200  1.00  9.03           C  
ANISOU  793  CA  ILE A  83     1105   1235   1090   -120    -74    123       C  
ATOM    794  C   ILE A  83       2.901 -21.258   7.697  1.00  8.96           C  
ANISOU  794  C   ILE A  83      973   1308   1123   -104    -44     57       C  
ATOM    795  O   ILE A  83       2.911 -21.008   6.490  1.00  9.54           O  
ANISOU  795  O   ILE A  83     1038   1408   1177   -161   -121    228       O  
ATOM    796  CB  ILE A  83       3.231 -23.738   7.783  1.00  9.68           C  
ANISOU  796  CB  ILE A  83     1168   1327   1184    -23      6    142       C  
ATOM    797  CG1 ILE A  83       2.620 -25.085   8.166  1.00 10.79           C  
ANISOU  797  CG1 ILE A  83     1221   1413   1467    -74    -13    218       C  
ATOM    798  CG2 ILE A  83       4.606 -23.581   8.398  1.00 10.44           C  
ANISOU  798  CG2 ILE A  83     1152   1357   1458     95    -94    170       C  
ATOM    799  CD1 ILE A  83       3.309 -26.294   7.574  1.00 12.64           C  
ANISOU  799  CD1 ILE A  83     1454   1494   1853     30     89    131       C  
ATOM    800  H   ILE A  83       0.892 -22.481   6.850  1.00 10.83           H  
ATOM    801  HA  ILE A  83       2.298 -22.534   9.169  1.00 10.83           H  
ATOM    802  HB  ILE A  83       3.328 -23.715   6.818  1.00 11.62           H  
ATOM    803 HG12 ILE A  83       2.651 -25.174   9.131  1.00 12.95           H  
ATOM    804 HG13 ILE A  83       1.697 -25.100   7.868  1.00 12.95           H  
ATOM    805 HG21 ILE A  83       5.162 -24.327   8.123  1.00 12.53           H  
ATOM    806 HG23 ILE A  83       4.520 -23.569   9.364  1.00 12.53           H  
ATOM    807 HD11 ILE A  83       2.757 -27.078   7.726  1.00 15.16           H  
ATOM    808  N  ASER A  84       3.374 -20.411   8.599  0.39 10.33           N  
ANISOU  808  N  ASER A  84     1228   1391   1304    -92    -86      0       N  
ATOM    809  N  BSER A  84       3.361 -20.409   8.618  0.61  9.67           N  
ANISOU  809  N  BSER A  84     1100   1346   1229    -77     66    196       N  
ATOM    810  CA ASER A  84       3.898 -19.139   8.138  0.39 10.46           C  
ANISOU  810  CA ASER A  84     1210   1302   1463   -118   -144   -185       C  
ATOM    811  CA BSER A  84       3.991 -19.148   8.260  0.61  9.73           C  
ANISOU  811  CA BSER A  84     1058   1214   1426   -173    115    108       C  
ATOM    812  C  ASER A  84       5.323 -19.274   7.618  0.39  9.91           C  
ANISOU  812  C  ASER A  84     1237   1214   1315   -168   -167    -16       C  
ATOM    813  C  BSER A  84       5.308 -19.375   7.522  0.61  9.20           C  
ANISOU  813  C  BSER A  84     1082   1093   1319    -10    -56    101       C  
ATOM    814  O  ASER A  84       6.104 -20.122   8.060  0.39  9.70           O  
ANISOU  814  O  ASER A  84     1269   1183   1235   -305   -129    -47       O  
ATOM    815  O  BSER A  84       6.012 -20.369   7.734  0.61  9.66           O  
ANISOU  815  O  BSER A  84      965   1351   1355     53   -138     76       O  
ATOM    816  CB ASER A  84       3.803 -18.086   9.233  0.39 12.44           C  
ANISOU  816  CB ASER A  84     1381   1420   1925    131    182   -204       C  
ATOM    817  CB BSER A  84       4.280 -18.344   9.535  0.61 12.33           C  
ANISOU  817  CB BSER A  84     1434   1395   1854   -275    349   -247       C  
ATOM    818  OG ASER A  84       2.458 -17.669   9.328  0.39 13.58           O  
ANISOU  818  OG ASER A  84     1344   1725   2090    224    282   -157       O  
ATOM    819  OG BSER A  84       3.103 -18.004  10.223  0.61 15.18           O  
ANISOU  819  OG BSER A  84     2097   1793   1877   -144    499   -384       O  
ATOM    820  H  ASER A  84       3.402 -20.541   9.449  0.39 12.39           H  
ATOM    821  H  BSER A  84       3.317 -20.547   9.466  0.61 11.61           H  
ATOM    822  HA ASER A  84       3.349 -18.835   7.398  0.39 12.56           H  
ATOM    823  HA BSER A  84       3.397 -18.632   7.692  0.61 11.68           H  
ATOM    824  N   ALA A  85       5.635 -18.437   6.636  1.00 10.42           N  
ANISOU  824  N   ALA A  85     1276   1170   1512     50     56    102       N  
ATOM    825  CA  ALA A  85       6.967 -18.403   6.045  1.00 10.78           C  
ANISOU  825  CA  ALA A  85     1259   1377   1462   -111    195    -26       C  
ATOM    826  C   ALA A  85       7.972 -17.853   7.056  1.00 10.57           C  
ANISOU  826  C   ALA A  85     1292   1341   1383   -157    310   -117       C  
ATOM    827  O   ALA A  85       7.714 -16.864   7.746  1.00 12.32           O  
ANISOU  827  O   ALA A  85     1527   1550   1606    -75    195   -326       O  
ATOM    828  CB  ALA A  85       6.950 -17.498   4.815  1.00 12.02           C  
ANISOU  828  CB  ALA A  85     1696   1551   1320    -20    221    -60       C  
ATOM    829  H  AALA A  85       5.087 -17.872   6.291  0.39 12.50           H  
ATOM    830  H  BALA A  85       5.109 -17.814   6.364  0.61 12.50           H  
ATOM    831  N   SER A  86       9.148 -18.476   7.101  1.00 10.43           N  
ANISOU  831  N   SER A  86     1241   1329   1392   -292    152     48       N  
ATOM    832  CA  SER A  86      10.278 -17.948   7.858  1.00 10.78           C  
ANISOU  832  CA  SER A  86     1351   1433   1311   -135     97     11       C  
ATOM    833  C   SER A  86      11.252 -17.118   7.035  1.00 10.01           C  
ANISOU  833  C   SER A  86     1378   1278   1148   -174     66     21       C  
ATOM    834  O   SER A  86      11.953 -16.261   7.594  1.00 11.65           O  
ANISOU  834  O   SER A  86     1746   1397   1284   -461    161   -195       O  
ATOM    835  CB  SER A  86      11.070 -19.081   8.503  1.00 12.74           C  
ANISOU  835  CB  SER A  86     1785   1680   1376     73      5    178       C  
ATOM    836  OG  SER A  86      11.547 -19.968   7.521  1.00 13.94           O  
ANISOU  836  OG  SER A  86     2144   1617   1536    195   -229    104       O  
ATOM    837  HB2 SER A  86      11.824 -18.707   8.985  1.00 15.29           H  
ATOM    838  HB3 SER A  86      10.491 -19.565   9.113  1.00 15.29           H  
ATOM    839  N  ALYS A  87      11.338 -17.386   5.735  0.61 10.07           N  
ANISOU  839  N  ALYS A  87     1394   1261   1173    -69    107     48       N  
ATOM    840  N  BLYS A  87      11.337 -17.368   5.738  0.39  9.33           N  
ANISOU  840  N  BLYS A  87     1185   1174   1184   -488     59   -179       N  
ATOM    841  CA ALYS A  87      12.275 -16.721   4.844  0.61  9.25           C  
ANISOU  841  CA ALYS A  87     1231   1158   1126    -11     16    316       C  
ATOM    842  CA BLYS A  87      12.256 -16.631   4.889  0.39  9.68           C  
ANISOU  842  CA BLYS A  87     1305   1192   1181   -374    159   -243       C  
ATOM    843  C  ALYS A  87      11.682 -16.757   3.447  0.61  9.05           C  
ANISOU  843  C  ALYS A  87     1151   1193   1094    -65    135     91       C  
ATOM    844  C  BLYS A  87      11.809 -16.830   3.453  0.39  9.66           C  
ANISOU  844  C  BLYS A  87     1430   1026   1215   -402    161   -269       C  
ATOM    845  O  ALYS A  87      11.015 -17.726   3.058  0.61 10.05           O  
ANISOU  845  O  ALYS A  87     1242   1204   1374   -133     37    132       O  
ATOM    846  O  BLYS A  87      11.371 -17.923   3.072  0.39 10.13           O  
ANISOU  846  O  BLYS A  87     1652    843   1355   -333   -177   -383       O  
ATOM    847  CB ALYS A  87      13.637 -17.438   4.842  0.61 11.77           C  
ANISOU  847  CB ALYS A  87     1270   1895   1309     65   -137    328       C  
ATOM    848  CB BLYS A  87      13.703 -17.106   5.079  0.39 12.00           C  
ANISOU  848  CB BLYS A  87     1458   1770   1331   -118    306   -453       C  
ATOM    849  CG ALYS A  87      14.757 -16.728   4.069  0.61 13.34           C  
ANISOU  849  CG ALYS A  87     1322   2151   1597   -183    100   -124       C  
ATOM    850  CG BLYS A  87      13.962 -18.533   4.625  0.39 14.72           C  
ANISOU  850  CG BLYS A  87     1706   1924   1962    122    155   -365       C  
ATOM    851  CD ALYS A  87      16.088 -17.499   4.086  0.61 14.14           C  
ANISOU  851  CD ALYS A  87     1240   2393   1740    -34    199   -608       C  
ATOM    852  CD BLYS A  87      15.407 -18.967   4.914  0.39 15.01           C  
ANISOU  852  CD BLYS A  87     1631   1790   2281     89    188   -372       C  
ATOM    853  CE ALYS A  87      16.935 -17.129   5.293  0.61 16.16           C  
ANISOU  853  CE ALYS A  87     1358   2570   2213    -92    -35   -914       C  
ATOM    854  CE BLYS A  87      15.728 -19.121   6.410  0.39 15.73           C  
ANISOU  854  CE BLYS A  87     1924   1667   2384    265    203   -543       C  
ATOM    855  NZ ALYS A  87      18.255 -17.819   5.277  0.61 17.41           N  
ANISOU  855  NZ ALYS A  87     1950   2381   2285     12    303  -1228       N  
ATOM    856  NZ BLYS A  87      17.068 -19.768   6.654  0.39 16.19           N  
ANISOU  856  NZ BLYS A  87     2197   1585   2371    380    143   -498       N  
ATOM    857  H  ALYS A  87      10.846 -17.969   5.337  0.61 12.09           H  
ATOM    858  H  BLYS A  87      10.873 -17.961   5.324  0.39 11.19           H  
ATOM    859  N  ASER A  88      11.940 -15.696   2.694  0.81  9.49           N  
ANISOU  859  N  ASER A  88     1328   1228   1050    -80     31      5       N  
ATOM    860  N  BSER A  88      11.903 -15.764   2.669  0.19  8.89           N  
ANISOU  860  N  BSER A  88     1347    920   1109   -593     86   -264       N  
ATOM    861  CA ASER A  88      11.654 -15.678   1.272  0.81  9.66           C  
ANISOU  861  CA ASER A  88     1271   1239   1160     37     76    -87       C  
ATOM    862  CA BSER A  88      11.632 -15.820   1.244  0.19  8.79           C  
ANISOU  862  CA BSER A  88     1254    969   1116   -580     49   -181       C  
ATOM    863  C  ASER A  88      12.953 -15.345   0.546  0.81  9.31           C  
ANISOU  863  C  ASER A  88     1517    981   1041   -293   -201     69       C  
ATOM    864  C  BSER A  88      12.863 -15.320   0.507  0.19  8.18           C  
ANISOU  864  C  BSER A  88     1260    800   1047   -161    115   -203       C  
ATOM    865  O  ASER A  88      13.766 -14.545   1.029  0.81 10.85           O  
ANISOU  865  O  ASER A  88     1801   1268   1055   -681   -144     68       O  
ATOM    866  O  BSER A  88      13.515 -14.364   0.939  0.19  7.50           O  
ANISOU  866  O  BSER A  88     1147    651   1053    311    220   -217       O  
ATOM    867  CB ASER A  88      10.528 -14.686   0.961  0.81 15.28           C  
ANISOU  867  CB ASER A  88     1570   2438   1798    286   -132     24       C  
ATOM    868  CB BSER A  88      10.435 -14.956   0.875  0.19 10.70           C  
ANISOU  868  CB BSER A  88     1092   1554   1421   -753    -90    107       C  
ATOM    869  OG ASER A  88       9.291 -15.144   1.519  0.81 17.38           O  
ANISOU  869  OG ASER A  88     1291   3018   2295    366    172   -271       O  
ATOM    870  OG BSER A  88      10.822 -13.599   0.887  0.19 12.21           O  
ANISOU  870  OG BSER A  88     1134   1990   1518   -490      8    140       O  
ATOM    871  HA ASER A  88      11.366 -16.561   0.992  0.81 11.59           H  
ATOM    872  HA BSER A  88      11.454 -16.735   0.976  0.19 10.54           H  
ATOM    873  N   ILE A  89      13.164 -15.980  -0.607  1.00  8.13           N  
ANISOU  873  N   ILE A  89     1175    880   1033   -229   -144    -10       N  
ATOM    874  CA  ILE A  89      14.357 -15.735  -1.424  1.00  7.87           C  
ANISOU  874  CA  ILE A  89      972    929   1087   -226   -119     17       C  
ATOM    875  C   ILE A  89      13.907 -15.561  -2.874  1.00  7.60           C  
ANISOU  875  C   ILE A  89      928    943   1016   -184    -82     73       C  
ATOM    876  O   ILE A  89      13.618 -16.535  -3.582  1.00  7.97           O  
ANISOU  876  O   ILE A  89     1099    875   1054   -180   -198     -2       O  
ATOM    877  CB  ILE A  89      15.390 -16.852  -1.301  1.00  8.53           C  
ANISOU  877  CB  ILE A  89      972    993   1276   -154   -202     78       C  
ATOM    878  CG1 ILE A  89      15.758 -17.100   0.171  1.00 10.10           C  
ANISOU  878  CG1 ILE A  89     1421   1137   1282    -60   -349    164       C  
ATOM    879  CG2 ILE A  89      16.591 -16.528  -2.175  1.00  9.55           C  
ANISOU  879  CG2 ILE A  89     1101   1189   1339     38   -201   -105       C  
ATOM    880  CD1 ILE A  89      16.573 -18.356   0.396  1.00 10.87           C  
ANISOU  880  CD1 ILE A  89     1401   1281   1449     91   -169    160       C  
ATOM    881  H  AILE A  89      12.627 -16.562  -0.942  0.81  9.75           H  
ATOM    882  H  BILE A  89      12.668 -16.605  -0.927  0.19  9.75           H  
ATOM    883  HA  ILE A  89      14.774 -14.908  -1.137  1.00  9.44           H  
ATOM    884  HB  ILE A  89      14.987 -17.665  -1.645  1.00 10.24           H  
ATOM    885 HG12 ILE A  89      16.272 -16.346   0.499  1.00 12.13           H  
ATOM    886 HG21 ILE A  89      17.243 -17.241  -2.092  1.00 11.46           H  
ATOM    887 HG22 ILE A  89      16.300 -16.451  -3.097  1.00 11.46           H  
ATOM    888 HG23 ILE A  89      16.979 -15.689  -1.879  1.00 11.46           H  
ATOM    889  N   VAL A  90      13.867 -14.309  -3.321  1.00  7.45           N  
ANISOU  889  N   VAL A  90     1030    826    974    -97    -48     15       N  
ATOM    890  CA  VAL A  90      13.648 -13.973  -4.722  1.00  7.29           C  
ANISOU  890  CA  VAL A  90      920    875    976    -52    -77     67       C  
ATOM    891  C   VAL A  90      14.916 -14.299  -5.501  1.00  7.45           C  
ANISOU  891  C   VAL A  90      910    853   1068    -48     -9     39       C  
ATOM    892  O   VAL A  90      16.032 -14.078  -5.017  1.00  8.07           O  
ANISOU  892  O   VAL A  90      934   1079   1055    -59    -81     47       O  
ATOM    893  CB  VAL A  90      13.232 -12.492  -4.815  1.00  7.66           C  
ANISOU  893  CB  VAL A  90     1002    943    966   -162    -90      8       C  
ATOM    894  CG1 VAL A  90      13.322 -11.951  -6.242  1.00  8.70           C  
ANISOU  894  CG1 VAL A  90     1189   1047   1070     -4    -64     80       C  
ATOM    895  CG2 VAL A  90      11.835 -12.311  -4.245  1.00  8.47           C  
ANISOU  895  CG2 VAL A  90      955    911   1352    -66     36    -38       C  
ATOM    896  H   VAL A  90      13.966 -13.619  -2.817  1.00  8.94           H  
ATOM    897  HA  VAL A  90      12.926 -14.516  -5.074  1.00  8.75           H  
ATOM    898  HB  VAL A  90      13.838 -11.969  -4.268  1.00  9.19           H  
ATOM    899 HG21 VAL A  90      11.603 -11.369  -4.271  1.00 10.16           H  
ATOM    900  N   HIS A  91      14.755 -14.799  -6.738  1.00  7.19           N  
ANISOU  900  N   HIS A  91      908    867    956     -6     21    -33       N  
ATOM    901  CA  HIS A  91      15.913 -15.134  -7.546  1.00  7.42           C  
ANISOU  901  CA  HIS A  91      944    862   1014      4   -108     84       C  
ATOM    902  C   HIS A  91      16.887 -13.959  -7.610  1.00  7.25           C  
ANISOU  902  C   HIS A  91      891    910    952     15   -108     83       C  
ATOM    903  O   HIS A  91      16.457 -12.802  -7.772  1.00  7.49           O  
ANISOU  903  O   HIS A  91      861    947   1039    -59    -95     46       O  
ATOM    904  CB  HIS A  91      15.474 -15.515  -8.963  1.00  7.33           C  
ANISOU  904  CB  HIS A  91      845    814   1128    -21    -13    -53       C  
ATOM    905  CG  HIS A  91      16.556 -16.176  -9.730  1.00  7.47           C  
ANISOU  905  CG  HIS A  91      955    869   1015    -99   -105     50       C  
ATOM    906  ND1 HIS A  91      17.504 -15.462 -10.440  1.00  8.22           N  
ANISOU  906  ND1 HIS A  91     1047    965   1110      6    -39     30       N  
ATOM    907  CD2 HIS A  91      16.881 -17.492  -9.802  1.00  7.99           C  
ANISOU  907  CD2 HIS A  91      967    914   1154     34    -16     10       C  
ATOM    908  CE1 HIS A  91      18.370 -16.343 -10.922  1.00  8.36           C  
ANISOU  908  CE1 HIS A  91     1008   1021   1147    104     24    124       C  
ATOM    909  NE2 HIS A  91      18.031 -17.572 -10.535  1.00  8.70           N  
ANISOU  909  NE2 HIS A  91     1062   1051   1192    103    -67    -79       N  
ATOM    910  HA  HIS A  91      16.373 -15.892  -7.152  1.00  8.91           H  
ATOM    911  HB2 HIS A  91      14.725 -16.129  -8.908  1.00  8.80           H  
ATOM    912  HB3 HIS A  91      15.213 -14.713  -9.441  1.00  8.80           H  
ATOM    913  HD2 HIS A  91      16.431 -18.198  -9.396  1.00  9.59           H  
ATOM    914  HE1 HIS A  91      19.101 -16.135 -11.458  1.00 10.03           H  
ATOM    915  N  APRO A  92      18.194 -14.225  -7.586  0.69  7.69           N  
ANISOU  915  N  APRO A  92      903    922   1096   -129   -161    263       N  
ATOM    916  N  BPRO A  92      18.202 -14.217  -7.528  0.31  7.86           N  
ANISOU  916  N  BPRO A  92      784   1175   1027    108   -155   -122       N  
ATOM    917  CA APRO A  92      19.174 -13.133  -7.618  0.69  8.49           C  
ANISOU  917  CA APRO A  92      912   1042   1273   -286   -283    318       C  
ATOM    918  CA BPRO A  92      19.180 -13.121  -7.621  0.31  8.69           C  
ANISOU  918  CA BPRO A  92      936   1198   1171    168   -169      9       C  
ATOM    919  C  APRO A  92      19.026 -12.218  -8.812  0.69  8.39           C  
ANISOU  919  C  APRO A  92      940    996   1254   -368   -252    152       C  
ATOM    920  C  BPRO A  92      18.961 -12.190  -8.798  0.31  7.54           C  
ANISOU  920  C  BPRO A  92      701   1024   1141    410    113     50       C  
ATOM    921  O  APRO A  92      19.361 -11.033  -8.702  0.69 10.17           O  
ANISOU  921  O  APRO A  92     1328   1169   1366   -552   -595    259       O  
ATOM    922  O  BPRO A  92      19.159 -10.975  -8.668  0.31  8.52           O  
ANISOU  922  O  BPRO A  92      899   1135   1205    558    192    -70       O  
ATOM    923  CB APRO A  92      20.530 -13.876  -7.604  0.69 10.15           C  
ANISOU  923  CB APRO A  92      913   1273   1671   -123   -178    460       C  
ATOM    924  CB BPRO A  92      20.527 -13.865  -7.717  0.31 10.56           C  
ANISOU  924  CB BPRO A  92     1071   1501   1441    234   -135     61       C  
ATOM    925  CG APRO A  92      20.219 -15.272  -8.030  0.69  9.14           C  
ANISOU  925  CG APRO A  92      790   1177   1507     75   -120    345       C  
ATOM    926  CG BPRO A  92      20.292 -15.153  -7.032  0.31 10.36           C  
ANISOU  926  CG BPRO A  92      951   1523   1460    161      7   -210       C  
ATOM    927  CD APRO A  92      18.842 -15.542  -7.461  0.69  9.10           C  
ANISOU  927  CD APRO A  92     1055   1038   1365    252   -100    473       C  
ATOM    928  CD BPRO A  92      18.855 -15.516  -7.284  0.31  8.68           C  
ANISOU  928  CD BPRO A  92      768   1255   1275   -125   -180   -200       C  
ATOM    929  HG2BPRO A  92      20.876 -15.826  -7.415  0.31 12.43           H  
ATOM    930  HG3APRO A  92      20.866 -15.876  -7.633  0.69 10.97           H  
ATOM    931  HD3APRO A  92      18.927 -15.764  -6.521  0.69 10.92           H  
ATOM    932  HD3BPRO A  92      18.483 -15.910  -6.480  0.31 10.42           H  
ATOM    933  N   SER A  93      18.570 -12.732  -9.946  1.00  7.77           N  
ANISOU  933  N   SER A  93      831   1006   1116      1    -99    125       N  
ATOM    934  CA  SER A  93      18.507 -11.990 -11.192  1.00  8.00           C  
ANISOU  934  CA  SER A  93      972   1021   1048     -2    -42    105       C  
ATOM    935  C   SER A  93      17.091 -11.624 -11.610  1.00  7.61           C  
ANISOU  935  C   SER A  93      877    915   1101     -9    -33     99       C  
ATOM    936  O   SER A  93      16.858 -11.247 -12.772  1.00  8.24           O  
ANISOU  936  O   SER A  93      970   1156   1005     30    -41    227       O  
ATOM    937  CB  SER A  93      19.213 -12.772 -12.293  1.00  9.63           C  
ANISOU  937  CB  SER A  93      956   1402   1302    183     46    114       C  
ATOM    938  OG  SER A  93      20.582 -12.930 -11.946  1.00 13.30           O  
ANISOU  938  OG  SER A  93     1119   2412   1522    408     -1     75       O  
ATOM    939  H  ASER A  93      18.282 -13.539 -10.019  0.69  9.33           H  
ATOM    940  H  BSER A  93      18.330 -13.554 -10.028  0.31  9.33           H  
ATOM    941  HB2 SER A  93      18.801 -13.646 -12.381  1.00 11.56           H  
ATOM    942  HB3 SER A  93      19.147 -12.282 -13.127  1.00 11.56           H  
ATOM    943  N   TYR A  94      16.119 -11.714 -10.705  1.00  7.31           N  
ANISOU  943  N   TYR A  94      885    922    969     25   -139    119       N  
ATOM    944  CA  TYR A  94      14.754 -11.320 -11.050  1.00  7.14           C  
ANISOU  944  CA  TYR A  94      912    878    924     -2    -59     79       C  
ATOM    945  C   TYR A  94      14.713  -9.865 -11.505  1.00  7.18           C  
ANISOU  945  C   TYR A  94      849    867   1013    -10    -88     76       C  
ATOM    946  O   TYR A  94      15.213  -8.972 -10.815  1.00  7.88           O  
ANISOU  946  O   TYR A  94     1037    834   1122    -41   -187    120       O  
ATOM    947  CB  TYR A  94      13.835 -11.489  -9.851  1.00  7.58           C  
ANISOU  947  CB  TYR A  94      975    880   1024    -24    -82     88       C  
ATOM    948  CG  TYR A  94      12.437 -10.955 -10.067  1.00  7.09           C  
ANISOU  948  CG  TYR A  94      900    781   1012     15      5    144       C  
ATOM    949  CD1 TYR A  94      11.652 -11.412 -11.129  1.00  6.83           C  
ANISOU  949  CD1 TYR A  94      891    783    923     12    -77     91       C  
ATOM    950  CD2 TYR A  94      11.901 -10.026  -9.215  1.00  7.40           C  
ANISOU  950  CD2 TYR A  94      949    871    993     -1    -93    101       C  
ATOM    951  CE1 TYR A  94      10.375 -10.933 -11.323  1.00  7.53           C  
ANISOU  951  CE1 TYR A  94      930    843   1088     -9    -19    158       C  
ATOM    952  CE2 TYR A  94      10.614  -9.544  -9.383  1.00  7.68           C  
ANISOU  952  CE2 TYR A  94     1077    784   1057     49     34     72       C  
ATOM    953  CZ  TYR A  94       9.856 -10.008 -10.449  1.00  7.76           C  
ANISOU  953  CZ  TYR A  94      955    892   1104     90    -17    204       C  
ATOM    954  OH  TYR A  94       8.575  -9.541 -10.659  1.00  8.69           O  
ANISOU  954  OH  TYR A  94      940   1126   1235    108    -85    173       O  
ATOM    955  H   TYR A  94      16.220 -11.995  -9.898  1.00  8.77           H  
ATOM    956  HA  TYR A  94      14.426 -11.879 -11.771  1.00  8.57           H  
ATOM    957  HB2 TYR A  94      13.762 -12.434  -9.644  1.00  9.09           H  
ATOM    958  HB3 TYR A  94      14.219 -11.017  -9.095  1.00  9.09           H  
ATOM    959  HD1 TYR A  94      12.000 -12.042 -11.718  1.00  8.20           H  
ATOM    960  HD2 TYR A  94      12.409  -9.722  -8.498  1.00  8.89           H  
ATOM    961  HE2 TYR A  94      10.266  -8.911  -8.797  1.00  9.22           H  
ATOM    962  N   ASN A  95      14.047  -9.638 -12.649  1.00  7.27           N  
ANISOU  962  N   ASN A  95      977    772   1015    -49   -134    148       N  
ATOM    963  CA  ASN A  95      13.803  -8.306 -13.187  1.00  7.44           C  
ANISOU  963  CA  ASN A  95     1003    830    995     14    -85    111       C  
ATOM    964  C   ASN A  95      12.293  -8.104 -13.259  1.00  7.61           C  
ANISOU  964  C   ASN A  95     1105    762   1025     54    -82    145       C  
ATOM    965  O   ASN A  95      11.606  -8.753 -14.054  1.00  8.08           O  
ANISOU  965  O   ASN A  95     1095    842   1134     72   -165     56       O  
ATOM    966  CB  ASN A  95      14.432  -8.160 -14.570  1.00  9.09           C  
ANISOU  966  CB  ASN A  95     1159   1127   1167     32   -107    228       C  
ATOM    967  CG  ASN A  95      14.238  -6.771 -15.158  1.00  9.74           C  
ANISOU  967  CG  ASN A  95     1274   1159   1266     16      4    370       C  
ATOM    968  OD1 ASN A  95      13.131  -6.276 -15.192  1.00 10.16           O  
ANISOU  968  OD1 ASN A  95     1440   1064   1355     75    -42    282       O  
ATOM    969  ND2 ASN A  95      15.274  -6.187 -15.714  1.00 13.89           N  
ANISOU  969  ND2 ASN A  95     1546   1643   2088   -162    160    788       N  
ATOM    970  H   ASN A  95      13.721 -10.264 -13.140  1.00  8.73           H  
ATOM    971  HA  ASN A  95      14.183  -7.637 -12.596  1.00  8.93           H  
ATOM    972  N   SER A  96      11.777  -7.212 -12.420  1.00  7.81           N  
ANISOU  972  N   SER A  96     1115    846   1007    172    -53    149       N  
ATOM    973  CA  SER A  96      10.334  -7.019 -12.323  1.00  8.75           C  
ANISOU  973  CA  SER A  96     1190    938   1195    173    -40    218       C  
ATOM    974  C   SER A  96       9.746  -6.296 -13.534  1.00  8.37           C  
ANISOU  974  C   SER A  96     1105    918   1155    133    -96    175       C  
ATOM    975  O   SER A  96       8.523  -6.328 -13.714  1.00 10.73           O  
ANISOU  975  O   SER A  96     1244   1268   1566    139   -138    395       O  
ATOM    976  CB  SER A  96       9.996  -6.245 -11.046  1.00 10.08           C  
ANISOU  976  CB  SER A  96     1516   1086   1228    287     46    167       C  
ATOM    977  OG  SER A  96      10.678  -4.995 -11.016  1.00 11.58           O  
ANISOU  977  OG  SER A  96     2105   1132   1164    402    -72     72       O  
ATOM    978  HA  SER A  96       9.908  -7.888 -12.263  1.00 10.49           H  
ATOM    979  HB3 SER A  96      10.267  -6.771 -10.277  1.00 12.09           H  
ATOM    980  N   ASN A  97      10.570  -5.642 -14.352  1.00  8.23           N  
ANISOU  980  N   ASN A  97     1333    794    998    130   -106    152       N  
ATOM    981  CA  ASN A  97      10.066  -5.000 -15.569  1.00  8.25           C  
ANISOU  981  CA  ASN A  97     1257    789   1088    141   -109    140       C  
ATOM    982  C   ASN A  97       9.862  -5.996 -16.700  1.00  8.99           C  
ANISOU  982  C   ASN A  97     1415    935   1065    125   -232    142       C  
ATOM    983  O   ASN A  97       8.829  -5.964 -17.376  1.00 12.28           O  
ANISOU  983  O   ASN A  97     1701   1540   1425    551   -506   -157       O  
ATOM    984  CB  ASN A  97      11.003  -3.889 -16.003  1.00  9.00           C  
ANISOU  984  CB  ASN A  97     1438    920   1063    141   -113    135       C  
ATOM    985  CG  ASN A  97      11.006  -2.750 -15.046  1.00  9.61           C  
ANISOU  985  CG  ASN A  97     1482    941   1228    141   -190    246       C  
ATOM    986  OD1 ASN A  97       9.965  -2.416 -14.450  1.00 10.88           O  
ANISOU  986  OD1 ASN A  97     1976   1006   1153    264    -71     69       O  
ATOM    987  ND2 ASN A  97      12.177  -2.144 -14.864  1.00 12.84           N  
ANISOU  987  ND2 ASN A  97     1788   1272   1818    125   -550    263       N  
ATOM    988  HA  ASN A  97       9.205  -4.599 -15.373  1.00  9.90           H  
ATOM    989  HB3 ASN A  97      10.717  -3.553 -16.867  1.00 10.80           H  
ATOM    990 HD22 ASN A  97      12.873  -2.418 -15.288  1.00 15.41           H  
ATOM    991  N   THR A  98      10.803  -6.908 -16.910  1.00  8.86           N  
ANISOU  991  N   THR A  98     1395    852   1118    134   -158     -8       N  
ATOM    992  CA  THR A  98      10.721  -7.893 -17.983  1.00  9.10           C  
ANISOU  992  CA  THR A  98     1483    899   1074    168   -210    155       C  
ATOM    993  C   THR A  98      10.119  -9.219 -17.529  1.00  9.08           C  
ANISOU  993  C   THR A  98     1401    978   1069    212   -333    -84       C  
ATOM    994  O   THR A  98       9.739 -10.047 -18.368  1.00  9.74           O  
ANISOU  994  O   THR A  98     1623   1015   1063    134   -256    -51       O  
ATOM    995  CB  THR A  98      12.095  -8.192 -18.561  1.00 10.09           C  
ANISOU  995  CB  THR A  98     1677   1044   1113     90    -42     87       C  
ATOM    996  OG1 THR A  98      12.885  -8.768 -17.519  1.00  9.57           O  
ANISOU  996  OG1 THR A  98     1536    981   1121     49    -16    143       O  
ATOM    997  CG2 THR A  98      12.740  -6.928 -19.144  1.00 11.36           C  
ANISOU  997  CG2 THR A  98     1942   1080   1295     65    201    320       C  
ATOM    998  HA  THR A  98      10.165  -7.539 -18.695  1.00 10.92           H  
ATOM    999  HB  THR A  98      12.002  -8.838 -19.278  1.00 12.11           H  
ATOM   1000  N   LEU A  99      10.076  -9.446 -16.210  1.00  8.16           N  
ANISOU 1000  N   LEU A  99     1284    741   1076     97   -225    -20       N  
ATOM   1001  CA  LEU A  99       9.689 -10.707 -15.582  1.00  8.32           C  
ANISOU 1001  CA  LEU A  99     1132    892   1135    153   -143    -37       C  
ATOM   1002  C   LEU A  99      10.665 -11.835 -15.892  1.00  7.49           C  
ANISOU 1002  C   LEU A  99     1150    829    868    -43   -104     53       C  
ATOM   1003  O   LEU A  99      10.369 -13.007 -15.628  1.00  7.84           O  
ANISOU 1003  O   LEU A  99     1035    850   1093     50     28     49       O  
ATOM   1004  CB  LEU A  99       8.235 -11.090 -15.811  1.00  9.29           C  
ANISOU 1004  CB  LEU A  99     1100    961   1469    151    -36    -40       C  
ATOM   1005  CG  LEU A  99       7.264 -10.017 -15.305  1.00 11.58           C  
ANISOU 1005  CG  LEU A  99     1275   1601   1524    247   -225   -174       C  
ATOM   1006  CD1 LEU A  99       5.863 -10.419 -15.621  1.00 13.89           C  
ANISOU 1006  CD1 LEU A  99     1482   1783   2014    368   -334   -569       C  
ATOM   1007  CD2 LEU A  99       7.387  -9.709 -13.800  1.00 12.60           C  
ANISOU 1007  CD2 LEU A  99     1364   1992   1432    -19    -18   -454       C  
ATOM   1008  H   LEU A  99      10.280  -8.844 -15.631  1.00  9.79           H  
ATOM   1009  HB3 LEU A  99       8.047 -11.914 -15.335  1.00 11.15           H  
ATOM   1010  N   ASN A 100      11.878 -11.516 -16.341  1.00  7.51           N  
ANISOU 1010  N   ASN A 100     1079    816    960    -47    -39     89       N  
ATOM   1011  CA  ASN A 100      12.892 -12.546 -16.471  1.00  7.54           C  
ANISOU 1011  CA  ASN A 100     1060    826    980     48      6     -9       C  
ATOM   1012  C   ASN A 100      13.274 -13.055 -15.080  1.00  7.08           C  
ANISOU 1012  C   ASN A 100      912    816    962     14     -6     69       C  
ATOM   1013  O   ASN A 100      13.461 -12.276 -14.144  1.00  7.61           O  
ANISOU 1013  O   ASN A 100     1125    808    959     54    -74     34       O  
ATOM   1014  CB  ASN A 100      14.108 -11.991 -17.204  1.00  8.03           C  
ANISOU 1014  CB  ASN A 100     1126    967    958    -33     19     76       C  
ATOM   1015  CG  ASN A 100      15.015 -13.067 -17.754  1.00  8.36           C  
ANISOU 1015  CG  ASN A 100     1142   1071    962    -48     49    108       C  
ATOM   1016  OD1 ASN A 100      14.585 -14.182 -18.068  1.00  8.85           O  
ANISOU 1016  OD1 ASN A 100     1172   1082   1109     37     78    -11       O  
ATOM   1017  ND2 ASN A 100      16.283 -12.708 -17.920  1.00 10.26           N  
ANISOU 1017  ND2 ASN A 100     1219   1368   1312    -82    168    135       N  
ATOM   1018  H   ASN A 100      12.131 -10.727 -16.572  1.00  9.02           H  
ATOM   1019  HA  ASN A 100      12.536 -13.289 -16.983  1.00  9.05           H  
ATOM   1020  HB2 ASN A 100      13.805 -11.447 -17.948  1.00  9.64           H  
ATOM   1021  HB3 ASN A 100      14.626 -11.450 -16.588  1.00  9.64           H  
ATOM   1022  N   ASN A 101      13.439 -14.371 -14.968  1.00  7.07           N  
ANISOU 1022  N   ASN A 101      950    844    893     53     57     47       N  
ATOM   1023  CA  ASN A 101      13.792 -15.039 -13.706  1.00  7.51           C  
ANISOU 1023  CA  ASN A 101     1029    828    995     82     -1     35       C  
ATOM   1024  C   ASN A 101      12.696 -14.878 -12.650  1.00  6.85           C  
ANISOU 1024  C   ASN A 101      917    749    937     16    -10     34       C  
ATOM   1025  O   ASN A 101      12.965 -14.592 -11.483  1.00  7.21           O  
ANISOU 1025  O   ASN A 101      906    850    982     -6    -12      1       O  
ATOM   1026  CB  ASN A 101      15.157 -14.614 -13.158  1.00  7.67           C  
ANISOU 1026  CB  ASN A 101      859   1073    982     76    -43     78       C  
ATOM   1027  CG  ASN A 101      16.261 -14.752 -14.181  1.00  8.10           C  
ANISOU 1027  CG  ASN A 101      935   1148    995     36     -8     66       C  
ATOM   1028  OD1 ASN A 101      16.627 -15.861 -14.595  1.00  9.46           O  
ANISOU 1028  OD1 ASN A 101     1100   1148   1347    201    189    -36       O  
ATOM   1029  ND2 ASN A 101      16.811 -13.610 -14.589  1.00  9.41           N  
ANISOU 1029  ND2 ASN A 101     1046   1364   1167   -229     30    142       N  
ATOM   1030  H   ASN A 101      13.349 -14.918 -15.626  1.00  8.49           H  
ATOM   1031  HA  ASN A 101      13.856 -15.989 -13.891  1.00  9.01           H  
ATOM   1032  HB3 ASN A 101      15.381 -15.175 -12.398  1.00  9.20           H  
ATOM   1033  N   ASP A 102      11.449 -15.100 -13.072  1.00  7.21           N  
ANISOU 1033  N   ASP A 102      972    903    865     14      1     29       N  
ATOM   1034  CA  ASP A 102      10.282 -14.911 -12.192  1.00  6.76           C  
ANISOU 1034  CA  ASP A 102      892    763    914     48      9    -39       C  
ATOM   1035  C   ASP A 102      10.068 -16.154 -11.324  1.00  6.33           C  
ANISOU 1035  C   ASP A 102      847    679    881     54    -23      7       C  
ATOM   1036  O   ASP A 102       9.177 -16.986 -11.550  1.00  7.04           O  
ANISOU 1036  O   ASP A 102      939    816    920     14    -56    -11       O  
ATOM   1037  CB  ASP A 102       9.034 -14.594 -13.012  1.00  6.83           C  
ANISOU 1037  CB  ASP A 102      980    740    875     66    -62    -10       C  
ATOM   1038  CG  ASP A 102       7.867 -14.139 -12.142  1.00  7.16           C  
ANISOU 1038  CG  ASP A 102      900    837    984     20    -68     21       C  
ATOM   1039  OD1 ASP A 102       8.087 -13.849 -10.944  1.00  7.31           O  
ANISOU 1039  OD1 ASP A 102      966    918    892     36    -11    -72       O  
ATOM   1040  OD2 ASP A 102       6.741 -14.043 -12.701  1.00  7.90           O  
ANISOU 1040  OD2 ASP A 102      955   1040   1006     69    -93    -57       O  
ATOM   1041  H   ASP A 102      11.247 -15.363 -13.866  1.00  8.65           H  
ATOM   1042  HA  ASP A 102      10.452 -14.160 -11.602  1.00  8.11           H  
ATOM   1043  HB3 ASP A 102       8.758 -15.391 -13.489  1.00  8.20           H  
ATOM   1044  N   ILE A 103      10.910 -16.273 -10.291  1.00  6.77           N  
ANISOU 1044  N   ILE A 103      894    741    936     24    -62     31       N  
ATOM   1045  CA  ILE A 103      10.909 -17.430  -9.396  1.00  6.66           C  
ANISOU 1045  CA  ILE A 103      821    777    933     -7    -85     12       C  
ATOM   1046  C   ILE A 103      11.382 -16.981  -8.021  1.00  6.43           C  
ANISOU 1046  C   ILE A 103      799    669    973      5      0     34       C  
ATOM   1047  O   ILE A 103      12.276 -16.127  -7.893  1.00  6.92           O  
ANISOU 1047  O   ILE A 103      907    770    954      6    -45     41       O  
ATOM   1048  CB  ILE A 103      11.746 -18.595  -9.976  1.00  6.93           C  
ANISOU 1048  CB  ILE A 103      907    845    882     40    -36    -69       C  
ATOM   1049  CG1 ILE A 103      11.595 -19.860  -9.130  1.00  7.59           C  
ANISOU 1049  CG1 ILE A 103      951    781   1154     79    -30    -41       C  
ATOM   1050  CG2 ILE A 103      13.209 -18.229 -10.192  1.00  7.52           C  
ANISOU 1050  CG2 ILE A 103      934    809   1114     58      7    -50       C  
ATOM   1051  CD1 ILE A 103      12.194 -21.102  -9.794  1.00  9.36           C  
ANISOU 1051  CD1 ILE A 103     1234    888   1433    119    168    -70       C  
ATOM   1052  H   ILE A 103      11.501 -15.684 -10.088  1.00  8.12           H  
ATOM   1053  HA  ILE A 103       9.997 -17.745  -9.301  1.00  7.99           H  
ATOM   1054  HB  ILE A 103      11.376 -18.797 -10.850  1.00  8.32           H  
ATOM   1055 HG12 ILE A 103      12.046 -19.727  -8.282  1.00  9.11           H  
ATOM   1056 HG13 ILE A 103      10.651 -20.027  -8.980  1.00  9.11           H  
ATOM   1057 HG21 ILE A 103      13.677 -18.997 -10.555  1.00  9.02           H  
ATOM   1058 HG22 ILE A 103      13.260 -17.486 -10.813  1.00  9.02           H  
ATOM   1059 HG23 ILE A 103      13.600 -17.976  -9.341  1.00  9.02           H  
ATOM   1060 HD11 ILE A 103      11.998 -21.878  -9.247  1.00 11.23           H  
ATOM   1061 HD12 ILE A 103      11.802 -21.209 -10.675  1.00 11.23           H  
ATOM   1062  N  AMET A 104      10.760 -17.538  -6.989  0.51  6.80           N  
ANISOU 1062  N  AMET A 104      887    819    879   -287    -93     76       N  
ATOM   1063  N  BMET A 104      10.808 -17.607  -6.990  0.49  6.74           N  
ANISOU 1063  N  BMET A 104      795    753   1012    129    -52    -57       N  
ATOM   1064  CA AMET A 104      11.200 -17.338  -5.615  0.51  6.10           C  
ANISOU 1064  CA AMET A 104      794    696    829   -114    -36     98       C  
ATOM   1065  CA BMET A 104      11.052 -17.289  -5.584  0.49  7.22           C  
ANISOU 1065  CA BMET A 104      945    886    914     86    -75    -14       C  
ATOM   1066  C  AMET A 104      10.978 -18.627  -4.837  0.51  5.59           C  
ANISOU 1066  C  AMET A 104      675    611    837     23   -128     -9       C  
ATOM   1067  C  BMET A 104      10.881 -18.567  -4.767  0.49  7.78           C  
ANISOU 1067  C  BMET A 104      918   1011   1029     38    -49    -98       C  
ATOM   1068  O  AMET A 104      10.133 -19.454  -5.170  0.51  7.21           O  
ANISOU 1068  O  AMET A 104      972    822    947     55   -214    236       O  
ATOM   1069  O  BMET A 104       9.973 -19.355  -5.027  0.49  8.92           O  
ANISOU 1069  O  BMET A 104     1065   1090   1233   -478   -227    -13       O  
ATOM   1070  CB AMET A 104      10.466 -16.174  -4.917  0.51  6.85           C  
ANISOU 1070  CB AMET A 104      901    667   1034    -95    -27    178       C  
ATOM   1071  CB BMET A 104      10.050 -16.230  -5.085  0.49  8.01           C  
ANISOU 1071  CB BMET A 104     1099    986    958     58   -163    -59       C  
ATOM   1072  CG AMET A 104       8.994 -16.439  -4.690  0.51  7.35           C  
ANISOU 1072  CG AMET A 104      851    660   1280   -121    -75    -95       C  
ATOM   1073  CG BMET A 104      10.131 -15.898  -3.613  0.49  7.78           C  
ANISOU 1073  CG BMET A 104     1048   1005    902     50   -151   -111       C  
ATOM   1074  SD AMET A 104       8.190 -15.050  -3.848  0.51  8.42           S  
ANISOU 1074  SD AMET A 104     1128    919   1154     50     29   -146       S  
ATOM   1075  SD BMET A 104       8.957 -14.585  -3.149  0.49  8.81           S  
ANISOU 1075  SD BMET A 104     1090   1002   1257    120    -32   -177       S  
ATOM   1076  CE AMET A 104       9.068 -14.971  -2.310  0.51 10.89           C  
ANISOU 1076  CE AMET A 104     1468   1270   1400     92     28   -298       C  
ATOM   1077  CE BMET A 104       7.397 -15.456  -3.334  0.49  9.73           C  
ANISOU 1077  CE BMET A 104     1567    974   1158     23    316     41       C  
ATOM   1078  H  AMET A 104      10.069 -18.046  -7.060  0.51  8.17           H  
ATOM   1079  H  BMET A 104      10.246 -18.251  -7.089  0.49  8.09           H  
ATOM   1080  HA AMET A 104      12.148 -17.132  -5.617  0.51  7.32           H  
ATOM   1081  HA BMET A 104      11.953 -16.946  -5.475  0.49  8.67           H  
ATOM   1082  HB2BMET A 104      10.182 -15.410  -5.585  0.49  9.61           H  
ATOM   1083  HB3AMET A 104      10.546 -15.376  -5.463  0.51  8.22           H  
ATOM   1084  N   LEU A 105      11.744 -18.751  -3.764  1.00  6.83           N  
ANISOU 1084  N   LEU A 105      792    785   1016      6    -66     50       N  
ATOM   1085  CA  LEU A 105      11.620 -19.828  -2.794  1.00  6.75           C  
ANISOU 1085  CA  LEU A 105      805    762    997    -63    -99     96       C  
ATOM   1086  C   LEU A 105      11.110 -19.264  -1.472  1.00  6.98           C  
ANISOU 1086  C   LEU A 105      898    799    954     82   -154      3       C  
ATOM   1087  O   LEU A 105      11.493 -18.168  -1.057  1.00  8.08           O  
ANISOU 1087  O   LEU A 105     1108    929   1032   -203     29    -55       O  
ATOM   1088  CB  LEU A 105      12.979 -20.492  -2.588  1.00  7.13           C  
ANISOU 1088  CB  LEU A 105      925    786    998     57    -81     65       C  
ATOM   1089  CG  LEU A 105      13.418 -21.415  -3.715  1.00  8.14           C  
ANISOU 1089  CG  LEU A 105      876   1018   1198     92     -4   -100       C  
ATOM   1090  CD1 LEU A 105      14.895 -21.691  -3.623  1.00 10.07           C  
ANISOU 1090  CD1 LEU A 105     1026   1248   1552    140    -57   -196       C  
ATOM   1091  CD2 LEU A 105      12.604 -22.727  -3.685  1.00 10.39           C  
ANISOU 1091  CD2 LEU A 105     1172   1097   1681     69     34   -351       C  
ATOM   1092  H  ALEU A 105      12.372 -18.197  -3.568  0.51  8.19           H  
ATOM   1093  H  BLEU A 105      12.427 -18.247  -3.626  0.49  8.19           H  
ATOM   1094  HA  LEU A 105      10.991 -20.493  -3.116  1.00  8.10           H  
ATOM   1095  HB2 LEU A 105      13.651 -19.797  -2.500  1.00  8.55           H  
ATOM   1096  HB3 LEU A 105      12.946 -21.018  -1.774  1.00  8.55           H  
ATOM   1097  HG  LEU A 105      13.249 -20.978  -4.565  1.00  9.76           H  
ATOM   1098 HD12 LEU A 105      15.378 -20.853  -3.693  1.00 12.09           H  
ATOM   1099 HD13 LEU A 105      15.085 -22.114  -2.771  1.00 12.09           H  
ATOM   1100 HD21 LEU A 105      12.900 -23.300  -4.409  1.00 12.47           H  
ATOM   1101 HD23 LEU A 105      11.663 -22.517  -3.792  1.00 12.47           H  
ATOM   1102  N   ILE A 106      10.256 -20.034  -0.813  1.00  6.89           N  
ANISOU 1102  N   ILE A 106      891    693   1032    -19     11     32       N  
ATOM   1103  CA  ILE A 106       9.692 -19.688   0.488  1.00  7.30           C  
ANISOU 1103  CA  ILE A 106      937    836   1002      6     -6    -12       C  
ATOM   1104  C   ILE A 106       9.963 -20.860   1.430  1.00  7.74           C  
ANISOU 1104  C   ILE A 106      989    911   1039    -87     54    -29       C  
ATOM   1105  O   ILE A 106       9.561 -21.992   1.131  1.00  8.43           O  
ANISOU 1105  O   ILE A 106     1224    888   1092   -117    -52     85       O  
ATOM   1106  CB  ILE A 106       8.183 -19.429   0.393  1.00  8.14           C  
ANISOU 1106  CB  ILE A 106      994    900   1200     29    112    -50       C  
ATOM   1107  CG1 ILE A 106       7.882 -18.292  -0.568  1.00  9.53           C  
ANISOU 1107  CG1 ILE A 106      992   1121   1507    203     10     63       C  
ATOM   1108  CG2 ILE A 106       7.608 -19.115   1.782  1.00 10.88           C  
ANISOU 1108  CG2 ILE A 106     1238   1430   1466    -24    238    -78       C  
ATOM   1109  CD1 ILE A 106       6.387 -18.206  -0.965  1.00 12.31           C  
ANISOU 1109  CD1 ILE A 106     1075   1617   1985    317    -39    126       C  
ATOM   1110  H   ILE A 106       9.976 -20.791  -1.110  1.00  8.26           H  
ATOM   1111  HA  ILE A 106      10.127 -18.895   0.838  1.00  8.76           H  
ATOM   1112  HB  ILE A 106       7.755 -20.233   0.059  1.00  9.77           H  
ATOM   1113 HG12 ILE A 106       8.129 -17.453  -0.150  1.00 11.43           H  
ATOM   1114 HG13 ILE A 106       8.399 -18.421  -1.379  1.00 11.43           H  
ATOM   1115 HG23 ILE A 106       8.047 -18.325   2.134  1.00 13.06           H  
ATOM   1116  N   LYS A 107      10.636 -20.595   2.547  1.00  8.39           N  
ANISOU 1116  N   LYS A 107     1212    940   1038   -145   -121    106       N  
ATOM   1117  CA  LYS A 107      10.845 -21.615   3.566  1.00  8.77           C  
ANISOU 1117  CA  LYS A 107     1323    960   1048    -79    -74    140       C  
ATOM   1118  C   LYS A 107       9.746 -21.514   4.608  1.00  8.96           C  
ANISOU 1118  C   LYS A 107     1325   1087    991     46    -28    159       C  
ATOM   1119  O   LYS A 107       9.384 -20.411   5.048  1.00 10.52           O  
ANISOU 1119  O   LYS A 107     1674   1087   1234    -69    155     31       O  
ATOM   1120  CB  LYS A 107      12.208 -21.466   4.234  1.00  9.40           C  
ANISOU 1120  CB  LYS A 107     1256   1110   1206   -115    -99    173       C  
ATOM   1121  CG  LYS A 107      12.556 -22.682   5.079  1.00 10.04           C  
ANISOU 1121  CG  LYS A 107     1235   1278   1301     48    -37    274       C  
ATOM   1122  CD  LYS A 107      13.924 -22.582   5.758  1.00 11.21           C  
ANISOU 1122  CD  LYS A 107     1222   1616   1420     42   -123    284       C  
ATOM   1123  CE  LYS A 107      14.254 -23.893   6.437  1.00 12.77           C  
ANISOU 1123  CE  LYS A 107     1198   1833   1822    250    -51    581       C  
ATOM   1124  NZ  LYS A 107      15.592 -23.759   7.103  1.00 14.43           N  
ANISOU 1124  NZ  LYS A 107     1345   2071   2065    190   -164    631       N  
ATOM   1125  H   LYS A 107      10.981 -19.830   2.737  1.00 10.07           H  
ATOM   1126  HA  LYS A 107      10.798 -22.493   3.157  1.00 10.52           H  
ATOM   1127  HB3 LYS A 107      12.191 -20.691   4.816  1.00 11.28           H  
ATOM   1128  HG3 LYS A 107      12.559 -23.470   4.513  1.00 12.05           H  
ATOM   1129  HE2 LYS A 107      13.593 -24.067   7.126  1.00 15.32           H  
ATOM   1130  N   LEU A 108       9.232 -22.665   5.013  1.00  9.22           N  
ANISOU 1130  N   LEU A 108     1160   1116   1227     -3      6    277       N  
ATOM   1131  CA  LEU A 108       8.220 -22.745   6.055  1.00  9.62           C  
ANISOU 1131  CA  LEU A 108     1217   1211   1226    101     43    312       C  
ATOM   1132  C   LEU A 108       8.863 -22.763   7.441  1.00 10.25           C  
ANISOU 1132  C   LEU A 108     1269   1277   1350     87     56    424       C  
ATOM   1133  O   LEU A 108       9.909 -23.370   7.647  1.00 11.27           O  
ANISOU 1133  O   LEU A 108     1359   1544   1378    186   -129    324       O  
ATOM   1134  CB  LEU A 108       7.410 -24.027   5.861  1.00  9.97           C  
ANISOU 1134  CB  LEU A 108     1089   1371   1328     20      3    321       C  
ATOM   1135  CG  LEU A 108       6.760 -24.208   4.497  1.00 11.98           C  
ANISOU 1135  CG  LEU A 108     1598   1469   1487    -29   -326    420       C  
ATOM   1136  CD1 LEU A 108       5.941 -25.493   4.449  1.00 13.47           C  
ANISOU 1136  CD1 LEU A 108     1570   1723   1824   -147   -249    315       C  
ATOM   1137  CD2 LEU A 108       5.945 -23.011   4.116  1.00 14.37           C  
ANISOU 1137  CD2 LEU A 108     1833   1697   1928    296   -385     21       C  
ATOM   1138  HB3 LEU A 108       6.712 -24.064   6.534  1.00 11.96           H  
ATOM   1139 HD12 LEU A 108       6.526 -26.247   4.621  1.00 16.16           H  
ATOM   1140 HD13 LEU A 108       5.247 -25.451   5.126  1.00 16.16           H  
ATOM   1141  N   LYS A 109       8.182 -22.140   8.411  1.00 10.13           N  
ANISOU 1141  N   LYS A 109     1261   1386   1201    134    -10    260       N  
ATOM   1142  CA  LYS A 109       8.698 -22.105   9.780  1.00 11.49           C  
ANISOU 1142  CA  LYS A 109     1547   1593   1225    -14   -259    309       C  
ATOM   1143  C   LYS A 109       8.781 -23.490  10.398  1.00 12.30           C  
ANISOU 1143  C   LYS A 109     1680   1589   1403   -255   -368    485       C  
ATOM   1144  O   LYS A 109       9.627 -23.718  11.259  1.00 15.53           O  
ANISOU 1144  O   LYS A 109     2216   1945   1741   -366   -768    671       O  
ATOM   1145  CB  LYS A 109       7.827 -21.219  10.664  1.00 14.05           C  
ANISOU 1145  CB  LYS A 109     2178   1883   1277     39     34     -3       C  
ATOM   1146  CG  LYS A 109       8.095 -19.750  10.565  1.00 18.49           C  
ANISOU 1146  CG  LYS A 109     2500   2400   2124    142    404   -151       C  
ATOM   1147  CD  LYS A 109       7.140 -18.957  11.448  1.00 26.33           C  
ANISOU 1147  CD  LYS A 109     3475   3205   3323    -80    594  -1100       C  
ATOM   1148  CE  LYS A 109       7.466 -17.475  11.382  1.00 32.79           C  
ANISOU 1148  CE  LYS A 109     4141   4034   4284   -536    663  -1677       C  
ATOM   1149  NZ  LYS A 109       8.486 -17.107  12.404  1.00 35.15           N  
ANISOU 1149  NZ  LYS A 109     4283   4422   4650  -1126    559  -2024       N  
ATOM   1150  H   LYS A 109       7.431 -21.736   8.303  1.00 12.15           H  
ATOM   1151  N   SER A 110       7.914 -24.414   9.987  1.00 12.44           N  
ANISOU 1151  N   SER A 110     1644   1652   1432   -186   -318    598       N  
ATOM   1152  CA  SER A 110       7.951 -25.805  10.412  1.00 14.06           C  
ANISOU 1152  CA  SER A 110     1938   1781   1623   -329   -292    724       C  
ATOM   1153  C   SER A 110       7.675 -26.688   9.212  1.00 12.44           C  
ANISOU 1153  C   SER A 110     1535   1658   1532   -265   -361    622       C  
ATOM   1154  O   SER A 110       7.071 -26.248   8.241  1.00 12.65           O  
ANISOU 1154  O   SER A 110     1619   1564   1624    -18   -358    617       O  
ATOM   1155  CB  SER A 110       6.911 -26.071  11.511  1.00 17.85           C  
ANISOU 1155  CB  SER A 110     2591   2262   1929   -204   -194    834       C  
ATOM   1156  OG  SER A 110       5.592 -25.708  11.102  1.00 18.91           O  
ANISOU 1156  OG  SER A 110     2688   2312   2185   -378    368    735       O  
ATOM   1157  H   SER A 110       7.271 -24.248   9.440  1.00 14.93           H  
ATOM   1158  N   ALA A 111       8.096 -27.952   9.298  1.00 14.00           N  
ANISOU 1158  N   ALA A 111     1753   1603   1963   -156   -665    773       N  
ATOM   1159  CA  ALA A 111       7.867 -28.860   8.190  1.00 13.15           C  
ANISOU 1159  CA  ALA A 111     1612   1420   1965   -142   -481    552       C  
ATOM   1160  C   ALA A 111       6.398 -29.240   8.115  1.00 11.80           C  
ANISOU 1160  C   ALA A 111     1302   1504   1679   -173   -162    404       C  
ATOM   1161  O   ALA A 111       5.758 -29.548   9.128  1.00 14.40           O  
ANISOU 1161  O   ALA A 111     1948   1905   1620   -432     15    572       O  
ATOM   1162  CB  ALA A 111       8.695 -30.129   8.371  1.00 15.05           C  
ANISOU 1162  CB  ALA A 111     1585   1720   2414      8   -498    574       C  
ATOM   1163  HB2 ALA A 111       9.635 -29.906   8.291  1.00 18.06           H  
ATOM   1164  N   ALA A 112       5.872 -29.268   6.897  1.00 10.96           N  
ANISOU 1164  N   ALA A 112     1263   1302   1601     53   -105    507       N  
ATOM   1165  CA  ALA A 112       4.549 -29.812   6.671  1.00 10.79           C  
ANISOU 1165  CA  ALA A 112     1123   1236   1742     -5    -84    241       C  
ATOM   1166  C   ALA A 112       4.563 -31.306   6.951  1.00 11.11           C  
ANISOU 1166  C   ALA A 112     1365   1201   1656     61    -81    321       C  
ATOM   1167  O   ALA A 112       5.574 -31.992   6.773  1.00 12.61           O  
ANISOU 1167  O   ALA A 112     1323   1248   2219    213     89    344       O  
ATOM   1168  CB  ALA A 112       4.142 -29.594   5.210  1.00 12.85           C  
ANISOU 1168  CB  ALA A 112     1465   1548   1870   -115   -348    476       C  
ATOM   1169  H   ALA A 112       6.263 -28.978   6.188  1.00 13.16           H  
ATOM   1170  HA  ALA A 112       3.903 -29.381   7.252  1.00 12.95           H  
ATOM   1171  N  ASER A 113       3.415 -31.810   7.371  0.51 11.23           N  
ANISOU 1171  N  ASER A 113     1334   1164   1769   -184   -128    336       N  
ATOM   1172  N  BSER A 113       3.434 -31.797   7.440  0.49 10.98           N  
ANISOU 1172  N  BSER A 113     1191   1195   1786     22    -54    300       N  
ATOM   1173  CA ASER A 113       3.201 -33.243   7.534  0.51 12.15           C  
ANISOU 1173  CA ASER A 113     1664   1183   1769   -169   -275    468       C  
ATOM   1174  CA BSER A 113       3.191 -33.230   7.522  0.49 12.40           C  
ANISOU 1174  CA BSER A 113     1465   1442   1805    -69    -57    287       C  
ATOM   1175  C  ASER A 113       2.705 -33.805   6.205  0.51 11.26           C  
ANISOU 1175  C  ASER A 113     1506    922   1852    -40   -253    376       C  
ATOM   1176  C  BSER A 113       2.758 -33.714   6.144  0.49 12.23           C  
ANISOU 1176  C  BSER A 113     1488   1294   1865     31   -239    193       C  
ATOM   1177  O  ASER A 113       1.576 -33.535   5.793  0.51 12.23           O  
ANISOU 1177  O  ASER A 113     1351   1174   2122    -46   -282     82       O  
ATOM   1178  O  BSER A 113       1.740 -33.262   5.611  0.49 13.76           O  
ANISOU 1178  O  BSER A 113     1482   1552   2195    259   -241   -261       O  
ATOM   1179  CB ASER A 113       2.190 -33.486   8.648  0.51 14.37           C  
ANISOU 1179  CB ASER A 113     2080   1511   1868   -373   -123    505       C  
ATOM   1180  CB BSER A 113       2.103 -33.509   8.558  0.49 14.00           C  
ANISOU 1180  CB BSER A 113     1581   1871   1866   -179    394    265       C  
ATOM   1181  OG ASER A 113       1.928 -34.869   8.790  0.51 16.25           O  
ANISOU 1181  OG ASER A 113     2465   1576   2132   -437   -169    631       O  
ATOM   1182  OG BSER A 113       2.502 -33.093   9.852  0.49 16.00           O  
ANISOU 1182  OG BSER A 113     1843   2137   2101   -317    166    250       O  
ATOM   1183  H  ASER A 113       2.727 -31.335   7.573  0.51 13.48           H  
ATOM   1184  H  BSER A 113       2.785 -31.316   7.735  0.49 13.17           H  
ATOM   1185  HA ASER A 113       4.037 -33.678   7.768  0.51 14.58           H  
ATOM   1186  HA BSER A 113       4.003 -33.692   7.781  0.49 14.88           H  
ATOM   1187  N   LEU A 114       3.536 -34.602   5.554  1.00 12.03           N  
ANISOU 1187  N   LEU A 114     1593   1199   1780    247   -227    227       N  
ATOM   1188  CA  LEU A 114       3.235 -35.076   4.225  1.00 12.20           C  
ANISOU 1188  CA  LEU A 114     1595   1208   1832    176   -328    274       C  
ATOM   1189  C   LEU A 114       2.333 -36.292   4.300  1.00 13.09           C  
ANISOU 1189  C   LEU A 114     1681   1500   1795   -113   -187    486       C  
ATOM   1190  O   LEU A 114       2.498 -37.154   5.166  1.00 15.88           O  
ANISOU 1190  O   LEU A 114     2233   1585   2216   -227   -443    562       O  
ATOM   1191  CB  LEU A 114       4.519 -35.357   3.452  1.00 13.28           C  
ANISOU 1191  CB  LEU A 114     1621   1297   2128     67   -389    337       C  
ATOM   1192  CG  LEU A 114       5.453 -34.148   3.337  1.00 14.14           C  
ANISOU 1192  CG  LEU A 114     1606   1537   2229    -61   -182    174       C  
ATOM   1193  CD1 LEU A 114       6.672 -34.483   2.484  1.00 17.74           C  
ANISOU 1193  CD1 LEU A 114     1834   2327   2579   -141    134    -87       C  
ATOM   1194  CD2 LEU A 114       4.749 -32.927   2.749  1.00 15.91           C  
ANISOU 1194  CD2 LEU A 114     1862   1776   2406   -228   -366    776       C  
ATOM   1195  HA  LEU A 114       2.753 -34.381   3.750  1.00 14.64           H  
ATOM   1196  N   ASN A 115       1.336 -36.314   3.415  1.00 12.57           N  
ANISOU 1196  N   ASN A 115     1472   1525   1780    -64    -69    290       N  
ATOM   1197  CA  ASN A 115       0.326 -37.360   3.362  1.00 13.47           C  
ANISOU 1197  CA  ASN A 115     1636   1682   1801    -55   -185    415       C  
ATOM   1198  C   ASN A 115      -0.235 -37.403   1.941  1.00 13.39           C  
ANISOU 1198  C   ASN A 115     1729   1584   1773     18   -207    239       C  
ATOM   1199  O   ASN A 115       0.314 -36.765   1.039  1.00 14.39           O  
ANISOU 1199  O   ASN A 115     1975   1628   1864   -121   -233    455       O  
ATOM   1200  CB  ASN A 115      -0.702 -37.144   4.474  1.00 14.62           C  
ANISOU 1200  CB  ASN A 115     1942   1733   1879     32    -45    510       C  
ATOM   1201  CG  ASN A 115      -1.396 -35.807   4.360  1.00 14.34           C  
ANISOU 1201  CG  ASN A 115     2083   1640   1724    159    -78    343       C  
ATOM   1202  OD1 ASN A 115      -1.866 -35.462   3.282  1.00 14.40           O  
ANISOU 1202  OD1 ASN A 115     2225   1542   1705     33   -141    133       O  
ATOM   1203  ND2 ASN A 115      -1.456 -35.044   5.452  1.00 16.45           N  
ANISOU 1203  ND2 ASN A 115     2699   1854   1698     73     47    162       N  
ATOM   1204  N   SER A 116      -1.298 -38.181   1.705  1.00 13.44           N  
ANISOU 1204  N   SER A 116     1820   1296   1989     42   -158    405       N  
ATOM   1205  CA  SER A 116      -1.774 -38.294   0.321  1.00 12.76           C  
ANISOU 1205  CA  SER A 116     1672   1035   2141    -44   -225    114       C  
ATOM   1206  C   SER A 116      -2.330 -36.987  -0.226  1.00 11.60           C  
ANISOU 1206  C   SER A 116     1671   1191   1546     47   -138     27       C  
ATOM   1207  O   SER A 116      -2.392 -36.812  -1.451  1.00 13.33           O  
ANISOU 1207  O   SER A 116     1992   1387   1686    353   -214    -55       O  
ATOM   1208  CB  SER A 116      -2.888 -39.330   0.245  1.00 15.43           C  
ANISOU 1208  CB  SER A 116     2040   1407   2416    130     -7    194       C  
ATOM   1209  OG  SER A 116      -3.973 -38.937   1.083  1.00 15.78           O  
ANISOU 1209  OG  SER A 116     2290   1730   1977   -192     55     56       O  
ATOM   1210  N  AARG A 117      -2.757 -36.087   0.647  0.69 11.44           N  
ANISOU 1210  N  AARG A 117     1578   1268   1502    343     81     79       N  
ATOM   1211  N  BARG A 117      -2.777 -36.087   0.645  0.31 10.80           N  
ANISOU 1211  N  BARG A 117     1451   1093   1560    -15   -250    255       N  
ATOM   1212  CA AARG A 117      -3.405 -34.848   0.272  0.69 11.31           C  
ANISOU 1212  CA AARG A 117     1536   1335   1426    410    184     26       C  
ATOM   1213  CA BARG A 117      -3.402 -34.840   0.242  0.31 10.38           C  
ANISOU 1213  CA BARG A 117     1394   1010   1541    -82   -248    351       C  
ATOM   1214  C  AARG A 117      -2.491 -33.640   0.365  0.69 11.24           C  
ANISOU 1214  C  AARG A 117     1564   1282   1427    383     60    234       C  
ATOM   1215  C  BARG A 117      -2.462 -33.646   0.313  0.31  9.75           C  
ANISOU 1215  C  BARG A 117     1251   1041   1414   -211    -45    374       C  
ATOM   1216  O  AARG A 117      -2.879 -32.568  -0.112  0.69 13.22           O  
ANISOU 1216  O  AARG A 117     1847   1444   1732    556    -43    354       O  
ATOM   1217  O  BARG A 117      -2.787 -32.595  -0.249  0.31  9.85           O  
ANISOU 1217  O  BARG A 117     1120   1139   1481   -367     90    357       O  
ATOM   1218  CB AARG A 117      -4.657 -34.646   1.125  0.69 11.04           C  
ANISOU 1218  CB AARG A 117     1538   1290   1365     83    191   -103       C  
ATOM   1219  CB BARG A 117      -4.669 -34.598   1.077  0.31 10.11           C  
ANISOU 1219  CB BARG A 117     1458    807   1574    -10   -326    282       C  
ATOM   1220  CG AARG A 117      -5.685 -35.716   0.847  0.69 12.56           C  
ANISOU 1220  CG AARG A 117     1464   1758   1548   -157    248   -215       C  
ATOM   1221  CG BARG A 117      -5.738 -35.669   0.854  0.31 10.35           C  
ANISOU 1221  CG BARG A 117     1528    677   1726     78   -281    281       C  
ATOM   1222  CD AARG A 117      -6.925 -35.504   1.689  0.69 14.82           C  
ANISOU 1222  CD AARG A 117     1574   2159   1897   -297    399   -273       C  
ATOM   1223  CD BARG A 117      -6.970 -35.468   1.727  0.31 11.56           C  
ANISOU 1223  CD BARG A 117     1626    823   1943    -38     37    368       C  
ATOM   1224  NE AARG A 117      -7.983 -36.441   1.334  0.69 16.67           N  
ANISOU 1224  NE AARG A 117     1776   2406   2151   -561    342    -73       N  
ATOM   1225  NE BARG A 117      -7.974 -36.519   1.550  0.31 13.38           N  
ANISOU 1225  NE BARG A 117     1799   1073   2212   -161    227    289       N  
ATOM   1226  CZ AARG A 117      -8.062 -37.683   1.792  0.69 17.31           C  
ANISOU 1226  CZ AARG A 117     1907   2463   2209  -1011    -99    152       C  
ATOM   1227  CZ BARG A 117      -9.063 -36.426   0.790  0.31 15.42           C  
ANISOU 1227  CZ BARG A 117     1967   1526   2366   -323    396    122       C  
ATOM   1228  NH1AARG A 117      -7.139 -38.155   2.624  0.69 19.30           N  
ANISOU 1228  NH1AARG A 117     2440   2444   2449   -944   -413    526       N  
ATOM   1229  NH1BARG A 117      -9.312 -35.322   0.102  0.31 15.14           N  
ANISOU 1229  NH1BARG A 117     1920   1511   2320   -518    554    -14       N  
ATOM   1230  NH2AARG A 117      -9.061 -38.458   1.399  0.69 20.11           N  
ANISOU 1230  NH2AARG A 117     2457   2864   2322  -1190     67     28       N  
ATOM   1231  NH2BARG A 117      -9.905 -37.454   0.711  0.31 16.56           N  
ANISOU 1231  NH2BARG A 117     1965   1886   2442   -438    511    -35       N  
ATOM   1232  H  AARG A 117      -2.677 -36.180   1.498  0.69 13.73           H  
ATOM   1233  H  BARG A 117      -2.725 -36.184   1.499  0.31 12.96           H  
ATOM   1234  HB3AARG A 117      -5.052 -33.787   0.907  0.69 13.24           H  
ATOM   1235  HB3BARG A 117      -5.049 -33.739   0.832  0.31 12.13           H  
ATOM   1236  HD2AARG A 117      -6.701 -35.645   2.622  0.69 17.78           H  
ATOM   1237  HD2BARG A 117      -6.700 -35.466   2.659  0.31 13.87           H  
ATOM   1238  N   VAL A 118      -1.315 -33.786   0.977  1.00 10.75           N  
ANISOU 1238  N   VAL A 118     1444   1201   1438    132    -14    265       N  
ATOM   1239  CA  VAL A 118      -0.314 -32.742   1.090  1.00 10.20           C  
ANISOU 1239  CA  VAL A 118     1276   1200   1399     29    -16    336       C  
ATOM   1240  C   VAL A 118       1.006 -33.422   0.739  1.00 10.64           C  
ANISOU 1240  C   VAL A 118     1401   1137   1505      6     -3    200       C  
ATOM   1241  O   VAL A 118       1.523 -34.239   1.512  1.00 11.94           O  
ANISOU 1241  O   VAL A 118     1531   1443   1563    423    -60    473       O  
ATOM   1242  CB  VAL A 118      -0.279 -32.101   2.480  1.00 10.33           C  
ANISOU 1242  CB  VAL A 118     1384   1048   1492     27    -14    303       C  
ATOM   1243  CG1 VAL A 118       0.854 -31.102   2.567  1.00 11.66           C  
ANISOU 1243  CG1 VAL A 118     1591   1042   1799    -53    -39    129       C  
ATOM   1244  CG2 VAL A 118      -1.615 -31.457   2.790  1.00 11.71           C  
ANISOU 1244  CG2 VAL A 118     1624   1278   1549     60     98    143       C  
ATOM   1245  H  AVAL A 118      -1.071 -34.521   1.351  1.00 12.90           H  
ATOM   1246  H  BVAL A 118      -1.093 -34.510   1.386  0.00 12.90           H  
ATOM   1247  HA  VAL A 118      -0.491 -32.050   0.434  1.00 12.24           H  
ATOM   1248  HB  VAL A 118      -0.120 -32.792   3.141  1.00 12.40           H  
ATOM   1249 HG11 VAL A 118       0.940 -30.802   3.485  1.00 14.00           H  
ATOM   1250 HG21 VAL A 118      -1.574 -31.056   3.673  1.00 14.06           H  
ATOM   1251 HG22 VAL A 118      -1.798 -30.775   2.125  1.00 14.06           H  
ATOM   1252 HG23 VAL A 118      -2.306 -32.137   2.767  1.00 14.06           H  
ATOM   1253  N   ALA A 119       1.518 -33.140  -0.449  1.00  9.41           N  
ANISOU 1253  N   ALA A 119     1239    910   1428     65    -17    112       N  
ATOM   1254  CA  ALA A 119       2.626 -33.910  -0.990  1.00  9.54           C  
ANISOU 1254  CA  ALA A 119     1425    788   1413     76   -140    102       C  
ATOM   1255  C   ALA A 119       3.496 -32.987  -1.821  1.00  9.62           C  
ANISOU 1255  C   ALA A 119     1437    878   1339     98   -176     47       C  
ATOM   1256  O   ALA A 119       3.000 -32.062  -2.457  1.00 10.59           O  
ANISOU 1256  O   ALA A 119     1361   1023   1638    169    -94    214       O  
ATOM   1257  CB  ALA A 119       2.130 -35.074  -1.852  1.00 11.69           C  
ANISOU 1257  CB  ALA A 119     1499   1129   1814     64   -201   -221       C  
ATOM   1258  HA  ALA A 119       3.160 -34.267  -0.263  1.00 11.45           H  
ATOM   1259  HB1 ALA A 119       2.895 -35.564  -2.193  1.00 14.03           H  
ATOM   1260  HB3 ALA A 119       1.607 -34.722  -2.589  1.00 14.03           H  
ATOM   1261  N   SER A 120       4.797 -33.273  -1.839  1.00  9.47           N  
ANISOU 1261  N   SER A 120     1185    882   1532     68    -22    121       N  
ATOM   1262  CA  SER A 120       5.699 -32.520  -2.686  1.00  9.59           C  
ANISOU 1262  CA  SER A 120     1296    856   1493     61    -46     43       C  
ATOM   1263  C   SER A 120       5.594 -32.961  -4.145  1.00  9.35           C  
ANISOU 1263  C   SER A 120     1307    772   1473    128   -115    -42       C  
ATOM   1264  O   SER A 120       5.201 -34.088  -4.459  1.00 11.55           O  
ANISOU 1264  O   SER A 120     1883    805   1702   -146     16    -63       O  
ATOM   1265  CB  SER A 120       7.137 -32.628  -2.191  1.00 11.46           C  
ANISOU 1265  CB  SER A 120     1575   1212   1565     81   -158    136       C  
ATOM   1266  OG  SER A 120       7.516 -33.962  -2.035  1.00 13.73           O  
ANISOU 1266  OG  SER A 120     1599   1478   2142    238    -11    114       O  
ATOM   1267  HA  SER A 120       5.448 -31.584  -2.646  1.00 11.51           H  
ATOM   1268  HB2 SER A 120       7.725 -32.207  -2.838  1.00 13.75           H  
ATOM   1269  HB3 SER A 120       7.210 -32.177  -1.335  1.00 13.75           H  
ATOM   1270  N   ILE A 121       5.982 -32.052  -5.036  1.00  9.29           N  
ANISOU 1270  N   ILE A 121     1299    861   1369     36    -63    -20       N  
ATOM   1271  CA  ILE A 121       6.112 -32.331  -6.471  1.00  9.82           C  
ANISOU 1271  CA  ILE A 121     1417    938   1375     68    -17   -131       C  
ATOM   1272  C   ILE A 121       7.593 -32.369  -6.840  1.00  9.58           C  
ANISOU 1272  C   ILE A 121     1285    859   1495    144     24     29       C  
ATOM   1273  O   ILE A 121       8.365 -31.489  -6.456  1.00 10.84           O  
ANISOU 1273  O   ILE A 121     1257   1014   1846    138     10    -71       O  
ATOM   1274  CB  ILE A 121       5.317 -31.310  -7.319  1.00 10.70           C  
ANISOU 1274  CB  ILE A 121     1279   1491   1295    331     38   -215       C  
ATOM   1275  CG1 ILE A 121       5.349 -31.669  -8.818  1.00 13.37           C  
ANISOU 1275  CG1 ILE A 121     1621   1899   1562    540   -204   -383       C  
ATOM   1276  CG2 ILE A 121       5.819 -29.867  -7.126  1.00 10.91           C  
ANISOU 1276  CG2 ILE A 121     1612   1095   1438    264     12     19       C  
ATOM   1277  CD1 ILE A 121       4.606 -32.902  -9.118  1.00 15.80           C  
ANISOU 1277  CD1 ILE A 121     1796   2486   1723    437   -239   -594       C  
ATOM   1278  HA  ILE A 121       5.743 -33.210  -6.649  1.00 11.78           H  
ATOM   1279  HB  ILE A 121       4.393 -31.342  -7.027  1.00 12.84           H  
ATOM   1280  N   SER A 122       7.984 -33.385  -7.603  1.00 10.74           N  
ANISOU 1280  N   SER A 122     1476    962   1643    254    144    -12       N  
ATOM   1281  CA  SER A 122       9.353 -33.533  -8.064  1.00 11.92           C  
ANISOU 1281  CA  SER A 122     1543    951   2034    480    301    130       C  
ATOM   1282  C   SER A 122       9.783 -32.384  -8.971  1.00 10.56           C  
ANISOU 1282  C   SER A 122     1528    966   1520    506    231     -7       C  
ATOM   1283  O   SER A 122       9.028 -31.931  -9.843  1.00 10.81           O  
ANISOU 1283  O   SER A 122     1528    994   1584    360    -39    -68       O  
ATOM   1284  CB  SER A 122       9.456 -34.836  -8.861  1.00 16.30           C  
ANISOU 1284  CB  SER A 122     2349   1154   2689    580    948    223       C  
ATOM   1285  OG  SER A 122       9.182 -35.970  -8.061  1.00 21.81           O  
ANISOU 1285  OG  SER A 122     3386   1486   3413    686   1203    437       O  
ATOM   1286  HB3 SER A 122      10.352 -34.914  -9.224  1.00 19.56           H  
ATOM   1287  N   LEU A 123      11.058 -31.981  -8.808  1.00 11.64           N  
ANISOU 1287  N   LEU A 123     1583   1192   1650    380    163     86       N  
ATOM   1288  CA  LEU A 123      11.678 -31.068  -9.741  1.00 11.05           C  
ANISOU 1288  CA  LEU A 123     1512   1144   1541    196     15   -116       C  
ATOM   1289  C   LEU A 123      12.104 -31.823 -10.989  1.00 11.38           C  
ANISOU 1289  C   LEU A 123     1449   1125   1751    298     24   -316       C  
ATOM   1290  O   LEU A 123      12.361 -33.024 -10.933  1.00 14.91           O  
ANISOU 1290  O   LEU A 123     2341   1248   2076    433    237   -388       O  
ATOM   1291  CB  LEU A 123      12.893 -30.396  -9.105  1.00 12.47           C  
ANISOU 1291  CB  LEU A 123     1897   1264   1575     75     21   -128       C  
ATOM   1292  CG  LEU A 123      12.574 -29.463  -7.936  1.00 16.39           C  
ANISOU 1292  CG  LEU A 123     2963   1595   1671   -188    186   -283       C  
ATOM   1293  CD1 LEU A 123      13.855 -28.938  -7.324  1.00 20.58           C  
ANISOU 1293  CD1 LEU A 123     3618   2259   1944   -495   -276   -461       C  
ATOM   1294  CD2 LEU A 123      11.700 -28.309  -8.405  1.00 17.86           C  
ANISOU 1294  CD2 LEU A 123     3001   1550   2237     59    495   -562       C  
ATOM   1295  HB2 LEU A 123      13.489 -31.086  -8.774  1.00 14.96           H  
ATOM   1296  HB3 LEU A 123      13.346 -29.872  -9.783  1.00 14.96           H  
ATOM   1297  HG  LEU A 123      12.089 -29.955  -7.255  1.00 19.67           H  
ATOM   1298  N  APRO A 124      12.148 -31.149 -12.141  0.49 11.92           N  
ANISOU 1298  N  APRO A 124     1441   1405   1683    465   -121   -225       N  
ATOM   1299  N  BPRO A 124      12.178 -31.144 -12.123  0.51 11.32           N  
ANISOU 1299  N  BPRO A 124     1455   1411   1435     79     24   -542       N  
ATOM   1300  CA APRO A 124      12.587 -31.822 -13.371  0.49 13.20           C  
ANISOU 1300  CA APRO A 124     1562   1617   1835    595    -42   -327       C  
ATOM   1301  CA BPRO A 124      12.474 -31.845 -13.375  0.51 13.53           C  
ANISOU 1301  CA BPRO A 124     1616   1848   1679     61    118   -579       C  
ATOM   1302  C  APRO A 124      14.039 -32.228 -13.262  0.49 12.84           C  
ANISOU 1302  C  APRO A 124     1648   1554   1675    747   -108   -137       C  
ATOM   1303  C  BPRO A 124      13.946 -32.187 -13.496  0.51 14.78           C  
ANISOU 1303  C  BPRO A 124     1868   2045   1702    420     45   -694       C  
ATOM   1304  O  APRO A 124      14.825 -31.606 -12.557  0.49 12.81           O  
ANISOU 1304  O  APRO A 124     1403   1836   1628    408   -102   -139       O  
ATOM   1305  O  BPRO A 124      14.824 -31.409 -13.123  0.51 15.62           O  
ANISOU 1305  O  BPRO A 124     1753   2522   1659    328    312   -458       O  
ATOM   1306  CB APRO A 124      12.437 -30.742 -14.452  0.49 15.59           C  
ANISOU 1306  CB APRO A 124     1894   2030   1997    912   -169   -160       C  
ATOM   1307  CB BPRO A 124      12.039 -30.840 -14.447  0.51 15.02           C  
ANISOU 1307  CB BPRO A 124     1832   2278   1596     73    150   -231       C  
ATOM   1308  CG APRO A 124      11.634 -29.646 -13.850  0.49 16.11           C  
ANISOU 1308  CG APRO A 124     2089   2025   2008    482    -72     -1       C  
ATOM   1309  CG BPRO A 124      12.222 -29.507 -13.798  0.51 12.27           C  
ANISOU 1309  CG BPRO A 124     1485   1885   1291    -76    324    -86       C  
ATOM   1310  CD APRO A 124      11.831 -29.727 -12.361  0.49 13.54           C  
ANISOU 1310  CD APRO A 124     1710   1515   1918    757   -137     91       C  
ATOM   1311  CD BPRO A 124      11.900 -29.713 -12.327  0.51 12.19           C  
ANISOU 1311  CD BPRO A 124     1457   1637   1537    136     71   -172       C  
ATOM   1312  HD3APRO A 124      10.992 -29.519 -11.920  0.49 16.24           H  
ATOM   1313  HD3BPRO A 124      10.954 -29.552 -12.186  0.51 14.62           H  
ATOM   1314  N  ATHR A 125      14.389 -33.297 -13.957  0.49 17.36           N  
ANISOU 1314  N  ATHR A 125     2376   2131   2091   1139    334     -9       N  
ATOM   1315  N  BTHR A 125      14.198 -33.393 -13.999  0.51 17.69           N  
ANISOU 1315  N  BTHR A 125     2318   2296   2108   1117    184   -456       N  
ATOM   1316  CA ATHR A 125      15.782 -33.527 -14.278  0.49 19.98           C  
ANISOU 1316  CA ATHR A 125     2737   2604   2249   1546    283    128       C  
ATOM   1317  CA BTHR A 125      15.552 -33.812 -14.321  0.51 18.93           C  
ANISOU 1317  CA BTHR A 125     2481   2473   2240   1409    209   -284       C  
ATOM   1318  C  ATHR A 125      16.064 -33.215 -15.732  0.49 19.09           C  
ANISOU 1318  C  ATHR A 125     2587   2647   2021   1538     62    -16       C  
ATOM   1319  C  BTHR A 125      15.983 -33.225 -15.654  0.51 19.01           C  
ANISOU 1319  C  BTHR A 125     2421   2635   2169   1386    332   -279       C  
ATOM   1320  O  ATHR A 125      17.237 -33.125 -16.118  0.49 19.70           O  
ANISOU 1320  O  ATHR A 125     2540   2902   2045   1048   -171   -188       O  
ATOM   1321  O  BTHR A 125      17.163 -32.914 -15.860  0.51 20.61           O  
ANISOU 1321  O  BTHR A 125     2471   2926   2435    976    219   -320       O  
ATOM   1322  CB ATHR A 125      16.183 -34.977 -13.987  0.49 22.98           C  
ANISOU 1322  CB ATHR A 125     3339   2684   2709   1539    453    336       C  
ATOM   1323  CB BTHR A 125      15.578 -35.338 -14.404  0.51 20.77           C  
ANISOU 1323  CB BTHR A 125     2928   2443   2521   1528     27   -228       C  
ATOM   1324  OG1ATHR A 125      15.329 -35.844 -14.737  0.49 24.10           O  
ANISOU 1324  OG1ATHR A 125     3638   2512   3008   1228    777      0       O  
ATOM   1325  OG1BTHR A 125      15.294 -35.888 -13.109  0.51 21.54           O  
ANISOU 1325  OG1BTHR A 125     3070   2675   2439   1444   -232    -12       O  
ATOM   1326  CG2ATHR A 125      16.061 -35.287 -12.499  0.49 24.28           C  
ANISOU 1326  CG2ATHR A 125     3523   3043   2660   1626    558    407       C  
ATOM   1327  CG2BTHR A 125      16.923 -35.839 -14.894  0.51 21.44           C  
ANISOU 1327  CG2BTHR A 125     2986   2432   2728   1408     -9    -68       C  
ATOM   1328  N   SER A 127      15.028 -33.066 -16.551  1.00 19.14           N  
ANISOU 1328  N   SER A 127     2681   2698   1892   1487    217    -71       N  
ATOM   1329  CA  SER A 127      15.228 -32.566 -17.894  1.00 19.24           C  
ANISOU 1329  CA  SER A 127     2515   2709   2087   1382    247   -454       C  
ATOM   1330  C   SER A 127      14.092 -31.615 -18.231  1.00 15.68           C  
ANISOU 1330  C   SER A 127     1922   2277   1760    747    365   -188       C  
ATOM   1331  O   SER A 127      12.981 -31.726 -17.720  1.00 15.40           O  
ANISOU 1331  O   SER A 127     1767   2260   1823    805    214    -44       O  
ATOM   1332  CB  SER A 127      15.292 -33.661 -18.956  1.00 26.16           C  
ANISOU 1332  CB  SER A 127     3417   3557   2965   1821    -66   -982       C  
ATOM   1333  OG  SER A 127      14.133 -34.467 -18.937  1.00 33.48           O  
ANISOU 1333  OG  SER A 127     4404   4672   3644   1568    -61  -1107       O  
ATOM   1334  N   CYS A 128      14.395 -30.669 -19.088  1.00 15.62           N  
ANISOU 1334  N   CYS A 128     2143   2164   1629    775    576   -129       N  
ATOM   1335  CA  CYS A 128      13.395 -29.733 -19.550  1.00 14.88           C  
ANISOU 1335  CA  CYS A 128     2367   2015   1274    736    284   -385       C  
ATOM   1336  C   CYS A 128      12.367 -30.455 -20.402  1.00 14.56           C  
ANISOU 1336  C   CYS A 128     2478   1745   1309    853    232   -423       C  
ATOM   1337  O   CYS A 128      12.617 -31.533 -20.948  1.00 20.42           O  
ANISOU 1337  O   CYS A 128     3520   2191   2048   1016   -164   -903       O  
ATOM   1338  CB  CYS A 128      14.064 -28.616 -20.346  1.00 17.28           C  
ANISOU 1338  CB  CYS A 128     2285   2975   1304   1094    353   -263       C  
ATOM   1339  SG  CYS A 128      15.269 -27.681 -19.435  1.00 16.82           S  
ANISOU 1339  SG  CYS A 128     1846   3006   1539    302    386   -260       S  
ATOM   1340  HA  CYS A 128      12.943 -29.340 -18.788  1.00 17.86           H  
ATOM   1341  N   ALA A 129      11.189 -29.875 -20.479  1.00 14.10           N  
ANISOU 1341  N   ALA A 129     2398   1652   1307    447   -138   -352       N  
ATOM   1342  CA  ALA A 129      10.116 -30.417 -21.275  1.00 14.15           C  
ANISOU 1342  CA  ALA A 129     2423   1609   1344    436    -39   -157       C  
ATOM   1343  C   ALA A 129      10.090 -29.772 -22.655  1.00 14.87           C  
ANISOU 1343  C   ALA A 129     2631   1434   1586    212    -85   -246       C  
ATOM   1344  O   ALA A 129      10.557 -28.655 -22.874  1.00 20.23           O  
ANISOU 1344  O   ALA A 129     3876   1704   2107   -300   -558     38       O  
ATOM   1345  CB  ALA A 129       8.774 -30.229 -20.580  1.00 15.27           C  
ANISOU 1345  CB  ALA A 129     2169   2008   1625    129   -327    -82       C  
ATOM   1346  N   SER A 130       9.514 -30.503 -23.578  1.00 12.74           N  
ANISOU 1346  N   SER A 130     1886   1773   1183     96    124   -197       N  
ATOM   1347  CA  SER A 130       9.443 -30.123 -24.978  1.00 13.52           C  
ANISOU 1347  CA  SER A 130     1682   1997   1459    187     12   -458       C  
ATOM   1348  C   SER A 130       8.052 -29.611 -25.368  1.00 12.45           C  
ANISOU 1348  C   SER A 130     1750   1755   1226     11    191   -370       C  
ATOM   1349  O   SER A 130       7.028 -30.055 -24.836  1.00 12.92           O  
ANISOU 1349  O   SER A 130     1764   1812   1334    278     85   -318       O  
ATOM   1350  CB  SER A 130       9.773 -31.342 -25.853  1.00 15.56           C  
ANISOU 1350  CB  SER A 130     1770   2358   1782    592     33   -779       C  
ATOM   1351  OG  SER A 130      11.088 -31.838 -25.610  1.00 18.68           O  
ANISOU 1351  OG  SER A 130     2206   2798   2094    664     84   -697       O  
ATOM   1352  N   ALA A 132       8.017 -28.753 -26.386  1.00 12.83           N  
ANISOU 1352  N   ALA A 132     1908   1467   1500     43    -20   -386       N  
ATOM   1353  CA  ALA A 132       6.742 -28.377 -26.974  1.00 12.64           C  
ANISOU 1353  CA  ALA A 132     1928   1346   1529     74     85   -268       C  
ATOM   1354  C   ALA A 132       5.955 -29.628 -27.352  1.00 11.45           C  
ANISOU 1354  C   ALA A 132     1836   1263   1253    139    226   -250       C  
ATOM   1355  O   ALA A 132       6.515 -30.612 -27.853  1.00 12.38           O  
ANISOU 1355  O   ALA A 132     1828   1407   1468     58    233   -307       O  
ATOM   1356  CB  ALA A 132       6.984 -27.518 -28.218  1.00 15.76           C  
ANISOU 1356  CB  ALA A 132     2416   1557   2014    -77     77     -6       C  
ATOM   1357  N   GLY A 133       4.636 -29.581 -27.105  1.00 11.84           N  
ANISOU 1357  N   GLY A 133     1709   1612   1178    109     53   -224       N  
ATOM   1358  CA  GLY A 133       3.730 -30.677 -27.333  1.00 12.77           C  
ANISOU 1358  CA  GLY A 133     1708   1986   1158    -57    -86   -275       C  
ATOM   1359  C   GLY A 133       3.425 -31.495 -26.096  1.00 12.89           C  
ANISOU 1359  C   GLY A 133     1891   1863   1144    -75    105   -407       C  
ATOM   1360  O   GLY A 133       2.402 -32.196 -26.064  1.00 15.34           O  
ANISOU 1360  O   GLY A 133     2232   2088   1508   -362    -54   -312       O  
ATOM   1361  HA2 GLY A 133       2.898 -30.347 -27.707  1.00 15.32           H  
ATOM   1362  N   THR A 134       4.274 -31.410 -25.072  1.00 12.95           N  
ANISOU 1362  N   THR A 134     2132   1561   1226    256    305   -205       N  
ATOM   1363  CA  THR A 134       4.013 -32.129 -23.832  1.00 13.11           C  
ANISOU 1363  CA  THR A 134     2069   1633   1278    419    307    -77       C  
ATOM   1364  C   THR A 134       2.787 -31.544 -23.151  1.00 11.50           C  
ANISOU 1364  C   THR A 134     1974   1225   1171     -2     77   -227       C  
ATOM   1365  O   THR A 134       2.641 -30.320 -23.052  1.00 11.62           O  
ANISOU 1365  O   THR A 134     1772   1210   1432    -33    139   -243       O  
ATOM   1366  CB  THR A 134       5.226 -32.012 -22.901  1.00 17.47           C  
ANISOU 1366  CB  THR A 134     2037   3095   1506    661    447    352       C  
ATOM   1367  OG1 THR A 134       6.355 -32.603 -23.539  1.00 23.03           O  
ANISOU 1367  OG1 THR A 134     2327   4388   2036   1227    748    583       O  
ATOM   1368  CG2 THR A 134       4.998 -32.746 -21.567  1.00 18.05           C  
ANISOU 1368  CG2 THR A 134     2216   3162   1479    728    236    287       C  
ATOM   1369  N   GLN A 135       1.915 -32.429 -22.652  1.00 12.86           N  
ANISOU 1369  N   GLN A 135     2146   1437   1305   -220    452   -386       N  
ATOM   1370  CA  GLN A 135       0.744 -31.999 -21.915  1.00 12.42           C  
ANISOU 1370  CA  GLN A 135     1877   1554   1289   -332    167   -368       C  
ATOM   1371  C   GLN A 135       1.070 -31.754 -20.456  1.00 11.60           C  
ANISOU 1371  C   GLN A 135     1714   1370   1323    243     93    -48       C  
ATOM   1372  O   GLN A 135       1.797 -32.533 -19.817  1.00 14.09           O  
ANISOU 1372  O   GLN A 135     2241   1591   1519    442    308    -72       O  
ATOM   1373  CB  GLN A 135      -0.352 -33.048 -21.991  1.00 18.66           C  
ANISOU 1373  CB  GLN A 135     2324   2575   2190  -1073    -65   -518       C  
ATOM   1374  CG  GLN A 135      -1.651 -32.580 -21.341  1.00 28.99           C  
ANISOU 1374  CG  GLN A 135     3350   4165   3500  -1030    198   -529       C  
ATOM   1375  CD  GLN A 135      -2.665 -33.701 -21.163  1.00 37.21           C  
ANISOU 1375  CD  GLN A 135     3948   5769   4422   -638     70   -813       C  
ATOM   1376  OE1 GLN A 135      -3.427 -34.020 -22.078  1.00 43.53           O  
ANISOU 1376  OE1 GLN A 135     4689   7142   4708   -434   -653  -1118       O  
ATOM   1377  NE2 GLN A 135      -2.682 -34.299 -19.973  1.00 34.81           N  
ANISOU 1377  NE2 GLN A 135     3242   5402   4583   -651    657   -625       N  
ATOM   1378  N   CYS A 136       0.454 -30.714 -19.922  1.00 10.48           N  
ANISOU 1378  N   CYS A 136     1709   1208   1067    229     93   -103       N  
ATOM   1379  CA  CYS A 136       0.696 -30.337 -18.550  1.00 10.07           C  
ANISOU 1379  CA  CYS A 136     1427   1251   1150    262     38    -54       C  
ATOM   1380  C   CYS A 136      -0.622 -29.999 -17.857  1.00  8.95           C  
ANISOU 1380  C   CYS A 136     1353   1069    979     94    -10    -29       C  
ATOM   1381  O   CYS A 136      -1.642 -29.733 -18.493  1.00 11.10           O  
ANISOU 1381  O   CYS A 136     1331   1784   1101    284     79     12       O  
ATOM   1382  CB  CYS A 136       1.640 -29.129 -18.498  1.00 10.90           C  
ANISOU 1382  CB  CYS A 136     1447   1476   1217    111     69     90       C  
ATOM   1383  SG  CYS A 136       3.196 -29.321 -19.409  1.00 13.12           S  
ANISOU 1383  SG  CYS A 136     1392   2200   1392    259    194    293       S  
ATOM   1384  H   CYS A 136      -0.108 -30.211 -20.336  1.00 12.58           H  
ATOM   1385  HB2 CYS A 136       1.178 -28.362 -18.870  1.00 13.08           H  
ATOM   1386  HB3 CYS A 136       1.865 -28.954 -17.571  1.00 13.08           H  
ATOM   1387  N   LEU A 137      -0.557 -29.958 -16.535  1.00  7.93           N  
ANISOU 1387  N   LEU A 137     1163    792   1057     83     14   -238       N  
ATOM   1388  CA  LEU A 137      -1.671 -29.596 -15.665  1.00  7.71           C  
ANISOU 1388  CA  LEU A 137     1110    777   1044    -15    -98   -182       C  
ATOM   1389  C   LEU A 137      -1.330 -28.278 -14.974  1.00  7.67           C  
ANISOU 1389  C   LEU A 137     1024    874   1017     86     54    -59       C  
ATOM   1390  O   LEU A 137      -0.323 -28.186 -14.249  1.00  7.92           O  
ANISOU 1390  O   LEU A 137     1022    866   1122     76   -108   -169       O  
ATOM   1391  CB  LEU A 137      -1.929 -30.666 -14.620  1.00  8.29           C  
ANISOU 1391  CB  LEU A 137     1202    803   1144      8    -74   -178       C  
ATOM   1392  CG  LEU A 137      -3.153 -30.413 -13.734  1.00  8.94           C  
ANISOU 1392  CG  LEU A 137     1320    863   1215   -233    -19   -120       C  
ATOM   1393  CD1 LEU A 137      -4.453 -30.559 -14.522  1.00 10.67           C  
ANISOU 1393  CD1 LEU A 137     1305   1241   1509   -259   -196    -11       C  
ATOM   1394  CD2 LEU A 137      -3.170 -31.360 -12.547  1.00 10.66           C  
ANISOU 1394  CD2 LEU A 137     1531   1320   1198   -337    -28    -17       C  
ATOM   1395  HA  LEU A 137      -2.475 -29.473 -16.193  1.00  9.26           H  
ATOM   1396  HB2 LEU A 137      -2.064 -31.514 -15.072  1.00  9.95           H  
ATOM   1397  HB3 LEU A 137      -1.154 -30.726 -14.040  1.00  9.95           H  
ATOM   1398  HG  LEU A 137      -3.112 -29.506 -13.392  1.00 10.73           H  
ATOM   1399 HD21 LEU A 137      -3.945 -31.163 -11.997  1.00 12.79           H  
ATOM   1400 HD22 LEU A 137      -3.217 -32.272 -12.871  1.00 12.79           H  
ATOM   1401  N   ILE A 138      -2.169 -27.272 -15.190  1.00  7.36           N  
ANISOU 1401  N   ILE A 138      986    825    984      9    -79   -172       N  
ATOM   1402  CA  ILE A 138      -2.023 -25.932 -14.617  1.00  7.43           C  
ANISOU 1402  CA  ILE A 138     1034    796    993     35    -96   -173       C  
ATOM   1403  C   ILE A 138      -3.194 -25.741 -13.666  1.00  7.49           C  
ANISOU 1403  C   ILE A 138     1089    800    955     31    -79   -184       C  
ATOM   1404  O   ILE A 138      -4.325 -26.115 -13.994  1.00  8.80           O  
ANISOU 1404  O   ILE A 138      951   1275   1118   -119    -27   -378       O  
ATOM   1405  CB  ILE A 138      -2.045 -24.869 -15.735  1.00  7.83           C  
ANISOU 1405  CB  ILE A 138     1122    770   1085    -18    -20    -61       C  
ATOM   1406  CG1 ILE A 138      -1.057 -25.239 -16.841  1.00  9.74           C  
ANISOU 1406  CG1 ILE A 138     1439   1143   1117   -164    157   -135       C  
ATOM   1407  CG2 ILE A 138      -1.768 -23.489 -15.152  1.00  9.06           C  
ANISOU 1407  CG2 ILE A 138     1279    902   1260    -22      6    -90       C  
ATOM   1408  CD1 ILE A 138      -1.034 -24.286 -17.987  1.00 12.90           C  
ANISOU 1408  CD1 ILE A 138     2230   1315   1355    -52    529   -115       C  
ATOM   1409  H   ILE A 138      -2.865 -27.344 -15.690  1.00  8.83           H  
ATOM   1410  HA  ILE A 138      -1.191 -25.864 -14.123  1.00  8.92           H  
ATOM   1411  HB  ILE A 138      -2.935 -24.858 -16.120  1.00  9.40           H  
ATOM   1412 HG12 ILE A 138      -0.164 -25.267 -16.464  1.00 11.68           H  
ATOM   1413 HG13 ILE A 138      -1.293 -26.113 -17.190  1.00 11.68           H  
ATOM   1414 HG21 ILE A 138      -1.786 -22.835 -15.868  1.00 10.87           H  
ATOM   1415 HG22 ILE A 138      -2.451 -23.280 -14.496  1.00 10.87           H  
ATOM   1416 HG23 ILE A 138      -0.894 -23.494 -14.730  1.00 10.87           H  
ATOM   1417  N   SER A 139      -2.951 -25.190 -12.481  1.00  7.31           N  
ANISOU 1417  N   SER A 139      982    784   1013     39      0   -152       N  
ATOM   1418  CA  SER A 139      -4.012 -25.123 -11.474  1.00  7.21           C  
ANISOU 1418  CA  SER A 139      947    807    986     -4    -47   -160       C  
ATOM   1419  C   SER A 139      -3.926 -23.835 -10.673  1.00  6.75           C  
ANISOU 1419  C   SER A 139      866    750    948    -31    -93   -107       C  
ATOM   1420  O   SER A 139      -2.861 -23.226 -10.550  1.00  7.25           O  
ANISOU 1420  O   SER A 139      906    794   1055    -35    -16   -181       O  
ATOM   1421  CB  SER A 139      -3.983 -26.367 -10.577  1.00  7.64           C  
ANISOU 1421  CB  SER A 139      994    813   1095   -109    -24   -195       C  
ATOM   1422  OG  SER A 139      -2.674 -26.657 -10.097  1.00  8.03           O  
ANISOU 1422  OG  SER A 139     1099    823   1127     49    -67    -86       O  
ATOM   1423  HA  SER A 139      -4.867 -25.120 -11.933  1.00  8.65           H  
ATOM   1424  HB2 SER A 139      -4.566 -26.217  -9.817  1.00  9.17           H  
ATOM   1425  HB3 SER A 139      -4.301 -27.128 -11.088  1.00  9.17           H  
ATOM   1426  N   GLY A 140      -5.062 -23.443 -10.093  1.00  7.04           N  
ANISOU 1426  N   GLY A 140      987    731    958     33      2   -134       N  
ATOM   1427  CA  GLY A 140      -5.083 -22.276  -9.233  1.00  7.05           C  
ANISOU 1427  CA  GLY A 140      884    802    991     11    -33   -178       C  
ATOM   1428  C   GLY A 140      -6.486 -21.807  -8.902  1.00  6.93           C  
ANISOU 1428  C   GLY A 140      896    703   1032    -55    -53    -88       C  
ATOM   1429  O   GLY A 140      -7.503 -22.310  -9.400  1.00  7.37           O  
ANISOU 1429  O   GLY A 140      924    807   1068    -17    -29   -104       O  
ATOM   1430  HA2 GLY A 140      -4.610 -22.465  -8.407  1.00  8.46           H  
ATOM   1431  N   TRP A 141      -6.505 -20.767  -8.062  1.00  6.87           N  
ANISOU 1431  N   TRP A 141      831    779    999    -24    -11   -100       N  
ATOM   1432  CA  TRP A 141      -7.708 -20.107  -7.560  1.00  7.49           C  
ANISOU 1432  CA  TRP A 141      856    838   1151      4      3   -151       C  
ATOM   1433  C   TRP A 141      -7.916 -18.738  -8.210  1.00  8.20           C  
ANISOU 1433  C   TRP A 141      903    856   1356    154    -68   -191       C  
ATOM   1434  O   TRP A 141      -8.642 -17.890  -7.685  1.00  9.69           O  
ANISOU 1434  O   TRP A 141     1275   1075   1332    237    -91   -241       O  
ATOM   1435  CB  TRP A 141      -7.670 -19.965  -6.030  1.00  7.75           C  
ANISOU 1435  CB  TRP A 141     1026    804   1113    -63    112   -133       C  
ATOM   1436  CG  TRP A 141      -7.805 -21.240  -5.280  1.00  7.68           C  
ANISOU 1436  CG  TRP A 141     1026    778   1113    -43    120   -214       C  
ATOM   1437  CD1 TRP A 141      -8.974 -21.833  -4.928  1.00  8.01           C  
ANISOU 1437  CD1 TRP A 141     1048    963   1032   -122    107    -72       C  
ATOM   1438  CD2 TRP A 141      -6.765 -22.064  -4.738  1.00  7.74           C  
ANISOU 1438  CD2 TRP A 141      964    892   1086   -126    188   -211       C  
ATOM   1439  NE1 TRP A 141      -8.738 -22.980  -4.212  1.00  8.40           N  
ANISOU 1439  NE1 TRP A 141     1010   1047   1135   -226    125   -116       N  
ATOM   1440  CE2 TRP A 141      -7.383 -23.135  -4.073  1.00  7.99           C  
ANISOU 1440  CE2 TRP A 141     1136    891   1009   -135    103   -231       C  
ATOM   1441  CE3 TRP A 141      -5.369 -21.979  -4.715  1.00  7.85           C  
ANISOU 1441  CE3 TRP A 141     1058    856   1070    -86    155   -197       C  
ATOM   1442  CZ2 TRP A 141      -6.656 -24.112  -3.393  1.00  8.42           C  
ANISOU 1442  CZ2 TRP A 141     1262    917   1022    -63    128   -101       C  
ATOM   1443  CZ3 TRP A 141      -4.650 -22.944  -4.044  1.00  8.42           C  
ANISOU 1443  CZ3 TRP A 141     1138    993   1069     56     69   -163       C  
ATOM   1444  CH2 TRP A 141      -5.289 -24.010  -3.382  1.00  8.66           C  
ANISOU 1444  CH2 TRP A 141     1237    999   1053     52    115   -148       C  
ATOM   1445  H   TRP A 141      -5.786 -20.410  -7.753  1.00  8.24           H  
ATOM   1446  HA  TRP A 141      -8.476 -20.656  -7.783  1.00  8.98           H  
ATOM   1447  HB2 TRP A 141      -6.830 -19.553  -5.773  1.00  9.30           H  
ATOM   1448  HD1 TRP A 141      -9.817 -21.522  -5.168  1.00  9.61           H  
ATOM   1449  HE1 TRP A 141      -9.339 -23.509  -3.898  1.00 10.08           H  
ATOM   1450  HE3 TRP A 141      -4.934 -21.266  -5.124  1.00  9.43           H  
ATOM   1451  HZ2 TRP A 141      -7.086 -24.821  -2.972  1.00 10.11           H  
ATOM   1452  HZ3 TRP A 141      -3.721 -22.898  -4.041  1.00 10.11           H  
ATOM   1453  N   GLY A 142      -7.312 -18.498  -9.370  1.00  8.33           N  
ANISOU 1453  N   GLY A 142     1029    857   1278     68    -14    -29       N  
ATOM   1454  CA  GLY A 142      -7.453 -17.236 -10.051  1.00  9.54           C  
ANISOU 1454  CA  GLY A 142     1150    977   1498    -36   -241     58       C  
ATOM   1455  C   GLY A 142      -8.780 -17.060 -10.769  1.00  8.44           C  
ANISOU 1455  C   GLY A 142     1096    818   1293     72    -45   -112       C  
ATOM   1456  O   GLY A 142      -9.649 -17.932 -10.797  1.00  8.85           O  
ANISOU 1456  O   GLY A 142     1105    945   1313     32    -95    -55       O  
ATOM   1457  H   GLY A 142      -6.810 -19.063  -9.780  1.00  9.99           H  
ATOM   1458  N   ASN A 143      -8.927 -15.876 -11.361  1.00  9.37           N  
ANISOU 1458  N   ASN A 143     1159    823   1579     86   -148     15       N  
ATOM   1459  CA  ASN A 143     -10.130 -15.479 -12.078  1.00  9.87           C  
ANISOU 1459  CA  ASN A 143     1280    948   1521    221   -215    -52       C  
ATOM   1460  C   ASN A 143     -10.472 -16.530 -13.130  1.00  9.44           C  
ANISOU 1460  C   ASN A 143     1119   1005   1463    165    -86     -1       C  
ATOM   1461  O   ASN A 143      -9.593 -17.066 -13.823  1.00  9.70           O  
ANISOU 1461  O   ASN A 143     1219   1099   1366    188      2     20       O  
ATOM   1462  CB  ASN A 143      -9.824 -14.111 -12.726  1.00 11.29           C  
ANISOU 1462  CB  ASN A 143     1494    955   1841    262   -277     80       C  
ATOM   1463  CG  ASN A 143     -11.036 -13.383 -13.290  1.00 11.97           C  
ANISOU 1463  CG  ASN A 143     1745   1037   1766    218   -200    -63       C  
ATOM   1464  OD1 ASN A 143     -12.156 -13.870 -13.276  1.00 11.77           O  
ANISOU 1464  OD1 ASN A 143     1575   1106   1790    234   -222     -6       O  
ATOM   1465  ND2 ASN A 143     -10.779 -12.203 -13.860  1.00 15.01           N  
ANISOU 1465  ND2 ASN A 143     2034   1313   2355    141   -253    298       N  
ATOM   1466  H   ASN A 143      -8.321 -15.266 -11.357  1.00 11.25           H  
ATOM   1467  N   THR A 144     -11.772 -16.809 -13.238  1.00 10.05           N  
ANISOU 1467  N   THR A 144     1177   1258   1382    176   -189   -182       N  
ATOM   1468  CA  THR A 144     -12.272 -17.749 -14.232  1.00  9.85           C  
ANISOU 1468  CA  THR A 144     1291   1200   1251    123    -97      5       C  
ATOM   1469  C   THR A 144     -12.893 -17.045 -15.437  1.00 10.62           C  
ANISOU 1469  C   THR A 144     1325   1297   1413    238    -67    -41       C  
ATOM   1470  O   THR A 144     -13.372 -17.731 -16.354  1.00 11.85           O  
ANISOU 1470  O   THR A 144     1626   1483   1394     99   -173    -46       O  
ATOM   1471  CB  THR A 144     -13.297 -18.701 -13.610  1.00 10.57           C  
ANISOU 1471  CB  THR A 144     1319   1485   1214     98    -33    -94       C  
ATOM   1472  OG1 THR A 144     -14.415 -17.932 -13.138  1.00 12.19           O  
ANISOU 1472  OG1 THR A 144     1210   1895   1525     77    -10   -148       O  
ATOM   1473  CG2 THR A 144     -12.681 -19.544 -12.476  1.00 11.52           C  
ANISOU 1473  CG2 THR A 144     1474   1480   1424     44    -69     95       C  
ATOM   1474  N   LYS A 145     -12.851 -15.703 -15.505  1.00 12.28           N  
ANISOU 1474  N   LYS A 145     1535   1354   1775    373   -348    135       N  
ATOM   1475  CA  LYS A 145     -13.394 -14.955 -16.650  1.00 13.59           C  
ANISOU 1475  CA  LYS A 145     1535   1597   2030    279   -210    211       C  
ATOM   1476  C   LYS A 145     -12.300 -14.186 -17.391  1.00 13.32           C  
ANISOU 1476  C   LYS A 145     1666   1699   1696    219     15    195       C  
ATOM   1477  O   LYS A 145     -11.412 -13.587 -16.775  1.00 15.74           O  
ANISOU 1477  O   LYS A 145     1762   2160   2060     14    -12    157       O  
ATOM   1478  CB  LYS A 145     -14.475 -13.986 -16.195  1.00 17.40           C  
ANISOU 1478  CB  LYS A 145     2041   2225   2347    858    366    681       C  
ATOM   1479  CG  LYS A 145     -15.667 -14.729 -15.685  1.00 20.61           C  
ANISOU 1479  CG  LYS A 145     2018   3087   2728    959    461   1116       C  
ATOM   1480  N   SER A 146     -12.390 -14.151 -18.720  1.00 13.60           N  
ANISOU 1480  N   SER A 146     1698   1787   1682    182    -95    363       N  
ATOM   1481  CA  SER A 146     -11.451 -13.350 -19.496  1.00 16.66           C  
ANISOU 1481  CA  SER A 146     2068   2260   2002    427     56    487       C  
ATOM   1482  C   SER A 146     -11.912 -11.914 -19.692  1.00 18.04           C  
ANISOU 1482  C   SER A 146     2059   1884   2910    369   -104    792       C  
ATOM   1483  O   SER A 146     -11.075 -11.023 -19.922  1.00 21.34           O  
ANISOU 1483  O   SER A 146     2111   2105   3892   -178   -290    792       O  
ATOM   1484  CB  SER A 146     -11.116 -14.031 -20.822  1.00 23.18           C  
ANISOU 1484  CB  SER A 146     3372   3310   2125    327    816    379       C  
ATOM   1485  OG  SER A 146     -12.299 -14.411 -21.494  1.00 29.27           O  
ANISOU 1485  OG  SER A 146     4287   4203   2632    559   1014    161       O  
ATOM   1486  N   SER A 147     -13.221 -11.686 -19.608  1.00 19.62           N  
ANISOU 1486  N   SER A 147     2390   2067   2999    939   -219    650       N  
ATOM   1487  CA  SER A 147     -13.816 -10.361 -19.526  1.00 26.93           C  
ANISOU 1487  CA  SER A 147     3419   3277   3538   1237   -490    643       C  
ATOM   1488  C   SER A 147     -14.605 -10.313 -18.225  1.00 29.66           C  
ANISOU 1488  C   SER A 147     3604   3940   3725   1653    117     -7       C  
ATOM   1489  O   SER A 147     -15.520 -11.116 -18.012  1.00 32.42           O  
ANISOU 1489  O   SER A 147     3627   4430   4263   1518    150   -484       O  
ATOM   1490  CB  SER A 147     -14.732 -10.111 -20.723  1.00 32.80           C  
ANISOU 1490  CB  SER A 147     4570   3888   4004   1064  -1395   1177       C  
ATOM   1491  OG  SER A 147     -13.988 -10.149 -21.931  1.00 36.99           O  
ANISOU 1491  OG  SER A 147     5499   4339   4216    708  -1916   1568       O  
ATOM   1492  N   GLY A 148     -14.246  -9.405 -17.356  1.00 30.10           N  
ANISOU 1492  N   GLY A 148     4334   4092   3011   1718    392    736       N  
ATOM   1493  CA  GLY A 148     -14.905  -9.371 -16.076  1.00 27.87           C  
ANISOU 1493  CA  GLY A 148     4421   3566   2602   1839    742   1031       C  
ATOM   1494  C   GLY A 148     -14.195 -10.265 -15.090  1.00 22.99           C  
ANISOU 1494  C   GLY A 148     3854   2521   2360   1533    553    871       C  
ATOM   1495  O   GLY A 148     -13.057 -10.708 -15.305  1.00 21.63           O  
ANISOU 1495  O   GLY A 148     3723   2011   2484   1226    446    787       O  
ATOM   1496  N   THR A 149     -14.888 -10.534 -13.981  1.00 21.53           N  
ANISOU 1496  N   THR A 149     3775   2125   2280   1339    500    741       N  
ATOM   1497  CA  THR A 149     -14.218 -11.058 -12.805  1.00 19.89           C  
ANISOU 1497  CA  THR A 149     3954   1366   2235    780    188    325       C  
ATOM   1498  C   THR A 149     -15.128 -12.005 -12.035  1.00 15.40           C  
ANISOU 1498  C   THR A 149     2596   1475   1781    846    -15    188       C  
ATOM   1499  O   THR A 149     -16.230 -11.635 -11.616  1.00 17.00           O  
ANISOU 1499  O   THR A 149     2446   2014   2000   1103      2    162       O  
ATOM   1500  CB  THR A 149     -13.730  -9.919 -11.894  1.00 26.60           C  
ANISOU 1500  CB  THR A 149     5687   1458   2963   -225    149    163       C  
ATOM   1501  OG1 THR A 149     -12.729  -9.138 -12.574  1.00 32.00           O  
ANISOU 1501  OG1 THR A 149     6774   2116   3270   -667    481    -72       O  
ATOM   1502  CG2 THR A 149     -13.150 -10.483 -10.625  1.00 30.13           C  
ANISOU 1502  CG2 THR A 149     6181   2016   3250   -376     66    -10       C  
ATOM   1503  N   SER A 150     -14.625 -13.212 -11.803  1.00 12.82           N  
ANISOU 1503  N   SER A 150     1897   1341   1633    506    -39    146       N  
ATOM   1504  CA  SER A 150     -15.264 -14.185 -10.925  1.00 12.03           C  
ANISOU 1504  CA  SER A 150     1535   1557   1477    380     96    155       C  
ATOM   1505  C   SER A 150     -14.178 -15.079 -10.346  1.00 10.85           C  
ANISOU 1505  C   SER A 150     1377   1353   1391    352     12     42       C  
ATOM   1506  O   SER A 150     -13.473 -15.759 -11.097  1.00 12.52           O  
ANISOU 1506  O   SER A 150     1665   1727   1366    600    109    -94       O  
ATOM   1507  CB  SER A 150     -16.273 -15.050 -11.640  1.00 15.11           C  
ANISOU 1507  CB  SER A 150     1592   2057   2091    130    -28    451       C  
ATOM   1508  OG  SER A 150     -16.920 -15.906 -10.692  1.00 17.26           O  
ANISOU 1508  OG  SER A 150     1747   2477   2336     49   -280    387       O  
ATOM   1509  N   TYR A 151     -14.040 -15.042  -9.031  1.00 10.74           N  
ANISOU 1509  N   TYR A 151     1468   1293   1321    386     17   -101       N  
ATOM   1510  CA  TYR A 151     -12.999 -15.821  -8.375  1.00 10.67           C  
ANISOU 1510  CA  TYR A 151     1346   1262   1445    400    -93    -86       C  
ATOM   1511  C   TYR A 151     -13.626 -17.030  -7.714  1.00 11.10           C  
ANISOU 1511  C   TYR A 151     1436   1487   1294    577     69   -105       C  
ATOM   1512  O   TYR A 151     -14.583 -16.863  -6.955  1.00 13.04           O  
ANISOU 1512  O   TYR A 151     1733   1724   1498    736    362    224       O  
ATOM   1513  CB  TYR A 151     -12.255 -14.953  -7.350  1.00 14.13           C  
ANISOU 1513  CB  TYR A 151     1843   1758   1769    363   -119   -643       C  
ATOM   1514  CG  TYR A 151     -11.300 -13.990  -8.038  1.00 16.62           C  
ANISOU 1514  CG  TYR A 151     2029   1978   2307    152    407  -1103       C  
ATOM   1515  CD1 TYR A 151     -11.741 -12.763  -8.526  1.00 20.07           C  
ANISOU 1515  CD1 TYR A 151     2775   2339   2511   -122    788  -1013       C  
ATOM   1516  CD2 TYR A 151      -9.973 -14.340  -8.257  1.00 19.78           C  
ANISOU 1516  CD2 TYR A 151     2322   2075   3118     19    687  -1097       C  
ATOM   1517  CE1 TYR A 151     -10.853 -11.900  -9.178  1.00 23.36           C  
ANISOU 1517  CE1 TYR A 151     3037   2723   3116   -788   1194   -978       C  
ATOM   1518  CE2 TYR A 151      -9.098 -13.487  -8.893  1.00 23.08           C  
ANISOU 1518  CE2 TYR A 151     2872   2334   3562   -673   1122  -1251       C  
ATOM   1519  CZ  TYR A 151      -9.541 -12.276  -9.360  1.00 25.17           C  
ANISOU 1519  CZ  TYR A 151     3283   2721   3559  -1296   1446  -1504       C  
ATOM   1520  OH  TYR A 151      -8.640 -11.438 -10.004  1.00 30.68           O  
ANISOU 1520  OH  TYR A 151     4080   3479   4097  -1781   1870  -1674       O  
ATOM   1521  HB2 TYR A 151     -12.901 -14.429  -6.851  1.00 16.96           H  
ATOM   1522  N  APRO A 152     -13.072 -18.193  -7.991  0.70  9.84           N  
ANISOU 1522  N  APRO A 152     1196   1231   1311    381     65    -86       N  
ATOM   1523  N  BPRO A 152     -13.143 -18.312  -7.922  0.30 10.86           N  
ANISOU 1523  N  BPRO A 152     1530   1672    923    381    115    148       N  
ATOM   1524  CA APRO A 152     -13.611 -19.425  -7.439  0.70  9.73           C  
ANISOU 1524  CA APRO A 152     1020   1303   1375    159     48    -49       C  
ATOM   1525  CA BPRO A 152     -13.995 -19.528  -7.721  0.30 11.22           C  
ANISOU 1525  CA BPRO A 152     1641   1670    954    346     95    453       C  
ATOM   1526  C  APRO A 152     -13.186 -19.620  -6.002  0.70  8.07           C  
ANISOU 1526  C  APRO A 152      693   1163   1210   -132   -225   -155       C  
ATOM   1527  C  BPRO A 152     -14.065 -20.249  -6.361  0.30  9.89           C  
ANISOU 1527  C  BPRO A 152     1173   1509   1075    267    108    280       C  
ATOM   1528  O  APRO A 152     -12.184 -19.091  -5.534  0.70 10.45           O  
ANISOU 1528  O  APRO A 152     1234   1237   1498   -186    -71     90       O  
ATOM   1529  O  BPRO A 152     -14.919 -21.130  -6.143  0.30 11.39           O  
ANISOU 1529  O  BPRO A 152     1085   1936   1306    437    123    601       O  
ATOM   1530  CB APRO A 152     -12.988 -20.491  -8.347  0.70  9.66           C  
ANISOU 1530  CB APRO A 152     1303   1155   1212    183     69    133       C  
ATOM   1531  CB BPRO A 152     -13.405 -20.507  -8.743  0.30 11.05           C  
ANISOU 1531  CB BPRO A 152     1559   1571   1070    176    -44    318       C  
ATOM   1532  CG APRO A 152     -11.640 -19.927  -8.628  0.70  9.88           C  
ANISOU 1532  CG APRO A 152     1185   1012   1556    247    144   -154       C  
ATOM   1533  CG BPRO A 152     -11.950 -20.130  -8.794  0.30 11.06           C  
ANISOU 1533  CG BPRO A 152     1683   1614    907     98   -184     56       C  
ATOM   1534  CD APRO A 152     -11.924 -18.457  -8.885  0.70  9.29           C  
ANISOU 1534  CD APRO A 152     1003   1057   1470    221    226   -245       C  
ATOM   1535  CD BPRO A 152     -11.918 -18.619  -8.686  0.30 10.85           C  
ANISOU 1535  CD BPRO A 152     1695   1641    784    277    -41    -49       C  
ATOM   1536  N  AASP A 153     -13.975 -20.414  -5.313  0.70  8.91           N  
ANISOU 1536  N  AASP A 153      879   1333   1175     40    -96   -169       N  
ATOM   1537  N  BASP A 153     -13.134 -19.943  -5.469  0.30  9.78           N  
ANISOU 1537  N  BASP A 153     1382   1339    994    601    -69    196       N  
ATOM   1538  CA AASP A 153     -13.598 -20.836  -3.975  0.70  9.97           C  
ANISOU 1538  CA AASP A 153     1031   1708   1049    287     67   -336       C  
ATOM   1539  CA BASP A 153     -13.048 -20.594  -4.160  0.30  8.78           C  
ANISOU 1539  CA BASP A 153     1179    999   1158    561    186    176       C  
ATOM   1540  C  AASP A 153     -12.794 -22.113  -3.993  0.70  8.89           C  
ANISOU 1540  C  AASP A 153     1047   1384    945    -49     85   -126       C  
ATOM   1541  C  BASP A 153     -12.509 -22.031  -4.148  0.30  8.83           C  
ANISOU 1541  C  BASP A 153     1138   1101   1114    221    177    132       C  
ATOM   1542  O  AASP A 153     -11.938 -22.307  -3.130  0.70  8.92           O  
ANISOU 1542  O  AASP A 153     1142   1306    941     79   -100    -62       O  
ATOM   1543  O  BASP A 153     -11.590 -22.300  -3.369  0.30  8.84           O  
ANISOU 1543  O  BASP A 153     1015   1222   1123    137    302    198       O  
ATOM   1544  CB AASP A 153     -14.850 -21.028  -3.127  0.70 13.06           C  
ANISOU 1544  CB AASP A 153     1368   2498   1096    382     95   -156       C  
ATOM   1545  CB BASP A 153     -14.346 -20.454  -3.364  0.30 10.84           C  
ANISOU 1545  CB BASP A 153     1550    789   1782    256     -6   -150       C  
ATOM   1546  CG AASP A 153     -15.609 -19.737  -2.936  0.70 16.19           C  
ANISOU 1546  CG AASP A 153     1266   3527   1360    432   -358   -615       C  
ATOM   1547  CG BASP A 153     -14.708 -19.001  -3.092  0.30 13.97           C  
ANISOU 1547  CG BASP A 153     1863    933   2510    233   -276   -162       C  
ATOM   1548  OD1AASP A 153     -16.832 -19.746  -3.134  0.70 19.81           O  
ANISOU 1548  OD1AASP A 153     1325   4486   1718    568   -107   -880       O  
ATOM   1549  OD1BASP A 153     -13.886 -18.114  -3.381  0.30 14.29           O  
ANISOU 1549  OD1BASP A 153     1824    969   2635     34   -741   -132       O  
ATOM   1550  OD2AASP A 153     -15.011 -18.710  -2.539  0.70 18.50           O  
ANISOU 1550  OD2AASP A 153     1708   3506   1814    538   -574  -1119       O  
ATOM   1551  OD2BASP A 153     -15.811 -18.747  -2.582  0.30 16.45           O  
ANISOU 1551  OD2BASP A 153     2076   1205   2969    133     68    -27       O  
ATOM   1552  N   VAL A 154     -13.059 -22.996  -4.939  1.00  9.47           N  
ANISOU 1552  N   VAL A 154     1010   1439   1150    186    -48   -103       N  
ATOM   1553  CA  VAL A 154     -12.406 -24.293  -5.050  1.00  9.07           C  
ANISOU 1553  CA  VAL A 154      983   1388   1073     -6      2    -60       C  
ATOM   1554  C   VAL A 154     -11.355 -24.271  -6.162  1.00  7.98           C  
ANISOU 1554  C   VAL A 154      948    951   1132    -92    -48    -61       C  
ATOM   1555  O   VAL A 154     -11.371 -23.410  -7.045  1.00  8.91           O  
ANISOU 1555  O   VAL A 154     1087   1101   1198     10     58     12       O  
ATOM   1556  CB  VAL A 154     -13.408 -25.457  -5.248  1.00 10.64           C  
ANISOU 1556  CB  VAL A 154     1152   1715   1176   -400    109   -151       C  
ATOM   1557  CG1 VAL A 154     -14.401 -25.500  -4.095  1.00 12.28           C  
ANISOU 1557  CG1 VAL A 154     1322   1975   1368   -300    211   -147       C  
ATOM   1558  CG2 VAL A 154     -14.128 -25.346  -6.600  1.00 12.71           C  
ANISOU 1558  CG2 VAL A 154     1400   2145   1283   -479   -106   -104       C  
ATOM   1559  H  AVAL A 154     -13.639 -22.860  -5.559  1.00 11.37           H  
ATOM   1560  H  BVAL A 154     -13.781 -22.911  -5.398  0.00 11.37           H  
ATOM   1561  N   LEU A 155     -10.423 -25.223  -6.092  1.00  7.94           N  
ANISOU 1561  N   LEU A 155     1046    914   1057    -76    -19   -141       N  
ATOM   1562  CA  LEU A 155      -9.284 -25.228  -7.010  1.00  7.66           C  
ANISOU 1562  CA  LEU A 155      896    900   1113   -106     50    -86       C  
ATOM   1563  C   LEU A 155      -9.735 -25.617  -8.419  1.00  7.24           C  
ANISOU 1563  C   LEU A 155      908    812   1029    -89    -54   -106       C  
ATOM   1564  O   LEU A 155     -10.470 -26.585  -8.605  1.00  8.13           O  
ANISOU 1564  O   LEU A 155     1063    941   1083   -239    -51   -104       O  
ATOM   1565  CB  LEU A 155      -8.220 -26.194  -6.496  1.00  7.76           C  
ANISOU 1565  CB  LEU A 155     1036    842   1070   -144    -52    -92       C  
ATOM   1566  CG  LEU A 155      -6.892 -26.170  -7.242  1.00  7.88           C  
ANISOU 1566  CG  LEU A 155     1086    904   1003      9    -58   -109       C  
ATOM   1567  CD1 LEU A 155      -6.168 -24.849  -7.063  1.00  7.78           C  
ANISOU 1567  CD1 LEU A 155      975    884   1095     13     18   -118       C  
ATOM   1568  CD2 LEU A 155      -5.996 -27.323  -6.796  1.00  8.89           C  
ANISOU 1568  CD2 LEU A 155     1164   1000   1213     70    -42    -43       C  
ATOM   1569  HA  LEU A 155      -8.897 -24.339  -7.047  1.00  9.19           H  
ATOM   1570  HB2 LEU A 155      -8.036 -25.981  -5.568  1.00  9.31           H  
ATOM   1571  HB3 LEU A 155      -8.571 -27.097  -6.557  1.00  9.31           H  
ATOM   1572  HG  LEU A 155      -7.066 -26.283  -8.189  1.00  9.45           H  
ATOM   1573 HD11 LEU A 155      -5.361 -24.855  -7.601  1.00  9.33           H  
ATOM   1574 HD21 LEU A 155      -5.123 -27.222  -7.208  1.00 10.66           H  
ATOM   1575 HD22 LEU A 155      -5.911 -27.301  -5.830  1.00 10.66           H  
ATOM   1576  N  ALYS A 156      -9.263 -24.856  -9.402  0.52  8.05           N  
ANISOU 1576  N  ALYS A 156     1037    962   1062   -153    -14     -1       N  
ATOM   1577  N  BLYS A 156      -9.263 -24.864  -9.405  0.48  6.68           N  
ANISOU 1577  N  BLYS A 156      969    640    930    -85    -46   -237       N  
ATOM   1578  CA ALYS A 156      -9.507 -25.099 -10.820  0.52  8.23           C  
ANISOU 1578  CA ALYS A 156      927   1090   1112   -117    -57    -11       C  
ATOM   1579  CA BLYS A 156      -9.531 -25.117 -10.817  0.48  6.30           C  
ANISOU 1579  CA BLYS A 156      880    593    920    -66    -77   -127       C  
ATOM   1580  C  ALYS A 156      -8.246 -25.639 -11.485  0.52  7.83           C  
ANISOU 1580  C  ALYS A 156      966    931   1076    -44    -74   -216       C  
ATOM   1581  C  BLYS A 156      -8.260 -25.613 -11.499  0.48  6.65           C  
ANISOU 1581  C  BLYS A 156     1027    582    918   -127   -145     56       C  
ATOM   1582  O  ALYS A 156      -7.121 -25.352 -11.067  0.52  8.06           O  
ANISOU 1582  O  ALYS A 156      855   1066   1141    -67     62   -415       O  
ATOM   1583  O  BLYS A 156      -7.140 -25.273 -11.104  0.48  7.17           O  
ANISOU 1583  O  BLYS A 156     1059    737    928   -129   -111    141       O  
ATOM   1584  CB ALYS A 156      -9.963 -23.819 -11.531  0.52  9.97           C  
ANISOU 1584  CB ALYS A 156     1128   1387   1275    -89    -24    -44       C  
ATOM   1585  CB BLYS A 156     -10.092 -23.860 -11.507  0.48  6.11           C  
ANISOU 1585  CB BLYS A 156      836    557    927     11   -144    -54       C  
ATOM   1586  CG ALYS A 156     -11.329 -23.327 -11.101  0.52 10.56           C  
ANISOU 1586  CG ALYS A 156     1260   1377   1376    -73     53     43       C  
ATOM   1587  CG BLYS A 156     -11.312 -23.264 -10.808  0.48  7.30           C  
ANISOU 1587  CG BLYS A 156      942    706   1126    136    -55   -142       C  
ATOM   1588  CD ALYS A 156     -12.474 -24.192 -11.666  0.52 11.48           C  
ANISOU 1588  CD ALYS A 156     1367   1295   1699    147    550   -137       C  
ATOM   1589  CD BLYS A 156     -12.558 -24.176 -10.849  0.48  8.97           C  
ANISOU 1589  CD BLYS A 156      663   1098   1646    124    112   -153       C  
ATOM   1590  CE ALYS A 156     -13.829 -23.775 -11.122  0.52 13.31           C  
ANISOU 1590  CE ALYS A 156     1746   1405   1907    -72    146      8       C  
ATOM   1591  CE BLYS A 156     -13.777 -23.576 -10.197  0.48 13.23           C  
ANISOU 1591  CE BLYS A 156     1200   1430   2399   -230    236   -256       C  
ATOM   1592  NZ ALYS A 156     -14.873 -24.606 -11.759  0.52 12.65           N  
ANISOU 1592  NZ ALYS A 156     1343   1409   2053   -306   -403     99       N  
ATOM   1593  NZ BLYS A 156     -14.929 -24.450 -10.543  0.48 16.36           N  
ANISOU 1593  NZ BLYS A 156     1446   1812   2959   -158    163    -66       N  
ATOM   1594  H  ALYS A 156      -8.776 -24.160  -9.264  0.52  9.66           H  
ATOM   1595  H  BLYS A 156      -8.766 -24.174  -9.276  0.48  8.02           H  
ATOM   1596  HA ALYS A 156     -10.208 -25.763 -10.914  0.52  9.88           H  
ATOM   1597  HA BLYS A 156     -10.198 -25.817 -10.888  0.48  7.56           H  
ATOM   1598  HB2ALYS A 156      -9.322 -23.114 -11.345  0.52 11.97           H  
ATOM   1599  HB2BLYS A 156      -9.400 -23.181 -11.528  0.48  7.33           H  
ATOM   1600  HB3ALYS A 156      -9.997 -23.988 -12.486  0.52 11.97           H  
ATOM   1601  HB3BLYS A 156     -10.353 -24.092 -12.413  0.48  7.33           H  
ATOM   1602  HG2ALYS A 156     -11.383 -23.353 -10.132  0.52 12.67           H  
ATOM   1603  HG2BLYS A 156     -11.093 -23.098  -9.878  0.48  8.76           H  
ATOM   1604  HD2BLYS A 156     -12.779 -24.361 -11.776  0.48 10.76           H  
ATOM   1605  HD3BLYS A 156     -12.354 -25.005 -10.389  0.48 10.76           H  
ATOM   1606  N   CYS A 157      -8.478 -26.396 -12.554  1.00  7.72           N  
ANISOU 1606  N   CYS A 157      970    920   1042    -83    -87   -152       N  
ATOM   1607  CA  CYS A 157      -7.457 -27.109 -13.295  1.00  7.58           C  
ANISOU 1607  CA  CYS A 157     1056    782   1040    -17   -133   -112       C  
ATOM   1608  C   CYS A 157      -7.643 -26.883 -14.792  1.00  7.42           C  
ANISOU 1608  C   CYS A 157     1098    703   1020    -62    -62    -73       C  
ATOM   1609  O   CYS A 157      -8.767 -26.694 -15.283  1.00  8.16           O  
ANISOU 1609  O   CYS A 157     1022    962   1115    -43   -125   -108       O  
ATOM   1610  CB  CYS A 157      -7.586 -28.634 -13.029  1.00  8.72           C  
ANISOU 1610  CB  CYS A 157     1110   1112   1093    -28   -150   -241       C  
ATOM   1611  SG  CYS A 157      -6.748 -29.214 -11.539  1.00  8.91           S  
ANISOU 1611  SG  CYS A 157     1337    951   1096    -28   -114    -62       S  
ATOM   1612  H  ACYS A 157      -9.265 -26.513 -12.881  0.52  9.26           H  
ATOM   1613  H  BCYS A 157      -9.265 -26.532 -12.874  0.48  9.26           H  
ATOM   1614  HA  CYS A 157      -6.573 -26.809 -13.030  1.00  9.09           H  
ATOM   1615  HB2 CYS A 157      -8.526 -28.855 -12.941  1.00 10.47           H  
ATOM   1616  HB3 CYS A 157      -7.208 -29.113 -13.783  1.00 10.47           H  
ATOM   1617  N   LEU A 158      -6.533 -26.977 -15.519  1.00  7.75           N  
ANISOU 1617  N   LEU A 158     1055    978    912   -103   -174    -64       N  
ATOM   1618  CA  LEU A 158      -6.531 -26.881 -16.977  1.00  7.72           C  
ANISOU 1618  CA  LEU A 158     1079    863    991    -16    -87   -107       C  
ATOM   1619  C   LEU A 158      -5.444 -27.788 -17.514  1.00  7.49           C  
ANISOU 1619  C   LEU A 158     1200    729    918    -72   -124    -82       C  
ATOM   1620  O   LEU A 158      -4.288 -27.675 -17.094  1.00  8.22           O  
ANISOU 1620  O   LEU A 158     1190    942    990    -74   -109   -184       O  
ATOM   1621  CB  LEU A 158      -6.266 -25.451 -17.413  1.00  8.48           C  
ANISOU 1621  CB  LEU A 158     1283    834   1104    -39    -90   -130       C  
ATOM   1622  CG  LEU A 158      -6.104 -25.221 -18.919  1.00  9.50           C  
ANISOU 1622  CG  LEU A 158     1557    919   1136    -63    -40     94       C  
ATOM   1623  CD1 LEU A 158      -7.391 -25.536 -19.674  1.00 11.27           C  
ANISOU 1623  CD1 LEU A 158     1769   1255   1256   -109   -359    105       C  
ATOM   1624  CD2 LEU A 158      -5.625 -23.804 -19.180  1.00 11.08           C  
ANISOU 1624  CD2 LEU A 158     1727    983   1501    -82    -22    196       C  
ATOM   1625  H   LEU A 158      -5.751 -27.098 -15.183  1.00  9.30           H  
ATOM   1626  HA  LEU A 158      -7.388 -27.168 -17.331  1.00  9.26           H  
ATOM   1627  HB2 LEU A 158      -7.007 -24.900 -17.116  1.00 10.17           H  
ATOM   1628  HB3 LEU A 158      -5.449 -25.149 -16.986  1.00 10.17           H  
ATOM   1629 HD13 LEU A 158      -8.099 -24.960 -19.345  1.00 13.52           H  
ATOM   1630 HD22 LEU A 158      -6.307 -23.181 -18.884  1.00 13.30           H  
ATOM   1631  N   LYS A 159      -5.791 -28.654 -18.465  1.00  7.98           N  
ANISOU 1631  N   LYS A 159     1132    883   1016    -49    -83   -103       N  
ATOM   1632  CA  LYS A 159      -4.794 -29.417 -19.211  1.00  8.59           C  
ANISOU 1632  CA  LYS A 159     1259    917   1086    -27   -146   -130       C  
ATOM   1633  C   LYS A 159      -4.405 -28.609 -20.448  1.00  8.54           C  
ANISOU 1633  C   LYS A 159     1231   1011   1004     54   -102    -67       C  
ATOM   1634  O   LYS A 159      -5.279 -28.156 -21.198  1.00 10.96           O  
ANISOU 1634  O   LYS A 159     1411   1602   1153      2    -83    107       O  
ATOM   1635  CB  LYS A 159      -5.314 -30.809 -19.564  1.00  9.31           C  
ANISOU 1635  CB  LYS A 159     1411    948   1178    -34   -156   -246       C  
ATOM   1636  CG  LYS A 159      -5.471 -31.683 -18.330  1.00  9.19           C  
ANISOU 1636  CG  LYS A 159     1353    961   1179   -184      9   -120       C  
ATOM   1637  CD  LYS A 159      -5.961 -33.073 -18.677  1.00  9.78           C  
ANISOU 1637  CD  LYS A 159     1313    937   1466    -71   -100    -89       C  
ATOM   1638  CE  LYS A 159      -6.029 -33.945 -17.457  1.00 10.53           C  
ANISOU 1638  CE  LYS A 159     1503    926   1573   -224   -202     56       C  
ATOM   1639  NZ  LYS A 159      -6.387 -35.358 -17.796  1.00 11.28           N  
ANISOU 1639  NZ  LYS A 159     1533   1034   1720    -37   -205    -97       N  
ATOM   1640  H   LYS A 159      -6.603 -28.817 -18.698  1.00  9.57           H  
ATOM   1641  HA  LYS A 159      -4.002 -29.524 -18.661  1.00 10.30           H  
ATOM   1642  HB2 LYS A 159      -6.184 -30.723 -19.984  1.00 11.17           H  
ATOM   1643  HD3 LYS A 159      -5.340 -33.480 -19.302  1.00 11.74           H  
ATOM   1644  N   ALA A 160      -3.109 -28.422 -20.658  1.00  8.89           N  
ANISOU 1644  N   ALA A 160     1275    998   1103    -32    -60     10       N  
ATOM   1645  CA  ALA A 160      -2.646 -27.580 -21.754  1.00 10.20           C  
ANISOU 1645  CA  ALA A 160     1366   1068   1442    -12     31    129       C  
ATOM   1646  C   ALA A 160      -1.293 -28.059 -22.230  1.00  9.33           C  
ANISOU 1646  C   ALA A 160     1251   1045   1249    -24    -41   -159       C  
ATOM   1647  O   ALA A 160      -0.457 -28.462 -21.413  1.00  9.70           O  
ANISOU 1647  O   ALA A 160     1370   1207   1108     80    -22    -74       O  
ATOM   1648  CB  ALA A 160      -2.515 -26.131 -21.276  1.00 12.50           C  
ANISOU 1648  CB  ALA A 160     1781   1077   1893     33    396    143       C  
ATOM   1649  H   ALA A 160      -2.480 -28.768 -20.184  1.00 10.66           H  
ATOM   1650  N   PRO A 161      -1.005 -27.916 -23.524  1.00  9.58           N  
ANISOU 1650  N   PRO A 161     1433   1211    994    -62    -51   -118       N  
ATOM   1651  CA  PRO A 161       0.313 -28.293 -24.042  1.00 10.05           C  
ANISOU 1651  CA  PRO A 161     1418   1297   1103    -86    101   -292       C  
ATOM   1652  C   PRO A 161       1.276 -27.121 -23.995  1.00  9.30           C  
ANISOU 1652  C   PRO A 161     1468   1124    941     26     42   -178       C  
ATOM   1653  O   PRO A 161       0.903 -25.955 -24.140  1.00  9.59           O  
ANISOU 1653  O   PRO A 161     1359   1068   1218     29    -58   -173       O  
ATOM   1654  CB  PRO A 161       0.002 -28.645 -25.503  1.00 11.41           C  
ANISOU 1654  CB  PRO A 161     1747   1343   1247   -271    130   -375       C  
ATOM   1655  CG  PRO A 161      -1.110 -27.700 -25.851  1.00 12.07           C  
ANISOU 1655  CG  PRO A 161     1782   1718   1087   -304    -19   -329       C  
ATOM   1656  CD  PRO A 161      -1.968 -27.606 -24.607  1.00 11.15           C  
ANISOU 1656  CD  PRO A 161     1665   1425   1145   -167   -184      0       C  
ATOM   1657  HB3 PRO A 161      -0.314 -29.561 -25.547  1.00 13.70           H  
ATOM   1658  HD2 PRO A 161      -2.275 -26.691 -24.504  1.00 13.38           H  
ATOM   1659  N   ILE A 162       2.554 -27.470 -23.876  1.00  9.37           N  
ANISOU 1659  N   ILE A 162     1363   1090   1106    156      4   -187       N  
ATOM   1660  CA  ILE A 162       3.628 -26.509 -24.087  1.00  9.40           C  
ANISOU 1660  CA  ILE A 162     1267   1113   1189    -46    106   -313       C  
ATOM   1661  C   ILE A 162       3.651 -26.157 -25.568  1.00  9.87           C  
ANISOU 1661  C   ILE A 162     1398   1202   1150   -102     76   -249       C  
ATOM   1662  O   ILE A 162       3.525 -27.040 -26.429  1.00 11.25           O  
ANISOU 1662  O   ILE A 162     1923   1198   1154   -187    141   -324       O  
ATOM   1663  CB  ILE A 162       4.961 -27.120 -23.622  1.00 10.13           C  
ANISOU 1663  CB  ILE A 162     1291   1321   1235     71      8   -236       C  
ATOM   1664  CG1 ILE A 162       4.901 -27.449 -22.110  1.00 12.00           C  
ANISOU 1664  CG1 ILE A 162     1494   1699   1366    167    -70     36       C  
ATOM   1665  CG2 ILE A 162       6.132 -26.204 -23.930  1.00 11.59           C  
ANISOU 1665  CG2 ILE A 162     1669   1479   1254    -66     68   -140       C  
ATOM   1666  CD1 ILE A 162       6.158 -28.104 -21.593  1.00 14.96           C  
ANISOU 1666  CD1 ILE A 162     2001   2243   1439    424     86    223       C  
ATOM   1667  H   ILE A 162       2.825 -28.261 -23.673  1.00 11.24           H  
ATOM   1668  HA  ILE A 162       3.456 -25.703 -23.575  1.00 11.27           H  
ATOM   1669  HB  ILE A 162       5.095 -27.950 -24.105  1.00 12.15           H  
ATOM   1670  N   LEU A 163       3.810 -24.873 -25.875  1.00  9.92           N  
ANISOU 1670  N   LEU A 163     1511   1142   1115    -18     11   -163       N  
ATOM   1671  CA  LEU A 163       3.904 -24.377 -27.240  1.00 10.66           C  
ANISOU 1671  CA  LEU A 163     1719   1211   1122   -146   -186   -187       C  
ATOM   1672  C   LEU A 163       5.366 -24.238 -27.646  1.00 10.52           C  
ANISOU 1672  C   LEU A 163     1836   1053   1108    -55     74   -160       C  
ATOM   1673  O   LEU A 163       6.256 -24.060 -26.806  1.00 11.66           O  
ANISOU 1673  O   LEU A 163     1770   1455   1204    -53    -33   -105       O  
ATOM   1674  CB  LEU A 163       3.176 -23.039 -27.356  1.00 10.94           C  
ANISOU 1674  CB  LEU A 163     1802   1149   1205     99   -192   -174       C  
ATOM   1675  CG  LEU A 163       1.668 -23.133 -27.057  1.00 12.79           C  
ANISOU 1675  CG  LEU A 163     1869   1566   1425    256   -197   -296       C  
ATOM   1676  CD1 LEU A 163       1.061 -21.760 -26.980  1.00 15.18           C  
ANISOU 1676  CD1 LEU A 163     1694   1775   2301    149   -366   -484       C  
ATOM   1677  CD2 LEU A 163       0.914 -23.951 -28.087  1.00 17.41           C  
ANISOU 1677  CD2 LEU A 163     2109   2063   2443     85    -59   -730       C  
ATOM   1678  HA  LEU A 163       3.480 -25.008 -27.842  1.00 12.80           H  
ATOM   1679  HB3 LEU A 163       3.283 -22.698 -28.257  1.00 13.12           H  
ATOM   1680 HD11 LEU A 163       0.126 -21.841 -26.735  1.00 18.22           H  
ATOM   1681  N   SER A 164       5.607 -24.305 -28.955  1.00 11.23           N  
ANISOU 1681  N   SER A 164     1958   1036   1274    -19    185   -115       N  
ATOM   1682  CA  SER A 164       6.956 -24.130 -29.468  1.00 11.72           C  
ANISOU 1682  CA  SER A 164     1870   1203   1379     25    342   -134       C  
ATOM   1683  C   SER A 164       7.506 -22.764 -29.081  1.00 12.22           C  
ANISOU 1683  C   SER A 164     1934   1460   1251    -18    225    -47       C  
ATOM   1684  O   SER A 164       6.779 -21.771 -28.971  1.00 11.70           O  
ANISOU 1684  O   SER A 164     1853   1265   1330    -17    148   -134       O  
ATOM   1685  CB  SER A 164       6.965 -24.261 -30.992  1.00 14.19           C  
ANISOU 1685  CB  SER A 164     2288   1633   1470   -132    333   -370       C  
ATOM   1686  OG  SER A 164       6.210 -23.220 -31.578  1.00 14.41           O  
ANISOU 1686  OG  SER A 164     2822   1374   1280   -119    200    -99       O  
ATOM   1687  HA  SER A 164       7.535 -24.813 -29.096  1.00 14.06           H  
ATOM   1688  N  AASP A 165       8.833 -22.716 -28.927  0.57 13.83           N  
ANISOU 1688  N  AASP A 165     1979   1437   1840    -29    134    -29       N  
ATOM   1689  N  BASP A 165       8.817 -22.715 -28.866  0.43 13.48           N  
ANISOU 1689  N  BASP A 165     1958   1584   1579     98     44   -136       N  
ATOM   1690  CA AASP A 165       9.529 -21.449 -28.737  0.57 14.09           C  
ANISOU 1690  CA AASP A 165     1852   1530   1970   -220    146   -108       C  
ATOM   1691  CA BASP A 165       9.443 -21.432 -28.597  0.43 13.92           C  
ANISOU 1691  CA BASP A 165     1876   1926   1487    -75   -138   -110       C  
ATOM   1692  C  AASP A 165       9.179 -20.467 -29.845  0.57 14.01           C  
ANISOU 1692  C  AASP A 165     2063   1397   1865    -50    393    -91       C  
ATOM   1693  C  BASP A 165       9.218 -20.463 -29.748  0.43 12.91           C  
ANISOU 1693  C  BASP A 165     1745   1829   1330   -147     63    -84       C  
ATOM   1694  O  AASP A 165       8.885 -19.297 -29.580  0.57 13.96           O  
ANISOU 1694  O  AASP A 165     1996   1347   1963     97    151   -176       O  
ATOM   1695  O  BASP A 165       9.084 -19.259 -29.519  0.43 11.75           O  
ANISOU 1695  O  BASP A 165     1403   1701   1360   -345    134    -74       O  
ATOM   1696  CB AASP A 165      11.038 -21.697 -28.678  0.57 15.99           C  
ANISOU 1696  CB AASP A 165     2160   1759   2158   -283    323   -141       C  
ATOM   1697  CB BASP A 165      10.915 -21.622 -28.242  0.43 17.14           C  
ANISOU 1697  CB BASP A 165     2426   2445   1642    -45   -146    140       C  
ATOM   1698  CG AASP A 165      11.815 -20.469 -28.257  0.57 18.53           C  
ANISOU 1698  CG AASP A 165     2711   2057   2274   -304    939   -325       C  
ATOM   1699  CG BASP A 165      11.094 -22.422 -26.960  0.43 21.92           C  
ANISOU 1699  CG BASP A 165     3287   3137   1903    -84    -24    261       C  
ATOM   1700  OD1AASP A 165      12.790 -20.123 -28.961  0.57 22.02           O  
ANISOU 1700  OD1AASP A 165     3324   2595   2449   -274   1060   -430       O  
ATOM   1701  OD1BASP A 165      10.238 -22.298 -26.051  0.43 22.49           O  
ANISOU 1701  OD1BASP A 165     3514   3150   1881     24   -291    103       O  
ATOM   1702  OD2AASP A 165      11.459 -19.859 -27.223  0.57 18.98           O  
ANISOU 1702  OD2AASP A 165     2786   1971   2456   -493    705   -393       O  
ATOM   1703  OD2BASP A 165      12.083 -23.179 -26.860  0.43 26.24           O  
ANISOU 1703  OD2BASP A 165     3922   3721   2326   -156     72    329       O  
ATOM   1704  H  AASP A 165       9.348 -23.404 -28.930  0.57 16.60           H  
ATOM   1705  H  BASP A 165       9.350 -23.390 -28.871  0.43 16.17           H  
ATOM   1706  N  ASER A 166       9.195 -20.928 -31.103  0.58 13.45           N  
ANISOU 1706  N  ASER A 166     2184   1116   1809     -9    808    -31       N  
ATOM   1707  N  BSER A 166       9.122 -20.970 -30.983  0.42 14.01           N  
ANISOU 1707  N  BSER A 166     2156   1885   1280    124     34   -166       N  
ATOM   1708  CA ASER A 166       8.936 -20.009 -32.207  0.58 14.79           C  
ANISOU 1708  CA ASER A 166     2553   1388   1677     25    908      2       C  
ATOM   1709  CA BSER A 166       8.852 -20.087 -32.115  0.42 14.67           C  
ANISOU 1709  CA BSER A 166     2531   1969   1072    188    248   -105       C  
ATOM   1710  C  ASER A 166       7.534 -19.409 -32.133  0.58 14.35           C  
ANISOU 1710  C  ASER A 166     2467   1364   1620     90    694     54       C  
ATOM   1711  C  BSER A 166       7.458 -19.475 -32.024  0.42 12.56           C  
ANISOU 1711  C  BSER A 166     2447   1659    666    -36    138   -175       C  
ATOM   1712  O  ASER A 166       7.346 -18.222 -32.432  0.58 14.35           O  
ANISOU 1712  O  ASER A 166     2799   1053   1601     61    598    166       O  
ATOM   1713  O  BSER A 166       7.285 -18.263 -32.212  0.42 12.91           O  
ANISOU 1713  O  BSER A 166     2558   1457    889    -33    164    -94       O  
ATOM   1714  CB ASER A 166       9.158 -20.700 -33.551  0.58 17.38           C  
ANISOU 1714  CB ASER A 166     3163   1865   1574    142    887   -279       C  
ATOM   1715  CB BSER A 166       9.022 -20.848 -33.434  0.42 17.56           C  
ANISOU 1715  CB BSER A 166     2917   2487   1269    549    404     30       C  
ATOM   1716  OG ASER A 166       8.284 -21.796 -33.694  0.58 19.00           O  
ANISOU 1716  OG ASER A 166     3595   1809   1813    -14    613   -589       O  
ATOM   1717  OG BSER A 166       8.665 -20.045 -34.548  0.42 20.52           O  
ANISOU 1717  OG BSER A 166     3288   2837   1672    506    316     29       O  
ATOM   1718  HA ASER A 166       9.569 -19.276 -32.149  0.58 17.74           H  
ATOM   1719  HA BSER A 166       9.496 -19.361 -32.105  0.42 17.60           H  
ATOM   1720  N  ASER A 167       6.529 -20.200 -31.748  0.58 13.28           N  
ANISOU 1720  N  ASER A 167     2249   1270   1527     88    441    168       N  
ATOM   1721  N  BSER A 167       6.442 -20.296 -31.741  0.42 11.92           N  
ANISOU 1721  N  BSER A 167     2430   1344    754   -321     -3   -225       N  
ATOM   1722  CA ASER A 167       5.190 -19.623 -31.672  0.58 13.46           C  
ANISOU 1722  CA ASER A 167     2098   1447   1570    -38     68     55       C  
ATOM   1723  CA BSER A 167       5.094 -19.756 -31.586  0.42 12.12           C  
ANISOU 1723  CA BSER A 167     2180   1453    970   -456   -147   -144       C  
ATOM   1724  C  ASER A 167       5.027 -18.731 -30.446  0.58 11.76           C  
ANISOU 1724  C  ASER A 167     1789   1300   1379   -153     49    105       C  
ATOM   1725  C  BSER A 167       5.050 -18.737 -30.456  0.42 10.82           C  
ANISOU 1725  C  BSER A 167     1825   1275   1012   -338   -184    -28       C  
ATOM   1726  O  ASER A 167       4.264 -17.760 -30.488  0.58 12.58           O  
ANISOU 1726  O  ASER A 167     1922   1405   1452    161    203    172       O  
ATOM   1727  O  BSER A 167       4.417 -17.682 -30.573  0.42 11.15           O  
ANISOU 1727  O  BSER A 167     2001   1240    996   -122   -300   -163       O  
ATOM   1728  CB ASER A 167       4.105 -20.697 -31.730  0.58 14.47           C  
ANISOU 1728  CB ASER A 167     2422   1429   1648     16   -131     23       C  
ATOM   1729  CB BSER A 167       4.094 -20.880 -31.311  0.42 13.88           C  
ANISOU 1729  CB BSER A 167     2523   1728   1024   -420   -285   -215       C  
ATOM   1730  OG ASER A 167       4.089 -21.471 -30.557  0.58 15.00           O  
ANISOU 1730  OG ASER A 167     2350   1494   1855     73    -43    -13       O  
ATOM   1731  OG BSER A 167       3.820 -21.614 -32.482  0.42 15.65           O  
ANISOU 1731  OG BSER A 167     2724   1998   1223   -366   -109   -332       O  
ATOM   1732  H  ASER A 167       6.592 -21.030 -31.535  0.58 15.93           H  
ATOM   1733  H  BSER A 167       6.507 -21.147 -31.637  0.42 14.30           H  
ATOM   1734  N   CYS A 168       5.731 -19.041 -29.354  1.00 10.71           N  
ANISOU 1734  N   CYS A 168     1656   1236   1176    -78     16    -91       N  
ATOM   1735  CA  CYS A 168       5.728 -18.167 -28.187  1.00 10.48           C  
ANISOU 1735  CA  CYS A 168     1558   1324   1098    126     -1    -54       C  
ATOM   1736  C   CYS A 168       6.329 -16.800 -28.522  1.00 10.36           C  
ANISOU 1736  C   CYS A 168     1624   1332    982    -30    -18   -101       C  
ATOM   1737  O   CYS A 168       5.748 -15.754 -28.208  1.00 10.89           O  
ANISOU 1737  O   CYS A 168     1635   1348   1154     12    -17   -150       O  
ATOM   1738  CB  CYS A 168       6.506 -18.871 -27.074  1.00 11.02           C  
ANISOU 1738  CB  CYS A 168     1527   1353   1307     37     63     68       C  
ATOM   1739  SG  CYS A 168       6.379 -18.149 -25.434  1.00 10.99           S  
ANISOU 1739  SG  CYS A 168     1592   1388   1195   -117    -74    -10       S  
ATOM   1740  H  ACYS A 168       6.214 -19.747 -29.267  0.58 12.85           H  
ATOM   1741  H  BCYS A 168       6.205 -19.752 -29.257  0.42 12.85           H  
ATOM   1742  HA  CYS A 168       4.815 -18.035 -27.886  1.00 12.57           H  
ATOM   1743  HB2 CYS A 168       6.187 -19.785 -27.012  1.00 13.22           H  
ATOM   1744  HB3 CYS A 168       7.445 -18.874 -27.315  1.00 13.22           H  
ATOM   1745  N   LYS A 169       7.491 -16.809 -29.186  1.00 11.57           N  
ANISOU 1745  N   LYS A 169     1689   1393   1313     16    285    -81       N  
ATOM   1746  CA  LYS A 169       8.147 -15.567 -29.566  1.00 13.02           C  
ANISOU 1746  CA  LYS A 169     1931   1379   1638   -178    271   -149       C  
ATOM   1747  C   LYS A 169       7.324 -14.792 -30.584  1.00 13.39           C  
ANISOU 1747  C   LYS A 169     2127   1367   1595    -25    392   -234       C  
ATOM   1748  O   LYS A 169       7.275 -13.563 -30.544  1.00 14.58           O  
ANISOU 1748  O   LYS A 169     2186   1348   2004     -8    327   -194       O  
ATOM   1749  CB  LYS A 169       9.542 -15.878 -30.102  1.00 12.76           C  
ANISOU 1749  CB  LYS A 169     1798   1520   1529      9    379   -143       C  
ATOM   1750  CG  LYS A 169      10.498 -16.334 -29.000  1.00 14.07           C  
ANISOU 1750  CG  LYS A 169     1688   1960   1697    -77    207   -367       C  
ATOM   1751  CD  LYS A 169      11.814 -16.771 -29.559  1.00 18.43           C  
ANISOU 1751  CD  LYS A 169     2014   3006   1983     21   -175   -510       C  
ATOM   1752  CE  LYS A 169      12.823 -16.820 -28.445  1.00 23.82           C  
ANISOU 1752  CE  LYS A 169     2373   3803   2875    199   -347   -455       C  
ATOM   1753  NZ  LYS A 169      14.065 -17.474 -28.894  1.00 27.31           N  
ANISOU 1753  NZ  LYS A 169     2411   4383   3584    314   -431   -399       N  
ATOM   1754  H   LYS A 169       7.913 -17.520 -29.424  1.00 13.88           H  
ATOM   1755  N   SER A 170       6.666 -15.490 -31.504  1.00 12.75           N  
ANISOU 1755  N   SER A 170     2255   1309   1281    -38    123     -8       N  
ATOM   1756  CA  SER A 170       5.811 -14.805 -32.468  1.00 14.76           C  
ANISOU 1756  CA  SER A 170     2714   1517   1375    154     62     22       C  
ATOM   1757  C   SER A 170       4.617 -14.149 -31.782  1.00 13.50           C  
ANISOU 1757  C   SER A 170     2370   1492   1266     15   -226    116       C  
ATOM   1758  O   SER A 170       4.163 -13.082 -32.217  1.00 15.57           O  
ANISOU 1758  O   SER A 170     2829   1605   1482    322   -317    188       O  
ATOM   1759  CB  SER A 170       5.337 -15.802 -33.514  1.00 18.15           C  
ANISOU 1759  CB  SER A 170     3755   1977   1165    413     13    -59       C  
ATOM   1760  OG  SER A 170       6.404 -16.162 -34.369  1.00 22.50           O  
ANISOU 1760  OG  SER A 170     4703   2294   1553    518    379      6       O  
ATOM   1761  H   SER A 170       6.696 -16.345 -31.592  1.00 15.30           H  
ATOM   1762  N   ALA A 171       4.085 -14.786 -30.721  1.00 12.66           N  
ANISOU 1762  N   ALA A 171     2030   1372   1407     28   -252    -79       N  
ATOM   1763  CA  ALA A 171       2.959 -14.214 -29.985  1.00 12.41           C  
ANISOU 1763  CA  ALA A 171     1750   1330   1636   -124   -390     54       C  
ATOM   1764  C   ALA A 171       3.359 -12.971 -29.191  1.00 11.55           C  
ANISOU 1764  C   ALA A 171     1706   1277   1406     47   -230     66       C  
ATOM   1765  O   ALA A 171       2.545 -12.050 -29.040  1.00 13.11           O  
ANISOU 1765  O   ALA A 171     1584   1645   1753    223   -385    -18       O  
ATOM   1766  CB  ALA A 171       2.346 -15.255 -29.043  1.00 13.94           C  
ANISOU 1766  CB  ALA A 171     1903   1581   1812   -328   -430     69       C  
ATOM   1767  HA  ALA A 171       2.275 -13.951 -30.620  1.00 14.89           H  
ATOM   1768  HB3 ALA A 171       3.023 -15.548 -28.412  1.00 16.73           H  
ATOM   1769  N   TYR A 172       4.589 -12.947 -28.669  1.00 10.31           N  
ANISOU 1769  N   TYR A 172     1467   1206   1246    114   -172     39       N  
ATOM   1770  CA  TYR A 172       5.090 -11.880 -27.808  1.00 10.18           C  
ANISOU 1770  CA  TYR A 172     1573   1127   1168     76   -110     78       C  
ATOM   1771  C   TYR A 172       6.447 -11.406 -28.320  1.00  9.76           C  
ANISOU 1771  C   TYR A 172     1512   1170   1025    -60    -80    122       C  
ATOM   1772  O   TYR A 172       7.478 -11.646 -27.686  1.00 10.39           O  
ANISOU 1772  O   TYR A 172     1606   1282   1060    -72    -84    202       O  
ATOM   1773  CB  TYR A 172       5.189 -12.375 -26.363  1.00 10.27           C  
ANISOU 1773  CB  TYR A 172     1536   1169   1196   -100    -95    162       C  
ATOM   1774  CG  TYR A 172       3.883 -12.743 -25.705  1.00  9.84           C  
ANISOU 1774  CG  TYR A 172     1514   1129   1094   -100    -97    135       C  
ATOM   1775  CD1 TYR A 172       3.048 -11.769 -25.189  1.00 11.34           C  
ANISOU 1775  CD1 TYR A 172     1692   1140   1477    -30    -63     15       C  
ATOM   1776  CD2 TYR A 172       3.510 -14.069 -25.543  1.00  9.91           C  
ANISOU 1776  CD2 TYR A 172     1451   1154   1159     73   -203    144       C  
ATOM   1777  CE1 TYR A 172       1.879 -12.091 -24.550  1.00 11.94           C  
ANISOU 1777  CE1 TYR A 172     1655   1336   1548    -20     94     99       C  
ATOM   1778  CE2 TYR A 172       2.325 -14.401 -24.900  1.00  9.66           C  
ANISOU 1778  CE2 TYR A 172     1354   1110   1208    -48    -58    196       C  
ATOM   1779  CZ  TYR A 172       1.516 -13.412 -24.399  1.00 10.18           C  
ANISOU 1779  CZ  TYR A 172     1392   1154   1320    -34    -98    103       C  
ATOM   1780  OH  TYR A 172       0.348 -13.702 -23.723  1.00 10.88           O  
ANISOU 1780  OH  TYR A 172     1365   1354   1414      2      2    141       O  
ATOM   1781  H   TYR A 172       5.171 -13.566 -28.807  1.00 12.38           H  
ATOM   1782  HA  TYR A 172       4.474 -11.131 -27.834  1.00 12.22           H  
ATOM   1783  HB3 TYR A 172       5.614 -11.690 -25.823  1.00 12.32           H  
ATOM   1784  HD2 TYR A 172       4.059 -14.743 -25.872  1.00 11.89           H  
ATOM   1785  HE2 TYR A 172       2.088 -15.294 -24.795  1.00 11.60           H  
ATOM   1786  N   PRO A 173       6.471 -10.680 -29.442  1.00 10.83           N  
ANISOU 1786  N   PRO A 173     1616   1396   1104      7   -113    211       N  
ATOM   1787  CA  PRO A 173       7.745 -10.232 -30.006  1.00 13.33           C  
ANISOU 1787  CA  PRO A 173     1723   2225   1118   -272   -154    463       C  
ATOM   1788  C   PRO A 173       8.545  -9.438 -28.992  1.00 12.71           C  
ANISOU 1788  C   PRO A 173     1598   1924   1307   -241     31    711       C  
ATOM   1789  O   PRO A 173       8.017  -8.564 -28.298  1.00 13.58           O  
ANISOU 1789  O   PRO A 173     1845   1589   1726   -245   -195    593       O  
ATOM   1790  CB  PRO A 173       7.312  -9.340 -31.182  1.00 16.61           C  
ANISOU 1790  CB  PRO A 173     2146   2798   1369   -456   -175    748       C  
ATOM   1791  CG  PRO A 173       5.945  -9.646 -31.452  1.00 15.25           C  
ANISOU 1791  CG  PRO A 173     2043   2220   1530     65    -36    750       C  
ATOM   1792  CD  PRO A 173       5.315 -10.317 -30.295  1.00 12.76           C  
ANISOU 1792  CD  PRO A 173     2088   1636   1125     43   -226    335       C  
ATOM   1793  N  AGLY A 174       9.839  -9.746 -28.904  0.56 13.89           N  
ANISOU 1793  N  AGLY A 174     1568   2135   1576   -131      5    720       N  
ATOM   1794  N  BGLY A 174       9.834  -9.770 -28.914  0.44 14.09           N  
ANISOU 1794  N  BGLY A 174     1682   2240   1432   -386     29    831       N  
ATOM   1795  CA AGLY A 174      10.727  -8.980 -28.048  0.56 14.68           C  
ANISOU 1795  CA AGLY A 174     1734   2136   1709   -349   -232    623       C  
ATOM   1796  CA BGLY A 174      10.773  -9.055 -28.092  0.44 15.01           C  
ANISOU 1796  CA BGLY A 174     1771   2434   1496   -659   -115    798       C  
ATOM   1797  C  AGLY A 174      10.568  -9.208 -26.562  0.56 13.49           C  
ANISOU 1797  C  AGLY A 174     1694   1630   1800   -328   -347    555       C  
ATOM   1798  C  BGLY A 174      10.809  -9.446 -26.633  0.44 14.21           C  
ANISOU 1798  C  BGLY A 174     1716   2130   1552   -576   -272    758       C  
ATOM   1799  O  AGLY A 174      11.107  -8.426 -25.763  0.56 12.99           O  
ANISOU 1799  O  AGLY A 174     1435   1415   2086   -180   -392    488       O  
ATOM   1800  O  BGLY A 174      11.745  -9.039 -25.943  0.44 14.99           O  
ANISOU 1800  O  BGLY A 174     1530   2423   1742   -687   -547    734       O  
ATOM   1801  H  AGLY A 174      10.220 -10.389 -29.329  0.56 16.67           H  
ATOM   1802  H  BGLY A 174      10.186 -10.425 -29.345  0.44 16.91           H  
ATOM   1803  N   GLN A 175       9.841 -10.250 -26.151  1.00 11.86           N  
ANISOU 1803  N   GLN A 175     1680   1442   1385   -353   -273    506       N  
ATOM   1804  CA  GLN A 175       9.561 -10.415 -24.727  1.00 10.68           C  
ANISOU 1804  CA  GLN A 175     1829   1040   1190   -259   -266    216       C  
ATOM   1805  C   GLN A 175       9.912 -11.774 -24.133  1.00 10.16           C  
ANISOU 1805  C   GLN A 175     1643   1067   1150   -188   -172    202       C  
ATOM   1806  O   GLN A 175       9.929 -11.902 -22.899  1.00 11.17           O  
ANISOU 1806  O   GLN A 175     2046   1173   1025    -55   -253    139       O  
ATOM   1807  CB  GLN A 175       8.071 -10.159 -24.474  1.00 10.82           C  
ANISOU 1807  CB  GLN A 175     1828   1041   1243   -103   -185    157       C  
ATOM   1808  CG  GLN A 175       7.618  -8.759 -24.910  1.00 12.27           C  
ANISOU 1808  CG  GLN A 175     1997   1059   1607   -201   -279    354       C  
ATOM   1809  CD  GLN A 175       6.117  -8.703 -25.203  1.00 13.93           C  
ANISOU 1809  CD  GLN A 175     2539   1086   1669    -11   -211    204       C  
ATOM   1810  OE1 GLN A 175       5.303  -8.774 -24.283  1.00 16.61           O  
ANISOU 1810  OE1 GLN A 175     2943   1512   1855    391    194    119       O  
ATOM   1811  NE2 GLN A 175       5.751  -8.581 -26.488  1.00 14.32           N  
ANISOU 1811  NE2 GLN A 175     2267   1270   1904    -23    -73    276       N  
ATOM   1812  H  AGLN A 175       9.509 -10.857 -26.661  0.56 14.24           H  
ATOM   1813  H  BGLN A 175       9.324 -10.719 -26.652  0.44 14.24           H  
ATOM   1814  HA  GLN A 175      10.061  -9.745 -24.236  1.00 12.82           H  
ATOM   1815  HB3 GLN A 175       7.892 -10.250 -23.525  1.00 12.99           H  
ATOM   1816  N   ILE A 176      10.122 -12.805 -24.938  1.00  9.97           N  
ANISOU 1816  N   ILE A 176     1613   1177   1000    -86    -86     68       N  
ATOM   1817  CA  ILE A 176      10.305 -14.155 -24.432  1.00  9.66           C  
ANISOU 1817  CA  ILE A 176     1532   1191    949     26    -37     92       C  
ATOM   1818  C   ILE A 176      11.793 -14.432 -24.299  1.00  9.84           C  
ANISOU 1818  C   ILE A 176     1519   1234    986      0     55     97       C  
ATOM   1819  O   ILE A 176      12.536 -14.419 -25.287  1.00 12.66           O  
ANISOU 1819  O   ILE A 176     1705   2092   1015     25    159    242       O  
ATOM   1820  CB  ILE A 176       9.643 -15.188 -25.351  1.00  9.81           C  
ANISOU 1820  CB  ILE A 176     1505   1136   1086    -40    -38     10       C  
ATOM   1821  CG1 ILE A 176       8.150 -14.895 -25.520  1.00 10.40           C  
ANISOU 1821  CG1 ILE A 176     1672   1184   1095   -105   -123    147       C  
ATOM   1822  CG2 ILE A 176       9.892 -16.599 -24.845  1.00 10.57           C  
ANISOU 1822  CG2 ILE A 176     1710   1160   1148     53    -90    -38       C  
ATOM   1823  CD1 ILE A 176       7.338 -14.832 -24.228  1.00 10.81           C  
ANISOU 1823  CD1 ILE A 176     1698   1277   1133      4   -137      0       C  
ATOM   1824  H   ILE A 176      10.162 -12.747 -25.795  1.00 11.97           H  
ATOM   1825  HA  ILE A 176       9.901 -14.226 -23.553  1.00 11.60           H  
ATOM   1826 HG12 ILE A 176       8.055 -14.038 -25.965  1.00 12.47           H  
ATOM   1827 HG13 ILE A 176       7.762 -15.591 -26.073  1.00 12.47           H  
ATOM   1828 HG23 ILE A 176       9.520 -16.685 -23.953  1.00 12.69           H  
ATOM   1829  N   THR A 177      12.246 -14.701 -23.074  1.00  9.25           N  
ANISOU 1829  N   THR A 177     1319   1235    961    -10     -5     66       N  
ATOM   1830  CA  THR A 177      13.626 -15.061 -22.811  1.00  9.13           C  
ANISOU 1830  CA  THR A 177     1216   1284    971    -83     81    141       C  
ATOM   1831  C   THR A 177      13.764 -16.581 -22.749  1.00  8.90           C  
ANISOU 1831  C   THR A 177     1131   1272    979     60     11     35       C  
ATOM   1832  O   THR A 177      12.782 -17.331 -22.754  1.00  9.58           O  
ANISOU 1832  O   THR A 177     1324   1241   1075     71    -67    -80       O  
ATOM   1833  CB  THR A 177      14.139 -14.447 -21.509  1.00  9.87           C  
ANISOU 1833  CB  THR A 177     1506   1161   1083   -151     70    127       C  
ATOM   1834  OG1 THR A 177      13.545 -15.178 -20.434  1.00  9.19           O  
ANISOU 1834  OG1 THR A 177     1330   1104   1058    -56     11     27       O  
ATOM   1835  CG2 THR A 177      13.817 -12.967 -21.412  1.00 10.73           C  
ANISOU 1835  CG2 THR A 177     1608   1220   1247   -247    -60    142       C  
ATOM   1836  H   THR A 177      11.756 -14.679 -22.367  1.00 11.10           H  
ATOM   1837  HA  THR A 177      14.182 -14.737 -23.537  1.00 10.96           H  
ATOM   1838 HG21 THR A 177      14.109 -12.620 -20.555  1.00 12.87           H  
ATOM   1839 HG22 THR A 177      14.270 -12.482 -22.120  1.00 12.87           H  
ATOM   1840  N   SER A 178      15.020 -17.029 -22.623  1.00  9.74           N  
ANISOU 1840  N   SER A 178     1348   1345   1009    105    212     58       N  
ATOM   1841  CA  SER A 178      15.322 -18.453 -22.474  1.00 10.30           C  
ANISOU 1841  CA  SER A 178     1318   1520   1074     86    216    -63       C  
ATOM   1842  C   SER A 178      14.798 -19.028 -21.174  1.00  9.42           C  
ANISOU 1842  C   SER A 178     1323   1155   1102    169    102    -36       C  
ATOM   1843  O   SER A 178      14.824 -20.250 -20.998  1.00 10.44           O  
ANISOU 1843  O   SER A 178     1541   1285   1140    360    189    -47       O  
ATOM   1844  CB  SER A 178      16.828 -18.682 -22.588  1.00 13.59           C  
ANISOU 1844  CB  SER A 178     1400   2124   1638    347    459     17       C  
ATOM   1845  OG  SER A 178      17.503 -18.049 -21.520  1.00 18.09           O  
ANISOU 1845  OG  SER A 178     1488   2762   2621    365     95   -177       O  
ATOM   1846  HA  SER A 178      14.897 -18.936 -23.200  1.00 12.36           H  
ATOM   1847  HB3 SER A 178      17.142 -18.306 -23.426  1.00 16.30           H  
ATOM   1848  N   ASN A 179      14.333 -18.174 -20.263  1.00  8.44           N  
ANISOU 1848  N   ASN A 179     1019   1111   1078     77     65     19       N  
ATOM   1849  CA  ASN A 179      13.782 -18.597 -18.975  1.00  7.91           C  
ANISOU 1849  CA  ASN A 179     1016   1010    979     67     39     26       C  
ATOM   1850  C   ASN A 179      12.271 -18.625 -18.949  1.00  7.89           C  
ANISOU 1850  C   ASN A 179     1080    943    974     53     41     19       C  
ATOM   1851  O   ASN A 179      11.668 -18.720 -17.863  1.00  7.84           O  
ANISOU 1851  O   ASN A 179     1097    942    940     24     37    -39       O  
ATOM   1852  CB  ASN A 179      14.306 -17.697 -17.868  1.00  8.43           C  
ANISOU 1852  CB  ASN A 179     1079   1162    962    -21     39      1       C  
ATOM   1853  CG  ASN A 179      15.810 -17.718 -17.804  1.00  9.16           C  
ANISOU 1853  CG  ASN A 179     1026   1327   1128    226     24    -67       C  
ATOM   1854  OD1 ASN A 179      16.415 -18.798 -17.732  1.00  9.99           O  
ANISOU 1854  OD1 ASN A 179     1081   1330   1385    171    -74   -137       O  
ATOM   1855  ND2 ASN A 179      16.439 -16.544 -17.879  1.00  9.98           N  
ANISOU 1855  ND2 ASN A 179     1060   1318   1416    -73     72   -119       N  
ATOM   1856  H   ASN A 179      14.326 -17.321 -20.371  1.00 10.13           H  
ATOM   1857  HA  ASN A 179      14.093 -19.497 -18.789  1.00  9.49           H  
ATOM   1858  HB3 ASN A 179      13.966 -18.013 -17.017  1.00 10.12           H  
ATOM   1859  N   MET A 180      11.641 -18.611 -20.129  1.00  7.64           N  
ANISOU 1859  N   MET A 180     1039    977    886     58     70    -47       N  
ATOM   1860  CA  MET A 180      10.195 -18.564 -20.254  1.00  7.59           C  
ANISOU 1860  CA  MET A 180     1011    977    896    111     22    -70       C  
ATOM   1861  C   MET A 180       9.737 -19.565 -21.307  1.00  7.90           C  
ANISOU 1861  C   MET A 180     1062    956    985     98     73   -100       C  
ATOM   1862  O   MET A 180      10.451 -19.831 -22.278  1.00  9.50           O  
ANISOU 1862  O   MET A 180     1253   1261   1097     -5    163   -184       O  
ATOM   1863  CB  MET A 180       9.743 -17.165 -20.727  1.00  7.96           C  
ANISOU 1863  CB  MET A 180     1130   1017    879     87     27     71       C  
ATOM   1864  CG  MET A 180      10.104 -16.067 -19.755  1.00  8.15           C  
ANISOU 1864  CG  MET A 180     1144   1004    949      9     13    -62       C  
ATOM   1865  SD  MET A 180       9.732 -14.467 -20.520  1.00  8.32           S  
ANISOU 1865  SD  MET A 180     1226    950    984     45    -33     29       S  
ATOM   1866  CE  MET A 180      10.560 -13.366 -19.338  1.00  9.46           C  
ANISOU 1866  CE  MET A 180     1547   1074    975   -135   -103    -40       C  
ATOM   1867  H   MET A 180      12.048 -18.629 -20.886  1.00  9.16           H  
ATOM   1868  HA  MET A 180       9.779 -18.761 -19.401  1.00  9.11           H  
ATOM   1869  HB2 MET A 180      10.170 -16.966 -21.575  1.00  9.56           H  
ATOM   1870  HB3 MET A 180       8.779 -17.165 -20.834  1.00  9.56           H  
ATOM   1871  HG2 MET A 180       9.576 -16.158 -18.946  1.00  9.78           H  
ATOM   1872  HG3 MET A 180      11.052 -16.105 -19.554  1.00  9.78           H  
ATOM   1873  HE2 MET A 180      10.083 -13.392 -18.494  1.00 11.36           H  
ATOM   1874  N   PHE A 181       8.524 -20.090 -21.140  1.00  8.18           N  
ANISOU 1874  N   PHE A 181     1240   1024    843     18     12   -152       N  
ATOM   1875  CA  PHE A 181       7.858 -20.827 -22.201  1.00  8.11           C  
ANISOU 1875  CA  PHE A 181     1138   1053    890     34    -16    -54       C  
ATOM   1876  C   PHE A 181       6.385 -20.475 -22.190  1.00  7.70           C  
ANISOU 1876  C   PHE A 181     1225    852    848     46     -7   -167       C  
ATOM   1877  O   PHE A 181       5.829 -20.066 -21.174  1.00  8.43           O  
ANISOU 1877  O   PHE A 181     1168   1106    930     75    -41   -198       O  
ATOM   1878  CB  PHE A 181       8.057 -22.351 -22.108  1.00  8.88           C  
ANISOU 1878  CB  PHE A 181     1323   1038   1015    146    -75   -275       C  
ATOM   1879  CG  PHE A 181       7.418 -23.015 -20.909  1.00  8.37           C  
ANISOU 1879  CG  PHE A 181     1277    952    952     49    -60   -222       C  
ATOM   1880  CD1 PHE A 181       6.154 -23.564 -20.994  1.00  9.13           C  
ANISOU 1880  CD1 PHE A 181     1451    930   1090     52   -176   -143       C  
ATOM   1881  CD2 PHE A 181       8.094 -23.097 -19.689  1.00  9.47           C  
ANISOU 1881  CD2 PHE A 181     1369   1145   1085     60    -90    -87       C  
ATOM   1882  CE1 PHE A 181       5.579 -24.220 -19.921  1.00  9.83           C  
ANISOU 1882  CE1 PHE A 181     1557    969   1208    -73   -261   -148       C  
ATOM   1883  CE2 PHE A 181       7.508 -23.748 -18.607  1.00  9.63           C  
ANISOU 1883  CE2 PHE A 181     1383   1145   1130    -92   -177    -57       C  
ATOM   1884  CZ  PHE A 181       6.268 -24.334 -18.732  1.00  9.02           C  
ANISOU 1884  CZ  PHE A 181     1378    921   1128     66    -81   -165       C  
ATOM   1885  H   PHE A 181       8.066 -20.030 -20.415  1.00  9.81           H  
ATOM   1886  HA  PHE A 181       8.222 -20.538 -23.052  1.00  9.73           H  
ATOM   1887  HB2 PHE A 181       7.679 -22.759 -22.903  1.00 10.66           H  
ATOM   1888  HB3 PHE A 181       9.009 -22.535 -22.071  1.00 10.66           H  
ATOM   1889  HE1 PHE A 181       4.731 -24.591 -20.004  1.00 11.79           H  
ATOM   1890  HE2 PHE A 181       7.968 -23.809 -17.801  1.00 11.55           H  
ATOM   1891  N   CYS A 182       5.749 -20.688 -23.335  1.00  8.60           N  
ANISOU 1891  N   CYS A 182     1117   1152    998     69    -68   -203       N  
ATOM   1892  CA  CYS A 182       4.318 -20.513 -23.452  1.00  8.66           C  
ANISOU 1892  CA  CYS A 182     1293   1070    926      1    -78   -115       C  
ATOM   1893  C   CYS A 182       3.635 -21.871 -23.378  1.00  8.38           C  
ANISOU 1893  C   CYS A 182     1143   1180    861     23    -99   -166       C  
ATOM   1894  O   CYS A 182       4.168 -22.888 -23.836  1.00  9.00           O  
ANISOU 1894  O   CYS A 182     1322   1105    991     65    -61   -186       O  
ATOM   1895  CB  CYS A 182       3.936 -19.861 -24.787  1.00  9.80           C  
ANISOU 1895  CB  CYS A 182     1351   1318   1055    128   -107   -128       C  
ATOM   1896  SG  CYS A 182       4.370 -18.142 -25.040  1.00 10.16           S  
ANISOU 1896  SG  CYS A 182     1497   1141   1222     -3    -39    -15       S  
ATOM   1897  HB2 CYS A 182       4.361 -20.367 -25.497  1.00 11.76           H  
ATOM   1898  HB3 CYS A 182       2.973 -19.926 -24.886  1.00 11.76           H  
ATOM   1899  N   ALA A 183       2.416 -21.883 -22.828  1.00  8.65           N  
ANISOU 1899  N   ALA A 183     1138   1112   1038      4   -138   -155       N  
ATOM   1900  CA  ALA A 183       1.596 -23.082 -22.825  1.00  8.45           C  
ANISOU 1900  CA  ALA A 183     1205    965   1042     75    -93   -166       C  
ATOM   1901  C   ALA A 183       0.154 -22.638 -22.945  1.00  8.77           C  
ANISOU 1901  C   ALA A 183     1274    980   1077    -37    -25    -84       C  
ATOM   1902  O   ALA A 183      -0.208 -21.551 -22.483  1.00  9.75           O  
ANISOU 1902  O   ALA A 183     1289   1111   1304      6   -106   -252       O  
ATOM   1903  CB  ALA A 183       1.794 -23.919 -21.564  1.00  9.00           C  
ANISOU 1903  CB  ALA A 183     1316   1073   1031     95    -71   -183       C  
ATOM   1904  HA  ALA A 183       1.816 -23.628 -23.595  1.00 10.14           H  
ATOM   1905  HB1 ALA A 183       1.226 -24.703 -21.613  1.00 10.80           H  
ATOM   1906  HB2 ALA A 183       2.724 -24.187 -21.507  1.00 10.80           H  
ATOM   1907  HB3 ALA A 183       1.555 -23.385 -20.790  1.00 10.80           H  
ATOM   1908  N   GLY A 184      -0.673 -23.486 -23.554  1.00  9.23           N  
ANISOU 1908  N   GLY A 184     1232   1077   1200    -54   -113   -227       N  
ATOM   1909  CA  GLY A 184      -2.062 -23.141 -23.763  1.00  9.77           C  
ANISOU 1909  CA  GLY A 184     1351   1138   1224     34   -298   -266       C  
ATOM   1910  C   GLY A 184      -2.485 -23.320 -25.194  1.00 10.01           C  
ANISOU 1910  C   GLY A 184     1462   1176   1167   -111   -145   -119       C  
ATOM   1911  O   GLY A 184      -2.084 -24.288 -25.851  1.00 11.09           O  
ANISOU 1911  O   GLY A 184     1533   1403   1279   -111   -222   -211       O  
ATOM   1912  H   GLY A 184      -0.449 -24.261 -23.851  1.00 11.08           H  
ATOM   1913  HA3 GLY A 184      -2.219 -22.221 -23.500  1.00 11.72           H  
ATOM   1914  N   TYR A 184A     -3.293 -22.379 -25.665  1.00 10.91           N  
ANISOU 1914  N   TYR A 184A    1537   1375   1234     70   -209    -31       N  
ATOM   1915  CA  TYR A 184A     -4.071 -22.545 -26.889  1.00 12.40           C  
ANISOU 1915  CA  TYR A 184A    1823   1611   1276    172   -377     27       C  
ATOM   1916  C   TYR A 184A     -4.089 -21.213 -27.618  1.00 13.79           C  
ANISOU 1916  C   TYR A 184A    2076   1771   1391    273   -414    -32       C  
ATOM   1917  O   TYR A 184A     -4.664 -20.243 -27.114  1.00 15.30           O  
ANISOU 1917  O   TYR A 184A    2585   1843   1386    478   -356     98       O  
ATOM   1918  CB  TYR A 184A     -5.502 -22.989 -26.524  1.00 14.10           C  
ANISOU 1918  CB  TYR A 184A    1615   2147   1597    -67   -657     58       C  
ATOM   1919  CG  TYR A 184A     -5.527 -24.329 -25.852  1.00 13.45           C  
ANISOU 1919  CG  TYR A 184A    1338   2182   1591   -309   -411    168       C  
ATOM   1920  CD1 TYR A 184A     -5.589 -25.496 -26.597  1.00 14.88           C  
ANISOU 1920  CD1 TYR A 184A    1838   2209   1608   -446   -599    -27       C  
ATOM   1921  CD2 TYR A 184A     -5.449 -24.438 -24.464  1.00 13.92           C  
ANISOU 1921  CD2 TYR A 184A    1441   2234   1616   -253   -179     87       C  
ATOM   1922  CE1 TYR A 184A     -5.575 -26.736 -25.971  1.00 15.53           C  
ANISOU 1922  CE1 TYR A 184A    2019   2109   1774   -407   -475     69       C  
ATOM   1923  CE2 TYR A 184A     -5.431 -25.661 -23.840  1.00 14.06           C  
ANISOU 1923  CE2 TYR A 184A    1531   2062   1749   -365   -279    148       C  
ATOM   1924  CZ  TYR A 184A     -5.503 -26.815 -24.598  1.00 14.12           C  
ANISOU 1924  CZ  TYR A 184A    1576   2116   1672   -272   -447    206       C  
ATOM   1925  OH  TYR A 184A     -5.501 -28.069 -24.030  1.00 15.96           O  
ANISOU 1925  OH  TYR A 184A    2015   2051   1999   -483   -433    269       O  
ATOM   1926  H   TYR A 184A     -3.412 -21.616 -25.285  1.00 13.09           H  
ATOM   1927  HA  TYR A 184A     -3.663 -23.216 -27.458  1.00 14.88           H  
ATOM   1928  N   LEU A 185      -3.507 -21.167 -28.825  1.00 13.36           N  
ANISOU 1928  N   LEU A 185     2048   1682   1348     56   -390    170       N  
ATOM   1929  CA  LEU A 185      -3.498 -19.910 -29.566  1.00 13.77           C  
ANISOU 1929  CA  LEU A 185     2211   1659   1360   -125   -351    254       C  
ATOM   1930  C   LEU A 185      -4.899 -19.433 -29.946  1.00 14.91           C  
ANISOU 1930  C   LEU A 185     2400   1747   1517    -12   -538    237       C  
ATOM   1931  O   LEU A 185      -5.089 -18.234 -30.194  1.00 16.69           O  
ANISOU 1931  O   LEU A 185     2494   1855   1993    -28   -534    430       O  
ATOM   1932  CB  LEU A 185      -2.626 -20.032 -30.819  1.00 15.18           C  
ANISOU 1932  CB  LEU A 185     2410   1871   1488   -213   -429    131       C  
ATOM   1933  CG  LEU A 185      -1.135 -20.285 -30.574  1.00 17.06           C  
ANISOU 1933  CG  LEU A 185     2634   1974   1876   -199   -588    221       C  
ATOM   1934  CD1 LEU A 185      -0.372 -20.394 -31.879  1.00 18.67           C  
ANISOU 1934  CD1 LEU A 185     2908   2152   2034   -314   -287     18       C  
ATOM   1935  CD2 LEU A 185      -0.532 -19.194 -29.689  1.00 17.84           C  
ANISOU 1935  CD2 LEU A 185     2735   1872   2171   -324   -765    -10       C  
ATOM   1936  HB2 LEU A 185      -2.966 -20.754 -31.371  1.00 18.22           H  
ATOM   1937  HG  LEU A 185      -1.038 -21.129 -30.106  1.00 20.48           H  
ATOM   1938 HD13 LEU A 185      -0.471 -19.565 -32.373  1.00 22.40           H  
ATOM   1939 HD22 LEU A 185      -0.700 -18.330 -30.095  1.00 21.41           H  
ATOM   1940  N   GLU A 186      -5.877 -20.333 -30.017  1.00 15.29           N  
ANISOU 1940  N   GLU A 186     2202   2191   1414    -99   -523    163       N  
ATOM   1941  CA  GLU A 186      -7.228 -19.933 -30.379  1.00 17.33           C  
ANISOU 1941  CA  GLU A 186     2279   2416   1889     15   -444    353       C  
ATOM   1942  C   GLU A 186      -7.922 -19.169 -29.260  1.00 18.43           C  
ANISOU 1942  C   GLU A 186     2626   2286   2090     78   -250    643       C  
ATOM   1943  O   GLU A 186      -8.973 -18.569 -29.509  1.00 21.19           O  
ANISOU 1943  O   GLU A 186     2747   2623   2681    323    -60    542       O  
ATOM   1944  CB  GLU A 186      -8.049 -21.159 -30.796  1.00 21.58           C  
ANISOU 1944  CB  GLU A 186     2924   2726   2551    -49   -896    319       C  
ATOM   1945  CG  GLU A 186      -8.163 -22.260 -29.736  1.00 29.07           C  
ANISOU 1945  CG  GLU A 186     4428   3197   3419   -203  -1437     86       C  
ATOM   1946  CD  GLU A 186      -7.118 -23.381 -29.875  1.00 32.76           C  
ANISOU 1946  CD  GLU A 186     5233   3223   3990   -622  -2366    100       C  
ATOM   1947  OE1 GLU A 186      -5.900 -23.089 -29.997  1.00 30.43           O  
ANISOU 1947  OE1 GLU A 186     4912   2773   3878   -691  -2496    202       O  
ATOM   1948  OE2 GLU A 186      -7.526 -24.573 -29.854  1.00 36.03           O  
ANISOU 1948  OE2 GLU A 186     5736   3474   4480  -1009  -2793    132       O  
ATOM   1949  N   GLY A 187      -7.346 -19.142 -28.060  1.00 17.60           N  
ANISOU 1949  N   GLY A 187     2906   1899   1883    -98    133    534       N  
ATOM   1950  CA  GLY A 187      -7.971 -18.505 -26.919  1.00 18.74           C  
ANISOU 1950  CA  GLY A 187     3066   1879   2175   -340    392    408       C  
ATOM   1951  C   GLY A 187      -8.944 -19.423 -26.186  1.00 17.31           C  
ANISOU 1951  C   GLY A 187     2968   1612   1998   -460    161    168       C  
ATOM   1952  O   GLY A 187      -9.216 -20.559 -26.582  1.00 22.03           O  
ANISOU 1952  O   GLY A 187     4093   1848   2428   -627    764     20       O  
ATOM   1953  N   GLY A 188      -9.486 -18.905 -25.085  1.00 12.90           N  
ANISOU 1953  N   GLY A 188     1735   1542   1626    -94   -274    293       N  
ATOM   1954  CA  GLY A 188     -10.547 -19.562 -24.343  1.00 13.90           C  
ANISOU 1954  CA  GLY A 188     1572   1793   1917   -195   -446    377       C  
ATOM   1955  C   GLY A 188     -10.100 -20.372 -23.137  1.00 11.70           C  
ANISOU 1955  C   GLY A 188     1404   1439   1605   -127   -207    136       C  
ATOM   1956  O   GLY A 188     -10.936 -20.663 -22.270  1.00 12.34           O  
ANISOU 1956  O   GLY A 188     1292   1628   1766    -53   -228    136       O  
ATOM   1957  H   GLY A 188      -9.246 -18.153 -24.744  1.00 15.48           H  
ATOM   1958  N  ALYS A 188A     -8.826 -20.759 -23.075  0.69 11.07           N  
ANISOU 1958  N  ALYS A 188A    1356   1517   1333     60   -328     22       N  
ATOM   1959  N  BLYS A 188A     -8.827 -20.746 -23.050  0.31 10.42           N  
ANISOU 1959  N  BLYS A 188A    1434   1103   1421   -147   -137    295       N  
ATOM   1960  CA ALYS A 188A     -8.308 -21.634 -22.026  0.69 10.67           C  
ANISOU 1960  CA ALYS A 188A    1365   1472   1217    -77   -256    -32       C  
ATOM   1961  CA BLYS A 188A     -8.359 -21.616 -21.974  0.31  9.40           C  
ANISOU 1961  CA BLYS A 188A    1501    825   1244   -232   -238    332       C  
ATOM   1962  C  ALYS A 188A     -6.969 -21.063 -21.586  0.69 10.05           C  
ANISOU 1962  C  ALYS A 188A    1356   1226   1236     43   -158     47       C  
ATOM   1963  C  BLYS A 188A     -6.971 -21.152 -21.553  0.31  8.88           C  
ANISOU 1963  C  BLYS A 188A    1238    934   1203   -108    -40     23       C  
ATOM   1964  O  ALYS A 188A     -6.052 -20.976 -22.409  0.69 11.54           O  
ANISOU 1964  O  ALYS A 188A    1774   1472   1136   -110   -169    131       O  
ATOM   1965  O  BLYS A 188A     -6.032 -21.225 -22.350  0.31  9.18           O  
ANISOU 1965  O  BLYS A 188A    1211   1166   1113    110     83   -148       O  
ATOM   1966  CB ALYS A 188A     -8.092 -23.046 -22.574  0.69 11.59           C  
ANISOU 1966  CB ALYS A 188A    1562   1472   1369    -64   -264   -202       C  
ATOM   1967  CB BLYS A 188A     -8.338 -23.080 -22.438  0.31 10.79           C  
ANISOU 1967  CB BLYS A 188A    1886    893   1321   -170   -452    243       C  
ATOM   1968  CG ALYS A 188A     -9.352 -23.879 -22.724  0.69 13.58           C  
ANISOU 1968  CG ALYS A 188A    1757   1726   1676   -213     44   -384       C  
ATOM   1969  CG BLYS A 188A     -9.719 -23.639 -22.794  0.31 12.36           C  
ANISOU 1969  CG BLYS A 188A    2076    934   1686   -456   -392   -148       C  
ATOM   1970  CD ALYS A 188A     -8.998 -25.254 -23.264  0.69 17.11           C  
ANISOU 1970  CD ALYS A 188A    2339   1992   2172   -481    190   -848       C  
ATOM   1971  CD BLYS A 188A     -9.700 -25.153 -23.045  0.31 14.99           C  
ANISOU 1971  CD BLYS A 188A    2304   1262   2130   -347   -243   -448       C  
ATOM   1972  CE ALYS A 188A    -10.188 -26.158 -23.273  0.69 20.49           C  
ANISOU 1972  CE ALYS A 188A    2921   2028   2836   -708    186   -820       C  
ATOM   1973  CE BLYS A 188A     -8.978 -25.529 -24.338  0.31 16.61           C  
ANISOU 1973  CE BLYS A 188A    2341   1518   2452   -386   -141   -617       C  
ATOM   1974  NZ ALYS A 188A     -9.708 -27.482 -23.721  0.69 22.41           N  
ANISOU 1974  NZ ALYS A 188A    3477   1949   3089   -780    -26   -820       N  
ATOM   1975  NZ BLYS A 188A     -9.018 -27.012 -24.568  0.31 18.91           N  
ANISOU 1975  NZ BLYS A 188A    2619   1761   2806   -303    -54   -557       N  
ATOM   1976  HA ALYS A 188A     -8.916 -21.663 -21.271  0.69 12.80           H  
ATOM   1977  HA BLYS A 188A     -8.955 -21.542 -21.213  0.31 11.27           H  
ATOM   1978  HB2ALYS A 188A     -7.667 -22.986 -23.444  0.69 13.91           H  
ATOM   1979  HB2BLYS A 188A     -7.773 -23.154 -23.224  0.31 12.95           H  
ATOM   1980  N   ASP A 189      -6.831 -20.674 -20.314  1.00  8.96           N  
ANISOU 1980  N   ASP A 189     1287   1018   1098      3   -119     40       N  
ATOM   1981  CA  ASP A 189      -5.576 -20.058 -19.885  1.00  8.76           C  
ANISOU 1981  CA  ASP A 189     1239    993   1095    -67    -86     47       C  
ATOM   1982  C   ASP A 189      -5.555 -19.955 -18.362  1.00  8.28           C  
ANISOU 1982  C   ASP A 189     1190    882   1075     18    -20     71       C  
ATOM   1983  O   ASP A 189      -6.576 -20.102 -17.693  1.00  9.53           O  
ANISOU 1983  O   ASP A 189     1120   1325   1175    -67    -30     20       O  
ATOM   1984  CB  ASP A 189      -5.499 -18.649 -20.506  1.00  9.58           C  
ANISOU 1984  CB  ASP A 189     1256   1054   1329     -2    -25    153       C  
ATOM   1985  CG  ASP A 189      -4.101 -18.033 -20.597  1.00  9.58           C  
ANISOU 1985  CG  ASP A 189     1239    959   1440     10      1    144       C  
ATOM   1986  OD1 ASP A 189      -3.087 -18.626 -20.181  1.00 10.06           O  
ANISOU 1986  OD1 ASP A 189     1285   1213   1323     57     -5    154       O  
ATOM   1987  OD2 ASP A 189      -4.075 -16.897 -21.144  1.00 11.69           O  
ANISOU 1987  OD2 ASP A 189     1406   1293   1742    -29   -121    356       O  
ATOM   1988  HB3 ASP A 189      -6.060 -18.046 -19.993  1.00 11.49           H  
ATOM   1989  N   SER A 190      -4.380 -19.642 -17.826  1.00  8.28           N  
ANISOU 1989  N   SER A 190     1038   1043   1064     63    -47     28       N  
ATOM   1990  CA  SER A 190      -4.276 -19.141 -16.457  1.00  8.05           C  
ANISOU 1990  CA  SER A 190     1048    934   1075     32    -19    -40       C  
ATOM   1991  C   SER A 190      -4.599 -17.649 -16.430  1.00  8.90           C  
ANISOU 1991  C   SER A 190     1187   1030   1162     58    -90     26       C  
ATOM   1992  O   SER A 190      -4.654 -16.999 -17.480  1.00 10.55           O  
ANISOU 1992  O   SER A 190     1725   1128   1156     62      4     40       O  
ATOM   1993  CB  SER A 190      -2.892 -19.445 -15.886  1.00 10.34           C  
ANISOU 1993  CB  SER A 190     1261   1330   1338     81    -75   -118       C  
ATOM   1994  OG  SER A 190      -1.878 -18.906 -16.690  1.00 10.84           O  
ANISOU 1994  OG  SER A 190     1244   1479   1397   -122    -40   -158       O  
ATOM   1995  H   SER A 190      -3.626 -19.710 -18.234  1.00  9.94           H  
ATOM   1996  HA  SER A 190      -4.932 -19.596 -15.906  1.00  9.65           H  
ATOM   1997  N   CYS A 191      -4.854 -17.113 -15.228  1.00  9.00           N  
ANISOU 1997  N   CYS A 191     1362    866   1192     76     13    -91       N  
ATOM   1998  CA  CYS A 191      -5.331 -15.734 -15.124  1.00 10.21           C  
ANISOU 1998  CA  CYS A 191     1634    982   1264    183     72    -61       C  
ATOM   1999  C   CYS A 191      -4.886 -15.119 -13.803  1.00 11.03           C  
ANISOU 1999  C   CYS A 191     1928    935   1326    156    -54    103       C  
ATOM   2000  O   CYS A 191      -4.133 -15.728 -13.045  1.00 11.99           O  
ANISOU 2000  O   CYS A 191     1937   1173   1445    220     -5   -168       O  
ATOM   2001  CB  CYS A 191      -6.853 -15.697 -15.359  1.00 11.31           C  
ANISOU 2001  CB  CYS A 191     1726   1121   1450     94    -11      4       C  
ATOM   2002  SG  CYS A 191      -7.522 -14.073 -15.855  1.00 13.35           S  
ANISOU 2002  SG  CYS A 191     2141   1183   1749    451   -153     -8       S  
ATOM   2003  HB2 CYS A 191      -7.082 -16.339 -16.050  1.00 13.57           H  
ATOM   2004  N  AGLN A 192      -5.302 -13.877 -13.565  0.47 12.17           N  
ANISOU 2004  N  AGLN A 192     2263    847   1515   -123   -124   -118       N  
ATOM   2005  N  BGLN A 192      -5.356 -13.887 -13.540  0.53 12.89           N  
ANISOU 2005  N  BGLN A 192     2242   1075   1579    266   -169    -22       N  
ATOM   2006  CA AGLN A 192      -4.941 -13.181 -12.335  0.47 11.10           C  
ANISOU 2006  CA AGLN A 192     2093    717   1410   -187    -74   -167       C  
ATOM   2007  CA BGLN A 192      -5.063 -13.176 -12.293  0.53 12.43           C  
ANISOU 2007  CA BGLN A 192     2163   1066   1494    246    -15    109       C  
ATOM   2008  C  AGLN A 192      -5.359 -13.991 -11.107  0.47 10.19           C  
ANISOU 2008  C  AGLN A 192     1569    740   1564   -162   -128    -85       C  
ATOM   2009  C  BGLN A 192      -5.375 -14.059 -11.095  0.53 10.35           C  
ANISOU 2009  C  BGLN A 192     1635    851   1449    210    -19    -58       C  
ATOM   2010  O  AGLN A 192      -6.500 -14.451 -11.007  0.47 11.56           O  
ANISOU 2010  O  AGLN A 192     1498    961   1936   -472   -396     38       O  
ATOM   2011  O  BGLN A 192      -6.462 -14.632 -11.004  0.53 11.24           O  
ANISOU 2011  O  BGLN A 192     1585    898   1786    216   -255    -49       O  
ATOM   2012  CB AGLN A 192      -5.616 -11.808 -12.333  0.47 12.55           C  
ANISOU 2012  CB AGLN A 192     2335    778   1657   -103   -167   -423       C  
ATOM   2013  CB BGLN A 192      -5.927 -11.909 -12.195  0.53 15.36           C  
ANISOU 2013  CB BGLN A 192     2645   1165   2025    453    -81    394       C  
ATOM   2014  CG AGLN A 192      -4.842 -10.707 -13.090  0.47 15.39           C  
ANISOU 2014  CG AGLN A 192     2896   1125   1825    154     60   -198       C  
ATOM   2015  CG BGLN A 192      -5.866 -10.986 -13.394  0.53 18.06           C  
ANISOU 2015  CG BGLN A 192     2865   1528   2470    392   -173    338       C  
ATOM   2016  CD AGLN A 192      -4.750 -10.931 -14.592  0.47 16.88           C  
ANISOU 2016  CD AGLN A 192     3026   1356   2032   -158    262   -178       C  
ATOM   2017  CD BGLN A 192      -7.228 -10.809 -14.080  0.53 19.20           C  
ANISOU 2017  CD BGLN A 192     2780   1713   2802    389   -342    334       C  
ATOM   2018  OE1AGLN A 192      -5.764 -11.051 -15.280  0.47 17.59           O  
ANISOU 2018  OE1AGLN A 192     3394   1415   1873   -463    129    -44       O  
ATOM   2019  OE1BGLN A 192      -8.274 -10.776 -13.425  0.53 18.91           O  
ANISOU 2019  OE1BGLN A 192     2120   2179   2887    267    -54    300       O  
ATOM   2020  NE2AGLN A 192      -3.524 -10.986 -15.107  0.47 18.77           N  
ANISOU 2020  NE2AGLN A 192     2966   1799   2366    111    523   -111       N  
ATOM   2021  NE2BGLN A 192      -7.215 -10.676 -15.406  0.53 20.76           N  
ANISOU 2021  NE2BGLN A 192     3341   1403   3145    455   -600    222       N  
ATOM   2022  N   GLY A 193      -4.420 -14.160 -10.165  1.00  9.57           N  
ANISOU 2022  N   GLY A 193     1380    867   1389     93     10    -87       N  
ATOM   2023  CA  GLY A 193      -4.601 -14.970  -8.980  1.00  9.35           C  
ANISOU 2023  CA  GLY A 193     1273    954   1326     60     25   -145       C  
ATOM   2024  C   GLY A 193      -4.060 -16.387  -9.090  1.00  8.08           C  
ANISOU 2024  C   GLY A 193      961    988   1123      0     63    -99       C  
ATOM   2025  O   GLY A 193      -3.930 -17.067  -8.063  1.00  8.97           O  
ANISOU 2025  O   GLY A 193     1277   1003   1127    -65     75   -108       O  
ATOM   2026  HA3 GLY A 193      -5.542 -15.008  -8.745  1.00 11.22           H  
ATOM   2027  N   ASP A 194      -3.745 -16.834 -10.306  1.00  7.82           N  
ANISOU 2027  N   ASP A 194      970    974   1028    121     -5    -62       N  
ATOM   2028  CA  ASP A 194      -3.074 -18.102 -10.519  1.00  7.44           C  
ANISOU 2028  CA  ASP A 194      909    928    989     35    -14    -53       C  
ATOM   2029  C   ASP A 194      -1.562 -17.976 -10.417  1.00  7.09           C  
ANISOU 2029  C   ASP A 194      941    830    923     16     47    -64       C  
ATOM   2030  O   ASP A 194      -0.868 -18.993 -10.296  1.00  7.45           O  
ANISOU 2030  O   ASP A 194      875    847   1110    -18     23   -138       O  
ATOM   2031  CB  ASP A 194      -3.437 -18.681 -11.895  1.00  8.00           C  
ANISOU 2031  CB  ASP A 194      933   1038   1070     45      4    -82       C  
ATOM   2032  CG  ASP A 194      -4.891 -19.099 -12.009  1.00  8.07           C  
ANISOU 2032  CG  ASP A 194     1047    988   1031     16    -35     17       C  
ATOM   2033  OD1 ASP A 194      -5.418 -19.658 -11.035  1.00  8.43           O  
ANISOU 2033  OD1 ASP A 194      968   1119   1117    -27    -48     63       O  
ATOM   2034  OD2 ASP A 194      -5.459 -18.882 -13.101  1.00  8.79           O  
ANISOU 2034  OD2 ASP A 194     1000   1197   1142    -79   -140     26       O  
ATOM   2035  H   ASP A 194      -3.916 -16.408 -11.033  1.00  9.39           H  
ATOM   2036  HA  ASP A 194      -3.368 -18.732  -9.843  1.00  8.93           H  
ATOM   2037  HB2 ASP A 194      -3.267 -18.008 -12.573  1.00  9.60           H  
ATOM   2038  HB3 ASP A 194      -2.888 -19.463 -12.062  1.00  9.60           H  
ATOM   2039  N   SER A 195      -1.043 -16.747 -10.500  1.00  7.57           N  
ANISOU 2039  N   SER A 195      942    873   1060     17    -15    -28       N  
ATOM   2040  CA  SER A 195       0.387 -16.482 -10.490  1.00  7.57           C  
ANISOU 2040  CA  SER A 195     1022    811   1043    -49    -60     92       C  
ATOM   2041  C   SER A 195       1.088 -17.231  -9.380  1.00  6.77           C  
ANISOU 2041  C   SER A 195     1003    663    907    -88    -32    -95       C  
ATOM   2042  O   SER A 195       0.606 -17.318  -8.251  1.00  7.19           O  
ANISOU 2042  O   SER A 195     1007    812    911    -47     35   -110       O  
ATOM   2043  CB  SER A 195       0.632 -15.003 -10.243  1.00 13.06           C  
ANISOU 2043  CB  SER A 195     1642    922   2399   -138   -815    484       C  
ATOM   2044  OG  SER A 195       0.327 -14.252 -11.374  1.00 18.93           O  
ANISOU 2044  OG  SER A 195     2382   1622   3188   -574  -1155   1018       O  
ATOM   2045  N   GLY A 196       2.262 -17.755  -9.723  1.00  6.43           N  
ANISOU 2045  N   GLY A 196      889    632    922    -12      5   -103       N  
ATOM   2046  CA  GLY A 196       3.071 -18.490  -8.775  1.00  7.11           C  
ANISOU 2046  CA  GLY A 196     1016    729    957    -13    -78    -60       C  
ATOM   2047  C   GLY A 196       2.767 -19.971  -8.702  1.00  6.79           C  
ANISOU 2047  C   GLY A 196      875    766    938     -1     54    -81       C  
ATOM   2048  O   GLY A 196       3.556 -20.737  -8.129  1.00  7.28           O  
ANISOU 2048  O   GLY A 196      939    833    995     10     17    -19       O  
ATOM   2049  HA3 GLY A 196       2.977 -18.104  -7.890  1.00  8.53           H  
ATOM   2050  N   GLY A 197       1.630 -20.396  -9.245  1.00  7.08           N  
ANISOU 2050  N   GLY A 197      965    686   1040     14     43   -110       N  
ATOM   2051  CA  GLY A 197       1.213 -21.784  -9.173  1.00  7.43           C  
ANISOU 2051  CA  GLY A 197     1037    660   1125    -27     64    -87       C  
ATOM   2052  C   GLY A 197       1.881 -22.668 -10.199  1.00  7.05           C  
ANISOU 2052  C   GLY A 197      876    786   1018      8    -57    -81       C  
ATOM   2053  O   GLY A 197       2.674 -22.227 -11.041  1.00  7.55           O  
ANISOU 2053  O   GLY A 197      989    757   1123     14     63    -83       O  
ATOM   2054  H   GLY A 197       1.077 -19.889  -9.666  1.00  8.50           H  
ATOM   2055  N   PRO A 198       1.553 -23.953 -10.117  1.00  7.16           N  
ANISOU 2055  N   PRO A 198      928    662   1133    -51     26   -122       N  
ATOM   2056  CA  PRO A 198       2.283 -24.985 -10.862  1.00  7.37           C  
ANISOU 2056  CA  PRO A 198      942    668   1188     65     21   -124       C  
ATOM   2057  C   PRO A 198       1.808 -25.208 -12.287  1.00  7.01           C  
ANISOU 2057  C   PRO A 198      925    604   1134     23    -41   -131       C  
ATOM   2058  O   PRO A 198       0.620 -25.134 -12.614  1.00  8.05           O  
ANISOU 2058  O   PRO A 198     1039    869   1152     57    -43   -171       O  
ATOM   2059  CB  PRO A 198       1.977 -26.255 -10.055  1.00  7.98           C  
ANISOU 2059  CB  PRO A 198     1071    764   1197     51   -134   -148       C  
ATOM   2060  CG  PRO A 198       0.593 -25.968  -9.450  1.00  8.18           C  
ANISOU 2060  CG  PRO A 198     1045    807   1256    -32     60     14       C  
ATOM   2061  CD  PRO A 198       0.632 -24.511  -9.100  1.00  7.78           C  
ANISOU 2061  CD  PRO A 198     1114    703   1140    -41    129    -79       C  
ATOM   2062  HB2 PRO A 198       1.946 -27.024 -10.645  1.00  9.58           H  
ATOM   2063  HB3 PRO A 198       2.643 -26.375  -9.360  1.00  9.58           H  
ATOM   2064  HG2 PRO A 198      -0.097 -26.147 -10.108  1.00  9.82           H  
ATOM   2065  HG3 PRO A 198       0.462 -26.511  -8.656  1.00  9.82           H  
ATOM   2066  N   VAL A 199       2.785 -25.627 -13.097  1.00  7.79           N  
ANISOU 2066  N   VAL A 199     1023    718   1220     95     63   -220       N  
ATOM   2067  CA  VAL A 199       2.597 -26.293 -14.377  1.00  7.45           C  
ANISOU 2067  CA  VAL A 199      999    753   1077    -62     11   -172       C  
ATOM   2068  C   VAL A 199       3.337 -27.623 -14.259  1.00  7.50           C  
ANISOU 2068  C   VAL A 199     1081    759   1008     89     19   -144       C  
ATOM   2069  O   VAL A 199       4.577 -27.633 -14.196  1.00  7.79           O  
ANISOU 2069  O   VAL A 199      982    755   1221    110     14   -141       O  
ATOM   2070  CB  VAL A 199       3.159 -25.460 -15.544  1.00  8.25           C  
ANISOU 2070  CB  VAL A 199     1097    782   1255    105      8    -25       C  
ATOM   2071  CG1 VAL A 199       2.923 -26.188 -16.859  1.00  9.90           C  
ANISOU 2071  CG1 VAL A 199     1301   1188   1274     88     85     82       C  
ATOM   2072  CG2 VAL A 199       2.591 -24.045 -15.554  1.00 10.06           C  
ANISOU 2072  CG2 VAL A 199     1362    968   1492     63     29     62       C  
ATOM   2073  HA  VAL A 199       1.655 -26.465 -14.531  1.00  8.93           H  
ATOM   2074  HB  VAL A 199       4.119 -25.382 -15.427  1.00  9.90           H  
ATOM   2075 HG13 VAL A 199       1.970 -26.317 -16.982  1.00 11.89           H  
ATOM   2076 HG22 VAL A 199       1.626 -24.093 -15.646  1.00 12.07           H  
ATOM   2077 HG23 VAL A 199       2.823 -23.606 -14.721  1.00 12.07           H  
ATOM   2078  N   VAL A 200       2.591 -28.727 -14.188  1.00  7.54           N  
ANISOU 2078  N   VAL A 200     1095    650   1122     31     49   -147       N  
ATOM   2079  CA  VAL A 200       3.166 -30.048 -13.941  1.00  7.93           C  
ANISOU 2079  CA  VAL A 200     1092    728   1194     79    -31   -127       C  
ATOM   2080  C   VAL A 200       2.984 -30.907 -15.182  1.00  8.13           C  
ANISOU 2080  C   VAL A 200     1182    673   1235     58    -76    -68       C  
ATOM   2081  O   VAL A 200       1.874 -31.028 -15.709  1.00  8.89           O  
ANISOU 2081  O   VAL A 200     1231    916   1229     91   -130   -185       O  
ATOM   2082  CB  VAL A 200       2.559 -30.695 -12.678  1.00  8.35           C  
ANISOU 2082  CB  VAL A 200     1163    847   1163     49    -35     26       C  
ATOM   2083  CG1 VAL A 200       2.820 -32.188 -12.603  1.00  9.82           C  
ANISOU 2083  CG1 VAL A 200     1478    892   1360    123    -95    113       C  
ATOM   2084  CG2 VAL A 200       3.089 -29.975 -11.461  1.00  9.40           C  
ANISOU 2084  CG2 VAL A 200     1411   1033   1127     82     61   -124       C  
ATOM   2085  HA  VAL A 200       4.118 -29.949 -13.791  1.00  9.52           H  
ATOM   2086  HB  VAL A 200       1.598 -30.567 -12.697  1.00 10.02           H  
ATOM   2087 HG11 VAL A 200       2.417 -32.539 -11.793  1.00 11.78           H  
ATOM   2088 HG13 VAL A 200       3.778 -32.341 -12.590  1.00 11.78           H  
ATOM   2089 HG21 VAL A 200       2.770 -30.425 -10.663  1.00 11.28           H  
ATOM   2090  N   CYS A 201       4.065 -31.523 -15.629  1.00  8.97           N  
ANISOU 2090  N   CYS A 201     1259    826   1321    116    -45   -329       N  
ATOM   2091  CA  CYS A 201       4.058 -32.299 -16.864  1.00  9.81           C  
ANISOU 2091  CA  CYS A 201     1412    986   1330    116     29   -349       C  
ATOM   2092  C   CYS A 201       4.736 -33.620 -16.544  1.00 10.83           C  
ANISOU 2092  C   CYS A 201     1579   1015   1523    188     64   -399       C  
ATOM   2093  O   CYS A 201       5.865 -33.627 -16.047  1.00 11.58           O  
ANISOU 2093  O   CYS A 201     1415   1078   1906    303     -4   -273       O  
ATOM   2094  CB  CYS A 201       4.826 -31.558 -17.967  1.00 11.79           C  
ANISOU 2094  CB  CYS A 201     1602   1453   1423    175     47   -296       C  
ATOM   2095  SG  CYS A 201       4.597 -29.761 -18.012  1.00 12.10           S  
ANISOU 2095  SG  CYS A 201     1409   1468   1719     36    -25     50       S  
ATOM   2096  H   CYS A 201       4.828 -31.509 -15.232  1.00 10.76           H  
ATOM   2097  HB3 CYS A 201       4.564 -31.916 -18.829  1.00 14.14           H  
ATOM   2098  N   SER A 202       4.047 -34.732 -16.798  1.00 11.93           N  
ANISOU 2098  N   SER A 202     1955    967   1611     44     20   -455       N  
ATOM   2099  CA  SER A 202       4.576 -36.054 -16.479  1.00 14.24           C  
ANISOU 2099  CA  SER A 202     2438    997   1977    162     53   -523       C  
ATOM   2100  C   SER A 202       5.108 -36.140 -15.048  1.00 13.15           C  
ANISOU 2100  C   SER A 202     2313    749   1935     58     53   -236       C  
ATOM   2101  O   SER A 202       6.138 -36.761 -14.773  1.00 15.32           O  
ANISOU 2101  O   SER A 202     2580    950   2291    405   -222   -184       O  
ATOM   2102  CB  SER A 202       5.620 -36.467 -17.506  1.00 18.11           C  
ANISOU 2102  CB  SER A 202     3244   1404   2232    555    117   -609       C  
ATOM   2103  OG  SER A 202       5.042 -36.455 -18.802  1.00 21.92           O  
ANISOU 2103  OG  SER A 202     4105   2022   2201    853    444   -622       O  
ATOM   2104  N   GLY A 203       4.383 -35.537 -14.114  1.00 12.84           N  
ANISOU 2104  N   GLY A 203     2081    909   1887     18   -146   -229       N  
ATOM   2105  CA  GLY A 203       4.742 -35.658 -12.711  1.00 13.60           C  
ANISOU 2105  CA  GLY A 203     2221    991   1954   -148    -18   -105       C  
ATOM   2106  C   GLY A 203       5.908 -34.801 -12.258  1.00 12.66           C  
ANISOU 2106  C   GLY A 203     2183    885   1743    239   -274   -278       C  
ATOM   2107  O   GLY A 203       6.418 -35.008 -11.153  1.00 15.99           O  
ANISOU 2107  O   GLY A 203     2847   1463   1768    119   -408     60       O  
ATOM   2108  HA3 GLY A 203       4.929 -36.585 -12.495  1.00 16.32           H  
ATOM   2109  N   LYS A 204       6.333 -33.820 -13.068  1.00 10.90           N  
ANISOU 2109  N   LYS A 204     1606    718   1817    116   -198   -231       N  
ATOM   2110  CA  LYS A 204       7.433 -32.930 -12.714  1.00 12.07           C  
ANISOU 2110  CA  LYS A 204     1513    945   2127    386   -167   -349       C  
ATOM   2111  C   LYS A 204       6.969 -31.483 -12.828  1.00  9.77           C  
ANISOU 2111  C   LYS A 204     1292    836   1585    223   -119   -164       C  
ATOM   2112  O   LYS A 204       6.226 -31.118 -13.750  1.00  9.91           O  
ANISOU 2112  O   LYS A 204     1262    866   1639    167   -190   -211       O  
ATOM   2113  CB  LYS A 204       8.671 -33.093 -13.660  1.00 15.09           C  
ANISOU 2113  CB  LYS A 204     1496   1302   2935    451    -13   -539       C  
ATOM   2114  CG  LYS A 204       9.085 -34.500 -13.931  1.00 19.61           C  
ANISOU 2114  CG  LYS A 204     2322   1384   3745    623    287   -474       C  
ATOM   2115  CD  LYS A 204       9.671 -35.147 -12.731  1.00 24.90           C  
ANISOU 2115  CD  LYS A 204     3368   1715   4378    918    291   -308       C  
ATOM   2116  CE  LYS A 204       9.894 -36.623 -13.053  1.00 29.28           C  
ANISOU 2116  CE  LYS A 204     4270   1900   4954    962    190    -91       C  
ATOM   2117  NZ  LYS A 204      11.047 -37.170 -12.336  1.00 29.94           N  
ANISOU 2117  NZ  LYS A 204     4463   1834   5078    859    190   -184       N  
ATOM   2118  HB2 LYS A 204       8.476 -32.668 -14.510  1.00 18.11           H  
ATOM   2119  HD3 LYS A 204       9.036 -35.092 -12.000  1.00 29.88           H  
ATOM   2120  N   LEU A 209       7.482 -30.634 -11.935  1.00  8.75           N  
ANISOU 2120  N   LEU A 209     1145    770   1410    178      9    -99       N  
ATOM   2121  CA  LEU A 209       7.182 -29.200 -11.960  1.00  8.17           C  
ANISOU 2121  CA  LEU A 209     1030    832   1242    129     69    -68       C  
ATOM   2122  C   LEU A 209       8.027 -28.522 -13.047  1.00  8.28           C  
ANISOU 2122  C   LEU A 209      922    955   1271    175    107   -154       C  
ATOM   2123  O   LEU A 209       9.193 -28.192 -12.829  1.00 10.93           O  
ANISOU 2123  O   LEU A 209     1178   1628   1347     15     82    244       O  
ATOM   2124  CB  LEU A 209       7.464 -28.578 -10.598  1.00  8.21           C  
ANISOU 2124  CB  LEU A 209     1093    868   1158     67    -31    -46       C  
ATOM   2125  CG  LEU A 209       7.101 -27.094 -10.507  1.00  8.66           C  
ANISOU 2125  CG  LEU A 209     1246    820   1224    102    -26   -114       C  
ATOM   2126  CD1 LEU A 209       5.585 -26.884 -10.566  1.00  9.36           C  
ANISOU 2126  CD1 LEU A 209     1376    925   1254    215   -123   -159       C  
ATOM   2127  CD2 LEU A 209       7.660 -26.492  -9.228  1.00 10.17           C  
ANISOU 2127  CD2 LEU A 209     1374    962   1529    102   -126   -290       C  
ATOM   2128  HA  LEU A 209       6.244 -29.069 -12.171  1.00  9.80           H  
ATOM   2129  HB2 LEU A 209       6.956 -29.053  -9.922  1.00  9.85           H  
ATOM   2130  HG  LEU A 209       7.498 -26.625 -11.257  1.00 10.39           H  
ATOM   2131 HD11 LEU A 209       5.391 -25.943 -10.435  1.00 11.23           H  
ATOM   2132 HD12 LEU A 209       5.260 -27.172 -11.434  1.00 11.23           H  
ATOM   2133 HD21 LEU A 209       7.418 -25.553  -9.189  1.00 12.21           H  
ATOM   2134 HD23 LEU A 209       8.625 -26.586  -9.231  1.00 12.21           H  
ATOM   2135  N   GLN A 210       7.424 -28.265 -14.212  1.00  8.02           N  
ANISOU 2135  N   GLN A 210     1178    760   1109    109     15    -96       N  
ATOM   2136  CA  GLN A 210       8.153 -27.648 -15.316  1.00  8.06           C  
ANISOU 2136  CA  GLN A 210     1110    801   1151    100     84   -205       C  
ATOM   2137  C   GLN A 210       7.926 -26.148 -15.424  1.00  7.55           C  
ANISOU 2137  C   GLN A 210      959    852   1057     45     68   -164       C  
ATOM   2138  O   GLN A 210       8.748 -25.454 -16.028  1.00  8.04           O  
ANISOU 2138  O   GLN A 210     1013    897   1146     98     49   -162       O  
ATOM   2139  CB  GLN A 210       7.806 -28.325 -16.656  1.00  8.69           C  
ANISOU 2139  CB  GLN A 210     1252    885   1164    119     35   -198       C  
ATOM   2140  CG  GLN A 210       8.240 -29.776 -16.738  1.00 10.10           C  
ANISOU 2140  CG  GLN A 210     1557    941   1338    194    120   -351       C  
ATOM   2141  CD  GLN A 210       9.728 -29.984 -16.979  1.00 10.00           C  
ANISOU 2141  CD  GLN A 210     1506   1013   1279    221    188   -228       C  
ATOM   2142  OE1 GLN A 210      10.532 -29.051 -17.006  1.00 11.47           O  
ANISOU 2142  OE1 GLN A 210     1401   1096   1860    250    380   -108       O  
ATOM   2143  NE2 GLN A 210      10.103 -31.243 -17.154  1.00 11.17           N  
ANISOU 2143  NE2 GLN A 210     1490   1125   1631    339    108   -259       N  
ATOM   2144  HA  GLN A 210       9.101 -27.783 -15.164  1.00  9.67           H  
ATOM   2145  HB2 GLN A 210       6.845 -28.295 -16.782  1.00 10.43           H  
ATOM   2146  HB3 GLN A 210       8.247 -27.843 -17.374  1.00 10.43           H  
ATOM   2147  HG3 GLN A 210       7.756 -30.210 -17.458  1.00 12.12           H  
ATOM   2148 HE22 GLN A 210      10.931 -31.429 -17.294  1.00 13.41           H  
ATOM   2149  N   GLY A 211       6.834 -25.620 -14.884  1.00  7.74           N  
ANISOU 2149  N   GLY A 211     1050    715   1175     36     79    -42       N  
ATOM   2150  CA  GLY A 211       6.553 -24.206 -15.013  1.00  7.65           C  
ANISOU 2150  CA  GLY A 211     1058    737   1112     80     75    -69       C  
ATOM   2151  C   GLY A 211       5.957 -23.602 -13.763  1.00  7.02           C  
ANISOU 2151  C   GLY A 211      925    743   1000     49    -13   -125       C  
ATOM   2152  O   GLY A 211       5.405 -24.299 -12.901  1.00  7.83           O  
ANISOU 2152  O   GLY A 211     1112    809   1053    -12     42    -48       O  
ATOM   2153  H   GLY A 211       6.244 -26.061 -14.441  1.00  9.29           H  
ATOM   2154  HA2 GLY A 211       7.375 -23.733 -15.218  1.00  9.18           H  
ATOM   2155  HA3 GLY A 211       5.931 -24.068 -15.745  1.00  9.18           H  
ATOM   2156  N   ILE A 212       6.030 -22.266 -13.729  1.00  7.08           N  
ANISOU 2156  N   ILE A 212      953    731   1008     31     10   -147       N  
ATOM   2157  CA  ILE A 212       5.383 -21.438 -12.727  1.00  6.87           C  
ANISOU 2157  CA  ILE A 212      967    773    871     23     56    -84       C  
ATOM   2158  C   ILE A 212       4.545 -20.405 -13.478  1.00  6.73           C  
ANISOU 2158  C   ILE A 212      955    740    862    -62    -23   -136       C  
ATOM   2159  O   ILE A 212       5.047 -19.746 -14.398  1.00  7.06           O  
ANISOU 2159  O   ILE A 212      937    795    950     42     36    -94       O  
ATOM   2160  CB  ILE A 212       6.428 -20.711 -11.847  1.00  7.25           C  
ANISOU 2160  CB  ILE A 212      956    893    905     58     66   -160       C  
ATOM   2161  CG1 ILE A 212       7.324 -21.719 -11.128  1.00  9.52           C  
ANISOU 2161  CG1 ILE A 212     1149   1327   1143    383   -214   -358       C  
ATOM   2162  CG2 ILE A 212       5.756 -19.780 -10.854  1.00  7.62           C  
ANISOU 2162  CG2 ILE A 212      971    916   1008     49     13   -134       C  
ATOM   2163  CD1 ILE A 212       8.596 -21.082 -10.586  1.00 11.66           C  
ANISOU 2163  CD1 ILE A 212     1155   1832   1444    406   -335   -623       C  
ATOM   2164  HA  ILE A 212       4.805 -21.976 -12.164  1.00  8.25           H  
ATOM   2165  HB  ILE A 212       6.988 -20.174 -12.429  1.00  8.70           H  
ATOM   2166 HG12 ILE A 212       6.836 -22.100 -10.382  1.00 11.43           H  
ATOM   2167 HG13 ILE A 212       7.579 -22.417 -11.751  1.00 11.43           H  
ATOM   2168 HG21 ILE A 212       6.438 -19.342 -10.321  1.00  9.15           H  
ATOM   2169 HG22 ILE A 212       5.240 -19.119 -11.341  1.00  9.15           H  
ATOM   2170 HG23 ILE A 212       5.171 -20.301 -10.281  1.00  9.15           H  
ATOM   2171 HD11 ILE A 212       9.149 -21.771 -10.186  1.00 13.99           H  
ATOM   2172  N   VAL A 213       3.279 -20.226 -13.075  1.00  6.91           N  
ANISOU 2172  N   VAL A 213      883    762    983      6     51    -44       N  
ATOM   2173  CA  VAL A 213       2.426 -19.211 -13.701  1.00  7.03           C  
ANISOU 2173  CA  VAL A 213      946    791    933     -2    -10   -113       C  
ATOM   2174  C   VAL A 213       3.071 -17.842 -13.530  1.00  6.73           C  
ANISOU 2174  C   VAL A 213      854    841    860     48    -12    -77       C  
ATOM   2175  O   VAL A 213       3.281 -17.385 -12.399  1.00  7.33           O  
ANISOU 2175  O   VAL A 213      975    880    931    -40     12    -73       O  
ATOM   2176  CB  VAL A 213       1.022 -19.224 -13.079  1.00  7.41           C  
ANISOU 2176  CB  VAL A 213      888    977    950     33      2   -105       C  
ATOM   2177  CG1 VAL A 213       0.150 -18.170 -13.721  1.00  8.33           C  
ANISOU 2177  CG1 VAL A 213      909   1173   1082    130      8   -112       C  
ATOM   2178  CG2 VAL A 213       0.351 -20.601 -13.167  1.00  8.07           C  
ANISOU 2178  CG2 VAL A 213     1006    966   1096   -127     16   -112       C  
ATOM   2179  H   VAL A 213       2.897 -20.674 -12.449  1.00  8.30           H  
ATOM   2180  HA  VAL A 213       2.344 -19.397 -14.649  1.00  8.44           H  
ATOM   2181  HB  VAL A 213       1.102 -19.001 -12.139  1.00  8.89           H  
ATOM   2182 HG23 VAL A 213       0.896 -21.249 -12.694  1.00  9.69           H  
ATOM   2183  N   SER A 214       3.375 -17.162 -14.644  1.00  7.10           N  
ANISOU 2183  N   SER A 214      970    828    900    122    -10    -77       N  
ATOM   2184  CA  SER A 214       4.163 -15.931 -14.607  1.00  7.25           C  
ANISOU 2184  CA  SER A 214     1072    788    896    -32     66    -80       C  
ATOM   2185  C   SER A 214       3.403 -14.737 -15.187  1.00  7.74           C  
ANISOU 2185  C   SER A 214     1221    779    940     50     18    -96       C  
ATOM   2186  O   SER A 214       3.119 -13.795 -14.443  1.00  9.69           O  
ANISOU 2186  O   SER A 214     1683    954   1046    325    -36   -125       O  
ATOM   2187  CB  SER A 214       5.529 -16.157 -15.251  1.00  7.10           C  
ANISOU 2187  CB  SER A 214     1003    746    948    -19    -60    -35       C  
ATOM   2188  OG  SER A 214       6.320 -14.976 -15.216  1.00  7.71           O  
ANISOU 2188  OG  SER A 214     1110    934    883    -61    -50    -34       O  
ATOM   2189  H   SER A 214       3.133 -17.397 -15.435  1.00  8.52           H  
ATOM   2190  HA  SER A 214       4.331 -15.721 -13.675  1.00  8.70           H  
ATOM   2191  HB2 SER A 214       5.992 -16.860 -14.768  1.00  8.52           H  
ATOM   2192  HB3 SER A 214       5.400 -16.422 -16.175  1.00  8.52           H  
ATOM   2193  HG  SER A 214       6.441 -14.735 -14.421  1.00  9.25           H  
ATOM   2194  N   TRP A 215       3.092 -14.709 -16.487  1.00  7.65           N  
ANISOU 2194  N   TRP A 215     1004    838   1063     88    -13    -16       N  
ATOM   2195  CA  TRP A 215       2.471 -13.517 -17.065  1.00  8.08           C  
ANISOU 2195  CA  TRP A 215     1287    782   1003    200    -43    -37       C  
ATOM   2196  C   TRP A 215       1.771 -13.867 -18.368  1.00  8.33           C  
ANISOU 2196  C   TRP A 215     1223    809   1135    223     41     80       C  
ATOM   2197  O   TRP A 215       1.836 -14.981 -18.862  1.00  9.88           O  
ANISOU 2197  O   TRP A 215     1599    837   1320    313   -359    -84       O  
ATOM   2198  CB  TRP A 215       3.489 -12.383 -17.250  1.00  8.80           C  
ANISOU 2198  CB  TRP A 215     1496    786   1063     29    -70     -8       C  
ATOM   2199  CG  TRP A 215       4.619 -12.662 -18.229  1.00  8.40           C  
ANISOU 2199  CG  TRP A 215     1342    751   1100    -50    -22      9       C  
ATOM   2200  CD1 TRP A 215       5.758 -13.332 -17.967  1.00  8.27           C  
ANISOU 2200  CD1 TRP A 215     1318    838    988    -52     11    -12       C  
ATOM   2201  CD2 TRP A 215       4.702 -12.236 -19.600  1.00  8.81           C  
ANISOU 2201  CD2 TRP A 215     1456    839   1052     -8    -53     71       C  
ATOM   2202  NE1 TRP A 215       6.582 -13.349 -19.080  1.00  8.78           N  
ANISOU 2202  NE1 TRP A 215     1337    910   1089    -92    -74     -6       N  
ATOM   2203  CE2 TRP A 215       5.945 -12.681 -20.092  1.00  8.79           C  
ANISOU 2203  CE2 TRP A 215     1473    810   1058    -70     29     85       C  
ATOM   2204  CE3 TRP A 215       3.865 -11.497 -20.450  1.00 10.64           C  
ANISOU 2204  CE3 TRP A 215     1795   1097   1150    149     49    184       C  
ATOM   2205  CZ2 TRP A 215       6.359 -12.438 -21.403  1.00  9.85           C  
ANISOU 2205  CZ2 TRP A 215     1651    926   1165    -92     94    106       C  
ATOM   2206  CZ3 TRP A 215       4.278 -11.254 -21.748  1.00 11.96           C  
ANISOU 2206  CZ3 TRP A 215     2115   1128   1300     61   -136    382       C  
ATOM   2207  CH2 TRP A 215       5.505 -11.729 -22.213  1.00 11.32           C  
ANISOU 2207  CH2 TRP A 215     1966   1157   1180      7    133    143       C  
ATOM   2208  HA  TRP A 215       1.792 -13.198 -16.449  1.00  9.70           H  
ATOM   2209  HB2 TRP A 215       3.018 -11.597 -17.568  1.00 10.56           H  
ATOM   2210  HB3 TRP A 215       3.893 -12.191 -16.389  1.00 10.56           H  
ATOM   2211  HE3 TRP A 215       3.046 -11.177 -20.147  1.00 12.77           H  
ATOM   2212  HZ2 TRP A 215       7.175 -12.753 -21.719  1.00 11.82           H  
ATOM   2213  N  AGLY A 216       1.120 -12.872 -18.947  0.62 10.06           N  
ANISOU 2213  N  AGLY A 216     1575    987   1261    247   -311    -30       N  
ATOM   2214  N  BGLY A 216       1.087 -12.873 -18.901  0.38  9.94           N  
ANISOU 2214  N  BGLY A 216     1506    895   1376    459    -22     32       N  
ATOM   2215  CA AGLY A 216       0.518 -12.964 -20.269  0.62  9.87           C  
ANISOU 2215  CA AGLY A 216     1381   1111   1260    177   -436     95       C  
ATOM   2216  CA BGLY A 216       0.513 -12.951 -20.220  0.38 10.39           C  
ANISOU 2216  CA BGLY A 216     1513    885   1549    354     51    138       C  
ATOM   2217  C  AGLY A 216      -0.225 -11.663 -20.506  0.62 10.12           C  
ANISOU 2217  C  AGLY A 216     1281   1111   1451    239   -327    161       C  
ATOM   2218  C  BGLY A 216       0.055 -11.569 -20.634  0.38 11.42           C  
ANISOU 2218  C  BGLY A 216     1667    906   1765    372     -2    249       C  
ATOM   2219  O  AGLY A 216      -0.433 -10.860 -19.596  0.62 12.07           O  
ANISOU 2219  O  AGLY A 216     1727   1100   1760    433   -147   -167       O  
ATOM   2220  O  BGLY A 216       0.492 -10.558 -20.081  0.38 12.01           O  
ANISOU 2220  O  BGLY A 216     1893    837   1835    393   -111    307       O  
ATOM   2221  H  AGLY A 216       1.009 -12.103 -18.579  0.62 12.07           H  
ATOM   2222  H  BGLY A 216       0.940 -12.124 -18.504  0.38 11.93           H  
ATOM   2223  HA3AGLY A 216      -0.115 -13.698 -20.295  0.62 11.85           H  
ATOM   2224  HA3BGLY A 216      -0.250 -13.548 -20.215  0.38 12.47           H  
ATOM   2225  N  ASER A 217      -0.660 -11.441 -21.736  0.62 11.19           N  
ANISOU 2225  N  ASER A 217     1368   1079   1804     -8   -518    285       N  
ATOM   2226  N  BSER A 217      -0.828 -11.520 -21.622  0.38 13.94           N  
ANISOU 2226  N  BSER A 217     2044   1107   2146    506   -184    269       N  
ATOM   2227  CA ASER A 217      -1.464 -10.243 -21.978  0.62 12.31           C  
ANISOU 2227  CA ASER A 217     1432   1249   1995    120   -506    385       C  
ATOM   2228  CA BSER A 217      -1.493 -10.275 -22.008  0.38 14.36           C  
ANISOU 2228  CA BSER A 217     2048   1150   2259    510   -138    435       C  
ATOM   2229  C  ASER A 217      -2.944 -10.580 -21.811  0.62 12.73           C  
ANISOU 2229  C  ASER A 217     1597   1112   2129    -14   -507    281       C  
ATOM   2230  C  BSER A 217      -2.988 -10.527 -21.856  0.38 13.45           C  
ANISOU 2230  C  BSER A 217     1939    958   2214    412   -409    411       C  
ATOM   2231  O  ASER A 217      -3.523 -11.301 -22.634  0.62 13.41           O  
ANISOU 2231  O  ASER A 217     1594   1338   2162   -133   -487    326       O  
ATOM   2232  O  BSER A 217      -3.612 -11.153 -22.719  0.38 14.41           O  
ANISOU 2232  O  BSER A 217     1996   1295   2184    434   -649    485       O  
ATOM   2233  CB ASER A 217      -1.179  -9.655 -23.350  0.62 13.83           C  
ANISOU 2233  CB ASER A 217     1564   1581   2111    -88   -400    586       C  
ATOM   2234  CB BSER A 217      -1.121  -9.885 -23.433  0.38 15.94           C  
ANISOU 2234  CB BSER A 217     2151   1555   2350    408    175    577       C  
ATOM   2235  OG ASER A 217      -1.943  -8.479 -23.505  0.62 16.51           O  
ANISOU 2235  OG ASER A 217     2181   1641   2452    174   -271    943       O  
ATOM   2236  OG BSER A 217       0.207  -9.380 -23.500  0.38 16.76           O  
ANISOU 2236  OG BSER A 217     2281   1593   2495    479    304    519       O  
ATOM   2237  N   GLY A 219      -3.554 -10.077 -20.745  1.00 13.81           N  
ANISOU 2237  N   GLY A 219     1683    986   2579    309   -229    208       N  
ATOM   2238  CA  GLY A 219      -4.897 -10.552 -20.452  1.00 14.02           C  
ANISOU 2238  CA  GLY A 219     1699   1108   2520    118   -126     28       C  
ATOM   2239  C   GLY A 219      -4.863 -12.052 -20.186  1.00 12.30           C  
ANISOU 2239  C   GLY A 219     1692    986   1993    211   -184     82       C  
ATOM   2240  O   GLY A 219      -3.816 -12.645 -19.887  1.00 12.59           O  
ANISOU 2240  O   GLY A 219     1815   1011   1956    230   -258     28       O  
ATOM   2241  HA2 GLY A 219      -5.246 -10.099 -19.668  1.00 16.82           H  
ATOM   2242  HA3 GLY A 219      -5.483 -10.377 -21.205  1.00 16.82           H  
ATOM   2243  N  ACYS A 220      -6.052 -12.657 -20.298  0.76 11.85           N  
ANISOU 2243  N  ACYS A 220     1982    917   1602    269   -144    106       N  
ATOM   2244  N  BCYS A 220      -6.020 -12.686 -20.276  0.24 12.68           N  
ANISOU 2244  N  BCYS A 220     1840   1066   1910    151    -64     95       N  
ATOM   2245  CA ACYS A 220      -6.246 -14.091 -20.074  0.76 11.81           C  
ANISOU 2245  CA ACYS A 220     2066   1053   1366     78   -212     99       C  
ATOM   2246  CA BCYS A 220      -6.023 -14.131 -20.113  0.24 12.85           C  
ANISOU 2246  CA BCYS A 220     1959   1076   1846    -66     28    165       C  
ATOM   2247  C  ACYS A 220      -7.071 -14.665 -21.209  0.76 11.79           C  
ANISOU 2247  C  ACYS A 220     1789   1111   1580    158      9    310       C  
ATOM   2248  C  BCYS A 220      -7.057 -14.754 -21.038  0.24 11.59           C  
ANISOU 2248  C  BCYS A 220     1721   1077   1606      1     59    438       C  
ATOM   2249  O  ACYS A 220      -8.101 -14.084 -21.578  0.76 12.21           O  
ANISOU 2249  O  ACYS A 220     1708   1225   1705    371    -59    283       O  
ATOM   2250  O  BCYS A 220      -8.182 -14.256 -21.149  0.24 11.55           O  
ANISOU 2250  O  BCYS A 220     1807   1168   1412     86     45    758       O  
ATOM   2251  CB ACYS A 220      -7.024 -14.359 -18.777  0.76 13.02           C  
ANISOU 2251  CB ACYS A 220     2372   1169   1405    -28   -253    177       C  
ATOM   2252  CB BCYS A 220      -6.189 -14.557 -18.639  0.24 14.56           C  
ANISOU 2252  CB BCYS A 220     2241   1181   2111     -4     45    144       C  
ATOM   2253  SG ACYS A 220      -6.315 -13.486 -17.396  0.76 13.51           S  
ANISOU 2253  SG ACYS A 220     2540   1089   1504     25   -333    127       S  
ATOM   2254  SG BCYS A 220      -7.796 -14.223 -17.887  0.24 15.52           S  
ANISOU 2254  SG BCYS A 220     2353   1210   2332    -16     64    155       S  
ATOM   2255  H  ACYS A 220      -6.777 -12.245 -20.508  0.76 14.22           H  
ATOM   2256  H  BCYS A 220      -6.786 -12.324 -20.424  0.24 15.21           H  
ATOM   2257  N   ALA A 221      -6.643 -15.810 -21.735  1.00 10.67           N  
ANISOU 2257  N   ALA A 221     1564   1007   1483     17   -152    210       N  
ATOM   2258  CA  ALA A 221      -7.468 -16.570 -22.672  1.00 11.40           C  
ANISOU 2258  CA  ALA A 221     1522   1308   1500    -61   -260    251       C  
ATOM   2259  C   ALA A 221      -7.777 -15.815 -23.966  1.00 12.18           C  
ANISOU 2259  C   ALA A 221     1668   1323   1635    -81   -247    304       C  
ATOM   2260  O   ALA A 221      -8.729 -16.164 -24.659  1.00 13.89           O  
ANISOU 2260  O   ALA A 221     1973   1530   1776    -85   -542    379       O  
ATOM   2261  CB  ALA A 221      -8.742 -17.106 -21.999  1.00 12.55           C  
ANISOU 2261  CB  ALA A 221     1709   1452   1606   -188   -169    265       C  
ATOM   2262  N   GLN A 221A     -6.977 -14.817 -24.305  1.00 12.48           N  
ANISOU 2262  N   GLN A 221A    1776   1429   1536   -123   -257    447       N  
ATOM   2263  CA  GLN A 221A     -7.166 -14.082 -25.551  1.00 14.26           C  
ANISOU 2263  CA  GLN A 221A    2033   1643   1742     26   -267    558       C  
ATOM   2264  C   GLN A 221A     -6.506 -14.826 -26.706  1.00 13.46           C  
ANISOU 2264  C   GLN A 221A    1635   1823   1658     30   -221    487       C  
ATOM   2265  O   GLN A 221A     -5.462 -15.468 -26.546  1.00 14.09           O  
ANISOU 2265  O   GLN A 221A    1907   1867   1579     94   -387    428       O  
ATOM   2266  CB  GLN A 221A     -6.553 -12.683 -25.444  1.00 15.54           C  
ANISOU 2266  CB  GLN A 221A    2358   1560   1986    -60     25    691       C  
ATOM   2267  CG  GLN A 221A     -7.087 -11.871 -24.287  1.00 19.21           C  
ANISOU 2267  CG  GLN A 221A    2860   1801   2637    488   -117    914       C  
ATOM   2268  CD  GLN A 221A     -8.555 -11.688 -24.398  1.00 24.00           C  
ANISOU 2268  CD  GLN A 221A    3506   2608   3007   1223   -188    993       C  
ATOM   2269  OE1 GLN A 221A     -9.022 -11.026 -25.329  1.00 26.22           O  
ANISOU 2269  OE1 GLN A 221A    3607   3095   3259   1539    -94   1053       O  
ATOM   2270  NE2 GLN A 221A     -9.314 -12.281 -23.479  1.00 26.45           N  
ANISOU 2270  NE2 GLN A 221A    3828   2890   3331   1375   -251    766       N  
ATOM   2271  N   LYS A 222      -7.099 -14.681 -27.889  1.00 14.98           N  
ANISOU 2271  N   LYS A 222     1877   2301   1513     54   -445    556       N  
ATOM   2272  CA  LYS A 222      -6.506 -15.259 -29.080  1.00 15.64           C  
ANISOU 2272  CA  LYS A 222     1893   2594   1454   -142   -416    567       C  
ATOM   2273  C   LYS A 222      -5.079 -14.744 -29.256  1.00 14.76           C  
ANISOU 2273  C   LYS A 222     1825   2215   1566    -53   -367    729       C  
ATOM   2274  O   LYS A 222      -4.797 -13.542 -29.119  1.00 15.84           O  
ANISOU 2274  O   LYS A 222     2064   2131   1821    129   -312    687       O  
ATOM   2275  CB  LYS A 222      -7.363 -14.905 -30.300  1.00 17.83           C  
ANISOU 2275  CB  LYS A 222     2190   3009   1575     16   -614    540       C  
ATOM   2276  CG  LYS A 222      -6.955 -15.563 -31.596  1.00 21.50           C  
ANISOU 2276  CG  LYS A 222     2840   3236   2093      5   -730    544       C  
ATOM   2277  CD  LYS A 222      -7.917 -15.193 -32.725  1.00 23.82           C  
ANISOU 2277  CD  LYS A 222     3306   3257   2489    -60   -740    477       C  
ATOM   2278  H   LYS A 222      -7.835 -14.258 -28.024  1.00 17.97           H  
ATOM   2279  HB2 LYS A 222      -8.279 -15.167 -30.117  1.00 21.39           H  
ATOM   2280  HB3 LYS A 222      -7.321 -13.946 -30.435  1.00 21.39           H  
ATOM   2281  N   ASN A 223      -4.180 -15.655 -29.602  1.00 14.82           N  
ANISOU 2281  N   ASN A 223     1804   2229   1596     41   -345    629       N  
ATOM   2282  CA  ASN A 223      -2.785 -15.340 -29.903  1.00 16.21           C  
ANISOU 2282  CA  ASN A 223     1993   2514   1652   -141   -184    555       C  
ATOM   2283  C   ASN A 223      -1.995 -14.803 -28.718  1.00 15.25           C  
ANISOU 2283  C   ASN A 223     1646   2469   1680    -39   -337    582       C  
ATOM   2284  O   ASN A 223      -0.898 -14.267 -28.906  1.00 18.19           O  
ANISOU 2284  O   ASN A 223     1882   3167   1863   -336   -272    789       O  
ATOM   2285  CB  ASN A 223      -2.668 -14.437 -31.130  1.00 20.05           C  
ANISOU 2285  CB  ASN A 223     2855   3312   1452   -296   -348    612       C  
ATOM   2286  CG  ASN A 223      -3.016 -15.174 -32.359  1.00 27.02           C  
ANISOU 2286  CG  ASN A 223     4047   4176   2044   -351   -361    706       C  
ATOM   2287  OD1 ASN A 223      -2.635 -16.340 -32.505  1.00 30.08           O  
ANISOU 2287  OD1 ASN A 223     4735   4660   2036    -16   -320    575       O  
ATOM   2288  ND2 ASN A 223      -3.800 -14.560 -33.222  1.00 28.83           N  
ANISOU 2288  ND2 ASN A 223     4018   4532   2403   -463   -802    571       N  
ATOM   2289  H   ASN A 223      -4.359 -16.493 -29.672  1.00 17.78           H  
ATOM   2290  N   LYS A 224      -2.516 -14.951 -27.504  1.00 13.51           N  
ANISOU 2290  N   LYS A 224     1821   1844   1468      3   -371    413       N  
ATOM   2291  CA  LYS A 224      -1.857 -14.465 -26.289  1.00 13.37           C  
ANISOU 2291  CA  LYS A 224     1692   1629   1761     64   -405    355       C  
ATOM   2292  C   LYS A 224      -1.902 -15.563 -25.233  1.00 12.05           C  
ANISOU 2292  C   LYS A 224     1491   1376   1711    -24   -526    372       C  
ATOM   2293  O   LYS A 224      -2.603 -15.458 -24.212  1.00 12.72           O  
ANISOU 2293  O   LYS A 224     1525   1463   1845     26   -218    295       O  
ATOM   2294  CB  LYS A 224      -2.499 -13.168 -25.802  1.00 14.83           C  
ANISOU 2294  CB  LYS A 224     1933   1616   2085    -65   -419    544       C  
ATOM   2295  CG  LYS A 224      -2.326 -11.998 -26.764  1.00 17.32           C  
ANISOU 2295  CG  LYS A 224     2030   1944   2605   -125   -172    853       C  
ATOM   2296  CD  LYS A 224      -0.840 -11.623 -26.851  1.00 19.72           C  
ANISOU 2296  CD  LYS A 224     2358   2367   2770   -223     19    988       C  
ATOM   2297  CE  LYS A 224      -0.642 -10.530 -27.881  1.00 20.70           C  
ANISOU 2297  CE  LYS A 224     2451   2470   2942   -236    520    922       C  
ATOM   2298  NZ  LYS A 224       0.776 -10.082 -28.012  1.00 19.13           N  
ANISOU 2298  NZ  LYS A 224     2383   2016   2871   -133    301    979       N  
ATOM   2299  N   PRO A 225      -1.128 -16.622 -25.434  1.00 12.25           N  
ANISOU 2299  N   PRO A 225     1742   1575   1337    106   -444    209       N  
ATOM   2300  CA  PRO A 225      -1.118 -17.719 -24.467  1.00 11.17           C  
ANISOU 2300  CA  PRO A 225     1464   1356   1425     65   -477    104       C  
ATOM   2301  C   PRO A 225      -0.390 -17.298 -23.207  1.00  9.67           C  
ANISOU 2301  C   PRO A 225     1265   1173   1235      4   -186    101       C  
ATOM   2302  O   PRO A 225       0.381 -16.346 -23.193  1.00 10.31           O  
ANISOU 2302  O   PRO A 225     1445   1257   1217   -170   -138    175       O  
ATOM   2303  CB  PRO A 225      -0.339 -18.818 -25.192  1.00 12.88           C  
ANISOU 2303  CB  PRO A 225     1785   1543   1566     38   -563   -166       C  
ATOM   2304  CG  PRO A 225       0.600 -18.051 -26.090  1.00 13.32           C  
ANISOU 2304  CG  PRO A 225     1853   1768   1442    172   -391    -38       C  
ATOM   2305  CD  PRO A 225      -0.211 -16.867 -26.559  1.00 13.73           C  
ANISOU 2305  CD  PRO A 225     1938   1923   1354    187   -500    168       C  
ATOM   2306  HB2 PRO A 225       0.153 -19.354 -24.551  1.00 15.46           H  
ATOM   2307  HB3 PRO A 225      -0.947 -19.367 -25.712  1.00 15.46           H  
ATOM   2308  HD2 PRO A 225       0.363 -16.098 -26.702  1.00 16.47           H  
ATOM   2309  HD3 PRO A 225      -0.709 -17.094 -27.360  1.00 16.47           H  
ATOM   2310  N   GLY A 226      -0.608 -18.054 -22.147  1.00 10.15           N  
ANISOU 2310  N   GLY A 226     1178   1204   1472   -159   -346    275       N  
ATOM   2311  CA  GLY A 226       0.132 -17.809 -20.925  1.00  9.17           C  
ANISOU 2311  CA  GLY A 226     1128   1216   1139   -103    -95    241       C  
ATOM   2312  C   GLY A 226       1.620 -18.061 -21.096  1.00  8.04           C  
ANISOU 2312  C   GLY A 226     1122    925   1009     82   -103     31       C  
ATOM   2313  O   GLY A 226       2.054 -18.949 -21.842  1.00  8.47           O  
ANISOU 2313  O   GLY A 226     1205    975   1039    -42   -197    -46       O  
ATOM   2314  H   GLY A 226      -1.169 -18.705 -22.108  1.00 12.17           H  
ATOM   2315  HA3 GLY A 226      -0.205 -18.377 -20.214  1.00 11.00           H  
ATOM   2316  N   VAL A 227       2.389 -17.290 -20.319  1.00  7.93           N  
ANISOU 2316  N   VAL A 227     1113    895   1004    108   -119    -21       N  
ATOM   2317  CA  VAL A 227       3.841 -17.385 -20.239  1.00  7.69           C  
ANISOU 2317  CA  VAL A 227     1078    840   1004    130    -53    -18       C  
ATOM   2318  C   VAL A 227       4.220 -17.854 -18.835  1.00  7.20           C  
ANISOU 2318  C   VAL A 227     1045    732    960     68    -77    -50       C  
ATOM   2319  O   VAL A 227       3.664 -17.398 -17.821  1.00  7.92           O  
ANISOU 2319  O   VAL A 227     1109    910    993    233   -110   -135       O  
ATOM   2320  CB  VAL A 227       4.539 -16.065 -20.611  1.00  7.72           C  
ANISOU 2320  CB  VAL A 227     1114    841    979     87    -15    -70       C  
ATOM   2321  CG1 VAL A 227       6.039 -16.299 -20.739  1.00  8.60           C  
ANISOU 2321  CG1 VAL A 227     1159    903   1207     55    -80     20       C  
ATOM   2322  CG2 VAL A 227       3.971 -15.481 -21.914  1.00  8.71           C  
ANISOU 2322  CG2 VAL A 227     1208   1035   1068    128    -84    -23       C  
ATOM   2323  HB  VAL A 227       4.394 -15.418 -19.903  1.00  9.27           H  
ATOM   2324 HG11 VAL A 227       6.471 -15.463 -20.973  1.00 10.32           H  
ATOM   2325 HG13 VAL A 227       6.197 -16.959 -21.432  1.00 10.32           H  
ATOM   2326 HG22 VAL A 227       4.108 -16.119 -22.632  1.00 10.46           H  
ATOM   2327 HG23 VAL A 227       3.023 -15.311 -21.797  1.00 10.46           H  
ATOM   2328  N   TYR A 228       5.160 -18.784 -18.789  1.00  7.17           N  
ANISOU 2328  N   TYR A 228     1019    831    875    110    -34    -23       N  
ATOM   2329  CA  TYR A 228       5.505 -19.541 -17.606  1.00  6.94           C  
ANISOU 2329  CA  TYR A 228      950    783    903     73    -46    -96       C  
ATOM   2330  C   TYR A 228       7.013 -19.522 -17.387  1.00  6.88           C  
ANISOU 2330  C   TYR A 228     1032    713    870    126     -3   -128       C  
ATOM   2331  O   TYR A 228       7.798 -19.621 -18.339  1.00  7.67           O  
ANISOU 2331  O   TYR A 228     1000   1034    880     37    -11   -160       O  
ATOM   2332  CB  TYR A 228       4.992 -20.998 -17.773  1.00  7.04           C  
ANISOU 2332  CB  TYR A 228      977    763    937     73    -54   -101       C  
ATOM   2333  CG  TYR A 228       3.494 -21.017 -17.926  1.00  7.00           C  
ANISOU 2333  CG  TYR A 228     1027    691    940     19    -86    -68       C  
ATOM   2334  CD1 TYR A 228       2.681 -20.999 -16.802  1.00  7.30           C  
ANISOU 2334  CD1 TYR A 228     1062    756    956     93    -28   -120       C  
ATOM   2335  CD2 TYR A 228       2.877 -20.993 -19.171  1.00  7.60           C  
ANISOU 2335  CD2 TYR A 228     1145    844    900     73     -3    -59       C  
ATOM   2336  CE1 TYR A 228       1.314 -20.945 -16.906  1.00  7.98           C  
ANISOU 2336  CE1 TYR A 228     1097    993    942     47    -14    -59       C  
ATOM   2337  CE2 TYR A 228       1.493 -20.929 -19.283  1.00  7.81           C  
ANISOU 2337  CE2 TYR A 228     1067    919    981     45   -191    -82       C  
ATOM   2338  CZ  TYR A 228       0.706 -20.916 -18.149  1.00  7.73           C  
ANISOU 2338  CZ  TYR A 228     1028    909    999    105    -69   -125       C  
ATOM   2339  OH  TYR A 228      -0.666 -20.836 -18.180  1.00  9.00           O  
ANISOU 2339  OH  TYR A 228      993   1312   1117     72    -88   -104       O  
ATOM   2340  H   TYR A 228       5.635 -19.002 -19.471  1.00  8.61           H  
ATOM   2341  HA  TYR A 228       5.075 -19.148 -16.831  1.00  8.33           H  
ATOM   2342  HB2 TYR A 228       5.386 -21.391 -18.567  1.00  8.45           H  
ATOM   2343  HB3 TYR A 228       5.226 -21.515 -16.986  1.00  8.45           H  
ATOM   2344  HD1 TYR A 228       3.072 -20.998 -15.958  1.00  8.76           H  
ATOM   2345  HD2 TYR A 228       3.399 -20.983 -19.941  1.00  9.12           H  
ATOM   2346  HE1 TYR A 228       0.793 -20.927 -16.136  1.00  9.58           H  
ATOM   2347  HE2 TYR A 228       1.096 -20.910 -20.124  1.00  9.37           H  
ATOM   2348  HH  TYR A 228      -0.935 -20.825 -18.975  1.00 10.81           H  
ATOM   2349  N   THR A 229       7.433 -19.463 -16.122  1.00  6.77           N  
ANISOU 2349  N   THR A 229      898    785    889     51     17   -132       N  
ATOM   2350  CA  THR A 229       8.853 -19.571 -15.795  1.00  7.07           C  
ANISOU 2350  CA  THR A 229      837    905    943     69    -20    -15       C  
ATOM   2351  C   THR A 229       9.327 -20.994 -16.066  1.00  6.72           C  
ANISOU 2351  C   THR A 229      947    734    871    118    -65    -93       C  
ATOM   2352  O   THR A 229       8.673 -21.953 -15.653  1.00  7.54           O  
ANISOU 2352  O   THR A 229     1063    782   1020     43     28    -82       O  
ATOM   2353  CB  THR A 229       9.084 -19.217 -14.326  1.00  6.95           C  
ANISOU 2353  CB  THR A 229      921    828    890     89     20    -70       C  
ATOM   2354  OG1 THR A 229       8.449 -17.968 -14.092  1.00  7.78           O  
ANISOU 2354  OG1 THR A 229     1064    969    923    195   -137   -186       O  
ATOM   2355  CG2 THR A 229      10.567 -19.163 -13.999  1.00  7.93           C  
ANISOU 2355  CG2 THR A 229     1032    935   1047     93   -101   -138       C  
ATOM   2356  H   THR A 229       6.919 -19.362 -15.440  1.00  8.12           H  
ATOM   2357  HA  THR A 229       9.365 -18.960 -16.348  1.00  8.48           H  
ATOM   2358  HB  THR A 229       8.673 -19.894 -13.766  1.00  8.34           H  
ATOM   2359  HG1 THR A 229       8.554 -17.738 -13.291  1.00  9.34           H  
ATOM   2360 HG22 THR A 229      10.976 -20.025 -14.171  1.00  9.52           H  
ATOM   2361 HG23 THR A 229      11.003 -18.491 -14.545  1.00  9.52           H  
ATOM   2362  N   LYS A 230      10.483 -21.129 -16.735  1.00  7.19           N  
ANISOU 2362  N   LYS A 230      898    812   1021     92     82    -32       N  
ATOM   2363  CA  LYS A 230      11.003 -22.427 -17.164  1.00  7.57           C  
ANISOU 2363  CA  LYS A 230     1064    812   1000     99     31   -124       C  
ATOM   2364  C   LYS A 230      11.834 -23.034 -16.027  1.00  7.68           C  
ANISOU 2364  C   LYS A 230      993    833   1090    165     12   -131       C  
ATOM   2365  O   LYS A 230      13.045 -22.811 -15.901  1.00  8.27           O  
ANISOU 2365  O   LYS A 230     1022    960   1161     92      9    -49       O  
ATOM   2366  CB  LYS A 230      11.807 -22.248 -18.443  1.00  8.16           C  
ANISOU 2366  CB  LYS A 230     1098    974   1030    115     53   -133       C  
ATOM   2367  CG  LYS A 230      12.162 -23.562 -19.126  1.00 10.06           C  
ANISOU 2367  CG  LYS A 230     1620   1065   1136    319    157   -133       C  
ATOM   2368  CD  LYS A 230      12.871 -23.334 -20.468  1.00 11.13           C  
ANISOU 2368  CD  LYS A 230     1628   1304   1296    222    326   -302       C  
ATOM   2369  CE  LYS A 230      13.248 -24.631 -21.148  1.00 14.63           C  
ANISOU 2369  CE  LYS A 230     2377   1824   1360    201    564   -273       C  
ATOM   2370  NZ  LYS A 230      13.747 -24.422 -22.536  1.00 18.43           N  
ANISOU 2370  NZ  LYS A 230     3048   2372   1582    504    582   -431       N  
ATOM   2371  H   LYS A 230      10.988 -20.469 -16.954  1.00  8.62           H  
ATOM   2372  HA  LYS A 230      10.262 -23.024 -17.352  1.00  9.08           H  
ATOM   2373  HB2 LYS A 230      11.287 -21.719 -19.068  1.00  9.80           H  
ATOM   2374  HB3 LYS A 230      12.635 -21.789 -18.232  1.00  9.80           H  
ATOM   2375  HG2 LYS A 230      12.762 -24.064 -18.552  1.00 12.07           H  
ATOM   2376  HD2 LYS A 230      12.277 -22.847 -21.060  1.00 13.35           H  
ATOM   2377  N   VAL A 231      11.161 -23.823 -15.180  1.00  7.81           N  
ANISOU 2377  N   VAL A 231     1000    936   1032     85     60    -95       N  
ATOM   2378  CA  VAL A 231      11.736 -24.313 -13.917  1.00  7.95           C  
ANISOU 2378  CA  VAL A 231     1080    908   1032    146    -47    -57       C  
ATOM   2379  C   VAL A 231      13.017 -25.110 -14.119  1.00  8.08           C  
ANISOU 2379  C   VAL A 231     1102    954   1014     81     91    -89       C  
ATOM   2380  O   VAL A 231      13.897 -25.081 -13.260  1.00  8.61           O  
ANISOU 2380  O   VAL A 231     1057   1122   1094    196    -18    -22       O  
ATOM   2381  CB  VAL A 231      10.674 -25.103 -13.126  1.00  8.04           C  
ANISOU 2381  CB  VAL A 231     1071    916   1067     61      4    -34       C  
ATOM   2382  CG1 VAL A 231      11.254 -25.766 -11.885  1.00  9.20           C  
ANISOU 2382  CG1 VAL A 231     1088   1213   1193    157     90    157       C  
ATOM   2383  CG2 VAL A 231       9.531 -24.179 -12.717  1.00  8.36           C  
ANISOU 2383  CG2 VAL A 231      959   1040   1178    150    140    -26       C  
ATOM   2384  H   VAL A 231      10.356 -24.093 -15.316  1.00  9.37           H  
ATOM   2385  HB  VAL A 231      10.309 -25.798 -13.695  1.00  9.64           H  
ATOM   2386 HG11 VAL A 231      10.537 -26.194 -11.392  1.00 11.03           H  
ATOM   2387 HG12 VAL A 231      11.910 -26.427 -12.158  1.00 11.03           H  
ATOM   2388 HG21 VAL A 231       8.788 -24.716 -12.401  1.00 10.03           H  
ATOM   2389  N   CYS A 232      13.115 -25.883 -15.199  1.00  8.72           N  
ANISOU 2389  N   CYS A 232     1047   1024   1241    215    -39    -59       N  
ATOM   2390  CA  CYS A 232      14.294 -26.723 -15.361  1.00  9.49           C  
ANISOU 2390  CA  CYS A 232     1162   1134   1308    289     35   -211       C  
ATOM   2391  C   CYS A 232      15.581 -25.913 -15.355  1.00  9.97           C  
ANISOU 2391  C   CYS A 232     1206   1275   1307    439    131   -145       C  
ATOM   2392  O   CYS A 232      16.626 -26.449 -14.977  1.00 12.19           O  
ANISOU 2392  O   CYS A 232     1378   1232   2023    402     -4    -42       O  
ATOM   2393  CB  CYS A 232      14.167 -27.594 -16.614  1.00 10.18           C  
ANISOU 2393  CB  CYS A 232     1317   1249   1302    252     85   -207       C  
ATOM   2394  SG  CYS A 232      14.114 -26.613 -18.135  1.00 11.90           S  
ANISOU 2394  SG  CYS A 232     1646   1582   1294    157    185   -158       S  
ATOM   2395  H   CYS A 232      12.533 -25.939 -15.830  1.00 10.46           H  
ATOM   2396  HA  CYS A 232      14.338 -27.325 -14.602  1.00 11.38           H  
ATOM   2397  HB2 CYS A 232      14.932 -28.189 -16.666  1.00 12.22           H  
ATOM   2398  HB3 CYS A 232      13.347 -28.110 -16.560  1.00 12.22           H  
ATOM   2399  N   ASN A 233      15.535 -24.630 -15.731  1.00  8.56           N  
ANISOU 2399  N   ASN A 233     1092   1056   1104    215     79     -7       N  
ATOM   2400  CA  ASN A 233      16.720 -23.787 -15.720  1.00  8.83           C  
ANISOU 2400  CA  ASN A 233     1098   1050   1209    190     83    -45       C  
ATOM   2401  C   ASN A 233      17.200 -23.451 -14.311  1.00  9.11           C  
ANISOU 2401  C   ASN A 233     1121   1108   1232    172    -28    -10       C  
ATOM   2402  O   ASN A 233      18.324 -22.975 -14.147  1.00 12.02           O  
ANISOU 2402  O   ASN A 233     1183   1952   1434   -106     67   -196       O  
ATOM   2403  CB  ASN A 233      16.458 -22.472 -16.462  1.00  9.29           C  
ANISOU 2403  CB  ASN A 233     1114   1201   1214     94    115    -31       C  
ATOM   2404  CG  ASN A 233      16.260 -22.642 -17.939  1.00 10.12           C  
ANISOU 2404  CG  ASN A 233     1313   1228   1304    208     50     39       C  
ATOM   2405  OD1 ASN A 233      16.305 -23.748 -18.497  1.00 11.90           O  
ANISOU 2405  OD1 ASN A 233     1951   1324   1245     91    177    -72       O  
ATOM   2406  ND2 ASN A 233      15.981 -21.507 -18.597  1.00 10.81           N  
ANISOU 2406  ND2 ASN A 233     1333   1359   1415     90    -16    121       N  
ATOM   2407  H   ASN A 233      14.823 -24.228 -15.997  1.00 10.27           H  
ATOM   2408  HA  ASN A 233      17.438 -24.250 -16.178  1.00 10.60           H  
ATOM   2409  HB2 ASN A 233      15.656 -22.063 -16.100  1.00 11.15           H  
ATOM   2410  HB3 ASN A 233      17.216 -21.881 -16.330  1.00 11.15           H  
ATOM   2411  N   TYR A 234      16.365 -23.676 -13.303  1.00  8.64           N  
ANISOU 2411  N   TYR A 234     1040   1059   1182    149      4     43       N  
ATOM   2412  CA  TYR A 234      16.577 -23.196 -11.947  1.00  8.57           C  
ANISOU 2412  CA  TYR A 234     1151   1075   1031    119   -103    -64       C  
ATOM   2413  C   TYR A 234      16.845 -24.323 -10.956  1.00  8.79           C  
ANISOU 2413  C   TYR A 234     1172   1082   1087    122   -170    -28       C  
ATOM   2414  O   TYR A 234      17.012 -24.041  -9.774  1.00  9.24           O  
ANISOU 2414  O   TYR A 234     1244   1109   1158    168   -184    -15       O  
ATOM   2415  CB  TYR A 234      15.371 -22.361 -11.483  1.00  8.51           C  
ANISOU 2415  CB  TYR A 234     1099    991   1144     48   -130    -48       C  
ATOM   2416  CG  TYR A 234      15.221 -21.142 -12.349  1.00  8.12           C  
ANISOU 2416  CG  TYR A 234     1048    969   1068    160    -51    -92       C  
ATOM   2417  CD1 TYR A 234      16.057 -20.052 -12.181  1.00  9.05           C  
ANISOU 2417  CD1 TYR A 234     1200   1124   1114     11   -113   -171       C  
ATOM   2418  CD2 TYR A 234      14.282 -21.091 -13.370  1.00  8.62           C  
ANISOU 2418  CD2 TYR A 234     1078   1035   1162     55    -10    -89       C  
ATOM   2419  CE1 TYR A 234      15.966 -18.942 -12.997  1.00  8.69           C  
ANISOU 2419  CE1 TYR A 234     1167    994   1142      1    -50     26       C  
ATOM   2420  CE2 TYR A 234      14.205 -19.987 -14.212  1.00  8.21           C  
ANISOU 2420  CE2 TYR A 234     1032   1027   1060    109    -72   -113       C  
ATOM   2421  CZ  TYR A 234      15.022 -18.921 -14.019  1.00  8.16           C  
ANISOU 2421  CZ  TYR A 234     1137    984    980    266     14      8       C  
ATOM   2422  OH  TYR A 234      14.885 -17.846 -14.852  1.00  8.96           O  
ANISOU 2422  OH  TYR A 234     1291   1023   1090    272      3    -28       O  
ATOM   2423  H   TYR A 234      15.636 -24.125 -13.388  1.00 10.36           H  
ATOM   2424  HA  TYR A 234      17.353 -22.615 -11.944  1.00 10.29           H  
ATOM   2425  HB2 TYR A 234      14.562 -22.892 -11.555  1.00 10.22           H  
ATOM   2426  HB3 TYR A 234      15.509 -22.074 -10.566  1.00 10.22           H  
ATOM   2427  HE1 TYR A 234      16.532 -18.216 -12.866  1.00 10.43           H  
ATOM   2428  HE2 TYR A 234      13.565 -19.964 -14.886  1.00  9.85           H  
ATOM   2429  N   VAL A 235      16.880 -25.583 -11.398  1.00  9.98           N  
ANISOU 2429  N   VAL A 235     1612   1064   1115    104   -223      3       N  
ATOM   2430  CA  VAL A 235      17.006 -26.690 -10.455  1.00 10.10           C  
ANISOU 2430  CA  VAL A 235     1643   1009   1186     92   -197     39       C  
ATOM   2431  C   VAL A 235      18.309 -26.599  -9.665  1.00  9.59           C  
ANISOU 2431  C   VAL A 235     1501    956   1186    184    -38   -156       C  
ATOM   2432  O   VAL A 235      18.328 -26.866  -8.459  1.00  9.48           O  
ANISOU 2432  O   VAL A 235     1519    996   1089    181   -133    -63       O  
ATOM   2433  CB  VAL A 235      16.813 -28.030 -11.181  1.00 12.35           C  
ANISOU 2433  CB  VAL A 235     2268   1008   1418    -79   -493     73       C  
ATOM   2434  CG1 VAL A 235      17.145 -29.188 -10.256  1.00 15.93           C  
ANISOU 2434  CG1 VAL A 235     2860   1238   1955     -7   -554    -96       C  
ATOM   2435  CG2 VAL A 235      15.368 -28.142 -11.665  1.00 14.57           C  
ANISOU 2435  CG2 VAL A 235     2464   1488   1582   -460   -696    200       C  
ATOM   2436  HA  VAL A 235      16.284 -26.614  -9.812  1.00 12.12           H  
ATOM   2437  HB  VAL A 235      17.401 -28.070 -11.951  1.00 14.82           H  
ATOM   2438  N  ASER A 236      19.411 -26.217 -10.315  0.45  9.40           N  
ANISOU 2438  N  ASER A 236     1523    897   1153    295    -76     34       N  
ATOM   2439  N  BSER A 236      19.415 -26.230 -10.320  0.55 10.56           N  
ANISOU 2439  N  BSER A 236     1511   1248   1252    334   -100   -441       N  
ATOM   2440  CA ASER A 236      20.668 -26.132  -9.577  0.45  9.58           C  
ANISOU 2440  CA ASER A 236     1456    912   1270    442    169    160       C  
ATOM   2441  CA BSER A 236      20.678 -26.110  -9.593  0.55 11.92           C  
ANISOU 2441  CA BSER A 236     1579   1488   1461    454    -46   -585       C  
ATOM   2442  C  ASER A 236      20.614 -25.047  -8.500  0.45  9.24           C  
ANISOU 2442  C  ASER A 236     1308   1070   1133    190    -78    125       C  
ATOM   2443  C  BSER A 236      20.581 -25.053  -8.493  0.55  9.62           C  
ANISOU 2443  C  BSER A 236     1107   1296   1252    351     80   -264       C  
ATOM   2444  O  ASER A 236      21.087 -25.252  -7.368  0.45  9.60           O  
ANISOU 2444  O  ASER A 236     1409   1006   1231    228   -281    229       O  
ATOM   2445  O  BSER A 236      20.987 -25.283  -7.341  0.55  9.68           O  
ANISOU 2445  O  BSER A 236     1101   1157   1420    247     42    -98       O  
ATOM   2446  CB ASER A 236      21.835 -25.906 -10.533  0.45 12.25           C  
ANISOU 2446  CB ASER A 236     1503   1510   1640    425    532     16       C  
ATOM   2447  CB BSER A 236      21.810 -25.784 -10.565  0.55 16.31           C  
ANISOU 2447  CB BSER A 236     2000   2339   1857    628    115   -891       C  
ATOM   2448  OG ASER A 236      23.013 -25.674  -9.801  0.45 14.80           O  
ANISOU 2448  OG ASER A 236     1736   1781   2107    502    447     -1       O  
ATOM   2449  OG BSER A 236      22.009 -26.866 -11.456  0.55 19.96           O  
ANISOU 2449  OG BSER A 236     2582   2734   2267    766    138   -692       O  
ATOM   2450  HA ASER A 236      20.819 -26.979  -9.129  0.45 11.49           H  
ATOM   2451  HA BSER A 236      20.881 -26.961  -9.172  0.55 14.30           H  
ATOM   2452  N   TRP A 237      20.043 -23.882  -8.838  1.00  8.57           N  
ANISOU 2452  N   TRP A 237     1096    983   1177    251     15     68       N  
ATOM   2453  CA  TRP A 237      19.870 -22.814  -7.858  1.00  8.29           C  
ANISOU 2453  CA  TRP A 237     1061    968   1119    105    -18    -35       C  
ATOM   2454  C   TRP A 237      18.942 -23.247  -6.727  1.00  7.59           C  
ANISOU 2454  C   TRP A 237     1004    770   1111    140    -98    -27       C  
ATOM   2455  O   TRP A 237      19.213 -22.975  -5.555  1.00  8.13           O  
ANISOU 2455  O   TRP A 237     1135    906   1048     57    -96    -22       O  
ATOM   2456  CB  TRP A 237      19.346 -21.535  -8.556  1.00  8.96           C  
ANISOU 2456  CB  TRP A 237     1243    947   1215     48    -80     78       C  
ATOM   2457  CG  TRP A 237      18.902 -20.452  -7.606  1.00  7.97           C  
ANISOU 2457  CG  TRP A 237     1098    850   1079     47   -127     26       C  
ATOM   2458  CD1 TRP A 237      19.712 -19.601  -6.893  1.00  8.98           C  
ANISOU 2458  CD1 TRP A 237     1183    942   1286     30   -213     88       C  
ATOM   2459  CD2 TRP A 237      17.561 -20.107  -7.257  1.00  7.60           C  
ANISOU 2459  CD2 TRP A 237     1071    780   1038    -24   -207     47       C  
ATOM   2460  NE1 TRP A 237      18.956 -18.755  -6.129  1.00  8.56           N  
ANISOU 2460  NE1 TRP A 237     1241    828   1184     11   -265    -45       N  
ATOM   2461  CE2 TRP A 237      17.630 -19.042  -6.338  1.00  7.98           C  
ANISOU 2461  CE2 TRP A 237     1142    803   1088     17   -191    111       C  
ATOM   2462  CE3 TRP A 237      16.308 -20.575  -7.657  1.00  8.57           C  
ANISOU 2462  CE3 TRP A 237     1162    908   1186     86   -263     93       C  
ATOM   2463  CZ2 TRP A 237      16.496 -18.449  -5.793  1.00  8.63           C  
ANISOU 2463  CZ2 TRP A 237     1209    902   1167     82   -186     10       C  
ATOM   2464  CZ3 TRP A 237      15.191 -19.986  -7.120  1.00  9.23           C  
ANISOU 2464  CZ3 TRP A 237     1156    958   1394     18   -241    120       C  
ATOM   2465  CH2 TRP A 237      15.288 -18.928  -6.195  1.00  9.35           C  
ANISOU 2465  CH2 TRP A 237     1240    937   1374     13   -117     90       C  
ATOM   2466  H  ATRP A 237      19.751 -23.691  -9.624  0.45 10.29           H  
ATOM   2467  H  BTRP A 237      19.772 -23.683  -9.630  0.55 10.29           H  
ATOM   2468  HB3 TRP A 237      18.591 -21.769  -9.118  1.00 10.76           H  
ATOM   2469  HE1 TRP A 237      19.261 -18.148  -5.602  1.00 10.27           H  
ATOM   2470  HZ3 TRP A 237      14.350 -20.297  -7.367  1.00 11.08           H  
ATOM   2471  N   ILE A 238      17.827 -23.911  -7.054  1.00  7.65           N  
ANISOU 2471  N   ILE A 238      987    836   1084    146   -104    -75       N  
ATOM   2472  CA  ILE A 238      16.909 -24.365  -6.019  1.00  7.81           C  
ANISOU 2472  CA  ILE A 238     1057    811   1099    114    -15    -93       C  
ATOM   2473  C   ILE A 238      17.629 -25.297  -5.056  1.00  8.09           C  
ANISOU 2473  C   ILE A 238     1125    789   1159     44    -52    -40       C  
ATOM   2474  O   ILE A 238      17.535 -25.148  -3.827  1.00  8.52           O  
ANISOU 2474  O   ILE A 238     1166   1035   1038     30    -52     -3       O  
ATOM   2475  CB  ILE A 238      15.669 -25.036  -6.628  1.00  8.12           C  
ANISOU 2475  CB  ILE A 238     1021    837   1229     83   -155    -71       C  
ATOM   2476  CG1 ILE A 238      14.808 -24.016  -7.389  1.00  8.90           C  
ANISOU 2476  CG1 ILE A 238     1097    943   1343    161    -70    -79       C  
ATOM   2477  CG2 ILE A 238      14.856 -25.714  -5.528  1.00  9.48           C  
ANISOU 2477  CG2 ILE A 238     1185   1062   1353    -27    -78      0       C  
ATOM   2478  CD1 ILE A 238      13.726 -24.651  -8.222  1.00 10.34           C  
ANISOU 2478  CD1 ILE A 238     1297   1071   1561     39   -322     -2       C  
ATOM   2479  H   ILE A 238      17.587 -24.105  -7.856  1.00  9.18           H  
ATOM   2480  HA  ILE A 238      16.608 -23.595  -5.512  1.00  9.37           H  
ATOM   2481 HG12 ILE A 238      14.382 -23.424  -6.749  1.00 10.68           H  
ATOM   2482 HG13 ILE A 238      15.379 -23.504  -7.983  1.00 10.68           H  
ATOM   2483 HG21 ILE A 238      14.077 -26.135  -5.924  1.00 11.37           H  
ATOM   2484 HG23 ILE A 238      14.580 -25.046  -4.881  1.00 11.37           H  
ATOM   2485  N   LYS A 239      18.321 -26.307  -5.597  1.00  8.22           N  
ANISOU 2485  N   LYS A 239     1196    855   1072    122    -76      6       N  
ATOM   2486  CA  LYS A 239      18.949 -27.295  -4.737  1.00  9.20           C  
ANISOU 2486  CA  LYS A 239     1452    898   1147    129   -123     45       C  
ATOM   2487  C   LYS A 239      20.032 -26.674  -3.874  1.00  8.66           C  
ANISOU 2487  C   LYS A 239     1291    850   1150    160   -121    -24       C  
ATOM   2488  O   LYS A 239      20.134 -26.979  -2.681  1.00  9.36           O  
ANISOU 2488  O   LYS A 239     1352   1021   1185    227   -134     77       O  
ATOM   2489  CB  LYS A 239      19.490 -28.449  -5.599  1.00 10.97           C  
ANISOU 2489  CB  LYS A 239     1942    886   1341    420   -361     13       C  
ATOM   2490  CG  LYS A 239      18.374 -29.319  -6.173  1.00 14.56           C  
ANISOU 2490  CG  LYS A 239     2651   1100   1783    196   -744   -221       C  
ATOM   2491  CD  LYS A 239      18.938 -30.451  -7.019  1.00 20.42           C  
ANISOU 2491  CD  LYS A 239     3682   1490   2587    448  -1093   -690       C  
ATOM   2492  CE  LYS A 239      17.853 -31.435  -7.398  1.00 25.59           C  
ANISOU 2492  CE  LYS A 239     4320   2183   3221    565  -1268   -737       C  
ATOM   2493  H   LYS A 239      18.437 -26.435  -6.440  1.00  9.86           H  
ATOM   2494  HA  LYS A 239      18.275 -27.662  -4.143  1.00 11.04           H  
ATOM   2495  HB2 LYS A 239      19.996 -28.081  -6.340  1.00 13.17           H  
ATOM   2496  HB3 LYS A 239      20.060 -29.013  -5.053  1.00 13.17           H  
ATOM   2497  N  AGLN A 240      20.848 -25.783  -4.435  0.59  8.76           N  
ANISOU 2497  N  AGLN A 240     1211    892   1225    119    -13   -146       N  
ATOM   2498  N  BGLN A 240      20.851 -25.798  -4.454  0.41  9.07           N  
ANISOU 2498  N  BGLN A 240     1099   1078   1269    146   -174     -9       N  
ATOM   2499  CA AGLN A 240      21.931 -25.231  -3.625  0.59  9.68           C  
ANISOU 2499  CA AGLN A 240     1197   1101   1380    -66     -2    -90       C  
ATOM   2500  CA BGLN A 240      21.920 -25.169  -3.688  0.41  9.84           C  
ANISOU 2500  CA BGLN A 240     1003   1321   1414    200   -299    147       C  
ATOM   2501  C  AGLN A 240      21.391 -24.231  -2.613  0.59  8.51           C  
ANISOU 2501  C  AGLN A 240     1130   1045   1060    -53   -128    -32       C  
ATOM   2502  C  BGLN A 240      21.342 -24.290  -2.601  0.41  9.36           C  
ANISOU 2502  C  BGLN A 240     1078   1126   1353    141   -164     -1       C  
ATOM   2503  O  AGLN A 240      21.924 -24.119  -1.506  0.59  9.42           O  
ANISOU 2503  O  AGLN A 240     1182   1297   1102    -69   -291    128       O  
ATOM   2504  O  BGLN A 240      21.809 -24.302  -1.456  0.41 10.78           O  
ANISOU 2504  O  BGLN A 240     1192   1257   1647    421     77    -42       O  
ATOM   2505  CB AGLN A 240      23.083 -24.709  -4.495  0.59 10.89           C  
ANISOU 2505  CB AGLN A 240     1446   1227   1463   -116    189    -67       C  
ATOM   2506  CB BGLN A 240      22.806 -24.362  -4.624  0.41 12.02           C  
ANISOU 2506  CB BGLN A 240     1246   1847   1476     -7   -295     60       C  
ATOM   2507  CG AGLN A 240      22.800 -23.419  -5.198  0.59 12.07           C  
ANISOU 2507  CG AGLN A 240     1617   1275   1695     31   -243   -276       C  
ATOM   2508  CG BGLN A 240      23.564 -25.257  -5.564  0.41 12.99           C  
ANISOU 2508  CG BGLN A 240     1221   2255   1458    182     94    -65       C  
ATOM   2509  CD AGLN A 240      23.280 -22.196  -4.429  0.59 11.98           C  
ANISOU 2509  CD AGLN A 240     1560   1305   1688     29   -155      6       C  
ATOM   2510  OE1AGLN A 240      23.694 -22.286  -3.268  0.59 12.61           O  
ANISOU 2510  OE1AGLN A 240     1668   1471   1650    191   -295    -44       O  
ATOM   2511  NE2AGLN A 240      23.193 -21.030  -5.068  0.59 13.33           N  
ANISOU 2511  NE2AGLN A 240     1866   1194   2005   -198   -385   -115       N  
ATOM   2512  N   THR A 241      20.301 -23.536  -2.937  1.00  8.31           N  
ANISOU 2512  N   THR A 241     1091    947   1120     63   -185    -43       N  
ATOM   2513  CA  THR A 241      19.691 -22.632  -1.976  1.00  8.72           C  
ANISOU 2513  CA  THR A 241     1109   1045   1157    -23   -119   -107       C  
ATOM   2514  C   THR A 241      19.118 -23.412  -0.792  1.00  9.05           C  
ANISOU 2514  C   THR A 241     1209    988   1243     60   -125    -86       C  
ATOM   2515  O   THR A 241      19.347 -23.067   0.377  1.00  9.58           O  
ANISOU 2515  O   THR A 241     1463   1179    997     -6   -144   -131       O  
ATOM   2516  CB  THR A 241      18.645 -21.757  -2.677  1.00  9.32           C  
ANISOU 2516  CB  THR A 241     1253   1017   1271    104   -280   -224       C  
ATOM   2517  OG1 THR A 241      19.277 -20.937  -3.654  1.00  9.81           O  
ANISOU 2517  OG1 THR A 241     1471    887   1370    -51   -334    -32       O  
ATOM   2518  CG2 THR A 241      17.900 -20.847  -1.697  1.00 10.13           C  
ANISOU 2518  CG2 THR A 241     1303   1158   1388      6   -189   -314       C  
ATOM   2519  H  ATHR A 241      19.902 -23.571  -3.698  1.00  9.97           H  
ATOM   2520  H  BTHR A 241      19.931 -23.530  -3.713  0.00  9.97           H  
ATOM   2521  HA  THR A 241      20.379 -22.042  -1.629  1.00 10.46           H  
ATOM   2522  HB  THR A 241      17.994 -22.328  -3.114  1.00 11.18           H  
ATOM   2523 HG22 THR A 241      17.439 -21.382  -1.032  1.00 12.16           H  
ATOM   2524 HG23 THR A 241      18.527 -20.258  -1.249  1.00 12.16           H  
ATOM   2525  N   ILE A 242      18.386 -24.476  -1.076  1.00  8.67           N  
ANISOU 2525  N   ILE A 242     1178   1064   1051     11    -24    -44       N  
ATOM   2526  CA  ILE A 242      17.835 -25.308  -0.008  1.00  9.35           C  
ANISOU 2526  CA  ILE A 242     1266   1146   1140    -40      1     28       C  
ATOM   2527  C   ILE A 242      18.958 -25.854   0.862  1.00  9.75           C  
ANISOU 2527  C   ILE A 242     1371   1287   1045     -7    -84    135       C  
ATOM   2528  O   ILE A 242      18.843 -25.871   2.087  1.00 11.75           O  
ANISOU 2528  O   ILE A 242     1460   1884   1119    132    -61    184       O  
ATOM   2529  CB  ILE A 242      16.960 -26.429  -0.600  1.00 10.48           C  
ANISOU 2529  CB  ILE A 242     1323   1434   1227   -181     -7     33       C  
ATOM   2530  CG1 ILE A 242      15.664 -25.836  -1.135  1.00 12.24           C  
ANISOU 2530  CG1 ILE A 242     1322   1995   1335   -314    -86    115       C  
ATOM   2531  CG2 ILE A 242      16.703 -27.527   0.423  1.00 12.89           C  
ANISOU 2531  CG2 ILE A 242     1729   1797   1371   -375     96    187       C  
ATOM   2532  CD1 ILE A 242      14.857 -26.816  -1.939  1.00 15.51           C  
ANISOU 2532  CD1 ILE A 242     1972   2374   1545   -728   -465    386       C  
ATOM   2533  H   ILE A 242      18.192 -24.741  -1.871  1.00 10.40           H  
ATOM   2534  HA  ILE A 242      17.268 -24.757   0.554  1.00 11.22           H  
ATOM   2535  HB  ILE A 242      17.440 -26.821  -1.346  1.00 12.58           H  
ATOM   2536 HG13 ILE A 242      15.875 -25.081  -1.707  1.00 14.69           H  
ATOM   2537  N   ALA A 243      20.058 -26.304   0.247  1.00  9.62           N  
ANISOU 2537  N   ALA A 243     1340   1249   1066     58    -29     76       N  
ATOM   2538  CA  ALA A 243      21.155 -26.938   0.981  1.00 10.33           C  
ANISOU 2538  CA  ALA A 243     1567   1163   1195    202   -125    203       C  
ATOM   2539  C   ALA A 243      21.854 -26.010   1.972  1.00 10.52           C  
ANISOU 2539  C   ALA A 243     1475   1377   1144     50    -34    106       C  
ATOM   2540  O   ALA A 243      22.536 -26.501   2.883  1.00 12.62           O  
ANISOU 2540  O   ALA A 243     1939   1670   1186    146   -349    346       O  
ATOM   2541  CB  ALA A 243      22.172 -27.481  -0.030  1.00 11.89           C  
ANISOU 2541  CB  ALA A 243     1584   1681   1252    688    -15    250       C  
ATOM   2542  H   ALA A 243      20.192 -26.253  -0.601  1.00 11.55           H  
ATOM   2543  HA  ALA A 243      20.802 -27.691   1.480  1.00 12.39           H  
ATOM   2544  HB1 ALA A 243      22.867 -27.960   0.448  1.00 14.27           H  
ATOM   2545  N  ASER A 244      21.745 -24.693   1.794  0.71 10.33           N  
ANISOU 2545  N  ASER A 244     1407   1248   1268    -46   -189     32       N  
ATOM   2546  N  BSER A 244      21.671 -24.703   1.807  0.29 10.68           N  
ANISOU 2546  N  BSER A 244     1388   1452   1217    184    -53    120       N  
ATOM   2547  CA ASER A 244      22.419 -23.744   2.669  0.71 10.92           C  
ANISOU 2547  CA ASER A 244     1186   1381   1584    -45    -69      1       C  
ATOM   2548  CA BSER A 244      22.390 -23.682   2.539  0.29 10.49           C  
ANISOU 2548  CA BSER A 244     1106   1534   1346    194    -75    136       C  
ATOM   2549  C  ASER A 244      21.472 -22.819   3.425  0.71 11.29           C  
ANISOU 2549  C  ASER A 244     1137   1677   1475   -329   -279   -134       C  
ATOM   2550  C  BSER A 244      21.470 -22.801   3.375  0.29 10.49           C  
ANISOU 2550  C  BSER A 244     1089   1580   1317    -65     57     65       C  
ATOM   2551  O  ASER A 244      21.934 -21.849   4.032  0.71 13.80           O  
ANISOU 2551  O  ASER A 244     1384   2062   1798   -543   -288   -535       O  
ATOM   2552  O  BSER A 244      21.952 -21.860   4.013  0.29 10.75           O  
ANISOU 2552  O  BSER A 244     1127   1683   1275    112    238    -26       O  
ATOM   2553  CB ASER A 244      23.473 -22.923   1.922  0.71 13.84           C  
ANISOU 2553  CB ASER A 244     1516   1895   1847    262    216     83       C  
ATOM   2554  CB BSER A 244      23.183 -22.823   1.545  0.29 13.16           C  
ANISOU 2554  CB BSER A 244     1367   1943   1691    116     89    -96       C  
ATOM   2555  OG ASER A 244      24.551 -23.748   1.534  0.71 13.86           O  
ANISOU 2555  OG ASER A 244     1286   2137   1845    316     89   -112       O  
ATOM   2556  OG BSER A 244      23.864 -23.654   0.613  0.29 14.98           O  
ANISOU 2556  OG BSER A 244     1565   2340   1788   -192   -128   -125       O  
ATOM   2557  N   ASN A 245      20.165 -23.074   3.385  1.00 10.89           N  
ANISOU 2557  N   ASN A 245     1145   1555   1437   -166    -46   -172       N  
ATOM   2558  CA  ASN A 245      19.185 -22.205   4.064  1.00 11.22           C  
ANISOU 2558  CA  ASN A 245     1257   1673   1332   -332     33   -288       C  
ATOM   2559  C   ASN A 245      18.176 -22.995   4.850  1.00 13.07           C  
ANISOU 2559  C   ASN A 245     1570   2062   1333    -36      6   -214       C  
ATOM   2560  O   ASN A 245      17.207 -22.402   5.331  1.00 14.85           O  
ANISOU 2560  O   ASN A 245     1508   2600   1535    -39    143      8       O  
ATOM   2561  CB  ASN A 245      18.467 -21.314   3.057  1.00 11.11           C  
ANISOU 2561  CB  ASN A 245     1148   1686   1388    -81   -103   -247       C  
ATOM   2562  CG  ASN A 245      19.363 -20.247   2.561  1.00 11.86           C  
ANISOU 2562  CG  ASN A 245     1070   1618   1819   -234   -207   -438       C  
ATOM   2563  OD1 ASN A 245      19.515 -19.209   3.214  1.00 14.24           O  
ANISOU 2563  OD1 ASN A 245     1511   1685   2213   -276    -19   -802       O  
ATOM   2564  ND2 ASN A 245      19.996 -20.496   1.422  1.00 10.81           N  
ANISOU 2564  ND2 ASN A 245     1343   1296   1468    -33   -133   -289       N  
ATOM   2565  OXT ASN A 245      18.324 -24.209   4.985  1.00 15.36           O  
ANISOU 2565  OXT ASN A 245     1878   2133   1827   -118    343     57       O  
ATOM   2566  HA  ASN A 245      19.657 -21.629   4.685  1.00 13.46           H  
ATOM   2567 HD22 ASN A 245      19.874 -21.245   1.017  1.00 12.97           H  
TER    2568      ASN A 245                                                      
HETATM 2569 CA    CA A 301     -10.157 -24.693   3.130  1.00  7.59          CA  
ANISOU 2569 CA    CA A 301      941    914   1029    -27     70    -12      CA  
HETATM 2570  S   SO4 A 302      12.183 -11.952 -30.493  0.74 24.05           S  
ANISOU 2570  S   SO4 A 302     2567   2741   3829    525    826   1151       S  
HETATM 2571  O1  SO4 A 302      13.032 -12.322 -31.609  0.74 30.37           O  
ANISOU 2571  O1  SO4 A 302     3553   3862   4124   1206    857    823       O  
HETATM 2572  O2  SO4 A 302      10.950 -11.307 -30.949  0.74 21.92           O  
ANISOU 2572  O2  SO4 A 302     2615   2626   3087    808    773    591       O  
HETATM 2573  O3  SO4 A 302      11.912 -13.123 -29.660  0.74 23.31           O  
ANISOU 2573  O3  SO4 A 302     2978   2207   3673    408    669    671       O  
HETATM 2574  O4  SO4 A 302      12.912 -10.995 -29.664  0.74 30.55           O  
ANISOU 2574  O4  SO4 A 302     3635   3214   4758    473    339    420       O  
HETATM 2575  S   SO4 A 303      -1.288 -11.472 -11.094  0.61 26.58           S  
ANISOU 2575  S   SO4 A 303     2001   2010   6087    310    473    -92       S  
HETATM 2576  O1  SO4 A 303      -2.042 -10.246 -10.889  0.61 28.45           O  
ANISOU 2576  O1  SO4 A 303     2502   2254   6053    453    714    -44       O  
HETATM 2577  O2  SO4 A 303      -1.120 -11.664 -12.536  0.61 32.73           O  
ANISOU 2577  O2  SO4 A 303     3075   2828   6534    219    424    195       O  
HETATM 2578  O3  SO4 A 303      -1.993 -12.639 -10.570  0.61 22.83           O  
ANISOU 2578  O3  SO4 A 303     1800   1635   5238   -377    -97    351       O  
HETATM 2579  O4  SO4 A 303       0.038 -11.458 -10.479  0.61 25.35           O  
ANISOU 2579  O4  SO4 A 303     1500   2406   5727     63    389   -421       O  
HETATM 2580  S   SO4 A 304      16.869 -21.776   9.647  0.48 15.14           S  
ANISOU 2580  S   SO4 A 304     2241   1664   1846     85   -112    -21       S  
HETATM 2581  O1  SO4 A 304      17.555 -23.026   9.290  0.48 15.33           O  
ANISOU 2581  O1  SO4 A 304     2370   1693   1762    -28   -538     79       O  
HETATM 2582  O2  SO4 A 304      15.643 -21.642   8.883  0.48 14.82           O  
ANISOU 2582  O2  SO4 A 304     1927   2060   1644    824   -474   -159       O  
HETATM 2583  O3  SO4 A 304      16.490 -21.766  11.062  0.48 17.02           O  
ANISOU 2583  O3  SO4 A 304     2707   2040   1722     36   -408     57       O  
HETATM 2584  O4  SO4 A 304      17.746 -20.653   9.340  0.48 17.85           O  
ANISOU 2584  O4  SO4 A 304     2829   1652   2303   -262   -230    148       O  
HETATM 2585  S  ASO4 A 305      11.577 -35.734 -16.098  0.36 12.92           S  
ANISOU 2585  S  ASO4 A 305     1466   1583   1862    105   -243   -372       S  
HETATM 2586  O1 ASO4 A 305      12.241 -36.165 -17.311  0.36 14.88           O  
ANISOU 2586  O1 ASO4 A 305     1720   1770   2165    154    -41   -812       O  
HETATM 2587  O2 ASO4 A 305      10.144 -35.752 -16.371  0.36 15.34           O  
ANISOU 2587  O2 ASO4 A 305     1476   1965   2386    347   -136   -769       O  
HETATM 2588  O3 ASO4 A 305      11.880 -36.717 -15.077  0.36 13.90           O  
ANISOU 2588  O3 ASO4 A 305     1550   1588   2145    294     -6    -62       O  
HETATM 2589  O4 ASO4 A 305      12.048 -34.401 -15.733  0.36 13.30           O  
ANISOU 2589  O4 ASO4 A 305     1627   1444   1981      8   -196   -533       O  
HETATM 2590  O   HOH A 401     -17.257 -17.321  -3.719  1.00 27.74           O  
ANISOU 2590  O   HOH A 401     3084   4132   3325   1380    812    904       O  
HETATM 2591  O   HOH A 402      -1.866 -13.947  -8.572  1.00 41.52           O  
ANISOU 2591  O   HOH A 402     3148   8491   4138   -978   -970   2520       O  
HETATM 2592  O  AHOH A 403      17.199 -20.190   6.380  0.61 32.66           O  
ANISOU 2592  O  AHOH A 403     5387   2108   4914    357   3015    273       O  
HETATM 2593  O  BHOH A 403      18.785 -18.004   5.323  0.39 29.64           O  
ANISOU 2593  O  BHOH A 403     3118   4353   3789  -1926   -764   1467       O  
HETATM 2594  O   HOH A 404       1.540 -15.429   8.845  1.00 40.17           O  
ANISOU 2594  O   HOH A 404     4822   7095   3346   -967  -1087   -540       O  
HETATM 2595  O   HOH A 405       6.338  -8.059 -22.133  1.00 31.64           O  
ANISOU 2595  O   HOH A 405     3728   1798   6494   -125   -953    623       O  
HETATM 2596  O   HOH A 406      12.290 -32.684 -23.592  1.00 41.84           O  
ANISOU 2596  O   HOH A 406     7508   4943   3446   2181    439  -1322       O  
HETATM 2597  O  AHOH A 407     -12.807 -17.609  -3.103  0.70 14.50           O  
ANISOU 2597  O  AHOH A 407     1874   1735   1902    -30    140   -287       O  
HETATM 2598  O  BHOH A 408      12.639 -34.601 -15.615  0.64 31.88           O  
ANISOU 2598  O  BHOH A 408     2364   5776   3971   -873   1282   -710       O  
HETATM 2599  O   HOH A 409      10.715 -31.788  -5.149  1.00 19.77           O  
ANISOU 2599  O   HOH A 409     2301   2940   2271   1170   -423   -465       O  
HETATM 2600  O   HOH A 410      -3.345 -34.190  -9.906  1.00 24.03           O  
ANISOU 2600  O   HOH A 410     4180   2102   2850  -1251   1684   -889       O  
HETATM 2601  O   HOH A 411       2.164 -23.464 -31.730  1.00 24.77           O  
ANISOU 2601  O   HOH A 411     3560   2134   3717   -286   -298    858       O  
HETATM 2602  O   HOH A 412       8.731 -33.126 -22.634  1.00 29.14           O  
ANISOU 2602  O   HOH A 412     3826   4864   2382  -1383  -1239    -39       O  
HETATM 2603  O   HOH A 413     -10.231 -26.802   2.014  1.00  8.68           O  
ANISOU 2603  O   HOH A 413     1151    986   1162   -115    139    -36       O  
HETATM 2604  O   HOH A 414     -14.510 -28.756  -1.413  1.00 23.07           O  
ANISOU 2604  O   HOH A 414     2244   4677   1844  -1595    499   -863       O  
HETATM 2605  O   HOH A 415      -6.836 -27.064 -29.554  1.00 29.07           O  
ANISOU 2605  O   HOH A 415     3956   3845   3244    161  -1514   -822       O  
HETATM 2606  O   HOH A 416      12.464 -19.961 -31.538  1.00 36.66           O  
ANISOU 2606  O   HOH A 416     6328   3694   3907  -1982   1824   -981       O  
HETATM 2607  O   HOH A 417      11.511 -23.530 -24.139  1.00 41.94           O  
ANISOU 2607  O   HOH A 417     3045   7646   5245   -128    -16  -1167       O  
HETATM 2608  O  AHOH A 418      -7.014 -33.083 -12.967  0.50 15.58           O  
ANISOU 2608  O  AHOH A 418     2546   1387   1988    -27   -538   -230       O  
HETATM 2609  O  BHOH A 418      -7.429 -33.883 -13.649  0.50 19.01           O  
ANISOU 2609  O  BHOH A 418     2777   1396   3050     52    301    341       O  
HETATM 2610  O   HOH A 419      -1.981 -21.127 -20.417  1.00 10.00           O  
ANISOU 2610  O   HOH A 419     1258   1338   1205     -3   -189   -122       O  
HETATM 2611  O   HOH A 420      19.247 -15.473   4.664  1.00 44.74           O  
ANISOU 2611  O   HOH A 420    11116   2970   2915   -398   -793    -35       O  
HETATM 2612  O  AHOH A 421     -10.282 -17.206  -5.759  0.70 11.54           O  
ANISOU 2612  O  AHOH A 421     1265   1194   1925    -48    233   -300       O  
HETATM 2613  O  BHOH A 421     -10.901 -18.275  -5.566  0.30  8.95           O  
ANISOU 2613  O  BHOH A 421      822   1437   1142    -74     85   -157       O  
HETATM 2614  O   HOH A 422      -4.166 -36.289 -19.090  1.00 26.47           O  
ANISOU 2614  O   HOH A 422     2142   1730   6185   -178   1257   -575       O  
HETATM 2615  O   HOH A 423      12.541 -22.030   8.850  1.00 29.98           O  
ANISOU 2615  O   HOH A 423     5378   3399   2614   1947    545   1030       O  
HETATM 2616  O  AHOH A 424      24.517 -24.548  -1.002  0.71 17.21           O  
ANISOU 2616  O  AHOH A 424     1481   3496   1564    414    -72    378       O  
HETATM 2617  O   HOH A 425      -3.924 -17.637 -26.628  1.00 31.01           O  
ANISOU 2617  O   HOH A 425     4667   4586   2529   -352   -958   1617       O  
HETATM 2618  O   HOH A 426      11.036 -26.435 -17.111  1.00  9.84           O  
ANISOU 2618  O   HOH A 426     1260   1223   1254    188    192   -215       O  
HETATM 2619  H2  HOH A 426      10.374 -25.983 -16.860  1.00 11.80           H  
HETATM 2620  O   HOH A 427       7.956 -13.089   2.602  1.00 22.90           O  
ANISOU 2620  O   HOH A 427     3147   3542   2013   1111   -610   -723       O  
HETATM 2621  O   HOH A 428       7.306 -33.742   7.813  1.00 31.53           O  
ANISOU 2621  O   HOH A 428     2364   2702   6914    392    -19   1616       O  
HETATM 2622  O   HOH A 429      12.976 -35.675 -11.240  1.00 27.07           O  
ANISOU 2622  O   HOH A 429     2632   1678   5974    357   -472    314       O  
HETATM 2623  O   HOH A 430       5.319 -31.615  10.775  1.00 43.90           O  
ANISOU 2623  O   HOH A 430     7966   4517   4198   -147    999   2166       O  
HETATM 2624  O   HOH A 431      -7.753 -28.699 -22.078  1.00 17.40           O  
ANISOU 2624  O   HOH A 431     1883   2762   1968   -475    -93     18       O  
HETATM 2625  O   HOH A 432     -13.818 -29.097  -5.502  1.00 11.59           O  
ANISOU 2625  O   HOH A 432     1380   1765   1261   -484    -27    -18       O  
HETATM 2626  H1  HOH A 432     -13.184 -28.962  -6.036  1.00 13.91           H  
HETATM 2627  H2  HOH A 432     -13.485 -29.120  -4.731  1.00 13.91           H  
HETATM 2628  O   HOH A 433       7.602  -7.760  -8.897  1.00 14.99           O  
ANISOU 2628  O   HOH A 433     1968   1575   2154    239    567   -215       O  
HETATM 2629  O   HOH A 434      -6.009 -11.148 -28.921  1.00 34.59           O  
ANISOU 2629  O   HOH A 434     4540   3447   5156   1499    543   1964       O  
HETATM 2630  O   HOH A 435       6.168  -8.225  -5.293  1.00 27.69           O  
ANISOU 2630  O   HOH A 435     4120   2708   3695   1419   1911    644       O  
HETATM 2631  O   HOH A 436      10.296  -9.895 -21.139  1.00 13.88           O  
ANISOU 2631  O   HOH A 436     2648   1299   1329    -51   -351     63       O  
HETATM 2632  O   HOH A 437      12.900 -27.401 -23.326  1.00 26.88           O  
ANISOU 2632  O   HOH A 437     4047   4351   1813   -797     39   -492       O  
HETATM 2633  O  AHOH A 438       9.812 -20.674 -25.249  0.57 17.75           O  
ANISOU 2633  O  AHOH A 438     2158   2612   1974   -622    536   -832       O  
HETATM 2634  O   HOH A 439      10.266 -33.251   7.126  1.00 36.10           O  
ANISOU 2634  O   HOH A 439     4676   4507   4534   1498     73   2298       O  
HETATM 2635  O   HOH A 440       9.088  -3.011 -11.925  1.00 19.75           O  
ANISOU 2635  O   HOH A 440     3344   2197   1965   1436    719    687       O  
HETATM 2636  O   HOH A 441       9.933 -12.969 -27.829  1.00 12.44           O  
ANISOU 2636  O   HOH A 441     1854   1709   1163    157    -45    168       O  
HETATM 2637  O   HOH A 442      -3.838 -36.240  -3.790  1.00 12.02           O  
ANISOU 2637  O   HOH A 442     1492   1292   1785     14    -86    -66       O  
HETATM 2638  O   HOH A 443      -0.775 -28.573 -11.370  1.00  8.49           O  
ANISOU 2638  O   HOH A 443     1251    902   1072    -11    -38   -123       O  
HETATM 2639  H1  HOH A 443      -0.564 -28.315 -12.141  1.00 10.19           H  
HETATM 2640  H2  HOH A 443      -1.326 -28.015 -11.069  1.00 10.19           H  
HETATM 2641  O   HOH A 444       4.124 -28.053  10.678  1.00 18.29           O  
ANISOU 2641  O   HOH A 444     2205   2560   2185   -349   -109    574       O  
HETATM 2642  O   HOH A 445     -17.621 -27.626  -9.809  1.00 35.44           O  
ANISOU 2642  O   HOH A 445     1869   5958   5638     44   1140    243       O  
HETATM 2643  O   HOH A 446      12.497 -30.898   4.224  1.00 23.19           O  
ANISOU 2643  O   HOH A 446     2270   2115   4425    414    308    900       O  
HETATM 2644  O   HOH A 447      23.374 -29.072   2.944  1.00 24.71           O  
ANISOU 2644  O   HOH A 447     5312   2179   1898   1147  -1024    -84       O  
HETATM 2645  O   HOH A 448       0.423 -21.770  11.791  1.00 34.56           O  
ANISOU 2645  O   HOH A 448     4678   5993   2461  -1092    -97   -878       O  
HETATM 2646  O   HOH A 449     -13.926 -20.230 -17.250  1.00 14.89           O  
ANISOU 2646  O   HOH A 449     1318   2066   2273    -50     64   -464       O  
HETATM 2647  O   HOH A 450      15.522  -8.593 -18.139  1.00 15.51           O  
ANISOU 2647  O   HOH A 450     1657   2510   1726   -219    164    428       O  
HETATM 2648  O   HOH A 451      23.685 -19.783   4.256  1.00 24.94           O  
ANISOU 2648  O   HOH A 451     4174   2617   2685  -1412    -46    -74       O  
HETATM 2649  O   HOH A 452      -4.455 -30.680  -1.266  1.00 11.13           O  
ANISOU 2649  O   HOH A 452     1387   1240   1604    134   -149    -40       O  
HETATM 2650  O   HOH A 453     -13.481 -19.727 -22.099  1.00 24.31           O  
ANISOU 2650  O   HOH A 453     1865   4376   2997    899   -574   -581       O  
HETATM 2651  O  AHOH A 454     -10.955 -35.883  -2.640  0.50 18.73           O  
ANISOU 2651  O  AHOH A 454     3351   1752   2012   -807    931   -448       O  
HETATM 2652  O  BHOH A 454     -11.709 -35.290  -3.886  0.50 15.41           O  
ANISOU 2652  O  BHOH A 454     2001   1369   2485   -490    291   -508       O  
HETATM 2653  O   HOH A 455     -16.790 -18.535 -14.315  1.00 28.89           O  
ANISOU 2653  O   HOH A 455     2031   5060   3885   -203  -1070   -417       O  
HETATM 2654  O   HOH A 456       6.453 -33.311 -27.535  1.00 24.07           O  
ANISOU 2654  O   HOH A 456     3882   1937   3326    350    209   -273       O  
HETATM 2655  O   HOH A 457      -6.234 -30.078   9.122  1.00 26.14           O  
ANISOU 2655  O   HOH A 457     3785   3314   2833  -1557   -156   1156       O  
HETATM 2656  O   HOH A 458      18.707 -19.229 -19.385  1.00 36.47           O  
ANISOU 2656  O   HOH A 458     5060   4337   4460    445   2800    604       O  
HETATM 2657  O   HOH A 459      13.624 -19.011 -25.805  1.00 26.59           O  
ANISOU 2657  O   HOH A 459     3857   2608   3638    -52   -867    -37       O  
HETATM 2658  O   HOH A 460       8.262  -6.220   1.861  1.00 45.81           O  
ANISOU 2658  O   HOH A 460     4133   5277   7997  -2051   1631  -1943       O  
HETATM 2659  O   HOH A 461     -10.188 -31.159   2.032  1.00 13.14           O  
ANISOU 2659  O   HOH A 461     1683   1462   1847   -458     60   -282       O  
HETATM 2660  O   HOH A 462      -1.227  -9.051  -3.061  1.00 19.11           O  
ANISOU 2660  O   HOH A 462     2498   2060   2701     29    216    173       O  
HETATM 2661  O  AHOH A 463       5.118 -23.330  12.350  0.50 21.80           O  
ANISOU 2661  O  AHOH A 463     3502   2762   2017   -802    193   -124       O  
HETATM 2662  O  BHOH A 463       3.978 -23.741  12.225  0.50 23.63           O  
ANISOU 2662  O  BHOH A 463     4566   2963   1448   -215   -426    599       O  
HETATM 2663  O   HOH A 464      19.156 -16.804 -15.000  1.00 26.80           O  
ANISOU 2663  O   HOH A 464     2234   4169   3778   1350    914   1411       O  
HETATM 2664  O   HOH A 465     -10.016 -18.082 -31.984  1.00 50.17           O  
ANISOU 2664  O   HOH A 465     6264   7776   5023  -1511  -2933   1661       O  
HETATM 2665  O   HOH A 466     -12.823 -16.787 -22.732  1.00 38.90           O  
ANISOU 2665  O   HOH A 466     6332   3870   4578   2607  -1237   -475       O  
HETATM 2666  O   HOH A 467      18.796 -19.651 -16.704  1.00 35.39           O  
ANISOU 2666  O   HOH A 467     2490   4058   6898    870  -1358   -303       O  
HETATM 2667  O   HOH A 468      14.726 -21.959 -23.209  1.00 28.00           O  
ANISOU 2667  O   HOH A 468     5818   2841   1979   -227    668   -751       O  
HETATM 2668  O   HOH A 469      -9.204 -20.619 -11.075  1.00  8.59           O  
ANISOU 2668  O   HOH A 469     1101    995   1170     -2    -65    -88       O  
HETATM 2669  H2  HOH A 469      -8.867 -20.774 -10.322  1.00 10.31           H  
HETATM 2670  O   HOH A 470      16.512 -23.492 -21.215  1.00 21.98           O  
ANISOU 2670  O   HOH A 470     2898   3849   1604    934    336    -88       O  
HETATM 2671  O   HOH A 471       8.712 -34.778  -4.359  1.00 40.83           O  
ANISOU 2671  O   HOH A 471     7092   5706   2715   2785    775    947       O  
HETATM 2672  O   HOH A 472       9.414 -34.437  -0.116  1.00 19.42           O  
ANISOU 2672  O   HOH A 472     2688   1994   2695    497   -816    267       O  
HETATM 2673  O  AHOH A 473      -2.157 -15.016 -20.599  0.75 13.66           O  
ANISOU 2673  O  AHOH A 473     1343   1247   2602     65     34    -26       O  
HETATM 2674  O  BHOH A 473      -2.134 -14.302 -21.216  0.25 14.48           O  
ANISOU 2674  O  BHOH A 473     1016   1740   2746   -206   -173   -923       O  
HETATM 2675  O   HOH A 474      -6.577 -19.997 -24.915  1.00 30.40           O  
ANISOU 2675  O   HOH A 474     3192   4922   3437  -1489  -1477   1860       O  
HETATM 2676  O   HOH A 475      12.231 -29.366   9.817  1.00 31.74           O  
ANISOU 2676  O   HOH A 475     4724   4347   2987    829  -1233   1523       O  
HETATM 2677  O   HOH A 476       2.648  -8.141 -23.737  1.00 29.15           O  
ANISOU 2677  O   HOH A 476     4314   3281   3480   1783   1854   1197       O  
HETATM 2678  O   HOH A 477      -0.451 -35.955   7.945  1.00 33.03           O  
ANISOU 2678  O   HOH A 477     3882   5983   2686  -1691   -865   1746       O  
HETATM 2679  O   HOH A 478       2.455 -27.468 -28.928  1.00 14.43           O  
ANISOU 2679  O   HOH A 478     2259   1822   1401    179    -94   -520       O  
HETATM 2680  O   HOH A 479       5.015 -23.081  -8.349  1.00  9.59           O  
ANISOU 2680  O   HOH A 479     1207    999   1437    102     15     55       O  
HETATM 2681  O   HOH A 480       8.820 -15.033 -16.668  1.00  9.30           O  
ANISOU 2681  O   HOH A 480     1201   1230   1101      5     92   -122       O  
HETATM 2682  O   HOH A 481      -3.702 -20.239 -23.648  1.00 12.87           O  
ANISOU 2682  O   HOH A 481     1679   1327   1882    -42    268   -213       O  
HETATM 2683  H2  HOH A 481      -4.280 -20.645 -23.193  1.00 15.44           H  
HETATM 2684  O   HOH A 482      -1.973 -21.206  -8.895  1.00  7.59           O  
ANISOU 2684  O   HOH A 482      875    928   1082    -32    -52   -159       O  
HETATM 2685  O   HOH A 483       2.181 -17.575 -32.287  1.00 20.17           O  
ANISOU 2685  O   HOH A 483     2791   2600   2273   -123   -742   -360       O  
HETATM 2686  O   HOH A 484       5.980 -21.140 -35.062  1.00 43.71           O  
ANISOU 2686  O   HOH A 484     7908   5847   2854  -1275    155   -718       O  
HETATM 2687  O   HOH A 485      19.362 -29.487  -1.830  1.00 15.30           O  
ANISOU 2687  O   HOH A 485     2284   1376   2154    -57   -189    459       O  
HETATM 2688  O   HOH A 486       0.720 -19.279  10.780  1.00 19.63           O  
ANISOU 2688  O   HOH A 486     1828   3791   1837   -119   -112    195       O  
HETATM 2689  O   HOH A 487      18.191  -9.564 -14.509  1.00 17.07           O  
ANISOU 2689  O   HOH A 487     2080   2466   1939   -771    -32    657       O  
HETATM 2690  O   HOH A 488      -7.482 -20.164   2.607  1.00  8.47           O  
ANISOU 2690  O   HOH A 488      967   1060   1190    -65     51    -27       O  
HETATM 2691  O   HOH A 489      -4.531 -13.873 -23.025  1.00 13.27           O  
ANISOU 2691  O   HOH A 489     1896   1482   1663   -221   -148    288       O  
HETATM 2692  O  AHOH A 490     -16.646 -29.246   2.431  0.50 25.20           O  
ANISOU 2692  O  AHOH A 490     2736   3555   3284  -1520   1184   -617       O  
HETATM 2693  O  BHOH A 490     -17.144 -27.582   2.083  0.50 23.68           O  
ANISOU 2693  O  BHOH A 490     1707   4649   2642   -429    238   -835       O  
HETATM 2694  O   HOH A 491       0.134 -12.248 -30.496  1.00 23.35           O  
ANISOU 2694  O   HOH A 491     2445   3745   2681    110   -205    900       O  
HETATM 2695  O   HOH A 492     -14.643 -23.767 -17.917  1.00 29.25           O  
ANISOU 2695  O   HOH A 492     2421   3678   5016   -280   -961   2109       O  
HETATM 2696  O   HOH A 493     -10.799 -27.483 -19.649  1.00 20.34           O  
ANISOU 2696  O   HOH A 493     1969   1306   4453    134   -370     36       O  
HETATM 2697  O   HOH A 494      -3.134 -32.300   5.898  1.00 13.19           O  
ANISOU 2697  O   HOH A 494     1619   1599   1794    137    -55    297       O  
HETATM 2698  O  AHOH A 495       2.203 -11.195 -14.122  0.50 17.17           O  
ANISOU 2698  O  AHOH A 495     3481   1430   1611   1020    401     57       O  
HETATM 2699  O  BHOH A 495       1.049 -11.574 -14.209  0.50 30.49           O  
ANISOU 2699  O  BHOH A 495     6799   2059   2725   -290  -1217   -145       O  
HETATM 2700  O   HOH A 496       1.673  -8.254 -21.086  1.00 20.30           O  
ANISOU 2700  O   HOH A 496     3124   1476   3112    388    872    636       O  
HETATM 2701  O   HOH A 497       0.459 -33.411 -15.893  1.00 33.44           O  
ANISOU 2701  O   HOH A 497     4707   2109   5889   -303  -1956   -596       O  
HETATM 2702  O   HOH A 498      -0.181 -10.876   6.279  1.00 26.25           O  
ANISOU 2702  O   HOH A 498     3407   3395   3172     10    430  -1100       O  
HETATM 2703  O   HOH A 499       3.071 -35.184  -5.867  1.00 39.73           O  
ANISOU 2703  O   HOH A 499     4489   3818   6787  -1289  -2200   -605       O  
HETATM 2704  O   HOH A 500       8.736 -30.526 -29.521  1.00 19.43           O  
ANISOU 2704  O   HOH A 500     2473   2845   2062  -1030    823  -1088       O  
HETATM 2705  O   HOH A 501      -5.804 -18.495   1.096  1.00  8.63           O  
ANISOU 2705  O   HOH A 501     1245    923   1110     41    162    -13       O  
HETATM 2706  O   HOH A 502     -11.870 -22.637 -15.153  1.00 13.06           O  
ANISOU 2706  O   HOH A 502     1691   1616   1655   -383     35   -116       O  
HETATM 2707  O   HOH A 503       0.331  -8.554 -30.292  1.00 15.45           O  
ANISOU 2707  O   HOH A 503     2485   1512   1874    -99    113    171       O  
HETATM 2708  O   HOH A 504       8.622  -8.960  -6.447  1.00 13.32           O  
ANISOU 2708  O   HOH A 504     1862   1491   1708   -114    -60    -86       O  
HETATM 2709  O   HOH A 505       1.442 -34.564 -17.948  1.00 27.46           O  
ANISOU 2709  O   HOH A 505     3970   2504   3959  -1082  -2174    666       O  
HETATM 2710  O  AHOH A 506      15.842 -32.679 -10.199  0.50 20.98           O  
ANISOU 2710  O  AHOH A 506     2879   2233   2861    700  -1174    -23       O  
HETATM 2711  O  BHOH A 506      15.536 -33.513  -8.570  0.50 27.92           O  
ANISOU 2711  O  BHOH A 506     3187   3121   4302    586  -1228    359       O  
HETATM 2712  O   HOH A 507     -11.367 -28.558  -6.831  1.00  8.99           O  
ANISOU 2712  O   HOH A 507     1264   1020   1133   -288     26   -126       O  
HETATM 2713  O   HOH A 508      12.524 -20.298 -24.076  1.00 29.29           O  
ANISOU 2713  O   HOH A 508     3219   4361   3548     15    818  -2113       O  
HETATM 2714  O   HOH A 509       9.370 -16.921 -33.832  1.00 24.41           O  
ANISOU 2714  O   HOH A 509     3832   2823   2621    -64   1325    523       O  
HETATM 2715  O   HOH A 510      13.634 -10.447 -24.458  1.00 30.24           O  
ANISOU 2715  O   HOH A 510     5293   4500   1696    -39   -287   -492       O  
HETATM 2716  O   HOH A 511       3.036 -37.190   0.617  1.00 17.84           O  
ANISOU 2716  O   HOH A 511     2139   1920   2721   -200    360    226       O  
HETATM 2717  O   HOH A 512      -1.765 -33.479 -17.471  1.00 44.17           O  
ANISOU 2717  O   HOH A 512     6387   5956   4439   3095   -773  -1964       O  
HETATM 2718  O   HOH A 513       5.496 -36.526  -3.138  1.00 16.25           O  
ANISOU 2718  O   HOH A 513     2472   1238   2462      2    129     -2       O  
HETATM 2719  O   HOH A 514      -5.749 -36.769 -15.475  1.00 24.01           O  
ANISOU 2719  O   HOH A 514     4207   2127   2790  -1167  -1204    913       O  
HETATM 2720  O   HOH A 515      -8.319 -10.852 -20.324  1.00 17.38           O  
ANISOU 2720  O   HOH A 515     1716   1361   3526    298   -414   -146       O  
HETATM 2721  O   HOH A 516      -9.255 -32.706  10.346  1.00 41.08           O  
ANISOU 2721  O   HOH A 516     6237   4715   4657    401     16   1304       O  
HETATM 2722  O   HOH A 517     -13.113 -24.756 -21.871  1.00 24.93           O  
ANISOU 2722  O   HOH A 517     3323   3187   2961   -191  -1476   -618       O  
HETATM 2723  O   HOH A 518       8.924 -12.496 -32.549  1.00 41.27           O  
ANISOU 2723  O   HOH A 518     5812   5367   4503  -1901    606   2143       O  
HETATM 2724  O   HOH A 519     -15.280 -18.170 -10.442  1.00 18.07           O  
ANISOU 2724  O   HOH A 519     1923   2861   2082    136    -31     81       O  
HETATM 2725  O   HOH A 520      -8.384 -13.162  -2.437  1.00 21.99           O  
ANISOU 2725  O   HOH A 520     2363   3358   2633   1352    560    685       O  
HETATM 2726  O   HOH A 521       5.701 -18.694 -35.361  1.00 37.05           O  
ANISOU 2726  O   HOH A 521     7467   3607   3003    -41   -355  -1382       O  
HETATM 2727  O   HOH A 522       8.304 -33.451 -17.429  1.00 18.08           O  
ANISOU 2727  O   HOH A 522     1994   1548   3328    -43    642  -1031       O  
HETATM 2728  O   HOH A 523      -3.330 -25.826  -0.568  1.00  8.19           O  
ANISOU 2728  O   HOH A 523     1016    945   1149    -53     45   -110       O  
HETATM 2729  H2  HOH A 523      -3.073 -25.206  -0.062  1.00  9.82           H  
HETATM 2730  O   HOH A 524      17.990 -25.999 -18.473  1.00 24.81           O  
ANISOU 2730  O   HOH A 524     3820   3117   2489   1393   -132   -845       O  
HETATM 2731  O   HOH A 525       9.016 -14.536   8.645  1.00 39.95           O  
ANISOU 2731  O   HOH A 525     3672   3254   8251    853  -2554  -1981       O  
HETATM 2732  O   HOH A 526      -0.195 -14.118   7.003  1.00 21.55           O  
ANISOU 2732  O   HOH A 526     3227   2145   2816   -712   1453   -505       O  
HETATM 2733  O   HOH A 527      -5.621 -30.179  -4.628  1.00  8.98           O  
ANISOU 2733  O   HOH A 527     1131    866   1416    -10      3   -209       O  
HETATM 2734  H1  HOH A 527      -6.380 -29.869  -4.443  1.00 10.78           H  
HETATM 2735  H2  HOH A 527      -5.057 -29.669  -4.272  1.00 10.78           H  
HETATM 2736  O   HOH A 528       5.366 -12.008 -34.528  1.00 27.99           O  
ANISOU 2736  O   HOH A 528     6017   2486   2133   1786    283    261       O  
HETATM 2737  O   HOH A 529      -9.389 -22.820   4.330  1.00  9.00           O  
ANISOU 2737  O   HOH A 529     1131   1091   1198   -110    122   -148       O  
HETATM 2738  O   HOH A 530      13.147 -12.085 -26.744  1.00 37.56           O  
ANISOU 2738  O   HOH A 530     4236   4985   5048    510   1702   2497       O  
HETATM 2739  O  AHOH A 531     -10.084 -34.937   0.094  0.69 15.91           O  
ANISOU 2739  O  AHOH A 531     1793   1309   2944   -616    -54    -14       O  
HETATM 2740  O   HOH A 532      -9.025 -29.003   3.309  1.00  9.48           O  
ANISOU 2740  O   HOH A 532     1245    971   1387   -113    141     14       O  
HETATM 2741  H1  HOH A 532      -9.254 -29.776   3.074  1.00 11.38           H  
HETATM 2742  O   HOH A 533      -0.847 -33.542 -10.832  1.00 14.10           O  
ANISOU 2742  O   HOH A 533     2016   1108   2234   -166   -390   -433       O  
HETATM 2743  O   HOH A 534       8.812 -25.049 -26.129  1.00 20.92           O  
ANISOU 2743  O   HOH A 534     2133   2093   3724    287   -261    -10       O  
HETATM 2744  O   HOH A 535      -7.982 -29.018  -3.767  1.00  8.66           O  
ANISOU 2744  O   HOH A 535     1157    890   1245    -61     19   -126       O  
HETATM 2745  H1  HOH A 535      -8.551 -28.507  -4.115  1.00 10.39           H  
HETATM 2746  H2  HOH A 535      -7.656 -28.607  -3.110  1.00 10.39           H  
HETATM 2747  O  AHOH A 536      10.893  -8.905 -32.433  0.50 17.80           O  
ANISOU 2747  O  AHOH A 536     2189   2357   2216    596    444    526       O  
HETATM 2748  O   HOH A 537       1.520 -28.699   9.862  1.00 17.51           O  
ANISOU 2748  O   HOH A 537     2020   2760   1874   -260   -129    125       O  
HETATM 2749  O   HOH A 538      -2.266 -25.615 -28.339  1.00 14.23           O  
ANISOU 2749  O   HOH A 538     2338   1775   1294   -185   -127   -297       O  
HETATM 2750  O   HOH A 539      14.412 -16.347 -26.162  1.00 34.74           O  
ANISOU 2750  O   HOH A 539     5255   4750   3197   -144   2166   -832       O  
HETATM 2751  O   HOH A 540       6.374 -35.711  -7.685  1.00 29.01           O  
ANISOU 2751  O   HOH A 540     3628   1708   5687   -290   -287   -867       O  
HETATM 2752  O   HOH A 541      -8.375 -28.235   9.095  1.00 19.65           O  
ANISOU 2752  O   HOH A 541     3273   2391   1804    557   -148    363       O  
HETATM 2753  O   HOH A 542      11.446 -34.043 -19.720  1.00 34.94           O  
ANISOU 2753  O   HOH A 542     5174   2473   5627    150   1972    822       O  
HETATM 2754  O   HOH A 543       3.035  -8.436 -27.560  1.00 18.87           O  
ANISOU 2754  O   HOH A 543     2146   2514   2510    -46   -112    853       O  
HETATM 2755  O   HOH A 544      -5.611 -11.322  -3.972  1.00 17.90           O  
ANISOU 2755  O   HOH A 544     2211   2455   2134    831    320     -6       O  
HETATM 2756  O   HOH A 545       6.433 -13.827   4.825  1.00 19.44           O  
ANISOU 2756  O   HOH A 545     1599   2354   3434   -543    -75     45       O  
HETATM 2757  O   HOH A 546      -3.848 -19.798  -7.291  1.00  7.76           O  
ANISOU 2757  O   HOH A 546      885    982   1082    -60     38   -165       O  
HETATM 2758  H1  HOH A 546      -3.213 -20.161  -7.704  1.00  9.31           H  
HETATM 2759  O   HOH A 547       7.285 -21.768 -25.481  1.00 12.14           O  
ANISOU 2759  O   HOH A 547     1734   1811   1068     58    137   -321       O  
HETATM 2760  O   HOH A 548       3.434 -21.179  11.352  1.00 18.85           O  
ANISOU 2760  O   HOH A 548     3463   2523   1175   -359   -229     40       O  
HETATM 2761  O   HOH A 549     -10.122 -11.055 -16.829  1.00 33.83           O  
ANISOU 2761  O   HOH A 549     5515   4898   2440  -2302   1044   -207       O  
HETATM 2762  O   HOH A 550     -15.174 -24.966 -14.565  1.00 44.58           O  
ANISOU 2762  O   HOH A 550     4673   6104   6162   2833  -1214    425       O  
HETATM 2763  O   HOH A 551      -6.057 -32.770   9.198  1.00 48.68           O  
ANISOU 2763  O   HOH A 551     4827   6357   7312    708  -1494   2577       O  
HETATM 2764  O   HOH A 552       4.688  -7.878  -8.640  1.00 42.21           O  
ANISOU 2764  O   HOH A 552     4799   2376   8864    400    970   -340       O  
HETATM 2765  O  AHOH A 553      22.959 -27.379  -7.008  0.59 15.48           O  
ANISOU 2765  O  AHOH A 553     2065   1898   1919   1056   -302   -219       O  
HETATM 2766  O   HOH A 554      -9.574 -13.259 -28.081  1.00 32.40           O  
ANISOU 2766  O   HOH A 554     3007   5682   3620   1858   -833    -14       O  
HETATM 2767  O   HOH A 555      -1.131 -28.691  -0.549  1.00  9.96           O  
ANISOU 2767  O   HOH A 555     1451   1056   1276    213    220     60       O  
HETATM 2768  O  AHOH A 556      18.404 -14.298 -19.001  0.77 31.72           O  
ANISOU 2768  O  AHOH A 556     3694   2592   5766   -294   2627   -485       O  
HETATM 2769  O  BHOH A 556      17.892 -13.960 -20.135  0.23 12.02           O  
ANISOU 2769  O  BHOH A 556     1197   1798   1573    704    299   -268       O  
HETATM 2770  O   HOH A 557     -15.765 -28.511 -13.636  1.00 20.85           O  
ANISOU 2770  O   HOH A 557     1600   4145   2175   -638   -303   -100       O  
HETATM 2771  O   HOH A 558      -4.762 -34.793   5.196  1.00 38.28           O  
ANISOU 2771  O   HOH A 558     4176   3181   7189   -880  -1206    226       O  
HETATM 2772  O   HOH A 559     -14.960 -22.770   7.762  1.00 10.34           O  
ANISOU 2772  O   HOH A 559     1362   1383   1183     98    147   -144       O  
HETATM 2773  O   HOH A 560       1.022  -8.084 -25.924  1.00 33.24           O  
ANISOU 2773  O   HOH A 560     5014   4706   2911   1719    -77    499       O  
HETATM 2774  O   HOH A 561      10.406 -27.530 -27.395  1.00 30.78           O  
ANISOU 2774  O   HOH A 561     2315   5098   4280   -787    -60  -1682       O  
HETATM 2775  O  AHOH A 562      10.261 -23.464 -31.920  0.50 15.63           O  
ANISOU 2775  O  AHOH A 562     1793   1410   2736    448    700   -169       O  
HETATM 2776  O  BHOH A 562      11.459 -23.515 -32.364  0.50 25.14           O  
ANISOU 2776  O  BHOH A 562     3868   3011   2672   1909  -1048   -762       O  
HETATM 2777  O   HOH A 563       5.387 -15.174   7.599  1.00 21.47           O  
ANISOU 2777  O   HOH A 563     3087   2305   2763   -155  -1032   -341       O  
HETATM 2778  O   HOH A 564      -1.927 -40.276   3.565  1.00 35.10           O  
ANISOU 2778  O   HOH A 564     5880   3767   3689  -2113  -1040   1532       O  
HETATM 2779  O  AHOH A 565      23.630 -22.964  -9.075  0.50 22.84           O  
ANISOU 2779  O  AHOH A 565     2570   3485   2622   -184    158    -49       O  
HETATM 2780  O  BHOH A 565      22.871 -20.962  -7.945  0.50 16.74           O  
ANISOU 2780  O  BHOH A 565     1241   2444   2676   -137     37    110       O  
HETATM 2781  O   HOH A 566      10.429 -33.561   2.269  1.00 15.58           O  
ANISOU 2781  O   HOH A 566     2094   1350   2476    188   -107    504       O  
HETATM 2782  O   HOH A 567       0.826 -17.543 -17.368  1.00 13.51           O  
ANISOU 2782  O   HOH A 567     1900   1529   1703   -256    140      2       O  
HETATM 2783  O   HOH A 568      -2.660 -25.672  10.441  1.00 23.34           O  
ANISOU 2783  O   HOH A 568     4398   2616   1853   -962   1127     61       O  
HETATM 2784  O  AHOH A 569     -15.648 -22.383  -6.584  0.70 19.66           O  
ANISOU 2784  O  AHOH A 569     1915   1875   3679   -263   -930   -403       O  
HETATM 2785  O  BHOH A 569     -16.686 -22.504  -7.270  0.30 11.65           O  
ANISOU 2785  O  BHOH A 569      713   2051   1663    -78   -158   -712       O  
HETATM 2786  O   HOH A 570      -4.310  -9.339 -24.902  1.00 38.02           O  
ANISOU 2786  O   HOH A 570     3062   5453   5930    430  -1403   2091       O  
HETATM 2787  O   HOH A 571      -2.547 -23.568 -30.093  1.00 15.60           O  
ANISOU 2787  O   HOH A 571     2674   1910   1344    101   -181   -113       O  
HETATM 2788  O   HOH A 572      19.611 -19.782 -11.504  1.00 12.13           O  
ANISOU 2788  O   HOH A 572     1527   1545   1537    441     74    -18       O  
HETATM 2789  O   HOH A 573      12.638 -32.950  -6.596  1.00 23.44           O  
ANISOU 2789  O   HOH A 573     2480   3600   2827    698   -539    831       O  
HETATM 2790  O   HOH A 574       1.530 -35.281 -14.469  1.00 18.32           O  
ANISOU 2790  O   HOH A 574     1998   1593   3370   -136     56   -244       O  
HETATM 2791  O   HOH A 575      -2.325 -12.150 -17.465  1.00 21.91           O  
ANISOU 2791  O   HOH A 575     2431   3206   2686    282   -373    203       O  
HETATM 2792  O   HOH A 576       3.565 -25.494 -30.617  1.00 15.79           O  
ANISOU 2792  O   HOH A 576     2563   2025   1413    -41   -144   -515       O  
HETATM 2793  O   HOH A 577     -10.160 -17.029   2.918  1.00 15.10           O  
ANISOU 2793  O   HOH A 577     1188   1735   2814   -177   -193    678       O  
HETATM 2794  O  AHOH A 578      -6.386 -32.960 -10.419  0.50 16.51           O  
ANISOU 2794  O  AHOH A 578     2746   1940   1588    251    206    277       O  
HETATM 2795  O  BHOH A 578      -7.844 -33.441 -10.570  0.50 21.77           O  
ANISOU 2795  O  BHOH A 578     2593   3295   2385    480    485   -362       O  
HETATM 2796  O   HOH A 579       2.316 -35.262 -23.085  1.00 27.73           O  
ANISOU 2796  O   HOH A 579     4415   1766   4355    -94   1363   -864       O  
HETATM 2797  O   HOH A 580      15.106 -32.390 -22.156  1.00 35.23           O  
ANISOU 2797  O   HOH A 580     5168   4776   3443   2205   1807    455       O  
HETATM 2798  O  AHOH A 581      -8.976 -15.664   0.450  0.50  9.10           O  
ANISOU 2798  O  AHOH A 581      992   1049   1418    -32    338    159       O  
HETATM 2799  O  BHOH A 581      -9.002 -15.228  -0.031  0.50 21.40           O  
ANISOU 2799  O  BHOH A 581     1498   3740   2892    455    -32  -1660       O  
HETATM 2800  O   HOH A 582     -16.722 -26.110  -1.442  1.00 30.62           O  
ANISOU 2800  O   HOH A 582     3385   4220   4030  -2032   1067  -1353       O  
HETATM 2801  O   HOH A 583      10.929 -27.048 -19.892  1.00 15.45           O  
ANISOU 2801  O   HOH A 583     2519   1634   1717    281    262   -564       O  
HETATM 2802  O   HOH A 584      12.956   0.224 -13.374  1.00 24.51           O  
ANISOU 2802  O   HOH A 584     3935   1558   3820    264  -2181   -186       O  
HETATM 2803  O   HOH A 585       0.164 -15.916 -31.855  1.00 33.24           O  
ANISOU 2803  O   HOH A 585     4218   3370   5040    831  -2183    158       O  
HETATM 2804  O   HOH A 586     -12.269 -33.277 -12.172  1.00 20.56           O  
ANISOU 2804  O   HOH A 586     4187   1722   1902  -1180   -262   -154       O  
HETATM 2805  O   HOH A 587       5.870 -35.751   6.866  1.00 26.67           O  
ANISOU 2805  O   HOH A 587     3883   3234   3018   1747  -1268   -216       O  
HETATM 2806  O   HOH A 588      -4.280 -28.271  -2.699  1.00  9.41           O  
ANISOU 2806  O   HOH A 588     1202   1009   1363    -27    -15   -186       O  
HETATM 2807  O   HOH A 589     -14.208 -31.892  -4.859  1.00 21.58           O  
ANISOU 2807  O   HOH A 589     1545   4127   2529   -610     14   -648       O  
HETATM 2808  O   HOH A 590      -4.495 -37.309   3.529  1.00 26.42           O  
ANISOU 2808  O   HOH A 590     2945   3732   3360    514   -671    801       O  
HETATM 2809  O  AHOH A 591      19.218 -13.619 -16.247  0.77 17.69           O  
ANISOU 2809  O  AHOH A 591     1337   3196   2187      3    677    706       O  
HETATM 2810  O   HOH A 592       0.269 -10.916 -16.752  1.00 27.69           O  
ANISOU 2810  O   HOH A 592     5223   2816   2481   1924    -87   -492       O  
HETATM 2811  O   HOH A 593      21.028 -29.420 -10.397  1.00 46.30           O  
ANISOU 2811  O   HOH A 593     5627   5961   6004    378   1782  -1834       O  
HETATM 2812  O   HOH A 594       5.298  -6.600   1.386  1.00 29.35           O  
ANISOU 2812  O   HOH A 594     4200   2070   4882   -907   -265   -801       O  
HETATM 2813  O   HOH A 595       5.423  -6.734  -1.930  1.00 39.29           O  
ANISOU 2813  O   HOH A 595     4952   3088   6890  -1027    303   1167       O  
HETATM 2814  O  AHOH A 596      -1.556 -16.280 -17.985  0.75 22.62           O  
ANISOU 2814  O  AHOH A 596     3007   1723   3866   -642   1665   -609       O  
HETATM 2815  O  BHOH A 596      -2.419 -15.733 -18.399  0.25 27.57           O  
ANISOU 2815  O  BHOH A 596     3153   4263   3060   -755   1559    779       O  
HETATM 2816  O  AHOH A 597      19.360 -16.141 -17.764  0.77 21.32           O  
ANISOU 2816  O  AHOH A 597      986   3470   3644   -145    358     20       O  
HETATM 2817  O  BHOH A 597      19.584 -14.534 -17.644  0.23  6.48           O  
ANISOU 2817  O  BHOH A 597      434   1180    850   -163    141    234       O  
HETATM 2818  O   HOH A 598       9.729 -25.902 -23.554  1.00 29.37           O  
ANISOU 2818  O   HOH A 598     2171   3794   5195    273   -443   -312       O  
HETATM 2819  O   HOH A 599      19.917 -22.783 -11.660  1.00 12.81           O  
ANISOU 2819  O   HOH A 599     1351   2167   1349    160     19     59       O  
HETATM 2820  O   HOH A 600      -8.060 -15.354   4.118  1.00 10.86           O  
ANISOU 2820  O   HOH A 600     1253   1365   1508     13    460    -45       O  
HETATM 2821  O   HOH A 601      -4.632 -17.608 -23.968  1.00 16.18           O  
ANISOU 2821  O   HOH A 601     1973   1476   2698   -164    495   -252       O  
HETATM 2822  O   HOH A 602      12.913 -13.310   4.169  1.00 16.09           O  
ANISOU 2822  O   HOH A 602     3057   1541   1516   -704   -484   -100       O  
HETATM 2823  O   HOH A 603       7.002  -9.616 -19.439  1.00 20.83           O  
ANISOU 2823  O   HOH A 603     4195   1527   2193   -272    -61   -293       O  
HETATM 2824  O   HOH A 604      17.380 -10.969  -5.621  1.00 12.15           O  
ANISOU 2824  O   HOH A 604     1858   1258   1502   -106   -322    -98       O  
HETATM 2825  O   HOH A 605      17.270 -10.022 -17.110  1.00 20.48           O  
ANISOU 2825  O   HOH A 605     1688   3557   2535   -785    356  -1417       O  
HETATM 2826  O   HOH A 606       9.796 -28.743  11.607  1.00 24.91           O  
ANISOU 2826  O   HOH A 606     2783   2809   3872    210  -1428   1141       O  
HETATM 2827  O   HOH A 607     -15.513 -30.875   5.345  1.00 48.01           O  
ANISOU 2827  O   HOH A 607     3671   6606   7964  -2426   -421   1151       O  
HETATM 2828  O   HOH A 608      19.326 -26.115 -13.298  1.00 24.87           O  
ANISOU 2828  O   HOH A 608     3969   3577   1904   2029    881    566       O  
HETATM 2829  O   HOH A 609      10.183 -25.349 -29.310  1.00 24.23           O  
ANISOU 2829  O   HOH A 609     2769   2955   3482    344     37   -374       O  
HETATM 2830  O  AHOH A 610      -9.194 -27.226 -26.652  0.50 26.58           O  
ANISOU 2830  O  AHOH A 610     3639   2104   4355    147  -2148   -696       O  
HETATM 2831  O   HOH A 611      -8.616 -29.039 -19.363  1.00 10.24           O  
ANISOU 2831  O   HOH A 611     1376   1022   1492   -245   -198     25       O  
HETATM 2832  O   HOH A 612      11.423 -16.218 -16.179  1.00  8.65           O  
ANISOU 2832  O   HOH A 612     1177    925   1186     -8    -57    -28       O  
HETATM 2833  O   HOH A 613      14.257 -28.967   3.337  1.00 32.29           O  
ANISOU 2833  O   HOH A 613     2683   3998   5589   -220   -841   2604       O  
HETATM 2834  O   HOH A 614      16.638 -29.474 -14.886  1.00 36.85           O  
ANISOU 2834  O   HOH A 614     4739   3158   6105   1983  -1020   -526       O  
HETATM 2835  O   HOH A 615       5.267 -36.003  -0.465  1.00 14.19           O  
ANISOU 2835  O   HOH A 615     1828   1165   2399    375   -133    124       O  
HETATM 2836  O   HOH A 616     -14.475 -32.279  -9.623  1.00 45.18           O  
ANISOU 2836  O   HOH A 616     5168   3540   8460  -1516   -546  -1528       O  
HETATM 2837  O   HOH A 617      -4.546 -30.878 -23.068  1.00 36.49           O  
ANISOU 2837  O   HOH A 617     8608   2841   2415     91  -1036   -200       O  
HETATM 2838  O   HOH A 618      -4.998 -17.825  10.051  1.00 28.73           O  
ANISOU 2838  O   HOH A 618     2638   6287   1990  -1544    234   -961       O  
HETATM 2839  O   HOH A 619      14.501  -3.297 -16.632  1.00 21.02           O  
ANISOU 2839  O   HOH A 619     2177   2639   3171   -443   -389   1402       O  
HETATM 2840  O   HOH A 620      11.952 -36.143  -6.420  1.00 41.15           O  
ANISOU 2840  O   HOH A 620     4836   4333   6467    674   1125   2017       O  
HETATM 2841  O  AHOH A 621      22.392 -15.597 -11.324  0.50 20.64           O  
ANISOU 2841  O  AHOH A 621     1642   3849   2351   -334   -601    982       O  
HETATM 2842  O  BHOH A 621      21.320 -15.478 -12.488  0.50 25.33           O  
ANISOU 2842  O  BHOH A 621     1820   2471   5332   -104   1184    265       O  
HETATM 2843  O   HOH A 622      -6.335 -35.433 -21.497  1.00 24.61           O  
ANISOU 2843  O   HOH A 622     2162   4068   3121   -576    972  -1295       O  
HETATM 2844  O   HOH A 623      13.035 -25.234 -29.244  1.00 44.33           O  
ANISOU 2844  O   HOH A 623     5224   3464   8156   1492  -2720  -1614       O  
HETATM 2845  O   HOH A 624      -6.513 -32.906 -22.428  1.00 31.95           O  
ANISOU 2845  O   HOH A 624     4123   5257   2761  -1009    202  -1928       O  
HETATM 2846  O   HOH A 625      -1.489  -7.759 -28.654  1.00 49.08           O  
ANISOU 2846  O   HOH A 625     8548   6271   3829   1140    914   2160       O  
HETATM 2847  O   HOH A 626       3.832 -38.960   2.722  1.00 39.30           O  
ANISOU 2847  O   HOH A 626     7682   2527   4723    -59    859   1184       O  
HETATM 2848  O   HOH A 627       2.338 -19.258 -34.326  1.00 38.37           O  
ANISOU 2848  O   HOH A 627     6103   5276   3200    201  -1100  -1668       O  
HETATM 2849  O   HOH A 628      11.023 -32.255 -28.948  1.00 16.27           O  
ANISOU 2849  O   HOH A 628     2044   1785   2354     97    918   -209       O  
HETATM 2850  O   HOH A 629       2.123 -37.971 -14.901  1.00 19.31           O  
ANISOU 2850  O   HOH A 629     2998   1738   2602   -481     48     48       O  
HETATM 2851  O   HOH A 630      16.244  -5.894 -19.008  1.00 28.41           O  
ANISOU 2851  O   HOH A 630     3347   3744   3703  -1128   -606   1711       O  
HETATM 2852  O   HOH A 631      18.450 -33.686 -19.337  1.00 42.71           O  
ANISOU 2852  O   HOH A 631     5210   6683   4334  -2583   2080   -941       O  
HETATM 2853  O   HOH A 632      23.241 -28.371  -4.286  1.00 30.31           O  
ANISOU 2853  O   HOH A 632     4307   2811   4397   1177   1002    556       O  
HETATM 2854  O   HOH A 633     -12.684 -34.429   0.589  1.00 42.36           O  
ANISOU 2854  O   HOH A 633     5380   5883   4830  -1789   1727    477       O  
HETATM 2855  O   HOH A 634      18.679 -21.396 -20.888  1.00 34.65           O  
ANISOU 2855  O   HOH A 634     3765   5421   3981   1335    965   1239       O  
HETATM 2856  O   HOH A 635       8.978 -25.960 -21.199  1.00 25.56           O  
ANISOU 2856  O   HOH A 635     3614   2472   3624   1353  -1060  -1163       O  
HETATM 2857  O   HOH A 636     -16.637 -24.806   8.318  1.00 20.59           O  
ANISOU 2857  O   HOH A 636     4297   2085   1441  -1219    458    -78       O  
HETATM 2858  O   HOH A 637       9.729  -5.333 -20.804  1.00 34.12           O  
ANISOU 2858  O   HOH A 637     4521   2358   6084    698  -3005   -881       O  
HETATM 2859  O   HOH A 638     -10.075 -20.871   6.090  1.00 13.55           O  
ANISOU 2859  O   HOH A 638     2344   1338   1466    381    404    -95       O  
HETATM 2860  O   HOH A 639      22.864 -29.338  -8.908  1.00 41.50           O  
ANISOU 2860  O   HOH A 639     5476   3269   7025   1449  -1797  -1058       O  
HETATM 2861  O  AHOH A 640      22.888 -18.657  -7.837  0.50 24.20           O  
ANISOU 2861  O  AHOH A 640     1760   4783   2652  -1117    254  -1034       O  
HETATM 2862  O   HOH A 641      -2.381 -31.440 -24.473  1.00 44.88           O  
ANISOU 2862  O   HOH A 641     3827   4655   8570  -1283   1826  -1875       O  
HETATM 2863  O  AHOH A 642     -11.190 -15.829  -4.087  0.70 26.83           O  
ANISOU 2863  O  AHOH A 642     3014   5035   2147   1956   -274   -631       O  
HETATM 2864  O  BHOH A 642      -9.950 -15.044  -4.070  0.30 10.59           O  
ANISOU 2864  O  BHOH A 642     1132   1054   1838   -428    260   -493       O  
HETATM 2865  O   HOH A 643      15.048 -10.096 -20.248  1.00 21.24           O  
ANISOU 2865  O   HOH A 643     2555   2171   3343    233   -742   -804       O  
HETATM 2866  O   HOH A 644     -12.810 -23.230 -24.231  1.00 45.52           O  
ANISOU 2866  O   HOH A 644     4329   6926   6040    281  -2291   1973       O  
HETATM 2867  O   HOH A 645     -16.235 -20.946 -10.769  1.00 43.68           O  
ANISOU 2867  O   HOH A 645     3345   4689   8562    348   -399   2205       O  
HETATM 2868  O   HOH A 646      -3.458 -15.650   9.472  1.00 26.89           O  
ANISOU 2868  O   HOH A 646     3176   5488   1552  -1318    -63   -229       O  
HETATM 2869  O   HOH A 647       1.845 -38.776  -1.785  1.00 32.19           O  
ANISOU 2869  O   HOH A 647     3158   2388   6685    783    946    933       O  
HETATM 2870  O   HOH A 648      -0.936 -15.594  10.748  1.00 43.23           O  
ANISOU 2870  O   HOH A 648     5912   6127   4385  -1453  -2660   -186       O  
HETATM 2871  O   HOH A 649       8.451 -37.622  -2.518  1.00 49.15           O  
ANISOU 2871  O   HOH A 649     6358   2680   9637    658   1499     31       O  
HETATM 2872  O   HOH A 650     -14.960 -19.916 -19.812  1.00 36.79           O  
ANISOU 2872  O   HOH A 650     2621   8676   2680   1441   -105    157       O  
HETATM 2873  O  AHOH A 651     -16.374 -21.203 -13.591  0.50 24.82           O  
ANISOU 2873  O  AHOH A 651     2189   3280   3961   -190    566   -398       O  
HETATM 2874  O   HOH A 652      -1.837 -14.370 -15.961  1.00 39.60           O  
ANISOU 2874  O   HOH A 652     8274   2733   4038   -184  -1219   -938       O  
HETATM 2875  O   HOH A 653      21.659 -30.526  -3.066  1.00 27.10           O  
ANISOU 2875  O   HOH A 653     4464   3346   2487   1941   -348    425       O  
HETATM 2876  O   HOH A 654       8.084 -33.819 -20.278  1.00 35.13           O  
ANISOU 2876  O   HOH A 654     5861   2981   4506   -644   -962    547       O  
HETATM 2877  O   HOH A 655      22.618 -22.381 -11.828  1.00 42.20           O  
ANISOU 2877  O   HOH A 655     2359   5458   8218    566    871   1006       O  
HETATM 2878  O   HOH A 656      11.754 -17.998 -33.287  1.00 30.18           O  
ANISOU 2878  O   HOH A 656     4036   4950   2482    555    797    378       O  
HETATM 2879  O   HOH A 657      17.277 -11.305 -21.485  1.00 27.89           O  
ANISOU 2879  O   HOH A 657     3013   3726   3857   -212   1319   -587       O  
HETATM 2880  O   HOH A 658      -3.473 -32.543   8.530  1.00 32.05           O  
ANISOU 2880  O   HOH A 658     4948   4300   2930    881   1030   1797       O  
HETATM 2881  O   HOH A 659       3.282  -9.154 -12.841  1.00 36.64           O  
ANISOU 2881  O   HOH A 659     5608   2423   5889    587   2734    953       O  
HETATM 2882  O   HOH A 660     -12.848 -31.538   1.351  1.00 24.40           O  
ANISOU 2882  O   HOH A 660     1870   4166   3236   -680    -46  -1302       O  
HETATM 2883  O   HOH A 661       7.582 -37.127   0.442  1.00 32.33           O  
ANISOU 2883  O   HOH A 661     3361   4682   4240   2120  -1061   -537       O  
HETATM 2884  O   HOH A 662      12.936  -9.385 -22.003  1.00 18.84           O  
ANISOU 2884  O   HOH A 662     3093   2388   1678    177   -106   -118       O  
HETATM 2885  O  AHOH A 663     -16.490 -22.711  -8.592  0.70 34.04           O  
ANISOU 2885  O  AHOH A 663     2760   6006   4168   1370   -334     55       O  
HETATM 2886  O   HOH A 664      -7.761 -28.709 -28.042  1.00 38.47           O  
ANISOU 2886  O   HOH A 664     4649   4557   5410  -2530  -1390    724       O  
HETATM 2887  O   HOH A 665      -0.207 -17.246  12.542  1.00 50.78           O  
ANISOU 2887  O   HOH A 665     8139   5810   5347  -1031   1898  -1639       O  
HETATM 2888  O   HOH A 666     -12.566 -35.424  -6.634  1.00 23.24           O  
ANISOU 2888  O   HOH A 666     3347   1911   3573    146    -42     52       O  
HETATM 2889  O   HOH A 667      12.614 -27.138 -26.062  1.00 32.80           O  
ANISOU 2889  O   HOH A 667     2856   6403   3203   -196  -1165    423       O  
HETATM 2890  O   HOH A 668     -16.275 -30.677 -13.056  1.00 42.04           O  
ANISOU 2890  O   HOH A 668     5342   7061   3572   -964  -1203   -135       O  
HETATM 2891  O  AHOH A 669     -14.585 -22.149 -15.015  0.50 17.97           O  
ANISOU 2891  O  AHOH A 669     1335   2016   3476   -279     69   -394       O  
HETATM 2892  O  BHOH A 669     -15.768 -22.269 -14.520  0.50 22.27           O  
ANISOU 2892  O  BHOH A 669     1665   2764   4033   -750    630  -1175       O  
HETATM 2893  O   HOH A 670     -14.305 -32.890 -13.993  1.00 22.41           O  
ANISOU 2893  O   HOH A 670     3082   1931   3503     73    737   -559       O  
HETATM 2894  O  AHOH A 671      19.917 -19.114 -14.119  0.50 20.44           O  
ANISOU 2894  O  AHOH A 671     2877   3192   1695   1623    776    848       O  
HETATM 2895  O  BHOH A 671      19.381 -20.256 -14.094  0.50 27.44           O  
ANISOU 2895  O  BHOH A 671     2761   3211   4454  -1496    204   -301       O  
HETATM 2896  O  AHOH A 672      -4.864 -34.669 -13.900  0.50 14.74           O  
ANISOU 2896  O  AHOH A 672     1969   1369   2263   -104   -554   -284       O  
HETATM 2897  O  BHOH A 672      -5.512 -34.606 -11.662  0.50 26.36           O  
ANISOU 2897  O  BHOH A 672     3228   2165   4622   -323  -1642   1250       O  
HETATM 2898  O   HOH A 673      22.000 -19.156 -10.308  1.00 32.69           O  
ANISOU 2898  O   HOH A 673     2338   6465   3618  -1504   -536    323       O  
HETATM 2899  O  AHOH A 674       3.498 -19.158  13.273  0.50 28.30           O  
ANISOU 2899  O  AHOH A 674     3977   4264   2512    272   -592  -1332       O  
HETATM 2900  O  BHOH A 674       3.950 -17.111  12.600  0.50 28.62           O  
ANISOU 2900  O  BHOH A 674     4109   4661   2106    -18     31   -840       O  
HETATM 2901  O   HOH A 675     -10.784 -30.863 -26.252  1.00 31.37           O  
ANISOU 2901  O   HOH A 675     3532   5001   3388  -1788     45   -210       O  
HETATM 2902  O   HOH A 676       9.094  -7.574 -21.972  1.00 25.65           O  
ANISOU 2902  O   HOH A 676     4640   1537   3568    223  -1883    -86       O  
HETATM 2903  O   HOH A 677     -10.351 -28.690  10.877  1.00 37.53           O  
ANISOU 2903  O   HOH A 677     7323   3894   3044    900    343   1012       O  
HETATM 2904  O   HOH A 678      25.146 -27.089  -2.117  1.00 36.55           O  
ANISOU 2904  O   HOH A 678     3656   4521   5712   1018   1592    641       O  
HETATM 2905  O   HOH A 679      19.621 -30.669   0.558  1.00 28.67           O  
ANISOU 2905  O   HOH A 679     4348   3514   3030   -365   -262   1909       O  
HETATM 2906  O  AHOH A 680     -10.564 -15.035  -1.628  0.50 12.97           O  
ANISOU 2906  O  AHOH A 680     1315   1641   1973    407    316    181       O  
HETATM 2907  O  BHOH A 680     -11.256 -15.768  -1.585  0.50 11.37           O  
ANISOU 2907  O  BHOH A 680     1083   1528   1710     24     45   -380       O  
HETATM 2908  O   HOH A 681      17.070 -29.736   3.280  1.00 45.95           O  
ANISOU 2908  O   HOH A 681     4859   6518   6082  -2206  -2014   3490       O  
HETATM 2909  O   HOH A 682     -13.736 -22.439  10.212  1.00  9.96           O  
ANISOU 2909  O   HOH A 682     1405   1134   1246    -12    226   -107       O  
HETATM 2910  O   HOH A 683     -17.297 -28.145   4.893  1.00 40.95           O  
ANISOU 2910  O   HOH A 683     5143   4847   5569  -2400   2070   -385       O  
HETATM 2911  O   HOH A 684     -16.912 -28.216  -2.764  1.00 35.42           O  
ANISOU 2911  O   HOH A 684     3683   6777   2996  -2337   1092  -1758       O  
HETATM 2912  O   HOH A 685      -3.863  -9.189 -28.995  1.00 34.37           O  
ANISOU 2912  O   HOH A 685     2861   2428   7770    481  -1093    219       O  
HETATM 2913  O  AHOH A 686      27.636 -21.846  -1.063  0.50 22.27           O  
ANISOU 2913  O  AHOH A 686     2188   1979   4297    545   -906  -1368       O  
HETATM 2914  O  BHOH A 686      26.345 -22.413  -1.879  0.50 28.83           O  
ANISOU 2914  O  BHOH A 686     5444   2832   2678    137    927   -814       O  
HETATM 2915  O   HOH A 687       7.589  -5.478  -2.821  1.00 49.02           O  
ANISOU 2915  O   HOH A 687     3627   4920  10077   1397    543  -1126       O  
HETATM 2916  O   HOH A 688       3.131  -8.133 -17.391  1.00 40.91           O  
ANISOU 2916  O   HOH A 688     6046   3706   5792   1525   2410   2135       O  
HETATM 2917  O   HOH A 689      16.272 -12.205 -24.176  1.00 42.80           O  
ANISOU 2917  O   HOH A 689     5695   6455   4112  -2353   2027  -1144       O  
HETATM 2918  O   HOH A 690     -16.832 -31.285 -10.278  1.00 42.46           O  
ANISOU 2918  O   HOH A 690     3582   6348   6204  -1887   -330    936       O  
HETATM 2919  O   HOH A 691      -4.078 -27.470 -29.264  1.00 25.47           O  
ANISOU 2919  O   HOH A 691     3600   2990   3089  -1121     60  -1311       O  
HETATM 2920  O   HOH A 692      -2.576 -34.358 -15.429  1.00 25.16           O  
ANISOU 2920  O   HOH A 692     2824   2678   4059    289  -1311  -1491       O  
HETATM 2921  O   HOH A 693     -17.752 -26.248  -6.912  1.00 43.07           O  
ANISOU 2921  O   HOH A 693     2084   6769   7512   -131   -162     51       O  
HETATM 2922  O   HOH A 694      20.821 -22.181  12.435  1.00 34.40           O  
ANISOU 2922  O   HOH A 694     4687   4280   4103    853   -694   -788       O  
HETATM 2923  O  AHOH A 695     -17.966 -23.673  -5.214  0.70 37.46           O  
ANISOU 2923  O  AHOH A 695     2531   5716   5985    590  -1118  -1056       O  
HETATM 2924  O   HOH A 696      11.267  -8.361  -6.284  1.00 11.69           O  
ANISOU 2924  O   HOH A 696     1552   1603   1287   -252   -287    -35       O  
HETATM 2925  O  AHOH A 697      -3.964 -29.987 -27.957  0.50 24.22           O  
ANISOU 2925  O  AHOH A 697     3875   1750   3577   -202    100   -159       O  
HETATM 2926  O  BHOH A 697      -4.831 -30.405 -26.961  0.50 21.13           O  
ANISOU 2926  O  BHOH A 697     3442   2083   2504   -465   -648    323       O  
HETATM 2927  O   HOH A 698     -16.483 -28.375  -5.594  1.00 16.31           O  
ANISOU 2927  O   HOH A 698     1555   2629   2012   -440      0   -309       O  
HETATM 2928  O   HOH A 699      17.037 -30.474  -2.741  1.00 29.10           O  
ANISOU 2928  O   HOH A 699     3369   3354   4333   -406   -812   -111       O  
HETATM 2929  O   HOH A 700      16.949 -21.257 -25.056  1.00 39.43           O  
ANISOU 2929  O   HOH A 700     7270   4087   3626    292    919  -1822       O  
HETATM 2930  O   HOH A 701      22.240 -30.932   1.315  1.00 21.51           O  
ANISOU 2930  O   HOH A 701     3772   1922   2479    -29   -563    919       O  
HETATM 2931  O   HOH A 702      -0.278 -27.361 -29.215  1.00 15.95           O  
ANISOU 2931  O   HOH A 702     2235   2223   1602    -12   -114   -473       O  
HETATM 2932  O   HOH A 703      15.152   1.412 -15.819  1.00 40.64           O  
ANISOU 2932  O   HOH A 703     4303   4486   6652   -613  -3020    455       O  
HETATM 2933  O  AHOH A 704      18.420 -27.124 -21.056  0.50 20.77           O  
ANISOU 2933  O  AHOH A 704     2921   2512   2457   -248   1366   -867       O  
HETATM 2934  O  BHOH A 704      17.720 -25.789 -22.387  0.50 27.13           O  
ANISOU 2934  O  BHOH A 704     2420   4799   3089    117    573  -1918       O  
HETATM 2935  O   HOH A 705      -0.563 -42.415  -0.488  1.00 43.04           O  
ANISOU 2935  O   HOH A 705     6085   7941   2326   1727   -412   -181       O  
HETATM 2936  O   HOH A 706      -9.894 -20.328   8.977  1.00 11.12           O  
ANISOU 2936  O   HOH A 706     1429   1240   1555    -37    466    -84       O  
HETATM 2937  O   HOH A 707      -6.224 -20.208  11.540  1.00 29.34           O  
ANISOU 2937  O   HOH A 707     3478   4975   2696   -418    490  -1093       O  
HETATM 2938  O  AHOH A 708      24.902 -17.182  -7.534  0.50 23.81           O  
ANISOU 2938  O  AHOH A 708     2115   4677   2253   -202    188  -1129       O  
HETATM 2939  O  BHOH A 708      23.493 -16.342  -8.091  0.50 24.17           O  
ANISOU 2939  O  BHOH A 708     1479   3268   4435     68    -38  -1115       O  
HETATM 2940  O   HOH A 709      -7.391 -43.053   2.886  1.00 44.03           O  
ANISOU 2940  O   HOH A 709     6441   7064   3225  -2777     99  -1175       O  
HETATM 2941  O   HOH A 710      -1.140 -30.093 -28.784  1.00 36.65           O  
ANISOU 2941  O   HOH A 710     6737   4013   3174  -2419   1104  -1245       O  
HETATM 2942  O   HOH A 711      11.544 -32.003   9.879  1.00 29.78           O  
ANISOU 2942  O   HOH A 711     4500   3028   3785    607  -1992    646       O  
HETATM 2943  O   HOH A 712       8.457  -4.007  -0.827  1.00 41.95           O  
ANISOU 2943  O   HOH A 712     3399   8052   4488   2005   -256   -847       O  
HETATM 2944  O   HOH A 713      -0.542 -23.986 -31.948  1.00 20.78           O  
ANISOU 2944  O   HOH A 713     3512   2396   1989   -256    339    -91       O  
HETATM 2945  O   HOH A 714       0.873  -5.551 -20.108  1.00 30.10           O  
ANISOU 2945  O   HOH A 714     4096   4052   3289   1229   1025   1967       O  
HETATM 2946  O   HOH A 715       1.091 -35.363  -7.662  1.00 40.97           O  
ANISOU 2946  O   HOH A 715     6126   2122   7319     76    489   1045       O  
HETATM 2947  O   HOH A 716      17.179 -22.912 -29.179  1.00 21.78           O  
ANISOU 2947  O   HOH A 716     2973   2390   2914     15    396   -912       O  
HETATM 2948  O  AHOH A 717     -12.351 -24.136  11.823  0.50 17.78           O  
ANISOU 2948  O  AHOH A 717     3337   1899   1518    656    488    410       O  
HETATM 2949  O  BHOH A 717     -13.081 -25.099  12.081  0.50 27.97           O  
ANISOU 2949  O  BHOH A 717     3705   3125   3798   -500   2106    212       O  
HETATM 2950  O   HOH A 718      -3.292 -27.535 -31.988  1.00 43.71           O  
ANISOU 2950  O   HOH A 718     6946   4866   4797  -2092   2571  -1959       O  
HETATM 2951  O   HOH A 719      23.447 -31.208  -1.118  1.00 37.98           O  
ANISOU 2951  O   HOH A 719     6355   5546   2528   2969   -963   -559       O  
HETATM 2952  O   HOH A 720     -17.683 -30.532  -6.809  1.00 39.12           O  
ANISOU 2952  O   HOH A 720     2871   5369   6625   -817   -366  -2642       O  
HETATM 2953  O   HOH A 721      29.286 -21.082  -3.452  1.00 41.77           O  
ANISOU 2953  O   HOH A 721     4587   5411   5873   -847   -444  -2923       O  
HETATM 2954  O   HOH A 722      -8.421 -21.807  10.822  1.00 28.30           O  
ANISOU 2954  O   HOH A 722     1957   6200   2596    384    -52   1428       O  
HETATM 2955  O   HOH A 723      -1.443 -23.034 -34.429  1.00 39.80           O  
ANISOU 2955  O   HOH A 723     8598   4036   2489   -277  -1204    -17       O  
HETATM 2956  O   HOH A 724      24.590 -14.049  -6.938  1.00 18.29           O  
ANISOU 2956  O   HOH A 724     1947   3494   1507   -817    -11    -75       O  
HETATM 2957  O   HOH A 725      -0.515 -26.717 -31.891  1.00 26.32           O  
ANISOU 2957  O   HOH A 725     5310   2804   1887   -634   -521   -166       O  
HETATM 2958  O   HOH A 726      -9.965 -23.488  12.320  1.00 45.18           O  
ANISOU 2958  O   HOH A 726     6771   7157   3239   1419  -1874     18       O  
HETATM 2959  O   HOH A 727      -6.411 -19.244  14.125  1.00 36.17           O  
ANISOU 2959  O   HOH A 727     3208   7844   2692   2364    151    347       O  
HETATM 2960  O   HOH A 728      21.447 -34.343  -0.705  1.00 30.45           O  
ANISOU 2960  O   HOH A 728     6065   3862   1641      3    538    323       O  
HETATM 2961  O   HOH A 729      23.052 -29.721 -20.073  1.00 43.28           O  
ANISOU 2961  O   HOH A 729     6235   7485   2726  -1025   -152  -1728       O  
HETATM 2962  O   HOH A 730      -9.415 -22.135  14.610  1.00 34.69           O  
ANISOU 2962  O   HOH A 730     2240   3653   7288    390   1180    -86       O  
HETATM 2963  O   HOH A 731      26.069 -27.224 -22.010  1.00 45.84           O  
ANISOU 2963  O   HOH A 731     9100   4197   4120   -212  -2414   -746       O  
CONECT   71 1611                                                                
CONECT  292  494                                                                
CONECT  494  292                                                                
CONECT  635 2569                                                                
CONECT  658 2569                                                                
CONECT  698 2569                                                                
CONECT  758 2569                                                                
CONECT 1339 2394                                                                
CONECT 1383 2095                                                                
CONECT 1611   71                                                                
CONECT 1739 1896                                                                
CONECT 1896 1739                                                                
CONECT 2002 2253 2254                                                           
CONECT 2095 1383                                                                
CONECT 2253 2002                                                                
CONECT 2254 2002                                                                
CONECT 2394 1339                                                                
CONECT 2569  635  658  698  758                                                 
CONECT 2569 2603 2737                                                           
CONECT 2570 2571 2572 2573 2574                                                 
CONECT 2571 2570                                                                
CONECT 2572 2570                                                                
CONECT 2573 2570                                                                
CONECT 2574 2570                                                                
CONECT 2575 2576 2577 2578 2579                                                 
CONECT 2576 2575                                                                
CONECT 2577 2575                                                                
CONECT 2578 2575                                                                
CONECT 2579 2575                                                                
CONECT 2580 2581 2582 2583 2584                                                 
CONECT 2581 2580                                                                
CONECT 2582 2580                                                                
CONECT 2583 2580                                                                
CONECT 2584 2580                                                                
CONECT 2585 2586 2587 2588 2589                                                 
CONECT 2586 2585                                                                
CONECT 2587 2585                                                                
CONECT 2588 2585                                                                
CONECT 2589 2585                                                                
CONECT 2603 2569                                                                
CONECT 2737 2569                                                                
MASTER      307    0    5    3   14    0   10    6 1975    1   41   18          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.