CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 21-AUG-18 6M8F  ***

elNémo ID: 21021620234717538

Job options:

ID        	=	 21021620234717538
JOBID     	=	 TRANSFERASE 21-AUG-18 6M8F
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    TRANSFERASE                             21-AUG-18   6M8F              
TITLE     ENGINEERED SPERM WHALE MYOGLOBIN-BASED CARBENE TRANSFERASE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOGLOBIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;                               
SOURCE   3 ORGANISM_COMMON: SPERM WHALE;                                        
SOURCE   4 ORGANISM_TAXID: 9755;                                                
SOURCE   5 GENE: MB;                                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    METALLOPROTEIN, MYOGLOBIN, CARBENE TRANSFERASE, CYCLOPROPANATION,     
KEYWDS   2 HEME, TRANSFERASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.BACIK,N.ANDO,R.FASAN                                              
REVDAT   3   29-JUL-20 6M8F    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                   1       HETSYN FORMUL LINK   SITE                
REVDAT   3 3                   1       ATOM                                     
REVDAT   2   12-JUN-19 6M8F    1       JRNL                                     
REVDAT   1   23-JAN-19 6M8F    0                                                
JRNL        AUTH   A.TINOCO,Y.WEI,J.P.BACIK,D.M.CARMINATI,E.J.MOORE,N.ANDO,     
JRNL        AUTH 2 Y.ZHANG,R.FASAN                                              
JRNL        TITL   ORIGIN OF HIGH STEREOCONTROL IN OLEFIN CYCLOPROPANATION      
JRNL        TITL 2 CATALYZED BY AN ENGINEERED CARBENE TRANSFERASE.              
JRNL        REF    ACS CATALYSIS                 V.   9  1514 2019              
JRNL        REFN                   ESSN 2155-5435                               
JRNL        PMID   31134138                                                     
JRNL        DOI    10.1021/ACSCATAL.8B04073                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.16                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 76038                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.127                           
REMARK   3   R VALUE            (WORKING SET) : 0.126                           
REMARK   3   FREE R VALUE                     : 0.146                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3765                            
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 32.1765 -  3.2989    1.00     3175   158  0.1434 0.1612        
REMARK   3     2  3.2989 -  2.6188    1.00     3063   209  0.1291 0.1513        
REMARK   3     3  2.6188 -  2.2879    1.00     3056   183  0.1131 0.1311        
REMARK   3     4  2.2879 -  2.0788    1.00     3077   151  0.1059 0.1247        
REMARK   3     5  2.0788 -  1.9298    1.00     3063   172  0.1149 0.1207        
REMARK   3     6  1.9298 -  1.8160    1.00     3042   159  0.1105 0.1221        
REMARK   3     7  1.8160 -  1.7251    1.00     3098   150  0.1104 0.1461        
REMARK   3     8  1.7251 -  1.6500    1.00     3065   148  0.1068 0.1381        
REMARK   3     9  1.6500 -  1.5865    1.00     3012   190  0.1084 0.1169        
REMARK   3    10  1.5865 -  1.5317    1.00     3082   139  0.1006 0.1158        
REMARK   3    11  1.5317 -  1.4838    1.00     3072   161  0.0990 0.1426        
REMARK   3    12  1.4838 -  1.4414    1.00     3047   149  0.1066 0.1132        
REMARK   3    13  1.4414 -  1.4035    1.00     3072   141  0.1128 0.1181        
REMARK   3    14  1.4035 -  1.3692    1.00     3069   127  0.1112 0.1375        
REMARK   3    15  1.3692 -  1.3381    1.00     3040   156  0.1107 0.1224        
REMARK   3    16  1.3381 -  1.3096    1.00     3059   165  0.1179 0.1485        
REMARK   3    17  1.3096 -  1.2834    0.98     2989   134  0.1275 0.1589        
REMARK   3    18  1.2834 -  1.2592    0.98     2978   159  0.1352 0.1482        
REMARK   3    19  1.2592 -  1.2367    0.94     2840   171  0.1569 0.2009        
REMARK   3    20  1.2367 -  1.2157    0.87     2667   145  0.1717 0.2217        
REMARK   3    21  1.2157 -  1.1961    0.82     2479   111  0.1877 0.2123        
REMARK   3    22  1.1961 -  1.1777    0.75     2286   115  0.1954 0.2226        
REMARK   3    23  1.1777 -  1.1604    0.68     2072   125  0.2130 0.2374        
REMARK   3    24  1.1604 -  1.1441    0.58     1735    97  0.2331 0.2407        
REMARK   3    25  1.1441 -  1.1286    0.47     1433    67  0.2685 0.2604        
REMARK   3    26  1.1286 -  1.1139    0.36     1107    48  0.2753 0.3029        
REMARK   3    27  1.1139 -  1.1000    0.20      595    35  0.3220 0.3356        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.070            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.270           
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      :  0.008           1408                                  
REMARK   3   ANGLE     :  1.134           1919                                  
REMARK   3   CHIRALITY :  0.076            203                                  
REMARK   3   PLANARITY :  0.006            230                                  
REMARK   3   DIHEDRAL  : 29.707            524                                  
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 6M8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236303.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9768                             
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76057                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1JW8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: A CRYSTAL WAS GROWN BY MIXING 1 UL OF    
REMARK 280  RESERVOIR BUFFER (2 M AMMONIUM SULFATE, 0.2 M TRIS PH 8.6) WITH     
REMARK 280  1 UL OF PROTEIN IN BUFFER (20 MM TRIS PH 8.0, 1 MM EDTA). THE       
REMARK 280  CRYSTAL WAS CRYOPROTECTED BY SOAKING IT IN A DROP CONTAINING        
REMARK 280  RESERVOIR BUFFER SUPPLEMENTED WITH 25% SUCROSE FOR 5 MINUTES        
REMARK 280  PRIOR TO BEING FLASH-COOLED IN LIQUID NITROGEN, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 296K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 492  LIES ON A SPECIAL POSITION.                          
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 102    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  20       73.81   -157.08                                   
REMARK 500    PHE A  46       26.83   -144.59                                   
REMARK 500    LYS A  98       61.85     61.94                                   
REMARK 500    PHE A 123       49.78   -141.46                                   
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 523        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH A 524        DISTANCE =  6.55 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                             HEM A 202  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 HEM A 202   NA   90.3                                              
REMARK 620 3 HEM A 202   NB   91.2  89.5                                        
REMARK 620 4 HEM A 202   NC   94.3 175.4  89.9                                  
REMARK 620 5 HEM A 202   ND   93.6  90.4 175.1  89.8                            
REMARK 620 6 HOH A 395   O   176.8  86.5  89.4  88.9  85.7                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  6M8F A    0   153  UNP    P02185   MYG_PHYCD        1    154             
SEQADV 6M8F VAL A   64  UNP  P02185    HIS    65 CONFLICT                       
SEQADV 6M8F ALA A   68  UNP  P02185    VAL    69 CONFLICT                       
SEQADV 6M8F ASN A  122  UNP  P02185    ASP   123 CONFLICT                       
SEQRES   1 A  154  MET VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS          
SEQRES   2 A  154  VAL TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY          
SEQRES   3 A  154  GLN ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU          
SEQRES   4 A  154  THR LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR          
SEQRES   5 A  154  GLU ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS VAL          
SEQRES   6 A  154  GLY VAL THR ALA LEU THR ALA LEU GLY ALA ILE LEU LYS          
SEQRES   7 A  154  LYS LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA          
SEQRES   8 A  154  GLN SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR          
SEQRES   9 A  154  LEU GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS          
SEQRES  10 A  154  SER ARG HIS PRO GLY ASN PHE GLY ALA ASP ALA GLN GLY          
SEQRES  11 A  154  ALA MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE          
SEQRES  12 A  154  ALA ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY                  
HET    GLC  B   1      22                                                       
HET    FRU  B   2      23                                                       
HET    SO4  A 201       5                                                       
HET    HEM  A 202      73                                                       
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     FRU BETA-D-FRUCTOFURANOSE                                            
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     HEM HEME                                                             
FORMUL   2  GLC    C6 H12 O6                                                    
FORMUL   2  FRU    C6 H12 O6                                                    
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   4  HEM    C34 H32 FE N4 O4                                             
FORMUL   7  HOH   *224(H2 O)                                                    
HELIX    1 AA1 SER A    3  GLU A   18  1                                  16    
HELIX    2 AA2 ASP A   20  HIS A   36  1                                  17    
HELIX    3 AA3 PRO A   37  PHE A   43  5                                   7    
HELIX    4 AA4 THR A   51  SER A   58  1                                   8    
HELIX    5 AA5 SER A   58  LYS A   78  1                                  21    
HELIX    6 AA6 HIS A   82  LYS A   96  1                                  15    
HELIX    7 AA7 PRO A  100  HIS A  119  1                                  20    
HELIX    8 AA8 PRO A  120  PHE A  123  5                                   4    
HELIX    9 AA9 GLY A  124  LEU A  149  1                                  26    
LINK         C1  GLC B   1                 O2  FRU B   2     1555   1555  1.42  
LINK         NE2 HIS A  93                FE   HEM A 202     1555   1555  2.11  
LINK        FE   HEM A 202                 O   HOH A 395     1555   1555  2.16  
CRYST1   90.780   90.780   45.580  90.00  90.00 120.00 P 6           6          
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      0.011016  0.006360  0.000000        0.00000                         
SCALE2      0.000000  0.012720  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021939        0.00000                         
ATOM      1  N   MET A   0      23.597   8.636 -10.186  1.00 39.07           N  
ANISOU    1  N   MET A   0     3973   5291   5582   -189   -722     83       N  
ATOM      2  CA  MET A   0      23.848  10.096 -10.006  1.00 37.31           C  
ANISOU    2  CA  MET A   0     3877   5253   5045   -174   -864   -120       C  
ATOM      3  C   MET A   0      25.296  10.407 -10.350  1.00 32.70           C  
ANISOU    3  C   MET A   0     3599   4495   4328   -428   -842   -146       C  
ATOM      4  O   MET A   0      26.195   9.605 -10.084  1.00 32.46           O  
ANISOU    4  O   MET A   0     3723   4460   4150   -504   -753    130       O  
ATOM      5  CB  MET A   0      23.559  10.514  -8.566  1.00 38.72           C  
ANISOU    5  CB  MET A   0     3942   5712   5058   -160  -1089   -461       C  
ATOM      6  CG  MET A   0      24.357   9.718  -7.554  1.00 39.24           C  
ANISOU    6  CG  MET A   0     3905   5984   5021   -167  -1279   -672       C  
ATOM      7  SD  MET A   0      24.005  10.104  -5.835  1.00 38.57           S  
ANISOU    7  SD  MET A   0     3796   6166   4692   -216  -1648   -968       S  
ATOM      8  CE  MET A   0      24.674  11.776  -5.661  1.00 35.71           C  
ANISOU    8  CE  MET A   0     3652   5833   4085   -451  -1911  -1182       C  
ATOM      9  H1  MET A   0      23.107   8.333  -9.508  1.00 46.89           H  
ATOM     10  H2  MET A   0      23.160   8.502 -10.950  1.00 46.89           H  
ATOM     11  H3  MET A   0      24.374   8.202 -10.208  1.00 46.89           H  
ATOM     12  HA  MET A   0      23.262  10.598 -10.594  1.00 44.77           H  
ATOM     13  HB2 MET A   0      23.786  11.451  -8.458  1.00 46.47           H  
ATOM     14  HB3 MET A   0      22.617  10.377  -8.380  1.00 46.47           H  
ATOM     15  HG2 MET A   0      24.171   8.776  -7.686  1.00 47.09           H  
ATOM     16  HG3 MET A   0      25.301   9.887  -7.704  1.00 47.09           H  
ATOM     17  HE1 MET A   0      24.531  12.080  -4.751  1.00 42.86           H  
ATOM     18  HE2 MET A   0      25.624  11.758  -5.858  1.00 42.86           H  
ATOM     19  HE3 MET A   0      24.218  12.365  -6.283  1.00 42.86           H  
ATOM     20  N   VAL A   1      25.518  11.580 -10.935  1.00 27.99           N  
ANISOU   20  N   VAL A   1     3267   3680   3688   -386   -794   -437       N  
ATOM     21  CA  VAL A   1      26.832  11.974 -11.430  1.00 23.06           C  
ANISOU   21  CA  VAL A   1     2919   2932   2912   -179   -547   -821       C  
ATOM     22  C   VAL A   1      27.026  13.456 -11.151  1.00 19.38           C  
ANISOU   22  C   VAL A   1     2428   2506   2428     89   -422   -536       C  
ATOM     23  O   VAL A   1      26.206  14.282 -11.563  1.00 20.73           O  
ANISOU   23  O   VAL A   1     2412   2711   2754     51   -684   -403       O  
ATOM     24  CB  VAL A   1      26.962  11.686 -12.940  1.00 24.46           C  
ANISOU   24  CB  VAL A   1     3187   2996   3109    -55   -375  -1191       C  
ATOM     25  CG1 VAL A   1      28.271  12.216 -13.478  1.00 24.48           C  
ANISOU   25  CG1 VAL A   1     3082   3019   3200   -177   -240  -1217       C  
ATOM     26  CG2 VAL A   1      26.859  10.192 -13.211  1.00 27.04           C  
ANISOU   26  CG2 VAL A   1     3382   3255   3635     -5   -360  -1122       C  
ATOM     27  H   VAL A   1      24.911  12.176 -11.060  1.00 33.59           H  
ATOM     28  HA  VAL A   1      27.520  11.477 -10.960  1.00 27.68           H  
ATOM     29  HB  VAL A   1      26.239  12.129 -13.412  1.00 29.35           H  
ATOM     30 HG11 VAL A   1      28.324  12.021 -14.427  1.00 29.38           H  
ATOM     31 HG12 VAL A   1      28.306  13.175 -13.335  1.00 29.38           H  
ATOM     32 HG13 VAL A   1      29.002  11.784 -13.010  1.00 29.38           H  
ATOM     33 HG21 VAL A   1      26.944  10.039 -14.165  1.00 32.44           H  
ATOM     34 HG22 VAL A   1      27.573   9.736 -12.738  1.00 32.44           H  
ATOM     35 HG23 VAL A   1      25.998   9.874 -12.899  1.00 32.44           H  
ATOM     36  N   LEU A   2      28.113  13.794 -10.466  1.00 14.24           N  
ANISOU   36  N   LEU A   2     1946   1908   1555     91    -50   -201       N  
ATOM     37  CA  LEU A   2      28.459  15.190 -10.250  1.00 12.26           C  
ANISOU   37  CA  LEU A   2     1783   1566   1307    305   -201   -195       C  
ATOM     38  C   LEU A   2      29.107  15.777 -11.501  1.00 12.47           C  
ANISOU   38  C   LEU A   2     1805   1596   1336    333    -80   -272       C  
ATOM     39  O   LEU A   2      29.814  15.094 -12.248  1.00 13.99           O  
ANISOU   39  O   LEU A   2     2095   1680   1541    399     83   -110       O  
ATOM     40  CB  LEU A   2      29.434  15.329  -9.081  1.00 12.22           C  
ANISOU   40  CB  LEU A   2     1788   1509   1347    532     74   -127       C  
ATOM     41  CG  LEU A   2      28.818  15.287  -7.679  1.00 12.29           C  
ANISOU   41  CG  LEU A   2     1753   1605   1310    573     -9    -46       C  
ATOM     42  CD1 LEU A   2      28.374  13.875  -7.270  1.00 14.20           C  
ANISOU   42  CD1 LEU A   2     1856   1789   1749    519    131    136       C  
ATOM     43  CD2 LEU A   2      29.800  15.863  -6.657  1.00 12.66           C  
ANISOU   43  CD2 LEU A   2     1846   1699   1264    499     86   -173       C  
ATOM     44  H   LEU A   2      28.664  13.234 -10.116  1.00 17.08           H  
ATOM     45  HA  LEU A   2      27.658  15.698 -10.048  1.00 14.71           H  
ATOM     46  HB2 LEU A   2      30.078  14.606  -9.135  1.00 14.67           H  
ATOM     47  HB3 LEU A   2      29.895  16.178  -9.169  1.00 14.67           H  
ATOM     48  HG  LEU A   2      28.030  15.852  -7.674  1.00 14.74           H  
ATOM     49 HD11 LEU A   2      27.994  13.910  -6.378  1.00 17.04           H  
ATOM     50 HD12 LEU A   2      27.708  13.558  -7.901  1.00 17.04           H  
ATOM     51 HD13 LEU A   2      29.145  13.287  -7.278  1.00 17.04           H  
ATOM     52 HD21 LEU A   2      29.394  15.829  -5.776  1.00 15.19           H  
ATOM     53 HD22 LEU A   2      30.613  15.335  -6.668  1.00 15.19           H  
ATOM     54 HD23 LEU A   2      29.999  16.783  -6.894  1.00 15.19           H  
ATOM     55  N   SER A   3      28.868  17.062 -11.722  1.00 11.98           N  
ANISOU   55  N   SER A   3     1761   1551   1238    226   -116   -182       N  
ATOM     56  CA  SER A   3      29.586  17.786 -12.754  1.00 12.70           C  
ANISOU   56  CA  SER A   3     2005   1617   1203    429   -196   -136       C  
ATOM     57  C   SER A   3      30.989  18.127 -12.263  1.00 11.88           C  
ANISOU   57  C   SER A   3     1964   1417   1134    343    -15     -4       C  
ATOM     58  O   SER A   3      31.278  18.122 -11.063  1.00 11.44           O  
ANISOU   58  O   SER A   3     1868   1366   1111    242    -63   -134       O  
ATOM     59  CB  SER A   3      28.867  19.090 -13.083  1.00 13.91           C  
ANISOU   59  CB  SER A   3     2054   1772   1459    374   -345   -207       C  
ATOM     60  OG  SER A   3      28.942  19.972 -11.984  1.00 13.79           O  
ANISOU   60  OG  SER A   3     2131   1733   1374    485   -275   -218       O  
ATOM     61  H   SER A   3      28.297  17.536 -11.287  1.00 14.37           H  
ATOM     62  HA  SER A   3      29.652  17.246 -13.558  1.00 15.24           H  
ATOM     63  HB2 SER A   3      29.291  19.502 -13.852  1.00 16.69           H  
ATOM     64  HB3 SER A   3      27.936  18.900 -13.276  1.00 16.69           H  
ATOM     65  HG  SER A   3      28.546  20.691 -12.165  1.00 16.54           H  
ATOM     66  N   GLU A   4      31.862  18.484 -13.208  1.00 12.56           N  
ANISOU   66  N   GLU A   4     2072   1543   1158    256   -150     -6       N  
ATOM     67  CA  GLU A   4      33.191  18.951 -12.827  1.00 12.21           C  
ANISOU   67  CA  GLU A   4     2140   1390   1111     13     33    -90       C  
ATOM     68  C   GLU A   4      33.104  20.185 -11.932  1.00 12.38           C  
ANISOU   68  C   GLU A   4     2245   1329   1130     41     39    -11       C  
ATOM     69  O   GLU A   4      33.877  20.320 -10.982  1.00 12.45           O  
ANISOU   69  O   GLU A   4     2134   1445   1151    -19     98   -124       O  
ATOM     70  CB  GLU A   4      34.054  19.214 -14.068  1.00 13.59           C  
ANISOU   70  CB  GLU A   4     2250   1733   1180    159     21   -245       C  
ATOM     71  CG  GLU A   4      35.424  19.855 -13.781  1.00 15.14           C  
ANISOU   71  CG  GLU A   4     2307   1994   1451     -4    284   -239       C  
ATOM     72  CD  GLU A   4      36.431  18.984 -13.022  1.00 17.11           C  
ANISOU   72  CD  GLU A   4     2485   2130   1887   -133    273   -340       C  
ATOM     73  OE1 GLU A   4      36.178  17.792 -12.761  1.00 18.37           O  
ANISOU   73  OE1 GLU A   4     2546   2304   2131    149     98   -191       O  
ATOM     74  OE2 GLU A   4      37.509  19.521 -12.674  1.00 20.08           O  
ANISOU   74  OE2 GLU A   4     2582   2546   2500   -212    184   -427       O  
ATOM     75  H   GLU A   4      31.712  18.466 -14.055  1.00 15.07           H  
ATOM     76  HA  GLU A   4      33.625  18.251 -12.315  1.00 14.66           H  
ATOM     77  HB2 GLU A   4      34.215  18.370 -14.517  1.00 16.31           H  
ATOM     78  HB3 GLU A   4      33.570  19.811 -14.660  1.00 16.31           H  
ATOM     79  HG2 GLU A   4      35.831  20.096 -14.628  1.00 18.17           H  
ATOM     80  HG3 GLU A   4      35.281  20.657 -13.254  1.00 18.17           H  
ATOM     81  N   GLY A   5      32.194  21.113 -12.238  1.00 12.94           N  
ANISOU   81  N   GLY A   5     2420   1330   1168    235    -53     -4       N  
ATOM     82  CA  GLY A   5      32.042  22.287 -11.389  1.00 12.82           C  
ANISOU   82  CA  GLY A   5     2354   1328   1190    294     27    -50       C  
ATOM     83  C   GLY A   5      31.678  21.929  -9.958  1.00 12.02           C  
ANISOU   83  C   GLY A   5     2142   1180   1244    285    -54    -51       C  
ATOM     84  O   GLY A   5      32.166  22.551  -9.003  1.00 12.26           O  
ANISOU   84  O   GLY A   5     2124   1255   1279    168    167      5       O  
ATOM     85  H   GLY A   5      31.665  21.085 -12.916  1.00 15.53           H  
ATOM     86  HA2 GLY A   5      32.873  22.787 -11.377  1.00 15.39           H  
ATOM     87  HA3 GLY A   5      31.345  22.858 -11.749  1.00 15.39           H  
ATOM     88  N   GLU A   6      30.808  20.929  -9.789  1.00 11.41           N  
ANISOU   88  N   GLU A   6     1917   1270   1149    218    -78    -38       N  
ATOM     89  CA  GLU A   6      30.461  20.455  -8.453  1.00 10.76           C  
ANISOU   89  CA  GLU A   6     1693   1128   1268    254   -110   -153       C  
ATOM     90  C   GLU A   6      31.674  19.838  -7.760  1.00  9.91           C  
ANISOU   90  C   GLU A   6     1584   1147   1034    334     45     36       C  
ATOM     91  O   GLU A   6      31.948  20.137  -6.587  1.00  9.49           O  
ANISOU   91  O   GLU A   6     1511   1050   1045    142     40    -62       O  
ATOM     92  CB  GLU A   6      29.281  19.477  -8.522  1.00 11.61           C  
ANISOU   92  CB  GLU A   6     1640   1404   1367    334    -60   -194       C  
ATOM     93  CG  GLU A   6      27.938  20.174  -8.795  1.00 12.68           C  
ANISOU   93  CG  GLU A   6     1704   1614   1498    471    -78   -202       C  
ATOM     94  CD  GLU A   6      26.802  19.248  -9.201  1.00 13.85           C  
ANISOU   94  CD  GLU A   6     1708   1859   1694    483   -137   -302       C  
ATOM     95  OE1 GLU A   6      25.638  19.645  -9.017  1.00 17.13           O  
ANISOU   95  OE1 GLU A   6     1762   2241   2507    378   -229   -724       O  
ATOM     96  OE2 GLU A   6      27.044  18.143  -9.703  1.00 14.58           O  
ANISOU   96  OE2 GLU A   6     1825   1822   1892    461   -335   -237       O  
ATOM     97  H   GLU A   6      30.409  20.514 -10.428  1.00 13.69           H  
ATOM     98  HA  GLU A   6      30.177  21.215  -7.921  1.00 12.91           H  
ATOM     99  HB2 GLU A   6      29.439  18.842  -9.238  1.00 13.93           H  
ATOM    100  HB3 GLU A   6      29.209  19.010  -7.675  1.00 13.93           H  
ATOM    101  HG2 GLU A   6      27.662  20.639  -7.989  1.00 15.21           H  
ATOM    102  HG3 GLU A   6      28.063  20.815  -9.513  1.00 15.21           H  
ATOM    103  N   TRP A   7      32.437  18.994  -8.475  1.00  9.80           N  
ANISOU  103  N   TRP A   7     1475   1152   1098    221     33    -41       N  
ATOM    104  CA  TRP A   7      33.652  18.440  -7.884  1.00  9.72           C  
ANISOU  104  CA  TRP A   7     1463   1186   1043    197     23    -69       C  
ATOM    105  C   TRP A   7      34.615  19.541  -7.457  1.00  9.95           C  
ANISOU  105  C   TRP A   7     1576   1182   1021    206    107      5       C  
ATOM    106  O   TRP A   7      35.267  19.431  -6.412  1.00  9.74           O  
ANISOU  106  O   TRP A   7     1446   1123   1131    214     99   -118       O  
ATOM    107  CB  TRP A   7      34.356  17.460  -8.836  1.00  9.82           C  
ANISOU  107  CB  TRP A   7     1377   1279   1074    177     -8   -205       C  
ATOM    108  CG  TRP A   7      33.669  16.127  -8.923  1.00  9.33           C  
ANISOU  108  CG  TRP A   7     1460   1136    950    186     58   -135       C  
ATOM    109  CD1 TRP A   7      33.135  15.563 -10.042  1.00 10.27           C  
ANISOU  109  CD1 TRP A   7     1550   1224   1127    281     70    -66       C  
ATOM    110  CD2 TRP A   7      33.425  15.199  -7.848  1.00  9.57           C  
ANISOU  110  CD2 TRP A   7     1449   1104   1081    199     80   -108       C  
ATOM    111  NE1 TRP A   7      32.580  14.342  -9.739  1.00 10.53           N  
ANISOU  111  NE1 TRP A   7     1566   1120   1314    269     40   -114       N  
ATOM    112  CE2 TRP A   7      32.737  14.098  -8.398  1.00  9.77           C  
ANISOU  112  CE2 TRP A   7     1453   1124   1134    274     53    -43       C  
ATOM    113  CE3 TRP A   7      33.737  15.189  -6.482  1.00 10.00           C  
ANISOU  113  CE3 TRP A   7     1477   1124   1198    309      3    -55       C  
ATOM    114  CZ2 TRP A   7      32.321  13.017  -7.625  1.00 10.15           C  
ANISOU  114  CZ2 TRP A   7     1510   1082   1265    315    127    -52       C  
ATOM    115  CZ3 TRP A   7      33.337  14.097  -5.714  1.00 10.55           C  
ANISOU  115  CZ3 TRP A   7     1502   1274   1235    402     38   -150       C  
ATOM    116  CH2 TRP A   7      32.638  13.028  -6.291  1.00 10.16           C  
ANISOU  116  CH2 TRP A   7     1436   1106   1317    407    200    -19       C  
ATOM    117  H   TRP A   7      32.274  18.737  -9.279  1.00 11.76           H  
ATOM    118  HA  TRP A   7      33.406  17.944  -7.087  1.00 11.66           H  
ATOM    119  HB2 TRP A   7      34.377  17.845  -9.726  1.00 11.78           H  
ATOM    120  HB3 TRP A   7      35.261  17.309  -8.520  1.00 11.78           H  
ATOM    121  HD1 TRP A   7      33.142  15.950 -10.887  1.00 12.32           H  
ATOM    122  HE1 TRP A   7      32.175  13.826 -10.296  1.00 12.63           H  
ATOM    123  HE3 TRP A   7      34.182  15.906  -6.092  1.00 12.00           H  
ATOM    124  HZ2 TRP A   7      31.883  12.292  -8.008  1.00 12.18           H  
ATOM    125  HZ3 TRP A   7      33.524  14.084  -4.803  1.00 12.67           H  
ATOM    126  HH2 TRP A   7      32.389  12.307  -5.759  1.00 12.19           H  
ATOM    127  N   GLN A   8      34.736  20.604  -8.251  1.00 10.36           N  
ANISOU  127  N   GLN A   8     1576   1191   1169     84    102    -94       N  
ATOM    128  CA  GLN A   8      35.659  21.666  -7.866  1.00 10.80           C  
ANISOU  128  CA  GLN A   8     1703   1219   1181     11    378    -43       C  
ATOM    129  C   GLN A   8      35.214  22.381  -6.594  1.00  9.84           C  
ANISOU  129  C   GLN A   8     1634   1013   1092     34    259     14       C  
ATOM    130  O   GLN A   8      36.052  22.761  -5.771  1.00 10.53           O  
ANISOU  130  O   GLN A   8     1649   1022   1329    -69     97     12       O  
ATOM    131  CB  GLN A   8      35.881  22.644  -9.015  1.00 14.29           C  
ANISOU  131  CB  GLN A   8     2196   1673   1560   -104    493   -229       C  
ATOM    132  CG  GLN A   8      36.795  22.066 -10.131  1.00 19.46           C  
ANISOU  132  CG  GLN A   8     2546   2627   2220    -93    615   -490       C  
ATOM    133  CD  GLN A   8      38.138  21.534  -9.612  1.00 25.14           C  
ANISOU  133  CD  GLN A   8     2774   3575   3204     21    581   -993       C  
ATOM    134  OE1 GLN A   8      38.761  22.139  -8.734  1.00 27.34           O  
ANISOU  134  OE1 GLN A   8     2909   3895   3585   -135    555  -1046       O  
ATOM    135  NE2 GLN A   8      38.583  20.399 -10.153  1.00 27.41           N  
ANISOU  135  NE2 GLN A   8     2724   4029   3662    143    425  -1026       N  
ATOM    136  H   GLN A   8      34.312  20.731  -8.988  1.00 12.43           H  
ATOM    137  HA  GLN A   8      36.518  21.258  -7.674  1.00 12.96           H  
ATOM    138  HB2 GLN A   8      35.024  22.863  -9.413  1.00 17.15           H  
ATOM    139  HB3 GLN A   8      36.302  23.447  -8.669  1.00 17.15           H  
ATOM    140  HG2 GLN A   8      36.332  21.332 -10.565  1.00 23.35           H  
ATOM    141  HG3 GLN A   8      36.981  22.765 -10.776  1.00 23.35           H  
ATOM    142 HE21 GLN A   8      38.122  20.003 -10.761  1.00 32.89           H  
ATOM    143 HE22 GLN A   8      39.331  20.064  -9.893  1.00 32.89           H  
ATOM    144  N   LEU A   9      33.906  22.555  -6.390  1.00 10.00           N  
ANISOU  144  N   LEU A   9     1619    976   1205     49    236     -3       N  
ATOM    145  CA  LEU A   9      33.437  23.133  -5.132  1.00 10.24           C  
ANISOU  145  CA  LEU A   9     1626   1009   1255     22    322     43       C  
ATOM    146  C   LEU A   9      33.778  22.236  -3.949  1.00  9.29           C  
ANISOU  146  C   LEU A   9     1456    993   1079    -89    106    -70       C  
ATOM    147  O   LEU A   9      34.157  22.723  -2.873  1.00 10.02           O  
ANISOU  147  O   LEU A   9     1638    952   1218    -16     75    -53       O  
ATOM    148  CB  LEU A   9      31.928  23.380  -5.210  1.00 10.54           C  
ANISOU  148  CB  LEU A   9     1779    984   1242    163    208     12       C  
ATOM    149  CG  LEU A   9      31.474  24.483  -6.171  1.00 11.94           C  
ANISOU  149  CG  LEU A   9     2101    973   1461    323    285    147       C  
ATOM    150  CD1 LEU A   9      29.958  24.540  -6.269  1.00 15.28           C  
ANISOU  150  CD1 LEU A   9     2208   1506   2090    492    216    518       C  
ATOM    151  CD2 LEU A   9      32.040  25.837  -5.731  1.00 16.38           C  
ANISOU  151  CD2 LEU A   9     2643   1092   2490    481     -7     14       C  
ATOM    152  H   LEU A   9      33.286  22.351  -6.950  1.00 12.00           H  
ATOM    153  HA  LEU A   9      33.874  23.988  -4.996  1.00 12.29           H  
ATOM    154  HB2 LEU A   9      31.499  22.557  -5.492  1.00 12.65           H  
ATOM    155  HB3 LEU A   9      31.613  23.620  -4.325  1.00 12.65           H  
ATOM    156  HG  LEU A   9      31.822  24.290  -7.056  1.00 14.32           H  
ATOM    157 HD11 LEU A   9      29.708  25.247  -6.884  1.00 18.33           H  
ATOM    158 HD12 LEU A   9      29.631  23.687  -6.595  1.00 18.33           H  
ATOM    159 HD13 LEU A   9      29.592  24.720  -5.390  1.00 18.33           H  
ATOM    160 HD21 LEU A   9      31.742  26.521  -6.351  1.00 19.66           H  
ATOM    161 HD22 LEU A   9      31.719  26.038  -4.837  1.00 19.66           H  
ATOM    162 HD23 LEU A   9      33.009  25.789  -5.732  1.00 19.66           H  
ATOM    163  N   VAL A  10      33.633  20.920  -4.129  1.00  8.97           N  
ANISOU  163  N   VAL A  10     1375    902   1131    -23     54   -114       N  
ATOM    164  CA  VAL A  10      33.973  19.947  -3.090  1.00  8.59           C  
ANISOU  164  CA  VAL A  10     1195   1030   1040    -11    160     27       C  
ATOM    165  C   VAL A  10      35.459  20.025  -2.765  1.00  8.66           C  
ANISOU  165  C   VAL A  10     1320    897   1072    -82    109   -172       C  
ATOM    166  O   VAL A  10      35.865  20.101  -1.593  1.00  9.00           O  
ANISOU  166  O   VAL A  10     1268    989   1163    -89    176   -137       O  
ATOM    167  CB  VAL A  10      33.573  18.532  -3.560  1.00  9.00           C  
ANISOU  167  CB  VAL A  10     1249    955   1217   -125    164   -110       C  
ATOM    168  CG1 VAL A  10      34.140  17.449  -2.625  1.00  9.82           C  
ANISOU  168  CG1 VAL A  10     1481    874   1376     23   -103     79       C  
ATOM    169  CG2 VAL A  10      32.059  18.411  -3.689  1.00  9.58           C  
ANISOU  169  CG2 VAL A  10     1206   1107   1328    -80     89    -20       C  
ATOM    170  H   VAL A  10      33.337  20.563  -4.854  1.00 10.76           H  
ATOM    171  HA  VAL A  10      33.474  20.152  -2.284  1.00 10.31           H  
ATOM    172  HB  VAL A  10      33.952  18.383  -4.440  1.00 10.81           H  
ATOM    173 HG11 VAL A  10      33.868  16.577  -2.952  1.00 11.78           H  
ATOM    174 HG12 VAL A  10      35.108  17.514  -2.619  1.00 11.78           H  
ATOM    175 HG13 VAL A  10      33.792  17.591  -1.731  1.00 11.78           H  
ATOM    176 HG21 VAL A  10      31.838  17.513  -3.984  1.00 11.50           H  
ATOM    177 HG22 VAL A  10      31.654  18.583  -2.824  1.00 11.50           H  
ATOM    178 HG23 VAL A  10      31.744  19.060  -4.337  1.00 11.50           H  
ATOM    179  N   LEU A  11      36.297  19.977  -3.801  1.00  9.17           N  
ANISOU  179  N   LEU A  11     1203   1056   1223    -42    207    -89       N  
ATOM    180  CA  LEU A  11      37.736  19.917  -3.578  1.00  9.87           C  
ANISOU  180  CA  LEU A  11     1191   1162   1396    -35    217    -56       C  
ATOM    181  C   LEU A  11      38.290  21.246  -3.070  1.00 10.20           C  
ANISOU  181  C   LEU A  11     1168   1284   1424   -101    253     51       C  
ATOM    182  O   LEU A  11      39.298  21.263  -2.352  1.00 10.80           O  
ANISOU  182  O   LEU A  11     1147   1407   1550   -153    142   -131       O  
ATOM    183  CB  LEU A  11      38.439  19.400  -4.836  1.00 11.26           C  
ANISOU  183  CB  LEU A  11     1343   1408   1526    114    194   -177       C  
ATOM    184  CG  LEU A  11      38.064  17.957  -5.232  1.00 12.60           C  
ANISOU  184  CG  LEU A  11     1515   1633   1641    368     23   -472       C  
ATOM    185  CD1 LEU A  11      38.694  17.575  -6.559  1.00 15.85           C  
ANISOU  185  CD1 LEU A  11     1898   2046   2080    530    111   -565       C  
ATOM    186  CD2 LEU A  11      38.469  16.948  -4.163  1.00 14.70           C  
ANISOU  186  CD2 LEU A  11     1764   1687   2133    475   -262   -339       C  
ATOM    187  H   LEU A  11      36.061  19.977  -4.628  1.00 11.00           H  
ATOM    188  HA  LEU A  11      37.899  19.264  -2.880  1.00 11.84           H  
ATOM    189  HB2 LEU A  11      38.208  19.978  -5.580  1.00 13.51           H  
ATOM    190  HB3 LEU A  11      39.397  19.425  -4.688  1.00 13.51           H  
ATOM    191  HG  LEU A  11      37.101  17.904  -5.337  1.00 15.12           H  
ATOM    192 HD11 LEU A  11      38.439  16.665  -6.779  1.00 19.02           H  
ATOM    193 HD12 LEU A  11      38.376  18.182  -7.246  1.00 19.02           H  
ATOM    194 HD13 LEU A  11      39.659  17.639  -6.481  1.00 19.02           H  
ATOM    195 HD21 LEU A  11      38.214  16.059  -4.456  1.00 17.64           H  
ATOM    196 HD22 LEU A  11      39.430  16.992  -4.036  1.00 17.64           H  
ATOM    197 HD23 LEU A  11      38.015  17.167  -3.335  1.00 17.64           H  
ATOM    198  N   HIS A  12      37.639  22.362  -3.392  1.00 10.61           N  
ANISOU  198  N   HIS A  12     1464   1123   1444   -216    243    -12       N  
ATOM    199  CA AHIS A  12      38.091  23.659  -2.900  0.49 11.94           C  
ANISOU  199  CA AHIS A  12     1779   1188   1567   -198    248    -15       C  
ATOM    200  CA BHIS A  12      38.123  23.646  -2.894  0.51 12.16           C  
ANISOU  200  CA BHIS A  12     1751   1293   1576   -143    333    185       C  
ATOM    201  C   HIS A  12      37.918  23.785  -1.385  1.00 11.15           C  
ANISOU  201  C   HIS A  12     1498   1148   1589   -272    165    -33       C  
ATOM    202  O   HIS A  12      38.797  24.306  -0.693  1.00 12.71           O  
ANISOU  202  O   HIS A  12     1439   1668   1723   -506    257    -25       O  
ATOM    203  CB AHIS A  12      37.323  24.757  -3.631  0.49 14.21           C  
ANISOU  203  CB AHIS A  12     2412   1137   1851   -112    251    -83       C  
ATOM    204  CB BHIS A  12      37.499  24.810  -3.669  0.51 15.14           C  
ANISOU  204  CB BHIS A  12     2319   1501   1931     53    541    530       C  
ATOM    205  CG AHIS A  12      37.932  26.112  -3.495  0.49 17.82           C  
ANISOU  205  CG AHIS A  12     2884   1291   2596    -20    497    111       C  
ATOM    206  CG BHIS A  12      38.108  25.032  -5.020  0.51 19.72           C  
ANISOU  206  CG BHIS A  12     2763   1936   2792    330    834    916       C  
ATOM    207  ND1AHIS A  12      39.111  26.467  -4.111  0.49 19.43           N  
ANISOU  207  ND1AHIS A  12     3118   1511   2753     90    399    158       N  
ATOM    208  ND1BHIS A  12      37.960  26.207  -5.723  0.51 23.14           N  
ANISOU  208  ND1BHIS A  12     3031   2398   3362    587    979   1007       N  
ATOM    209  CD2AHIS A  12      37.519  27.202  -2.806  0.49 19.73           C  
ANISOU  209  CD2AHIS A  12     3012   1294   3191   -106    629     -3       C  
ATOM    210  CD2BHIS A  12      38.853  24.217  -5.802  0.51 21.92           C  
ANISOU  210  CD2BHIS A  12     3020   2296   3014    493   1113   1008       C  
ATOM    211  CE1AHIS A  12      39.398  27.721  -3.801  0.49 19.23           C  
ANISOU  211  CE1AHIS A  12     3145   1202   2959      1    415   -172       C  
ATOM    212  CE1BHIS A  12      38.595  26.109  -6.877  0.51 23.46           C  
ANISOU  212  CE1BHIS A  12     3110   2561   3243    623   1216   1217       C  
ATOM    213  NE2AHIS A  12      38.448  28.189  -3.017  0.49 21.20           N  
ANISOU  213  NE2AHIS A  12     3127   1439   3489     25    520   -102       N  
ATOM    214  NE2BHIS A  12      39.148  24.913  -6.949  0.51 23.29           N  
ANISOU  214  NE2BHIS A  12     3108   2573   3170    608   1294   1086       N  
ATOM    215  H  AHIS A  12      36.938  22.394  -3.890  0.49 12.73           H  
ATOM    216  H  BHIS A  12      36.934  22.403  -3.883  0.51 12.73           H  
ATOM    217  HA AHIS A  12      39.033  23.764  -3.104  0.49 14.32           H  
ATOM    218  HA BHIS A  12      39.079  23.684  -3.051  0.51 14.59           H  
ATOM    219  HB2AHIS A  12      37.291  24.540  -4.576  0.49 17.05           H  
ATOM    220  HB2BHIS A  12      36.554  24.630  -3.796  0.51 18.16           H  
ATOM    221  HB3AHIS A  12      36.422  24.800  -3.273  0.49 17.05           H  
ATOM    222  HB3BHIS A  12      37.613  25.625  -3.155  0.51 18.16           H  
ATOM    223  HD1AHIS A  12      39.587  25.955  -4.612  0.49 23.31           H  
ATOM    224  HD2AHIS A  12      36.750  27.269  -2.288  0.49 23.68           H  
ATOM    225  HD2BHIS A  12      39.121  23.351  -5.598  0.51 26.31           H  
ATOM    226  HE1AHIS A  12      40.142  28.195  -4.093  0.49 23.07           H  
ATOM    227  HE1BHIS A  12      38.647  26.772  -7.528  0.51 28.15           H  
ATOM    228  HE2BHIS A  12      39.613  24.616  -7.608  0.51 27.95           H  
ATOM    229  N   VAL A  13      36.786  23.317  -0.845  1.00  9.67           N  
ANISOU  229  N   VAL A  13     1210   1141   1322   -298     85    -86       N  
ATOM    230  CA  VAL A  13      36.643  23.330   0.610  1.00  9.98           C  
ANISOU  230  CA  VAL A  13     1097   1092   1604   -170    187   -181       C  
ATOM    231  C   VAL A  13      37.522  22.259   1.250  1.00  8.88           C  
ANISOU  231  C   VAL A  13     1063   1072   1239   -128    148   -201       C  
ATOM    232  O   VAL A  13      38.080  22.484   2.332  1.00  8.89           O  
ANISOU  232  O   VAL A  13      973   1048   1358    -95    151   -297       O  
ATOM    233  CB  VAL A  13      35.174  23.285   1.085  1.00  9.72           C  
ANISOU  233  CB  VAL A  13     1110   1125   1460    -17     97   -138       C  
ATOM    234  CG1 VAL A  13      34.536  21.924   0.880  1.00 10.29           C  
ANISOU  234  CG1 VAL A  13     1209   1222   1478   -199    216   -474       C  
ATOM    235  CG2 VAL A  13      35.066  23.697   2.565  1.00  9.99           C  
ANISOU  235  CG2 VAL A  13     1186   1198   1413    -26     86   -157       C  
ATOM    236  H   VAL A  13      36.114  23.001  -1.279  1.00 11.60           H  
ATOM    237  HA  VAL A  13      36.993  24.180   0.919  1.00 11.98           H  
ATOM    238  HB  VAL A  13      34.664  23.927   0.566  1.00 11.67           H  
ATOM    239 HG11 VAL A  13      33.619  21.955   1.194  1.00 12.34           H  
ATOM    240 HG12 VAL A  13      34.555  21.706  -0.065  1.00 12.34           H  
ATOM    241 HG13 VAL A  13      35.037  21.262   1.382  1.00 12.34           H  
ATOM    242 HG21 VAL A  13      34.135  23.659   2.836  1.00 11.99           H  
ATOM    243 HG22 VAL A  13      35.592  23.084   3.102  1.00 11.99           H  
ATOM    244 HG23 VAL A  13      35.404  24.600   2.667  1.00 11.99           H  
ATOM    245  N   TRP A  14      37.697  21.100   0.601  1.00  8.82           N  
ANISOU  245  N   TRP A  14     1109    987   1256    -93     49   -125       N  
ATOM    246  CA  TRP A  14      38.545  20.059   1.182  1.00  9.24           C  
ANISOU  246  CA  TRP A  14     1216    884   1411   -153    211    -99       C  
ATOM    247  C   TRP A  14      39.983  20.536   1.333  1.00  9.14           C  
ANISOU  247  C   TRP A  14     1242    873   1355   -124    255    -16       C  
ATOM    248  O   TRP A  14      40.677  20.156   2.284  1.00  9.39           O  
ANISOU  248  O   TRP A  14     1273    854   1441    -83    161   -218       O  
ATOM    249  CB  TRP A  14      38.471  18.753   0.377  1.00 10.12           C  
ANISOU  249  CB  TRP A  14     1239   1065   1542   -170    247   -188       C  
ATOM    250  CG  TRP A  14      38.793  17.574   1.280  1.00 11.19           C  
ANISOU  250  CG  TRP A  14     1119    998   2132   -180   -204   -356       C  
ATOM    251  CD1 TRP A  14      39.968  16.868   1.372  1.00 13.61           C  
ANISOU  251  CD1 TRP A  14     1455   1182   2534    -52   -423   -678       C  
ATOM    252  CD2 TRP A  14      37.936  17.053   2.302  1.00 10.66           C  
ANISOU  252  CD2 TRP A  14     1424    878   1748   -127   -505     67       C  
ATOM    253  NE1 TRP A  14      39.862  15.934   2.381  1.00 14.71           N  
ANISOU  253  NE1 TRP A  14     1747   1175   2666    354   -822   -751       N  
ATOM    254  CE2 TRP A  14      38.629  16.031   2.968  1.00 13.15           C  
ANISOU  254  CE2 TRP A  14     1907   1003   2085     94   -710   -115       C  
ATOM    255  CE3 TRP A  14      36.635  17.356   2.709  1.00 10.94           C  
ANISOU  255  CE3 TRP A  14     1415   1050   1691   -346   -273    242       C  
ATOM    256  CZ2 TRP A  14      38.049  15.291   4.015  1.00 13.57           C  
ANISOU  256  CZ2 TRP A  14     2186    919   2051    142   -652     13       C  
ATOM    257  CZ3 TRP A  14      36.067  16.637   3.739  1.00 14.28           C  
ANISOU  257  CZ3 TRP A  14     1945   1319   2161   -472   -195    -25       C  
ATOM    258  CH2 TRP A  14      36.771  15.625   4.378  1.00 15.58           C  
ANISOU  258  CH2 TRP A  14     2325   1297   2298    -75   -300      7       C  
ATOM    259  H   TRP A  14      37.345  20.899  -0.157  1.00 10.59           H  
ATOM    260  HA  TRP A  14      38.214  19.864   2.072  1.00 11.09           H  
ATOM    261  HB2 TRP A  14      37.575  18.637   0.025  1.00 12.15           H  
ATOM    262  HB3 TRP A  14      39.120  18.777  -0.343  1.00 12.15           H  
ATOM    263  HD1 TRP A  14      40.722  17.008   0.846  1.00 16.33           H  
ATOM    264  HE1 TRP A  14      40.475  15.374   2.605  1.00 17.65           H  
ATOM    265  HE3 TRP A  14      36.160  18.039   2.294  1.00 13.12           H  
ATOM    266  HZ2 TRP A  14      38.512  14.605   4.439  1.00 16.28           H  
ATOM    267  HZ3 TRP A  14      35.202  16.837   4.015  1.00 17.13           H  
ATOM    268  HH2 TRP A  14      36.359  15.153   5.064  1.00 18.69           H  
ATOM    269  N   ALA A  15      40.441  21.390   0.420  1.00  9.13           N  
ANISOU  269  N   ALA A  15     1100   1000   1370   -140    130    -83       N  
ATOM    270  CA  ALA A  15      41.785  21.938   0.518  1.00 10.27           C  
ANISOU  270  CA  ALA A  15     1060   1208   1633   -245    262    -86       C  
ATOM    271  C   ALA A  15      41.982  22.703   1.817  1.00  9.75           C  
ANISOU  271  C   ALA A  15      999   1033   1675   -200    170   -218       C  
ATOM    272  O   ALA A  15      43.097  22.744   2.349  1.00 10.39           O  
ANISOU  272  O   ALA A  15      996   1119   1832    -63    150   -275       O  
ATOM    273  CB  ALA A  15      42.056  22.841  -0.684  1.00 11.81           C  
ANISOU  273  CB  ALA A  15     1322   1476   1689   -335    130     29       C  
ATOM    274  H   ALA A  15      39.993  21.664  -0.261  1.00 10.96           H  
ATOM    275  HA  ALA A  15      42.426  21.210   0.498  1.00 12.32           H  
ATOM    276  HB1 ALA A  15      42.953  23.202  -0.611  1.00 14.17           H  
ATOM    277  HB2 ALA A  15      41.974  22.317  -1.496  1.00 14.17           H  
ATOM    278  HB3 ALA A  15      41.407  23.562  -0.688  1.00 14.17           H  
ATOM    279  N   LYS A  16      40.917  23.336   2.328  1.00  9.98           N  
ANISOU  279  N   LYS A  16     1020   1046   1726    -29    104   -311       N  
ATOM    280  CA  LYS A  16      40.986  24.045   3.612  1.00 10.31           C  
ANISOU  280  CA  LYS A  16      942   1095   1878   -170    152   -461       C  
ATOM    281  C   LYS A  16      40.985  23.077   4.790  1.00 10.41           C  
ANISOU  281  C   LYS A  16     1004   1246   1704   -181    300   -487       C  
ATOM    282  O   LYS A  16      41.723  23.282   5.757  1.00 11.14           O  
ANISOU  282  O   LYS A  16     1060   1278   1894    -60    112   -627       O  
ATOM    283  CB  LYS A  16      39.855  25.070   3.749  1.00 12.08           C  
ANISOU  283  CB  LYS A  16     1070   1116   2405     37    145   -422       C  
ATOM    284  CG  LYS A  16      39.728  26.006   2.571  1.00 13.17           C  
ANISOU  284  CG  LYS A  16     1263   1271   2469     13    -42   -478       C  
ATOM    285  CD  LYS A  16      41.007  26.780   2.286  1.00 14.67           C  
ANISOU  285  CD  LYS A  16     1544   1197   2832   -153   -279   -128       C  
ATOM    286  CE  LYS A  16      40.896  27.576   1.006  1.00 18.14           C  
ANISOU  286  CE  LYS A  16     1779   1661   3451   -193   -121   -183       C  
ATOM    287  NZ  LYS A  16      42.207  28.041   0.527  1.00 21.50           N  
ANISOU  287  NZ  LYS A  16     2223   1718   4229   -597    152   -111       N  
ATOM    288  H   LYS A  16      40.146  23.370   1.950  1.00 11.98           H  
ATOM    289  HA  LYS A  16      41.823  24.535   3.643  1.00 12.37           H  
ATOM    290  HB2 LYS A  16      39.014  24.596   3.842  1.00 14.50           H  
ATOM    291  HB3 LYS A  16      40.016  25.609   4.539  1.00 14.50           H  
ATOM    292  HG2 LYS A  16      39.509  25.489   1.780  1.00 15.80           H  
ATOM    293  HG3 LYS A  16      39.024  26.648   2.753  1.00 15.80           H  
ATOM    294  HD2 LYS A  16      41.177  27.397   3.015  1.00 17.60           H  
ATOM    295  HD3 LYS A  16      41.745  26.157   2.194  1.00 17.60           H  
ATOM    296  HE2 LYS A  16      40.503  27.017   0.317  1.00 21.77           H  
ATOM    297  HE3 LYS A  16      40.338  28.354   1.163  1.00 21.77           H  
ATOM    298  HZ1 LYS A  16      42.109  28.505  -0.226  1.00 25.81           H  
ATOM    299  HZ2 LYS A  16      42.588  28.562   1.140  1.00 25.81           H  
ATOM    300  HZ3 LYS A  16      42.738  27.344   0.370  1.00 25.81           H  
ATOM    301  N   VAL A  17      40.165  22.023   4.727  1.00 10.51           N  
ANISOU  301  N   VAL A  17      993   1346   1655   -324    316   -489       N  
ATOM    302  CA  VAL A  17      40.204  20.958   5.728  1.00 10.93           C  
ANISOU  302  CA  VAL A  17     1237   1439   1477   -591    328   -361       C  
ATOM    303  C   VAL A  17      41.632  20.469   5.902  1.00 10.21           C  
ANISOU  303  C   VAL A  17     1306   1247   1329   -522    388   -132       C  
ATOM    304  O   VAL A  17      42.092  20.240   7.030  1.00 11.05           O  
ANISOU  304  O   VAL A  17     1436   1328   1433   -492    304   -194       O  
ATOM    305  CB  VAL A  17      39.260  19.808   5.317  1.00 12.49           C  
ANISOU  305  CB  VAL A  17     1409   1816   1520   -723    334   -435       C  
ATOM    306  CG1 VAL A  17      39.425  18.585   6.229  1.00 12.86           C  
ANISOU  306  CG1 VAL A  17     1530   1737   1620   -862    182   -289       C  
ATOM    307  CG2 VAL A  17      37.815  20.277   5.293  1.00 13.28           C  
ANISOU  307  CG2 VAL A  17     1361   2343   1341   -875    143   -349       C  
ATOM    308  H   VAL A  17      39.575  21.904   4.113  1.00 12.62           H  
ATOM    309  HA  VAL A  17      39.899  21.309   6.579  1.00 13.12           H  
ATOM    310  HB  VAL A  17      39.490  19.530   4.416  1.00 14.99           H  
ATOM    311 HG11 VAL A  17      38.816  17.889   5.936  1.00 15.43           H  
ATOM    312 HG12 VAL A  17      40.341  18.270   6.171  1.00 15.43           H  
ATOM    313 HG13 VAL A  17      39.220  18.843   7.141  1.00 15.43           H  
ATOM    314 HG21 VAL A  17      37.247  19.536   5.032  1.00 15.93           H  
ATOM    315 HG22 VAL A  17      37.570  20.587   6.179  1.00 15.93           H  
ATOM    316 HG23 VAL A  17      37.729  21.002   4.653  1.00 15.93           H  
ATOM    317  N   GLU A  18      42.343  20.292   4.785  1.00  9.46           N  
ANISOU  317  N   GLU A  18     1279    937   1376   -287    404    -49       N  
ATOM    318  CA  GLU A  18      43.697  19.752   4.776  1.00  9.88           C  
ANISOU  318  CA  GLU A  18     1296    932   1525    -91    329     29       C  
ATOM    319  C   GLU A  18      44.739  20.677   5.390  1.00  9.34           C  
ANISOU  319  C   GLU A  18     1292    966   1289    -32    251      2       C  
ATOM    320  O   GLU A  18      45.857  20.220   5.624  1.00 10.56           O  
ANISOU  320  O   GLU A  18     1356    936   1720    161    129    -66       O  
ATOM    321  CB  GLU A  18      44.083  19.343   3.355  1.00 10.26           C  
ANISOU  321  CB  GLU A  18     1289   1089   1522    -96    186   -235       C  
ATOM    322  CG  GLU A  18      43.345  18.093   2.915  1.00 10.88           C  
ANISOU  322  CG  GLU A  18     1338   1137   1661    -34    174   -288       C  
ATOM    323  CD  GLU A  18      43.714  17.640   1.525  1.00 11.09           C  
ANISOU  323  CD  GLU A  18     1279   1184   1752   -106     55    -90       C  
ATOM    324  OE1 GLU A  18      43.579  16.436   1.252  1.00 12.55           O  
ANISOU  324  OE1 GLU A  18     1642   1329   1796     -8     91   -368       O  
ATOM    325  OE2 GLU A  18      44.142  18.498   0.717  1.00 11.48           O  
ANISOU  325  OE2 GLU A  18     1236   1523   1601     -6     10   -103       O  
ATOM    326  H   GLU A  18      42.050  20.485   4.000  1.00 11.35           H  
ATOM    327  HA  GLU A  18      43.695  18.942   5.309  1.00 11.85           H  
ATOM    328  HB2 GLU A  18      43.857  20.061   2.742  1.00 12.32           H  
ATOM    329  HB3 GLU A  18      45.035  19.162   3.322  1.00 12.32           H  
ATOM    330  HG2 GLU A  18      43.555  17.372   3.529  1.00 13.06           H  
ATOM    331  HG3 GLU A  18      42.391  18.270   2.927  1.00 13.06           H  
ATOM    332  N   ALA A  19      44.419  21.934   5.686  1.00  9.43           N  
ANISOU  332  N   ALA A  19     1124    969   1489    -42    301     43       N  
ATOM    333  CA  ALA A  19      45.340  22.735   6.488  1.00  9.65           C  
ANISOU  333  CA  ALA A  19     1057    964   1645   -316    226    -98       C  
ATOM    334  C   ALA A  19      45.490  22.168   7.896  1.00 10.76           C  
ANISOU  334  C   ALA A  19     1473   1180   1437   -504    129   -131       C  
ATOM    335  O   ALA A  19      46.530  22.388   8.541  1.00 12.65           O  
ANISOU  335  O   ALA A  19     1689   1476   1643   -832    -19     23       O  
ATOM    336  CB  ALA A  19      44.886  24.191   6.539  1.00 11.72           C  
ANISOU  336  CB  ALA A  19     1051    946   2457   -321    238   -122       C  
ATOM    337  H   ALA A  19      43.698  22.337   5.444  1.00 11.31           H  
ATOM    338  HA  ALA A  19      46.214  22.714   6.068  1.00 11.58           H  
ATOM    339  HB1 ALA A  19      45.514  24.699   7.077  1.00 14.07           H  
ATOM    340  HB2 ALA A  19      44.861  24.545   5.636  1.00 14.07           H  
ATOM    341  HB3 ALA A  19      44.001  24.232   6.936  1.00 14.07           H  
ATOM    342  N   ASP A  20      44.476  21.453   8.392  1.00 10.35           N  
ANISOU  342  N   ASP A  20     1519   1048   1364   -547    180   -131       N  
ATOM    343  CA  ASP A  20      44.498  20.944   9.757  1.00 10.90           C  
ANISOU  343  CA  ASP A  20     1699   1122   1323   -688    266   -195       C  
ATOM    344  C   ASP A  20      43.559  19.757   9.848  1.00  8.97           C  
ANISOU  344  C   ASP A  20     1168    990   1250   -341    224   -103       C  
ATOM    345  O   ASP A  20      42.456  19.854  10.403  1.00  8.66           O  
ANISOU  345  O   ASP A  20     1273    722   1296   -108    312      1       O  
ATOM    346  CB  ASP A  20      44.091  22.028  10.753  1.00 13.81           C  
ANISOU  346  CB  ASP A  20     2482   1200   1565   -738    574   -255       C  
ATOM    347  CG  ASP A  20      44.011  21.526  12.196  1.00 15.78           C  
ANISOU  347  CG  ASP A  20     2826   1574   1595  -1065    642   -494       C  
ATOM    348  OD1 ASP A  20      43.373  22.221  13.009  1.00 19.29           O  
ANISOU  348  OD1 ASP A  20     3664   1776   1890   -659    812   -382       O  
ATOM    349  OD2 ASP A  20      44.583  20.466  12.526  1.00 16.39           O  
ANISOU  349  OD2 ASP A  20     2538   2151   1537  -1382    272   -210       O  
ATOM    350  H   ASP A  20      43.763  21.252   7.954  1.00 12.42           H  
ATOM    351  HA  ASP A  20      45.395  20.646   9.976  1.00 13.09           H  
ATOM    352  HB2 ASP A  20      44.744  22.745  10.722  1.00 16.57           H  
ATOM    353  HB3 ASP A  20      43.216  22.369  10.507  1.00 16.57           H  
ATOM    354  N   VAL A  21      43.960  18.623   9.294  1.00  7.79           N  
ANISOU  354  N   VAL A  21      722    928   1311   -147     85   -106       N  
ATOM    355  CA  VAL A  21      43.037  17.495   9.276  1.00  7.95           C  
ANISOU  355  CA  VAL A  21      881    899   1241    -55     34    -67       C  
ATOM    356  C   VAL A  21      42.710  17.028  10.690  1.00  7.62           C  
ANISOU  356  C   VAL A  21      922    736   1238     -3     41    -61       C  
ATOM    357  O   VAL A  21      41.563  16.670  10.986  1.00  8.06           O  
ANISOU  357  O   VAL A  21      924    896   1244   -211     83   -103       O  
ATOM    358  CB  VAL A  21      43.493  16.358   8.332  1.00 10.09           C  
ANISOU  358  CB  VAL A  21     1503    955   1375      1    330     56       C  
ATOM    359  CG1 VAL A  21      44.705  15.605   8.805  1.00 13.09           C  
ANISOU  359  CG1 VAL A  21     1518   1538   1916    170    235   -109       C  
ATOM    360  CG2 VAL A  21      42.331  15.351   8.154  1.00 13.14           C  
ANISOU  360  CG2 VAL A  21     2058    987   1947    -52    485   -293       C  
ATOM    361  H   VAL A  21      44.729  18.480   8.934  1.00  9.35           H  
ATOM    362  HA  VAL A  21      42.202  17.823   8.908  1.00  9.54           H  
ATOM    363  HB  VAL A  21      43.697  16.735   7.462  1.00 12.10           H  
ATOM    364 HG11 VAL A  21      44.920  14.915   8.157  1.00 15.70           H  
ATOM    365 HG12 VAL A  21      45.447  16.223   8.889  1.00 15.70           H  
ATOM    366 HG13 VAL A  21      44.510  15.202   9.665  1.00 15.70           H  
ATOM    367 HG21 VAL A  21      42.618  14.639   7.561  1.00 15.77           H  
ATOM    368 HG22 VAL A  21      42.095  14.985   9.021  1.00 15.77           H  
ATOM    369 HG23 VAL A  21      41.569  15.813   7.771  1.00 15.77           H  
ATOM    370  N   ALA A  22      43.704  17.013  11.581  1.00  7.85           N  
ANISOU  370  N   ALA A  22      840    932   1212     53     -5    -89       N  
ATOM    371  CA  ALA A  22      43.472  16.559  12.954  1.00  8.37           C  
ANISOU  371  CA  ALA A  22     1019    968   1191     83    -52    -18       C  
ATOM    372  C   ALA A  22      42.379  17.374  13.657  1.00  7.73           C  
ANISOU  372  C   ALA A  22      926    927   1084    -84     -2      2       C  
ATOM    373  O   ALA A  22      41.501  16.799  14.313  1.00  7.96           O  
ANISOU  373  O   ALA A  22      895    929   1201     29     96     58       O  
ATOM    374  CB  ALA A  22      44.776  16.589  13.756  1.00  9.88           C  
ANISOU  374  CB  ALA A  22     1096   1380   1277    169     31     28       C  
ATOM    375  H   ALA A  22      44.512  17.257  11.418  1.00  9.42           H  
ATOM    376  HA  ALA A  22      43.172  15.637  12.924  1.00 10.04           H  
ATOM    377  HB1 ALA A  22      44.597  16.285  14.660  1.00 11.85           H  
ATOM    378  HB2 ALA A  22      45.422  16.003  13.331  1.00 11.85           H  
ATOM    379  HB3 ALA A  22      45.115  17.498  13.773  1.00 11.85           H  
ATOM    380  N   GLY A  23      42.434  18.708  13.572  1.00  7.96           N  
ANISOU  380  N   GLY A  23      924    941   1161   -130     53   -113       N  
ATOM    381  CA  GLY A  23      41.440  19.524  14.248  1.00  8.18           C  
ANISOU  381  CA  GLY A  23      973    896   1240    -64    -15   -148       C  
ATOM    382  C   GLY A  23      40.053  19.370  13.660  1.00  7.59           C  
ANISOU  382  C   GLY A  23      990    660   1234    -35     77   -134       C  
ATOM    383  O   GLY A  23      39.054  19.373  14.395  1.00  8.06           O  
ANISOU  383  O   GLY A  23     1009    878   1175     19    106    -74       O  
ATOM    384  H   GLY A  23      43.027  19.151  13.135  1.00  9.56           H  
ATOM    385  HA2 GLY A  23      41.404  19.276  15.185  1.00  9.82           H  
ATOM    386  HA3 GLY A  23      41.696  20.457  14.187  1.00  9.82           H  
ATOM    387  N   HIS A  24      39.966  19.258  12.333  1.00  7.50           N  
ANISOU  387  N   HIS A  24      977    758   1115     -3     61    -49       N  
ATOM    388  CA  HIS A  24      38.675  19.001  11.709  1.00  7.74           C  
ANISOU  388  CA  HIS A  24      936    836   1171      6    -19     18       C  
ATOM    389  C   HIS A  24      38.118  17.641  12.134  1.00  7.52           C  
ANISOU  389  C   HIS A  24      868    971   1017    -19    -23     47       C  
ATOM    390  O   HIS A  24      36.911  17.512  12.365  1.00  8.60           O  
ANISOU  390  O   HIS A  24      831   1210   1227    -46      9    141       O  
ATOM    391  CB  HIS A  24      38.777  19.077  10.183  1.00  7.87           C  
ANISOU  391  CB  HIS A  24     1074    846   1069    -25     54     59       C  
ATOM    392  CG  HIS A  24      38.918  20.472   9.640  1.00  8.44           C  
ANISOU  392  CG  HIS A  24     1220    796   1192    108    126     71       C  
ATOM    393  ND1 HIS A  24      40.110  21.162   9.638  1.00  8.86           N  
ANISOU  393  ND1 HIS A  24     1427    662   1278     25    314    102       N  
ATOM    394  CD2 HIS A  24      38.004  21.307   9.087  1.00 10.17           C  
ANISOU  394  CD2 HIS A  24     1562    896   1405    265    262    239       C  
ATOM    395  CE1 HIS A  24      39.928  22.358   9.104  1.00 10.54           C  
ANISOU  395  CE1 HIS A  24     1801    783   1423    150    244     56       C  
ATOM    396  NE2 HIS A  24      38.658  22.474   8.764  1.00 11.41           N  
ANISOU  396  NE2 HIS A  24     1984    845   1504    489    179    183       N  
ATOM    397  H   HIS A  24      40.626  19.326  11.785  1.00  9.00           H  
ATOM    398  HA  HIS A  24      38.047  19.681  11.999  1.00  9.29           H  
ATOM    399  HB2 HIS A  24      39.554  18.570   9.898  1.00  9.44           H  
ATOM    400  HB3 HIS A  24      37.976  18.690   9.798  1.00  9.44           H  
ATOM    401  HD1 HIS A  24      40.859  20.860   9.936  1.00 10.63           H  
ATOM    402  HD2 HIS A  24      37.102  21.126   8.951  1.00 12.20           H  
ATOM    403  HE1 HIS A  24      40.583  23.009   8.992  1.00 12.65           H  
ATOM    404  N   GLY A  25      38.972  16.615  12.216  1.00  7.27           N  
ANISOU  404  N   GLY A  25      835    829   1098    -36     74     84       N  
ATOM    405  CA  GLY A  25      38.500  15.301  12.618  1.00  8.10           C  
ANISOU  405  CA  GLY A  25      976    926   1176    -80    -18     50       C  
ATOM    406  C   GLY A  25      37.970  15.287  14.037  1.00  8.00           C  
ANISOU  406  C   GLY A  25     1026    818   1194   -112    -27    125       C  
ATOM    407  O   GLY A  25      36.969  14.621  14.328  1.00  8.46           O  
ANISOU  407  O   GLY A  25     1114    830   1269    -88    -72     70       O  
ATOM    408  H   GLY A  25      39.814  16.658  12.045  1.00  8.73           H  
ATOM    409  HA2 GLY A  25      37.791  15.015  12.022  1.00  9.72           H  
ATOM    410  HA3 GLY A  25      39.229  14.663  12.557  1.00  9.72           H  
ATOM    411  N   GLN A  26      38.628  16.024  14.938  1.00  8.30           N  
ANISOU  411  N   GLN A  26     1073    959   1121    -26    -42     96       N  
ATOM    412  CA  GLN A  26      38.128  16.142  16.302  1.00  8.65           C  
ANISOU  412  CA  GLN A  26     1112   1016   1158    -22    -55    110       C  
ATOM    413  C   GLN A  26      36.753  16.793  16.312  1.00  8.70           C  
ANISOU  413  C   GLN A  26     1080    995   1230    -87     24    -12       C  
ATOM    414  O   GLN A  26      35.819  16.296  16.955  1.00  9.07           O  
ANISOU  414  O   GLN A  26     1146   1065   1234   -151    -12    104       O  
ATOM    415  CB  GLN A  26      39.096  16.957  17.159  1.00  9.02           C  
ANISOU  415  CB  GLN A  26     1150   1121   1157    -42    -59     68       C  
ATOM    416  CG  GLN A  26      40.404  16.261  17.482  1.00  9.78           C  
ANISOU  416  CG  GLN A  26     1297   1260   1158   -164   -119     73       C  
ATOM    417  CD  GLN A  26      41.345  17.196  18.203  1.00 12.37           C  
ANISOU  417  CD  GLN A  26     1619   1575   1506   -264   -132    285       C  
ATOM    418  OE1 GLN A  26      41.644  18.286  17.700  1.00 14.83           O  
ANISOU  418  OE1 GLN A  26     1902   1761   1972   -507   -560    419       O  
ATOM    419  NE2 GLN A  26      41.835  16.784  19.375  1.00 13.36           N  
ANISOU  419  NE2 GLN A  26     1771   1662   1641   -319   -300    121       N  
ATOM    420  H   GLN A  26      39.354  16.458  14.783  1.00  9.96           H  
ATOM    421  HA  GLN A  26      38.049  15.257  16.692  1.00 10.38           H  
ATOM    422  HB2 GLN A  26      39.310  17.777  16.688  1.00 10.83           H  
ATOM    423  HB3 GLN A  26      38.661  17.169  18.000  1.00 10.83           H  
ATOM    424  HG2 GLN A  26      40.230  15.499  18.057  1.00 11.73           H  
ATOM    425  HG3 GLN A  26      40.828  15.973  16.659  1.00 11.73           H  
ATOM    426 HE21 GLN A  26      41.611  16.015  19.688  1.00 16.03           H  
ATOM    427 HE22 GLN A  26      42.374  17.288  19.816  1.00 16.03           H  
ATOM    428  N   ASP A  27      36.610  17.924  15.611  1.00  8.15           N  
ANISOU  428  N   ASP A  27     1049    961   1088    -30     41     97       N  
ATOM    429  CA  ASP A  27      35.326  18.620  15.604  1.00  8.20           C  
ANISOU  429  CA  ASP A  27     1084    935   1098     33      6     63       C  
ATOM    430  C   ASP A  27      34.213  17.729  15.043  1.00  8.15           C  
ANISOU  430  C   ASP A  27      988    857   1250     43    -48     45       C  
ATOM    431  O   ASP A  27      33.083  17.731  15.559  1.00  8.51           O  
ANISOU  431  O   ASP A  27      956    952   1324      4    121     54       O  
ATOM    432  CB  ASP A  27      35.410  19.899  14.760  1.00  9.05           C  
ANISOU  432  CB  ASP A  27     1110    894   1437    -78    -41    140       C  
ATOM    433  CG  ASP A  27      36.181  21.022  15.419  1.00 11.15           C  
ANISOU  433  CG  ASP A  27     1509    966   1762    -96     26    112       C  
ATOM    434  OD1 ASP A  27      36.703  20.862  16.535  1.00 13.53           O  
ANISOU  434  OD1 ASP A  27     1850   1223   2067   -260   -242   -143       O  
ATOM    435  OD2 ASP A  27      36.306  22.082  14.759  1.00 12.93           O  
ANISOU  435  OD2 ASP A  27     1901    951   2063   -112    -92      9       O  
ATOM    436  H   ASP A  27      37.227  18.298  15.143  1.00  9.78           H  
ATOM    437  HA  ASP A  27      35.090  18.868  16.512  1.00  9.84           H  
ATOM    438  HB2 ASP A  27      35.851  19.691  13.921  1.00 10.87           H  
ATOM    439  HB3 ASP A  27      34.511  20.219  14.588  1.00 10.87           H  
ATOM    440  N   ILE A  28      34.505  17.002  13.957  1.00  7.88           N  
ANISOU  440  N   ILE A  28      898    904   1194    -57     26    -51       N  
ATOM    441  CA  ILE A  28      33.501  16.170  13.294  1.00  7.75           C  
ANISOU  441  CA  ILE A  28      908    840   1197    -64     57    155       C  
ATOM    442  C   ILE A  28      33.081  14.987  14.176  1.00  8.08           C  
ANISOU  442  C   ILE A  28      990    920   1162     73     78    -48       C  
ATOM    443  O   ILE A  28      31.882  14.706  14.338  1.00  8.14           O  
ANISOU  443  O   ILE A  28      839    974   1281      2    156     75       O  
ATOM    444  CB  ILE A  28      34.010  15.740  11.901  1.00  7.88           C  
ANISOU  444  CB  ILE A  28      886    913   1194     94     53     88       C  
ATOM    445  CG1 ILE A  28      34.002  16.962  10.980  1.00  7.84           C  
ANISOU  445  CG1 ILE A  28      748    986   1244    -16    -50     54       C  
ATOM    446  CG2 ILE A  28      33.203  14.565  11.315  1.00  8.39           C  
ANISOU  446  CG2 ILE A  28      995    989   1202     26    123      6       C  
ATOM    447  CD1 ILE A  28      34.780  16.829   9.724  1.00  9.11           C  
ANISOU  447  CD1 ILE A  28      880   1150   1431    -12     -2     97       C  
ATOM    448  H   ILE A  28      35.281  16.976  13.586  1.00  9.46           H  
ATOM    449  HA  ILE A  28      32.709  16.712  13.152  1.00  9.30           H  
ATOM    450  HB  ILE A  28      34.930  15.448  11.999  1.00  9.46           H  
ATOM    451 HG12 ILE A  28      33.084  17.152  10.733  1.00  9.40           H  
ATOM    452 HG13 ILE A  28      34.368  17.716  11.469  1.00  9.40           H  
ATOM    453 HG21 ILE A  28      33.564  14.338  10.444  1.00 10.06           H  
ATOM    454 HG22 ILE A  28      33.274  13.804  11.913  1.00 10.06           H  
ATOM    455 HG23 ILE A  28      32.274  14.833  11.229  1.00 10.06           H  
ATOM    456 HD11 ILE A  28      34.708  17.654   9.219  1.00 10.93           H  
ATOM    457 HD12 ILE A  28      35.709  16.656   9.945  1.00 10.93           H  
ATOM    458 HD13 ILE A  28      34.421  16.091   9.207  1.00 10.93           H  
ATOM    459  N   LEU A  29      34.046  14.274  14.771  1.00  8.18           N  
ANISOU  459  N   LEU A  29      956    875   1277     -7     98     81       N  
ATOM    460  CA  LEU A  29      33.688  13.153  15.632  1.00  8.09           C  
ANISOU  460  CA  LEU A  29     1078    822   1174    -86     36    115       C  
ATOM    461  C   LEU A  29      32.955  13.624  16.882  1.00  9.31           C  
ANISOU  461  C   LEU A  29     1209    968   1360    -74     69     94       C  
ATOM    462  O   LEU A  29      31.988  12.988  17.317  1.00 10.02           O  
ANISOU  462  O   LEU A  29     1295   1058   1454   -152    238    144       O  
ATOM    463  CB  LEU A  29      34.922  12.319  15.986  1.00  9.00           C  
ANISOU  463  CB  LEU A  29     1174    920   1324    -39    109    148       C  
ATOM    464  CG  LEU A  29      35.518  11.484  14.856  1.00 10.02           C  
ANISOU  464  CG  LEU A  29     1308   1029   1469     99    166    152       C  
ATOM    465  CD1 LEU A  29      36.742  10.739  15.354  1.00 11.00           C  
ANISOU  465  CD1 LEU A  29     1323   1185   1672    303     94     51       C  
ATOM    466  CD2 LEU A  29      34.506  10.492  14.273  1.00 12.13           C  
ANISOU  466  CD2 LEU A  29     1387   1212   2008     11      0   -294       C  
ATOM    467  H   LEU A  29      34.891  14.418  14.692  1.00  9.82           H  
ATOM    468  HA  LEU A  29      33.081  12.576  15.142  1.00  9.71           H  
ATOM    469  HB2 LEU A  29      35.617  12.921  16.297  1.00 10.79           H  
ATOM    470  HB3 LEU A  29      34.682  11.709  16.700  1.00 10.79           H  
ATOM    471  HG  LEU A  29      35.799  12.076  14.142  1.00 12.02           H  
ATOM    472 HD11 LEU A  29      37.109  10.213  14.627  1.00 13.20           H  
ATOM    473 HD12 LEU A  29      37.399  11.383  15.662  1.00 13.20           H  
ATOM    474 HD13 LEU A  29      36.481  10.157  16.085  1.00 13.20           H  
ATOM    475 HD21 LEU A  29      34.933   9.988  13.562  1.00 14.55           H  
ATOM    476 HD22 LEU A  29      34.214   9.891  14.975  1.00 14.55           H  
ATOM    477 HD23 LEU A  29      33.749  10.985  13.921  1.00 14.55           H  
ATOM    478  N   ILE A  30      33.384  14.736  17.474  1.00  9.14           N  
ANISOU  478  N   ILE A  30     1271   1081   1118   -185    190     74       N  
ATOM    479  CA  ILE A  30      32.699  15.235  18.663  1.00  9.83           C  
ANISOU  479  CA  ILE A  30     1401   1239   1095    -68     99     48       C  
ATOM    480  C   ILE A  30      31.269  15.622  18.331  1.00 10.13           C  
ANISOU  480  C   ILE A  30     1291   1222   1335    -46    188    -79       C  
ATOM    481  O   ILE A  30      30.340  15.332  19.093  1.00 10.57           O  
ANISOU  481  O   ILE A  30     1306   1359   1350   -108    319   -187       O  
ATOM    482  CB  ILE A  30      33.495  16.390  19.298  1.00 11.11           C  
ANISOU  482  CB  ILE A  30     1446   1680   1095   -252    138    -82       C  
ATOM    483  CG1 ILE A  30      34.770  15.823  19.924  1.00 12.65           C  
ANISOU  483  CG1 ILE A  30     1520   2051   1237   -417     64    335       C  
ATOM    484  CG2 ILE A  30      32.662  17.139  20.352  1.00 12.45           C  
ANISOU  484  CG2 ILE A  30     1520   1876   1336   -346    144   -407       C  
ATOM    485  CD1 ILE A  30      35.796  16.865  20.363  1.00 14.67           C  
ANISOU  485  CD1 ILE A  30     1695   2422   1459   -335    208    -31       C  
ATOM    486  H   ILE A  30      34.053  15.210  17.215  1.00 10.96           H  
ATOM    487  HA  ILE A  30      32.660  14.519  19.315  1.00 11.80           H  
ATOM    488  HB  ILE A  30      33.744  17.015  18.600  1.00 13.33           H  
ATOM    489 HG12 ILE A  30      34.526  15.306  20.707  1.00 15.18           H  
ATOM    490 HG13 ILE A  30      35.201  15.245  19.275  1.00 15.18           H  
ATOM    491 HG21 ILE A  30      33.198  17.856  20.727  1.00 14.95           H  
ATOM    492 HG22 ILE A  30      31.871  17.505  19.927  1.00 14.95           H  
ATOM    493 HG23 ILE A  30      32.405  16.518  21.051  1.00 14.95           H  
ATOM    494 HD11 ILE A  30      36.564  16.410  20.744  1.00 17.61           H  
ATOM    495 HD12 ILE A  30      36.069  17.384  19.590  1.00 17.61           H  
ATOM    496 HD13 ILE A  30      35.392  17.445  21.026  1.00 17.61           H  
ATOM    497  N   ARG A  31      31.059  16.276  17.187  1.00  9.69           N  
ANISOU  497  N   ARG A  31     1114   1220   1348    -33    188    -79       N  
ATOM    498  CA  ARG A  31      29.702  16.609  16.764  1.00 10.38           C  
ANISOU  498  CA  ARG A  31     1133   1268   1545    -50    269   -204       C  
ATOM    499  C   ARG A  31      28.863  15.346  16.583  1.00 10.44           C  
ANISOU  499  C   ARG A  31     1135   1464   1366     54    202   -230       C  
ATOM    500  O   ARG A  31      27.705  15.288  17.019  1.00 11.83           O  
ANISOU  500  O   ARG A  31     1190   1651   1653     -7    306   -260       O  
ATOM    501  CB  ARG A  31      29.752  17.440  15.479  1.00 11.76           C  
ANISOU  501  CB  ARG A  31     1337   1435   1697     65     85   -125       C  
ATOM    502  CG  ARG A  31      28.404  17.737  14.866  1.00 14.87           C  
ANISOU  502  CG  ARG A  31     1602   2001   2047    343    204   -404       C  
ATOM    503  CD  ARG A  31      27.663  18.770  15.620  1.00 19.38           C  
ANISOU  503  CD  ARG A  31     1846   2575   2943    432     26     59       C  
ATOM    504  NE  ARG A  31      26.352  18.919  15.008  1.00 23.45           N  
ANISOU  504  NE  ARG A  31     1984   3025   3901    563     54    540       N  
ATOM    505  CZ  ARG A  31      25.457  19.824  15.367  1.00 28.15           C  
ANISOU  505  CZ  ARG A  31     2309   3597   4788   1072   -145    723       C  
ATOM    506  NH1 ARG A  31      25.738  20.669  16.346  1.00 30.46           N  
ANISOU  506  NH1 ARG A  31     2524   3961   5089   1270   -160    703       N  
ATOM    507  NH2 ARG A  31      24.286  19.879  14.744  1.00 30.21           N  
ANISOU  507  NH2 ARG A  31     2370   3778   5330   1119   -106    893       N  
ATOM    508  H   ARG A  31      31.676  16.533  16.647  1.00 11.63           H  
ATOM    509  HA  ARG A  31      29.283  17.149  17.452  1.00 12.46           H  
ATOM    510  HB2 ARG A  31      30.178  18.289  15.676  1.00 14.12           H  
ATOM    511  HB3 ARG A  31      30.274  16.959  14.819  1.00 14.12           H  
ATOM    512  HG2 ARG A  31      28.530  18.058  13.960  1.00 17.85           H  
ATOM    513  HG3 ARG A  31      27.871  16.927  14.862  1.00 17.85           H  
ATOM    514  HD2 ARG A  31      27.550  18.490  16.542  1.00 23.26           H  
ATOM    515  HD3 ARG A  31      28.133  19.617  15.569  1.00 23.26           H  
ATOM    516  HE  ARG A  31      26.144  18.383  14.368  1.00 28.14           H  
ATOM    517 HH11 ARG A  31      26.498  20.628  16.745  1.00 36.55           H  
ATOM    518 HH12 ARG A  31      25.159  21.260  16.583  1.00 36.55           H  
ATOM    519 HH21 ARG A  31      24.110  19.327  14.109  1.00 36.25           H  
ATOM    520 HH22 ARG A  31      23.703  20.467  14.977  1.00 36.25           H  
ATOM    521  N   LEU A  32      29.424  14.332  15.916  1.00  9.94           N  
ANISOU  521  N   LEU A  32     1032   1342   1401    -83    230   -198       N  
ATOM    522  CA  LEU A  32      28.747  13.048  15.743  1.00 10.25           C  
ANISOU  522  CA  LEU A  32     1145   1325   1424   -286    299   -220       C  
ATOM    523  C   LEU A  32      28.328  12.449  17.087  1.00 10.93           C  
ANISOU  523  C   LEU A  32     1290   1429   1434   -360    364   -256       C  
ATOM    524  O   LEU A  32      27.181  12.013  17.260  1.00 12.19           O  
ANISOU  524  O   LEU A  32     1286   1628   1718   -395    495   -339       O  
ATOM    525  CB  LEU A  32      29.686  12.099  14.991  1.00 10.20           C  
ANISOU  525  CB  LEU A  32     1253   1308   1316   -128    272   -210       C  
ATOM    526  CG  LEU A  32      29.154  10.678  14.803  1.00 10.07           C  
ANISOU  526  CG  LEU A  32     1343   1195   1289   -211    240   -120       C  
ATOM    527  CD1 LEU A  32      27.927  10.638  13.912  1.00 11.57           C  
ANISOU  527  CD1 LEU A  32     1487   1239   1669   -194    164   -112       C  
ATOM    528  CD2 LEU A  32      30.248   9.798  14.241  1.00 11.05           C  
ANISOU  528  CD2 LEU A  32     1424   1193   1583    -74    222   -110       C  
ATOM    529  H   LEU A  32      30.202  14.366  15.551  1.00 11.92           H  
ATOM    530  HA  LEU A  32      27.950  13.176  15.206  1.00 12.30           H  
ATOM    531  HB2 LEU A  32      29.855  12.467  14.110  1.00 12.24           H  
ATOM    532  HB3 LEU A  32      30.520  12.036  15.483  1.00 12.24           H  
ATOM    533  HG  LEU A  32      28.903  10.321  15.670  1.00 12.09           H  
ATOM    534 HD11 LEU A  32      27.630   9.719  13.826  1.00 13.88           H  
ATOM    535 HD12 LEU A  32      27.227  11.175  14.316  1.00 13.88           H  
ATOM    536 HD13 LEU A  32      28.158  10.995  13.041  1.00 13.88           H  
ATOM    537 HD21 LEU A  32      29.901   8.900  14.125  1.00 13.27           H  
ATOM    538 HD22 LEU A  32      30.532  10.157  13.386  1.00 13.27           H  
ATOM    539 HD23 LEU A  32      30.994   9.789  14.860  1.00 13.27           H  
ATOM    540  N   PHE A  33      29.260  12.383  18.039  1.00 10.93           N  
ANISOU  540  N   PHE A  33     1459   1378   1317   -373    334   -147       N  
ATOM    541  CA  PHE A  33      29.007  11.732  19.324  1.00 12.37           C  
ANISOU  541  CA  PHE A  33     1885   1482   1334   -398    559   -183       C  
ATOM    542  C   PHE A  33      28.037  12.523  20.187  1.00 14.70           C  
ANISOU  542  C   PHE A  33     2048   1820   1716   -628    844   -362       C  
ATOM    543  O   PHE A  33      27.282  11.927  20.962  1.00 16.51           O  
ANISOU  543  O   PHE A  33     2384   2054   1835   -659    921   -209       O  
ATOM    544  CB  PHE A  33      30.325  11.502  20.072  1.00 12.61           C  
ANISOU  544  CB  PHE A  33     2017   1391   1383   -336    287     11       C  
ATOM    545  CG  PHE A  33      31.292  10.586  19.357  1.00 11.99           C  
ANISOU  545  CG  PHE A  33     1991   1276   1289   -393    162     77       C  
ATOM    546  CD1 PHE A  33      30.841   9.566  18.522  1.00 12.22           C  
ANISOU  546  CD1 PHE A  33     2015   1326   1303   -349    163      7       C  
ATOM    547  CD2 PHE A  33      32.661  10.759  19.507  1.00 12.65           C  
ANISOU  547  CD2 PHE A  33     1987   1322   1498   -382     41    301       C  
ATOM    548  CE1 PHE A  33      31.748   8.742  17.867  1.00 12.92           C  
ANISOU  548  CE1 PHE A  33     2108   1355   1447   -353     69     28       C  
ATOM    549  CE2 PHE A  33      33.561   9.942  18.861  1.00 13.58           C  
ANISOU  549  CE2 PHE A  33     2068   1417   1674   -442    134    203       C  
ATOM    550  CZ  PHE A  33      33.106   8.925  18.047  1.00 13.69           C  
ANISOU  550  CZ  PHE A  33     2151   1442   1608   -359    149    116       C  
ATOM    551  H   PHE A  33      30.052  12.709  17.963  1.00 13.12           H  
ATOM    552  HA  PHE A  33      28.608  10.863  19.157  1.00 14.85           H  
ATOM    553  HB2 PHE A  33      30.765  12.357  20.196  1.00 15.13           H  
ATOM    554  HB3 PHE A  33      30.127  11.107  20.935  1.00 15.13           H  
ATOM    555  HD1 PHE A  33      29.928   9.434  18.404  1.00 14.67           H  
ATOM    556  HD2 PHE A  33      32.977  11.437  20.059  1.00 15.18           H  
ATOM    557  HE1 PHE A  33      31.441   8.058  17.317  1.00 15.51           H  
ATOM    558  HE2 PHE A  33      34.474  10.070  18.980  1.00 16.29           H  
ATOM    559  HZ  PHE A  33      33.712   8.375  17.606  1.00 16.43           H  
ATOM    560  N   LYS A  34      28.030  13.847  20.070  1.00 15.43           N  
ANISOU  560  N   LYS A  34     2123   1907   1831   -570    869   -701       N  
ATOM    561  CA  LYS A  34      27.096  14.661  20.840  1.00 17.71           C  
ANISOU  561  CA  LYS A  34     2300   2035   2393   -402   1084   -741       C  
ATOM    562  C   LYS A  34      25.698  14.632  20.232  1.00 17.55           C  
ANISOU  562  C   LYS A  34     2088   1993   2586   -493   1283   -689       C  
ATOM    563  O   LYS A  34      24.704  14.569  20.965  1.00 19.24           O  
ANISOU  563  O   LYS A  34     2165   2239   2905   -513   1396   -735       O  
ATOM    564  CB  LYS A  34      27.618  16.097  20.944  1.00 20.89           C  
ANISOU  564  CB  LYS A  34     2574   2220   3143   -220   1122  -1118       C  
ATOM    565  CG  LYS A  34      28.785  16.262  21.922  1.00 25.19           C  
ANISOU  565  CG  LYS A  34     3018   2395   4157    -85    788  -1117       C  
ATOM    566  CD  LYS A  34      29.520  17.611  21.791  1.00 31.29           C  
ANISOU  566  CD  LYS A  34     3531   2900   5457    421    353  -1210       C  
ATOM    567  CE  LYS A  34      28.618  18.837  21.910  1.00 35.23           C  
ANISOU  567  CE  LYS A  34     3878   3187   6320    653    -41  -1299       C  
ATOM    568  NZ  LYS A  34      29.405  20.096  21.689  1.00 37.50           N  
ANISOU  568  NZ  LYS A  34     4095   3419   6732    860   -334  -1392       N  
ATOM    569  H   LYS A  34      28.552  14.296  19.555  1.00 18.51           H  
ATOM    570  HA  LYS A  34      27.035  14.301  21.739  1.00 21.25           H  
ATOM    571  HB2 LYS A  34      27.922  16.383  20.069  1.00 25.07           H  
ATOM    572  HB3 LYS A  34      26.896  16.671  21.245  1.00 25.07           H  
ATOM    573  HG2 LYS A  34      28.446  16.196  22.828  1.00 30.23           H  
ATOM    574  HG3 LYS A  34      29.431  15.556  21.760  1.00 30.23           H  
ATOM    575  HD2 LYS A  34      30.189  17.669  22.491  1.00 37.55           H  
ATOM    576  HD3 LYS A  34      29.951  17.646  20.923  1.00 37.55           H  
ATOM    577  HE2 LYS A  34      27.919  18.790  21.238  1.00 42.28           H  
ATOM    578  HE3 LYS A  34      28.231  18.868  22.799  1.00 42.28           H  
ATOM    579  HZ1 LYS A  34      28.871  20.804  21.760  1.00 45.00           H  
ATOM    580  HZ2 LYS A  34      30.053  20.159  22.296  1.00 45.00           H  
ATOM    581  HZ3 LYS A  34      29.769  20.088  20.877  1.00 45.00           H  
ATOM    582  N   SER A  35      25.596  14.680  18.903  1.00 16.35           N  
ANISOU  582  N   SER A  35     1903   1778   2532   -539   1124   -787       N  
ATOM    583  CA  SER A  35      24.294  14.665  18.245  1.00 16.47           C  
ANISOU  583  CA  SER A  35     1804   1689   2763   -406    958   -711       C  
ATOM    584  C   SER A  35      23.665  13.276  18.230  1.00 15.59           C  
ANISOU  584  C   SER A  35     1668   1641   2614   -332   1050   -568       C  
ATOM    585  O   SER A  35      22.434  13.163  18.214  1.00 17.57           O  
ANISOU  585  O   SER A  35     1617   1901   3158   -237   1127   -551       O  
ATOM    586  CB  SER A  35      24.419  15.177  16.808  1.00 18.47           C  
ANISOU  586  CB  SER A  35     1993   1739   3286   -421    841   -479       C  
ATOM    587  OG  SER A  35      24.808  16.536  16.765  1.00 21.24           O  
ANISOU  587  OG  SER A  35     2415   1986   3668   -355    659   -253       O  
ATOM    588  H   SER A  35      26.265  14.721  18.364  1.00 19.62           H  
ATOM    589  HA  SER A  35      23.694  15.259  18.723  1.00 19.76           H  
ATOM    590  HB2 SER A  35      25.086  14.647  16.344  1.00 22.16           H  
ATOM    591  HB3 SER A  35      23.561  15.084  16.367  1.00 22.16           H  
ATOM    592  HG  SER A  35      25.553  16.633  17.141  1.00 25.48           H  
ATOM    593  N   HIS A  36      24.481  12.214  18.220  1.00 14.45           N  
ANISOU  593  N   HIS A  36     1619   1572   2298   -354    909   -576       N  
ATOM    594  CA  HIS A  36      24.003  10.833  18.099  1.00 14.57           C  
ANISOU  594  CA  HIS A  36     1761   1605   2169   -354    824   -534       C  
ATOM    595  C   HIS A  36      24.838   9.953  19.017  1.00 14.33           C  
ANISOU  595  C   HIS A  36     1777   1623   2044   -455    806   -422       C  
ATOM    596  O   HIS A  36      25.723   9.215  18.567  1.00 13.47           O  
ANISOU  596  O   HIS A  36     1711   1477   1932   -327    694   -245       O  
ATOM    597  CB  HIS A  36      24.098  10.368  16.645  1.00 14.68           C  
ANISOU  597  CB  HIS A  36     1730   1569   2277   -480    809   -365       C  
ATOM    598  CG  HIS A  36      23.403  11.284  15.691  1.00 15.03           C  
ANISOU  598  CG  HIS A  36     1840   1699   2173   -494    822   -257       C  
ATOM    599  ND1 HIS A  36      22.040  11.254  15.492  1.00 16.87           N  
ANISOU  599  ND1 HIS A  36     2026   1824   2561   -321    565   -278       N  
ATOM    600  CD2 HIS A  36      23.879  12.278  14.903  1.00 16.32           C  
ANISOU  600  CD2 HIS A  36     2093   1746   2362   -396    668   -404       C  
ATOM    601  CE1 HIS A  36      21.707  12.185  14.613  1.00 18.01           C  
ANISOU  601  CE1 HIS A  36     2160   2035   2649   -227    454   -187       C  
ATOM    602  NE2 HIS A  36      22.803  12.825  14.247  1.00 17.61           N  
ANISOU  602  NE2 HIS A  36     2274   1945   2472   -210    498   -223       N  
ATOM    603  H   HIS A  36      25.336  12.272  18.285  1.00 17.34           H  
ATOM    604  HA  HIS A  36      23.076  10.783  18.380  1.00 17.48           H  
ATOM    605  HB2 HIS A  36      25.033  10.323  16.389  1.00 17.61           H  
ATOM    606  HB3 HIS A  36      23.691   9.491  16.567  1.00 17.61           H  
ATOM    607  HD2 HIS A  36      24.767  12.544  14.827  1.00 19.58           H  
ATOM    608  HE1 HIS A  36      20.847  12.362  14.308  1.00 21.61           H  
ATOM    609  HE2 HIS A  36      22.840  13.469  13.677  1.00 21.13           H  
ATOM    610  N   PRO A  37      24.596  10.025  20.330  1.00 16.12           N  
ANISOU  610  N   PRO A  37     1990   2080   2057   -391    818   -471       N  
ATOM    611  CA  PRO A  37      25.488   9.331  21.276  1.00 16.54           C  
ANISOU  611  CA  PRO A  37     2070   2190   2026   -471    845   -457       C  
ATOM    612  C   PRO A  37      25.599   7.835  21.055  1.00 15.97           C  
ANISOU  612  C   PRO A  37     2082   2095   1893   -564    837    -59       C  
ATOM    613  O   PRO A  37      26.626   7.247  21.417  1.00 17.12           O  
ANISOU  613  O   PRO A  37     2237   2334   1935   -329    534   -103       O  
ATOM    614  CB  PRO A  37      24.885   9.678  22.645  1.00 18.98           C  
ANISOU  614  CB  PRO A  37     2382   2460   2370   -199    760   -577       C  
ATOM    615  CG  PRO A  37      24.174  10.955  22.416  1.00 19.53           C  
ANISOU  615  CG  PRO A  37     2427   2664   2331      7    771   -483       C  
ATOM    616  CD  PRO A  37      23.623  10.886  21.027  1.00 17.11           C  
ANISOU  616  CD  PRO A  37     2212   2367   1922   -158    906   -421       C  
ATOM    617  HA  PRO A  37      26.377   9.715  21.224  1.00 19.85           H  
ATOM    618  HB2 PRO A  37      24.267   8.983  22.919  1.00 22.78           H  
ATOM    619  HB3 PRO A  37      25.593   9.790  23.298  1.00 22.78           H  
ATOM    620  HG2 PRO A  37      23.456  11.045  23.061  1.00 23.44           H  
ATOM    621  HG3 PRO A  37      24.798  11.692  22.497  1.00 23.44           H  
ATOM    622  HD2 PRO A  37      22.745  10.473  21.030  1.00 20.53           H  
ATOM    623  HD3 PRO A  37      23.602  11.769  20.626  1.00 20.53           H  
ATOM    624  N   GLU A  38      24.582   7.198  20.467  1.00 15.93           N  
ANISOU  624  N   GLU A  38     2077   1874   2100   -707    882    131       N  
ATOM    625  CA  GLU A  38      24.663   5.767  20.206  1.00 17.35           C  
ANISOU  625  CA  GLU A  38     2164   1923   2503   -588    681    136       C  
ATOM    626  C   GLU A  38      25.856   5.412  19.317  1.00 16.08           C  
ANISOU  626  C   GLU A  38     2197   1654   2260   -453    472     88       C  
ATOM    627  O   GLU A  38      26.372   4.291  19.395  1.00 17.19           O  
ANISOU  627  O   GLU A  38     2296   1553   2684   -561    520    151       O  
ATOM    628  CB  GLU A  38      23.338   5.258  19.616  1.00 18.50           C  
ANISOU  628  CB  GLU A  38     2225   2006   2799   -657    771    -42       C  
ATOM    629  CG  GLU A  38      22.988   5.790  18.224  1.00 19.65           C  
ANISOU  629  CG  GLU A  38     2247   2340   2880   -613    748   -234       C  
ATOM    630  CD  GLU A  38      22.208   7.101  18.222  1.00 21.28           C  
ANISOU  630  CD  GLU A  38     2333   2567   3185   -624    705   -105       C  
ATOM    631  OE1 GLU A  38      21.443   7.303  17.255  1.00 22.52           O  
ANISOU  631  OE1 GLU A  38     2450   2744   3361   -486    895    193       O  
ATOM    632  OE2 GLU A  38      22.359   7.931  19.153  1.00 21.55           O  
ANISOU  632  OE2 GLU A  38     2427   2492   3269   -722    679   -149       O  
ATOM    633  H   GLU A  38      23.847   7.568  20.215  1.00 19.11           H  
ATOM    634  HA  GLU A  38      24.793   5.312  21.053  1.00 20.81           H  
ATOM    635  HB2 GLU A  38      23.381   4.291  19.555  1.00 22.20           H  
ATOM    636  HB3 GLU A  38      22.618   5.513  20.214  1.00 22.20           H  
ATOM    637  HG2 GLU A  38      23.811   5.938  17.733  1.00 23.58           H  
ATOM    638  HG3 GLU A  38      22.449   5.127  17.766  1.00 23.58           H  
ATOM    639  N   THR A  39      26.318   6.346  18.479  1.00 14.09           N  
ANISOU  639  N   THR A  39     1986   1379   1988   -445    467     63       N  
ATOM    640  CA  THR A  39      27.423   6.040  17.567  1.00 12.78           C  
ANISOU  640  CA  THR A  39     2008   1162   1687   -244    377   -229       C  
ATOM    641  C   THR A  39      28.738   5.830  18.310  1.00 12.87           C  
ANISOU  641  C   THR A  39     2085   1148   1659   -270    331   -146       C  
ATOM    642  O   THR A  39      29.614   5.098  17.836  1.00 13.64           O  
ANISOU  642  O   THR A  39     2247   1195   1738   -192    348   -109       O  
ATOM    643  CB  THR A  39      27.604   7.143  16.511  1.00 12.35           C  
ANISOU  643  CB  THR A  39     1864   1236   1594   -279    454   -165       C  
ATOM    644  OG1 THR A  39      27.979   8.394  17.120  1.00 12.00           O  
ANISOU  644  OG1 THR A  39     1663   1143   1752   -315    581   -258       O  
ATOM    645  CG2 THR A  39      26.355   7.298  15.662  1.00 13.57           C  
ANISOU  645  CG2 THR A  39     1882   1311   1962   -263    325   -261       C  
ATOM    646  H   THR A  39      26.016   7.149  18.420  1.00 16.90           H  
ATOM    647  HA  THR A  39      27.217   5.216  17.098  1.00 15.34           H  
ATOM    648  HB  THR A  39      28.320   6.873  15.915  1.00 14.83           H  
ATOM    649  HG1 THR A  39      27.384   8.640  17.660  1.00 14.39           H  
ATOM    650 HG21 THR A  39      26.488   7.998  15.003  1.00 16.28           H  
ATOM    651 HG22 THR A  39      26.161   6.466  15.203  1.00 16.28           H  
ATOM    652 HG23 THR A  39      25.600   7.534  16.223  1.00 16.28           H  
ATOM    653  N   LEU A  40      28.888   6.447  19.478  1.00 13.43           N  
ANISOU  653  N   LEU A  40     2146   1309   1648   -294    161   -301       N  
ATOM    654  CA  LEU A  40      30.120   6.306  20.244  1.00 13.59           C  
ANISOU  654  CA  LEU A  40     2374   1415   1373   -167    272   -234       C  
ATOM    655  C   LEU A  40      30.320   4.858  20.691  1.00 14.07           C  
ANISOU  655  C   LEU A  40     2556   1462   1327   -286    503   -145       C  
ATOM    656  O   LEU A  40      31.460   4.397  20.839  1.00 15.58           O  
ANISOU  656  O   LEU A  40     2693   1530   1697     16    491   -284       O  
ATOM    657  CB  LEU A  40      30.063   7.258  21.447  1.00 14.33           C  
ANISOU  657  CB  LEU A  40     2426   1578   1440    -63    174    105       C  
ATOM    658  CG  LEU A  40      31.245   7.244  22.411  1.00 14.40           C  
ANISOU  658  CG  LEU A  40     2501   1675   1297   -116     70      5       C  
ATOM    659  CD1 LEU A  40      32.527   7.597  21.684  1.00 15.33           C  
ANISOU  659  CD1 LEU A  40     2584   1594   1649   -285     -4    345       C  
ATOM    660  CD2 LEU A  40      31.004   8.193  23.575  1.00 15.85           C  
ANISOU  660  CD2 LEU A  40     2605   1906   1512     33   -129   -117       C  
ATOM    661  H   LEU A  40      28.296   6.950  19.846  1.00 16.12           H  
ATOM    662  HA  LEU A  40      30.874   6.560  19.690  1.00 16.30           H  
ATOM    663  HB2 LEU A  40      29.983   8.164  21.109  1.00 17.19           H  
ATOM    664  HB3 LEU A  40      29.271   7.041  21.964  1.00 17.19           H  
ATOM    665  HG  LEU A  40      31.344   6.349  22.773  1.00 17.28           H  
ATOM    666 HD11 LEU A  40      33.263   7.581  22.317  1.00 18.40           H  
ATOM    667 HD12 LEU A  40      32.681   6.946  20.982  1.00 18.40           H  
ATOM    668 HD13 LEU A  40      32.439   8.483  21.301  1.00 18.40           H  
ATOM    669 HD21 LEU A  40      31.770   8.163  24.169  1.00 19.02           H  
ATOM    670 HD22 LEU A  40      30.888   9.092  23.229  1.00 19.02           H  
ATOM    671 HD23 LEU A  40      30.205   7.915  24.049  1.00 19.02           H  
ATOM    672  N   GLU A  41      29.224   4.113  20.873  1.00 15.20           N  
ANISOU  672  N   GLU A  41     2828   1505   1443   -294    648     11       N  
ATOM    673  CA  GLU A  41      29.303   2.727  21.323  1.00 16.93           C  
ANISOU  673  CA  GLU A  41     3111   1661   1661   -442    675    187       C  
ATOM    674  C   GLU A  41      30.023   1.822  20.330  1.00 17.34           C  
ANISOU  674  C   GLU A  41     3301   1591   1695   -188    427     86       C  
ATOM    675  O   GLU A  41      30.467   0.733  20.712  1.00 18.52           O  
ANISOU  675  O   GLU A  41     3651   1617   1770    -21    508    359       O  
ATOM    676  CB  GLU A  41      27.898   2.160  21.530  1.00 19.65           C  
ANISOU  676  CB  GLU A  41     3405   2073   1988   -427   1035    261       C  
ATOM    677  CG  GLU A  41      27.046   2.904  22.540  1.00 24.53           C  
ANISOU  677  CG  GLU A  41     3746   2732   2844   -338   1166    344       C  
ATOM    678  CD  GLU A  41      25.634   2.355  22.614  1.00 31.76           C  
ANISOU  678  CD  GLU A  41     4184   3428   4455     13   1138     42       C  
ATOM    679  OE1 GLU A  41      24.770   3.015  23.225  1.00 34.34           O  
ANISOU  679  OE1 GLU A  41     4295   3636   5115     64   1153     28       O  
ATOM    680  OE2 GLU A  41      25.388   1.262  22.059  1.00 35.10           O  
ANISOU  680  OE2 GLU A  41     4388   3756   5193     87   1106    -13       O  
ATOM    681  H   GLU A  41      28.421   4.392  20.742  1.00 18.24           H  
ATOM    682  HA  GLU A  41      29.776   2.690  22.169  1.00 20.32           H  
ATOM    683  HB2 GLU A  41      27.429   2.181  20.681  1.00 23.58           H  
ATOM    684  HB3 GLU A  41      27.978   1.243  21.835  1.00 23.58           H  
ATOM    685  HG2 GLU A  41      27.448   2.820  23.419  1.00 29.44           H  
ATOM    686  HG3 GLU A  41      26.993   3.838  22.285  1.00 29.44           H  
ATOM    687  N   LYS A  42      30.117   2.219  19.062  1.00 15.90           N  
ANISOU  687  N   LYS A  42     3150   1368   1523   -291    676     32       N  
ATOM    688  CA  LYS A  42      30.816   1.414  18.066  1.00 15.90           C  
ANISOU  688  CA  LYS A  42     3171   1291   1579   -248    695    -42       C  
ATOM    689  C   LYS A  42      32.336   1.495  18.182  1.00 15.80           C  
ANISOU  689  C   LYS A  42     3126   1233   1646    -72    750    -84       C  
ATOM    690  O   LYS A  42      33.029   0.663  17.576  1.00 16.19           O  
ANISOU  690  O   LYS A  42     3108   1258   1787    -69    580    -62       O  
ATOM    691  CB  LYS A  42      30.397   1.837  16.654  1.00 15.96           C  
ANISOU  691  CB  LYS A  42     3223   1271   1570   -376    651     -1       C  
ATOM    692  CG  LYS A  42      28.953   1.521  16.295  1.00 17.25           C  
ANISOU  692  CG  LYS A  42     3311   1385   1858   -308    580   -265       C  
ATOM    693  CD  LYS A  42      28.731   0.034  16.091  1.00 18.23           C  
ANISOU  693  CD  LYS A  42     3295   1454   2176   -521    586   -256       C  
ATOM    694  CE  LYS A  42      27.271  -0.272  15.811  1.00 19.14           C  
ANISOU  694  CE  LYS A  42     3294   1782   2197   -657    654   -442       C  
ATOM    695  NZ  LYS A  42      27.055  -1.716  15.529  1.00 20.08           N  
ANISOU  695  NZ  LYS A  42     3325   1868   2435   -786    637   -143       N  
ATOM    696  H   LYS A  42      29.785   2.950  18.755  1.00 19.08           H  
ATOM    697  HA  LYS A  42      30.561   0.485  18.184  1.00 19.08           H  
ATOM    698  HB2 LYS A  42      30.517   2.795  16.570  1.00 19.15           H  
ATOM    699  HB3 LYS A  42      30.965   1.380  16.013  1.00 19.15           H  
ATOM    700  HG2 LYS A  42      28.374   1.818  17.014  1.00 20.70           H  
ATOM    701  HG3 LYS A  42      28.723   1.977  15.470  1.00 20.70           H  
ATOM    702  HD2 LYS A  42      29.257  -0.268  15.335  1.00 21.87           H  
ATOM    703  HD3 LYS A  42      28.993  -0.442  16.895  1.00 21.87           H  
ATOM    704  HE2 LYS A  42      26.739  -0.032  16.586  1.00 22.97           H  
ATOM    705  HE3 LYS A  42      26.982   0.234  15.036  1.00 22.97           H  
ATOM    706  HZ1 LYS A  42      26.193  -1.868  15.368  1.00 24.09           H  
ATOM    707  HZ2 LYS A  42      27.530  -1.961  14.817  1.00 24.09           H  
ATOM    708  HZ3 LYS A  42      27.309  -2.204  16.228  1.00 24.09           H  
ATOM    709  N   PHE A  43      32.865   2.457  18.944  1.00 16.51           N  
ANISOU  709  N   PHE A  43     3047   1419   1806   -180    734   -179       N  
ATOM    710  CA  PHE A  43      34.309   2.670  19.074  1.00 17.15           C  
ANISOU  710  CA  PHE A  43     3029   1543   1943    -32    538   -273       C  
ATOM    711  C   PHE A  43      34.760   2.046  20.387  1.00 18.88           C  
ANISOU  711  C   PHE A  43     3554   1676   1943    254    323   -209       C  
ATOM    712  O   PHE A  43      34.833   2.706  21.428  1.00 19.47           O  
ANISOU  712  O   PHE A  43     3559   1989   1848    642    114   -320       O  
ATOM    713  CB  PHE A  43      34.656   4.155  19.006  1.00 16.15           C  
ANISOU  713  CB  PHE A  43     2687   1531   1920     55    507   -486       C  
ATOM    714  CG  PHE A  43      34.426   4.756  17.650  1.00 14.70           C  
ANISOU  714  CG  PHE A  43     2349   1527   1709   -163    429   -597       C  
ATOM    715  CD1 PHE A  43      35.439   4.779  16.706  1.00 14.77           C  
ANISOU  715  CD1 PHE A  43     2253   1476   1882   -473    395   -514       C  
ATOM    716  CD2 PHE A  43      33.185   5.288  17.314  1.00 15.31           C  
ANISOU  716  CD2 PHE A  43     2243   1762   1813    -31    364   -481       C  
ATOM    717  CE1 PHE A  43      35.219   5.312  15.447  1.00 14.30           C  
ANISOU  717  CE1 PHE A  43     2127   1506   1799   -506    348   -484       C  
ATOM    718  CE2 PHE A  43      32.962   5.818  16.062  1.00 15.01           C  
ANISOU  718  CE2 PHE A  43     2231   1690   1781    -52    240   -530       C  
ATOM    719  CZ  PHE A  43      33.988   5.839  15.132  1.00 14.82           C  
ANISOU  719  CZ  PHE A  43     2138   1676   1816   -324    128   -571       C  
ATOM    720  H   PHE A  43      32.397   3.011  19.405  1.00 19.81           H  
ATOM    721  HA  PHE A  43      34.766   2.217  18.348  1.00 20.57           H  
ATOM    722  HB2 PHE A  43      34.105   4.636  19.643  1.00 19.38           H  
ATOM    723  HB3 PHE A  43      35.594   4.269  19.228  1.00 19.38           H  
ATOM    724  HD1 PHE A  43      36.272   4.422  16.915  1.00 17.72           H  
ATOM    725  HD2 PHE A  43      32.495   5.273  17.937  1.00 18.38           H  
ATOM    726  HE1 PHE A  43      35.906   5.327  14.821  1.00 17.16           H  
ATOM    727  HE2 PHE A  43      32.131   6.176  15.848  1.00 18.01           H  
ATOM    728  HZ  PHE A  43      33.841   6.202  14.288  1.00 17.78           H  
ATOM    729  N   ASP A  44      35.075   0.756  20.333  1.00 19.69           N  
ANISOU  729  N   ASP A  44     4033   1368   2082     44    249     52       N  
ATOM    730  CA  ASP A  44      35.455   0.062  21.557  1.00 24.00           C  
ANISOU  730  CA  ASP A  44     4552   1708   2859    303     91   -159       C  
ATOM    731  C   ASP A  44      36.641   0.730  22.229  1.00 24.73           C  
ANISOU  731  C   ASP A  44     4565   1879   2953    430    -59   -123       C  
ATOM    732  O   ASP A  44      36.761   0.683  23.457  1.00 24.27           O  
ANISOU  732  O   ASP A  44     4516   1998   2706    476   -248    -25       O  
ATOM    733  CB  ASP A  44      35.754  -1.410  21.268  1.00 29.36           C  
ANISOU  733  CB  ASP A  44     5061   2066   4029    481    124   -328       C  
ATOM    734  CG  ASP A  44      34.506  -2.191  20.891  1.00 35.38           C  
ANISOU  734  CG  ASP A  44     5517   2549   5376    708    196   -653       C  
ATOM    735  OD1 ASP A  44      33.412  -1.839  21.393  1.00 37.57           O  
ANISOU  735  OD1 ASP A  44     5693   2735   5845    634    332   -707       O  
ATOM    736  OD2 ASP A  44      34.616  -3.146  20.097  1.00 38.23           O  
ANISOU  736  OD2 ASP A  44     5722   2920   5885    683    149   -613       O  
ATOM    737  H   ASP A  44      35.077   0.271  19.623  1.00 23.63           H  
ATOM    738  HA  ASP A  44      34.709   0.095  22.176  1.00 28.80           H  
ATOM    739  HB2 ASP A  44      36.380  -1.467  20.530  1.00 35.23           H  
ATOM    740  HB3 ASP A  44      36.136  -1.817  22.061  1.00 35.23           H  
ATOM    741  N   ARG A  45      37.507   1.384  21.458  1.00 25.29           N  
ANISOU  741  N   ARG A  45     4618   2016   2974    382   -115   -163       N  
ATOM    742  CA  ARG A  45      38.714   1.942  22.049  1.00 26.95           C  
ANISOU  742  CA  ARG A  45     4794   2322   3124    356   -233   -234       C  
ATOM    743  C   ARG A  45      38.453   3.174  22.900  1.00 24.90           C  
ANISOU  743  C   ARG A  45     4474   2130   2858     28   -251   -266       C  
ATOM    744  O   ARG A  45      39.268   3.469  23.776  1.00 25.05           O  
ANISOU  744  O   ARG A  45     4448   2367   2704   -203   -496   -156       O  
ATOM    745  CB  ARG A  45      39.760   2.242  20.980  1.00 31.47           C  
ANISOU  745  CB  ARG A  45     5313   2835   3811    538    -31   -265       C  
ATOM    746  CG  ARG A  45      40.496   0.988  20.511  1.00 36.21           C  
ANISOU  746  CG  ARG A  45     5862   3483   4413    771     28    -78       C  
ATOM    747  CD  ARG A  45      41.969   1.244  20.193  1.00 40.26           C  
ANISOU  747  CD  ARG A  45     6376   4084   4836   1082     -5     37       C  
ATOM    748  NE  ARG A  45      42.148   1.872  18.887  1.00 43.14           N  
ANISOU  748  NE  ARG A  45     6783   4500   5108   1324    -99     22       N  
ATOM    749  CZ  ARG A  45      42.144   3.182  18.673  1.00 45.62           C  
ANISOU  749  CZ  ARG A  45     7113   4780   5440   1583   -171   -156       C  
ATOM    750  NH1 ARG A  45      41.971   4.027  19.674  1.00 46.81           N  
ANISOU  750  NH1 ARG A  45     7249   4918   5621   1666   -211   -157       N  
ATOM    751  NH2 ARG A  45      42.316   3.656  17.448  1.00 47.00           N  
ANISOU  751  NH2 ARG A  45     7255   4925   5676   1713   -283   -223       N  
ATOM    752  H   ARG A  45      37.422   1.514  20.612  1.00 30.35           H  
ATOM    753  HA  ARG A  45      39.095   1.271  22.636  1.00 32.34           H  
ATOM    754  HB2 ARG A  45      39.322   2.638  20.210  1.00 37.77           H  
ATOM    755  HB3 ARG A  45      40.416   2.857  21.342  1.00 37.77           H  
ATOM    756  HG2 ARG A  45      40.453   0.317  21.211  1.00 43.45           H  
ATOM    757  HG3 ARG A  45      40.070   0.654  19.706  1.00 43.45           H  
ATOM    758  HD2 ARG A  45      42.341   1.836  20.866  1.00 48.31           H  
ATOM    759  HD3 ARG A  45      42.445   0.400  20.191  1.00 48.31           H  
ATOM    760  HE  ARG A  45      42.265   1.356  18.208  1.00 51.77           H  
ATOM    761 HH11 ARG A  45      41.859   3.729  20.473  1.00 56.18           H  
ATOM    762 HH12 ARG A  45      41.970   4.874  19.526  1.00 56.18           H  
ATOM    763 HH21 ARG A  45      42.429   3.114  16.789  1.00 56.40           H  
ATOM    764 HH22 ARG A  45      42.313   4.505  17.311  1.00 56.40           H  
ATOM    765  N   PHE A  46      37.351   3.903  22.685  1.00 22.16           N  
ANISOU  765  N   PHE A  46     4173   1765   2482     -8    -58   -208       N  
ATOM    766  CA  PHE A  46      37.108   5.082  23.515  1.00 21.64           C  
ANISOU  766  CA  PHE A  46     3966   1846   2409    -36    129    -25       C  
ATOM    767  C   PHE A  46      35.621   5.304  23.817  1.00 19.37           C  
ANISOU  767  C   PHE A  46     3878   1583   1900     21    -47    -46       C  
ATOM    768  O   PHE A  46      35.212   6.427  24.140  1.00 19.01           O  
ANISOU  768  O   PHE A  46     3914   1590   1717     87   -169     96       O  
ATOM    769  CB  PHE A  46      37.812   6.337  22.967  1.00 21.49           C  
ANISOU  769  CB  PHE A  46     3775   1989   2402    -91    167   -118       C  
ATOM    770  CG  PHE A  46      37.615   6.570  21.499  1.00 19.79           C  
ANISOU  770  CG  PHE A  46     3603   1867   2051   -217    554     58       C  
ATOM    771  CD1 PHE A  46      36.436   7.118  21.024  1.00 18.91           C  
ANISOU  771  CD1 PHE A  46     3525   1841   1820   -578    494     94       C  
ATOM    772  CD2 PHE A  46      38.627   6.291  20.600  1.00 22.51           C  
ANISOU  772  CD2 PHE A  46     3659   2038   2854    -77    569     27       C  
ATOM    773  CE1 PHE A  46      36.255   7.347  19.681  1.00 19.11           C  
ANISOU  773  CE1 PHE A  46     3552   1802   1907   -726    444    110       C  
ATOM    774  CE2 PHE A  46      38.455   6.516  19.258  1.00 21.39           C  
ANISOU  774  CE2 PHE A  46     3594   1885   2649   -419    671    127       C  
ATOM    775  CZ  PHE A  46      37.271   7.048  18.793  1.00 19.63           C  
ANISOU  775  CZ  PHE A  46     3561   1763   2136   -666    619    103       C  
ATOM    776  H   PHE A  46      36.753   3.743  22.089  1.00 26.59           H  
ATOM    777  HA  PHE A  46      37.523   4.905  24.374  1.00 25.97           H  
ATOM    778  HB2 PHE A  46      37.470   7.114  23.436  1.00 25.79           H  
ATOM    779  HB3 PHE A  46      38.765   6.253  23.127  1.00 25.79           H  
ATOM    780  HD1 PHE A  46      35.750   7.317  21.620  1.00 22.70           H  
ATOM    781  HD2 PHE A  46      39.427   5.929  20.907  1.00 27.01           H  
ATOM    782  HE1 PHE A  46      35.455   7.706  19.372  1.00 22.93           H  
ATOM    783  HE2 PHE A  46      39.139   6.314  18.661  1.00 25.67           H  
ATOM    784  HZ  PHE A  46      37.155   7.202  17.883  1.00 23.56           H  
ATOM    785  N   LYS A  47      34.815   4.234  23.817  1.00 19.95           N  
ANISOU  785  N   LYS A  47     3917   1848   1815    154   -164    -80       N  
ATOM    786  CA  LYS A  47      33.386   4.390  24.075  1.00 19.67           C  
ANISOU  786  CA  LYS A  47     3877   1887   1709     42   -375   -318       C  
ATOM    787  C   LYS A  47      33.080   4.820  25.500  1.00 19.91           C  
ANISOU  787  C   LYS A  47     3793   1997   1776    106   -318   -211       C  
ATOM    788  O   LYS A  47      31.939   5.205  25.784  1.00 21.70           O  
ANISOU  788  O   LYS A  47     3865   2342   2037    312   -244   -144       O  
ATOM    789  CB  LYS A  47      32.624   3.112  23.739  1.00 21.56           C  
ANISOU  789  CB  LYS A  47     4108   1946   2138     67   -189   -245       C  
ATOM    790  CG  LYS A  47      33.000   1.908  24.559  1.00 23.72           C  
ANISOU  790  CG  LYS A  47     4339   1907   2766    -14     68   -423       C  
ATOM    791  CD  LYS A  47      32.223   0.703  24.067  1.00 27.91           C  
ANISOU  791  CD  LYS A  47     4592   2110   3901     18     57   -418       C  
ATOM    792  CE  LYS A  47      32.568  -0.551  24.825  1.00 31.41           C  
ANISOU  792  CE  LYS A  47     4823   2249   4862     79     60   -400       C  
ATOM    793  NZ  LYS A  47      31.837  -1.708  24.239  1.00 33.91           N  
ANISOU  793  NZ  LYS A  47     4968   2436   5480    135     58   -459       N  
ATOM    794  H   LYS A  47      35.069   3.425  23.674  1.00 23.94           H  
ATOM    795  HA  LYS A  47      33.049   5.085  23.489  1.00 23.60           H  
ATOM    796  HB2 LYS A  47      31.677   3.274  23.874  1.00 25.87           H  
ATOM    797  HB3 LYS A  47      32.786   2.893  22.808  1.00 25.87           H  
ATOM    798  HG2 LYS A  47      33.948   1.728  24.460  1.00 28.46           H  
ATOM    799  HG3 LYS A  47      32.776   2.064  25.489  1.00 28.46           H  
ATOM    800  HD2 LYS A  47      31.274   0.870  24.179  1.00 33.49           H  
ATOM    801  HD3 LYS A  47      32.427   0.554  23.131  1.00 33.49           H  
ATOM    802  HE2 LYS A  47      33.521  -0.720  24.758  1.00 37.69           H  
ATOM    803  HE3 LYS A  47      32.302  -0.454  25.753  1.00 37.69           H  
ATOM    804  HZ1 LYS A  47      32.039  -2.452  24.684  1.00 40.69           H  
ATOM    805  HZ2 LYS A  47      30.959  -1.570  24.288  1.00 40.69           H  
ATOM    806  HZ3 LYS A  47      32.066  -1.811  23.385  1.00 40.69           H  
ATOM    807  N   HIS A  48      34.062   4.777  26.392  1.00 18.70           N  
ANISOU  807  N   HIS A  48     3789   1840   1477     29   -329   -122       N  
ATOM    808  CA  HIS A  48      33.877   5.198  27.770  1.00 19.59           C  
ANISOU  808  CA  HIS A  48     3919   2026   1500     55   -371    -81       C  
ATOM    809  C   HIS A  48      33.982   6.706  27.968  1.00 18.45           C  
ANISOU  809  C   HIS A  48     3739   1994   1280    -67   -225   -294       C  
ATOM    810  O   HIS A  48      33.717   7.184  29.075  1.00 19.08           O  
ANISOU  810  O   HIS A  48     3896   2019   1334   -163   -151   -211       O  
ATOM    811  CB  HIS A  48      34.953   4.533  28.623  1.00 24.70           C  
ANISOU  811  CB  HIS A  48     4159   2575   2652    210   -458   -140       C  
ATOM    812  CG  HIS A  48      36.341   4.925  28.221  1.00 30.04           C  
ANISOU  812  CG  HIS A  48     4293   3221   3899    333   -369   -473       C  
ATOM    813  ND1 HIS A  48      36.955   4.430  27.089  1.00 31.92           N  
ANISOU  813  ND1 HIS A  48     4388   3456   4283    335   -322   -546       N  
ATOM    814  CD2 HIS A  48      37.219   5.793  28.777  1.00 32.75           C  
ANISOU  814  CD2 HIS A  48     4385   3485   4574    384   -328   -548       C  
ATOM    815  CE1 HIS A  48      38.160   4.960  26.978  1.00 33.60           C  
ANISOU  815  CE1 HIS A  48     4463   3620   4684    404   -241   -609       C  
ATOM    816  NE2 HIS A  48      38.344   5.791  27.989  1.00 33.68           N  
ANISOU  816  NE2 HIS A  48     4459   3529   4809    402   -326   -683       N  
ATOM    817  H   HIS A  48      34.858   4.502  26.218  1.00 22.44           H  
ATOM    818  HA  HIS A  48      33.007   4.905  28.086  1.00 23.51           H  
ATOM    819  HB2 HIS A  48      34.826   4.791  29.549  1.00 29.64           H  
ATOM    820  HB3 HIS A  48      34.877   3.570  28.533  1.00 29.64           H  
ATOM    821  HD1 HIS A  48      36.611   3.858  26.547  1.00 38.30           H  
ATOM    822  HD2 HIS A  48      37.089   6.289  29.553  1.00 39.30           H  
ATOM    823  HE1 HIS A  48      38.773   4.781  26.302  1.00 40.32           H  
ATOM    824  N   LEU A  49      34.367   7.468  26.948  1.00 17.61           N  
ANISOU  824  N   LEU A  49     3407   1782   1503     18    111     71       N  
ATOM    825  CA  LEU A  49      34.511   8.909  27.122  1.00 16.71           C  
ANISOU  825  CA  LEU A  49     3182   1782   1386    -32    250    -82       C  
ATOM    826  C   LEU A  49      33.160   9.539  27.437  1.00 16.47           C  
ANISOU  826  C   LEU A  49     3026   1788   1443    -51    110   -290       C  
ATOM    827  O   LEU A  49      32.152   9.236  26.789  1.00 17.49           O  
ANISOU  827  O   LEU A  49     2928   2048   1671    -27    -18   -382       O  
ATOM    828  CB  LEU A  49      35.093   9.528  25.851  1.00 18.45           C  
ANISOU  828  CB  LEU A  49     3156   1950   1903     56    352   -183       C  
ATOM    829  CG  LEU A  49      36.494   9.070  25.431  1.00 20.44           C  
ANISOU  829  CG  LEU A  49     3212   2067   2489     57    403   -439       C  
ATOM    830  CD1 LEU A  49      36.848   9.629  24.049  1.00 22.01           C  
ANISOU  830  CD1 LEU A  49     3304   2004   3055    128    723     35       C  
ATOM    831  CD2 LEU A  49      37.539   9.474  26.458  1.00 23.67           C  
ANISOU  831  CD2 LEU A  49     3294   2334   3363    166    210   -796       C  
ATOM    832  H   LEU A  49      34.549   7.181  26.158  1.00 21.13           H  
ATOM    833  HA  LEU A  49      35.115   9.089  27.859  1.00 20.06           H  
ATOM    834  HB2 LEU A  49      34.494   9.325  25.115  1.00 22.14           H  
ATOM    835  HB3 LEU A  49      35.132  10.489  25.974  1.00 22.14           H  
ATOM    836  HG  LEU A  49      36.500   8.102  25.369  1.00 24.53           H  
ATOM    837 HD11 LEU A  49      37.737   9.327  23.805  1.00 26.41           H  
ATOM    838 HD12 LEU A  49      36.200   9.307  23.404  1.00 26.41           H  
ATOM    839 HD13 LEU A  49      36.826  10.598  24.086  1.00 26.41           H  
ATOM    840 HD21 LEU A  49      38.410   9.168  26.158  1.00 28.40           H  
ATOM    841 HD22 LEU A  49      37.539  10.440  26.544  1.00 28.40           H  
ATOM    842 HD23 LEU A  49      37.319   9.065  27.309  1.00 28.40           H  
ATOM    843  N   LYS A  50      33.142  10.433  28.425  1.00 16.59           N  
ANISOU  843  N   LYS A  50     2888   1881   1533     29    234   -440       N  
ATOM    844  CA  LYS A  50      31.893  10.937  28.982  1.00 17.07           C  
ANISOU  844  CA  LYS A  50     2761   2156   1570    200    188   -331       C  
ATOM    845  C   LYS A  50      31.551  12.371  28.591  1.00 17.46           C  
ANISOU  845  C   LYS A  50     2603   2371   1662    489    235    150       C  
ATOM    846  O   LYS A  50      30.370  12.723  28.630  1.00 21.48           O  
ANISOU  846  O   LYS A  50     2687   2643   2830    736     46    335       O  
ATOM    847  CB  LYS A  50      31.911  10.849  30.516  1.00 17.60           C  
ANISOU  847  CB  LYS A  50     3035   2034   1618    171    284   -206       C  
ATOM    848  CG  LYS A  50      32.026   9.439  31.092  1.00 17.97           C  
ANISOU  848  CG  LYS A  50     3224   1891   1711    145    147   -198       C  
ATOM    849  CD  LYS A  50      32.091   9.478  32.631  1.00 19.16           C  
ANISOU  849  CD  LYS A  50     3387   2003   1890    305     86   -143       C  
ATOM    850  CE  LYS A  50      32.292   8.106  33.261  1.00 20.28           C  
ANISOU  850  CE  LYS A  50     3546   2087   2074    292     26    -91       C  
ATOM    851  NZ  LYS A  50      31.079   7.269  33.167  1.00 21.67           N  
ANISOU  851  NZ  LYS A  50     3747   2069   2418    296     99    126       N  
ATOM    852  H   LYS A  50      33.846  10.764  28.792  1.00 19.91           H  
ATOM    853  HA  LYS A  50      31.171  10.372  28.667  1.00 20.48           H  
ATOM    854  HB2 LYS A  50      32.668  11.360  30.843  1.00 21.12           H  
ATOM    855  HB3 LYS A  50      31.089  11.236  30.855  1.00 21.12           H  
ATOM    856  HG2 LYS A  50      31.248   8.920  30.832  1.00 21.56           H  
ATOM    857  HG3 LYS A  50      32.836   9.021  30.762  1.00 21.56           H  
ATOM    858  HD2 LYS A  50      32.834  10.041  32.899  1.00 22.99           H  
ATOM    859  HD3 LYS A  50      31.259   9.843  32.971  1.00 22.99           H  
ATOM    860  HE2 LYS A  50      33.013   7.647  32.801  1.00 24.34           H  
ATOM    861  HE3 LYS A  50      32.511   8.216  34.200  1.00 24.34           H  
ATOM    862  HZ1 LYS A  50      31.228   6.475  33.543  1.00 26.01           H  
ATOM    863  HZ2 LYS A  50      30.403   7.666  33.587  1.00 26.01           H  
ATOM    864  HZ3 LYS A  50      30.859   7.148  32.313  1.00 26.01           H  
ATOM    865  N   THR A  51      32.537  13.211  28.247  1.00 16.43           N  
ANISOU  865  N   THR A  51     2606   2253   1381    550    575    274       N  
ATOM    866  CA  THR A  51      32.351  14.646  28.036  1.00 16.32           C  
ANISOU  866  CA  THR A  51     2503   2376   1320    592    461     56       C  
ATOM    867  C   THR A  51      33.144  15.118  26.815  1.00 15.93           C  
ANISOU  867  C   THR A  51     2397   2266   1388    462    139    -67       C  
ATOM    868  O   THR A  51      34.091  14.466  26.368  1.00 14.43           O  
ANISOU  868  O   THR A  51     2209   2153   1120    371    110     97       O  
ATOM    869  CB  THR A  51      32.862  15.448  29.249  1.00 17.18           C  
ANISOU  869  CB  THR A  51     2657   2523   1346    751    441    181       C  
ATOM    870  OG1 THR A  51      34.276  15.233  29.372  1.00 16.75           O  
ANISOU  870  OG1 THR A  51     2658   2520   1186    654    103    -46       O  
ATOM    871  CG2 THR A  51      32.145  15.049  30.544  1.00 18.47           C  
ANISOU  871  CG2 THR A  51     2881   2683   1455   1099    582    363       C  
ATOM    872  H   THR A  51      33.350  12.958  28.126  1.00 19.71           H  
ATOM    873  HA  THR A  51      31.412  14.844  27.899  1.00 19.58           H  
ATOM    874  HB  THR A  51      32.699  16.392  29.095  1.00 20.61           H  
ATOM    875  HG1 THR A  51      34.576  15.662  30.029  1.00 20.10           H  
ATOM    876 HG21 THR A  51      32.488  15.571  31.287  1.00 22.17           H  
ATOM    877 HG22 THR A  51      31.192  15.211  30.459  1.00 22.17           H  
ATOM    878 HG23 THR A  51      32.289  14.108  30.726  1.00 22.17           H  
ATOM    879  N   GLU A  52      32.771  16.297  26.301  1.00 15.52           N  
ANISOU  879  N   GLU A  52     2553   2107   1239    436     64     15       N  
ATOM    880  CA  GLU A  52      33.515  16.897  25.196  1.00 15.18           C  
ANISOU  880  CA  GLU A  52     2729   1941   1095    504    -70      8       C  
ATOM    881  C   GLU A  52      34.965  17.162  25.584  1.00 14.31           C  
ANISOU  881  C   GLU A  52     2617   1760   1060    333    -40   -162       C  
ATOM    882  O   GLU A  52      35.874  16.962  24.774  1.00 13.96           O  
ANISOU  882  O   GLU A  52     2499   1674   1130    127     43    -51       O  
ATOM    883  CB  GLU A  52      32.834  18.195  24.740  1.00 16.67           C  
ANISOU  883  CB  GLU A  52     3059   2070   1205    624    -87     67       C  
ATOM    884  CG  GLU A  52      33.602  18.952  23.669  1.00 19.37           C  
ANISOU  884  CG  GLU A  52     3475   2386   1498    862     20      3       C  
ATOM    885  CD  GLU A  52      32.773  20.022  22.985  1.00 23.33           C  
ANISOU  885  CD  GLU A  52     3909   2740   2216   1123    209    410       C  
ATOM    886  OE1 GLU A  52      33.284  20.644  22.031  1.00 23.97           O  
ANISOU  886  OE1 GLU A  52     4104   2706   2297   1043    212    458       O  
ATOM    887  OE2 GLU A  52      31.606  20.231  23.376  1.00 25.76           O  
ANISOU  887  OE2 GLU A  52     4014   3062   2714   1341    137    850       O  
ATOM    888  H   GLU A  52      32.100  16.761  26.574  1.00 18.63           H  
ATOM    889  HA  GLU A  52      33.514  16.282  24.446  1.00 18.21           H  
ATOM    890  HB2 GLU A  52      31.960  17.978  24.380  1.00 20.01           H  
ATOM    891  HB3 GLU A  52      32.738  18.782  25.506  1.00 20.01           H  
ATOM    892  HG2 GLU A  52      34.368  19.385  24.078  1.00 23.24           H  
ATOM    893  HG3 GLU A  52      33.898  18.325  22.992  1.00 23.24           H  
ATOM    894  N   ALA A  53      35.204  17.608  26.818  1.00 14.80           N  
ANISOU  894  N   ALA A  53     2643   1851   1130    299     37   -189       N  
ATOM    895  CA  ALA A  53      36.573  17.832  27.274  1.00 15.99           C  
ANISOU  895  CA  ALA A  53     2696   2042   1340    400    -74   -281       C  
ATOM    896  C   ALA A  53      37.404  16.554  27.178  1.00 15.02           C  
ANISOU  896  C   ALA A  53     2530   1990   1188    263   -123   -265       C  
ATOM    897  O   ALA A  53      38.551  16.580  26.706  1.00 15.15           O  
ANISOU  897  O   ALA A  53     2581   1998   1177    269   -102   -223       O  
ATOM    898  CB  ALA A  53      36.556  18.366  28.707  1.00 17.24           C  
ANISOU  898  CB  ALA A  53     2804   2333   1413    550   -204   -471       C  
ATOM    899  H   ALA A  53      34.599  17.786  27.402  1.00 17.76           H  
ATOM    900  HA  ALA A  53      36.988  18.502  26.709  1.00 19.19           H  
ATOM    901  HB1 ALA A  53      37.469  18.512  29.001  1.00 20.69           H  
ATOM    902  HB2 ALA A  53      36.065  19.203  28.726  1.00 20.69           H  
ATOM    903  HB3 ALA A  53      36.123  17.715  29.281  1.00 20.69           H  
ATOM    904  N   GLU A  54      36.844  15.419  27.608  1.00 14.84           N  
ANISOU  904  N   GLU A  54     2479   1991   1167    303    -75     13       N  
ATOM    905  CA  GLU A  54      37.568  14.152  27.510  1.00 15.24           C  
ANISOU  905  CA  GLU A  54     2493   2013   1286    357     12    214       C  
ATOM    906  C   GLU A  54      37.820  13.780  26.059  1.00 13.50           C  
ANISOU  906  C   GLU A  54     2116   1822   1192    146     51    123       C  
ATOM    907  O   GLU A  54      38.891  13.266  25.713  1.00 14.21           O  
ANISOU  907  O   GLU A  54     2023   1921   1453    207   -240     37       O  
ATOM    908  CB  GLU A  54      36.794  13.034  28.222  1.00 15.65           C  
ANISOU  908  CB  GLU A  54     2679   2098   1169    273   -110    209       C  
ATOM    909  CG  GLU A  54      36.830  13.172  29.742  1.00 16.90           C  
ANISOU  909  CG  GLU A  54     2728   2227   1465     81    -58    116       C  
ATOM    910  CD  GLU A  54      36.171  12.029  30.497  1.00 17.58           C  
ANISOU  910  CD  GLU A  54     2789   2335   1555    -15    115    133       C  
ATOM    911  OE1 GLU A  54      36.344  11.980  31.731  1.00 17.72           O  
ANISOU  911  OE1 GLU A  54     2830   2361   1542    349    351    228       O  
ATOM    912  OE2 GLU A  54      35.490  11.180  29.889  1.00 19.35           O  
ANISOU  912  OE2 GLU A  54     2885   2515   1954   -318    -70    229       O  
ATOM    913  H   GLU A  54      36.060  15.357  27.955  1.00 17.80           H  
ATOM    914  HA  GLU A  54      38.429  14.245  27.948  1.00 18.29           H  
ATOM    915  HB2 GLU A  54      35.866  13.062  27.940  1.00 18.78           H  
ATOM    916  HB3 GLU A  54      37.187  12.178  27.989  1.00 18.78           H  
ATOM    917  HG2 GLU A  54      37.756  13.218  30.027  1.00 20.28           H  
ATOM    918  HG3 GLU A  54      36.371  13.991  29.989  1.00 20.28           H  
ATOM    919  N   MET A  55      36.843  14.042  25.191  1.00 12.81           N  
ANISOU  919  N   MET A  55     1980   1691   1195     60    -60     45       N  
ATOM    920  CA  MET A  55      37.000  13.736  23.778  1.00 11.88           C  
ANISOU  920  CA  MET A  55     1868   1555   1089    -42      3   -113       C  
ATOM    921  C   MET A  55      38.117  14.565  23.154  1.00 12.25           C  
ANISOU  921  C   MET A  55     1885   1642   1125   -178    -15    -45       C  
ATOM    922  O   MET A  55      38.919  14.046  22.367  1.00 12.27           O  
ANISOU  922  O   MET A  55     1861   1605   1197   -171    122    -73       O  
ATOM    923  CB  MET A  55      35.670  13.967  23.058  1.00 11.67           C  
ANISOU  923  CB  MET A  55     1806   1585   1044     17    109    -89       C  
ATOM    924  CG  MET A  55      34.596  12.972  23.450  1.00 12.66           C  
ANISOU  924  CG  MET A  55     1782   1758   1270     27    124    -48       C  
ATOM    925  SD  MET A  55      33.005  13.411  22.750  1.00 13.46           S  
ANISOU  925  SD  MET A  55     1705   1930   1478   -187    136   -100       S  
ATOM    926  CE  MET A  55      31.958  12.275  23.649  1.00 16.78           C  
ANISOU  926  CE  MET A  55     2023   2177   2174   -162    195     90       C  
ATOM    927  H   MET A  55      36.085  14.393  25.397  1.00 15.37           H  
ATOM    928  HA  MET A  55      37.225  12.797  23.687  1.00 14.25           H  
ATOM    929  HB2 MET A  55      35.346  14.856  23.274  1.00 14.01           H  
ATOM    930  HB3 MET A  55      35.812  13.890  22.102  1.00 14.01           H  
ATOM    931  HG2 MET A  55      34.840  12.092  23.123  1.00 15.19           H  
ATOM    932  HG3 MET A  55      34.510  12.959  24.416  1.00 15.19           H  
ATOM    933  HE1 MET A  55      31.039  12.402  23.365  1.00 20.13           H  
ATOM    934  HE2 MET A  55      32.241  11.367  23.458  1.00 20.13           H  
ATOM    935  HE3 MET A  55      32.040  12.455  24.598  1.00 20.13           H  
ATOM    936  N   LYS A  56      38.170  15.865  23.473  1.00 13.28           N  
ANISOU  936  N   LYS A  56     2173   1709   1164   -127    -13     92       N  
ATOM    937  CA  LYS A  56      39.207  16.740  22.926  1.00 14.31           C  
ANISOU  937  CA  LYS A  56     2425   1804   1209   -151   -116     32       C  
ATOM    938  C   LYS A  56      40.599  16.329  23.391  1.00 14.85           C  
ANISOU  938  C   LYS A  56     2244   1940   1459   -226   -205   -115       C  
ATOM    939  O   LYS A  56      41.582  16.536  22.664  1.00 16.22           O  
ANISOU  939  O   LYS A  56     2325   2130   1709   -364   -124     44       O  
ATOM    940  CB  LYS A  56      38.940  18.192  23.332  1.00 17.98           C  
ANISOU  940  CB  LYS A  56     2920   1928   1985     84   -530   -345       C  
ATOM    941  CG  LYS A  56      37.852  18.875  22.541  1.00 22.89           C  
ANISOU  941  CG  LYS A  56     3520   2250   2928    526   -848   -599       C  
ATOM    942  CD  LYS A  56      37.649  20.303  23.022  1.00 28.42           C  
ANISOU  942  CD  LYS A  56     3991   2680   4126    887  -1052   -460       C  
ATOM    943  CE  LYS A  56      36.540  21.001  22.273  1.00 32.35           C  
ANISOU  943  CE  LYS A  56     4299   3032   4963   1157  -1112   -386       C  
ATOM    944  NZ  LYS A  56      36.195  22.289  22.927  1.00 34.95           N  
ANISOU  944  NZ  LYS A  56     4585   3208   5486   1353  -1059   -444       N  
ATOM    945  H   LYS A  56      37.619  16.260  24.001  1.00 15.94           H  
ATOM    946  HA  LYS A  56      39.186  16.689  21.958  1.00 17.17           H  
ATOM    947  HB2 LYS A  56      38.679  18.209  24.266  1.00 21.58           H  
ATOM    948  HB3 LYS A  56      39.756  18.702  23.211  1.00 21.58           H  
ATOM    949  HG2 LYS A  56      38.103  18.900  21.604  1.00 27.47           H  
ATOM    950  HG3 LYS A  56      37.019  18.392  22.655  1.00 27.47           H  
ATOM    951  HD2 LYS A  56      37.417  20.292  23.964  1.00 34.10           H  
ATOM    952  HD3 LYS A  56      38.468  20.805  22.885  1.00 34.10           H  
ATOM    953  HE2 LYS A  56      36.829  21.185  21.365  1.00 38.83           H  
ATOM    954  HE3 LYS A  56      35.750  20.438  22.268  1.00 38.83           H  
ATOM    955  HZ1 LYS A  56      35.540  22.692  22.479  1.00 41.94           H  
ATOM    956  HZ2 LYS A  56      35.925  22.142  23.763  1.00 41.94           H  
ATOM    957  HZ3 LYS A  56      36.907  22.822  22.942  1.00 41.94           H  
ATOM    958  N   ALA A  57      40.709  15.767  24.600  1.00 14.23           N  
ANISOU  958  N   ALA A  57     2022   1867   1517   -215   -259   -167       N  
ATOM    959  CA  ALA A  57      41.997  15.384  25.169  1.00 14.48           C  
ANISOU  959  CA  ALA A  57     1996   2083   1425   -121   -336   -384       C  
ATOM    960  C   ALA A  57      42.475  14.009  24.710  1.00 14.73           C  
ANISOU  960  C   ALA A  57     1902   2158   1537     82   -312   -247       C  
ATOM    961  O   ALA A  57      43.618  13.642  25.006  1.00 17.38           O  
ANISOU  961  O   ALA A  57     1964   2443   2198    233   -550   -515       O  
ATOM    962  CB  ALA A  57      41.909  15.408  26.698  1.00 16.08           C  
ANISOU  962  CB  ALA A  57     2149   2254   1708    176   -463   -468       C  
ATOM    963  H   ALA A  57      40.040  15.597  25.113  1.00 17.07           H  
ATOM    964  HA  ALA A  57      42.664  16.035  24.899  1.00 17.38           H  
ATOM    965  HB1 ALA A  57      42.768  15.152  27.067  1.00 19.30           H  
ATOM    966  HB2 ALA A  57      41.677  16.304  26.987  1.00 19.30           H  
ATOM    967  HB3 ALA A  57      41.226  14.781  26.984  1.00 19.30           H  
ATOM    968  N   SER A  58      41.647  13.257  23.983  1.00 12.78           N  
ANISOU  968  N   SER A  58     1896   1724   1238      1   -164   -130       N  
ATOM    969  CA  SER A  58      41.942  11.870  23.622  1.00 12.94           C  
ANISOU  969  CA  SER A  58     2042   1690   1184     81   -125     -7       C  
ATOM    970  C   SER A  58      42.805  11.822  22.366  1.00 12.83           C  
ANISOU  970  C   SER A  58     1891   1919   1065    161   -177     22       C  
ATOM    971  O   SER A  58      42.342  12.132  21.262  1.00 12.18           O  
ANISOU  971  O   SER A  58     1783   1800   1045     53      2     23       O  
ATOM    972  CB  SER A  58      40.644  11.099  23.394  1.00 13.18           C  
ANISOU  972  CB  SER A  58     2119   1589   1300   -171      8     35       C  
ATOM    973  OG  SER A  58      40.899   9.825  22.836  1.00 13.72           O  
ANISOU  973  OG  SER A  58     2388   1585   1241     17    -41    104       O  
ATOM    974  H   SER A  58      40.891  13.535  23.681  1.00 15.34           H  
ATOM    975  HA  SER A  58      42.428  11.445  24.345  1.00 15.52           H  
ATOM    976  HB2 SER A  58      40.192  10.985  24.245  1.00 15.82           H  
ATOM    977  HB3 SER A  58      40.081  11.602  22.786  1.00 15.82           H  
ATOM    978  HG  SER A  58      41.386   9.377  23.353  1.00 16.46           H  
ATOM    979  N   GLU A  59      44.051  11.388  22.518  1.00 14.74           N  
ANISOU  979  N   GLU A  59     1881   2313   1405    237   -292    -82       N  
ATOM    980  CA  GLU A  59      44.896  11.218  21.345  1.00 15.50           C  
ANISOU  980  CA  GLU A  59     1871   2511   1507    280   -124    -85       C  
ATOM    981  C   GLU A  59      44.368  10.105  20.446  1.00 15.30           C  
ANISOU  981  C   GLU A  59     2074   2354   1384    518   -125    172       C  
ATOM    982  O   GLU A  59      44.475  10.204  19.220  1.00 15.31           O  
ANISOU  982  O   GLU A  59     1961   2490   1364    590   -176    118       O  
ATOM    983  CB AGLU A  59      46.341  10.947  21.777  0.46 17.85           C  
ANISOU  983  CB AGLU A  59     1973   2813   1994    458    122    -84       C  
ATOM    984  CB BGLU A  59      46.348  10.973  21.762  0.54 19.16           C  
ANISOU  984  CB BGLU A  59     2109   2980   2190    538   -222   -213       C  
ATOM    985  CG AGLU A  59      47.341  10.827  20.629  0.46 20.27           C  
ANISOU  985  CG AGLU A  59     2202   3010   2491    654    271   -118       C  
ATOM    986  CG BGLU A  59      46.966  12.130  22.540  0.54 22.92           C  
ANISOU  986  CG BGLU A  59     2439   3368   2902    745   -431   -351       C  
ATOM    987  CD AGLU A  59      47.758  12.163  20.054  0.46 22.83           C  
ANISOU  987  CD AGLU A  59     2390   3202   3080    764    514    -62       C  
ATOM    988  CD BGLU A  59      46.791  13.475  21.846  0.54 26.13           C  
ANISOU  988  CD BGLU A  59     2735   3672   3520    882   -445   -535       C  
ATOM    989  OE1AGLU A  59      48.331  12.174  18.943  0.46 24.21           O  
ANISOU  989  OE1AGLU A  59     2579   3316   3304    926    610   -133       O  
ATOM    990  OE1BGLU A  59      46.966  13.549  20.609  0.54 26.77           O  
ANISOU  990  OE1BGLU A  59     2763   3831   3576    866   -622   -429       O  
ATOM    991  OE2AGLU A  59      47.526  13.198  20.708  0.46 24.62           O  
ANISOU  991  OE2AGLU A  59     2375   3316   3664    791    579     61       O  
ATOM    992  OE2BGLU A  59      46.460  14.458  22.543  0.54 27.57           O  
ANISOU  992  OE2BGLU A  59     2876   3716   3885    952   -492   -659       O  
ATOM    993  H   GLU A  59      44.423  11.191  23.268  1.00 17.68           H  
ATOM    994  HA  GLU A  59      44.874  12.040  20.831  1.00 18.60           H  
ATOM    995  HB2AGLU A  59      46.635  11.674  22.347  0.46 21.41           H  
ATOM    996  HB2BGLU A  59      46.383  10.184  22.326  0.54 22.99           H  
ATOM    997  HB3AGLU A  59      46.363  10.114  22.274  0.46 21.41           H  
ATOM    998  HB3BGLU A  59      46.883  10.831  20.966  0.54 22.99           H  
ATOM    999  HG2AGLU A  59      48.138  10.380  20.954  0.46 24.33           H  
ATOM   1000  HG2BGLU A  59      46.544  12.186  23.411  0.54 27.50           H  
ATOM   1001  HG3AGLU A  59      46.939  10.308  19.916  0.46 24.33           H  
ATOM   1002  HG3BGLU A  59      47.917  11.969  22.643  0.54 27.50           H  
ATOM   1003  N   ASP A  60      43.765   9.064  21.030  1.00 15.51           N  
ANISOU 1003  N   ASP A  60     2372   2184   1337    693   -289     88       N  
ATOM   1004  CA  ASP A  60      43.187   7.980  20.234  1.00 16.28           C  
ANISOU 1004  CA  ASP A  60     2650   1927   1610    733    -86    275       C  
ATOM   1005  C   ASP A  60      42.068   8.489  19.333  1.00 13.93           C  
ANISOU 1005  C   ASP A  60     2421   1605   1267    463     46    261       C  
ATOM   1006  O   ASP A  60      41.994   8.133  18.151  1.00 13.83           O  
ANISOU 1006  O   ASP A  60     2440   1495   1318    384     50    124       O  
ATOM   1007  CB  ASP A  60      42.637   6.889  21.162  1.00 19.88           C  
ANISOU 1007  CB  ASP A  60     3226   2150   2177    956   -139    525       C  
ATOM   1008  CG  ASP A  60      43.709   5.939  21.688  1.00 25.60           C  
ANISOU 1008  CG  ASP A  60     3663   2600   3464   1137    -64    730       C  
ATOM   1009  OD1 ASP A  60      43.384   5.178  22.624  1.00 28.06           O  
ANISOU 1009  OD1 ASP A  60     3916   2709   4038   1046   -184    878       O  
ATOM   1010  OD2 ASP A  60      44.858   5.930  21.180  1.00 27.61           O  
ANISOU 1010  OD2 ASP A  60     3682   2854   3956   1315   -162    645       O  
ATOM   1011  H   ASP A  60      43.678   8.963  21.879  1.00 18.61           H  
ATOM   1012  HA  ASP A  60      43.876   7.588  19.675  1.00 19.54           H  
ATOM   1013  HB2 ASP A  60      42.214   7.312  21.926  1.00 23.86           H  
ATOM   1014  HB3 ASP A  60      41.985   6.361  20.675  1.00 23.86           H  
ATOM   1015  N   LEU A  61      41.170   9.308  19.882  1.00 12.73           N  
ANISOU 1015  N   LEU A  61     2124   1542   1170    226    -10    170       N  
ATOM   1016  CA  LEU A  61      40.086   9.866  19.078  1.00 11.47           C  
ANISOU 1016  CA  LEU A  61     1834   1379   1144    -61    190     34       C  
ATOM   1017  C   LEU A  61      40.642  10.729  17.952  1.00  9.89           C  
ANISOU 1017  C   LEU A  61     1528   1170   1058     34     90    -74       C  
ATOM   1018  O   LEU A  61      40.191  10.633  16.802  1.00  9.52           O  
ANISOU 1018  O   LEU A  61     1338   1225   1054      0     72    -35       O  
ATOM   1019  CB  LEU A  61      39.126  10.655  19.985  1.00 11.68           C  
ANISOU 1019  CB  LEU A  61     1729   1703   1006   -168    158    -17       C  
ATOM   1020  CG  LEU A  61      37.847  11.249  19.356  1.00 12.06           C  
ANISOU 1020  CG  LEU A  61     1695   1719   1171   -268     23    -68       C  
ATOM   1021  CD1 LEU A  61      36.785  11.419  20.410  1.00 13.67           C  
ANISOU 1021  CD1 LEU A  61     1841   1905   1449   -110    120   -183       C  
ATOM   1022  CD2 LEU A  61      38.069  12.595  18.682  1.00 12.88           C  
ANISOU 1022  CD2 LEU A  61     1728   1676   1491     45     77    -79       C  
ATOM   1023  H   LEU A  61      41.167   9.553  20.706  1.00 15.27           H  
ATOM   1024  HA  LEU A  61      39.587   9.138  18.676  1.00 13.76           H  
ATOM   1025  HB2 LEU A  61      38.839  10.065  20.699  1.00 14.02           H  
ATOM   1026  HB3 LEU A  61      39.621  11.396  20.368  1.00 14.02           H  
ATOM   1027  HG  LEU A  61      37.509  10.633  18.688  1.00 14.48           H  
ATOM   1028 HD11 LEU A  61      35.990  11.792  19.999  1.00 16.41           H  
ATOM   1029 HD12 LEU A  61      36.583  10.552  20.796  1.00 16.41           H  
ATOM   1030 HD13 LEU A  61      37.116  12.018  21.097  1.00 16.41           H  
ATOM   1031 HD21 LEU A  61      37.228  12.905  18.312  1.00 15.46           H  
ATOM   1032 HD22 LEU A  61      38.394  13.228  19.342  1.00 15.46           H  
ATOM   1033 HD23 LEU A  61      38.724  12.489  17.974  1.00 15.46           H  
ATOM   1034  N   LYS A  62      41.650  11.554  18.258  1.00 10.04           N  
ANISOU 1034  N   LYS A  62     1510   1149   1157     21    -37    -79       N  
ATOM   1035  CA  LYS A  62      42.264  12.396  17.236  1.00 10.08           C  
ANISOU 1035  CA  LYS A  62     1435   1187   1208    -74     -7   -123       C  
ATOM   1036  C   LYS A  62      42.814  11.552  16.086  1.00  9.50           C  
ANISOU 1036  C   LYS A  62     1342   1196   1073     18    -88   -106       C  
ATOM   1037  O   LYS A  62      42.621  11.876  14.904  1.00  9.11           O  
ANISOU 1037  O   LYS A  62     1315   1091   1057     89    -16    -47       O  
ATOM   1038  CB  LYS A  62      43.365  13.250  17.867  1.00 11.16           C  
ANISOU 1038  CB  LYS A  62     1573   1414   1252   -123    202    -35       C  
ATOM   1039  CG  LYS A  62      44.009  14.223  16.903  1.00 12.00           C  
ANISOU 1039  CG  LYS A  62     1718   1512   1327   -413   -102   -240       C  
ATOM   1040  CD  LYS A  62      45.305  14.810  17.433  1.00 18.00           C  
ANISOU 1040  CD  LYS A  62     2268   2174   2397   -385   -119   -191       C  
ATOM   1041  CE  LYS A  62      45.099  15.665  18.646  1.00 23.57           C  
ANISOU 1041  CE  LYS A  62     2557   2740   3660   -584   -354   -546       C  
ATOM   1042  NZ  LYS A  62      46.422  16.109  19.176  1.00 26.79           N  
ANISOU 1042  NZ  LYS A  62     2813   2974   4390   -565   -749  -1077       N  
ATOM   1043  H   LYS A  62      41.990  11.642  19.043  1.00 12.05           H  
ATOM   1044  HA  LYS A  62      41.591  12.993  16.874  1.00 12.10           H  
ATOM   1045  HB2 LYS A  62      42.984  13.763  18.596  1.00 13.39           H  
ATOM   1046  HB3 LYS A  62      44.060  12.664  18.206  1.00 13.39           H  
ATOM   1047  HG2 LYS A  62      44.207  13.761  16.073  1.00 14.40           H  
ATOM   1048  HG3 LYS A  62      43.395  14.955  16.736  1.00 14.40           H  
ATOM   1049  HD2 LYS A  62      45.904  14.086  17.674  1.00 21.60           H  
ATOM   1050  HD3 LYS A  62      45.708  15.360  16.743  1.00 21.60           H  
ATOM   1051  HE2 LYS A  62      44.581  16.449  18.408  1.00 28.29           H  
ATOM   1052  HE3 LYS A  62      44.646  15.152  19.334  1.00 28.29           H  
ATOM   1053  HZ1 LYS A  62      46.305  16.617  19.897  1.00 32.14           H  
ATOM   1054  HZ2 LYS A  62      46.913  15.401  19.398  1.00 32.14           H  
ATOM   1055  HZ3 LYS A  62      46.854  16.579  18.557  1.00 32.14           H  
ATOM   1056  N   LYS A  63      43.539  10.474  16.404  1.00 10.35           N  
ANISOU 1056  N   LYS A  63     1435   1379   1119    238    -86    -52       N  
ATOM   1057  CA  LYS A  63      44.117   9.641  15.352  1.00 11.11           C  
ANISOU 1057  CA  LYS A  63     1441   1474   1306    361    -86    -50       C  
ATOM   1058  C   LYS A  63      43.033   8.985  14.500  1.00  9.69           C  
ANISOU 1058  C   LYS A  63     1423   1240   1021    299     36     -3       C  
ATOM   1059  O   LYS A  63      43.165   8.895  13.276  1.00  9.65           O  
ANISOU 1059  O   LYS A  63     1399   1141   1127    269    -42    -16       O  
ATOM   1060  CB  LYS A  63      45.035   8.586  15.964  1.00 13.93           C  
ANISOU 1060  CB  LYS A  63     1608   2225   1460    653   -384   -171       C  
ATOM   1061  CG  LYS A  63      46.314   9.150  16.543  1.00 19.48           C  
ANISOU 1061  CG  LYS A  63     2057   2944   2401    978   -443   -111       C  
ATOM   1062  CD  LYS A  63      47.150   8.043  17.201  1.00 26.32           C  
ANISOU 1062  CD  LYS A  63     2455   3657   3889   1043   -459    -41       C  
ATOM   1063  CE  LYS A  63      48.401   8.592  17.861  1.00 32.81           C  
ANISOU 1063  CE  LYS A  63     2881   4264   5323   1137   -283    218       C  
ATOM   1064  NZ  LYS A  63      49.155   9.489  16.946  1.00 36.31           N  
ANISOU 1064  NZ  LYS A  63     3186   4484   6126   1234   -133    282       N  
ATOM   1065  H   LYS A  63      43.707  10.210  17.205  1.00 12.42           H  
ATOM   1066  HA  LYS A  63      44.655  10.200  14.770  1.00 13.33           H  
ATOM   1067  HB2 LYS A  63      44.559   8.135  16.679  1.00 16.72           H  
ATOM   1068  HB3 LYS A  63      45.277   7.946  15.277  1.00 16.72           H  
ATOM   1069  HG2 LYS A  63      46.841   9.550  15.834  1.00 23.38           H  
ATOM   1070  HG3 LYS A  63      46.098   9.812  17.219  1.00 23.38           H  
ATOM   1071  HD2 LYS A  63      46.617   7.603  17.881  1.00 31.59           H  
ATOM   1072  HD3 LYS A  63      47.421   7.404  16.523  1.00 31.59           H  
ATOM   1073  HE2 LYS A  63      48.150   9.102  18.647  1.00 39.38           H  
ATOM   1074  HE3 LYS A  63      48.980   7.855  18.110  1.00 39.38           H  
ATOM   1075  HZ1 LYS A  63      49.883   9.797  17.355  1.00 43.57           H  
ATOM   1076  HZ2 LYS A  63      49.401   9.042  16.217  1.00 43.57           H  
ATOM   1077  HZ3 LYS A  63      48.645  10.177  16.706  1.00 43.57           H  
ATOM   1078  N   VAL A  64      41.957   8.513  15.133  1.00  9.95           N  
ANISOU 1078  N   VAL A  64     1579   1026   1176    217    120     51       N  
ATOM   1079  CA  VAL A  64      40.849   7.915  14.391  1.00  9.96           C  
ANISOU 1079  CA  VAL A  64     1664    900   1220    -36    114     46       C  
ATOM   1080  C   VAL A  64      40.199   8.938  13.461  1.00  8.54           C  
ANISOU 1080  C   VAL A  64     1226    865   1156    -53     72     48       C  
ATOM   1081  O   VAL A  64      39.822   8.610  12.322  1.00  8.71           O  
ANISOU 1081  O   VAL A  64     1171    873   1264    -50    -16    -49       O  
ATOM   1082  CB  VAL A  64      39.857   7.281  15.391  1.00 12.38           C  
ANISOU 1082  CB  VAL A  64     2145   1069   1492   -182    234    101       C  
ATOM   1083  CG1 VAL A  64      38.494   6.980  14.749  1.00 13.80           C  
ANISOU 1083  CG1 VAL A  64     2284   1220   1741   -337    507     30       C  
ATOM   1084  CG2 VAL A  64      40.465   6.005  15.975  1.00 14.56           C  
ANISOU 1084  CG2 VAL A  64     2530   1273   1727    -13    212    190       C  
ATOM   1085  H   VAL A  64      41.845   8.528  15.985  1.00 11.94           H  
ATOM   1086  HA  VAL A  64      41.200   7.201  13.837  1.00 11.95           H  
ATOM   1087  HB  VAL A  64      39.710   7.902  16.121  1.00 14.86           H  
ATOM   1088 HG11 VAL A  64      37.912   6.584  15.417  1.00 16.57           H  
ATOM   1089 HG12 VAL A  64      38.109   7.808  14.422  1.00 16.57           H  
ATOM   1090 HG13 VAL A  64      38.622   6.361  14.013  1.00 16.57           H  
ATOM   1091 HG21 VAL A  64      39.836   5.614  16.602  1.00 17.47           H  
ATOM   1092 HG22 VAL A  64      40.645   5.382  15.254  1.00 17.47           H  
ATOM   1093 HG23 VAL A  64      41.291   6.230  16.432  1.00 17.47           H  
ATOM   1094  N   GLY A  65      40.078  10.198  13.907  1.00  7.88           N  
ANISOU 1094  N   GLY A  65     1072    790   1133    -80     89     37       N  
ATOM   1095  CA  GLY A  65      39.546  11.234  13.031  1.00  8.05           C  
ANISOU 1095  CA  GLY A  65      945    818   1296    -71     60    -48       C  
ATOM   1096  C   GLY A  65      40.428  11.509  11.828  1.00  7.62           C  
ANISOU 1096  C   GLY A  65     1002    804   1091     53      0    -23       C  
ATOM   1097  O   GLY A  65      39.934  11.688  10.713  1.00  8.37           O  
ANISOU 1097  O   GLY A  65     1082    913   1185    105    -45    -28       O  
ATOM   1098  H   GLY A  65      40.294  10.467  14.694  1.00  9.46           H  
ATOM   1099  HA2 GLY A  65      38.671  10.965  12.712  1.00  9.66           H  
ATOM   1100  HA3 GLY A  65      39.449  12.058  13.533  1.00  9.66           H  
ATOM   1101  N   VAL A  66      41.746  11.560  12.038  1.00  7.71           N  
ANISOU 1101  N   VAL A  66      929    892   1110    -29    122    -74       N  
ATOM   1102  CA  VAL A  66      42.670  11.758  10.921  1.00  8.40           C  
ANISOU 1102  CA  VAL A  66     1064    935   1194    -10    108      9       C  
ATOM   1103  C   VAL A  66      42.538  10.636   9.903  1.00  7.66           C  
ANISOU 1103  C   VAL A  66     1104    742   1064   -112     20   -129       C  
ATOM   1104  O   VAL A  66      42.502  10.866   8.693  1.00  8.18           O  
ANISOU 1104  O   VAL A  66     1183    917   1008    -65    -52     -6       O  
ATOM   1105  CB  VAL A  66      44.116  11.890  11.436  1.00  8.75           C  
ANISOU 1105  CB  VAL A  66     1152    938   1234   -115    154   -144       C  
ATOM   1106  CG1 VAL A  66      45.135  11.872  10.274  1.00 10.08           C  
ANISOU 1106  CG1 VAL A  66     1208   1114   1509   -159    191    -97       C  
ATOM   1107  CG2 VAL A  66      44.285  13.160  12.239  1.00  9.26           C  
ANISOU 1107  CG2 VAL A  66     1156   1088   1276   -141    164    -86       C  
ATOM   1108  H   VAL A  66      42.125  11.483  12.806  1.00  9.26           H  
ATOM   1109  HA  VAL A  66      42.441  12.588  10.474  1.00 10.08           H  
ATOM   1110  HB  VAL A  66      44.313  11.140  12.018  1.00 10.50           H  
ATOM   1111 HG11 VAL A  66      46.030  11.957  10.638  1.00 12.10           H  
ATOM   1112 HG12 VAL A  66      45.051  11.033   9.794  1.00 12.10           H  
ATOM   1113 HG13 VAL A  66      44.948  12.614   9.679  1.00 12.10           H  
ATOM   1114 HG21 VAL A  66      45.202  13.216  12.550  1.00 11.12           H  
ATOM   1115 HG22 VAL A  66      44.079  13.920  11.674  1.00 11.12           H  
ATOM   1116 HG23 VAL A  66      43.680  13.136  12.997  1.00 11.12           H  
ATOM   1117  N   THR A  67      42.502   9.399  10.381  1.00  8.04           N  
ANISOU 1117  N   THR A  67     1202    658   1196    -12    103    -64       N  
ATOM   1118  CA  THR A  67      42.406   8.247   9.488  1.00  7.91           C  
ANISOU 1118  CA  THR A  67     1185    638   1183    -58     96    -95       C  
ATOM   1119  C   THR A  67      41.128   8.299   8.648  1.00  7.56           C  
ANISOU 1119  C   THR A  67     1118    650   1106    -67    118      8       C  
ATOM   1120  O   THR A  67      41.164   8.056   7.432  1.00  8.12           O  
ANISOU 1120  O   THR A  67     1137    786   1162    -11     64    -92       O  
ATOM   1121  CB  THR A  67      42.491   6.973  10.338  1.00  8.77           C  
ANISOU 1121  CB  THR A  67     1293    687   1351     54    -85   -143       C  
ATOM   1122  OG1 THR A  67      43.789   6.914  10.952  1.00 10.02           O  
ANISOU 1122  OG1 THR A  67     1323    947   1539     96   -170     45       O  
ATOM   1123  CG2 THR A  67      42.231   5.716   9.533  1.00 10.30           C  
ANISOU 1123  CG2 THR A  67     1573    778   1563     94    -17     23       C  
ATOM   1124  H   THR A  67      42.531   9.197  11.216  1.00  9.65           H  
ATOM   1125  HA  THR A  67      43.163   8.253   8.882  1.00  9.50           H  
ATOM   1126  HB  THR A  67      41.819   7.021  11.035  1.00 10.52           H  
ATOM   1127  HG1 THR A  67      43.853   6.220  11.423  1.00 12.03           H  
ATOM   1128 HG21 THR A  67      42.294   4.937  10.107  1.00 12.36           H  
ATOM   1129 HG22 THR A  67      41.343   5.750   9.144  1.00 12.36           H  
ATOM   1130 HG23 THR A  67      42.885   5.637   8.821  1.00 12.36           H  
ATOM   1131  N   ALA A  68      39.989   8.620   9.270  1.00  7.61           N  
ANISOU 1131  N   ALA A  68     1110    737   1045    -86    127    -57       N  
ATOM   1132  CA  ALA A  68      38.730   8.664   8.530  1.00  8.34           C  
ANISOU 1132  CA  ALA A  68      963    887   1321    -99    -11    -55       C  
ATOM   1133  C   ALA A  68      38.725   9.780   7.494  1.00  7.59           C  
ANISOU 1133  C   ALA A  68      992    798   1095     24     82    -65       C  
ATOM   1134  O   ALA A  68      38.327   9.569   6.344  1.00  7.94           O  
ANISOU 1134  O   ALA A  68     1101    822   1093     64    -12   -111       O  
ATOM   1135  CB  ALA A  68      37.547   8.834   9.482  1.00  9.53           C  
ANISOU 1135  CB  ALA A  68     1072   1100   1450    -28    108    209       C  
ATOM   1136  H   ALA A  68      39.921   8.813  10.105  1.00  9.13           H  
ATOM   1137  HA  ALA A  68      38.614   7.823   8.061  1.00 10.01           H  
ATOM   1138  HB1 ALA A  68      36.727   8.860   8.965  1.00 11.44           H  
ATOM   1139  HB2 ALA A  68      37.527   8.085  10.097  1.00 11.44           H  
ATOM   1140  HB3 ALA A  68      37.655   9.663   9.974  1.00 11.44           H  
ATOM   1141  N   LEU A  69      39.156  10.984   7.882  1.00  7.67           N  
ANISOU 1141  N   LEU A  69     1132    712   1069     34    -45    -48       N  
ATOM   1142  CA  LEU A  69      39.121  12.092   6.931  1.00  8.14           C  
ANISOU 1142  CA  LEU A  69     1197    731   1164     30    -97    -25       C  
ATOM   1143  C   LEU A  69      40.116  11.892   5.796  1.00  7.87           C  
ANISOU 1143  C   LEU A  69     1249    643   1098    -42      9      2       C  
ATOM   1144  O   LEU A  69      39.850  12.316   4.664  1.00  8.43           O  
ANISOU 1144  O   LEU A  69     1390    748   1065      5    -64     -5       O  
ATOM   1145  CB  LEU A  69      39.348  13.430   7.635  1.00  8.31           C  
ANISOU 1145  CB  LEU A  69     1334    753   1069     93    -27    -94       C  
ATOM   1146  CG  LEU A  69      38.247  13.891   8.598  1.00  9.67           C  
ANISOU 1146  CG  LEU A  69     1485    851   1339     84    -78   -179       C  
ATOM   1147  CD1 LEU A  69      38.533  15.323   9.031  1.00  9.94           C  
ANISOU 1147  CD1 LEU A  69     1543    866   1367    290   -212   -240       C  
ATOM   1148  CD2 LEU A  69      36.825  13.746   8.023  1.00 12.01           C  
ANISOU 1148  CD2 LEU A  69     1618   1195   1749    151    -84   -334       C  
ATOM   1149  H   LEU A  69      39.463  11.179   8.662  1.00  9.20           H  
ATOM   1150  HA  LEU A  69      38.236  12.123   6.534  1.00  9.76           H  
ATOM   1151  HB2 LEU A  69      40.169  13.368   8.146  1.00  9.97           H  
ATOM   1152  HB3 LEU A  69      39.443  14.117   6.957  1.00  9.97           H  
ATOM   1153  HG  LEU A  69      38.290  13.338   9.394  1.00 11.61           H  
ATOM   1154 HD11 LEU A  69      37.837  15.613   9.640  1.00 11.92           H  
ATOM   1155 HD12 LEU A  69      39.395  15.351   9.475  1.00 11.92           H  
ATOM   1156 HD13 LEU A  69      38.546  15.893   8.246  1.00 11.92           H  
ATOM   1157 HD21 LEU A  69      36.184  14.055   8.682  1.00 14.41           H  
ATOM   1158 HD22 LEU A  69      36.754  14.281   7.217  1.00 14.41           H  
ATOM   1159 HD23 LEU A  69      36.663  12.812   7.815  1.00 14.41           H  
ATOM   1160  N   THR A  70      41.268  11.262   6.062  1.00  7.93           N  
ANISOU 1160  N   THR A  70     1186    720   1109    -74     20     -8       N  
ATOM   1161  CA  THR A  70      42.227  10.993   4.992  1.00  8.28           C  
ANISOU 1161  CA  THR A  70     1100    916   1133    -96     17     73       C  
ATOM   1162  C   THR A  70      41.659   9.997   3.980  1.00  7.26           C  
ANISOU 1162  C   THR A  70      937    806   1015    -85    -61   -142       C  
ATOM   1163  O   THR A  70      41.805  10.180   2.760  1.00  7.80           O  
ANISOU 1163  O   THR A  70      921    949   1093     67     23    -99       O  
ATOM   1164  CB  THR A  70      43.559  10.528   5.599  1.00  9.16           C  
ANISOU 1164  CB  THR A  70     1133   1363    985   -372    194   -111       C  
ATOM   1165  OG1 THR A  70      44.082  11.579   6.421  1.00 10.41           O  
ANISOU 1165  OG1 THR A  70     1369   1384   1202   -542    -32    -17       O  
ATOM   1166  CG2 THR A  70      44.590  10.205   4.527  1.00 11.44           C  
ANISOU 1166  CG2 THR A  70      985   1957   1403   -282     16    -74       C  
ATOM   1167  H   THR A  70      41.511  10.987   6.839  1.00  9.52           H  
ATOM   1168  HA  THR A  70      42.398  11.822   4.518  1.00  9.94           H  
ATOM   1169  HB  THR A  70      43.413   9.735   6.137  1.00 10.99           H  
ATOM   1170  HG1 THR A  70      43.539  11.758   7.037  1.00 12.49           H  
ATOM   1171 HG21 THR A  70      45.418   9.915   4.940  1.00 13.72           H  
ATOM   1172 HG22 THR A  70      44.259   9.496   3.952  1.00 13.72           H  
ATOM   1173 HG23 THR A  70      44.765  10.992   3.988  1.00 13.72           H  
ATOM   1174  N   ALA A  71      40.998   8.938   4.459  1.00  7.20           N  
ANISOU 1174  N   ALA A  71      977    643   1115    -12      3    -76       N  
ATOM   1175  CA  ALA A  71      40.352   7.997   3.546  1.00  7.32           C  
ANISOU 1175  CA  ALA A  71      884    779   1119    -34    -50   -143       C  
ATOM   1176  C   ALA A  71      39.250   8.677   2.740  1.00  7.22           C  
ANISOU 1176  C   ALA A  71      916    720   1108     19     -9   -137       C  
ATOM   1177  O   ALA A  71      39.113   8.428   1.537  1.00  7.62           O  
ANISOU 1177  O   ALA A  71      898    812   1186     84    -18   -135       O  
ATOM   1178  CB  ALA A  71      39.812   6.792   4.317  1.00  7.80           C  
ANISOU 1178  CB  ALA A  71      946    780   1239    -87     36     -2       C  
ATOM   1179  H   ALA A  71      40.912   8.746   5.293  1.00  8.64           H  
ATOM   1180  HA  ALA A  71      41.016   7.670   2.918  1.00  8.79           H  
ATOM   1181  HB1 ALA A  71      39.388   6.183   3.692  1.00  9.37           H  
ATOM   1182  HB2 ALA A  71      40.549   6.348   4.765  1.00  9.37           H  
ATOM   1183  HB3 ALA A  71      39.164   7.100   4.970  1.00  9.37           H  
ATOM   1184  N   LEU A  72      38.432   9.509   3.390  1.00  7.46           N  
ANISOU 1184  N   LEU A  72      947    804   1084     87    -79    -51       N  
ATOM   1185  CA  LEU A  72      37.386  10.232   2.664  1.00  7.65           C  
ANISOU 1185  CA  LEU A  72      944    929   1033     49    -17    -71       C  
ATOM   1186  C   LEU A  72      37.985  11.184   1.632  1.00  7.52           C  
ANISOU 1186  C   LEU A  72      972    814   1072    189     98    -70       C  
ATOM   1187  O   LEU A  72      37.483  11.281   0.502  1.00  7.88           O  
ANISOU 1187  O   LEU A  72      979    990   1027    160     10    -69       O  
ATOM   1188  CB  LEU A  72      36.470  10.978   3.642  1.00  8.12           C  
ANISOU 1188  CB  LEU A  72      938   1033   1113    168     34      8       C  
ATOM   1189  CG  LEU A  72      35.329  11.769   2.987  1.00  9.31           C  
ANISOU 1189  CG  LEU A  72     1026   1206   1305    310     -7     22       C  
ATOM   1190  CD1 LEU A  72      34.417  10.859   2.165  1.00 10.75           C  
ANISOU 1190  CD1 LEU A  72     1016   1682   1387    278      6    -83       C  
ATOM   1191  CD2 LEU A  72      34.517  12.511   4.047  1.00  9.47           C  
ANISOU 1191  CD2 LEU A  72     1171   1130   1296    369    213      1       C  
ATOM   1192  H   LEU A  72      38.462   9.671   4.234  1.00  8.95           H  
ATOM   1193  HA  LEU A  72      36.841   9.588   2.186  1.00  9.18           H  
ATOM   1194  HB2 LEU A  72      36.070  10.332   4.244  1.00  9.74           H  
ATOM   1195  HB3 LEU A  72      37.007  11.606   4.150  1.00  9.74           H  
ATOM   1196  HG  LEU A  72      35.710  12.429   2.387  1.00 11.17           H  
ATOM   1197 HD11 LEU A  72      33.712  11.394   1.769  1.00 12.90           H  
ATOM   1198 HD12 LEU A  72      34.941  10.433   1.468  1.00 12.90           H  
ATOM   1199 HD13 LEU A  72      34.033  10.186   2.749  1.00 12.90           H  
ATOM   1200 HD21 LEU A  72      33.804  13.002   3.610  1.00 11.36           H  
ATOM   1201 HD22 LEU A  72      34.144  11.866   4.667  1.00 11.36           H  
ATOM   1202 HD23 LEU A  72      35.102  13.125   4.519  1.00 11.36           H  
ATOM   1203  N   GLY A  73      39.047  11.909   1.997  1.00  7.67           N  
ANISOU 1203  N   GLY A  73     1089    726   1097     98    -43    -69       N  
ATOM   1204  CA  GLY A  73      39.695  12.791   1.035  1.00  8.51           C  
ANISOU 1204  CA  GLY A  73     1145    915   1174     84     51     24       C  
ATOM   1205  C   GLY A  73      40.168  12.057  -0.205  1.00  8.02           C  
ANISOU 1205  C   GLY A  73     1064    826   1158     11    -24    -42       C  
ATOM   1206  O   GLY A  73      40.040  12.558  -1.328  1.00  8.24           O  
ANISOU 1206  O   GLY A  73      999    955   1176     -7      2    -82       O  
ATOM   1207  H   GLY A  73      39.402  11.907   2.780  1.00  9.20           H  
ATOM   1208  HA2 GLY A  73      39.072  13.483   0.763  1.00 10.21           H  
ATOM   1209  HA3 GLY A  73      40.462  13.214   1.452  1.00 10.21           H  
ATOM   1210  N   ALA A  74      40.749  10.867  -0.025  1.00  7.78           N  
ANISOU 1210  N   ALA A  74     1007    825   1124     47     24    -55       N  
ATOM   1211  CA  ALA A  74      41.216  10.105  -1.178  1.00  8.33           C  
ANISOU 1211  CA  ALA A  74     1023    956   1187     62     36    -86       C  
ATOM   1212  C   ALA A  74      40.048   9.722  -2.081  1.00  8.26           C  
ANISOU 1212  C   ALA A  74      983   1010   1147    -10     63   -181       C  
ATOM   1213  O   ALA A  74      40.154   9.764  -3.315  1.00  9.29           O  
ANISOU 1213  O   ALA A  74     1138   1187   1203     15     70   -167       O  
ATOM   1214  CB  ALA A  74      41.968   8.858  -0.707  1.00  9.06           C  
ANISOU 1214  CB  ALA A  74      997   1174   1273     30     32   -134       C  
ATOM   1215  H   ALA A  74      40.882  10.490   0.736  1.00  9.34           H  
ATOM   1216  HA  ALA A  74      41.830  10.651  -1.693  1.00 10.00           H  
ATOM   1217  HB1 ALA A  74      42.272   8.361  -1.483  1.00 10.88           H  
ATOM   1218  HB2 ALA A  74      42.728   9.132  -0.171  1.00 10.88           H  
ATOM   1219  HB3 ALA A  74      41.369   8.309  -0.177  1.00 10.88           H  
ATOM   1220  N   ILE A  75      38.917   9.354  -1.479  1.00  8.28           N  
ANISOU 1220  N   ILE A  75      977    943   1227    -22    -14   -164       N  
ATOM   1221  CA  ILE A  75      37.698   9.050  -2.226  1.00  7.99           C  
ANISOU 1221  CA  ILE A  75      997    881   1159    -22    -71   -235       C  
ATOM   1222  C   ILE A  75      37.216  10.277  -3.004  1.00  8.00           C  
ANISOU 1222  C   ILE A  75     1055    804   1180     83   -146   -115       C  
ATOM   1223  O   ILE A  75      36.922  10.191  -4.203  1.00  8.57           O  
ANISOU 1223  O   ILE A  75     1092   1019   1143     -1   -131    -80       O  
ATOM   1224  CB  ILE A  75      36.627   8.476  -1.271  1.00  8.43           C  
ANISOU 1224  CB  ILE A  75     1012    924   1267    -67    -62    -65       C  
ATOM   1225  CG1 ILE A  75      36.998   7.037  -0.864  1.00  9.82           C  
ANISOU 1225  CG1 ILE A  75     1156   1040   1536   -197   -201    -43       C  
ATOM   1226  CG2 ILE A  75      35.229   8.524  -1.902  1.00  9.09           C  
ANISOU 1226  CG2 ILE A  75     1044   1045   1366    -81     24    -26       C  
ATOM   1227  CD1 ILE A  75      36.312   6.545   0.392  1.00 10.99           C  
ANISOU 1227  CD1 ILE A  75     1509   1199   1470   -127   -239     22       C  
ATOM   1228  H   ILE A  75      38.830   9.271  -0.628  1.00  9.94           H  
ATOM   1229  HA  ILE A  75      37.903   8.360  -2.876  1.00  9.59           H  
ATOM   1230  HB  ILE A  75      36.615   9.022  -0.470  1.00 10.11           H  
ATOM   1231 HG12 ILE A  75      36.755   6.438  -1.587  1.00 11.79           H  
ATOM   1232 HG13 ILE A  75      37.956   6.995  -0.713  1.00 11.79           H  
ATOM   1233 HG21 ILE A  75      34.587   8.157  -1.274  1.00 10.91           H  
ATOM   1234 HG22 ILE A  75      35.005   9.447  -2.102  1.00 10.91           H  
ATOM   1235 HG23 ILE A  75      35.233   8.000  -2.717  1.00 10.91           H  
ATOM   1236 HD11 ILE A  75      36.601   5.637   0.574  1.00 13.19           H  
ATOM   1237 HD12 ILE A  75      36.555   7.124   1.132  1.00 13.19           H  
ATOM   1238 HD13 ILE A  75      35.352   6.566   0.256  1.00 13.19           H  
ATOM   1239  N   LEU A  76      37.121  11.434  -2.338  1.00  7.63           N  
ANISOU 1239  N   LEU A  76      867    830   1200     73    -88    -81       N  
ATOM   1240  CA  LEU A  76      36.614  12.631  -3.006  1.00  7.93           C  
ANISOU 1240  CA  LEU A  76      961    887   1166     87    -43     27       C  
ATOM   1241  C   LEU A  76      37.497  13.019  -4.187  1.00  8.56           C  
ANISOU 1241  C   LEU A  76     1062   1021   1169     31    -24    -67       C  
ATOM   1242  O   LEU A  76      36.995  13.440  -5.237  1.00  8.50           O  
ANISOU 1242  O   LEU A  76     1121   1019   1090    127    -15    -79       O  
ATOM   1243  CB  LEU A  76      36.486  13.790  -2.012  1.00  7.80           C  
ANISOU 1243  CB  LEU A  76     1032    876   1055     55    -53    -11       C  
ATOM   1244  CG  LEU A  76      35.464  13.623  -0.874  1.00  8.42           C  
ANISOU 1244  CG  LEU A  76     1063    914   1222    106     46    -10       C  
ATOM   1245  CD1 LEU A  76      35.566  14.765   0.105  1.00  9.76           C  
ANISOU 1245  CD1 LEU A  76     1407   1140   1160    339     30    -19       C  
ATOM   1246  CD2 LEU A  76      34.045  13.473  -1.393  1.00  9.22           C  
ANISOU 1246  CD2 LEU A  76     1097   1168   1237    104    159    -53       C  
ATOM   1247  H   LEU A  76      37.339  11.547  -1.514  1.00  9.15           H  
ATOM   1248  HA  LEU A  76      35.728  12.441  -3.351  1.00  9.52           H  
ATOM   1249  HB2 LEU A  76      37.353  13.931  -1.600  1.00  9.36           H  
ATOM   1250  HB3 LEU A  76      36.235  14.585  -2.507  1.00  9.36           H  
ATOM   1251  HG  LEU A  76      35.680  12.810  -0.391  1.00 10.10           H  
ATOM   1252 HD11 LEU A  76      34.913  14.635   0.810  1.00 11.71           H  
ATOM   1253 HD12 LEU A  76      36.461  14.779   0.481  1.00 11.71           H  
ATOM   1254 HD13 LEU A  76      35.390  15.597  -0.361  1.00 11.71           H  
ATOM   1255 HD21 LEU A  76      33.443  13.371  -0.639  1.00 11.06           H  
ATOM   1256 HD22 LEU A  76      33.809  14.265  -1.901  1.00 11.06           H  
ATOM   1257 HD23 LEU A  76      33.998  12.688  -1.962  1.00 11.06           H  
ATOM   1258  N   LYS A  77      38.818  12.881  -4.034  1.00  8.48           N  
ANISOU 1258  N   LYS A  77     1058   1013   1152    -51     40    -55       N  
ATOM   1259  CA  LYS A  77      39.741  13.241  -5.103  1.00  8.81           C  
ANISOU 1259  CA  LYS A  77     1132   1034   1180    -92    113    -32       C  
ATOM   1260  C   LYS A  77      39.620  12.333  -6.323  1.00  9.41           C  
ANISOU 1260  C   LYS A  77     1231   1221   1123    -57     61    -61       C  
ATOM   1261  O   LYS A  77      40.046  12.734  -7.413  1.00 10.63           O  
ANISOU 1261  O   LYS A  77     1437   1374   1229    -34    215    -57       O  
ATOM   1262  CB  LYS A  77      41.173  13.271  -4.564  1.00  9.52           C  
ANISOU 1262  CB  LYS A  77     1198   1119   1300   -121     72    -55       C  
ATOM   1263  CG  LYS A  77      41.429  14.419  -3.605  1.00  9.89           C  
ANISOU 1263  CG  LYS A  77     1193   1317   1248   -215    131   -197       C  
ATOM   1264  CD  LYS A  77      42.765  14.291  -2.905  1.00 11.25           C  
ANISOU 1264  CD  LYS A  77     1239   1690   1346   -257     77   -274       C  
ATOM   1265  CE  LYS A  77      42.870  15.256  -1.734  1.00 12.28           C  
ANISOU 1265  CE  LYS A  77     1314   1799   1555   -238     22   -319       C  
ATOM   1266  NZ  LYS A  77      44.213  15.219  -1.072  1.00 13.50           N  
ANISOU 1266  NZ  LYS A  77     1240   2143   1745   -243    -67   -536       N  
ATOM   1267  H   LYS A  77      39.199  12.582  -3.323  1.00 10.18           H  
ATOM   1268  HA  LYS A  77      39.527  14.141  -5.395  1.00 10.57           H  
ATOM   1269  HB2 LYS A  77      41.347  12.442  -4.090  1.00 11.42           H  
ATOM   1270  HB3 LYS A  77      41.787  13.361  -5.309  1.00 11.42           H  
ATOM   1271  HG2 LYS A  77      41.426  15.253  -4.099  1.00 11.87           H  
ATOM   1272  HG3 LYS A  77      40.734  14.429  -2.928  1.00 11.87           H  
ATOM   1273  HD2 LYS A  77      42.865  13.387  -2.565  1.00 13.50           H  
ATOM   1274  HD3 LYS A  77      43.477  14.494  -3.532  1.00 13.50           H  
ATOM   1275  HE2 LYS A  77      42.718  16.159  -2.053  1.00 14.74           H  
ATOM   1276  HE3 LYS A  77      42.202  15.021  -1.070  1.00 14.74           H  
ATOM   1277  HZ1 LYS A  77      44.234  15.796  -0.394  1.00 16.20           H  
ATOM   1278  HZ2 LYS A  77      44.377  14.401  -0.761  1.00 16.20           H  
ATOM   1279  HZ3 LYS A  77      44.847  15.438  -1.658  1.00 16.20           H  
ATOM   1280  N   LYS A  78      39.037  11.136  -6.181  1.00  9.18           N  
ANISOU 1280  N   LYS A  78     1257   1094   1136     51    -34    -86       N  
ATOM   1281  CA  LYS A  78      38.727  10.296  -7.336  1.00  9.50           C  
ANISOU 1281  CA  LYS A  78     1325   1142   1144    152    -72   -228       C  
ATOM   1282  C   LYS A  78      37.507  10.771  -8.125  1.00  9.51           C  
ANISOU 1282  C   LYS A  78     1392    923   1298      9     13    -92       C  
ATOM   1283  O   LYS A  78      37.256  10.236  -9.217  1.00 10.38           O  
ANISOU 1283  O   LYS A  78     1489   1207   1248    160     -2   -272       O  
ATOM   1284  CB  LYS A  78      38.513   8.836  -6.910  1.00 10.87           C  
ANISOU 1284  CB  LYS A  78     1603   1163   1363    299    -45   -112       C  
ATOM   1285  CG  LYS A  78      39.743   8.138  -6.352  1.00 13.42           C  
ANISOU 1285  CG  LYS A  78     1959   1272   1869    336   -275   -242       C  
ATOM   1286  CD  LYS A  78      40.938   8.215  -7.259  1.00 19.45           C  
ANISOU 1286  CD  LYS A  78     2196   1998   3196    380   -172   -161       C  
ATOM   1287  CE  LYS A  78      40.719   7.417  -8.495  1.00 24.11           C  
ANISOU 1287  CE  LYS A  78     2621   2507   4033    542    122    -77       C  
ATOM   1288  NZ  LYS A  78      40.669   5.963  -8.173  1.00 27.80           N  
ANISOU 1288  NZ  LYS A  78     3006   2839   4719    732    274   -183       N  
ATOM   1289  H   LYS A  78      38.811  10.792  -5.426  1.00 11.01           H  
ATOM   1290  HA  LYS A  78      39.487  10.314  -7.939  1.00 11.40           H  
ATOM   1291  HB2 LYS A  78      37.828   8.814  -6.223  1.00 13.04           H  
ATOM   1292  HB3 LYS A  78      38.215   8.331  -7.682  1.00 13.04           H  
ATOM   1293  HG2 LYS A  78      39.983   8.552  -5.508  1.00 16.11           H  
ATOM   1294  HG3 LYS A  78      39.535   7.201  -6.212  1.00 16.11           H  
ATOM   1295  HD2 LYS A  78      41.090   9.138  -7.514  1.00 23.34           H  
ATOM   1296  HD3 LYS A  78      41.715   7.859  -6.800  1.00 23.34           H  
ATOM   1297  HE2 LYS A  78      39.874   7.672  -8.899  1.00 28.93           H  
ATOM   1298  HE3 LYS A  78      41.451   7.571  -9.113  1.00 28.93           H  
ATOM   1299  HZ1 LYS A  78      40.538   5.492  -8.916  1.00 33.36           H  
ATOM   1300  HZ2 LYS A  78      41.436   5.708  -7.800  1.00 33.36           H  
ATOM   1301  HZ3 LYS A  78      40.004   5.800  -7.605  1.00 33.36           H  
ATOM   1302  N   LYS A  79      36.751  11.746  -7.616  1.00  9.36           N  
ANISOU 1302  N   LYS A  79     1285   1071   1201     49    -59   -100       N  
ATOM   1303  CA  LYS A  79      35.642  12.350  -8.364  1.00  9.66           C  
ANISOU 1303  CA  LYS A  79     1386   1071   1215    118     -1    -69       C  
ATOM   1304  C   LYS A  79      34.679  11.290  -8.906  1.00  9.92           C  
ANISOU 1304  C   LYS A  79     1435   1170   1163    175   -209   -161       C  
ATOM   1305  O   LYS A  79      34.263  11.317 -10.069  1.00 10.81           O  
ANISOU 1305  O   LYS A  79     1664   1227   1214    214   -110   -190       O  
ATOM   1306  CB  LYS A  79      36.156  13.307  -9.449  1.00 10.31           C  
ANISOU 1306  CB  LYS A  79     1500   1128   1288    116    -77   -148       C  
ATOM   1307  CG  LYS A  79      37.035  14.427  -8.909  1.00 11.58           C  
ANISOU 1307  CG  LYS A  79     1640   1219   1541    -63    149     55       C  
ATOM   1308  CD  LYS A  79      37.282  15.523  -9.948  1.00 16.20           C  
ANISOU 1308  CD  LYS A  79     1987   1771   2399    -62    154   -162       C  
ATOM   1309  CE  LYS A  79      38.038  15.075 -11.165  1.00 20.78           C  
ANISOU 1309  CE  LYS A  79     2379   2292   3224    284    430    345       C  
ATOM   1310  NZ  LYS A  79      38.453  16.315 -11.917  1.00 21.93           N  
ANISOU 1310  NZ  LYS A  79     2701   2494   3136    536    843   1007       N  
ATOM   1311  H   LYS A  79      36.860  12.079  -6.830  1.00 11.23           H  
ATOM   1312  HA  LYS A  79      35.132  12.891  -7.741  1.00 11.60           H  
ATOM   1313  HB2 LYS A  79      36.680  12.801 -10.090  1.00 12.37           H  
ATOM   1314  HB3 LYS A  79      35.396  13.714  -9.893  1.00 12.37           H  
ATOM   1315  HG2 LYS A  79      36.599  14.831  -8.142  1.00 13.90           H  
ATOM   1316  HG3 LYS A  79      37.894  14.059  -8.649  1.00 13.90           H  
ATOM   1317  HD2 LYS A  79      36.426  15.867 -10.245  1.00 19.44           H  
ATOM   1318  HD3 LYS A  79      37.793  16.235  -9.531  1.00 19.44           H  
ATOM   1319  HE2 LYS A  79      38.832  14.584 -10.902  1.00 24.93           H  
ATOM   1320  HE3 LYS A  79      37.466  14.537 -11.733  1.00 24.93           H  
ATOM   1321  HZ1 LYS A  79      38.906  16.089 -12.649  1.00 26.31           H  
ATOM   1322  HZ2 LYS A  79      37.733  16.781 -12.155  1.00 26.31           H  
ATOM   1323  HZ3 LYS A  79      38.970  16.824 -11.402  1.00 26.31           H  
ATOM   1324  N   GLY A  80      34.312  10.340  -8.042  1.00 10.02           N  
ANISOU 1324  N   GLY A  80     1494   1050   1262    137   -144    -45       N  
ATOM   1325  CA  GLY A  80      33.354   9.314  -8.373  1.00 10.69           C  
ANISOU 1325  CA  GLY A  80     1480   1249   1333     31   -217   -150       C  
ATOM   1326  C   GLY A  80      33.959   8.003  -8.835  1.00 10.21           C  
ANISOU 1326  C   GLY A  80     1502   1071   1307    -47   -258   -153       C  
ATOM   1327  O   GLY A  80      33.262   6.975  -8.819  1.00 11.92           O  
ANISOU 1327  O   GLY A  80     1594   1315   1618    -37   -180   -204       O  
ATOM   1328  H   GLY A  80      34.619  10.277  -7.241  1.00 12.02           H  
ATOM   1329  HA2 GLY A  80      32.806   9.132  -7.594  1.00 12.83           H  
ATOM   1330  HA3 GLY A  80      32.774   9.641  -9.078  1.00 12.83           H  
ATOM   1331  N   HIS A  81      35.233   8.002  -9.234  1.00 10.21           N  
ANISOU 1331  N   HIS A  81     1595   1006   1276      3    -48   -145       N  
ATOM   1332  CA  HIS A  81      35.906   6.791  -9.713  1.00 10.47           C  
ANISOU 1332  CA  HIS A  81     1626   1111   1242     87     47   -120       C  
ATOM   1333  C   HIS A  81      36.588   6.091  -8.539  1.00 10.57           C  
ANISOU 1333  C   HIS A  81     1544   1158   1314     86      4   -132       C  
ATOM   1334  O   HIS A  81      37.799   5.908  -8.523  1.00 11.83           O  
ANISOU 1334  O   HIS A  81     1567   1596   1331    194     12    -80       O  
ATOM   1335  CB  HIS A  81      36.941   7.152 -10.776  1.00 12.18           C  
ANISOU 1335  CB  HIS A  81     1920   1278   1431    247     58    -95       C  
ATOM   1336  CG  HIS A  81      36.373   7.815 -11.985  1.00 13.40           C  
ANISOU 1336  CG  HIS A  81     2343   1490   1259     83    -33   -114       C  
ATOM   1337  ND1 HIS A  81      35.814   7.102 -13.022  1.00 15.98           N  
ANISOU 1337  ND1 HIS A  81     2750   1866   1455     88   -219     20       N  
ATOM   1338  CD2 HIS A  81      36.287   9.121 -12.336  1.00 14.86           C  
ANISOU 1338  CD2 HIS A  81     2514   1557   1575    105      7     68       C  
ATOM   1339  CE1 HIS A  81      35.414   7.941 -13.962  1.00 16.78           C  
ANISOU 1339  CE1 HIS A  81     2871   2012   1493    264   -117    324       C  
ATOM   1340  NE2 HIS A  81      35.682   9.172 -13.567  1.00 16.60           N  
ANISOU 1340  NE2 HIS A  81     2757   1886   1665    258     90    391       N  
ATOM   1341  H   HIS A  81      35.736   8.700  -9.236  1.00 12.25           H  
ATOM   1342  HA  HIS A  81      35.255   6.185 -10.102  1.00 12.57           H  
ATOM   1343  HB2 HIS A  81      37.590   7.757 -10.385  1.00 14.62           H  
ATOM   1344  HB3 HIS A  81      37.384   6.339 -11.067  1.00 14.62           H  
ATOM   1345  HD2 HIS A  81      36.582   9.848 -11.836  1.00 17.83           H  
ATOM   1346  HE1 HIS A  81      34.999   7.704 -14.759  1.00 20.14           H  
ATOM   1347  HE2 HIS A  81      35.509   9.888 -14.010  1.00 19.92           H  
ATOM   1348  N   HIS A  82      35.787   5.677  -7.556  1.00 10.49           N  
ANISOU 1348  N   HIS A  82     1444   1186   1358    114    -90   -111       N  
ATOM   1349  CA  HIS A  82      36.288   5.269  -6.244  1.00  9.63           C  
ANISOU 1349  CA  HIS A  82     1438   1126   1093    119   -149      1       C  
ATOM   1350  C   HIS A  82      36.019   3.798  -5.928  1.00 11.06           C  
ANISOU 1350  C   HIS A  82     1596   1075   1529    160   -164   -114       C  
ATOM   1351  O   HIS A  82      36.065   3.396  -4.759  1.00 11.15           O  
ANISOU 1351  O   HIS A  82     1564   1166   1508    250    -65     32       O  
ATOM   1352  CB  HIS A  82      35.699   6.180  -5.161  1.00 10.31           C  
ANISOU 1352  CB  HIS A  82     1420   1205   1292    135   -155   -122       C  
ATOM   1353  CG  HIS A  82      34.211   6.299  -5.213  1.00  9.84           C  
ANISOU 1353  CG  HIS A  82     1333   1156   1249    114   -114    -99       C  
ATOM   1354  ND1 HIS A  82      33.553   7.495  -5.016  1.00 11.10           N  
ANISOU 1354  ND1 HIS A  82     1457   1064   1699     84   -176   -151       N  
ATOM   1355  CD2 HIS A  82      33.252   5.372  -5.447  1.00 11.05           C  
ANISOU 1355  CD2 HIS A  82     1460   1225   1513    145    -12    -94       C  
ATOM   1356  CE1 HIS A  82      32.251   7.294  -5.117  1.00 10.27           C  
ANISOU 1356  CE1 HIS A  82     1330   1075   1496    -27    -91    -71       C  
ATOM   1357  NE2 HIS A  82      32.040   6.014  -5.381  1.00 10.40           N  
ANISOU 1357  NE2 HIS A  82     1442   1156   1355    -93   -171    -35       N  
ATOM   1358  H   HIS A  82      34.932   5.623  -7.628  1.00 12.59           H  
ATOM   1359  HA  HIS A  82      37.250   5.394  -6.234  1.00 11.55           H  
ATOM   1360  HB2 HIS A  82      35.938   5.825  -4.291  1.00 12.37           H  
ATOM   1361  HB3 HIS A  82      36.071   7.070  -5.266  1.00 12.37           H  
ATOM   1362  HD2 HIS A  82      33.389   4.468  -5.616  1.00 13.26           H  
ATOM   1363  HE1 HIS A  82      31.593   7.945  -5.025  1.00 12.32           H  
ATOM   1364  HE2 HIS A  82      31.271   5.646  -5.493  1.00 12.48           H  
ATOM   1365  N   GLU A  83      35.811   2.974  -6.943  1.00 12.42           N  
ANISOU 1365  N   GLU A  83     1904   1241   1575     55   -307   -303       N  
ATOM   1366  CA  GLU A  83      35.500   1.568  -6.707  1.00 14.71           C  
ANISOU 1366  CA  GLU A  83     2290   1259   2039    -22   -286   -411       C  
ATOM   1367  C   GLU A  83      36.591   0.884  -5.877  1.00 12.94           C  
ANISOU 1367  C   GLU A  83     1987   1094   1835     33     77   -198       C  
ATOM   1368  O   GLU A  83      36.291   0.155  -4.922  1.00 13.45           O  
ANISOU 1368  O   GLU A  83     1845   1242   2022     24     60    -36       O  
ATOM   1369  CB AGLU A  83      35.295   0.887  -8.066  0.47 17.10           C  
ANISOU 1369  CB AGLU A  83     2622   1492   2384     25   -281   -337       C  
ATOM   1370  CB BGLU A  83      35.289   0.817  -8.027  0.53 18.01           C  
ANISOU 1370  CB BGLU A  83     2836   1362   2643    105   -407   -679       C  
ATOM   1371  CG AGLU A  83      34.160   1.509  -8.956  0.47 19.56           C  
ANISOU 1371  CG AGLU A  83     2851   1792   2791     74   -151   -161       C  
ATOM   1372  CG BGLU A  83      35.249  -0.727  -7.903  0.53 21.60           C  
ANISOU 1372  CG BGLU A  83     3257   1604   3346    277   -353   -726       C  
ATOM   1373  CD AGLU A  83      34.416   2.969  -9.427  0.47 20.44           C  
ANISOU 1373  CD AGLU A  83     3051   1862   2853    151   -141     66       C  
ATOM   1374  CD BGLU A  83      33.978  -1.258  -7.246  0.53 24.71           C  
ANISOU 1374  CD BGLU A  83     3618   1868   3901    565   -271   -520       C  
ATOM   1375  OE1AGLU A  83      35.550   3.299  -9.853  0.47 17.88           O  
ANISOU 1375  OE1AGLU A  83     3094   1611   2087    187   -203     96       O  
ATOM   1376  OE1BGLU A  83      33.096  -0.450  -6.906  0.53 26.09           O  
ANISOU 1376  OE1BGLU A  83     3755   2094   4062    608   -297   -436       O  
ATOM   1377  OE2AGLU A  83      33.486   3.807  -9.344  0.47 21.65           O  
ANISOU 1377  OE2AGLU A  83     3170   1842   3215    -39    -60    282       O  
ATOM   1378  OE2BGLU A  83      33.856  -2.493  -7.074  0.53 25.84           O  
ANISOU 1378  OE2BGLU A  83     3867   1872   4077    766   -233   -599       O  
ATOM   1379  H   GLU A  83      35.842   3.198  -7.773  1.00 14.91           H  
ATOM   1380  HA  GLU A  83      34.673   1.515  -6.203  1.00 17.65           H  
ATOM   1381  HB2AGLU A  83      36.124   0.943  -8.568  0.47 20.52           H  
ATOM   1382  HB2BGLU A  83      34.446   1.102  -8.413  0.53 21.61           H  
ATOM   1383  HB3AGLU A  83      35.070  -0.045  -7.914  0.47 20.52           H  
ATOM   1384  HB3BGLU A  83      36.015   1.043  -8.629  0.53 21.61           H  
ATOM   1385  HG2AGLU A  83      34.054   0.961  -9.748  0.47 23.47           H  
ATOM   1386  HG2BGLU A  83      35.308  -1.114  -8.791  0.53 25.92           H  
ATOM   1387  HG3AGLU A  83      33.334   1.507  -8.447  0.47 23.47           H  
ATOM   1388  HG3BGLU A  83      36.003  -1.018  -7.367  0.53 25.92           H  
ATOM   1389  N   ALA A  84      37.863   1.104  -6.223  1.00 13.26           N  
ANISOU 1389  N   ALA A  84     1977   1244   1818    301    163    -69       N  
ATOM   1390  CA  ALA A  84      38.939   0.409  -5.520  1.00 13.18           C  
ANISOU 1390  CA  ALA A  84     1913   1417   1680    368    313     28       C  
ATOM   1391  C   ALA A  84      39.003   0.830  -4.058  1.00 12.22           C  
ANISOU 1391  C   ALA A  84     1872   1215   1555    378    137     45       C  
ATOM   1392  O   ALA A  84      39.210  -0.007  -3.168  1.00 13.84           O  
ANISOU 1392  O   ALA A  84     2125   1262   1871    534    232    106       O  
ATOM   1393  CB  ALA A  84      40.281   0.655  -6.217  1.00 15.16           C  
ANISOU 1393  CB  ALA A  84     2004   1832   1925    306    385    -26       C  
ATOM   1394  H   ALA A  84      38.122   1.637  -6.846  1.00 15.91           H  
ATOM   1395  HA  ALA A  84      38.763  -0.544  -5.546  1.00 15.82           H  
ATOM   1396  HB1 ALA A  84      40.978   0.185  -5.733  1.00 18.19           H  
ATOM   1397  HB2 ALA A  84      40.228   0.324  -7.127  1.00 18.19           H  
ATOM   1398  HB3 ALA A  84      40.464   1.607  -6.221  1.00 18.19           H  
ATOM   1399  N   GLU A  85      38.797   2.122  -3.792  1.00 11.26           N  
ANISOU 1399  N   GLU A  85     1619    982   1679    259    -74     60       N  
ATOM   1400  CA  GLU A  85      38.888   2.648  -2.432  1.00 11.09           C  
ANISOU 1400  CA  GLU A  85     1542   1067   1603    187   -318   -125       C  
ATOM   1401  C   GLU A  85      37.739   2.153  -1.561  1.00 10.92           C  
ANISOU 1401  C   GLU A  85     1566    992   1593    230   -222   -159       C  
ATOM   1402  O   GLU A  85      37.914   1.954  -0.350  1.00 11.02           O  
ANISOU 1402  O   GLU A  85     1603   1087   1498    174   -233   -161       O  
ATOM   1403  CB  GLU A  85      38.888   4.180  -2.477  1.00 11.94           C  
ANISOU 1403  CB  GLU A  85     1526   1130   1883    191   -182   -140       C  
ATOM   1404  CG  GLU A  85      40.164   4.812  -3.051  1.00 13.50           C  
ANISOU 1404  CG  GLU A  85     1596   1198   2336     95   -110     -5       C  
ATOM   1405  CD  GLU A  85      40.287   4.759  -4.575  1.00 13.93           C  
ANISOU 1405  CD  GLU A  85     1543   1341   2408    -44    177     84       C  
ATOM   1406  OE1 GLU A  85      39.309   4.435  -5.286  1.00 13.51           O  
ANISOU 1406  OE1 GLU A  85     1619   1396   2118    155     98    269       O  
ATOM   1407  OE2 GLU A  85      41.389   5.084  -5.076  1.00 16.54           O  
ANISOU 1407  OE2 GLU A  85     1624   1714   2945    -86     41   -194       O  
ATOM   1408  H   GLU A  85      38.602   2.714  -4.384  1.00 13.52           H  
ATOM   1409  HA  GLU A  85      39.721   2.356  -2.031  1.00 13.30           H  
ATOM   1410  HB2 GLU A  85      38.144   4.472  -3.027  1.00 14.33           H  
ATOM   1411  HB3 GLU A  85      38.776   4.515  -1.574  1.00 14.33           H  
ATOM   1412  HG2 GLU A  85      40.191   5.745  -2.788  1.00 16.20           H  
ATOM   1413  HG3 GLU A  85      40.931   4.347  -2.680  1.00 16.20           H  
ATOM   1414  N   LEU A  86      36.562   1.941  -2.149  1.00 10.21           N  
ANISOU 1414  N   LEU A  86     1469    997   1414    278   -137    -49       N  
ATOM   1415  CA  LEU A  86      35.413   1.523  -1.354  1.00 10.43           C  
ANISOU 1415  CA  LEU A  86     1497   1303   1162    255    -60    -70       C  
ATOM   1416  C   LEU A  86      35.480   0.061  -0.932  1.00 10.61           C  
ANISOU 1416  C   LEU A  86     1404   1351   1275    277   -143    -82       C  
ATOM   1417  O   LEU A  86      34.827  -0.303   0.051  1.00 11.89           O  
ANISOU 1417  O   LEU A  86     1634   1549   1335    404     76    110       O  
ATOM   1418  CB  LEU A  86      34.089   1.784  -2.091  1.00 12.04           C  
ANISOU 1418  CB  LEU A  86     1611   1475   1490    257   -149   -140       C  
ATOM   1419  CG  LEU A  86      33.685   3.229  -2.357  1.00 14.77           C  
ANISOU 1419  CG  LEU A  86     1774   1642   2196    356   -399   -352       C  
ATOM   1420  CD1 LEU A  86      32.201   3.284  -2.726  1.00 15.23           C  
ANISOU 1420  CD1 LEU A  86     1551   1878   2359    221   -464    196       C  
ATOM   1421  CD2 LEU A  86      33.974   4.155  -1.204  1.00 17.67           C  
ANISOU 1421  CD2 LEU A  86     2177   1948   2587    892   -459   -572       C  
ATOM   1422  H   LEU A  86      36.406   2.030  -2.990  1.00 12.25           H  
ATOM   1423  HA  LEU A  86      35.398   2.054  -0.542  1.00 12.51           H  
ATOM   1424  HB2 LEU A  86      34.137   1.342  -2.953  1.00 14.45           H  
ATOM   1425  HB3 LEU A  86      33.375   1.383  -1.570  1.00 14.45           H  
ATOM   1426  HG  LEU A  86      34.186   3.551  -3.121  1.00 17.72           H  
ATOM   1427 HD11 LEU A  86      31.952   4.206  -2.893  1.00 18.28           H  
ATOM   1428 HD12 LEU A  86      32.054   2.751  -3.523  1.00 18.28           H  
ATOM   1429 HD13 LEU A  86      31.679   2.928  -1.989  1.00 18.28           H  
ATOM   1430 HD21 LEU A  86      33.693   5.052  -1.442  1.00 21.20           H  
ATOM   1431 HD22 LEU A  86      33.485   3.850  -0.424  1.00 21.20           H  
ATOM   1432 HD23 LEU A  86      34.927   4.143  -1.022  1.00 21.20           H  
ATOM   1433  N   LYS A  87      36.224  -0.791  -1.646  1.00 10.10           N  
ANISOU 1433  N   LYS A  87     1380   1087   1369     30    113   -132       N  
ATOM   1434  CA  LYS A  87      36.230  -2.213  -1.301  1.00 11.13           C  
ANISOU 1434  CA  LYS A  87     1558   1009   1663    -11     96   -154       C  
ATOM   1435  C   LYS A  87      36.713  -2.485   0.116  1.00 10.40           C  
ANISOU 1435  C   LYS A  87     1512   1009   1430    -16    161    -78       C  
ATOM   1436  O   LYS A  87      35.969  -3.119   0.893  1.00 11.00           O  
ANISOU 1436  O   LYS A  87     1555    982   1642     64    170   -100       O  
ATOM   1437  CB  LYS A  87      37.011  -3.019  -2.342  1.00 12.87           C  
ANISOU 1437  CB  LYS A  87     2049   1284   1558   -112    225   -243       C  
ATOM   1438  CG  LYS A  87      36.276  -3.209  -3.647  1.00 14.49           C  
ANISOU 1438  CG  LYS A  87     2561   1313   1632   -127    203   -170       C  
ATOM   1439  CD  LYS A  87      37.088  -4.054  -4.599  1.00 17.39           C  
ANISOU 1439  CD  LYS A  87     3080   1672   1858     50    138   -235       C  
ATOM   1440  CE  LYS A  87      36.426  -4.155  -5.960  1.00 20.30           C  
ANISOU 1440  CE  LYS A  87     3583   1808   2323    124    469     70       C  
ATOM   1441  NZ  LYS A  87      37.163  -5.100  -6.832  1.00 21.36           N  
ANISOU 1441  NZ  LYS A  87     3828   1715   2571     66    659     38       N  
ATOM   1442  H   LYS A  87      36.720  -0.577  -2.315  1.00 12.12           H  
ATOM   1443  HA  LYS A  87      35.313  -2.526  -1.342  1.00 13.36           H  
ATOM   1444  HB2 LYS A  87      37.842  -2.556  -2.535  1.00 15.45           H  
ATOM   1445  HB3 LYS A  87      37.202  -3.897  -1.978  1.00 15.45           H  
ATOM   1446  HG2 LYS A  87      35.433  -3.660  -3.479  1.00 17.39           H  
ATOM   1447  HG3 LYS A  87      36.121  -2.345  -4.059  1.00 17.39           H  
ATOM   1448  HD2 LYS A  87      37.963  -3.652  -4.717  1.00 20.87           H  
ATOM   1449  HD3 LYS A  87      37.176  -4.949  -4.237  1.00 20.87           H  
ATOM   1450  HE2 LYS A  87      35.518  -4.480  -5.854  1.00 24.37           H  
ATOM   1451  HE3 LYS A  87      36.426  -3.283  -6.385  1.00 24.37           H  
ATOM   1452  HZ1 LYS A  87      36.766  -5.152  -7.627  1.00 25.63           H  
ATOM   1453  HZ2 LYS A  87      38.000  -4.820  -6.944  1.00 25.63           H  
ATOM   1454  HZ3 LYS A  87      37.175  -5.909  -6.461  1.00 25.63           H  
ATOM   1455  N   PRO A  88      37.928  -2.077   0.520  1.00 10.21           N  
ANISOU 1455  N   PRO A  88     1356    971   1552    -13    131   -101       N  
ATOM   1456  CA  PRO A  88      38.365  -2.405   1.884  1.00 10.74           C  
ANISOU 1456  CA  PRO A  88     1451    990   1641    137      0    -89       C  
ATOM   1457  C   PRO A  88      37.528  -1.702   2.931  1.00  9.36           C  
ANISOU 1457  C   PRO A  88     1258    901   1398     43     55      7       C  
ATOM   1458  O   PRO A  88      37.284  -2.256   4.010  1.00  9.78           O  
ANISOU 1458  O   PRO A  88     1229    862   1625     93     -9     -2       O  
ATOM   1459  CB  PRO A  88      39.830  -1.942   1.913  1.00 11.81           C  
ANISOU 1459  CB  PRO A  88     1509   1231   1748     82     90     43       C  
ATOM   1460  CG  PRO A  88      39.935  -0.911   0.825  1.00 11.79           C  
ANISOU 1460  CG  PRO A  88     1480   1145   1856    -50    -51     -8       C  
ATOM   1461  CD  PRO A  88      39.017  -1.433  -0.249  1.00 10.96           C  
ANISOU 1461  CD  PRO A  88     1475   1071   1619     17    113    -11       C  
ATOM   1462  HA  PRO A  88      38.327  -3.363   2.031  1.00 12.89           H  
ATOM   1463  HB2 PRO A  88      40.033  -1.551   2.777  1.00 14.17           H  
ATOM   1464  HB3 PRO A  88      40.415  -2.694   1.730  1.00 14.17           H  
ATOM   1465  HG2 PRO A  88      39.631  -0.050   1.154  1.00 14.15           H  
ATOM   1466  HG3 PRO A  88      40.850  -0.858   0.506  1.00 14.15           H  
ATOM   1467  HD2 PRO A  88      38.669  -0.702  -0.782  1.00 13.16           H  
ATOM   1468  HD3 PRO A  88      39.477  -2.088  -0.798  1.00 13.16           H  
ATOM   1469  N   LEU A  89      37.066  -0.487   2.628  1.00  9.32           N  
ANISOU 1469  N   LEU A  89     1279    761   1500     82    -13    -91       N  
ATOM   1470  CA  LEU A  89      36.287   0.290   3.582  1.00  9.20           C  
ANISOU 1470  CA  LEU A  89     1302    756   1439    -32   -141   -133       C  
ATOM   1471  C   LEU A  89      34.918  -0.344   3.821  1.00  8.69           C  
ANISOU 1471  C   LEU A  89     1343    692   1268    115     59   -182       C  
ATOM   1472  O   LEU A  89      34.462  -0.474   4.968  1.00  9.06           O  
ANISOU 1472  O   LEU A  89     1352    696   1395    144     -8   -181       O  
ATOM   1473  CB  LEU A  89      36.121   1.708   3.044  1.00 10.01           C  
ANISOU 1473  CB  LEU A  89     1503    786   1516     32   -105    -95       C  
ATOM   1474  CG  LEU A  89      35.467   2.699   3.978  1.00 12.10           C  
ANISOU 1474  CG  LEU A  89     1990    996   1612     86   -107     25       C  
ATOM   1475  CD1 LEU A  89      36.383   2.977   5.158  1.00 14.19           C  
ANISOU 1475  CD1 LEU A  89     2462   1256   1675    300   -234   -124       C  
ATOM   1476  CD2 LEU A  89      35.159   3.991   3.234  1.00 14.10           C  
ANISOU 1476  CD2 LEU A  89     2134   1068   2155    200    -95   -102       C  
ATOM   1477  H   LEU A  89      37.193  -0.093   1.874  1.00 11.18           H  
ATOM   1478  HA  LEU A  89      36.759   0.333   4.428  1.00 11.04           H  
ATOM   1479  HB2 LEU A  89      36.999   2.055   2.823  1.00 12.02           H  
ATOM   1480  HB3 LEU A  89      35.579   1.668   2.240  1.00 12.02           H  
ATOM   1481  HG  LEU A  89      34.635   2.330   4.313  1.00 14.52           H  
ATOM   1482 HD11 LEU A  89      35.951   3.614   5.749  1.00 17.03           H  
ATOM   1483 HD12 LEU A  89      36.549   2.146   5.630  1.00 17.03           H  
ATOM   1484 HD13 LEU A  89      37.218   3.343   4.829  1.00 17.03           H  
ATOM   1485 HD21 LEU A  89      34.740   4.616   3.847  1.00 16.92           H  
ATOM   1486 HD22 LEU A  89      35.987   4.365   2.895  1.00 16.92           H  
ATOM   1487 HD23 LEU A  89      34.558   3.796   2.498  1.00 16.92           H  
ATOM   1488  N   ALA A  90      34.231  -0.726   2.746  1.00  8.67           N  
ANISOU 1488  N   ALA A  90     1312    717   1265     23    -30   -118       N  
ATOM   1489  CA  ALA A  90      32.953  -1.411   2.899  1.00  9.67           C  
ANISOU 1489  CA  ALA A  90     1268    830   1575    -40    -43    -32       C  
ATOM   1490  C   ALA A  90      33.118  -2.732   3.640  1.00  9.10           C  
ANISOU 1490  C   ALA A  90     1197    744   1518    -92      9   -166       C  
ATOM   1491  O   ALA A  90      32.315  -3.073   4.513  1.00 10.04           O  
ANISOU 1491  O   ALA A  90     1208    877   1730    -91     71    -73       O  
ATOM   1492  CB  ALA A  90      32.328  -1.669   1.538  1.00 10.67           C  
ANISOU 1492  CB  ALA A  90     1329    911   1814     -8   -132    145       C  
ATOM   1493  H   ALA A  90      34.479  -0.603   1.932  1.00 10.40           H  
ATOM   1494  HA  ALA A  90      32.348  -0.849   3.409  1.00 11.60           H  
ATOM   1495  HB1 ALA A  90      31.480  -2.124   1.662  1.00 12.80           H  
ATOM   1496  HB2 ALA A  90      32.186  -0.820   1.090  1.00 12.80           H  
ATOM   1497  HB3 ALA A  90      32.929  -2.223   1.016  1.00 12.80           H  
ATOM   1498  N   GLN A  91      34.158  -3.500   3.321  1.00  8.97           N  
ANISOU 1498  N   GLN A  91     1269    608   1532    -14     38    -52       N  
ATOM   1499  CA  GLN A  91      34.329  -4.776   4.003  1.00  9.08           C  
ANISOU 1499  CA  GLN A  91     1240    611   1599    -83    -33   -184       C  
ATOM   1500  C   GLN A  91      34.535  -4.589   5.504  1.00  8.60           C  
ANISOU 1500  C   GLN A  91     1264    600   1403    -85    -31   -110       C  
ATOM   1501  O   GLN A  91      33.919  -5.297   6.309  1.00  9.86           O  
ANISOU 1501  O   GLN A  91     1442    673   1630   -193     69      4       O  
ATOM   1502  CB  GLN A  91      35.465  -5.597   3.396  1.00  9.57           C  
ANISOU 1502  CB  GLN A  91     1303    635   1698    -93    -50   -108       C  
ATOM   1503  CG  GLN A  91      35.572  -6.975   4.070  1.00  9.78           C  
ANISOU 1503  CG  GLN A  91     1378    675   1663      7    116    -24       C  
ATOM   1504  CD  GLN A  91      36.592  -7.899   3.451  1.00  9.71           C  
ANISOU 1504  CD  GLN A  91     1279    684   1725   -116     11    -57       C  
ATOM   1505  OE1 GLN A  91      37.739  -7.515   3.207  1.00 12.35           O  
ANISOU 1505  OE1 GLN A  91     1363    901   2429   -171     74    -63       O  
ATOM   1506  NE2 GLN A  91      36.185  -9.143   3.234  1.00  9.56           N  
ANISOU 1506  NE2 GLN A  91     1220    750   1661    -18   -181   -114       N  
ATOM   1507  H   GLN A  91      34.758  -3.312   2.734  1.00 10.77           H  
ATOM   1508  HA  GLN A  91      33.513  -5.289   3.889  1.00 10.90           H  
ATOM   1509  HB2 GLN A  91      35.294  -5.732   2.450  1.00 11.48           H  
ATOM   1510  HB3 GLN A  91      36.304  -5.128   3.523  1.00 11.48           H  
ATOM   1511  HG2 GLN A  91      35.818  -6.847   4.999  1.00 11.74           H  
ATOM   1512  HG3 GLN A  91      34.709  -7.413   4.018  1.00 11.74           H  
ATOM   1513 HE21 GLN A  91      35.385  -9.376   3.444  1.00 11.47           H  
ATOM   1514 HE22 GLN A  91      36.722  -9.716   2.883  1.00 11.47           H  
ATOM   1515  N   SER A  92      35.412  -3.666   5.913  1.00  8.65           N  
ANISOU 1515  N   SER A  92     1199    611   1478     -3     45   -150       N  
ATOM   1516  CA  SER A  92      35.645  -3.525   7.347  1.00  8.77           C  
ANISOU 1516  CA  SER A  92     1207    764   1362    -20   -175   -108       C  
ATOM   1517  C   SER A  92      34.414  -2.953   8.050  1.00  9.44           C  
ANISOU 1517  C   SER A  92     1330    699   1557     -5    -71    -80       C  
ATOM   1518  O   SER A  92      34.071  -3.379   9.162  1.00  9.95           O  
ANISOU 1518  O   SER A  92     1403    892   1486    -29    -68    -28       O  
ATOM   1519  CB  SER A  92      36.862  -2.656   7.617  1.00 10.18           C  
ANISOU 1519  CB  SER A  92     1258    906   1705     90    -53   -238       C  
ATOM   1520  OG  SER A  92      36.625  -1.344   7.173  1.00  9.81           O  
ANISOU 1520  OG  SER A  92     1286    812   1628      0    -82   -120       O  
ATOM   1521  H   SER A  92      35.862  -3.135   5.407  1.00 10.39           H  
ATOM   1522  HA  SER A  92      35.819  -4.403   7.722  1.00 10.53           H  
ATOM   1523  HB2 SER A  92      37.038  -2.642   8.571  1.00 12.22           H  
ATOM   1524  HB3 SER A  92      37.625  -3.020   7.141  1.00 12.22           H  
ATOM   1525  HG  SER A  92      37.298  -0.864   7.322  1.00 11.77           H  
ATOM   1526  N   HIS A  93      33.758  -1.955   7.441  1.00  9.13           N  
ANISOU 1526  N   HIS A  93     1296    739   1434     -4     18   -105       N  
ATOM   1527  CA  HIS A  93      32.647  -1.294   8.123  1.00  9.32           C  
ANISOU 1527  CA  HIS A  93     1287    599   1654    -23    -28   -193       C  
ATOM   1528  C   HIS A  93      31.397  -2.172   8.164  1.00 10.02           C  
ANISOU 1528  C   HIS A  93     1336    691   1782    -92    110     79       C  
ATOM   1529  O   HIS A  93      30.631  -2.106   9.130  1.00 11.56           O  
ANISOU 1529  O   HIS A  93     1496    827   2068   -212    390   -156       O  
ATOM   1530  CB  HIS A  93      32.440   0.118   7.547  1.00  8.88           C  
ANISOU 1530  CB  HIS A  93     1066    883   1424      8     57    -75       C  
ATOM   1531  CG  HIS A  93      33.494   1.082   8.005  1.00  8.69           C  
ANISOU 1531  CG  HIS A  93      978    710   1613   -149     51   -116       C  
ATOM   1532  ND1 HIS A  93      34.833   0.880   7.756  1.00  9.48           N  
ANISOU 1532  ND1 HIS A  93     1123    792   1687    -98     13   -336       N  
ATOM   1533  CD2 HIS A  93      33.422   2.199   8.774  1.00  7.81           C  
ANISOU 1533  CD2 HIS A  93      941    782   1246   -224    178    -25       C  
ATOM   1534  CE1 HIS A  93      35.532   1.851   8.319  1.00  9.19           C  
ANISOU 1534  CE1 HIS A  93     1062    799   1630    -47    131   -303       C  
ATOM   1535  NE2 HIS A  93      34.702   2.661   8.946  1.00  8.83           N  
ANISOU 1535  NE2 HIS A  93     1195    780   1381     33    126    -72       N  
ATOM   1536  H   HIS A  93      33.933  -1.653   6.655  1.00 10.96           H  
ATOM   1537  HA  HIS A  93      32.914  -1.169   9.048  1.00 11.18           H  
ATOM   1538  HB2 HIS A  93      32.474   0.074   6.578  1.00 10.65           H  
ATOM   1539  HB3 HIS A  93      31.578   0.456   7.835  1.00 10.65           H  
ATOM   1540  HD1 HIS A  93      35.162   0.232   7.297  1.00 11.38           H  
ATOM   1541  HD2 HIS A  93      32.647   2.586   9.113  1.00  9.38           H  
ATOM   1542  HE1 HIS A  93      36.456   1.948   8.278  1.00 11.02           H  
ATOM   1543  N   ALA A  94      31.196  -3.018   7.158  1.00  9.75           N  
ANISOU 1543  N   ALA A  94     1308    803   1595   -195    -28    -26       N  
ATOM   1544  CA  ALA A  94      30.083  -3.963   7.192  1.00  9.91           C  
ANISOU 1544  CA  ALA A  94     1332    771   1660   -231      8     28       C  
ATOM   1545  C   ALA A  94      30.336  -5.107   8.165  1.00 10.68           C  
ANISOU 1545  C   ALA A  94     1467    808   1783   -169     96     47       C  
ATOM   1546  O   ALA A  94      29.443  -5.490   8.926  1.00 12.58           O  
ANISOU 1546  O   ALA A  94     1674    922   2182     18    370    234       O  
ATOM   1547  CB  ALA A  94      29.841  -4.538   5.798  1.00 11.35           C  
ANISOU 1547  CB  ALA A  94     1391    958   1965   -311   -194    159       C  
ATOM   1548  H   ALA A  94      31.684  -3.067   6.451  1.00 11.70           H  
ATOM   1549  HA  ALA A  94      29.278  -3.498   7.473  1.00 11.89           H  
ATOM   1550  HB1 ALA A  94      29.100  -5.162   5.838  1.00 13.62           H  
ATOM   1551  HB2 ALA A  94      29.630  -3.812   5.190  1.00 13.62           H  
ATOM   1552  HB3 ALA A  94      30.644  -4.995   5.502  1.00 13.62           H  
ATOM   1553  N   THR A  95      31.530  -5.697   8.125  1.00 10.70           N  
ANISOU 1553  N   THR A  95     1573    791   1702    -66    -38     -1       N  
ATOM   1554  CA  THR A  95      31.767  -7.015   8.708  1.00 11.45           C  
ANISOU 1554  CA  THR A  95     1851    843   1656     -6     22    175       C  
ATOM   1555  C   THR A  95      32.441  -6.953  10.066  1.00 12.34           C  
ANISOU 1555  C   THR A  95     2352    748   1589     58   -150     32       C  
ATOM   1556  O   THR A  95      32.111  -7.757  10.951  1.00 14.73           O  
ANISOU 1556  O   THR A  95     2827   1184   1588     37    -60    237       O  
ATOM   1557  CB  THR A  95      32.630  -7.873   7.762  1.00 11.79           C  
ANISOU 1557  CB  THR A  95     1957    818   1706     -4   -422    -51       C  
ATOM   1558  OG1 THR A  95      32.129  -7.759   6.431  1.00 16.14           O  
ANISOU 1558  OG1 THR A  95     2605   1323   2205    770   -666   -364       O  
ATOM   1559  CG2 THR A  95      32.665  -9.347   8.191  1.00 11.89           C  
ANISOU 1559  CG2 THR A  95     1774    764   1980      6    -34    -12       C  
ATOM   1560  H   THR A  95      32.227  -5.349   7.761  1.00 12.85           H  
ATOM   1561  HA  THR A  95      30.915  -7.463   8.821  1.00 13.74           H  
ATOM   1562  HB  THR A  95      33.540  -7.539   7.781  1.00 14.15           H  
ATOM   1563  HG1 THR A  95      31.333  -8.026   6.400  1.00 19.37           H  
ATOM   1564 HG21 THR A  95      33.215  -9.858   7.576  1.00 14.27           H  
ATOM   1565 HG22 THR A  95      33.037  -9.424   9.084  1.00 14.27           H  
ATOM   1566 HG23 THR A  95      31.767  -9.714   8.191  1.00 14.27           H  
ATOM   1567  N   LYS A  96      33.395  -6.045  10.243  1.00 12.91           N  
ANISOU 1567  N   LYS A  96     2525    910   1469     49   -241      0       N  
ATOM   1568  CA  LYS A  96      34.103  -5.931  11.513  1.00 15.18           C  
ANISOU 1568  CA  LYS A  96     2833   1315   1619    271   -496   -145       C  
ATOM   1569  C   LYS A  96      33.457  -4.895  12.429  1.00 13.87           C  
ANISOU 1569  C   LYS A  96     2723   1070   1478    -60   -149     18       C  
ATOM   1570  O   LYS A  96      33.088  -5.205  13.568  1.00 15.84           O  
ANISOU 1570  O   LYS A  96     3185   1036   1799     50   -115    152       O  
ATOM   1571  CB  LYS A  96      35.575  -5.588  11.270  1.00 17.92           C  
ANISOU 1571  CB  LYS A  96     3154   1700   1956    694   -793   -607       C  
ATOM   1572  CG  LYS A  96      36.357  -5.429  12.569  1.00 22.98           C  
ANISOU 1572  CG  LYS A  96     3549   2258   2924   1015  -1157   -606       C  
ATOM   1573  CD  LYS A  96      37.824  -5.139  12.334  1.00 29.28           C  
ANISOU 1573  CD  LYS A  96     4170   2903   4051   1323  -1213   -483       C  
ATOM   1574  CE  LYS A  96      38.543  -4.813  13.646  1.00 34.26           C  
ANISOU 1574  CE  LYS A  96     4641   3478   4896   1715  -1338   -234       C  
ATOM   1575  NZ  LYS A  96      38.405  -5.882  14.677  1.00 37.47           N  
ANISOU 1575  NZ  LYS A  96     4874   3921   5444   1940  -1384    -62       N  
ATOM   1576  H   LYS A  96      33.652  -5.483   9.644  1.00 15.49           H  
ATOM   1577  HA  LYS A  96      34.070  -6.788  11.966  1.00 18.21           H  
ATOM   1578  HB2 LYS A  96      35.986  -6.301  10.756  1.00 21.51           H  
ATOM   1579  HB3 LYS A  96      35.629  -4.752  10.781  1.00 21.51           H  
ATOM   1580  HG2 LYS A  96      35.983  -4.692  13.076  1.00 27.58           H  
ATOM   1581  HG3 LYS A  96      36.292  -6.251  13.081  1.00 27.58           H  
ATOM   1582  HD2 LYS A  96      38.246  -5.919  11.941  1.00 35.13           H  
ATOM   1583  HD3 LYS A  96      37.909  -4.376  11.742  1.00 35.13           H  
ATOM   1584  HE2 LYS A  96      39.488  -4.693  13.464  1.00 41.11           H  
ATOM   1585  HE3 LYS A  96      38.171  -3.995  14.013  1.00 41.11           H  
ATOM   1586  HZ1 LYS A  96      38.838  -5.647  15.418  1.00 44.97           H  
ATOM   1587  HZ2 LYS A  96      37.546  -6.008  14.871  1.00 44.97           H  
ATOM   1588  HZ3 LYS A  96      38.747  -6.645  14.371  1.00 44.97           H  
ATOM   1589  N   HIS A  97      33.323  -3.658  11.953  1.00 12.65           N  
ANISOU 1589  N   HIS A  97     2366    939   1503   -159    -51    -54       N  
ATOM   1590  CA  HIS A  97      32.849  -2.592  12.824  1.00 12.39           C  
ANISOU 1590  CA  HIS A  97     2149    916   1642   -207    134   -143       C  
ATOM   1591  C   HIS A  97      31.327  -2.563  12.937  1.00 13.13           C  
ANISOU 1591  C   HIS A  97     2125   1072   1793   -322    395    -99       C  
ATOM   1592  O   HIS A  97      30.794  -2.056  13.933  1.00 14.56           O  
ANISOU 1592  O   HIS A  97     2342   1360   1831   -163    468   -103       O  
ATOM   1593  CB  HIS A  97      33.354  -1.245  12.313  1.00 12.17           C  
ANISOU 1593  CB  HIS A  97     2055    919   1649    -61   -158   -190       C  
ATOM   1594  CG  HIS A  97      34.831  -1.201  12.044  1.00 12.29           C  
ANISOU 1594  CG  HIS A  97     1916   1167   1586    -73   -240   -110       C  
ATOM   1595  ND1 HIS A  97      35.781  -1.635  12.946  1.00 12.91           N  
ANISOU 1595  ND1 HIS A  97     2097   1107   1700     -7   -210     48       N  
ATOM   1596  CD2 HIS A  97      35.512  -0.760  10.958  1.00 12.36           C  
ANISOU 1596  CD2 HIS A  97     1967   1081   1649    -59    -87   -164       C  
ATOM   1597  CE1 HIS A  97      36.984  -1.463  12.422  1.00 13.61           C  
ANISOU 1597  CE1 HIS A  97     2032   1223   1917    -33   -171    102       C  
ATOM   1598  NE2 HIS A  97      36.850  -0.931  11.217  1.00 13.00           N  
ANISOU 1598  NE2 HIS A  97     1962   1115   1864   -176    -75   -128       N  
ATOM   1599  H   HIS A  97      33.495  -3.416  11.146  1.00 15.18           H  
ATOM   1600  HA  HIS A  97      33.212  -2.729  13.713  1.00 14.87           H  
ATOM   1601  HB2 HIS A  97      32.897  -1.035  11.483  1.00 14.60           H  
ATOM   1602  HB3 HIS A  97      33.155  -0.566  12.977  1.00 14.60           H  
ATOM   1603  HD2 HIS A  97      35.143  -0.404  10.182  1.00 14.83           H  
ATOM   1604  HE1 HIS A  97      37.790  -1.678  12.832  1.00 16.34           H  
ATOM   1605  HE2 HIS A  97      37.494  -0.731  10.684  1.00 15.60           H  
ATOM   1606  N   LYS A  98      30.627  -3.057  11.911  1.00 13.29           N  
ANISOU 1606  N   LYS A  98     2055    861   2134   -377    437    -45       N  
ATOM   1607  CA  LYS A  98      29.162  -3.135  11.875  1.00 15.07           C  
ANISOU 1607  CA  LYS A  98     2157    932   2636   -282    569    229       C  
ATOM   1608  C   LYS A  98      28.505  -1.748  11.953  1.00 13.54           C  
ANISOU 1608  C   LYS A  98     1870   1094   2180   -256    517     41       C  
ATOM   1609  O   LYS A  98      27.724  -1.447  12.862  1.00 13.94           O  
ANISOU 1609  O   LYS A  98     1808   1281   2207   -364    508    -40       O  
ATOM   1610  CB  LYS A  98      28.632  -4.083  12.957  1.00 20.79           C  
ANISOU 1610  CB  LYS A  98     2627   1265   4006   -219    779    469       C  
ATOM   1611  CG  LYS A  98      29.260  -5.480  12.933  1.00 28.53           C  
ANISOU 1611  CG  LYS A  98     3222   2086   5533    146    796    510       C  
ATOM   1612  CD  LYS A  98      28.340  -6.536  12.329  1.00 35.70           C  
ANISOU 1612  CD  LYS A  98     3759   2960   6844    640    556     -6       C  
ATOM   1613  CE  LYS A  98      28.954  -7.937  12.427  1.00 40.03           C  
ANISOU 1613  CE  LYS A  98     4109   3407   7692    838    409   -358       C  
ATOM   1614  NZ  LYS A  98      28.021  -9.021  11.985  1.00 42.96           N  
ANISOU 1614  NZ  LYS A  98     4338   3840   8145   1022    307   -515       N  
ATOM   1615  H   LYS A  98      30.994  -3.365  11.197  1.00 15.95           H  
ATOM   1616  HA  LYS A  98      28.908  -3.516  11.020  1.00 18.08           H  
ATOM   1617  HB2 LYS A  98      28.812  -3.694  13.827  1.00 24.94           H  
ATOM   1618  HB3 LYS A  98      27.675  -4.188  12.837  1.00 24.94           H  
ATOM   1619  HG2 LYS A  98      30.071  -5.451  12.402  1.00 34.24           H  
ATOM   1620  HG3 LYS A  98      29.468  -5.748  13.842  1.00 34.24           H  
ATOM   1621  HD2 LYS A  98      27.497  -6.539  12.810  1.00 42.84           H  
ATOM   1622  HD3 LYS A  98      28.191  -6.334  11.392  1.00 42.84           H  
ATOM   1623  HE2 LYS A  98      29.743  -7.974  11.864  1.00 48.03           H  
ATOM   1624  HE3 LYS A  98      29.198  -8.110  13.350  1.00 48.03           H  
ATOM   1625  HZ1 LYS A  98      28.419  -9.813  12.059  1.00 51.55           H  
ATOM   1626  HZ2 LYS A  98      27.289  -9.016  12.491  1.00 51.55           H  
ATOM   1627  HZ3 LYS A  98      27.786  -8.892  11.136  1.00 51.55           H  
ATOM   1628  N   ILE A  99      28.795  -0.919  10.951  1.00 12.86           N  
ANISOU 1628  N   ILE A  99     1767   1075   2045   -180    530   -219       N  
ATOM   1629  CA  ILE A  99      28.344   0.471  10.908  1.00 12.62           C  
ANISOU 1629  CA  ILE A  99     1771    909   2115    -91    398   -372       C  
ATOM   1630  C   ILE A  99      27.146   0.563   9.958  1.00 12.89           C  
ANISOU 1630  C   ILE A  99     1599   1037   2263   -190    390   -457       C  
ATOM   1631  O   ILE A  99      27.330   0.444   8.735  1.00 13.60           O  
ANISOU 1631  O   ILE A  99     1664   1299   2204   -266    318   -694       O  
ATOM   1632  CB  ILE A  99      29.472   1.409  10.461  1.00 11.59           C  
ANISOU 1632  CB  ILE A  99     1540    945   1918   -305    401   -176       C  
ATOM   1633  CG1 ILE A  99      30.726   1.216  11.337  1.00 11.80           C  
ANISOU 1633  CG1 ILE A  99     1642   1092   1752    -62    375   -153       C  
ATOM   1634  CG2 ILE A  99      28.985   2.868  10.479  1.00 11.99           C  
ANISOU 1634  CG2 ILE A  99     1589    969   1997   -212    283    -99       C  
ATOM   1635  CD1 ILE A  99      30.490   1.241  12.836  1.00 11.93           C  
ANISOU 1635  CD1 ILE A  99     1761    991   1781    -69    537    -79       C  
ATOM   1636  H   ILE A  99      29.264  -1.146  10.267  1.00 15.43           H  
ATOM   1637  HA  ILE A  99      28.054   0.742  11.792  1.00 15.14           H  
ATOM   1638  HB  ILE A  99      29.707   1.182   9.547  1.00 13.91           H  
ATOM   1639 HG12 ILE A  99      31.122   0.358  11.119  1.00 14.17           H  
ATOM   1640 HG13 ILE A  99      31.356   1.924  11.130  1.00 14.17           H  
ATOM   1641 HG21 ILE A  99      29.710   3.446  10.194  1.00 14.38           H  
ATOM   1642 HG22 ILE A  99      28.233   2.957   9.872  1.00 14.38           H  
ATOM   1643 HG23 ILE A  99      28.712   3.099  11.381  1.00 14.38           H  
ATOM   1644 HD11 ILE A  99      31.337   1.112  13.291  1.00 14.31           H  
ATOM   1645 HD12 ILE A  99      30.110   2.099  13.082  1.00 14.31           H  
ATOM   1646 HD13 ILE A  99      29.876   0.528  13.071  1.00 14.31           H  
ATOM   1647  N   PRO A 100      25.928   0.784  10.454  1.00 13.06           N  
ANISOU 1647  N   PRO A 100     1507   1116   2339   -209    339   -305       N  
ATOM   1648  CA  PRO A 100      24.781   0.920   9.543  1.00 13.86           C  
ANISOU 1648  CA  PRO A 100     1490   1182   2592   -375    354   -329       C  
ATOM   1649  C   PRO A 100      24.880   2.170   8.670  1.00 12.60           C  
ANISOU 1649  C   PRO A 100     1545   1093   2148   -403    436   -378       C  
ATOM   1650  O   PRO A 100      25.520   3.167   9.021  1.00 12.83           O  
ANISOU 1650  O   PRO A 100     1502   1123   2251   -429    498   -399       O  
ATOM   1651  CB  PRO A 100      23.574   0.996  10.490  1.00 16.32           C  
ANISOU 1651  CB  PRO A 100     1642   1584   2976   -374    542    -36       C  
ATOM   1652  CG  PRO A 100      24.122   1.441  11.770  1.00 17.98           C  
ANISOU 1652  CG  PRO A 100     1682   2125   3025    -66    556   -241       C  
ATOM   1653  CD  PRO A 100      25.525   0.903  11.861  1.00 14.95           C  
ANISOU 1653  CD  PRO A 100     1557   1584   2540    -83    482   -244       C  
ATOM   1654  HA  PRO A 100      24.701   0.135   8.978  1.00 16.63           H  
ATOM   1655  HB2 PRO A 100      22.932   1.639  10.150  1.00 19.59           H  
ATOM   1656  HB3 PRO A 100      23.170   0.119  10.576  1.00 19.59           H  
ATOM   1657  HG2 PRO A 100      24.130   2.411  11.797  1.00 21.58           H  
ATOM   1658  HG3 PRO A 100      23.579   1.089  12.492  1.00 21.58           H  
ATOM   1659  HD2 PRO A 100      26.099   1.531  12.326  1.00 17.94           H  
ATOM   1660  HD3 PRO A 100      25.527   0.033  12.288  1.00 17.94           H  
ATOM   1661  N   ILE A 101      24.226   2.106   7.509  1.00 13.35           N  
ANISOU 1661  N   ILE A 101     1701   1092   2280   -588    283   -409       N  
ATOM   1662  CA  ILE A 101      24.183   3.262   6.613  1.00 14.67           C  
ANISOU 1662  CA  ILE A 101     1980   1327   2266   -558    163   -518       C  
ATOM   1663  C   ILE A 101      23.668   4.502   7.339  1.00 13.18           C  
ANISOU 1663  C   ILE A 101     1785   1276   1948   -489    217   -340       C  
ATOM   1664  O   ILE A 101      24.151   5.613   7.104  1.00 13.03           O  
ANISOU 1664  O   ILE A 101     1679   1191   2083   -520     34   -204       O  
ATOM   1665  CB  ILE A 101      23.372   2.937   5.339  1.00 17.17           C  
ANISOU 1665  CB  ILE A 101     2432   1613   2478   -662     49   -536       C  
ATOM   1666  CG1 ILE A 101      24.029   1.791   4.542  1.00 18.33           C  
ANISOU 1666  CG1 ILE A 101     2439   2040   2486   -761    324   -734       C  
ATOM   1667  CG2 ILE A 101      23.225   4.181   4.461  1.00 19.02           C  
ANISOU 1667  CG2 ILE A 101     2748   1901   2579   -516   -135   -408       C  
ATOM   1668  CD1 ILE A 101      25.432   2.096   3.991  1.00 20.49           C  
ANISOU 1668  CD1 ILE A 101     2575   2356   2853   -702    548   -912       C  
ATOM   1669  H   ILE A 101      23.805   1.414   7.219  1.00 16.02           H  
ATOM   1670  HA  ILE A 101      25.091   3.456   6.330  1.00 17.60           H  
ATOM   1671  HB  ILE A 101      22.486   2.650   5.609  1.00 20.60           H  
ATOM   1672 HG12 ILE A 101      24.106   1.017   5.123  1.00 22.00           H  
ATOM   1673 HG13 ILE A 101      23.460   1.575   3.787  1.00 22.00           H  
ATOM   1674 HG21 ILE A 101      22.713   3.950   3.670  1.00 22.83           H  
ATOM   1675 HG22 ILE A 101      22.763   4.870   4.964  1.00 22.83           H  
ATOM   1676 HG23 ILE A 101      24.107   4.493   4.205  1.00 22.83           H  
ATOM   1677 HD11 ILE A 101      25.758   1.319   3.510  1.00 24.58           H  
ATOM   1678 HD12 ILE A 101      25.378   2.857   3.393  1.00 24.58           H  
ATOM   1679 HD13 ILE A 101      26.025   2.298   4.732  1.00 24.58           H  
ATOM   1680  N   LYS A 102      22.709   4.317   8.224  1.00 13.20           N  
ANISOU 1680  N   LYS A 102     1604   1200   2212   -440    134   -179       N  
ATOM   1681  CA  LYS A 102      22.172   5.454   8.998  1.00 13.87           C  
ANISOU 1681  CA  LYS A 102     1537   1295   2440   -527    191   -159       C  
ATOM   1682  C   LYS A 102      23.333   6.212   9.729  1.00 11.55           C  
ANISOU 1682  C   LYS A 102     1343   1073   1972   -362    120   -123       C  
ATOM   1683  O   LYS A 102      23.306   7.459   9.855  1.00 11.90           O  
ANISOU 1683  O   LYS A 102     1319   1005   2198   -338     56    -91       O  
ATOM   1684  CB  LYS A 102      21.080   5.037  10.045  1.00 17.94           C  
ANISOU 1684  CB  LYS A 102     1712   1788   3316   -543    162   -610       C  
ATOM   1685  H   LYS A 102      22.405   3.505   8.327  1.00 15.84           H  
ATOM   1686  HA  LYS A 102      21.689   5.992   8.319  1.00 16.65           H  
ATOM   1687  N   TYR A 103      24.315   5.478  10.253  1.00 10.60           N  
ANISOU 1687  N   TYR A 103     1225    960   1842   -260    274    -98       N  
ATOM   1688  CA  TYR A 103      25.423   6.146  10.939  1.00  9.93           C  
ANISOU 1688  CA  TYR A 103     1254    841   1680   -198    340     53       C  
ATOM   1689  C   TYR A 103      26.345   6.873   9.960  1.00  9.34           C  
ANISOU 1689  C   TYR A 103     1127    821   1600   -130    415    -65       C  
ATOM   1690  O   TYR A 103      26.956   7.888  10.320  1.00  9.09           O  
ANISOU 1690  O   TYR A 103     1174    763   1516   -205    248     28       O  
ATOM   1691  CB  TYR A 103      26.230   5.156  11.791  1.00 10.77           C  
ANISOU 1691  CB  TYR A 103     1453    958   1681   -203    311     52       C  
ATOM   1692  CG  TYR A 103      25.550   4.619  13.045  1.00 11.91           C  
ANISOU 1692  CG  TYR A 103     1650   1006   1869   -366    407    -84       C  
ATOM   1693  CD1 TYR A 103      26.264   3.838  13.926  1.00 12.32           C  
ANISOU 1693  CD1 TYR A 103     1984    953   1743   -240    295     67       C  
ATOM   1694  CD2 TYR A 103      24.217   4.895  13.351  1.00 13.70           C  
ANISOU 1694  CD2 TYR A 103     1843   1324   2037   -408    460    171       C  
ATOM   1695  CE1 TYR A 103      25.683   3.311  15.068  1.00 13.38           C  
ANISOU 1695  CE1 TYR A 103     2145   1167   1772   -304    422    -57       C  
ATOM   1696  CE2 TYR A 103      23.618   4.378  14.509  1.00 15.48           C  
ANISOU 1696  CE2 TYR A 103     2122   1606   2153   -343    635     77       C  
ATOM   1697  CZ  TYR A 103      24.364   3.596  15.359  1.00 14.37           C  
ANISOU 1697  CZ  TYR A 103     2251   1320   1888   -519    646    107       C  
ATOM   1698  OH  TYR A 103      23.796   3.058  16.504  1.00 17.16           O  
ANISOU 1698  OH  TYR A 103     2543   1811   2164   -427    772    280       O  
ATOM   1699  H   TYR A 103      24.370   4.620  10.220  1.00 12.72           H  
ATOM   1700  HA  TYR A 103      25.053   6.812  11.540  1.00 11.92           H  
ATOM   1701  HB2 TYR A 103      26.454   4.392  11.237  1.00 12.92           H  
ATOM   1702  HB3 TYR A 103      27.046   5.597  12.074  1.00 12.92           H  
ATOM   1703  HD1 TYR A 103      27.153   3.638  13.737  1.00 14.78           H  
ATOM   1704  HD2 TYR A 103      23.715   5.423  12.773  1.00 16.44           H  
ATOM   1705  HE1 TYR A 103      26.184   2.782  15.646  1.00 16.05           H  
ATOM   1706  HE2 TYR A 103      22.727   4.564  14.700  1.00 18.57           H  
ATOM   1707  HH  TYR A 103      22.995   3.303  16.569  1.00 20.59           H  
ATOM   1708  N   LEU A 104      26.478   6.372   8.728  1.00  9.44           N  
ANISOU 1708  N   LEU A 104     1274    754   1557   -116    348     10       N  
ATOM   1709  CA  LEU A 104      27.182   7.113   7.683  1.00  9.18           C  
ANISOU 1709  CA  LEU A 104     1225    859   1405   -110    247    -71       C  
ATOM   1710  C   LEU A 104      26.427   8.390   7.309  1.00  8.84           C  
ANISOU 1710  C   LEU A 104     1042    808   1509   -215    181    -27       C  
ATOM   1711  O   LEU A 104      27.051   9.408   6.986  1.00  8.98           O  
ANISOU 1711  O   LEU A 104     1163    810   1441   -173     34    -86       O  
ATOM   1712  CB  LEU A 104      27.433   6.230   6.459  1.00 10.07           C  
ANISOU 1712  CB  LEU A 104     1300   1008   1517    -72    247    -24       C  
ATOM   1713  CG  LEU A 104      28.251   4.961   6.695  1.00 10.73           C  
ANISOU 1713  CG  LEU A 104     1504    971   1600    -64    260   -137       C  
ATOM   1714  CD1 LEU A 104      28.464   4.241   5.378  1.00 12.15           C  
ANISOU 1714  CD1 LEU A 104     1567   1149   1903     57    185   -184       C  
ATOM   1715  CD2 LEU A 104      29.579   5.247   7.365  1.00 12.26           C  
ANISOU 1715  CD2 LEU A 104     1460   1321   1877    127    278   -119       C  
ATOM   1716  H   LEU A 104      26.170   5.609   8.474  1.00 11.32           H  
ATOM   1717  HA  LEU A 104      28.048   7.380   8.030  1.00 11.02           H  
ATOM   1718  HB2 LEU A 104      26.574   5.956   6.101  1.00 12.08           H  
ATOM   1719  HB3 LEU A 104      27.904   6.757   5.795  1.00 12.08           H  
ATOM   1720  HG  LEU A 104      27.748   4.370   7.277  1.00 12.87           H  
ATOM   1721 HD11 LEU A 104      28.983   3.438   5.538  1.00 14.59           H  
ATOM   1722 HD12 LEU A 104      27.600   4.007   5.003  1.00 14.59           H  
ATOM   1723 HD13 LEU A 104      28.940   4.829   4.771  1.00 14.59           H  
ATOM   1724 HD21 LEU A 104      30.055   4.411   7.490  1.00 14.71           H  
ATOM   1725 HD22 LEU A 104      30.096   5.840   6.799  1.00 14.71           H  
ATOM   1726 HD23 LEU A 104      29.415   5.667   8.224  1.00 14.71           H  
ATOM   1727  N   GLU A 105      25.088   8.360   7.340  1.00  9.75           N  
ANISOU 1727  N   GLU A 105     1026    875   1804   -222    147   -224       N  
ATOM   1728  CA  GLU A 105      24.311   9.592   7.199  1.00 10.18           C  
ANISOU 1728  CA  GLU A 105     1060    999   1809   -151     41   -189       C  
ATOM   1729  C   GLU A 105      24.618  10.565   8.334  1.00  9.27           C  
ANISOU 1729  C   GLU A 105      909    928   1687    -77     94   -250       C  
ATOM   1730  O   GLU A 105      24.836  11.761   8.099  1.00  9.64           O  
ANISOU 1730  O   GLU A 105     1068    852   1744    -93    149   -119       O  
ATOM   1731  CB  GLU A 105      22.817   9.256   7.143  1.00 12.73           C  
ANISOU 1731  CB  GLU A 105     1219   1329   2288   -253    -96   -296       C  
ATOM   1732  CG  GLU A 105      22.409   8.454   5.903  1.00 15.78           C  
ANISOU 1732  CG  GLU A 105     1480   1983   2532   -349    151   -256       C  
ATOM   1733  CD  GLU A 105      20.996   7.870   5.923  1.00 18.70           C  
ANISOU 1733  CD  GLU A 105     1671   2713   2722   -357    291   -702       C  
ATOM   1734  OE1 GLU A 105      20.249   8.056   6.899  1.00 21.02           O  
ANISOU 1734  OE1 GLU A 105     1693   3351   2944   -477    262   -666       O  
ATOM   1735  OE2 GLU A 105      20.629   7.207   4.935  1.00 20.21           O  
ANISOU 1735  OE2 GLU A 105     1737   2879   3063   -621     90   -957       O  
ATOM   1736  H   GLU A 105      24.616   7.648   7.441  1.00 11.70           H  
ATOM   1737  HA  GLU A 105      24.552  10.022   6.364  1.00 12.21           H  
ATOM   1738  HB2 GLU A 105      22.585   8.731   7.925  1.00 15.28           H  
ATOM   1739  HB3 GLU A 105      22.310  10.084   7.140  1.00 15.28           H  
ATOM   1740  HG2 GLU A 105      22.471   9.036   5.129  1.00 18.93           H  
ATOM   1741  HG3 GLU A 105      23.027   7.714   5.801  1.00 18.93           H  
ATOM   1742  N   PHE A 106      24.676  10.062   9.570  1.00  9.33           N  
ANISOU 1742  N   PHE A 106     1061    902   1583    -83    128   -115       N  
ATOM   1743  CA  PHE A 106      24.971  10.932  10.707  1.00  9.20           C  
ANISOU 1743  CA  PHE A 106     1018    907   1571    -50    284    -64       C  
ATOM   1744  C   PHE A 106      26.350  11.588  10.574  1.00  8.59           C  
ANISOU 1744  C   PHE A 106      901    842   1521   -118    255      6       C  
ATOM   1745  O   PHE A 106      26.508  12.790  10.842  1.00  8.49           O  
ANISOU 1745  O   PHE A 106      946    720   1561    -93    258    -46       O  
ATOM   1746  CB  PHE A 106      24.910  10.158  12.030  1.00  9.80           C  
ANISOU 1746  CB  PHE A 106     1071   1066   1586   -175    432   -119       C  
ATOM   1747  CG  PHE A 106      23.548   9.635  12.432  1.00 11.05           C  
ANISOU 1747  CG  PHE A 106     1239   1150   1809   -177    482   -181       C  
ATOM   1748  CD1 PHE A 106      23.469   8.585  13.341  1.00 12.41           C  
ANISOU 1748  CD1 PHE A 106     1349   1275   2090   -316    447   -224       C  
ATOM   1749  CD2 PHE A 106      22.361  10.179  11.963  1.00 13.04           C  
ANISOU 1749  CD2 PHE A 106     1265   1419   2269   -291    528    -82       C  
ATOM   1750  CE1 PHE A 106      22.244   8.084  13.766  1.00 14.78           C  
ANISOU 1750  CE1 PHE A 106     1535   1549   2531   -260    602    -88       C  
ATOM   1751  CE2 PHE A 106      21.128   9.682  12.411  1.00 15.23           C  
ANISOU 1751  CE2 PHE A 106     1370   1796   2620   -320    541     11       C  
ATOM   1752  CZ  PHE A 106      21.091   8.630  13.297  1.00 15.34           C  
ANISOU 1752  CZ  PHE A 106     1416   1645   2766   -468    604    -39       C  
ATOM   1753  H   PHE A 106      24.550   9.236   9.773  1.00 11.20           H  
ATOM   1754  HA  PHE A 106      24.306  11.639  10.743  1.00 11.04           H  
ATOM   1755  HB2 PHE A 106      25.504   9.394  11.964  1.00 11.76           H  
ATOM   1756  HB3 PHE A 106      25.215  10.743  12.741  1.00 11.76           H  
ATOM   1757  HD1 PHE A 106      24.253   8.209  13.670  1.00 14.89           H  
ATOM   1758  HD2 PHE A 106      22.384  10.893  11.367  1.00 15.64           H  
ATOM   1759  HE1 PHE A 106      22.213   7.377  14.370  1.00 17.73           H  
ATOM   1760  HE2 PHE A 106      20.335  10.043  12.085  1.00 18.27           H  
ATOM   1761  HZ  PHE A 106      20.271   8.292  13.578  1.00 18.40           H  
ATOM   1762  N   ILE A 107      27.374  10.825  10.168  1.00  8.73           N  
ANISOU 1762  N   ILE A 107      942    857   1518   -108    327    -85       N  
ATOM   1763  CA  ILE A 107      28.699  11.450  10.048  1.00  8.43           C  
ANISOU 1763  CA  ILE A 107     1082    774   1349     -6    282     87       C  
ATOM   1764  C   ILE A 107      28.729  12.442   8.887  1.00  7.87           C  
ANISOU 1764  C   ILE A 107      937    667   1388     18    159   -151       C  
ATOM   1765  O   ILE A 107      29.436  13.463   8.944  1.00  7.77           O  
ANISOU 1765  O   ILE A 107      869    677   1406    -37    105    -65       O  
ATOM   1766  CB  ILE A 107      29.871  10.435  10.010  1.00  8.72           C  
ANISOU 1766  CB  ILE A 107     1151    794   1368    -54    194     72       C  
ATOM   1767  CG1 ILE A 107      31.185  11.117  10.455  1.00  8.62           C  
ANISOU 1767  CG1 ILE A 107     1109    843   1322      1     87    -42       C  
ATOM   1768  CG2 ILE A 107      30.021   9.780   8.611  1.00  9.35           C  
ANISOU 1768  CG2 ILE A 107     1192    866   1494     92    141    -35       C  
ATOM   1769  CD1 ILE A 107      32.369  10.175  10.580  1.00  9.58           C  
ANISOU 1769  CD1 ILE A 107     1132   1109   1401    101    114     97       C  
ATOM   1770  H   ILE A 107      27.335   9.990   9.966  1.00 10.47           H  
ATOM   1771  HA  ILE A 107      28.833  11.977  10.851  1.00 10.12           H  
ATOM   1772  HB  ILE A 107      29.673   9.731  10.647  1.00 10.47           H  
ATOM   1773 HG12 ILE A 107      31.417  11.798   9.804  1.00 10.34           H  
ATOM   1774 HG13 ILE A 107      31.043  11.529  11.322  1.00 10.34           H  
ATOM   1775 HG21 ILE A 107      30.763   9.155   8.634  1.00 11.22           H  
ATOM   1776 HG22 ILE A 107      29.200   9.311   8.393  1.00 11.22           H  
ATOM   1777 HG23 ILE A 107      30.191  10.473   7.955  1.00 11.22           H  
ATOM   1778 HD11 ILE A 107      33.146  10.682  10.861  1.00 11.50           H  
ATOM   1779 HD12 ILE A 107      32.161   9.494  11.238  1.00 11.50           H  
ATOM   1780 HD13 ILE A 107      32.536   9.763   9.718  1.00 11.50           H  
ATOM   1781  N   SER A 108      27.960  12.178   7.824  1.00  8.40           N  
ANISOU 1781  N   SER A 108     1081    737   1374    -64     55     12       N  
ATOM   1782  CA  SER A 108      27.868  13.133   6.721  1.00  7.98           C  
ANISOU 1782  CA  SER A 108      998    743   1292   -103     18    -64       C  
ATOM   1783  C   SER A 108      27.276  14.458   7.191  1.00  8.06           C  
ANISOU 1783  C   SER A 108      832    779   1451    -91     30   -109       C  
ATOM   1784  O   SER A 108      27.756  15.537   6.805  1.00  8.32           O  
ANISOU 1784  O   SER A 108      945    776   1439    -97    -98     13       O  
ATOM   1785  CB  SER A 108      27.013  12.556   5.586  1.00  8.61           C  
ANISOU 1785  CB  SER A 108     1194    772   1305    100    104    -69       C  
ATOM   1786  OG  SER A 108      27.611  11.400   4.999  1.00  9.07           O  
ANISOU 1786  OG  SER A 108     1174    852   1419    -27    -19     32       O  
ATOM   1787  H   SER A 108      27.491  11.465   7.721  1.00 10.08           H  
ATOM   1788  HA  SER A 108      28.757  13.305   6.373  1.00  9.58           H  
ATOM   1789  HB2 SER A 108      26.145  12.312   5.943  1.00 10.33           H  
ATOM   1790  HB3 SER A 108      26.907  13.234   4.901  1.00 10.33           H  
ATOM   1791  HG  SER A 108      27.707  10.800   5.580  1.00 10.88           H  
ATOM   1792  N   GLU A 109      26.230  14.398   8.029  1.00  8.91           N  
ANISOU 1792  N   GLU A 109      915    701   1768     23     55    -87       N  
ATOM   1793  CA  GLU A 109      25.645  15.606   8.606  1.00  9.89           C  
ANISOU 1793  CA  GLU A 109      770   1006   1980   -175     97   -165       C  
ATOM   1794  C   GLU A 109      26.661  16.356   9.465  1.00  8.58           C  
ANISOU 1794  C   GLU A 109      820    891   1548     20    190    100       C  
ATOM   1795  O   GLU A 109      26.732  17.591   9.413  1.00  8.42           O  
ANISOU 1795  O   GLU A 109      804    765   1632     54     11    -99       O  
ATOM   1796  CB AGLU A 109      24.427  15.277   9.468  0.57 12.13           C  
ANISOU 1796  CB AGLU A 109      866   1211   2533    -54     62   -367       C  
ATOM   1797  CB BGLU A 109      24.381  15.214   9.388  0.43 11.36           C  
ANISOU 1797  CB BGLU A 109      859   1299   2157   -184      7   -353       C  
ATOM   1798  CG AGLU A 109      23.629  16.519   9.924  0.57 14.78           C  
ANISOU 1798  CG AGLU A 109     1066   1377   3171    133    300   -569       C  
ATOM   1799  CG BGLU A 109      23.309  14.557   8.490  0.43 14.05           C  
ANISOU 1799  CG BGLU A 109     1037   1687   2615    -91    166   -250       C  
ATOM   1800  CD AGLU A 109      24.239  17.354  11.069  0.57 17.48           C  
ANISOU 1800  CD AGLU A 109     1531   1560   3551    515    595   -119       C  
ATOM   1801  CD BGLU A 109      22.291  13.668   9.219  0.43 16.33           C  
ANISOU 1801  CD BGLU A 109     1199   1981   3026    -15    178   -236       C  
ATOM   1802  OE1AGLU A 109      23.992  18.587  11.066  0.57 18.66           O  
ANISOU 1802  OE1AGLU A 109     1691   1439   3961    420    286   -121       O  
ATOM   1803  OE1BGLU A 109      22.268  13.604  10.468  0.43 16.72           O  
ANISOU 1803  OE1BGLU A 109     1256   2119   2976     41    532    242       O  
ATOM   1804  OE2AGLU A 109      24.914  16.803  11.980  0.57 20.10           O  
ANISOU 1804  OE2AGLU A 109     1995   1781   3860    654   1136    477       O  
ATOM   1805  OE2BGLU A 109      21.501  13.007   8.515  0.43 17.86           O  
ANISOU 1805  OE2BGLU A 109     1362   1927   3495   -143    230   -235       O  
ATOM   1806  H   GLU A 109      25.846  13.669   8.275  1.00 10.69           H  
ATOM   1807  HA  GLU A 109      25.374  16.197   7.886  1.00 11.86           H  
ATOM   1808  HB2AGLU A 109      23.827  14.711   8.958  0.57 14.56           H  
ATOM   1809  HB2BGLU A 109      24.622  14.579  10.081  0.43 13.63           H  
ATOM   1810  HB3AGLU A 109      24.724  14.808  10.263  0.57 14.56           H  
ATOM   1811  HB3BGLU A 109      23.994  16.010   9.785  0.43 13.63           H  
ATOM   1812  HG2AGLU A 109      23.528  17.110   9.161  0.57 17.73           H  
ATOM   1813  HG2BGLU A 109      22.813  15.260   8.041  0.43 16.86           H  
ATOM   1814  HG3AGLU A 109      22.753  16.225  10.219  0.57 17.73           H  
ATOM   1815  HG3BGLU A 109      23.757  14.005   7.831  0.43 16.86           H  
ATOM   1816  N   ALA A 110      27.465  15.627  10.247  1.00  8.02           N  
ANISOU 1816  N   ALA A 110      849    759   1439    -32    184    -71       N  
ATOM   1817  CA  ALA A 110      28.493  16.257  11.072  1.00  7.88           C  
ANISOU 1817  CA  ALA A 110      884    751   1360    -37     98    -39       C  
ATOM   1818  C   ALA A 110      29.551  16.948  10.219  1.00  7.19           C  
ANISOU 1818  C   ALA A 110      896    614   1222    -21     91     28       C  
ATOM   1819  O   ALA A 110      29.998  18.058  10.558  1.00  7.68           O  
ANISOU 1819  O   ALA A 110      900    668   1351      6     90    -37       O  
ATOM   1820  CB  ALA A 110      29.122  15.218  12.003  1.00  8.55           C  
ANISOU 1820  CB  ALA A 110     1032    930   1285   -100    249   -117       C  
ATOM   1821  H   ALA A 110      27.433  14.770  10.316  1.00  9.63           H  
ATOM   1822  HA  ALA A 110      28.075  16.934  11.627  1.00  9.46           H  
ATOM   1823  HB1 ALA A 110      29.802  15.650  12.544  1.00 10.25           H  
ATOM   1824  HB2 ALA A 110      28.431  14.847  12.574  1.00 10.25           H  
ATOM   1825  HB3 ALA A 110      29.522  14.515  11.467  1.00 10.25           H  
ATOM   1826  N   ILE A 111      29.975  16.307   9.117  1.00  6.99           N  
ANISOU 1826  N   ILE A 111      841    655   1162     38    114    -88       N  
ATOM   1827  CA  ILE A 111      30.926  16.926   8.188  1.00  7.02           C  
ANISOU 1827  CA  ILE A 111      817    680   1171     22     72    -46       C  
ATOM   1828  C   ILE A 111      30.354  18.235   7.648  1.00  6.56           C  
ANISOU 1828  C   ILE A 111      716    632   1144     36     99    -99       C  
ATOM   1829  O   ILE A 111      31.019  19.278   7.659  1.00  7.65           O  
ANISOU 1829  O   ILE A 111      827    718   1363      0     35    -31       O  
ATOM   1830  CB  ILE A 111      31.285  15.949   7.050  1.00  7.14           C  
ANISOU 1830  CB  ILE A 111      827    710   1175     91    119   -143       C  
ATOM   1831  CG1 ILE A 111      32.095  14.757   7.573  1.00  7.50           C  
ANISOU 1831  CG1 ILE A 111      757    733   1360      9    212    -52       C  
ATOM   1832  CG2 ILE A 111      32.028  16.671   5.924  1.00  7.91           C  
ANISOU 1832  CG2 ILE A 111      949    831   1227      5    196      6       C  
ATOM   1833  CD1 ILE A 111      32.121  13.552   6.624  1.00  8.85           C  
ANISOU 1833  CD1 ILE A 111      992    822   1547    120     77    -19       C  
ATOM   1834  H   ILE A 111      29.725  15.516   8.888  1.00  8.39           H  
ATOM   1835  HA  ILE A 111      31.743  17.134   8.669  1.00  8.43           H  
ATOM   1836  HB  ILE A 111      30.455  15.605   6.684  1.00  8.57           H  
ATOM   1837 HG12 ILE A 111      33.012  15.042   7.714  1.00  9.00           H  
ATOM   1838 HG13 ILE A 111      31.710  14.463   8.413  1.00  9.00           H  
ATOM   1839 HG21 ILE A 111      32.239  16.032   5.226  1.00  9.50           H  
ATOM   1840 HG22 ILE A 111      31.459  17.373   5.571  1.00  9.50           H  
ATOM   1841 HG23 ILE A 111      32.845  17.054   6.281  1.00  9.50           H  
ATOM   1842 HD11 ILE A 111      32.650  12.846   7.026  1.00 10.62           H  
ATOM   1843 HD12 ILE A 111      31.212  13.244   6.480  1.00 10.62           H  
ATOM   1844 HD13 ILE A 111      32.516  13.823   5.781  1.00 10.62           H  
ATOM   1845  N   ILE A 112      29.114  18.201   7.171  1.00  7.09           N  
ANISOU 1845  N   ILE A 112      717    628   1350    -14    -22     31       N  
ATOM   1846  CA  ILE A 112      28.474  19.394   6.624  1.00  8.08           C  
ANISOU 1846  CA  ILE A 112      771    717   1583     -9    -82    -56       C  
ATOM   1847  C   ILE A 112      28.391  20.493   7.686  1.00  7.94           C  
ANISOU 1847  C   ILE A 112      825    670   1523     63    -95    -71       C  
ATOM   1848  O   ILE A 112      28.680  21.665   7.409  1.00  8.40           O  
ANISOU 1848  O   ILE A 112      927    646   1620     37   -175     12       O  
ATOM   1849  CB  ILE A 112      27.101  19.021   6.015  1.00  8.40           C  
ANISOU 1849  CB  ILE A 112     1010    707   1476     -1   -148    -17       C  
ATOM   1850  CG1 ILE A 112      27.302  18.248   4.696  1.00  9.77           C  
ANISOU 1850  CG1 ILE A 112     1122    926   1663    -39   -347     68       C  
ATOM   1851  CG2 ILE A 112      26.226  20.267   5.803  1.00  9.29           C  
ANISOU 1851  CG2 ILE A 112      983    749   1797     29   -244    -28       C  
ATOM   1852  CD1 ILE A 112      26.039  17.581   4.135  1.00 11.79           C  
ANISOU 1852  CD1 ILE A 112     1348   1160   1973     78   -451   -139       C  
ATOM   1853  H   ILE A 112      28.619  17.498   7.151  1.00  8.51           H  
ATOM   1854  HA  ILE A 112      29.027  19.733   5.902  1.00  9.70           H  
ATOM   1855  HB  ILE A 112      26.644  18.436   6.639  1.00 10.09           H  
ATOM   1856 HG12 ILE A 112      27.630  18.866   4.024  1.00 11.72           H  
ATOM   1857 HG13 ILE A 112      27.959  17.551   4.845  1.00 11.72           H  
ATOM   1858 HG21 ILE A 112      25.377  19.995   5.421  1.00 11.14           H  
ATOM   1859 HG22 ILE A 112      26.081  20.700   6.659  1.00 11.14           H  
ATOM   1860 HG23 ILE A 112      26.682  20.874   5.198  1.00 11.14           H  
ATOM   1861 HD11 ILE A 112      26.264  17.123   3.310  1.00 14.15           H  
ATOM   1862 HD12 ILE A 112      25.702  16.946   4.786  1.00 14.15           H  
ATOM   1863 HD13 ILE A 112      25.371  18.264   3.963  1.00 14.15           H  
ATOM   1864  N   HIS A 113      27.986  20.138   8.910  1.00  8.18           N  
ANISOU 1864  N   HIS A 113      853    757   1499      4     15   -153       N  
ATOM   1865  CA  HIS A 113      27.858  21.128   9.980  1.00  9.29           C  
ANISOU 1865  CA  HIS A 113     1045    837   1648     27    202   -185       C  
ATOM   1866  C   HIS A 113      29.188  21.815  10.278  1.00  8.10           C  
ANISOU 1866  C   HIS A 113      967    756   1353     14    116   -123       C  
ATOM   1867  O   HIS A 113      29.256  23.046  10.416  1.00  8.78           O  
ANISOU 1867  O   HIS A 113     1044    738   1554    106    122    -96       O  
ATOM   1868  CB AHIS A 113      27.206  20.532  11.221  0.46 11.24           C  
ANISOU 1868  CB AHIS A 113     1206   1021   2044    -82    538   -206       C  
ATOM   1869  CB BHIS A 113      27.370  20.417  11.264  0.54 10.62           C  
ANISOU 1869  CB BHIS A 113     1346   1126   1564    -82    413   -286       C  
ATOM   1870  CG AHIS A 113      26.565  21.570  12.082  0.46 13.07           C  
ANISOU 1870  CG AHIS A 113     1540   1174   2253    208    569   -247       C  
ATOM   1871  CG BHIS A 113      27.246  21.315  12.468  0.54 12.80           C  
ANISOU 1871  CG BHIS A 113     1757   1475   1631    183    462    -30       C  
ATOM   1872  ND1AHIS A 113      25.258  21.989  11.927  0.46 13.36           N  
ANISOU 1872  ND1AHIS A 113     1686   1216   2172    332    773   -279       N  
ATOM   1873  ND1BHIS A 113      28.261  21.523  13.383  0.54 15.01           N  
ANISOU 1873  ND1BHIS A 113     2147   1674   1881    494    648   -174       N  
ATOM   1874  CD2AHIS A 113      27.085  22.319  13.077  0.46 13.31           C  
ANISOU 1874  CD2AHIS A 113     1730   1211   2117    346     68   -503       C  
ATOM   1875  CD2BHIS A 113      26.198  22.046  12.913  0.54 13.79           C  
ANISOU 1875  CD2BHIS A 113     2022   1699   1517    814    401   -280       C  
ATOM   1876  CE1AHIS A 113      24.996  22.930  12.815  0.46 12.61           C  
ANISOU 1876  CE1AHIS A 113     1577   1297   1920    317    447   -321       C  
ATOM   1877  CE1BHIS A 113      27.851  22.361  14.321  0.54 14.86           C  
ANISOU 1877  CE1BHIS A 113     2281   1759   1604    593    267   -396       C  
ATOM   1878  NE2AHIS A 113      26.089  23.151  13.523  0.46 14.47           N  
ANISOU 1878  NE2AHIS A 113     1838   1413   2248    629     45   -564       N  
ATOM   1879  NE2BHIS A 113      26.605  22.696  14.054  0.54 15.65           N  
ANISOU 1879  NE2BHIS A 113     2333   1892   1721    839    434   -548       N  
ATOM   1880  H   HIS A 113      27.782  19.336   9.144  1.00  9.82           H  
ATOM   1881  HA  HIS A 113      27.238  21.814   9.688  1.00 11.15           H  
ATOM   1882  HB2AHIS A 113      26.521  19.902  10.948  0.46 13.49           H  
ATOM   1883  HB2BHIS A 113      26.496  20.033  11.092  0.54 12.74           H  
ATOM   1884  HB3AHIS A 113      27.883  20.080  11.749  0.46 13.49           H  
ATOM   1885  HB3BHIS A 113      27.998  19.712  11.486  0.54 12.74           H  
ATOM   1886  HD2AHIS A 113      27.953  22.271  13.408  0.46 15.97           H  
ATOM   1887  HD2BHIS A 113      25.364  22.116  12.507  0.54 16.54           H  
ATOM   1888  HE1AHIS A 113      24.182  23.367  12.921  0.46 15.14           H  
ATOM   1889  HE1BHIS A 113      28.354  22.658  15.045  0.54 17.83           H  
ATOM   1890  HE2AHIS A 113      26.163  23.721  14.162  0.46 17.37           H  
ATOM   1891  HE2BHIS A 113      26.118  23.223  14.528  0.54 18.78           H  
ATOM   1892  N   VAL A 114      30.255  21.025  10.418  1.00  7.46           N  
ANISOU 1892  N   VAL A 114      854    632   1347      6     87    -86       N  
ATOM   1893  CA  VAL A 114      31.564  21.583  10.755  1.00  7.51           C  
ANISOU 1893  CA  VAL A 114      902    747   1205    -24     52   -103       C  
ATOM   1894  C   VAL A 114      32.119  22.442   9.620  1.00  7.00           C  
ANISOU 1894  C   VAL A 114      892    708   1060     36    -83    -92       C  
ATOM   1895  O   VAL A 114      32.708  23.505   9.863  1.00  8.23           O  
ANISOU 1895  O   VAL A 114     1071    698   1357    -88   -119    -95       O  
ATOM   1896  CB  VAL A 114      32.530  20.454  11.167  1.00  7.94           C  
ANISOU 1896  CB  VAL A 114     1090    776   1151    -40    -52    -33       C  
ATOM   1897  CG1 VAL A 114      33.960  20.948  11.277  1.00  8.88           C  
ANISOU 1897  CG1 VAL A 114     1082    965   1329     30   -175     46       C  
ATOM   1898  CG2 VAL A 114      32.058  19.849  12.499  1.00  8.63           C  
ANISOU 1898  CG2 VAL A 114     1155    895   1227    -84   -109    -60       C  
ATOM   1899  H   VAL A 114      30.246  20.171  10.323  1.00  8.95           H  
ATOM   1900  HA  VAL A 114      31.456  22.163  11.526  1.00  9.01           H  
ATOM   1901  HB  VAL A 114      32.505  19.755  10.494  1.00  9.53           H  
ATOM   1902 HG11 VAL A 114      34.531  20.208  11.537  1.00 10.66           H  
ATOM   1903 HG12 VAL A 114      34.241  21.297  10.417  1.00 10.66           H  
ATOM   1904 HG13 VAL A 114      34.000  21.649  11.948  1.00 10.66           H  
ATOM   1905 HG21 VAL A 114      32.667  19.139  12.756  1.00 10.35           H  
ATOM   1906 HG22 VAL A 114      32.054  20.543  13.177  1.00 10.35           H  
ATOM   1907 HG23 VAL A 114      31.163  19.493  12.384  1.00 10.35           H  
ATOM   1908  N   LEU A 115      31.978  22.000   8.372  1.00  7.05           N  
ANISOU 1908  N   LEU A 115      858    715   1106     20     60    -34       N  
ATOM   1909  CA  LEU A 115      32.448  22.806   7.247  1.00  7.26           C  
ANISOU 1909  CA  LEU A 115      917    710   1133     13    -40    -14       C  
ATOM   1910  C   LEU A 115      31.673  24.106   7.145  1.00  7.44           C  
ANISOU 1910  C   LEU A 115      953    598   1277     58     -6    -26       C  
ATOM   1911  O   LEU A 115      32.252  25.159   6.861  1.00  8.05           O  
ANISOU 1911  O   LEU A 115     1086    676   1298    -79    -45    -20       O  
ATOM   1912  CB  LEU A 115      32.400  21.998   5.940  1.00  8.01           C  
ANISOU 1912  CB  LEU A 115     1184    662   1197     -1    -26    -61       C  
ATOM   1913  CG  LEU A 115      33.612  21.095   5.635  1.00 12.50           C  
ANISOU 1913  CG  LEU A 115     1878   1387   1483    708   -207   -401       C  
ATOM   1914  CD1 LEU A 115      34.217  20.308   6.790  1.00 15.91           C  
ANISOU 1914  CD1 LEU A 115     1747   2049   2250    721   -172   -704       C  
ATOM   1915  CD2 LEU A 115      33.287  20.202   4.446  1.00 12.22           C  
ANISOU 1915  CD2 LEU A 115     2035   1153   1456    718     93   -154       C  
ATOM   1916  H   LEU A 115      31.620  21.250   8.151  1.00  8.46           H  
ATOM   1917  HA  LEU A 115      33.377  23.037   7.406  1.00  8.72           H  
ATOM   1918  HB2 LEU A 115      31.617  21.426   5.968  1.00  9.61           H  
ATOM   1919  HB3 LEU A 115      32.315  22.622   5.202  1.00  9.61           H  
ATOM   1920  HG  LEU A 115      34.320  21.684   5.331  1.00 14.99           H  
ATOM   1921 HD11 LEU A 115      34.966  19.788   6.459  1.00 19.10           H  
ATOM   1922 HD12 LEU A 115      34.521  20.930   7.470  1.00 19.10           H  
ATOM   1923 HD13 LEU A 115      33.541  19.719   7.158  1.00 19.10           H  
ATOM   1924 HD21 LEU A 115      34.052  19.636   4.258  1.00 14.67           H  
ATOM   1925 HD22 LEU A 115      32.516  19.655   4.664  1.00 14.67           H  
ATOM   1926 HD23 LEU A 115      33.091  20.760   3.677  1.00 14.67           H  
ATOM   1927  N   HIS A 116      30.372  24.069   7.405  1.00  7.91           N  
ANISOU 1927  N   HIS A 116      929    649   1426    134    -53   -125       N  
ATOM   1928  CA  HIS A 116      29.584  25.295   7.393  1.00  8.62           C  
ANISOU 1928  CA  HIS A 116      915    759   1602     16    -13   -112       C  
ATOM   1929  C   HIS A 116      30.067  26.275   8.465  1.00  8.52           C  
ANISOU 1929  C   HIS A 116      976    630   1632    -75     14   -165       C  
ATOM   1930  O   HIS A 116      30.123  27.490   8.226  1.00  9.74           O  
ANISOU 1930  O   HIS A 116     1250    717   1732     60     44   -271       O  
ATOM   1931  CB  HIS A 116      28.101  24.933   7.563  1.00  8.89           C  
ANISOU 1931  CB  HIS A 116      950    908   1519     91    -91    -90       C  
ATOM   1932  CG  HIS A 116      27.195  26.106   7.696  1.00 10.31           C  
ANISOU 1932  CG  HIS A 116     1074    980   1862    202   -218   -199       C  
ATOM   1933  ND1 HIS A 116      26.767  26.568   8.917  1.00 11.54           N  
ANISOU 1933  ND1 HIS A 116     1117   1090   2178    290    163    -18       N  
ATOM   1934  CD2 HIS A 116      26.596  26.882   6.766  1.00 13.58           C  
ANISOU 1934  CD2 HIS A 116     1479   1377   2304    644   -374   -340       C  
ATOM   1935  CE1 HIS A 116      25.978  27.611   8.736  1.00 12.86           C  
ANISOU 1935  CE1 HIS A 116     1234   1150   2502    288    206   -196       C  
ATOM   1936  NE2 HIS A 116      25.858  27.825   7.440  1.00 14.08           N  
ANISOU 1936  NE2 HIS A 116     1465   1229   2654    439   -202   -441       N  
ATOM   1937  H   HIS A 116      29.926  23.358   7.590  1.00  9.49           H  
ATOM   1938  HA  HIS A 116      29.688  25.726   6.530  1.00 10.35           H  
ATOM   1939  HB2 HIS A 116      27.814  24.426   6.788  1.00 10.66           H  
ATOM   1940  HB3 HIS A 116      28.002  24.393   8.362  1.00 10.66           H  
ATOM   1941  HD1 HIS A 116      27.002  26.248   9.680  1.00 13.85           H  
ATOM   1942  HD2 HIS A 116      26.693  26.814   5.844  1.00 16.30           H  
ATOM   1943  HE1 HIS A 116      25.566  28.103   9.409  1.00 15.43           H  
ATOM   1944  N   SER A 117      30.413  25.766   9.657  1.00  8.01           N  
ANISOU 1944  N   SER A 117      907    717   1419    -94     72   -185       N  
ATOM   1945  CA  SER A 117      30.881  26.611  10.761  1.00  9.24           C  
ANISOU 1945  CA  SER A 117     1110    941   1460    -73     96   -285       C  
ATOM   1946  C   SER A 117      32.264  27.188  10.492  1.00  8.20           C  
ANISOU 1946  C   SER A 117      992    788   1337    -31    -59   -148       C  
ATOM   1947  O   SER A 117      32.522  28.375  10.744  1.00  9.74           O  
ANISOU 1947  O   SER A 117     1041    845   1816    -15     -7   -330       O  
ATOM   1948  CB ASER A 117      30.886  25.797  12.058  0.64 11.03           C  
ANISOU 1948  CB ASER A 117     1383   1479   1329   -364    276   -338       C  
ATOM   1949  CB CSER A 117      30.931  25.788  12.054  0.36 10.92           C  
ANISOU 1949  CB CSER A 117     1297   1372   1481   -171    126   -286       C  
ATOM   1950  OG ASER A 117      31.367  26.580  13.135  0.64 13.67           O  
ANISOU 1950  OG ASER A 117     1785   1807   1601   -293    127   -455       O  
ATOM   1951  OG CSER A 117      29.647  25.397  12.491  0.36 12.92           O  
ANISOU 1951  OG CSER A 117     1531   1609   1770   -109     27   -421       O  
ATOM   1952  H   SER A 117      30.384  24.929   9.849  1.00  9.61           H  
ATOM   1953  HA  SER A 117      30.264  27.351  10.877  1.00 11.09           H  
ATOM   1954  HB2ASER A 117      29.981  25.510  12.255  0.64 13.23           H  
ATOM   1955  HB2CSER A 117      31.461  24.992  11.895  0.36 13.11           H  
ATOM   1956  HB3ASER A 117      31.463  25.026  11.945  0.64 13.23           H  
ATOM   1957  HB3CSER A 117      31.346  26.325  12.747  0.36 13.11           H  
ATOM   1958  HG ASER A 117      32.150  26.836  12.976  0.64 16.40           H  
ATOM   1959  HG CSER A 117      29.274  24.927  11.903  0.36 15.51           H  
ATOM   1960  N   ARG A 118      33.198  26.334  10.067  1.00  7.69           N  
ANISOU 1960  N   ARG A 118      896    753   1273     21     15    -41       N  
ATOM   1961  CA  ARG A 118      34.599  26.725   9.950  1.00  7.21           C  
ANISOU 1961  CA  ARG A 118      854    665   1221     -2   -109   -115       C  
ATOM   1962  C   ARG A 118      34.917  27.463   8.656  1.00  7.35           C  
ANISOU 1962  C   ARG A 118      876    553   1364   -101    -85    -77       C  
ATOM   1963  O   ARG A 118      35.861  28.253   8.649  1.00  8.10           O  
ANISOU 1963  O   ARG A 118      988    805   1284   -181   -123     -9       O  
ATOM   1964  CB AARG A 118      35.516  25.509  10.107  0.70  8.13           C  
ANISOU 1964  CB AARG A 118     1079    780   1230     83    -28    -89       C  
ATOM   1965  CB BARG A 118      35.497  25.491   9.985  0.30  7.76           C  
ANISOU 1965  CB BARG A 118      902    814   1232    -83    131     38       C  
ATOM   1966  CG AARG A 118      35.471  24.890  11.491  0.70  9.22           C  
ANISOU 1966  CG AARG A 118     1104    946   1452    107    -87     -9       C  
ATOM   1967  CG BARG A 118      35.867  24.966  11.351  0.30  8.06           C  
ANISOU 1967  CG BARG A 118      881    915   1267    -90    324     82       C  
ATOM   1968  CD AARG A 118      36.463  23.752  11.712  0.70  9.14           C  
ANISOU 1968  CD AARG A 118     1033   1000   1439    -60     -5    161       C  
ATOM   1969  CD BARG A 118      36.701  23.708  11.183  0.30  9.27           C  
ANISOU 1969  CD BARG A 118      919    978   1626    -90    281     92       C  
ATOM   1970  NE AARG A 118      37.865  24.159  11.593  0.70  9.18           N  
ANISOU 1970  NE AARG A 118     1084   1004   1399      9   -110    182       N  
ATOM   1971  NE BARG A 118      37.293  23.216  12.429  0.30  9.89           N  
ANISOU 1971  NE BARG A 118     1036   1032   1689    -49    115      4       N  
ATOM   1972  CZ AARG A 118      38.883  23.604  12.256  0.70 10.74           C  
ANISOU 1972  CZ AARG A 118     1170    973   1939    -13   -228     67       C  
ATOM   1973  CZ BARG A 118      38.580  23.308  12.757  0.30  9.62           C  
ANISOU 1973  CZ BARG A 118     1173    942   1542   -155     35   -123       C  
ATOM   1974  NH1AARG A 118      40.121  24.044  12.053  0.70 12.40           N  
ANISOU 1974  NH1AARG A 118     1232   1069   2409   -174   -428    -31       N  
ATOM   1975  NH1BARG A 118      39.000  22.796  13.906  0.30  9.97           N  
ANISOU 1975  NH1BARG A 118     1292   1038   1457    -85    182   -269       N  
ATOM   1976  NH2AARG A 118      38.684  22.623  13.131  0.70 11.82           N  
ANISOU 1976  NH2AARG A 118     1277    940   2272     87   -502     16       N  
ATOM   1977  NH2BARG A 118      39.453  23.900  11.955  0.30 10.25           N  
ANISOU 1977  NH2BARG A 118     1257   1069   1568   -158   -265   -224       N  
ATOM   1978  H   ARG A 118      33.043  25.519   9.841  1.00  9.23           H  
ATOM   1979  HA  ARG A 118      34.814  27.320  10.685  1.00  8.65           H  
ATOM   1980  HB2AARG A 118      35.249  24.830   9.468  0.70  9.76           H  
ATOM   1981  HB2BARG A 118      35.045  24.773   9.514  0.30  9.31           H  
ATOM   1982  HB3AARG A 118      36.431  25.783   9.933  0.70  9.76           H  
ATOM   1983  HB3BARG A 118      36.324  25.705   9.525  0.30  9.31           H  
ATOM   1984  HG2AARG A 118      35.664  25.579  12.145  0.70 11.06           H  
ATOM   1985  HG2BARG A 118      36.393  25.628  11.826  0.30  9.67           H  
ATOM   1986  HG3AARG A 118      34.581  24.536  11.643  0.70 11.06           H  
ATOM   1987  HG3BARG A 118      35.063  24.744  11.846  0.30  9.67           H  
ATOM   1988  HD2AARG A 118      36.334  23.394  12.604  0.70 10.97           H  
ATOM   1989  HD2BARG A 118      36.136  23.005  10.825  0.30 11.13           H  
ATOM   1990  HD3AARG A 118      36.298  23.061  11.053  0.70 10.97           H  
ATOM   1991  HD3BARG A 118      37.425  23.894  10.565  0.30 11.13           H  
ATOM   1992  HE AARG A 118      38.047  24.804  11.054  0.70 11.01           H  
ATOM   1993  HE BARG A 118      36.767  22.836  12.994  0.30 11.87           H  
ATOM   1994 HH11AARG A 118      40.264  24.683  11.495  0.70 14.87           H  
ATOM   1995 HH11BARG A 118      38.441  22.415  14.437  0.30 11.96           H  
ATOM   1996 HH12AARG A 118      40.778  23.697  12.486  0.70 14.87           H  
ATOM   1997 HH12BARG A 118      39.828  22.863  14.129  0.30 11.96           H  
ATOM   1998 HH21AARG A 118      37.890  22.325  13.270  0.70 14.18           H  
ATOM   1999 HH21BARG A 118      39.194  24.228  11.204  0.30 12.30           H  
ATOM   2000 HH22AARG A 118      39.351  22.281  13.552  0.70 14.18           H  
ATOM   2001 HH22BARG A 118      40.280  23.953  12.185  0.30 12.30           H  
ATOM   2002  N   HIS A 119      34.169  27.214   7.564  1.00  7.44           N  
ANISOU 2002  N   HIS A 119      906    697   1224     17    -42   -105       N  
ATOM   2003  CA  HIS A 119      34.553  27.653   6.213  1.00  8.19           C  
ANISOU 2003  CA  HIS A 119     1003    741   1369    -49    -11    -98       C  
ATOM   2004  C   HIS A 119      33.419  28.368   5.484  1.00  8.00           C  
ANISOU 2004  C   HIS A 119     1154    611   1275   -260    -71     22       C  
ATOM   2005  O   HIS A 119      33.101  28.046   4.340  1.00  9.23           O  
ANISOU 2005  O   HIS A 119     1520    726   1260   -170   -247    -48       O  
ATOM   2006  CB  HIS A 119      35.037  26.461   5.390  1.00  8.57           C  
ANISOU 2006  CB  HIS A 119     1092    838   1328   -106    182    -93       C  
ATOM   2007  CG  HIS A 119      36.230  25.828   6.000  1.00  8.82           C  
ANISOU 2007  CG  HIS A 119     1176    725   1449   -123    265   -158       C  
ATOM   2008  ND1 HIS A 119      37.430  26.495   6.087  1.00  9.83           N  
ANISOU 2008  ND1 HIS A 119     1128    827   1777     98    286     89       N  
ATOM   2009  CD2 HIS A 119      36.391  24.651   6.643  1.00  9.85           C  
ANISOU 2009  CD2 HIS A 119     1462    746   1537   -128    410    -85       C  
ATOM   2010  CE1 HIS A 119      38.291  25.732   6.736  1.00 10.67           C  
ANISOU 2010  CE1 HIS A 119     1090   1031   1933    229    242    233       C  
ATOM   2011  NE2 HIS A 119      37.685  24.611   7.085  1.00 10.43           N  
ANISOU 2011  NE2 HIS A 119     1409    889   1664    264    551    122       N  
ATOM   2012  H   HIS A 119      33.424  26.785   7.584  1.00  8.93           H  
ATOM   2013  HA  HIS A 119      35.292  28.277   6.289  1.00  9.83           H  
ATOM   2014  HB2 HIS A 119      34.332  25.796   5.344  1.00 10.29           H  
ATOM   2015  HB3 HIS A 119      35.274  26.761   4.499  1.00 10.29           H  
ATOM   2016  HD2 HIS A 119      35.746  23.991   6.760  1.00 11.82           H  
ATOM   2017  HE1 HIS A 119      39.180  25.944   6.909  1.00 12.80           H  
ATOM   2018  HE2 HIS A 119      38.050  23.954   7.504  1.00 12.51           H  
ATOM   2019  N   PRO A 120      32.829  29.401   6.085  1.00  8.85           N  
ANISOU 2019  N   PRO A 120     1243    802   1318    -31   -189    -68       N  
ATOM   2020  CA  PRO A 120      31.771  30.114   5.352  1.00 12.05           C  
ANISOU 2020  CA  PRO A 120     1870   1003   1703    334   -583   -115       C  
ATOM   2021  C   PRO A 120      32.243  30.699   4.016  1.00 14.58           C  
ANISOU 2021  C   PRO A 120     2591   1531   1418    737   -893   -167       C  
ATOM   2022  O   PRO A 120      31.447  30.740   3.075  1.00 21.00           O  
ANISOU 2022  O   PRO A 120     3487   2334   2159   1526   -881   -355       O  
ATOM   2023  CB  PRO A 120      31.303  31.179   6.352  1.00 13.37           C  
ANISOU 2023  CB  PRO A 120     1957   1225   1899    526   -573   -168       C  
ATOM   2024  CG  PRO A 120      32.455  31.364   7.263  1.00 11.57           C  
ANISOU 2024  CG  PRO A 120     1790   1040   1566    444   -315   -240       C  
ATOM   2025  CD  PRO A 120      33.093  30.017   7.401  1.00  9.08           C  
ANISOU 2025  CD  PRO A 120     1241    852   1356    -51   -114   -104       C  
ATOM   2026  HA  PRO A 120      31.033  29.509   5.179  1.00 14.45           H  
ATOM   2027  HB2 PRO A 120      31.098  32.003   5.883  1.00 16.05           H  
ATOM   2028  HB3 PRO A 120      30.528  30.856   6.838  1.00 16.05           H  
ATOM   2029  HG2 PRO A 120      33.078  31.997   6.873  1.00 13.88           H  
ATOM   2030  HG3 PRO A 120      32.140  31.682   8.124  1.00 13.88           H  
ATOM   2031  HD2 PRO A 120      34.047  30.106   7.550  1.00 10.89           H  
ATOM   2032  HD3 PRO A 120      32.665  29.508   8.107  1.00 10.89           H  
ATOM   2033  N   GLY A 121      33.543  31.008   3.864  1.00 15.35           N  
ANISOU 2033  N   GLY A 121     3148    978   1704     10   -581    136       N  
ATOM   2034  CA  GLY A 121      34.094  31.552   2.616  1.00 15.57           C  
ANISOU 2034  CA  GLY A 121     3078   1276   1564   -263   -262    -45       C  
ATOM   2035  C   GLY A 121      34.234  30.551   1.498  1.00 14.86           C  
ANISOU 2035  C   GLY A 121     2557   1680   1409   -377   -270      4       C  
ATOM   2036  O   GLY A 121      34.469  30.918   0.340  1.00 15.67           O  
ANISOU 2036  O   GLY A 121     2403   1752   1800   -460    -62    -19       O  
ATOM   2037  H   GLY A 121      34.132  30.907   4.482  1.00 18.41           H  
ATOM   2038  HA2 GLY A 121      33.521  32.270   2.305  1.00 18.69           H  
ATOM   2039  HA3 GLY A 121      34.971  31.925   2.796  1.00 18.69           H  
ATOM   2040  N   ASN A 122      34.096  29.298   1.810  1.00 12.27           N  
ANISOU 2040  N   ASN A 122     1861   1436   1364   -787   -211    178       N  
ATOM   2041  CA  ASN A 122      34.194  28.268   0.800  1.00 11.47           C  
ANISOU 2041  CA  ASN A 122     1384   1622   1352   -506   -117     94       C  
ATOM   2042  C   ASN A 122      33.071  27.259   0.926  1.00  9.22           C  
ANISOU 2042  C   ASN A 122     1097   1247   1162   -221   -137     19       C  
ATOM   2043  O   ASN A 122      33.144  26.188   0.308  1.00 10.06           O  
ANISOU 2043  O   ASN A 122      983   1401   1440   -122    -13   -386       O  
ATOM   2044  CB  ASN A 122      35.563  27.592   0.870  1.00 14.61           C  
ANISOU 2044  CB  ASN A 122     1378   2227   1944   -774   -213    546       C  
ATOM   2045  CG  ASN A 122      36.652  28.486   0.337  1.00 17.41           C  
ANISOU 2045  CG  ASN A 122     1736   2731   2146   -523   -249   1036       C  
ATOM   2046  OD1 ASN A 122      36.639  28.840  -0.830  1.00 22.30           O  
ANISOU 2046  OD1 ASN A 122     2026   3698   2751  -1133   -226   1333       O  
ATOM   2047  ND2 ASN A 122      37.555  28.898   1.190  1.00 15.01           N  
ANISOU 2047  ND2 ASN A 122     1343   2073   2286   -545   -157    162       N  
ATOM   2048  H   ASN A 122      33.944  29.004   2.604  1.00 14.72           H  
ATOM   2049  HA  ASN A 122      34.117  28.684  -0.073  1.00 13.76           H  
ATOM   2050  HB2 ASN A 122      35.769  27.382   1.795  1.00 17.53           H  
ATOM   2051  HB3 ASN A 122      35.547  26.782   0.337  1.00 17.53           H  
ATOM   2052 HD21 ASN A 122      38.194  29.409   0.926  1.00 18.01           H  
ATOM   2053 HD22 ASN A 122      37.510  28.656   2.014  1.00 18.01           H  
ATOM   2054  N   PHE A 123      32.035  27.574   1.696  1.00  8.59           N  
ANISOU 2054  N   PHE A 123     1091    815   1358    -89    -21   -133       N  
ATOM   2055  CA  PHE A 123      30.947  26.640   1.956  1.00  8.29           C  
ANISOU 2055  CA  PHE A 123      899    779   1471   -216    -34    -12       C  
ATOM   2056  C   PHE A 123      29.613  27.381   1.977  1.00  9.03           C  
ANISOU 2056  C   PHE A 123     1080    831   1520     31    -25   -103       C  
ATOM   2057  O   PHE A 123      28.798  27.205   2.883  1.00  9.62           O  
ANISOU 2057  O   PHE A 123     1054   1064   1536    150    -46   -181       O  
ATOM   2058  CB  PHE A 123      31.185  25.817   3.232  1.00  8.04           C  
ANISOU 2058  CB  PHE A 123      907    841   1307    -26    -62   -133       C  
ATOM   2059  CG  PHE A 123      30.592  24.422   3.191  1.00  7.72           C  
ANISOU 2059  CG  PHE A 123      885    773   1274    -88     19    -63       C  
ATOM   2060  CD1 PHE A 123      31.108  23.461   2.329  1.00  8.20           C  
ANISOU 2060  CD1 PHE A 123      901    706   1508     15     -1   -105       C  
ATOM   2061  CD2 PHE A 123      29.558  24.057   4.033  1.00  8.06           C  
ANISOU 2061  CD2 PHE A 123      899    817   1347    -57    -32   -185       C  
ATOM   2062  CE1 PHE A 123      30.599  22.171   2.316  1.00  8.84           C  
ANISOU 2062  CE1 PHE A 123      986    928   1444    106   -114   -261       C  
ATOM   2063  CE2 PHE A 123      29.064  22.762   4.031  1.00  8.19           C  
ANISOU 2063  CE2 PHE A 123      894    996   1221   -116    -44    -78       C  
ATOM   2064  CZ  PHE A 123      29.588  21.820   3.168  1.00  9.21           C  
ANISOU 2064  CZ  PHE A 123     1015    902   1584    -22   -105    -92       C  
ATOM   2065  H   PHE A 123      31.938  28.335   2.085  1.00 10.31           H  
ATOM   2066  HA  PHE A 123      30.910  26.012   1.218  1.00  9.95           H  
ATOM   2067  HB2 PHE A 123      32.141  25.728   3.371  1.00  9.65           H  
ATOM   2068  HB3 PHE A 123      30.787  26.285   3.983  1.00  9.65           H  
ATOM   2069  HD1 PHE A 123      31.808  23.684   1.759  1.00  9.84           H  
ATOM   2070  HD2 PHE A 123      29.213  24.679   4.632  1.00  9.68           H  
ATOM   2071  HE1 PHE A 123      30.953  21.540   1.732  1.00 10.60           H  
ATOM   2072  HE2 PHE A 123      28.365  22.532   4.599  1.00  9.83           H  
ATOM   2073  HZ  PHE A 123      29.237  20.959   3.146  1.00 11.06           H  
ATOM   2074  N   GLY A 124      29.376  28.188   0.944  1.00  9.80           N  
ANISOU 2074  N   GLY A 124     1193    838   1693     21    -64    133       N  
ATOM   2075  CA  GLY A 124      28.073  28.759   0.681  1.00 10.46           C  
ANISOU 2075  CA  GLY A 124     1221    920   1832    137   -204    -81       C  
ATOM   2076  C   GLY A 124      27.108  27.691   0.169  1.00  9.20           C  
ANISOU 2076  C   GLY A 124     1196    761   1538     90    -91    -26       C  
ATOM   2077  O   GLY A 124      27.409  26.498   0.139  1.00  8.99           O  
ANISOU 2077  O   GLY A 124     1192    714   1511    188    -50    -86       O  
ATOM   2078  H   GLY A 124      29.975  28.421   0.372  1.00 11.76           H  
ATOM   2079  HA2 GLY A 124      27.711  29.143   1.495  1.00 12.55           H  
ATOM   2080  HA3 GLY A 124      28.149  29.458   0.012  1.00 12.55           H  
ATOM   2081  N   ALA A 125      25.918  28.130  -0.247  1.00 10.04           N  
ANISOU 2081  N   ALA A 125     1270    766   1779    323   -283    -27       N  
ATOM   2082  CA  ALA A 125      24.843  27.185  -0.565  1.00 10.56           C  
ANISOU 2082  CA  ALA A 125     1170   1030   1814    275   -198   -101       C  
ATOM   2083  C   ALA A 125      25.231  26.223  -1.693  1.00  9.67           C  
ANISOU 2083  C   ALA A 125     1189    916   1569    334   -286     21       C  
ATOM   2084  O   ALA A 125      24.993  25.012  -1.602  1.00  9.99           O  
ANISOU 2084  O   ALA A 125     1230    863   1703    340   -243    -54       O  
ATOM   2085  CB  ALA A 125      23.569  27.945  -0.916  1.00 11.62           C  
ANISOU 2085  CB  ALA A 125     1286   1263   1867    505   -264    -86       C  
ATOM   2086  H   ALA A 125      25.708  28.958  -0.352  1.00 12.05           H  
ATOM   2087  HA  ALA A 125      24.658  26.651   0.223  1.00 12.68           H  
ATOM   2088  HB1 ALA A 125      22.868  27.306  -1.124  1.00 13.95           H  
ATOM   2089  HB2 ALA A 125      23.307  28.488  -0.157  1.00 13.95           H  
ATOM   2090  HB3 ALA A 125      23.740  28.510  -1.685  1.00 13.95           H  
ATOM   2091  N   ASP A 126      25.793  26.740  -2.787  1.00 10.09           N  
ANISOU 2091  N   ASP A 126     1522    737   1576    228   -275    -16       N  
ATOM   2092  CA  ASP A 126      26.162  25.866  -3.904  1.00 10.39           C  
ANISOU 2092  CA  ASP A 126     1563    970   1413    296   -301      8       C  
ATOM   2093  C   ASP A 126      27.243  24.869  -3.492  1.00  9.27           C  
ANISOU 2093  C   ASP A 126     1396    977   1150    276   -170     57       C  
ATOM   2094  O   ASP A 126      27.180  23.686  -3.859  1.00  9.28           O  
ANISOU 2094  O   ASP A 126     1364    798   1363    218    -95   -135       O  
ATOM   2095  CB  ASP A 126      26.634  26.680  -5.115  1.00 12.90           C  
ANISOU 2095  CB  ASP A 126     2106   1168   1628    377   -419    145       C  
ATOM   2096  CG  ASP A 126      25.520  27.489  -5.779  1.00 16.57           C  
ANISOU 2096  CG  ASP A 126     2591   1697   2007    425   -690    358       C  
ATOM   2097  OD1 ASP A 126      25.856  28.395  -6.568  1.00 22.13           O  
ANISOU 2097  OD1 ASP A 126     3126   2316   2966    263   -874    718       O  
ATOM   2098  OD2 ASP A 126      24.323  27.223  -5.556  1.00 16.94           O  
ANISOU 2098  OD2 ASP A 126     2354   2011   2072    828   -631    217       O  
ATOM   2099  H   ASP A 126      25.968  27.573  -2.907  1.00 12.11           H  
ATOM   2100  HA  ASP A 126      25.380  25.360  -4.174  1.00 12.46           H  
ATOM   2101  HB2 ASP A 126      27.321  27.301  -4.826  1.00 15.48           H  
ATOM   2102  HB3 ASP A 126      26.997  26.073  -5.778  1.00 15.48           H  
ATOM   2103  N   ALA A 127      28.241  25.316  -2.716  1.00  9.06           N  
ANISOU 2103  N   ALA A 127     1317    831   1295    207    -98    -54       N  
ATOM   2104  CA  ALA A 127      29.292  24.402  -2.270  1.00  8.65           C  
ANISOU 2104  CA  ALA A 127     1197    861   1228    147   -121     27       C  
ATOM   2105  C   ALA A 127      28.751  23.340  -1.328  1.00  8.28           C  
ANISOU 2105  C   ALA A 127     1071    784   1293     85    -71   -173       C  
ATOM   2106  O   ALA A 127      29.142  22.169  -1.414  1.00  8.05           O  
ANISOU 2106  O   ALA A 127     1056    681   1323    171     27   -170       O  
ATOM   2107  CB  ALA A 127      30.413  25.173  -1.597  1.00  9.46           C  
ANISOU 2107  CB  ALA A 127     1295    952   1349    120     19      5       C  
ATOM   2108  H   ALA A 127      28.328  26.127  -2.442  1.00 10.87           H  
ATOM   2109  HA  ALA A 127      29.664  23.951  -3.044  1.00 10.38           H  
ATOM   2110  HB1 ALA A 127      31.097  24.548  -1.310  1.00 11.36           H  
ATOM   2111  HB2 ALA A 127      30.787  25.804  -2.232  1.00 11.36           H  
ATOM   2112  HB3 ALA A 127      30.054  25.646  -0.830  1.00 11.36           H  
ATOM   2113  N   GLN A 128      27.850  23.725  -0.418  1.00  8.29           N  
ANISOU 2113  N   GLN A 128     1078    790   1283    227    -69    -55       N  
ATOM   2114  CA  GLN A 128      27.244  22.744   0.476  1.00  8.43           C  
ANISOU 2114  CA  GLN A 128     1092    765   1346    254    -43     -9       C  
ATOM   2115  C   GLN A 128      26.410  21.725  -0.305  1.00  8.20           C  
ANISOU 2115  C   GLN A 128      999    671   1444    161    -10    -80       C  
ATOM   2116  O   GLN A 128      26.432  20.529   0.001  1.00  8.29           O  
ANISOU 2116  O   GLN A 128     1033    724   1392    221     -3    -25       O  
ATOM   2117  CB  GLN A 128      26.420  23.437   1.566  1.00  8.43           C  
ANISOU 2117  CB  GLN A 128      923    896   1386    216   -107    -59       C  
ATOM   2118  CG  GLN A 128      25.726  22.465   2.492  1.00  8.41           C  
ANISOU 2118  CG  GLN A 128      998    892   1306    311     11    -63       C  
ATOM   2119  CD  GLN A 128      25.105  23.110   3.716  1.00  9.50           C  
ANISOU 2119  CD  GLN A 128     1216   1051   1341    416    -80    -96       C  
ATOM   2120  OE1 GLN A 128      25.557  24.167   4.196  1.00 11.12           O  
ANISOU 2120  OE1 GLN A 128     1551   1079   1597    432     75   -188       O  
ATOM   2121  NE2 GLN A 128      24.064  22.485   4.232  1.00 10.49           N  
ANISOU 2121  NE2 GLN A 128     1045   1375   1566    454    147     48       N  
ATOM   2122  H   GLN A 128      27.580  24.533  -0.303  1.00  9.95           H  
ATOM   2123  HA  GLN A 128      27.955  22.255   0.919  1.00 10.12           H  
ATOM   2124  HB2 GLN A 128      27.009  23.991   2.101  1.00 10.12           H  
ATOM   2125  HB3 GLN A 128      25.740  23.987   1.145  1.00 10.12           H  
ATOM   2126  HG2 GLN A 128      25.017  22.019   2.001  1.00 10.10           H  
ATOM   2127  HG3 GLN A 128      26.373  21.811   2.799  1.00 10.10           H  
ATOM   2128 HE21 GLN A 128      23.778  21.758   3.873  1.00 12.59           H  
ATOM   2129 HE22 GLN A 128      23.671  22.805   4.926  1.00 12.59           H  
ATOM   2130  N   GLY A 129      25.667  22.179  -1.318  1.00  8.89           N  
ANISOU 2130  N   GLY A 129     1077    775   1527    272   -108      8       N  
ATOM   2131  CA  GLY A 129      24.917  21.247  -2.147  1.00  8.56           C  
ANISOU 2131  CA  GLY A 129     1063    729   1462    220   -112    -44       C  
ATOM   2132  C   GLY A 129      25.815  20.258  -2.876  1.00  8.45           C  
ANISOU 2132  C   GLY A 129     1024    737   1450    339   -249     -3       C  
ATOM   2133  O   GLY A 129      25.495  19.070  -2.980  1.00  9.04           O  
ANISOU 2133  O   GLY A 129     1132    774   1529    265   -119    -80       O  
ATOM   2134  H   GLY A 129      25.585  23.006  -1.539  1.00 10.67           H  
ATOM   2135  HA2 GLY A 129      24.298  20.748  -1.592  1.00 10.27           H  
ATOM   2136  HA3 GLY A 129      24.407  21.742  -2.808  1.00 10.27           H  
ATOM   2137  N   ALA A 130      26.954  20.732  -3.392  1.00  8.15           N  
ANISOU 2137  N   ALA A 130     1083    707   1306    254   -173    -71       N  
ATOM   2138  CA  ALA A 130      27.909  19.856  -4.063  1.00  8.17           C  
ANISOU 2138  CA  ALA A 130     1194    798   1111    283   -114   -115       C  
ATOM   2139  C   ALA A 130      28.488  18.824  -3.100  1.00  7.57           C  
ANISOU 2139  C   ALA A 130     1078    697   1103    119    -13   -107       C  
ATOM   2140  O   ALA A 130      28.619  17.642  -3.449  1.00  7.96           O  
ANISOU 2140  O   ALA A 130     1062    736   1227    146    -50   -104       O  
ATOM   2141  CB  ALA A 130      29.005  20.703  -4.715  1.00  8.95           C  
ANISOU 2141  CB  ALA A 130     1275    836   1288    353    -42     26       C  
ATOM   2142  H   ALA A 130      27.194  21.557  -3.364  1.00  9.78           H  
ATOM   2143  HA  ALA A 130      27.448  19.375  -4.768  1.00  9.80           H  
ATOM   2144  HB1 ALA A 130      29.636  20.114  -5.159  1.00 10.74           H  
ATOM   2145  HB2 ALA A 130      28.599  21.301  -5.361  1.00 10.74           H  
ATOM   2146  HB3 ALA A 130      29.458  21.216  -4.028  1.00 10.74           H  
ATOM   2147  N   MET A 131      28.859  19.259  -1.887  1.00  7.66           N  
ANISOU 2147  N   MET A 131      990    762   1157    204    -34    -73       N  
ATOM   2148  CA  MET A 131      29.366  18.320  -0.887  1.00  7.64           C  
ANISOU 2148  CA  MET A 131      888    814   1201    198   -103      1       C  
ATOM   2149  C   MET A 131      28.303  17.304  -0.500  1.00  7.20           C  
ANISOU 2149  C   MET A 131      768    707   1259    196     -4   -194       C  
ATOM   2150  O   MET A 131      28.602  16.108  -0.383  1.00  7.60           O  
ANISOU 2150  O   MET A 131      907    651   1331    145    -45    -90       O  
ATOM   2151  CB  MET A 131      29.873  19.075   0.341  1.00  7.80           C  
ANISOU 2151  CB  MET A 131      906    863   1193    114    -47    -85       C  
ATOM   2152  CG  MET A 131      30.434  18.181   1.449  1.00  8.02           C  
ANISOU 2152  CG  MET A 131      945    920   1184    119   -100   -117       C  
ATOM   2153  SD  MET A 131      31.883  17.182   0.976  1.00  8.68           S  
ANISOU 2153  SD  MET A 131     1041    847   1408    209   -150   -152       S  
ATOM   2154  CE  MET A 131      33.138  18.464   0.989  1.00 10.62           C  
ANISOU 2154  CE  MET A 131     1056   1438   1543    146     -5   -379       C  
ATOM   2155  H   MET A 131      28.825  20.077  -1.626  1.00  9.19           H  
ATOM   2156  HA  MET A 131      30.121  17.845  -1.268  1.00  9.17           H  
ATOM   2157  HB2 MET A 131      30.580  19.678   0.064  1.00  9.36           H  
ATOM   2158  HB3 MET A 131      29.139  19.584   0.718  1.00  9.36           H  
ATOM   2159  HG2 MET A 131      30.697  18.744   2.194  1.00  9.63           H  
ATOM   2160  HG3 MET A 131      29.737  17.569   1.734  1.00  9.63           H  
ATOM   2161  HE1 MET A 131      33.992  18.071   0.749  1.00 12.75           H  
ATOM   2162  HE2 MET A 131      32.896  19.148   0.346  1.00 12.75           H  
ATOM   2163  HE3 MET A 131      33.188  18.847   1.878  1.00 12.75           H  
ATOM   2164  N   ASN A 132      27.056  17.745  -0.308  1.00  8.03           N  
ANISOU 2164  N   ASN A 132      876    650   1525    179      5     -7       N  
ATOM   2165  CA  ASN A 132      25.987  16.796  -0.040  1.00  8.57           C  
ANISOU 2165  CA  ASN A 132      852    728   1677    273    -41    -71       C  
ATOM   2166  C   ASN A 132      25.868  15.764  -1.161  1.00  8.19           C  
ANISOU 2166  C   ASN A 132      828    701   1585    213   -163   -106       C  
ATOM   2167  O   ASN A 132      25.731  14.563  -0.900  1.00  9.03           O  
ANISOU 2167  O   ASN A 132     1019    699   1711    199     -8    -77       O  
ATOM   2168  CB  ASN A 132      24.664  17.514   0.183  1.00  9.21           C  
ANISOU 2168  CB  ASN A 132      909    749   1843    179     10   -218       C  
ATOM   2169  CG  ASN A 132      23.540  16.524   0.398  1.00 10.86           C  
ANISOU 2169  CG  ASN A 132      954    922   2251    331    257    -73       C  
ATOM   2170  OD1 ASN A 132      23.602  15.695   1.308  1.00 11.93           O  
ANISOU 2170  OD1 ASN A 132     1086   1012   2435    250    345      3       O  
ATOM   2171  ND2 ASN A 132      22.516  16.580  -0.442  1.00 12.34           N  
ANISOU 2171  ND2 ASN A 132     1025   1116   2546    107    -78   -202       N  
ATOM   2172  H   ASN A 132      26.812  18.570  -0.328  1.00  9.64           H  
ATOM   2173  HA  ASN A 132      26.200  16.316   0.776  1.00 10.28           H  
ATOM   2174  HB2 ASN A 132      24.732  18.076   0.970  1.00 11.06           H  
ATOM   2175  HB3 ASN A 132      24.454  18.050  -0.598  1.00 11.06           H  
ATOM   2176 HD21 ASN A 132      21.857  16.035  -0.354  1.00 14.81           H  
ATOM   2177 HD22 ASN A 132      22.511  17.161  -1.076  1.00 14.81           H  
ATOM   2178  N  ALYS A 133      25.932  16.208  -2.412  0.56  8.75           N  
ANISOU 2178  N  ALYS A 133      929    775   1621    152   -249   -167       N  
ATOM   2179  N  BLYS A 133      25.875  16.218  -2.420  0.44  8.93           N  
ANISOU 2179  N  BLYS A 133      989    881   1524    210   -163    -64       N  
ATOM   2180  CA ALYS A 133      25.806  15.277  -3.528  0.56  9.38           C  
ANISOU 2180  CA ALYS A 133     1144    841   1579     77   -355   -185       C  
ATOM   2181  CA BLYS A 133      25.832  15.283  -3.545  0.44  9.97           C  
ANISOU 2181  CA BLYS A 133     1262   1029   1496    156   -265    -31       C  
ATOM   2182  C  ALYS A 133      26.975  14.289  -3.569  0.56  8.62           C  
ANISOU 2182  C  ALYS A 133     1219    746   1311    110    -37   -112       C  
ATOM   2183  C  BLYS A 133      26.960  14.263  -3.447  0.44  8.80           C  
ANISOU 2183  C  BLYS A 133     1306    882   1156    192   -117      4       C  
ATOM   2184  O  ALYS A 133      26.792  13.118  -3.927  0.56  8.18           O  
ANISOU 2184  O  ALYS A 133     1216    643   1250     59     46   -205       O  
ATOM   2185  O  BLYS A 133      26.738  13.053  -3.579  0.44  8.37           O  
ANISOU 2185  O  BLYS A 133     1380    844    956    192   -119     47       O  
ATOM   2186  CB ALYS A 133      25.707  16.081  -4.820  0.56 10.89           C  
ANISOU 2186  CB ALYS A 133     1363   1151   1623    147   -436    -88       C  
ATOM   2187  CB BLYS A 133      25.943  16.035  -4.875  0.44 11.82           C  
ANISOU 2187  CB BLYS A 133     1538   1338   1617    208   -332     67       C  
ATOM   2188  CG ALYS A 133      25.216  15.318  -6.016  0.56 11.95           C  
ANISOU 2188  CG ALYS A 133     1539   1348   1655    250   -315    -11       C  
ATOM   2189  CG BLYS A 133      24.633  16.523  -5.460  0.44 12.99           C  
ANISOU 2189  CG BLYS A 133     1694   1556   1685    171   -330    222       C  
ATOM   2190  CD ALYS A 133      25.108  16.249  -7.204  0.56 15.14           C  
ANISOU 2190  CD ALYS A 133     1716   1728   2310    239   -429   -210       C  
ATOM   2191  CD BLYS A 133      24.789  16.904  -6.921  0.44 15.03           C  
ANISOU 2191  CD BLYS A 133     1840   1827   2041    161   -222    304       C  
ATOM   2192  CE ALYS A 133      24.701  15.538  -8.465  0.56 18.06           C  
ANISOU 2192  CE ALYS A 133     1970   2062   2828    291   -646   -149       C  
ATOM   2193  CE BLYS A 133      23.479  17.327  -7.515  0.44 16.05           C  
ANISOU 2193  CE BLYS A 133     1866   1998   2233     42   -217    187       C  
ATOM   2194  NZ ALYS A 133      24.621  16.509  -9.595  0.56 19.15           N  
ANISOU 2194  NZ ALYS A 133     2069   2103   3102    222   -762   -108       N  
ATOM   2195  NZ BLYS A 133      23.631  17.613  -8.954  0.44 15.44           N  
ANISOU 2195  NZ BLYS A 133     1819   2078   1971     60   -509    162       N  
ATOM   2196  H  ALYS A 133      26.046  17.030  -2.640  0.56 10.50           H  
ATOM   2197  H  BLYS A 133      25.904  17.048  -2.644  0.44 10.72           H  
ATOM   2198  HA ALYS A 133      24.986  14.769  -3.425  0.56 11.26           H  
ATOM   2199  HA BLYS A 133      24.988  14.806  -3.533  0.44 11.96           H  
ATOM   2200  HB2ALYS A 133      25.096  16.820  -4.676  0.56 13.07           H  
ATOM   2201  HB2BLYS A 133      26.509  16.811  -4.743  0.44 14.19           H  
ATOM   2202  HB3ALYS A 133      26.587  16.426  -5.035  0.56 13.07           H  
ATOM   2203  HB3BLYS A 133      26.350  15.444  -5.528  0.44 14.19           H  
ATOM   2204  HG2ALYS A 133      25.845  14.612  -6.232  0.56 14.35           H  
ATOM   2205  HG2BLYS A 133      23.971  15.817  -5.398  0.44 15.59           H  
ATOM   2206  HG3ALYS A 133      24.338  14.950  -5.830  0.56 14.35           H  
ATOM   2207  HG3BLYS A 133      24.336  17.307  -4.971  0.44 15.59           H  
ATOM   2208  HD2ALYS A 133      24.443  16.928  -7.014  0.56 18.17           H  
ATOM   2209  HD2BLYS A 133      25.411  17.644  -6.995  0.44 18.03           H  
ATOM   2210  HD3ALYS A 133      25.971  16.664  -7.360  0.56 18.17           H  
ATOM   2211  HD3BLYS A 133      25.116  16.138  -7.419  0.44 18.03           H  
ATOM   2212  HE2ALYS A 133      25.361  14.863  -8.685  0.56 21.67           H  
ATOM   2213  HE2BLYS A 133      22.831  16.613  -7.411  0.44 19.26           H  
ATOM   2214  HE3ALYS A 133      23.827  15.135  -8.343  0.56 21.67           H  
ATOM   2215  HE3BLYS A 133      23.169  18.133  -7.073  0.44 19.26           H  
ATOM   2216  HZ1ALYS A 133      24.379  16.088 -10.341  0.56 22.97           H  
ATOM   2217  HZ1BLYS A 133      22.849  17.864  -9.298  0.44 18.53           H  
ATOM   2218  HZ2ALYS A 133      24.020  17.140  -9.412  0.56 22.97           H  
ATOM   2219  HZ2BLYS A 133      24.222  18.267  -9.073  0.44 18.53           H  
ATOM   2220  HZ3ALYS A 133      25.413  16.893  -9.723  0.56 22.97           H  
ATOM   2221  HZ3BLYS A 133      23.915  16.885  -9.380  0.44 18.53           H  
ATOM   2222  N   ALA A 134      28.188  14.739  -3.222  1.00  8.30           N  
ANISOU 2222  N   ALA A 134     1085    808   1263    102    -96   -155       N  
ATOM   2223  CA  ALA A 134      29.335  13.830  -3.166  1.00  7.98           C  
ANISOU 2223  CA  ALA A 134      974    866   1193     74     47    -79       C  
ATOM   2224  C   ALA A 134      29.188  12.803  -2.045  1.00  8.12           C  
ANISOU 2224  C   ALA A 134     1073    677   1337     74    -58    -90       C  
ATOM   2225  O   ALA A 134      29.517  11.619  -2.224  1.00  8.28           O  
ANISOU 2225  O   ALA A 134     1099    711   1335     69     41   -109       O  
ATOM   2226  CB  ALA A 134      30.629  14.633  -3.003  1.00  8.24           C  
ANISOU 2226  CB  ALA A 134     1062    843   1225    266     33    -71       C  
ATOM   2227  H   ALA A 134      28.372  15.562  -3.058  1.00  9.97           H  
ATOM   2228  HA  ALA A 134      29.391  13.347  -4.005  1.00  9.58           H  
ATOM   2229  HB1 ALA A 134      31.379  14.018  -2.968  1.00  9.89           H  
ATOM   2230  HB2 ALA A 134      30.727  15.232  -3.759  1.00  9.89           H  
ATOM   2231  HB3 ALA A 134      30.581  15.144  -2.180  1.00  9.89           H  
ATOM   2232  N   LEU A 135      28.712  13.233  -0.872  1.00  7.90           N  
ANISOU 2232  N   LEU A 135     1111    689   1199    160     15    -63       N  
ATOM   2233  CA  LEU A 135      28.519  12.309   0.245  1.00  7.75           C  
ANISOU 2233  CA  LEU A 135     1053    697   1196    142      3    -61       C  
ATOM   2234  C   LEU A 135      27.358  11.352  -0.020  1.00  8.58           C  
ANISOU 2234  C   LEU A 135     1069    647   1544    276     73   -160       C  
ATOM   2235  O   LEU A 135      27.428  10.178   0.366  1.00  8.91           O  
ANISOU 2235  O   LEU A 135     1161    673   1550    121     61    -39       O  
ATOM   2236  CB  LEU A 135      28.357  13.085   1.560  1.00  8.12           C  
ANISOU 2236  CB  LEU A 135     1076    714   1295     34    -54    144       C  
ATOM   2237  CG  LEU A 135      29.577  13.917   1.978  1.00  8.83           C  
ANISOU 2237  CG  LEU A 135     1062    883   1412     64    -72     31       C  
ATOM   2238  CD1 LEU A 135      29.284  14.746   3.219  1.00  9.91           C  
ANISOU 2238  CD1 LEU A 135     1363    986   1414    -73     34   -127       C  
ATOM   2239  CD2 LEU A 135      30.823  13.050   2.206  1.00 12.11           C  
ANISOU 2239  CD2 LEU A 135     1087   1275   2237    324   -407   -224       C  
ATOM   2240  H   LEU A 135      28.496  14.048  -0.700  1.00  9.47           H  
ATOM   2241  HA  LEU A 135      29.319  11.768   0.330  1.00  9.30           H  
ATOM   2242  HB2 LEU A 135      27.607  13.693   1.468  1.00  9.74           H  
ATOM   2243  HB3 LEU A 135      28.177  12.452   2.272  1.00  9.74           H  
ATOM   2244  HG  LEU A 135      29.784  14.536   1.261  1.00 10.60           H  
ATOM   2245 HD11 LEU A 135      30.076  15.256   3.452  1.00 11.89           H  
ATOM   2246 HD12 LEU A 135      28.547  15.347   3.030  1.00 11.89           H  
ATOM   2247 HD13 LEU A 135      29.048  14.151   3.948  1.00 11.89           H  
ATOM   2248 HD21 LEU A 135      31.562  13.622   2.468  1.00 14.53           H  
ATOM   2249 HD22 LEU A 135      30.636  12.408   2.909  1.00 14.53           H  
ATOM   2250 HD23 LEU A 135      31.039  12.586   1.382  1.00 14.53           H  
ATOM   2251  N   GLU A 136      26.292  11.834  -0.682  1.00  8.36           N  
ANISOU 2251  N   GLU A 136     1014    629   1533    111     18    -93       N  
ATOM   2252  CA  GLU A 136      25.202  10.944  -1.086  1.00  9.26           C  
ANISOU 2252  CA  GLU A 136     1037    744   1739     89     21   -158       C  
ATOM   2253  C   GLU A 136      25.694   9.862  -2.051  1.00  8.68           C  
ANISOU 2253  C   GLU A 136      944    795   1558     71   -141   -138       C  
ATOM   2254  O   GLU A 136      25.284   8.699  -1.949  1.00  9.71           O  
ANISOU 2254  O   GLU A 136     1219    694   1777     45     31   -176       O  
ATOM   2255  CB  GLU A 136      24.063  11.755  -1.726  1.00 11.15           C  
ANISOU 2255  CB  GLU A 136     1055    836   2345     47    -65   -345       C  
ATOM   2256  CG  GLU A 136      23.174  12.524  -0.738  1.00 16.41           C  
ANISOU 2256  CG  GLU A 136     1516   1463   3255    313   -187   -411       C  
ATOM   2257  CD  GLU A 136      22.026  13.320  -1.365  1.00 22.23           C  
ANISOU 2257  CD  GLU A 136     1962   2299   4186    891   -342   -794       C  
ATOM   2258  OE1 GLU A 136      21.172  13.820  -0.593  1.00 22.73           O  
ANISOU 2258  OE1 GLU A 136     1755   2118   4765    620   -537   -844       O  
ATOM   2259  OE2 GLU A 136      21.980  13.478  -2.602  1.00 26.58           O  
ANISOU 2259  OE2 GLU A 136     2455   2982   4660   1218   -771   -907       O  
ATOM   2260  H   GLU A 136      26.181  12.657  -0.903  1.00 10.03           H  
ATOM   2261  HA  GLU A 136      24.848  10.502  -0.299  1.00 11.12           H  
ATOM   2262  HB2 GLU A 136      24.451  12.402  -2.335  1.00 13.38           H  
ATOM   2263  HB3 GLU A 136      23.492  11.146  -2.220  1.00 13.38           H  
ATOM   2264  HG2 GLU A 136      22.783  11.888  -0.119  1.00 19.69           H  
ATOM   2265  HG3 GLU A 136      23.730  13.151  -0.249  1.00 19.69           H  
ATOM   2266  N   LEU A 137      26.558  10.224  -3.009  1.00  8.66           N  
ANISOU 2266  N   LEU A 137     1082    774   1436     84     -3   -208       N  
ATOM   2267  CA  LEU A 137      27.117   9.242  -3.937  1.00  8.70           C  
ANISOU 2267  CA  LEU A 137     1192    845   1269     68    -16   -238       C  
ATOM   2268  C   LEU A 137      27.960   8.209  -3.194  1.00  8.64           C  
ANISOU 2268  C   LEU A 137     1172    712   1399    -38     35    -94       C  
ATOM   2269  O   LEU A 137      27.844   6.999  -3.439  1.00  8.96           O  
ANISOU 2269  O   LEU A 137     1194    749   1461    -21   -110   -208       O  
ATOM   2270  CB  LEU A 137      27.948   9.958  -5.003  1.00  9.90           C  
ANISOU 2270  CB  LEU A 137     1368    997   1395    221   -142   -171       C  
ATOM   2271  CG  LEU A 137      28.676   9.067  -6.019  1.00 10.51           C  
ANISOU 2271  CG  LEU A 137     1468   1040   1487    182    122   -218       C  
ATOM   2272  CD1 LEU A 137      27.695   8.266  -6.885  1.00 11.99           C  
ANISOU 2272  CD1 LEU A 137     1572   1302   1682      4    147   -277       C  
ATOM   2273  CD2 LEU A 137      29.616   9.918  -6.886  1.00 12.15           C  
ANISOU 2273  CD2 LEU A 137     1664   1287   1667    387    171    -35       C  
ATOM   2274  H   LEU A 137      26.831  11.029  -3.140  1.00 10.40           H  
ATOM   2275  HA  LEU A 137      26.392   8.776  -4.382  1.00 10.44           H  
ATOM   2276  HB2 LEU A 137      27.358  10.542  -5.505  1.00 11.87           H  
ATOM   2277  HB3 LEU A 137      28.622  10.492  -4.554  1.00 11.87           H  
ATOM   2278  HG  LEU A 137      29.224   8.430  -5.533  1.00 12.62           H  
ATOM   2279 HD11 LEU A 137      28.198   7.720  -7.510  1.00 14.39           H  
ATOM   2280 HD12 LEU A 137      27.156   7.700  -6.311  1.00 14.39           H  
ATOM   2281 HD13 LEU A 137      27.126   8.884  -7.370  1.00 14.39           H  
ATOM   2282 HD21 LEU A 137      30.068   9.342  -7.521  1.00 14.59           H  
ATOM   2283 HD22 LEU A 137      29.092  10.585  -7.357  1.00 14.59           H  
ATOM   2284 HD23 LEU A 137      30.266  10.353  -6.312  1.00 14.59           H  
ATOM   2285  N   PHE A 138      28.839   8.680  -2.302  1.00  8.15           N  
ANISOU 2285  N   PHE A 138     1100    633   1365     38    -33   -221       N  
ATOM   2286  CA  PHE A 138      29.627   7.797  -1.450  1.00  8.50           C  
ANISOU 2286  CA  PHE A 138      982    759   1488     41    -79      5       C  
ATOM   2287  C   PHE A 138      28.727   6.809  -0.705  1.00  7.97           C  
ANISOU 2287  C   PHE A 138     1026    618   1386     49   -206   -165       C  
ATOM   2288  O   PHE A 138      28.978   5.597  -0.708  1.00  8.53           O  
ANISOU 2288  O   PHE A 138     1062    616   1565     66    -67    -80       O  
ATOM   2289  CB  PHE A 138      30.460   8.660  -0.486  1.00  8.56           C  
ANISOU 2289  CB  PHE A 138      963    762   1528     45     42    -51       C  
ATOM   2290  CG  PHE A 138      31.011   7.920   0.721  1.00  8.75           C  
ANISOU 2290  CG  PHE A 138      980    748   1597     -8    -88   -104       C  
ATOM   2291  CD1 PHE A 138      30.490   8.139   2.002  1.00 10.08           C  
ANISOU 2291  CD1 PHE A 138     1116   1178   1534    183    -69    -46       C  
ATOM   2292  CD2 PHE A 138      32.042   7.012   0.589  1.00  9.71           C  
ANISOU 2292  CD2 PHE A 138     1047    996   1646     68    -85     77       C  
ATOM   2293  CE1 PHE A 138      30.981   7.458   3.112  1.00 11.13           C  
ANISOU 2293  CE1 PHE A 138     1293   1292   1643    225   -148    -39       C  
ATOM   2294  CE2 PHE A 138      32.547   6.338   1.700  1.00 11.20           C  
ANISOU 2294  CE2 PHE A 138     1323   1125   1806    121    -86     16       C  
ATOM   2295  CZ  PHE A 138      32.004   6.557   2.964  1.00 11.06           C  
ANISOU 2295  CZ  PHE A 138     1414   1243   1546    198   -205    135       C  
ATOM   2296  H   PHE A 138      28.994   9.516  -2.174  1.00  9.78           H  
ATOM   2297  HA  PHE A 138      30.240   7.287  -2.002  1.00 10.20           H  
ATOM   2298  HB2 PHE A 138      31.213   9.028  -0.974  1.00 10.27           H  
ATOM   2299  HB3 PHE A 138      29.901   9.382  -0.158  1.00 10.27           H  
ATOM   2300  HD1 PHE A 138      29.791   8.742   2.111  1.00 12.09           H  
ATOM   2301  HD2 PHE A 138      32.408   6.852  -0.251  1.00 11.65           H  
ATOM   2302  HE1 PHE A 138      30.618   7.618   3.954  1.00 13.35           H  
ATOM   2303  HE2 PHE A 138      33.239   5.726   1.594  1.00 13.43           H  
ATOM   2304  HZ  PHE A 138      32.343   6.107   3.704  1.00 13.28           H  
ATOM   2305  N   ARG A 139      27.663   7.309  -0.061  1.00  8.54           N  
ANISOU 2305  N   ARG A 139     1014    603   1626     74     15    -70       N  
ATOM   2306  CA  ARG A 139      26.796   6.422   0.714  1.00  8.74           C  
ANISOU 2306  CA  ARG A 139     1100    693   1527     64    134     12       C  
ATOM   2307  C   ARG A 139      26.013   5.463  -0.184  1.00  8.55           C  
ANISOU 2307  C   ARG A 139     1135    656   1457    -85     54   -200       C  
ATOM   2308  O   ARG A 139      25.784   4.307   0.191  1.00  9.65           O  
ANISOU 2308  O   ARG A 139     1214    699   1753   -141    -19   -144       O  
ATOM   2309  CB  ARG A 139      25.823   7.226   1.580  1.00  8.88           C  
ANISOU 2309  CB  ARG A 139     1087    817   1469   -115     90    -55       C  
ATOM   2310  CG  ARG A 139      26.472   8.043   2.699  1.00  8.62           C  
ANISOU 2310  CG  ARG A 139     1122    831   1323   -104      2    -47       C  
ATOM   2311  CD  ARG A 139      25.489   8.545   3.730  1.00  9.50           C  
ANISOU 2311  CD  ARG A 139     1165    959   1485    -19     40    -65       C  
ATOM   2312  NE  ARG A 139      24.335   9.223   3.152  1.00 10.45           N  
ANISOU 2312  NE  ARG A 139     1165    943   1863    -64      4   -229       N  
ATOM   2313  CZ  ARG A 139      24.260  10.524   2.883  1.00 10.45           C  
ANISOU 2313  CZ  ARG A 139     1131    992   1848    -65      6   -161       C  
ATOM   2314  NH1 ARG A 139      23.153  11.026   2.361  1.00 12.84           N  
ANISOU 2314  NH1 ARG A 139     1192   1121   2566    -27   -215   -120       N  
ATOM   2315  NH2 ARG A 139      25.283  11.326   3.131  1.00 10.94           N  
ANISOU 2315  NH2 ARG A 139     1283    969   1905    -52   -135    -23       N  
ATOM   2316  H   ARG A 139      27.429   8.137  -0.058  1.00 10.24           H  
ATOM   2317  HA  ARG A 139      27.347   5.887   1.307  1.00 10.48           H  
ATOM   2318  HB2 ARG A 139      25.340   7.844   1.009  1.00 10.65           H  
ATOM   2319  HB3 ARG A 139      25.197   6.611   1.993  1.00 10.65           H  
ATOM   2320  HG2 ARG A 139      27.123   7.487   3.154  1.00 10.35           H  
ATOM   2321  HG3 ARG A 139      26.912   8.814   2.308  1.00 10.35           H  
ATOM   2322  HD2 ARG A 139      25.164   7.790   4.246  1.00 11.40           H  
ATOM   2323  HD3 ARG A 139      25.942   9.173   4.314  1.00 11.40           H  
ATOM   2324  HE  ARG A 139      23.645   8.742   2.970  1.00 12.54           H  
ATOM   2325 HH11 ARG A 139      22.484  10.511   2.195  1.00 15.41           H  
ATOM   2326 HH12 ARG A 139      23.104  11.866   2.184  1.00 15.41           H  
ATOM   2327 HH21 ARG A 139      26.006  11.008   3.471  1.00 13.13           H  
ATOM   2328 HH22 ARG A 139      25.224  12.165   2.952  1.00 13.13           H  
ATOM   2329  N   LYS A 140      25.562   5.925  -1.350  1.00  9.22           N  
ANISOU 2329  N   LYS A 140     1173    759   1571    -30   -161   -235       N  
ATOM   2330  CA  LYS A 140      24.849   5.045  -2.272  1.00 10.11           C  
ANISOU 2330  CA  LYS A 140     1269    882   1690    -69   -237   -236       C  
ATOM   2331  C   LYS A 140      25.741   3.890  -2.702  1.00  9.47           C  
ANISOU 2331  C   LYS A 140     1231    732   1635    -88   -270   -194       C  
ATOM   2332  O   LYS A 140      25.325   2.724  -2.711  1.00  9.92           O  
ANISOU 2332  O   LYS A 140     1148    771   1850    -58   -161   -261       O  
ATOM   2333  CB  LYS A 140      24.401   5.843  -3.496  1.00 12.71           C  
ANISOU 2333  CB  LYS A 140     1679   1121   2031     42   -531   -292       C  
ATOM   2334  CG  LYS A 140      23.738   5.019  -4.597  1.00 16.71           C  
ANISOU 2334  CG  LYS A 140     2305   1748   2294    215  -1062   -263       C  
ATOM   2335  CD  LYS A 140      23.463   5.886  -5.829  1.00 22.11           C  
ANISOU 2335  CD  LYS A 140     2897   2428   3076    369  -1564   -485       C  
ATOM   2336  CE  LYS A 140      23.058   5.071  -7.048  1.00 28.06           C  
ANISOU 2336  CE  LYS A 140     3349   3236   4078    590  -1653   -333       C  
ATOM   2337  NZ  LYS A 140      21.754   4.408  -6.841  1.00 32.28           N  
ANISOU 2337  NZ  LYS A 140     3701   3710   4853    859  -1490   -249       N  
ATOM   2338  H   LYS A 140      25.654   6.733  -1.627  1.00 11.06           H  
ATOM   2339  HA  LYS A 140      24.063   4.683  -1.834  1.00 12.13           H  
ATOM   2340  HB2 LYS A 140      23.763   6.515  -3.209  1.00 15.25           H  
ATOM   2341  HB3 LYS A 140      25.178   6.277  -3.882  1.00 15.25           H  
ATOM   2342  HG2 LYS A 140      24.328   4.295  -4.858  1.00 20.05           H  
ATOM   2343  HG3 LYS A 140      22.894   4.668  -4.274  1.00 20.05           H  
ATOM   2344  HD2 LYS A 140      22.741   6.501  -5.626  1.00 26.53           H  
ATOM   2345  HD3 LYS A 140      24.267   6.380  -6.052  1.00 26.53           H  
ATOM   2346  HE2 LYS A 140      22.982   5.659  -7.816  1.00 33.68           H  
ATOM   2347  HE3 LYS A 140      23.725   4.387  -7.213  1.00 33.68           H  
ATOM   2348  HZ1 LYS A 140      21.534   3.937  -7.563  1.00 38.73           H  
ATOM   2349  HZ2 LYS A 140      21.800   3.860  -6.141  1.00 38.73           H  
ATOM   2350  HZ3 LYS A 140      21.123   5.018  -6.690  1.00 38.73           H  
ATOM   2351  N   ASP A 141      26.981   4.200  -3.072  1.00  9.30           N  
ANISOU 2351  N   ASP A 141     1155    712   1668    -11   -178   -239       N  
ATOM   2352  CA  ASP A 141      27.883   3.166  -3.564  1.00 10.12           C  
ANISOU 2352  CA  ASP A 141     1252    827   1768     48   -167   -216       C  
ATOM   2353  C   ASP A 141      28.330   2.230  -2.437  1.00  9.83           C  
ANISOU 2353  C   ASP A 141     1280    819   1635    -55   -117   -198       C  
ATOM   2354  O   ASP A 141      28.430   1.012  -2.636  1.00 10.34           O  
ANISOU 2354  O   ASP A 141     1497    657   1775    -38    -97   -191       O  
ATOM   2355  CB  ASP A 141      29.070   3.799  -4.307  1.00  9.77           C  
ANISOU 2355  CB  ASP A 141     1110   1066   1534    -26    -89   -244       C  
ATOM   2356  CG  ASP A 141      28.692   4.388  -5.657  1.00 11.59           C  
ANISOU 2356  CG  ASP A 141     1292   1407   1707   -153     -9   -328       C  
ATOM   2357  OD1 ASP A 141      27.553   4.227  -6.138  1.00 13.14           O  
ANISOU 2357  OD1 ASP A 141     1548   1704   1742   -148   -246   -231       O  
ATOM   2358  OD2 ASP A 141      29.587   5.014  -6.258  1.00 12.59           O  
ANISOU 2358  OD2 ASP A 141     1407   1606   1770     -9    -48    -88       O  
ATOM   2359  H   ASP A 141      27.319   4.991  -3.049  1.00 11.17           H  
ATOM   2360  HA  ASP A 141      27.400   2.626  -4.208  1.00 12.15           H  
ATOM   2361  HB2 ASP A 141      29.436   4.513  -3.762  1.00 11.72           H  
ATOM   2362  HB3 ASP A 141      29.745   3.119  -4.457  1.00 11.72           H  
ATOM   2363  N   ILE A 142      28.570   2.763  -1.239  1.00  9.93           N  
ANISOU 2363  N   ILE A 142     1332    841   1601     79   -207   -117       N  
ATOM   2364  CA  ILE A 142      28.934   1.878  -0.133  1.00 10.58           C  
ANISOU 2364  CA  ILE A 142     1482    763   1776     28   -371   -183       C  
ATOM   2365  C   ILE A 142      27.768   0.974   0.256  1.00 10.10           C  
ANISOU 2365  C   ILE A 142     1480    610   1747    -78   -124   -319       C  
ATOM   2366  O   ILE A 142      27.971  -0.193   0.604  1.00 10.85           O  
ANISOU 2366  O   ILE A 142     1646    572   1907     13   -101   -209       O  
ATOM   2367  CB AILE A 142      29.308   2.713   1.112  0.38 11.96           C  
ANISOU 2367  CB AILE A 142     1588    970   1989    191   -521    136       C  
ATOM   2368  CB BILE A 142      29.676   2.619   0.998  0.62 10.77           C  
ANISOU 2368  CB BILE A 142     1384    911   1798     39   -416    -60       C  
ATOM   2369  CG1AILE A 142      30.691   3.339   0.998  0.38 12.24           C  
ANISOU 2369  CG1AILE A 142     1582   1008   2060     79   -491    185       C  
ATOM   2370  CG1BILE A 142      30.693   1.677   1.663  0.62 10.53           C  
ANISOU 2370  CG1BILE A 142     1312    837   1854     37   -317    -64       C  
ATOM   2371  CG2AILE A 142      29.170   1.868   2.434  0.38 11.86           C  
ANISOU 2371  CG2AILE A 142     1538   1041   1926     52   -462     89       C  
ATOM   2372  CG2BILE A 142      28.732   3.203   1.945  0.62  9.70           C  
ANISOU 2372  CG2BILE A 142     1144   1019   1523   -238     18   -126       C  
ATOM   2373  CD1AILE A 142      31.806   2.376   1.252  0.38 13.43           C  
ANISOU 2373  CD1AILE A 142     1608   1207   2288    200   -345    185       C  
ATOM   2374  CD1BILE A 142      31.541   2.331   2.735  0.62 10.27           C  
ANISOU 2374  CD1BILE A 142     1272    859   1772     28   -182     78       C  
ATOM   2375  H   ILE A 142      28.532   3.599  -1.044  1.00 11.92           H  
ATOM   2376  HA  ILE A 142      29.635   1.286  -0.449  1.00 12.70           H  
ATOM   2377  HB AILE A 142      28.670   3.441   1.170  0.38 14.36           H  
ATOM   2378  HB BILE A 142      30.173   3.348   0.594  0.62 12.93           H  
ATOM   2379 HG12AILE A 142      30.801   3.693   0.101  0.38 14.68           H  
ATOM   2380 HG12BILE A 142      30.212   0.942   2.075  0.62 12.64           H  
ATOM   2381 HG13AILE A 142      30.764   4.057   1.646  0.38 14.68           H  
ATOM   2382 HG13BILE A 142      31.292   1.335   0.981  0.62 12.64           H  
ATOM   2383 HG21AILE A 142      29.413   2.424   3.191  0.38 14.23           H  
ATOM   2384 HG21BILE A 142      29.227   3.660   2.642  0.62 11.64           H  
ATOM   2385 HG22AILE A 142      28.251   1.570   2.523  0.38 14.23           H  
ATOM   2386 HG22BILE A 142      28.163   3.832   1.475  0.62 11.64           H  
ATOM   2387 HG23AILE A 142      29.763   1.102   2.383  0.38 14.23           H  
ATOM   2388 HG23BILE A 142      28.194   2.494   2.331  0.62 11.64           H  
ATOM   2389 HD11AILE A 142      32.652   2.843   1.163  0.38 16.12           H  
ATOM   2390 HD11BILE A 142      32.151   1.671   3.100  0.62 12.33           H  
ATOM   2391 HD12AILE A 142      31.718   2.021   2.151  0.38 16.12           H  
ATOM   2392 HD12BILE A 142      32.041   3.062   2.339  0.62 12.33           H  
ATOM   2393 HD13AILE A 142      31.755   1.656   0.605  0.38 16.12           H  
ATOM   2394 HD13BILE A 142      30.960   2.668   3.435  0.62 12.33           H  
ATOM   2395  N   ALA A 143      26.535   1.502   0.238  1.00 10.66           N  
ANISOU 2395  N   ALA A 143     1484    697   1867    -38    -22   -192       N  
ATOM   2396  CA  ALA A 143      25.368   0.676   0.554  1.00 11.09           C  
ANISOU 2396  CA  ALA A 143     1431    781   2003    -51    -15   -154       C  
ATOM   2397  C   ALA A 143      25.230  -0.478  -0.427  1.00 10.87           C  
ANISOU 2397  C   ALA A 143     1295    824   2012      6   -181   -155       C  
ATOM   2398  O   ALA A 143      24.891  -1.604  -0.035  1.00 12.04           O  
ANISOU 2398  O   ALA A 143     1381    727   2465    -32   -122   -126       O  
ATOM   2399  CB  ALA A 143      24.097   1.535   0.571  1.00 12.67           C  
ANISOU 2399  CB  ALA A 143     1659    852   2301    -69    189     49       C  
ATOM   2400  H   ALA A 143      26.353   2.321   0.049  1.00 12.79           H  
ATOM   2401  HA  ALA A 143      25.483   0.300   1.441  1.00 13.31           H  
ATOM   2402  HB1 ALA A 143      23.337   0.970   0.782  1.00 15.20           H  
ATOM   2403  HB2 ALA A 143      24.192   2.227   1.244  1.00 15.20           H  
ATOM   2404  HB3 ALA A 143      23.977   1.938  -0.303  1.00 15.20           H  
ATOM   2405  N   ALA A 144      25.479  -0.222  -1.714  1.00 11.18           N  
ANISOU 2405  N   ALA A 144     1347    920   1981     20   -283   -288       N  
ATOM   2406  CA  ALA A 144      25.433  -1.299  -2.694  1.00 11.70           C  
ANISOU 2406  CA  ALA A 144     1493   1028   1924     67   -400   -257       C  
ATOM   2407  C   ALA A 144      26.506  -2.344  -2.402  1.00 11.16           C  
ANISOU 2407  C   ALA A 144     1415    828   1999     38   -299   -271       C  
ATOM   2408  O   ALA A 144      26.268  -3.553  -2.528  1.00 12.04           O  
ANISOU 2408  O   ALA A 144     1529    786   2260    -35   -472   -252       O  
ATOM   2409  CB  ALA A 144      25.596  -0.734  -4.103  1.00 13.00           C  
ANISOU 2409  CB  ALA A 144     1678   1032   2231    147   -522   -397       C  
ATOM   2410  H   ALA A 144      25.673   0.552  -2.036  1.00 13.42           H  
ATOM   2411  HA  ALA A 144      24.569  -1.735  -2.643  1.00 14.04           H  
ATOM   2412  HB1 ALA A 144      25.563  -1.464  -4.741  1.00 15.60           H  
ATOM   2413  HB2 ALA A 144      24.875  -0.109  -4.277  1.00 15.60           H  
ATOM   2414  HB3 ALA A 144      26.450  -0.280  -4.164  1.00 15.60           H  
ATOM   2415  N   LYS A 145      27.697  -1.905  -1.989  1.00 10.68           N  
ANISOU 2415  N   LYS A 145     1287    763   2009    -34   -215   -204       N  
ATOM   2416  CA  LYS A 145      28.744  -2.866  -1.654  1.00 10.23           C  
ANISOU 2416  CA  LYS A 145     1337    798   1752    -26    -99   -103       C  
ATOM   2417  C   LYS A 145      28.403  -3.656  -0.394  1.00  9.34           C  
ANISOU 2417  C   LYS A 145     1215    672   1662    -90      5   -175       C  
ATOM   2418  O   LYS A 145      28.657  -4.868  -0.327  1.00 10.03           O  
ANISOU 2418  O   LYS A 145     1231    688   1891     29   -113   -187       O  
ATOM   2419  CB  LYS A 145      30.089  -2.153  -1.521  1.00 11.40           C  
ANISOU 2419  CB  LYS A 145     1609    923   1801    -97   -105   -127       C  
ATOM   2420  CG  LYS A 145      31.296  -3.061  -1.442  1.00 17.31           C  
ANISOU 2420  CG  LYS A 145     2143   1644   2790    250   -516   -221       C  
ATOM   2421  CD  LYS A 145      31.462  -3.969  -2.657  1.00 21.52           C  
ANISOU 2421  CD  LYS A 145     2661   2274   3241    455   -748   -594       C  
ATOM   2422  CE  LYS A 145      31.933  -3.230  -3.901  1.00 21.67           C  
ANISOU 2422  CE  LYS A 145     2942   2340   2954    642   -852   -787       C  
ATOM   2423  NZ  LYS A 145      32.195  -4.177  -5.017  1.00 21.89           N  
ANISOU 2423  NZ  LYS A 145     3013   2527   2777   1067   -704   -644       N  
ATOM   2424  H   LYS A 145      27.918  -1.079  -1.896  1.00 12.82           H  
ATOM   2425  HA  LYS A 145      28.822  -3.501  -2.383  1.00 12.28           H  
ATOM   2426  HB2 LYS A 145      30.209  -1.576  -2.291  1.00 13.68           H  
ATOM   2427  HB3 LYS A 145      30.075  -1.617  -0.713  1.00 13.68           H  
ATOM   2428  HG2 LYS A 145      32.094  -2.515  -1.368  1.00 20.77           H  
ATOM   2429  HG3 LYS A 145      31.211  -3.627  -0.659  1.00 20.77           H  
ATOM   2430  HD2 LYS A 145      32.118  -4.653  -2.450  1.00 25.82           H  
ATOM   2431  HD3 LYS A 145      30.608  -4.381  -2.860  1.00 25.82           H  
ATOM   2432  HE2 LYS A 145      31.246  -2.607  -4.184  1.00 26.01           H  
ATOM   2433  HE3 LYS A 145      32.756  -2.758  -3.702  1.00 26.01           H  
ATOM   2434  HZ1 LYS A 145      32.469  -3.730  -5.737  1.00 26.27           H  
ATOM   2435  HZ2 LYS A 145      32.825  -4.759  -4.781  1.00 26.27           H  
ATOM   2436  HZ3 LYS A 145      31.451  -4.622  -5.219  1.00 26.27           H  
ATOM   2437  N   TYR A 146      27.848  -2.986   0.624  1.00 10.24           N  
ANISOU 2437  N   TYR A 146     1374    695   1822      0    119   -121       N  
ATOM   2438  CA  TYR A 146      27.372  -3.679   1.818  1.00 10.61           C  
ANISOU 2438  CA  TYR A 146     1358    753   1919   -122    116   -150       C  
ATOM   2439  C   TYR A 146      26.483  -4.861   1.435  1.00 11.65           C  
ANISOU 2439  C   TYR A 146     1459    867   2100   -184    153   -137       C  
ATOM   2440  O   TYR A 146      26.627  -5.977   1.955  1.00 12.10           O  
ANISOU 2440  O   TYR A 146     1765    917   1916   -203    380    -97       O  
ATOM   2441  CB  TYR A 146      26.554  -2.703   2.679  1.00 11.29           C  
ANISOU 2441  CB  TYR A 146     1339    911   2038    -75     50   -225       C  
ATOM   2442  CG  TYR A 146      27.282  -1.884   3.748  1.00 11.91           C  
ANISOU 2442  CG  TYR A 146     1339   1108   2079   -198    164   -534       C  
ATOM   2443  CD1 TYR A 146      26.566  -1.318   4.782  1.00 17.48           C  
ANISOU 2443  CD1 TYR A 146     1584   2049   3009   -416    321  -1141       C  
ATOM   2444  CD2 TYR A 146      28.634  -1.633   3.711  1.00 11.47           C  
ANISOU 2444  CD2 TYR A 146     1391   1369   1600   -101     57    -78       C  
ATOM   2445  CE1 TYR A 146      27.178  -0.580   5.770  1.00 17.77           C  
ANISOU 2445  CE1 TYR A 146     1613   2126   3014   -383    258  -1227       C  
ATOM   2446  CE2 TYR A 146      29.256  -0.888   4.712  1.00 11.92           C  
ANISOU 2446  CE2 TYR A 146     1342   1500   1687   -190    280     -9       C  
ATOM   2447  CZ  TYR A 146      28.529  -0.377   5.736  1.00 13.21           C  
ANISOU 2447  CZ  TYR A 146     1292   1546   2183   -328    158   -561       C  
ATOM   2448  OH  TYR A 146      29.160   0.350   6.722  1.00 13.19           O  
ANISOU 2448  OH  TYR A 146     1258   1573   2179   -126     69   -621       O  
ATOM   2449  H   TYR A 146      27.737  -2.133   0.644  1.00 12.29           H  
ATOM   2450  HA  TYR A 146      28.125  -4.004   2.336  1.00 12.73           H  
ATOM   2451  HB2 TYR A 146      26.128  -2.067   2.082  1.00 13.54           H  
ATOM   2452  HB3 TYR A 146      25.869  -3.214   3.136  1.00 13.54           H  
ATOM   2453  HD1 TYR A 146      25.650  -1.467   4.831  1.00 20.98           H  
ATOM   2454  HD2 TYR A 146      29.148  -1.998   3.027  1.00 13.77           H  
ATOM   2455  HE1 TYR A 146      26.673  -0.231   6.469  1.00 21.33           H  
ATOM   2456  HE2 TYR A 146      30.175  -0.750   4.683  1.00 14.30           H  
ATOM   2457  HH  TYR A 146      28.598   0.614   7.288  1.00 15.82           H  
ATOM   2458  N   LYS A 147      25.513  -4.611   0.553  1.00 12.39           N  
ANISOU 2458  N   LYS A 147     1402    857   2446   -101    -93   -225       N  
ATOM   2459  CA ALYS A 147      24.578  -5.657   0.153  0.53 13.31           C  
ANISOU 2459  CA ALYS A 147     1297   1013   2747   -157   -224   -320       C  
ATOM   2460  CA BLYS A 147      24.582  -5.666   0.171  0.47 13.94           C  
ANISOU 2460  CA BLYS A 147     1370   1084   2843    -21   -120   -235       C  
ATOM   2461  C   LYS A 147      25.294  -6.795  -0.567  1.00 12.45           C  
ANISOU 2461  C   LYS A 147     1377    860   2494    -98   -132   -177       C  
ATOM   2462  O   LYS A 147      25.011  -7.973  -0.320  1.00 13.35           O  
ANISOU 2462  O   LYS A 147     1533    855   2683   -153     33   -128       O  
ATOM   2463  CB ALYS A 147      23.470  -5.054  -0.716  0.53 16.39           C  
ANISOU 2463  CB ALYS A 147     1394   1357   3477   -242   -364   -650       C  
ATOM   2464  CB BLYS A 147      23.419  -5.084  -0.638  0.47 18.38           C  
ANISOU 2464  CB BLYS A 147     1507   1550   3928    123   -131   -445       C  
ATOM   2465  CG ALYS A 147      22.512  -4.144   0.059  0.53 21.60           C  
ANISOU 2465  CG ALYS A 147     1747   1745   4714     78   -261   -418       C  
ATOM   2466  CG BLYS A 147      22.391  -4.358   0.239  0.47 23.58           C  
ANISOU 2466  CG BLYS A 147     1881   2156   4922    488    -54   -203       C  
ATOM   2467  CD ALYS A 147      21.389  -3.614  -0.824  0.53 25.27           C  
ANISOU 2467  CD ALYS A 147     2103   2167   5330    335   -181   -234       C  
ATOM   2468  CD BLYS A 147      21.112  -4.006  -0.510  0.47 27.61           C  
ANISOU 2468  CD BLYS A 147     2208   2677   5605    695    -24    -91       C  
ATOM   2469  CE ALYS A 147      20.454  -2.680  -0.063  0.53 27.48           C  
ANISOU 2469  CE ALYS A 147     2324   2428   5690    440    -39    -83       C  
ATOM   2470  CE BLYS A 147      20.128  -3.288   0.405  0.47 30.25           C  
ANISOU 2470  CE BLYS A 147     2449   2998   6045    787     20    -66       C  
ATOM   2471  NZ ALYS A 147      21.119  -1.410   0.333  0.53 28.20           N  
ANISOU 2471  NZ ALYS A 147     2423   2447   5845    382    -50     49       N  
ATOM   2472  NZ BLYS A 147      18.942  -2.755  -0.317  0.47 31.54           N  
ANISOU 2472  NZ BLYS A 147     2572   3140   6272    768     28     21       N  
ATOM   2473  H  ALYS A 147      25.377  -3.850   0.176  0.53 14.86           H  
ATOM   2474  H  BLYS A 147      25.376  -3.853   0.170  0.47 14.86           H  
ATOM   2475  HA ALYS A 147      24.162  -6.025   0.949  0.53 15.97           H  
ATOM   2476  HA BLYS A 147      24.206  -6.046   0.980  0.47 16.73           H  
ATOM   2477  HB2ALYS A 147      23.877  -4.526  -1.421  0.53 19.67           H  
ATOM   2478  HB2BLYS A 147      23.768  -4.446  -1.280  0.47 22.06           H  
ATOM   2479  HB3ALYS A 147      22.948  -5.774  -1.103  0.53 19.67           H  
ATOM   2480  HB3BLYS A 147      22.963  -5.805  -1.100  0.47 22.06           H  
ATOM   2481  HG2ALYS A 147      22.114  -4.647   0.787  0.53 25.92           H  
ATOM   2482  HG2BLYS A 147      22.153  -4.931   0.985  0.47 28.29           H  
ATOM   2483  HG3ALYS A 147      23.006  -3.386   0.408  0.53 25.92           H  
ATOM   2484  HG3BLYS A 147      22.783  -3.533   0.566  0.47 28.29           H  
ATOM   2485  HD2ALYS A 147      21.772  -3.119  -1.565  0.53 30.32           H  
ATOM   2486  HD2BLYS A 147      21.324  -3.419  -1.253  0.47 33.13           H  
ATOM   2487  HD3ALYS A 147      20.865  -4.360  -1.156  0.53 30.32           H  
ATOM   2488  HD3BLYS A 147      20.693  -4.820  -0.832  0.47 33.13           H  
ATOM   2489  HE2ALYS A 147      19.697  -2.459  -0.627  0.53 32.98           H  
ATOM   2490  HE2BLYS A 147      19.813  -3.910   1.079  0.47 36.30           H  
ATOM   2491  HE3ALYS A 147      20.149  -3.124   0.744  0.53 32.98           H  
ATOM   2492  HE3BLYS A 147      20.580  -2.542   0.829  0.47 36.30           H  
ATOM   2493  HZ1ALYS A 147      20.545  -0.891   0.774  0.53 33.84           H  
ATOM   2494  HZ1BLYS A 147      18.397  -2.345   0.255  0.47 37.85           H  
ATOM   2495  HZ2ALYS A 147      21.816  -1.583   0.859  0.53 33.84           H  
ATOM   2496  HZ2BLYS A 147      19.200  -2.172  -0.938  0.47 37.85           H  
ATOM   2497  HZ3ALYS A 147      21.403  -0.977  -0.390  0.53 33.84           H  
ATOM   2498  HZ3BLYS A 147      18.500  -3.420  -0.710  0.47 37.85           H  
ATOM   2499  N   GLU A 148      26.241  -6.467  -1.454  1.00 11.63           N  
ANISOU 2499  N   GLU A 148     1422    830   2169    -53   -229   -342       N  
ATOM   2500  CA  GLU A 148      27.036  -7.512  -2.097  1.00 11.66           C  
ANISOU 2500  CA  GLU A 148     1600    767   2062    -36   -230   -232       C  
ATOM   2501  C   GLU A 148      27.785  -8.358  -1.076  1.00 10.49           C  
ANISOU 2501  C   GLU A 148     1433    685   1868   -120   -201   -212       C  
ATOM   2502  O   GLU A 148      27.976  -9.565  -1.297  1.00 11.42           O  
ANISOU 2502  O   GLU A 148     1484    765   2089    -53   -137   -236       O  
ATOM   2503  CB  GLU A 148      28.041  -6.889  -3.067  1.00 12.31           C  
ANISOU 2503  CB  GLU A 148     2012    989   1678   -150   -207   -160       C  
ATOM   2504  CG  GLU A 148      27.407  -6.256  -4.290  1.00 15.72           C  
ANISOU 2504  CG  GLU A 148     2527   1655   1792    126   -447    -81       C  
ATOM   2505  CD  GLU A 148      28.381  -5.458  -5.154  1.00 20.23           C  
ANISOU 2505  CD  GLU A 148     3104   2344   2238    297   -465    264       C  
ATOM   2506  OE1 GLU A 148      27.906  -4.668  -5.994  1.00 23.50           O  
ANISOU 2506  OE1 GLU A 148     3431   2696   2802    300   -510    428       O  
ATOM   2507  OE2 GLU A 148      29.606  -5.619  -5.017  1.00 21.74           O  
ANISOU 2507  OE2 GLU A 148     3300   2553   2406     91   -189    318       O  
ATOM   2508  H   GLU A 148      26.438  -5.665  -1.694  1.00 13.96           H  
ATOM   2509  HA  GLU A 148      26.447  -8.095  -2.602  1.00 13.99           H  
ATOM   2510  HB2 GLU A 148      28.538  -6.199  -2.600  1.00 14.78           H  
ATOM   2511  HB3 GLU A 148      28.648  -7.580  -3.373  1.00 14.78           H  
ATOM   2512  HG2 GLU A 148      27.027  -6.957  -4.843  1.00 18.87           H  
ATOM   2513  HG3 GLU A 148      26.706  -5.651  -4.000  1.00 18.87           H  
ATOM   2514  N   LEU A 149      28.237  -7.740   0.024  1.00 10.44           N  
ANISOU 2514  N   LEU A 149     1364    694   1906   -135    -82    -98       N  
ATOM   2515  CA  LEU A 149      29.036  -8.376   1.066  1.00 10.89           C  
ANISOU 2515  CA  LEU A 149     1590    818   1730   -229    -75    119       C  
ATOM   2516  C   LEU A 149      28.202  -9.151   2.079  1.00 12.46           C  
ANISOU 2516  C   LEU A 149     1870    777   2088   -267     10   -180       C  
ATOM   2517  O   LEU A 149      28.779  -9.820   2.948  1.00 13.43           O  
ANISOU 2517  O   LEU A 149     1947    936   2219   -181     37    116       O  
ATOM   2518  CB  LEU A 149      29.855  -7.307   1.806  1.00 11.86           C  
ANISOU 2518  CB  LEU A 149     1615    987   1907   -217   -233     30       C  
ATOM   2519  CG  LEU A 149      30.976  -6.643   1.015  1.00 13.54           C  
ANISOU 2519  CG  LEU A 149     1794   1077   2272   -177   -260    -21       C  
ATOM   2520  CD1 LEU A 149      31.441  -5.349   1.669  1.00 15.37           C  
ANISOU 2520  CD1 LEU A 149     1951   1280   2609   -279   -431    -35       C  
ATOM   2521  CD2 LEU A 149      32.122  -7.616   0.908  1.00 14.67           C  
ANISOU 2521  CD2 LEU A 149     1994   1110   2471     98     93    286       C  
ATOM   2522  H   LEU A 149      28.081  -6.911   0.189  1.00 12.52           H  
ATOM   2523  HA  LEU A 149      29.657  -8.996   0.653  1.00 13.07           H  
ATOM   2524  HB2 LEU A 149      29.250  -6.605   2.091  1.00 14.24           H  
ATOM   2525  HB3 LEU A 149      30.258  -7.719   2.585  1.00 14.24           H  
ATOM   2526  HG  LEU A 149      30.663  -6.439   0.119  1.00 16.24           H  
ATOM   2527 HD11 LEU A 149      32.152  -4.963   1.134  1.00 18.44           H  
ATOM   2528 HD12 LEU A 149      30.692  -4.735   1.718  1.00 18.44           H  
ATOM   2529 HD13 LEU A 149      31.767  -5.546   2.561  1.00 18.44           H  
ATOM   2530 HD21 LEU A 149      32.841  -7.202   0.406  1.00 17.61           H  
ATOM   2531 HD22 LEU A 149      32.428  -7.841   1.800  1.00 17.61           H  
ATOM   2532 HD23 LEU A 149      31.816  -8.415   0.451  1.00 17.61           H  
ATOM   2533  N   GLY A 150      26.873  -9.078   2.003  1.00 12.61           N  
ANISOU 2533  N   GLY A 150     1818    919   2055   -540    226   -272       N  
ATOM   2534  CA  GLY A 150      26.004  -9.809   2.901  1.00 14.55           C  
ANISOU 2534  CA  GLY A 150     1979   1225   2322   -699    356   -416       C  
ATOM   2535  C   GLY A 150      25.446  -9.035   4.082  1.00 14.85           C  
ANISOU 2535  C   GLY A 150     2122   1298   2223   -762    520   -264       C  
ATOM   2536  O   GLY A 150      24.902  -9.665   4.999  1.00 17.78           O  
ANISOU 2536  O   GLY A 150     2686   1570   2499   -724    670   -283       O  
ATOM   2537  H   GLY A 150      26.451  -8.601   1.425  1.00 15.13           H  
ATOM   2538  HA2 GLY A 150      25.252 -10.150   2.393  1.00 17.45           H  
ATOM   2539  HA3 GLY A 150      26.492 -10.569   3.254  1.00 17.45           H  
ATOM   2540  N  ATYR A 151      25.561  -7.702   4.087  0.57 13.80           N  
ANISOU 2540  N  ATYR A 151     1922   1292   2031   -738    326   -432       N  
ATOM   2541  N  BTYR A 151      25.520  -7.709   4.078  0.43 14.96           N  
ANISOU 2541  N  BTYR A 151     2019   1361   2304   -582    478   -467       N  
ATOM   2542  CA ATYR A 151      25.135  -6.846   5.194  0.57 15.05           C  
ANISOU 2542  CA ATYR A 151     2005   1465   2250   -569    448   -520       C  
ATOM   2543  CA BTYR A 151      25.084  -6.927   5.228  0.43 16.62           C  
ANISOU 2543  CA BTYR A 151     2083   1600   2632   -353    619   -658       C  
ATOM   2544  C  ATYR A 151      24.022  -5.925   4.709  0.57 18.06           C  
ANISOU 2544  C  ATYR A 151     1989   1649   3222   -773    544   -610       C  
ATOM   2545  C  BTYR A 151      24.069  -5.882   4.794  0.43 19.15           C  
ANISOU 2545  C  BTYR A 151     2135   1738   3404   -559    592   -669       C  
ATOM   2546  O  ATYR A 151      24.187  -5.221   3.708  0.57 19.58           O  
ANISOU 2546  O  ATYR A 151     1961   1952   3527   -503    205   -737       O  
ATOM   2547  O  BTYR A 151      24.356  -5.043   3.933  0.43 19.90           O  
ANISOU 2547  O  BTYR A 151     2183   1819   3561   -353    419   -631       O  
ATOM   2548  CB ATYR A 151      26.328  -6.000   5.684  0.57 13.88           C  
ANISOU 2548  CB ATYR A 151     2080   1234   1958   -589    273   -508       C  
ATOM   2549  CB BTYR A 151      26.286  -6.307   5.939  0.43 16.53           C  
ANISOU 2549  CB BTYR A 151     2060   1637   2585   -241    675   -700       C  
ATOM   2550  CG ATYR A 151      26.099  -5.067   6.874  0.57 14.28           C  
ANISOU 2550  CG ATYR A 151     2193   1202   2032   -476    316   -422       C  
ATOM   2551  CG BTYR A 151      27.125  -7.363   6.629  0.43 16.57           C  
ANISOU 2551  CG BTYR A 151     1973   1653   2671   -266    740   -591       C  
ATOM   2552  CD1ATYR A 151      26.555  -3.755   6.837  0.57 14.32           C  
ANISOU 2552  CD1ATYR A 151     2142   1264   2037   -501    318   -576       C  
ATOM   2553  CD1BTYR A 151      26.803  -7.794   7.907  0.43 17.02           C  
ANISOU 2553  CD1BTYR A 151     1998   1672   2797   -291    726   -559       C  
ATOM   2554  CD2ATYR A 151      25.471  -5.500   8.032  0.57 16.09           C  
ANISOU 2554  CD2ATYR A 151     2384   1274   2456   -457    341   -413       C  
ATOM   2555  CD2BTYR A 151      28.222  -7.944   5.999  0.43 16.46           C  
ANISOU 2555  CD2BTYR A 151     1920   1602   2732   -303    649   -711       C  
ATOM   2556  CE1ATYR A 151      26.383  -2.891   7.910  0.57 15.50           C  
ANISOU 2556  CE1ATYR A 151     2213   1373   2303   -556    405   -465       C  
ATOM   2557  CE1BTYR A 151      27.548  -8.760   8.544  0.43 17.46           C  
ANISOU 2557  CE1BTYR A 151     1897   1846   2891   -253    595   -737       C  
ATOM   2558  CE2ATYR A 151      25.286  -4.635   9.118  0.57 16.80           C  
ANISOU 2558  CE2ATYR A 151     2472   1300   2613   -444    532   -326       C  
ATOM   2559  CE2BTYR A 151      28.977  -8.925   6.635  0.43 17.19           C  
ANISOU 2559  CE2BTYR A 151     1873   1709   2949   -246    629   -945       C  
ATOM   2560  CZ ATYR A 151      25.747  -3.328   9.047  0.57 15.45           C  
ANISOU 2560  CZ ATYR A 151     2380   1203   2288   -532    546   -537       C  
ATOM   2561  CZ BTYR A 151      28.638  -9.318   7.912  0.43 17.25           C  
ANISOU 2561  CZ BTYR A 151     1806   1828   2921   -302    596   -778       C  
ATOM   2562  OH ATYR A 151      25.593  -2.434  10.098  0.57 16.87           O  
ANISOU 2562  OH ATYR A 151     2513   1285   2613   -504    617   -522       O  
ATOM   2563  OH BTYR A 151      29.357 -10.285   8.577  0.43 18.72           O  
ANISOU 2563  OH BTYR A 151     1787   2189   3137   -263    667   -698       O  
ATOM   2564  H  ATYR A 151      25.896  -7.257   3.432  0.57 16.56           H  
ATOM   2565  H  BTYR A 151      25.819  -7.239   3.423  0.43 17.95           H  
ATOM   2566  HA ATYR A 151      24.805  -7.387   5.928  0.57 18.06           H  
ATOM   2567  HA BTYR A 151      24.644  -7.520   5.857  0.43 19.95           H  
ATOM   2568  HB2ATYR A 151      27.042  -6.607   5.934  0.57 16.65           H  
ATOM   2569  HB2BTYR A 151      26.843  -5.852   5.289  0.43 19.84           H  
ATOM   2570  HB3ATYR A 151      26.625  -5.447   4.945  0.57 16.65           H  
ATOM   2571  HB3BTYR A 151      25.973  -5.680   6.610  0.43 19.84           H  
ATOM   2572  HD1ATYR A 151      26.987  -3.447   6.073  0.57 17.19           H  
ATOM   2573  HD1BTYR A 151      26.073  -7.420   8.344  0.43 20.42           H  
ATOM   2574  HD2ATYR A 151      25.160  -6.375   8.086  0.57 19.31           H  
ATOM   2575  HD2BTYR A 151      28.453  -7.675   5.140  0.43 19.75           H  
ATOM   2576  HE1ATYR A 151      26.692  -2.015   7.857  0.57 18.60           H  
ATOM   2577  HE1BTYR A 151      27.319  -9.031   9.404  0.43 20.95           H  
ATOM   2578  HE2ATYR A 151      24.858  -4.937   9.887  0.57 20.17           H  
ATOM   2579  HE2BTYR A 151      29.712  -9.302   6.207  0.43 20.63           H  
ATOM   2580  HH ATYR A 151      25.194  -2.806  10.736  0.57 20.25           H  
ATOM   2581  HH BTYR A 151      29.993 -10.550   8.098  0.43 22.46           H  
ATOM   2582  N   GLN A 152      22.887  -5.921   5.411  1.00 22.66           N  
ANISOU 2582  N   GLN A 152     2342   2019   4248   -582    346   -927       N  
ATOM   2583  CA  GLN A 152      21.818  -5.021   4.996  1.00 31.44           C  
ANISOU 2583  CA  GLN A 152     3009   2807   6130   -255    124  -1377       C  
ATOM   2584  C   GLN A 152      22.171  -3.568   5.258  1.00 32.22           C  
ANISOU 2584  C   GLN A 152     3052   2768   6422   -290     93  -1549       C  
ATOM   2585  O   GLN A 152      21.747  -2.689   4.499  1.00 34.82           O  
ANISOU 2585  O   GLN A 152     3283   3096   6853   -227    -53  -1570       O  
ATOM   2586  CB  GLN A 152      20.487  -5.383   5.659  1.00 40.00           C  
ANISOU 2586  CB  GLN A 152     3778   3803   7617    352   -179  -1457       C  
ATOM   2587  CG  GLN A 152      19.322  -5.418   4.668  1.00 47.09           C  
ANISOU 2587  CG  GLN A 152     4463   4684   8743   1003   -394  -1497       C  
ATOM   2588  CD  GLN A 152      19.608  -6.322   3.476  1.00 52.32           C  
ANISOU 2588  CD  GLN A 152     4958   5408   9512   1469   -526  -1534       C  
ATOM   2589  OE1 GLN A 152      20.374  -7.279   3.583  1.00 54.38           O  
ANISOU 2589  OE1 GLN A 152     5124   5638   9901   1591   -533  -1521       O  
ATOM   2590  NE2 GLN A 152      19.018  -6.003   2.329  1.00 53.82           N  
ANISOU 2590  NE2 GLN A 152     5132   5683   9635   1594   -631  -1543       N  
ATOM   2591  H   GLN A 152      22.706  -6.431   6.079  1.00 27.19           H  
ATOM   2592  HA  GLN A 152      21.697  -5.118   4.038  1.00 37.73           H  
ATOM   2593  HB2 GLN A 152      20.563  -6.262   6.062  1.00 48.00           H  
ATOM   2594  HB3 GLN A 152      20.282  -4.723   6.339  1.00 48.00           H  
ATOM   2595  HG2 GLN A 152      18.531  -5.754   5.119  1.00 56.50           H  
ATOM   2596  HG3 GLN A 152      19.161  -4.521   4.336  1.00 56.50           H  
ATOM   2597 HE21 GLN A 152      18.504  -5.315   2.287  1.00 64.59           H  
ATOM   2598 HE22 GLN A 152      19.150  -6.484   1.629  1.00 64.59           H  
ATOM   2599  N   GLY A 153      22.946  -3.296   6.301  1.00 29.17           N  
ANISOU 2599  N   GLY A 153     2784   2411   5887   -593    264  -1545       N  
ATOM   2600  CA  GLY A 153      23.326  -1.934   6.618  1.00 28.46           C  
ANISOU 2600  CA  GLY A 153     2705   2411   5700   -688    559  -1455       C  
ATOM   2601  C   GLY A 153      22.182  -1.142   7.211  1.00 26.84           C  
ANISOU 2601  C   GLY A 153     2585   2431   5181   -867    749  -1366       C  
ATOM   2602  O   GLY A 153      21.153  -1.696   7.618  1.00 28.20           O  
ANISOU 2602  O   GLY A 153     2744   2545   5425   -625    929  -1097       O  
ATOM   2603  OXT GLY A 153      22.279   0.078   7.302  1.00 24.87           O  
ANISOU 2603  OXT GLY A 153     2534   2365   4551   -854    729  -1413       O  
ATOM   2604  H   GLY A 153      23.264  -3.886   6.840  1.00 35.00           H  
ATOM   2605  HA2 GLY A 153      24.057  -1.942   7.255  1.00 34.16           H  
ATOM   2606  HA3 GLY A 153      23.625  -1.486   5.811  1.00 34.16           H  
TER    2607      GLY A 153                                                      
HETATM 2608  C1  GLC B   1      46.467   3.518   3.754  1.00 43.22           C  
HETATM 2609  C2  GLC B   1      47.583   4.550   3.926  1.00 20.50           C  
HETATM 2610  C3  GLC B   1      47.439   5.683   2.919  1.00 23.61           C  
HETATM 2611  C4  GLC B   1      47.393   5.113   1.506  1.00 27.99           C  
HETATM 2612  C5  GLC B   1      46.330   4.013   1.423  1.00 36.76           C  
HETATM 2613  C6  GLC B   1      46.334   3.323   0.060  1.00 57.35           C  
HETATM 2614  O2  GLC B   1      47.590   5.081   5.236  1.00 17.38           O  
HETATM 2615  O3  GLC B   1      48.521   6.583   3.064  1.00 25.47           O  
HETATM 2616  O4  GLC B   1      47.115   6.153   0.582  1.00 22.38           O  
HETATM 2617  O5  GLC B   1      46.533   3.029   2.425  1.00 25.39           O  
HETATM 2618  O6  GLC B   1      47.558   2.654  -0.158  1.00 30.00           O  
HETATM 2619  H1  GLC B   1      46.647   2.700   4.452  1.00 51.86           H  
HETATM 2620  H2  GLC B   1      48.534   4.052   3.738  1.00 24.60           H  
HETATM 2621  H3  GLC B   1      46.500   6.203   3.113  1.00 28.33           H  
HETATM 2622  H4  GLC B   1      48.364   4.673   1.280  1.00 33.58           H  
HETATM 2623  H5  GLC B   1      45.353   4.474   1.566  1.00 44.11           H  
HETATM 2624  H61 GLC B   1      46.179   4.064  -0.724  1.00 68.82           H  
HETATM 2625  H62 GLC B   1      45.514   2.606   0.012  1.00 68.82           H  
HETATM 2626  HO2 GLC B   1      46.871   4.669   5.759  1.00 20.85           H  
HETATM 2627  HO3 GLC B   1      49.113   6.269   3.779  1.00 30.56           H  
HETATM 2628  HO4 GLC B   1      47.016   7.000   1.065  1.00 26.85           H  
HETATM 2629  HO6 GLC B   1      48.142   2.780   0.619  1.00 36.00           H  
HETATM 2630  C1  FRU B   2      44.686   3.452   6.299  1.00 28.11           C  
HETATM 2631  C2  FRU B   2      44.300   3.323   4.820  1.00 70.92           C  
HETATM 2632  C3  FRU B   2      42.852   3.780   4.580  1.00 15.35           C  
HETATM 2633  C4  FRU B   2      42.364   2.839   3.490  1.00 24.44           C  
HETATM 2634  C5  FRU B   2      43.120   1.555   3.822  1.00 52.61           C  
HETATM 2635  C6  FRU B   2      43.343   0.641   2.614  1.00 28.67           C  
HETATM 2636  O1  FRU B   2      43.817   2.724   7.152  1.00 18.02           O  
HETATM 2637  O2  FRU B   2      45.198   4.100   4.022  1.00 20.75           O  
HETATM 2638  O3  FRU B   2      42.783   5.154   4.249  1.00 18.62           O  
HETATM 2639  O4  FRU B   2      40.959   2.633   3.496  1.00 18.64           O  
HETATM 2640  O5  FRU B   2      44.347   1.957   4.423  1.00 27.38           O  
HETATM 2641  O6  FRU B   2      44.177   1.271   1.662  1.00 35.52           O  
HETATM 2642  H11 FRU B   2      44.667   4.505   6.584  1.00 33.74           H  
HETATM 2643  H12 FRU B   2      45.706   3.092   6.436  1.00 33.74           H  
HETATM 2644  H3  FRU B   2      42.275   3.591   5.485  1.00 18.42           H  
HETATM 2645  H4  FRU B   2      42.692   3.210   2.520  1.00 29.33           H  
HETATM 2646  H5  FRU B   2      42.532   1.001   4.554  1.00 63.14           H  
HETATM 2647  H61 FRU B   2      42.383   0.401   2.156  1.00 34.40           H  
HETATM 2648  H62 FRU B   2      43.802  -0.291   2.941  1.00 34.40           H  
HETATM 2649  HO1 FRU B   2      44.300   2.460   7.963  1.00 21.62           H  
HETATM 2650  HO3 FRU B   2      43.686   5.534   4.243  1.00 22.34           H  
HETATM 2651  HO4 FRU B   2      40.556   3.152   4.224  1.00 22.37           H  
HETATM 2652  HO6 FRU B   2      44.431   2.160   1.987  1.00 42.63           H  
HETATM 2653  S   SO4 A 201      26.529  30.823  -2.670  1.00 49.36           S  
ANISOU 2653  S   SO4 A 201     5639   7305   5811   -107    660   3768       S  
HETATM 2654  O1  SO4 A 201      25.980  31.894  -3.504  1.00 52.09           O  
ANISOU 2654  O1  SO4 A 201     5818   7523   6451     53    557   3881       O  
HETATM 2655  O2  SO4 A 201      26.263  29.530  -3.291  1.00 45.20           O  
ANISOU 2655  O2  SO4 A 201     5541   6761   4872   -182    467   3298       O  
HETATM 2656  O3  SO4 A 201      27.973  31.029  -2.531  1.00 52.19           O  
ANISOU 2656  O3  SO4 A 201     5753   7525   6552    -79    619   3704       O  
HETATM 2657  O4  SO4 A 201      25.916  30.881  -1.343  1.00 48.90           O  
ANISOU 2657  O4  SO4 A 201     5693   7226   5659   -126    817   3643       O  
HETATM 2658  CHA HEM A 202      38.044   2.531  11.269  1.00  9.18           C  
ANISOU 2658  CHA HEM A 202     1200    904   1384     35    -60     62       C  
HETATM 2659  CHB HEM A 202      37.171   5.380   7.453  1.00  8.27           C  
ANISOU 2659  CHB HEM A 202      992    797   1353    -82     33   -123       C  
HETATM 2660  CHC HEM A 202      32.724   6.289   9.176  1.00  8.99           C  
ANISOU 2660  CHC HEM A 202     1217    862   1337    -15    131    -31       C  
HETATM 2661  CHD HEM A 202      33.559   3.285  12.884  1.00  9.43           C  
ANISOU 2661  CHD HEM A 202     1303    724   1556    -78    131    -56       C  
HETATM 2662  C1A HEM A 202      38.187   3.188  10.067  1.00  9.00           C  
ANISOU 2662  C1A HEM A 202     1178    821   1420     42    -86   -157       C  
HETATM 2663  C2A HEM A 202      39.368   3.155   9.216  1.00  9.56           C  
ANISOU 2663  C2A HEM A 202     1217    846   1569     17    -99   -182       C  
HETATM 2664  C3A HEM A 202      39.136   3.967   8.167  1.00  8.80           C  
ANISOU 2664  C3A HEM A 202     1212    847   1283    -85    -78   -173       C  
HETATM 2665  C4A HEM A 202      37.807   4.520   8.329  1.00  8.01           C  
ANISOU 2665  C4A HEM A 202     1041    727   1276   -113     63    -59       C  
HETATM 2666  CMA HEM A 202      40.051   4.275   6.972  1.00 10.01           C  
ANISOU 2666  CMA HEM A 202     1215   1154   1434    202    -10   -124       C  
HETATM 2667  CAA HEM A 202      40.638   2.310   9.443  1.00  9.86           C  
ANISOU 2667  CAA HEM A 202     1232    895   1621     57   -224   -132       C  
HETATM 2668  CBA HEM A 202      40.677   1.129   8.452  1.00 10.94           C  
ANISOU 2668  CBA HEM A 202     1220    985   1953     28   -238   -261       C  
HETATM 2669  CGA HEM A 202      39.413   0.300   8.471  1.00 12.47           C  
ANISOU 2669  CGA HEM A 202     1434   1051   2254    138   -330   -170       C  
HETATM 2670  O1A HEM A 202      39.155  -0.375   9.500  1.00 12.78           O  
ANISOU 2670  O1A HEM A 202     1747   1025   2085    -54   -205   -231       O  
HETATM 2671  O2A HEM A 202      38.671   0.294   7.457  1.00 12.83           O  
ANISOU 2671  O2A HEM A 202     1475   1100   2299   -152   -421    -55       O  
HETATM 2672  C1B HEM A 202      35.887   5.881   7.586  1.00  8.27           C  
ANISOU 2672  C1B HEM A 202     1137    617   1387   -107     58    -27       C  
HETATM 2673  C2B HEM A 202      35.236   6.799   6.672  1.00  8.18           C  
ANISOU 2673  C2B HEM A 202     1145    689   1273    -51     53   -108       C  
HETATM 2674  C3B HEM A 202      34.005   7.053   7.151  1.00  8.52           C  
ANISOU 2674  C3B HEM A 202     1093    744   1399    -17     86    -74       C  
HETATM 2675  C4B HEM A 202      33.850   6.287   8.377  1.00  8.47           C  
ANISOU 2675  C4B HEM A 202     1119    726   1372    -74    204    -67       C  
HETATM 2676  CMB HEM A 202      35.903   7.312   5.391  1.00  8.44           C  
ANISOU 2676  CMB HEM A 202     1075    884   1248      2     51    -26       C  
HETATM 2677  CAB HEM A 202      32.914   7.974   6.602  1.00  9.01           C  
ANISOU 2677  CAB HEM A 202     1041   1015   1366     -8    172     51       C  
HETATM 2678  CBB HEM A 202      33.178   9.124   5.978  1.00 10.50           C  
ANISOU 2678  CBB HEM A 202     1050   1163   1777     87    195    138       C  
HETATM 2679  C1C HEM A 202      32.576   5.588  10.360  1.00  9.20           C  
ANISOU 2679  C1C HEM A 202     1362    748   1385    -18     90    -39       C  
HETATM 2680  C2C HEM A 202      31.450   5.704  11.271  1.00  9.41           C  
ANISOU 2680  C2C HEM A 202     1353    695   1526   -157    273   -113       C  
HETATM 2681  C3C HEM A 202      31.684   4.882  12.310  1.00  9.50           C  
ANISOU 2681  C3C HEM A 202     1476    671   1463   -140    186   -117       C  
HETATM 2682  C4C HEM A 202      32.954   4.226  12.074  1.00  8.75           C  
ANISOU 2682  C4C HEM A 202     1351    606   1369    -13    209   -133       C  
HETATM 2683  CMC HEM A 202      30.247   6.637  11.025  1.00 10.18           C  
ANISOU 2683  CMC HEM A 202     1341    921   1608    -62    366   -138       C  
HETATM 2684  CAC HEM A 202      30.862   4.618  13.582  1.00 10.36           C  
ANISOU 2684  CAC HEM A 202     1588    853   1496    -99    212    -92       C  
HETATM 2685  CBC HEM A 202      29.695   5.182  13.921  1.00 11.49           C  
ANISOU 2685  CBC HEM A 202     1541   1175   1651   -147    371      6       C  
HETATM 2686  C1D HEM A 202      34.855   2.831  12.787  1.00  9.41           C  
ANISOU 2686  C1D HEM A 202     1380    817   1378    -14    124     37       C  
HETATM 2687  C2D HEM A 202      35.546   2.063  13.794  1.00 10.85           C  
ANISOU 2687  C2D HEM A 202     1525   1016   1581     -3    118    -41       C  
HETATM 2688  C3D HEM A 202      36.795   1.879  13.358  1.00 10.10           C  
ANISOU 2688  C3D HEM A 202     1369   1041   1430    -42    -77    -25       C  
HETATM 2689  C4D HEM A 202      36.919   2.524  12.064  1.00  9.42           C  
ANISOU 2689  C4D HEM A 202     1349    909   1322    -21     83     60       C  
HETATM 2690  CMD HEM A 202      34.932   1.579  15.119  1.00 11.64           C  
ANISOU 2690  CMD HEM A 202     1732   1276   1415    146    156    130       C  
HETATM 2691  CAD HEM A 202      37.954   1.217  14.129  1.00 12.31           C  
ANISOU 2691  CAD HEM A 202     1681   1369   1628    -25   -241    -72       C  
HETATM 2692  CBD HEM A 202      38.563   2.394  14.949  1.00 15.08           C  
ANISOU 2692  CBD HEM A 202     1921   2012   1798     46   -183     29       C  
HETATM 2693  CGD HEM A 202      39.708   2.067  15.877  1.00 18.59           C  
ANISOU 2693  CGD HEM A 202     2314   2738   2012    337   -184   -241       C  
HETATM 2694  O1D HEM A 202      39.587   2.287  17.109  1.00 21.12           O  
ANISOU 2694  O1D HEM A 202     2538   3213   2272    285   -282    -73       O  
HETATM 2695  O2D HEM A 202      40.768   1.621  15.398  1.00 20.66           O  
ANISOU 2695  O2D HEM A 202     2339   3236   2275    741   -441   -260       O  
HETATM 2696  NA  HEM A 202      37.245   4.021   9.495  1.00  8.77           N  
ANISOU 2696  NA  HEM A 202     1096    706   1532     -4    -22    -45       N  
HETATM 2697  NB  HEM A 202      35.019   5.589   8.619  1.00  8.30           N  
ANISOU 2697  NB  HEM A 202     1115    679   1358    -58     58    -11       N  
HETATM 2698  NC  HEM A 202      33.469   4.677  10.876  1.00  8.53           N  
ANISOU 2698  NC  HEM A 202     1263    635   1343   -200    164     20       N  
HETATM 2699  ND  HEM A 202      35.715   3.110  11.753  1.00  9.32           N  
ANISOU 2699  ND  HEM A 202     1339    905   1296    -58     13   -104       N  
HETATM 2700 FE   HEM A 202      35.341   4.280  10.142  1.00  8.41          FE  
ANISOU 2700 FE   HEM A 202     1197    696   1303    -65     87    -66      FE  
HETATM 2701  HHB HEM A 202      37.677   5.663   6.663  1.00  9.92           H  
HETATM 2702  HHC HEM A 202      32.012   6.919   8.941  1.00 10.79           H  
HETATM 2703  HHD HEM A 202      33.011   2.902  13.601  1.00 11.31           H  
HETATM 2704  HMA HEM A 202      40.887   4.671   7.295  1.00 12.01           H  
HETATM 2705 HMAA HEM A 202      39.601   4.905   6.371  1.00 12.01           H  
HETATM 2706 HMAB HEM A 202      40.247   3.446   6.489  1.00 12.01           H  
HETATM 2707  HAA HEM A 202      40.638   1.968  10.351  1.00 11.84           H  
HETATM 2708 HAAA HEM A 202      41.422   2.867   9.311  1.00 11.84           H  
HETATM 2709  HBA HEM A 202      41.428   0.558   8.676  1.00 13.13           H  
HETATM 2710 HBAA HEM A 202      40.807   1.478   7.556  1.00 13.13           H  
HETATM 2711  HMB HEM A 202      35.297   7.912   4.929  1.00 10.13           H  
HETATM 2712 HMBA HEM A 202      36.117   6.561   4.815  1.00 10.13           H  
HETATM 2713 HMBB HEM A 202      36.718   7.787   5.618  1.00 10.13           H  
HETATM 2714  HAB HEM A 202      31.997   7.713   6.712  1.00 10.81           H  
HETATM 2715  HBB HEM A 202      32.450   9.676   5.652  1.00 12.60           H  
HETATM 2716 HBBA HEM A 202      34.096   9.409   5.855  1.00 12.60           H  
HETATM 2717  HMC HEM A 202      29.618   6.553  11.759  1.00 12.22           H  
HETATM 2718 HMCA HEM A 202      29.811   6.391  10.195  1.00 12.22           H  
HETATM 2719 HMCB HEM A 202      30.556   7.555  10.968  1.00 12.22           H  
HETATM 2720  HAC HEM A 202      31.224   3.980  14.200  1.00 12.43           H  
HETATM 2721  HBC HEM A 202      29.263   4.939  14.755  1.00 13.79           H  
HETATM 2722 HBCA HEM A 202      29.282   5.834  13.334  1.00 13.79           H  
HETATM 2723  HMD HEM A 202      34.634   2.352  15.642  1.00 13.97           H  
HETATM 2724 HMDA HEM A 202      35.604   1.079  15.627  1.00 13.97           H  
HETATM 2725 HMDB HEM A 202      34.166   0.998  14.931  1.00 13.97           H  
HETATM 2726  HAD HEM A 202      38.610   0.854  13.513  1.00 14.77           H  
HETATM 2727 HADA HEM A 202      37.619   0.525  14.720  1.00 14.77           H  
HETATM 2728  HBD HEM A 202      37.852   2.784  15.481  1.00 18.10           H  
HETATM 2729 HBDA HEM A 202      38.872   3.065  14.321  1.00 18.10           H  
HETATM 2730  HHA HEM A 202      38.816   2.019  11.589  1.00 11.02           H  
HETATM 2731  S   SO4 A 203      27.633  23.109 -13.091  1.00 93.67           S  
ANISOU 2731  S   SO4 A 203    13608  10109  11874   3015   -609   -908       S  
HETATM 2732  O1  SO4 A 203      26.716  24.246 -13.129  1.00 93.70           O  
ANISOU 2732  O1  SO4 A 203    13610  10130  11862   3014   -599   -920       O  
HETATM 2733  O2  SO4 A 203      27.665  22.470 -14.403  1.00 94.04           O  
ANISOU 2733  O2  SO4 A 203    13610  10120  12000   3035   -587   -850       O  
HETATM 2734  O3  SO4 A 203      27.176  22.151 -12.088  1.00 93.29           O  
ANISOU 2734  O3  SO4 A 203    13604  10088  11753   3026   -615   -903       O  
HETATM 2735  O4  SO4 A 203      28.973  23.572 -12.745  1.00 93.75           O  
ANISOU 2735  O4  SO4 A 203    13604  10143  11875   3026   -610   -859       O  
HETATM 2736  S   SO4 A 204      30.339  18.400  28.591  1.00 30.81           S  
ANISOU 2736  S   SO4 A 204     6055   3384   2267   2218  -1010   -318       S  
HETATM 2737  O1  SO4 A 204      30.737  17.778  27.335  1.00 27.01           O  
ANISOU 2737  O1  SO4 A 204     5178   3139   1944   1476   -956   -733       O  
HETATM 2738  O2  SO4 A 204      29.771  19.700  28.282  1.00 33.26           O  
ANISOU 2738  O2  SO4 A 204     6102   3623   2913   2534   -840   -206       O  
HETATM 2739  O3  SO4 A 204      31.357  18.629  29.599  1.00 29.96           O  
ANISOU 2739  O3  SO4 A 204     5745   3428   2211   1813  -1204   -767       O  
HETATM 2740  O4  SO4 A 204      29.373  17.505  29.237  1.00 33.84           O  
ANISOU 2740  O4  SO4 A 204     6270   3919   2669   2424   -990   -714       O  
HETATM 2741  O   HOH A 301      22.801  14.746  12.384  1.00 25.78           O  
ANISOU 2741  O   HOH A 301     1985   3643   4168     43    697   1267       O  
HETATM 2742  O   HOH A 302      43.645   5.544  17.733  1.00 38.44           O  
ANISOU 2742  O   HOH A 302     8560   2719   3328     -5   -259    -59       O  
HETATM 2743  O   HOH A 303      40.862  22.767  15.348  1.00 28.20           O  
ANISOU 2743  O   HOH A 303     4445   2410   3861    920  -1728   -531       O  
HETATM 2744  O   HOH A 304      28.479  32.120  -0.489  1.00 31.91           O  
ANISOU 2744  O   HOH A 304     4685   2099   5342   -675  -2139    908       O  
HETATM 2745  O   HOH A 305      33.557  -0.794  -4.584  1.00 38.60           O  
ANISOU 2745  O   HOH A 305     5308   2469   6890    636   -445  -1183       O  
HETATM 2746  O   HOH A 306      31.623   1.068  -5.759  1.00 33.42           O  
ANISOU 2746  O   HOH A 306     4547   4547   3603   1950    254     71       O  
HETATM 2747  O   HOH A 307      48.639  23.446   7.938  1.00 24.60           O  
ANISOU 2747  O   HOH A 307     1499   4589   3259   -451   -180   1618       O  
HETATM 2748  O   HOH A 308      25.522  -4.194  -6.471  1.00 37.34           O  
ANISOU 2748  O   HOH A 308     4522   5315   4351     -2    338    320       O  
HETATM 2749  O   HOH A 309      20.439   9.122  20.209  1.00 35.97           O  
HETATM 2750  O   HOH A 310      22.912  -1.449   2.109  1.00 33.03           O  
ANISOU 2750  O   HOH A 310     3186   3948   5416   -628    967    524       O  
HETATM 2751  O   HOH A 311      43.917  19.173  -1.717  1.00 32.83           O  
ANISOU 2751  O   HOH A 311     3782   6389   2301   1075     13   1439       O  
HETATM 2752  O   HOH A 312      20.427   9.630  16.964  1.00 23.45           O  
ANISOU 2752  O   HOH A 312     2495   3275   3138   -825    405    504       O  
HETATM 2753  O   HOH A 313      31.837   4.825 -11.048  1.00 55.60           O  
ANISOU 2753  O   HOH A 313    10147   2622   8354   -289   -692    280       O  
HETATM 2754  O   HOH A 314      42.758  24.694  12.562  1.00 36.04           O  
ANISOU 2754  O   HOH A 314     5489   4595   3611   2920    822    877       O  
HETATM 2755  O   HOH A 315      41.354   1.696  12.865  1.00 18.47           O  
ANISOU 2755  O   HOH A 315     2595   1790   2631    307   -253     56       O  
HETATM 2756  O   HOH A 316      43.367   6.845   6.157  1.00 15.09           O  
ANISOU 2756  O   HOH A 316     1879   1818   2035    408    559    158       O  
HETATM 2757  O   HOH A 317      20.842   2.032   8.289  1.00 19.27           O  
ANISOU 2757  O   HOH A 317     1918   1663   3742   -722    416   -680       O  
HETATM 2758  O   HOH A 318      37.086  19.575  18.787  1.00 26.07           O  
ANISOU 2758  O   HOH A 318     4320   3375   2210    703   -417    492       O  
HETATM 2759  O   HOH A 319      31.869   6.028  30.569  1.00 41.13           O  
HETATM 2760  O   HOH A 320      39.974  17.288  -9.987  1.00 53.10           O  
ANISOU 2760  O   HOH A 320     9865   6562   3750   3283   -488    125       O  
HETATM 2761  O   HOH A 321      35.922  27.902  -5.915  1.00 51.08           O  
ANISOU 2761  O   HOH A 321     6617   6875   5917    722    578   1813       O  
HETATM 2762  O   HOH A 322      44.104  15.419  21.771  1.00 37.40           O  
ANISOU 2762  O   HOH A 322     3600   7002   3607   1261    839   1559       O  
HETATM 2763  O   HOH A 323      41.304   5.359  24.273  1.00 30.35           O  
ANISOU 2763  O   HOH A 323     4062   2409   5059     94   -951   1030       O  
HETATM 2764  O   HOH A 324      41.213   8.046  24.790  1.00 29.27           O  
ANISOU 2764  O   HOH A 324     5678   3328   2114    729   -103    713       O  
HETATM 2765  O   HOH A 325      24.082  -3.284  12.119  1.00 47.72           O  
ANISOU 2765  O   HOH A 325     6738   4534   6860   -578   4039   -800       O  
HETATM 2766  O   HOH A 326      36.671   1.985  26.073  1.00 37.21           O  
ANISOU 2766  O   HOH A 326     4947   5658   3532   -270    238    376       O  
HETATM 2767  O   HOH A 327      43.377   6.517   2.032  1.00 32.20           O  
ANISOU 2767  O   HOH A 327     3310   4319   4607   1828   1514   1924       O  
HETATM 2768  O   HOH A 328      40.575  -0.671  11.743  1.00 26.07           O  
ANISOU 2768  O   HOH A 328     3838   2898   3171    549   -667    821       O  
HETATM 2769  O   HOH A 329      44.084  -0.196  -0.583  1.00 43.47           O  
ANISOU 2769  O   HOH A 329     3985   4431   8100    822  -2163  -2487       O  
HETATM 2770  O   HOH A 330      20.187   5.499  15.715  1.00 27.46           O  
ANISOU 2770  O   HOH A 330     3388   3706   3339   -302    810   -139       O  
HETATM 2771  O   HOH A 331      22.268   7.304   2.800  1.00 17.76           O  
ANISOU 2771  O   HOH A 331     1991   1931   2828   -641   -171   -432       O  
HETATM 2772  O   HOH A 332      44.843   3.002   9.630  1.00 30.62           O  
ANISOU 2772  O   HOH A 332     3503   3770   4362   1956  -1014   -788       O  
HETATM 2773  O   HOH A 333      36.774  24.486  15.887  1.00 35.06           O  
ANISOU 2773  O   HOH A 333     5925   2342   5053  -1051    487  -1288       O  
HETATM 2774  O   HOH A 334      24.582  14.533  23.661  1.00 34.03           O  
HETATM 2775  O   HOH A 335      33.586  25.847  14.504  1.00 34.66           O  
ANISOU 2775  O   HOH A 335     3706   4402   5060    670    544  -1656       O  
HETATM 2776  O   HOH A 336      42.509  14.547   2.874  1.00 13.23           O  
ANISOU 2776  O   HOH A 336     1797   1285   1945     20   -161    -14       O  
HETATM 2777  O   HOH A 337      35.040  15.483 -13.619  1.00 22.40           O  
ANISOU 2777  O   HOH A 337     4887   1973   1650   -335   -470   -195       O  
HETATM 2778  O   HOH A 338      39.946   3.194   1.040  1.00 14.62           O  
ANISOU 2778  O   HOH A 338     2148   1294   2113    -75   -414     75       O  
HETATM 2779  O   HOH A 339      47.144  19.570  12.200  1.00 16.51           O  
ANISOU 2779  O   HOH A 339     2485   1836   1950   -752    445    -36       O  
HETATM 2780  O   HOH A 340      38.175  29.290   7.630  1.00 24.01           O  
ANISOU 2780  O   HOH A 340     2945   3313   2865  -1619   1319  -1462       O  
HETATM 2781  O   HOH A 341      26.048   2.005  -6.663  1.00 36.99           O  
ANISOU 2781  O   HOH A 341     6903   3700   3451  -2632  -1211    427       O  
HETATM 2782  O   HOH A 342      25.566   1.900  18.238  1.00 23.23           O  
ANISOU 2782  O   HOH A 342     3592   2397   2836   -490    315   -290       O  
HETATM 2783  O   HOH A 343      22.741   1.904  -3.082  1.00 19.14           O  
ANISOU 2783  O   HOH A 343     1501   1676   4096   -226   -680    139       O  
HETATM 2784  O   HOH A 344      25.858  22.941  -6.139  1.00 24.57           O  
ANISOU 2784  O   HOH A 344     4467   1891   2978    245  -2091   -248       O  
HETATM 2785  O   HOH A 345      43.940  -0.006   6.927  1.00 17.90           O  
ANISOU 2785  O   HOH A 345     1914   1747   3139    -14    145    329       O  
HETATM 2786  O   HOH A 346      22.277  26.261  -4.002  1.00 20.31           O  
ANISOU 2786  O   HOH A 346     2331   2894   2492   -501   -251   -332       O  
HETATM 2787  O   HOH A 347      27.255   6.512  23.985  1.00 26.54           O  
ANISOU 2787  O   HOH A 347     3260   4660   2165   -266    352   -213       O  
HETATM 2788  O   HOH A 348      30.733  30.427  11.094  1.00 23.59           O  
ANISOU 2788  O   HOH A 348     1893   2044   5025    405   -664  -1402       O  
HETATM 2789  O   HOH A 349      37.312   1.772  18.556  1.00 21.08           O  
ANISOU 2789  O   HOH A 349     2822   2837   2353    593     84    357       O  
HETATM 2790  O   HOH A 350      30.972  -1.674  -8.141  1.00 54.31           O  
ANISOU 2790  O   HOH A 350     7597   3861   9176   -986   1474  -1420       O  
HETATM 2791  O   HOH A 351      42.676   9.639  -4.392  1.00 14.06           O  
ANISOU 2791  O   HOH A 351     1369   2195   1776   -115    292   -493       O  
HETATM 2792  O   HOH A 352      37.996  22.062 -13.603  1.00 44.39           O  
HETATM 2793  O   HOH A 353      39.406  10.172 -10.938  1.00 23.25           O  
ANISOU 2793  O   HOH A 353     2393   4145   2296   -284    554   -961       O  
HETATM 2794  O   HOH A 354      40.721  -2.249  -3.703  1.00 21.72           O  
ANISOU 2794  O   HOH A 354     2884   2554   2816   1245    673    554       O  
HETATM 2795  O   HOH A 355      43.259   6.892  -4.158  1.00 22.01           O  
ANISOU 2795  O   HOH A 355     1640   2272   4449    -94    -85   -896       O  
HETATM 2796  O   HOH A 356      26.844   5.210  -8.619  1.00 32.15           O  
ANISOU 2796  O   HOH A 356     5268   3559   3387  -1659  -2071    992       O  
HETATM 2797  O   HOH A 357      41.068  11.873  -9.830  1.00 45.39           O  
ANISOU 2797  O   HOH A 357     6070   5059   6118  -2324   2999   -975       O  
HETATM 2798  O   HOH A 358      21.899  13.626   2.065  1.00 18.87           O  
ANISOU 2798  O   HOH A 358     1608   1389   4174    -68    237    472       O  
HETATM 2799  O   HOH A 359      34.054  25.495  -2.209  1.00 12.60           O  
ANISOU 2799  O   HOH A 359     1766   1426   1597   -136     89   -282       O  
HETATM 2800  O   HOH A 360      35.386  -2.231  15.620  1.00 22.94           O  
ANISOU 2800  O   HOH A 360     4509   2340   1866   -634   -477    129       O  
HETATM 2801  O   HOH A 361      31.487  12.891 -12.057  1.00 12.70           O  
ANISOU 2801  O   HOH A 361     2107   1429   1288     89   -169   -258       O  
HETATM 2802  O   HOH A 362      43.339   5.350  13.198  1.00 17.56           O  
ANISOU 2802  O   HOH A 362     2220   1836   2615     78   -301    561       O  
HETATM 2803  O   HOH A 363      40.142  18.842  26.929  1.00 24.58           O  
ANISOU 2803  O   HOH A 363     3944   2287   3107   -568   -343   -741       O  
HETATM 2804  O   HOH A 364      32.358  -1.667  16.220  1.00 22.78           O  
ANISOU 2804  O   HOH A 364     4641   1378   2636    -58     98   -564       O  
HETATM 2805  O   HOH A 365      44.182  19.075  16.888  1.00 35.67           O  
ANISOU 2805  O   HOH A 365     3344   5200   5008  -1694   -611   1582       O  
HETATM 2806  O   HOH A 366      24.444  30.120   6.729  1.00 21.48           O  
ANISOU 2806  O   HOH A 366     2737   2419   3006   1444   -454    211       O  
HETATM 2807  O   HOH A 367      45.840   5.772   9.448  1.00 27.40           O  
ANISOU 2807  O   HOH A 367     2946   3436   4031    258   1424  -1033       O  
HETATM 2808  O   HOH A 368      40.919  13.989  14.259  1.00 10.09           O  
ANISOU 2808  O   HOH A 368     1114   1141   1578     30     20    -68       O  
HETATM 2809  O   HOH A 369      27.177  24.964  11.162  1.00 15.76           O  
ANISOU 2809  O   HOH A 369     1703   1738   2549    168    583     89       O  
HETATM 2810  O   HOH A 370      33.055  25.161  -9.429  1.00 24.01           O  
ANISOU 2810  O   HOH A 370     5122   1822   2179   -796    820   -122       O  
HETATM 2811  O   HOH A 371      40.824  14.315  20.346  1.00 12.65           O  
ANISOU 2811  O   HOH A 371     1848   1738   1219     96     53    173       O  
HETATM 2812  O   HOH A 372      25.073  14.141   3.102  1.00 14.59           O  
ANISOU 2812  O   HOH A 372     1462    939   3144     24   -466   -100       O  
HETATM 2813  O   HOH A 373      30.503   6.604  -8.597  1.00 18.08           O  
ANISOU 2813  O   HOH A 373     1941   2419   2511    256    -45   -412       O  
HETATM 2814  O   HOH A 374      32.285  19.731  17.338  1.00 18.07           O  
ANISOU 2814  O   HOH A 374     2176   2039   2651     34    461   -911       O  
HETATM 2815  O   HOH A 375      43.348  12.234   1.650  1.00 11.87           O  
ANISOU 2815  O   HOH A 375     1579   1289   1643   -344    -96    -78       O  
HETATM 2816  O   HOH A 376      34.286  10.194  -5.156  1.00 10.30           O  
ANISOU 2816  O   HOH A 376     1335   1139   1438    177   -189    -46       O  
HETATM 2817  O   HOH A 377      27.372 -10.533  -3.858  1.00 23.71           O  
ANISOU 2817  O   HOH A 377     3513   2105   3392    653   -989  -1324       O  
HETATM 2818  O   HOH A 378      41.254  15.182  -8.053  1.00 24.55           O  
ANISOU 2818  O   HOH A 378     3211   2214   3904   -509   1132    371       O  
HETATM 2819  O   HOH A 379      40.603  11.865  27.438  1.00 23.01           O  
ANISOU 2819  O   HOH A 379     3293   2889   2562    640   -986     62       O  
HETATM 2820  O   HOH A 380      40.998  21.289  -7.263  1.00 48.29           O  
ANISOU 2820  O   HOH A 380     6370   8257   3719  -2330   -731    982       O  
HETATM 2821  O   HOH A 381      24.301  -4.234  -4.419  1.00 24.89           O  
ANISOU 2821  O   HOH A 381     2447   2262   4749      6  -1591   -838       O  
HETATM 2822  O   HOH A 382      39.779   0.393   4.874  1.00 15.73           O  
ANISOU 2822  O   HOH A 382     2186   1668   2123   -278   -455    -27       O  
HETATM 2823  O   HOH A 383      29.219  32.208   2.180  1.00 30.68           O  
ANISOU 2823  O   HOH A 383     2120   3056   6481    672   -756  -1261       O  
HETATM 2824  O   HOH A 384      34.442  29.752  12.279  1.00 16.92           O  
ANISOU 2824  O   HOH A 384     1612   1784   3034   -273    183  -1221       O  
HETATM 2825  O   HOH A 385      29.028  28.320   5.765  1.00 43.66           O  
ANISOU 2825  O   HOH A 385     5249   4846   6492   2246  -1619  -2606       O  
HETATM 2826  O   HOH A 386      20.478  15.818  -3.078  1.00 44.51           O  
ANISOU 2826  O   HOH A 386     5696   4224   6994   1535  -1985  -2156       O  
HETATM 2827  O   HOH A 387      22.732   8.045  -0.940  1.00 25.99           O  
ANISOU 2827  O   HOH A 387     1998   3048   4829   -757   1084  -1103       O  
HETATM 2828  O   HOH A 388      25.252  20.332  -6.308  1.00 19.28           O  
ANISOU 2828  O   HOH A 388     2551   2301   2474    584   -540   -650       O  
HETATM 2829  O   HOH A 389      29.190   0.100  -5.200  1.00 20.06           O  
ANISOU 2829  O   HOH A 389     2917   2174   2531   -114    232   -824       O  
HETATM 2830  O   HOH A 390      43.252   2.985  -4.735  1.00 37.31           O  
ANISOU 2830  O   HOH A 390     3025   3283   7867    976   -890  -1378       O  
HETATM 2831  O   HOH A 391      40.339   5.093 -10.851  1.00 49.93           O  
ANISOU 2831  O   HOH A 391     7956   5983   5034   -663   1453   2039       O  
HETATM 2832  O   HOH A 392      24.850   5.567  24.459  1.00 40.68           O  
ANISOU 2832  O   HOH A 392     4792   6513   4151   -169    962   -170       O  
HETATM 2833  O   HOH A 393      31.908  21.690  -0.958  1.00 15.30           O  
ANISOU 2833  O   HOH A 393     1910   1710   2193    143    159    -23       O  
HETATM 2834  O   HOH A 394      34.242  12.953 -12.401  1.00 14.74           O  
ANISOU 2834  O   HOH A 394     2259   1902   1441    372    -51     41       O  
HETATM 2835  O   HOH A 395      36.111   5.905  11.346  1.00 11.75           O  
ANISOU 2835  O   HOH A 395     1815    899   1753    -49    303     16       O  
HETATM 2836  O   HOH A 396      44.748  24.951   3.101  1.00 30.19           O  
ANISOU 2836  O   HOH A 396     3472   3222   4775  -1671     58    894       O  
HETATM 2837  O   HOH A 397      25.002  22.297  -9.870  1.00 41.08           O  
ANISOU 2837  O   HOH A 397     5894   4717   4996   2637   -879    929       O  
HETATM 2838  O   HOH A 398      38.925   6.080  11.336  1.00 12.86           O  
ANISOU 2838  O   HOH A 398     1840   1228   1820    -20     58    -70       O  
HETATM 2839  O   HOH A 399      27.907  11.926  23.756  1.00 30.99           O  
ANISOU 2839  O   HOH A 399     5857   3905   2013  -1348    202    351       O  
HETATM 2840  O   HOH A 400      31.698  31.640   0.363  1.00 36.69           O  
ANISOU 2840  O   HOH A 400     6204   5147   2589  -2655    -89    848       O  
HETATM 2841  O   HOH A 401      37.315  28.549   4.026  1.00 14.74           O  
ANISOU 2841  O   HOH A 401     2739    886   1975    -51    526    160       O  
HETATM 2842  O   HOH A 402      41.343  19.267  -2.601  1.00 29.44           O  
ANISOU 2842  O   HOH A 402     3453   4550   3184   2025   -784  -1134       O  
HETATM 2843  O   HOH A 403      21.018   9.400   1.334  1.00 33.41           O  
ANISOU 2843  O   HOH A 403     3240   3279   6174  -1150  -1741    183       O  
HETATM 2844  O   HOH A 404      30.285   7.041  27.252  1.00 31.91           O  
ANISOU 2844  O   HOH A 404     3827   4007   4292   -410    369   -783       O  
HETATM 2845  O   HOH A 405      33.744  23.253  14.178  1.00 24.57           O  
ANISOU 2845  O   HOH A 405     4251   2268   2815    611    283    457       O  
HETATM 2846  O   HOH A 406      28.258  14.910  28.664  1.00 45.18           O  
HETATM 2847  O   HOH A 407      25.797  14.245  13.226  1.00 16.17           O  
ANISOU 2847  O   HOH A 407     1936   1857   2349   -273    956   -515       O  
HETATM 2848  O   HOH A 408      44.699  20.844  15.382  1.00 33.62           O  
ANISOU 2848  O   HOH A 408     4216   5694   2864  -2642   -815    316       O  
HETATM 2849  O   HOH A 409      28.720  23.850  -9.879  1.00 37.45           O  
ANISOU 2849  O   HOH A 409     5587   3449   5192    601  -1327   -767       O  
HETATM 2850  O   HOH A 410      28.855  28.264  -2.701  1.00 14.92           O  
ANISOU 2850  O   HOH A 410     2122   1175   2373    192   -439     38       O  
HETATM 2851  O   HOH A 411      40.151   5.895   0.551  1.00 11.07           O  
ANISOU 2851  O   HOH A 411     1491    992   1722     96    -31   -105       O  
HETATM 2852  O   HOH A 412      21.923  -0.648  -2.359  1.00 28.52           O  
ANISOU 2852  O   HOH A 412     2341   2205   6289   -601   -677    470       O  
HETATM 2853  O   HOH A 413      39.540  21.003  17.186  1.00 38.65           O  
ANISOU 2853  O   HOH A 413     3758   7788   3140  -1934    413  -1868       O  
HETATM 2854  O   HOH A 414      28.824  -3.535  16.963  1.00 39.31           O  
ANISOU 2854  O   HOH A 414     5890   3733   5313   -950  -1007   2176       O  
HETATM 2855  O   HOH A 415      22.342  24.155  -2.491  1.00 30.92           O  
ANISOU 2855  O   HOH A 415     2313   3193   6243   -456  -1091   1212       O  
HETATM 2856  O   HOH A 416      30.909  21.468 -14.845  1.00 21.05           O  
ANISOU 2856  O   HOH A 416     3890   2343   1767    464   -433    319       O  
HETATM 2857  O   HOH A 417      40.252  18.815 -13.417  1.00 44.39           O  
ANISOU 2857  O   HOH A 417     7050   4258   5558   1539   1504    281       O  
HETATM 2858  O   HOH A 418      39.079   3.271  -7.966  1.00 25.04           O  
ANISOU 2858  O   HOH A 418     2902   3469   3142   1583   1305   1504       O  
HETATM 2859  O   HOH A 419      31.305  -4.921  15.878  1.00 37.93           O  
ANISOU 2859  O   HOH A 419     7424   3745   3243    354    571    -94       O  
HETATM 2860  O   HOH A 420      31.464   2.971  -7.365  1.00 31.14           O  
ANISOU 2860  O   HOH A 420     4546   3064   4221   -909   1142   -995       O  
HETATM 2861  O   HOH A 421      44.019   8.368  23.887  1.00 24.26           O  
ANISOU 2861  O   HOH A 421     4430   2338   2451    224   -703    522       O  
HETATM 2862  O   HOH A 422      31.242  29.032  -1.185  1.00 15.34           O  
ANISOU 2862  O   HOH A 422     2146   1749   1933   -213    -26    188       O  
HETATM 2863  O   HOH A 423      34.262  20.306  19.263  1.00 30.68           O  
ANISOU 2863  O   HOH A 423     3066   4429   4164   -171    280  -1382       O  
HETATM 2864  O   HOH A 424      48.510  20.914  10.168  1.00 13.35           O  
ANISOU 2864  O   HOH A 424     1201   1904   1966    103   -203     -3       O  
HETATM 2865  O   HOH A 425      19.457  15.441   1.194  1.00 44.59           O  
ANISOU 2865  O   HOH A 425     7266   2928   6750   1524   -212   1527       O  
HETATM 2866  O   HOH A 426      45.936   6.897   6.899  1.00 32.76           O  
ANISOU 2866  O   HOH A 426     3513   4491   4443     58   -354    191       O  
HETATM 2867  O   HOH A 427      45.111  10.410  25.116  1.00 28.83           O  
ANISOU 2867  O   HOH A 427     3482   5450   2024   1080   -924    107       O  
HETATM 2868  O   HOH A 428      31.625  10.139  -3.707  1.00 16.44           O  
ANISOU 2868  O   HOH A 428     1856   1550   2841   -199    532   -748       O  
HETATM 2869  O   HOH A 429      45.168  17.105  -3.168  1.00 34.53           O  
ANISOU 2869  O   HOH A 429     3552   3919   5648  -1851   1356   -388       O  
HETATM 2870  O   HOH A 430      26.933  24.504  16.399  1.00 58.65           O  
ANISOU 2870  O   HOH A 430     9631   6046   6608  -2621  -1043  -2177       O  
HETATM 2871  O   HOH A 431      29.550  10.488  26.055  1.00 36.45           O  
HETATM 2872  O   HOH A 432      29.346   4.605  24.438  1.00 32.07           O  
ANISOU 2872  O   HOH A 432     5275   4747   2164    530    282   -466       O  
HETATM 2873  O   HOH A 433      22.268  17.990  17.353  1.00 40.19           O  
ANISOU 2873  O   HOH A 433     4423   3695   7151   1235   1050   1007       O  
HETATM 2874  O   HOH A 434      42.351   2.622  -0.291  1.00 30.24           O  
ANISOU 2874  O   HOH A 434     2635   3234   5620    925   -293  -1071       O  
HETATM 2875  O   HOH A 435      45.971   8.661  12.247  1.00 19.54           O  
ANISOU 2875  O   HOH A 435     1251   1745   4428   -114     58    104       O  
HETATM 2876  O   HOH A 436      21.717  14.808  21.066  1.00 48.54           O  
ANISOU 2876  O   HOH A 436     4798   7188   6458   -443   2617  -2497       O  
HETATM 2877  O   HOH A 437      30.086  11.574 -10.032  1.00 14.20           O  
ANISOU 2877  O   HOH A 437     2163   1627   1604      4      8    -99       O  
HETATM 2878  O   HOH A 438      35.621  25.753  -7.564  1.00 39.38           O  
ANISOU 2878  O   HOH A 438     7756   2905   4301    190    845    -69       O  
HETATM 2879  O   HOH A 439      29.163  15.893  25.564  1.00 48.62           O  
ANISOU 2879  O   HOH A 439     3462   6895   8116  -1116   -865  -2124       O  
HETATM 2880  O   HOH A 440      28.348  27.643  -8.143  1.00 43.69           O  
ANISOU 2880  O   HOH A 440     5705   5847   5048   1069    956   2555       O  
HETATM 2881  O   HOH A 441      22.512  -7.897   7.702  1.00 40.42           O  
ANISOU 2881  O   HOH A 441     4210   5464   5684  -1483   1730    785       O  
HETATM 2882  O   HOH A 442      43.619  11.691  27.352  1.00 42.64           O  
ANISOU 2882  O   HOH A 442     6358   6958   2886   2079    -17   1037       O  
HETATM 2883  O   HOH A 443      33.636  33.725  -0.618  1.00 15.00           O  
ANISOU 2883  O   HOH A 443     2070   1814   1814    132   -105   -329       O  
HETATM 2884  O   HOH A 444      46.721  17.145  10.959  1.00 10.47           O  
ANISOU 2884  O   HOH A 444      876   1551   1550    -38     73    -77       O  
HETATM 2885  O   HOH A 445      29.915  19.642  18.680  1.00 30.62           O  
ANISOU 2885  O   HOH A 445     2888   5124   3622   -308    404  -1409       O  
HETATM 2886  O   HOH A 446      28.362  21.634  17.682  1.00 49.61           O  
ANISOU 2886  O   HOH A 446     3741   8187   6923   1155  -1594  -2055       O  
HETATM 2887  O   HOH A 447      36.213  -0.586  17.772  1.00 30.37           O  
ANISOU 2887  O   HOH A 447     7088   2353   2099    719   -474     53       O  
HETATM 2888  O   HOH A 448      35.360  21.401  25.801  1.00 47.88           O  
ANISOU 2888  O   HOH A 448     6956   5099   6139  -1455   -632   -362       O  
HETATM 2889  O   HOH A 449      22.851   5.173   0.914  1.00 23.84           O  
ANISOU 2889  O   HOH A 449     2811   3306   2939   -915    530   -774       O  
HETATM 2890  O   HOH A 450      23.154   1.701  -6.027  1.00 35.76           O  
ANISOU 2890  O   HOH A 450     4977   2724   5887   -629  -2638    685       O  
HETATM 2891  O   HOH A 451      39.307  15.552 -14.863  1.00 47.37           O  
ANISOU 2891  O   HOH A 451     6287   5522   6188  -1857  -1773  -1959       O  
HETATM 2892  O   HOH A 452      36.283  30.786   5.471  1.00 12.68           O  
ANISOU 2892  O   HOH A 452     1824   1433   1559   -105   -404     -7       O  
HETATM 2893  O   HOH A 453      24.036  33.705  -1.737  1.00 40.47           O  
ANISOU 2893  O   HOH A 453     2750   8525   4103  -1089   -506   1170       O  
HETATM 2894  O   HOH A 454      20.749   0.681   2.716  1.00 43.45           O  
ANISOU 2894  O   HOH A 454     3610   4700   8198  -1645   -525   -966       O  
HETATM 2895  O   HOH A 455      39.700  20.062  19.658  1.00 44.80           O  
HETATM 2896  O   HOH A 456      23.791  24.112  -6.520  1.00 54.83           O  
ANISOU 2896  O   HOH A 456     6159   5340   9332  -1790   -423  -2729       O  
HETATM 2897  O   HOH A 457      27.820  29.955   4.507  1.00 22.66           O  
ANISOU 2897  O   HOH A 457     2992   2056   3562   -334  -1150   -172       O  
HETATM 2898  O   HOH A 458      38.822   7.947  30.534  1.00 50.70           O  
ANISOU 2898  O   HOH A 458     6029   6953   6283  -2118   2707  -2775       O  
HETATM 2899  O   HOH A 459      26.454  16.174 -14.352  1.00 45.05           O  
ANISOU 2899  O   HOH A 459     6102   6033   4982  -1209  -2098   -865       O  
HETATM 2900  O   HOH A 460      22.479  21.927  16.757  1.00 41.43           O  
ANISOU 2900  O   HOH A 460     5408   5114   5221   2459   1374   1294       O  
HETATM 2901  O   HOH A 461      45.898   9.009   7.704  1.00 38.41           O  
ANISOU 2901  O   HOH A 461     3579   6827   4187   -726    789    785       O  
HETATM 2902  O   HOH A 462      35.885  -4.534  16.546  1.00 50.20           O  
ANISOU 2902  O   HOH A 462     9633   4284   5158   1126    159   -541       O  
HETATM 2903  O   HOH A 463      44.768   4.783  15.351  1.00 36.82           O  
ANISOU 2903  O   HOH A 463     4862   4662   4464    802   -951   1263       O  
HETATM 2904  O   HOH A 464      29.490   8.716 -10.357  1.00 20.20           O  
ANISOU 2904  O   HOH A 464     3652   2157   1865   -457     -5   -418       O  
HETATM 2905  O   HOH A 465      35.750  33.403   5.224  1.00 16.78           O  
ANISOU 2905  O   HOH A 465     2872   1587   1918    937    149    156       O  
HETATM 2906  O   HOH A 466      31.252  22.098  15.330  1.00 44.97           O  
ANISOU 2906  O   HOH A 466     6986   4768   5334    493   1805  -2349       O  
HETATM 2907  O   HOH A 467      38.103  26.595  14.382  1.00 31.47           O  
ANISOU 2907  O   HOH A 467     6061   3577   2321   -447   -332    544       O  
HETATM 2908  O   HOH A 468      24.077  30.594   9.169  1.00 26.28           O  
ANISOU 2908  O   HOH A 468     2279   4172   3535   1092   -448     48       O  
HETATM 2909  O   HOH A 469      23.636  -7.366  -3.966  1.00 53.91           O  
ANISOU 2909  O   HOH A 469     6456   7194   6833  -3157  -1101  -1836       O  
HETATM 2910  O   HOH A 470      30.488  29.196  -4.599  1.00 47.49           O  
ANISOU 2910  O   HOH A 470     7204   2823   8017   2059    -38     93       O  
HETATM 2911  O   HOH A 471      39.309  10.558  29.952  1.00 42.39           O  
ANISOU 2911  O   HOH A 471     4563   7864   3679   2561    117   -438       O  
HETATM 2912  O   HOH A 472      34.977  23.466 -13.128  1.00 51.30           O  
ANISOU 2912  O   HOH A 472     7310   4418   7763   -983   3738    457       O  
HETATM 2913  O   HOH A 473      40.323  -3.061  -6.782  1.00 37.66           O  
ANISOU 2913  O   HOH A 473     5287   3287   5735    534   2166  -1012       O  
HETATM 2914  O   HOH A 474      44.530   6.177  -2.160  1.00 28.66           O  
HETATM 2915  O   HOH A 475      43.070  25.168   9.947  1.00 30.76           O  
ANISOU 2915  O   HOH A 475     4134   3426   4128   1525    170   1689       O  
HETATM 2916  O   HOH A 476      42.326  26.436  14.010  1.00 50.07           O  
ANISOU 2916  O   HOH A 476    11366   3135   4522     87  -1124    275       O  
HETATM 2917  O   HOH A 477      33.204  22.978 -15.444  1.00 44.42           O  
ANISOU 2917  O   HOH A 477     5620   5033   6223  -2166  -1219   2461       O  
HETATM 2918  O   HOH A 478      42.705  19.033  25.396  1.00 41.64           O  
ANISOU 2918  O   HOH A 478     4923   3437   7464   -290   -398   -723       O  
HETATM 2919  O   HOH A 479      22.732  19.954  -5.558  1.00 38.62           O  
ANISOU 2919  O   HOH A 479     2433   6542   5698   -134   1115    458       O  
HETATM 2920  O   HOH A 480      40.804   4.394  12.585  1.00 15.35           O  
ANISOU 2920  O   HOH A 480     2437   1478   1916   -152    118     17       O  
HETATM 2921  O   HOH A 481      23.464  15.155   5.223  1.00 24.99           O  
ANISOU 2921  O   HOH A 481     3716   2618   3162    123    482    437       O  
HETATM 2922  O   HOH A 482      43.517  10.963  -6.697  1.00 29.21           O  
ANISOU 2922  O   HOH A 482     4265   3750   3085   -391   1943   -104       O  
HETATM 2923  O   HOH A 483      42.089  -1.193   5.308  1.00 22.80           O  
ANISOU 2923  O   HOH A 483     3412   2334   2917    332    243   -658       O  
HETATM 2924  O   HOH A 484      19.040   3.478   6.894  1.00 40.60           O  
ANISOU 2924  O   HOH A 484     3117   6071   6239    321  -1207   -912       O  
HETATM 2925  O   HOH A 485      29.654  34.582  -1.672  1.00 34.35           O  
ANISOU 2925  O   HOH A 485     6664   2273   4115   -546  -1936    779       O  
HETATM 2926  O   HOH A 486      27.840   0.299  -7.174  1.00 50.74           O  
ANISOU 2926  O   HOH A 486     7836   6897   4546   -139   1488    623       O  
HETATM 2927  O   HOH A 487      30.274  26.168  -9.652  1.00 49.98           O  
ANISOU 2927  O   HOH A 487     8367   7224   3400    -55   -233   2112       O  
HETATM 2928  O   HOH A 488      24.761  31.495   2.609  1.00 15.78           O  
ANISOU 2928  O   HOH A 488     1504   1664   2827    249    106     39       O  
HETATM 2929  O   HOH A 489      26.421  24.136  -8.483  1.00 36.81           O  
ANISOU 2929  O   HOH A 489     6614   4506   2866   1077  -1228    253       O  
HETATM 2930  O   HOH A 490      26.364  30.459  10.663  1.00 43.57           O  
ANISOU 2930  O   HOH A 490     3095   7459   6000   -917    986   -503       O  
HETATM 2931  O   HOH A 491      47.187   9.012   9.642  1.00 42.14           O  
ANISOU 2931  O   HOH A 491     4024   7366   4621   2175    313   1230       O  
HETATM 2932  O   HOH A 492      45.390  26.206  10.008  0.33 30.06           O  
HETATM 2933  O   HOH A 493      38.747  12.193 -12.994  1.00 29.62           O  
ANISOU 2933  O   HOH A 493     3844   4846   2566   -647   -521    940       O  
HETATM 2934  O   HOH A 494      47.421  10.679  13.225  1.00 20.96           O  
ANISOU 2934  O   HOH A 494     2366   2557   3040   -283     17    323       O  
HETATM 2935  O   HOH A 495      40.178   7.681 -12.066  1.00 40.68           O  
ANISOU 2935  O   HOH A 495     3854   5731   5872   -127   2240   -933       O  
HETATM 2936  O   HOH A 496      47.039   6.230  13.665  1.00 41.59           O  
ANISOU 2936  O   HOH A 496     4976   4999   5826   1714   -753  -1939       O  
HETATM 2937  O   HOH A 497      22.616  22.956  -4.520  1.00 24.73           O  
ANISOU 2937  O   HOH A 497     3462   2647   3287   1120   -109    482       O  
HETATM 2938  O   HOH A 498      38.331  21.356  26.537  1.00 49.90           O  
ANISOU 2938  O   HOH A 498     7753   4314   6892  -1757  -1823   -404       O  
HETATM 2939  O   HOH A 499      25.376  -1.622  -7.716  1.00 53.61           O  
ANISOU 2939  O   HOH A 499     8324   8262   3784   2108  -1020    160       O  
HETATM 2940  O   HOH A 500      19.556   1.564  10.432  1.00 49.08           O  
ANISOU 2940  O   HOH A 500     5083   7868   5695  -2362   1633  -2360       O  
HETATM 2941  O   HOH A 501      42.845   5.491  -0.324  1.00 21.99           O  
HETATM 2942  O   HOH A 502      35.331  27.871  14.589  1.00 51.59           O  
ANISOU 2942  O   HOH A 502     7245   6428   5930  -2882   1418   1068       O  
HETATM 2943  O   HOH A 503      43.594  -1.330   9.314  1.00 26.41           O  
ANISOU 2943  O   HOH A 503     2451   3328   4256    993    456   1301       O  
HETATM 2944  O   HOH A 504      43.989   2.488  11.989  1.00 40.74           O  
ANISOU 2944  O   HOH A 504     3170   6535   5774   1296    612    226       O  
HETATM 2945  O   HOH A 505      22.247  -2.445  -4.437  1.00 33.84           O  
ANISOU 2945  O   HOH A 505     3295   2592   6971    231  -1543   -483       O  
HETATM 2946  O   HOH A 506      34.839  25.277 -11.596  1.00 39.74           O  
ANISOU 2946  O   HOH A 506     7406   4014   3679   -671   2027    168       O  
HETATM 2947  O   HOH A 507      44.665  10.620  -2.780  1.00 24.10           O  
ANISOU 2947  O   HOH A 507     2232   4128   2796    -55   -253  -1683       O  
HETATM 2948  O   HOH A 508      25.093  -9.711  -4.950  1.00 45.32           O  
ANISOU 2948  O   HOH A 508     4205   6348   6665   1257  -1324  -2097       O  
HETATM 2949  O   HOH A 509      38.912  -2.287  18.495  1.00 45.50           O  
ANISOU 2949  O   HOH A 509     5461   6135   5692    -27   -400   -950       O  
HETATM 2950  O   HOH A 510      21.583   9.359  -4.823  1.00 45.31           O  
HETATM 2951  O   HOH A 511      21.166   3.512  -0.457  1.00 46.28           O  
ANISOU 2951  O   HOH A 511     4473   2938  10175   -754    -34   -355       O  
HETATM 2952  O   HOH A 512      40.577  17.700 -15.911  1.00 39.49           O  
ANISOU 2952  O   HOH A 512     5070   6700   3237   1066    372   -541       O  
HETATM 2953  O   HOH A 513      27.298  32.189   5.992  1.00 40.35           O  
ANISOU 2953  O   HOH A 513     5238   6609   3482   3184  -1326   -936       O  
HETATM 2954  O   HOH A 514      42.309  18.338  -4.725  1.00 38.53           O  
ANISOU 2954  O   HOH A 514     2831   6123   5687   -794    969  -1822       O  
HETATM 2955  O   HOH A 515      29.986  35.033   1.374  1.00 23.23           O  
ANISOU 2955  O   HOH A 515     2658   3060   3109   -312   -780    528       O  
HETATM 2956  O   HOH A 516      33.067  31.346  14.531  1.00 37.10           O  
ANISOU 2956  O   HOH A 516     3900   6043   4152  -2061   -281   1100       O  
HETATM 2957  O   HOH A 517      44.727  13.596  -6.341  1.00 40.81           O  
ANISOU 2957  O   HOH A 517     4549   7294   3665  -1121   1174   -517       O  
HETATM 2958  O   HOH A 518      20.394   3.393   1.886  1.00 44.64           O  
ANISOU 2958  O   HOH A 518     4770   5111   7080  -1879  -2423   1020       O  
HETATM 2959  O   HOH A 519      43.323  16.220  -6.181  1.00 48.67           O  
ANISOU 2959  O   HOH A 519     7710   6488   4296  -1299   1165   2444       O  
HETATM 2960  O   HOH A 520      23.150  31.697   4.855  1.00 12.79           O  
ANISOU 2960  O   HOH A 520     1238   1467   2154    -12   -157    115       O  
HETATM 2961  O   HOH A 521      22.910  -0.930  -7.058  1.00 49.77           O  
ANISOU 2961  O   HOH A 521     7283   6077   5552  -2012  -1730   1089       O  
HETATM 2962  O   HOH A 522      33.925  21.077 -17.641  1.00 43.10           O  
ANISOU 2962  O   HOH A 522     3932   7515   4931    687    -51   -551       O  
HETATM 2963  O   HOH A 523      22.744  33.183   9.257  1.00 36.50           O  
ANISOU 2963  O   HOH A 523     3035   5062   5770   1445   -966  -2723       O  
HETATM 2964  O   HOH A 524      23.706  33.939   6.473  1.00 20.61           O  
ANISOU 2964  O   HOH A 524     2145   2136   3549    -93    324   -541       O  
CONECT 1535 2700                                                                
CONECT 2608 2609 2617 2619 2637                                                 
CONECT 2609 2608 2610 2614 2620                                                 
CONECT 2610 2609 2611 2615 2621                                                 
CONECT 2611 2610 2612 2616 2622                                                 
CONECT 2612 2611 2613 2617 2623                                                 
CONECT 2613 2612 2618 2624 2625                                                 
CONECT 2614 2609 2626                                                           
CONECT 2615 2610 2627                                                           
CONECT 2616 2611 2628                                                           
CONECT 2617 2608 2612                                                           
CONECT 2618 2613 2629                                                           
CONECT 2619 2608                                                                
CONECT 2620 2609                                                                
CONECT 2621 2610                                                                
CONECT 2622 2611                                                                
CONECT 2623 2612                                                                
CONECT 2624 2613                                                                
CONECT 2625 2613                                                                
CONECT 2626 2614                                                                
CONECT 2627 2615                                                                
CONECT 2628 2616                                                                
CONECT 2629 2618                                                                
CONECT 2630 2631 2636 2642 2643                                                 
CONECT 2631 2630 2632 2637 2640                                                 
CONECT 2632 2631 2633 2638 2644                                                 
CONECT 2633 2632 2634 2639 2645                                                 
CONECT 2634 2633 2635 2640 2646                                                 
CONECT 2635 2634 2641 2647 2648                                                 
CONECT 2636 2630 2649                                                           
CONECT 2637 2608 2631                                                           
CONECT 2638 2632 2650                                                           
CONECT 2639 2633 2651                                                           
CONECT 2640 2631 2634                                                           
CONECT 2641 2635 2652                                                           
CONECT 2642 2630                                                                
CONECT 2643 2630                                                                
CONECT 2644 2632                                                                
CONECT 2645 2633                                                                
CONECT 2646 2634                                                                
CONECT 2647 2635                                                                
CONECT 2648 2635                                                                
CONECT 2649 2636                                                                
CONECT 2650 2638                                                                
CONECT 2651 2639                                                                
CONECT 2652 2641                                                                
CONECT 2653 2654 2655 2656 2657                                                 
CONECT 2654 2653                                                                
CONECT 2655 2653                                                                
CONECT 2656 2653                                                                
CONECT 2657 2653                                                                
CONECT 2658 2662 2689 2730                                                      
CONECT 2659 2665 2672 2701                                                      
CONECT 2660 2675 2679 2702                                                      
CONECT 2661 2682 2686 2703                                                      
CONECT 2662 2658 2663 2696                                                      
CONECT 2663 2662 2664 2667                                                      
CONECT 2664 2663 2665 2666                                                      
CONECT 2665 2659 2664 2696                                                      
CONECT 2666 2664 2704 2705 2706                                                 
CONECT 2667 2663 2668 2707 2708                                                 
CONECT 2668 2667 2669 2709 2710                                                 
CONECT 2669 2668 2670 2671                                                      
CONECT 2670 2669                                                                
CONECT 2671 2669                                                                
CONECT 2672 2659 2673 2697                                                      
CONECT 2673 2672 2674 2676                                                      
CONECT 2674 2673 2675 2677                                                      
CONECT 2675 2660 2674 2697                                                      
CONECT 2676 2673 2711 2712 2713                                                 
CONECT 2677 2674 2678 2714                                                      
CONECT 2678 2677 2715 2716                                                      
CONECT 2679 2660 2680 2698                                                      
CONECT 2680 2679 2681 2683                                                      
CONECT 2681 2680 2682 2684                                                      
CONECT 2682 2661 2681 2698                                                      
CONECT 2683 2680 2717 2718 2719                                                 
CONECT 2684 2681 2685 2720                                                      
CONECT 2685 2684 2721 2722                                                      
CONECT 2686 2661 2687 2699                                                      
CONECT 2687 2686 2688 2690                                                      
CONECT 2688 2687 2689 2691                                                      
CONECT 2689 2658 2688 2699                                                      
CONECT 2690 2687 2723 2724 2725                                                 
CONECT 2691 2688 2692 2726 2727                                                 
CONECT 2692 2691 2693 2728 2729                                                 
CONECT 2693 2692 2694 2695                                                      
CONECT 2694 2693                                                                
CONECT 2695 2693                                                                
CONECT 2696 2662 2665 2700                                                      
CONECT 2697 2672 2675 2700                                                      
CONECT 2698 2679 2682 2700                                                      
CONECT 2699 2686 2689 2700                                                      
CONECT 2700 1535 2696 2697 2698                                                 
CONECT 2700 2699 2835                                                           
CONECT 2701 2659                                                                
CONECT 2702 2660                                                                
CONECT 2703 2661                                                                
CONECT 2704 2666                                                                
CONECT 2705 2666                                                                
CONECT 2706 2666                                                                
CONECT 2707 2667                                                                
CONECT 2708 2667                                                                
CONECT 2709 2668                                                                
CONECT 2710 2668                                                                
CONECT 2711 2676                                                                
CONECT 2712 2676                                                                
CONECT 2713 2676                                                                
CONECT 2714 2677                                                                
CONECT 2715 2678                                                                
CONECT 2716 2678                                                                
CONECT 2717 2683                                                                
CONECT 2718 2683                                                                
CONECT 2719 2683                                                                
CONECT 2720 2684                                                                
CONECT 2721 2685                                                                
CONECT 2722 2685                                                                
CONECT 2723 2690                                                                
CONECT 2724 2690                                                                
CONECT 2725 2690                                                                
CONECT 2726 2691                                                                
CONECT 2727 2691                                                                
CONECT 2728 2692                                                                
CONECT 2729 2692                                                                
CONECT 2730 2658                                                                
CONECT 2731 2732 2733 2734 2735                                                 
CONECT 2732 2731                                                                
CONECT 2733 2731                                                                
CONECT 2734 2731                                                                
CONECT 2735 2731                                                                
CONECT 2736 2737 2738 2739 2740                                                 
CONECT 2737 2736                                                                
CONECT 2738 2736                                                                
CONECT 2739 2736                                                                
CONECT 2740 2736                                                                
CONECT 2835 2700                                                                
MASTER      293    0    6    9    0    0    0    6 1521    1  136   12          
END                                                                             



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