CNRS Nantes University UFIP UFIP
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***  TRANSCRIPTION 23-APR-18 5ZR4  ***

elNémo ID: 19092418220823606

Job options:

ID        	=	 19092418220823606
JOBID     	=	 TRANSCRIPTION 23-APR-18 5ZR4
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    TRANSCRIPTION                           23-APR-18   5ZR4              
TITLE     MANGANESE-DEPENDENT TRANSCRIPTIONAL REPRESSOR                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METAL-DEPENDENT TRANSCRIPTIONAL REGULATOR;                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TRANSCRIPTIONAL REPRESSOR SIRR;                             
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 GENE: SIRR, SIRR_2;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSCRIPTIONAL REPRESSOR, TRANSCRIPTION                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.Y.CONG,L.C.GU,J.B.WANG                                              
REVDAT   1   23-JAN-19 5ZR4    0                                                
JRNL        AUTH   X.Y.CONG,Z.L.YUAN,Z.WANG,B.WEI,S.J.XU,J.B.WANG               
JRNL        TITL   CRYSTAL STRUCTURES OF MANGANESE-DEPENDENT TRANSCRIPTIONAL    
JRNL        TITL 2 REPRESSOR MNTR (RV2788) FROM MYCOBACTERIUM TUBERCULOSIS IN   
JRNL        TITL 3 APO AND MANGANESE BOUND FORMS.                               
JRNL        REF    BIOCHEM. BIOPHYS. RES.        V. 501   423 2018              
JRNL        REF  2 COMMUN.                                                      
JRNL        REFN                   ESSN 1090-2104                               
JRNL        PMID   29730293                                                     
JRNL        DOI    10.1016/J.BBRC.2018.05.005                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2719: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 9651                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.300                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 960                             
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 58.0750 -  5.9283    0.98     1297   144  0.2499 0.2716        
REMARK   3     2  5.9283 -  4.7061    0.98     1235   138  0.2524 0.2948        
REMARK   3     3  4.7061 -  4.1114    0.98     1232   137  0.2212 0.2828        
REMARK   3     4  4.1114 -  3.7356    0.99     1239   137  0.2401 0.2844        
REMARK   3     5  3.7356 -  3.4679    0.99     1233   137  0.2717 0.3590        
REMARK   3     6  3.4679 -  3.2634    0.99     1238   132  0.2574 0.3420        
REMARK   3     7  3.2634 -  3.1000    0.99     1217   135  0.2971 0.3721        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.340           
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      :  0.003           2885                                  
REMARK   3   ANGLE     :  0.846           3909                                  
REMARK   3   CHIRALITY :  0.044            443                                  
REMARK   3   PLANARITY :  0.004            511                                  
REMARK   3   DIHEDRAL  :  9.942           1747                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0800 -14.8703 -13.6390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2917 T22:   0.8973                                     
REMARK   3      T33:   0.2286 T12:   0.0369                                     
REMARK   3      T13:   0.0472 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4683 L22:   0.7288                                     
REMARK   3      L33:   1.6201 L12:  -0.5131                                     
REMARK   3      L13:   1.3781 L23:  -0.3516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1272 S12:  -0.0852 S13:  -0.0533                       
REMARK   3      S21:   0.0786 S22:   0.0049 S23:  -0.0013                       
REMARK   3      S31:  -0.1795 S32:   0.0490 S33:   0.2267                       
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 5ZR4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007522.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-APR-14                          
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               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.89                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9651                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.065                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.3900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 30% PEG 400, VAPOR    
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.40500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.40500            
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  1.000000  0.000000  0.000000       44.75000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.52000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.75000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.52000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.40500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.75000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       54.52000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.40500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.75000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       54.52000            
REMARK 290   SMTRY3   8  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     TRP A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     GLN A    29                                                      
REMARK 465     ASP A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     VAL A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     THR A    34                                                      
REMARK 465     LYS A    35                                                      
REMARK 465     MET A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     ARG A    40                                                      
REMARK 465     ILE A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     VAL A    43                                                      
REMARK 465     SER A    44                                                      
REMARK 465     ALA A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     THR A    47                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     HIS A    63                                                      
REMARK 465     GLU A    64                                                      
REMARK 465     LYS A    65                                                      
REMARK 465     TYR A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     VAL A    69                                                      
REMARK 465     ALA A   209                                                      
REMARK 465     ASP A   210                                                      
REMARK 465     GLY A   211                                                      
REMARK 465     GLU A   230                                                      
REMARK 465     HIS A   231                                                      
REMARK 465     HIS A   232                                                      
REMARK 465     HIS A   233                                                      
REMARK 465     HIS A   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     MET B    11                                                      
REMARK 465     ALA B    12                                                      
REMARK 465     VAL B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     GLU B    26                                                      
REMARK 465     TRP B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     GLN B    29                                                      
REMARK 465     ASP B    30                                                      
REMARK 465     LYS B    31                                                      
REMARK 465     VAL B    32                                                      
REMARK 465     SER B    33                                                      
REMARK 465     THR B    34                                                      
REMARK 465     LYS B    35                                                      
REMARK 465     MET B    36                                                      
REMARK 465     LEU B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     ARG B    40                                                      
REMARK 465     ILE B    41                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     VAL B    43                                                      
REMARK 465     SER B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     THR B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ASP B    62                                                      
REMARK 465     HIS B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     LYS B    65                                                      
REMARK 465     TYR B    66                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     ALA B    68                                                      
REMARK 465     VAL B    69                                                      
REMARK 465     ALA B   209                                                      
REMARK 465     ASP B   210                                                      
REMARK 465     GLY B   211                                                      
REMARK 465     GLU B   230                                                      
REMARK 465     HIS B   231                                                      
REMARK 465     HIS B   232                                                      
REMARK 465     HIS B   233                                                      
REMARK 465     HIS B   234                                                      
REMARK 465     HIS B   235                                                      
REMARK 465     HIS B   236                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B   124     CE1  PHE B   129              1.85            
REMARK 500   OD1  ASP B   124     CD1  PHE B   129              1.86            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ILE A 224   CG1 -  CB  -  CG2 ANGL. DEV. = -13.6 DEGREES          
REMARK 500    PRO B 130   C   -  N   -  CA  ANGL. DEV. =  16.6 DEGREES          
REMARK 500    PRO B 130   C   -  N   -  CD  ANGL. DEV. = -25.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    LYS A  19       13.84    -69.46                                   
REMARK 500    ALA A 114       19.52   -154.00                                   
REMARK 500    VAL A 146       83.59     33.53                                   
REMARK 500    ILE A 182      -93.87    -71.74                                   
REMARK 500    ASP A 207       81.86    -62.87                                   
REMARK 500    ALA A 221       35.13    -91.04                                   
REMARK 500    ALA A 223      -65.74   -121.15                                   
REMARK 500    ARG B  85      -71.79    -57.98                                   
REMARK 500    ARG B  87      -55.74   -168.17                                   
REMARK 500    ARG B 100       51.51   -141.96                                   
REMARK 500    TRP B 101     -161.06     33.92                                   
REMARK 500    ASP B 102       -6.18     44.04                                   
REMARK 500    ALA B 114        1.58   -158.47                                   
REMARK 500    PHE B 129       85.09   -151.45                                   
REMARK 500    PRO B 130      122.12    -29.33                                   
REMARK 500    VAL B 146      107.72     61.29                                   
REMARK 500    PRO B 150       84.59    -62.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF1 5ZR4 A   12   228  UNP                  A0A045JFF4_MYCTX                 
DBREF2 5ZR4 A     A0A045JFF4                         12         228             
DBREF1 5ZR4 B   12   228  UNP                  A0A045JFF4_MYCTX                 
DBREF2 5ZR4 B     A0A045JFF4                         12         228             
SEQADV 5ZR4 MET A   11  UNP  A0A045JFF           INITIATING METHIONINE          
SEQADV 5ZR4 LEU A  229  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 GLU A  230  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS A  231  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS A  232  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS A  233  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS A  234  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS A  235  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS A  236  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 MET B   11  UNP  A0A045JFF           INITIATING METHIONINE          
SEQADV 5ZR4 LEU B  229  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 GLU B  230  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS B  231  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS B  232  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS B  233  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS B  234  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS B  235  UNP  A0A045JFF           EXPRESSION TAG                 
SEQADV 5ZR4 HIS B  236  UNP  A0A045JFF           EXPRESSION TAG                 
SEQRES   1 A  226  MET ALA VAL ALA GLN ASP TYR LEU LYS VAL ILE TRP THR          
SEQRES   2 A  226  ALA GLN GLU TRP SER GLN ASP LYS VAL SER THR LYS MET          
SEQRES   3 A  226  LEU ALA GLU ARG ILE GLY VAL SER ALA SER THR ALA SER          
SEQRES   4 A  226  GLU SER ILE ARG LYS LEU ALA GLU GLN GLY LEU VAL ASP          
SEQRES   5 A  226  HIS GLU LYS TYR GLY ALA VAL THR LEU THR ASP SER GLY          
SEQRES   6 A  226  ARG ARG ALA ALA LEU ALA MET VAL ARG ARG HIS ARG LEU          
SEQRES   7 A  226  LEU GLU THR PHE LEU VAL ASN GLU LEU GLY TYR ARG TRP          
SEQRES   8 A  226  ASP GLU VAL HIS ASP GLU ALA GLU VAL LEU GLU HIS ALA          
SEQRES   9 A  226  VAL SER ASP ARG LEU MET ALA ARG ILE ASP ALA LYS LEU          
SEQRES  10 A  226  GLY PHE PRO GLN ARG ASP PRO HIS GLY ASP PRO ILE PRO          
SEQRES  11 A  226  GLY ALA ASP GLY GLN VAL PRO THR PRO PRO ALA ARG GLN          
SEQRES  12 A  226  LEU TRP ALA CYS ARG ASP GLY ASP THR GLY THR VAL ALA          
SEQRES  13 A  226  ARG ILE SER ASP ALA ASP PRO GLN MET LEU ARG TYR PHE          
SEQRES  14 A  226  ALA SER ILE GLY ILE SER LEU ASP SER ARG LEU ARG VAL          
SEQRES  15 A  226  LEU ALA ARG ARG GLU PHE ALA GLY MET ILE SER VAL ALA          
SEQRES  16 A  226  ILE ASP SER ALA ASP GLY ALA THR VAL ASP LEU GLY SER          
SEQRES  17 A  226  PRO ALA ALA GLN ALA ILE TRP VAL VAL SER LEU GLU HIS          
SEQRES  18 A  226  HIS HIS HIS HIS HIS                                          
SEQRES   1 B  226  MET ALA VAL ALA GLN ASP TYR LEU LYS VAL ILE TRP THR          
SEQRES   2 B  226  ALA GLN GLU TRP SER GLN ASP LYS VAL SER THR LYS MET          
SEQRES   3 B  226  LEU ALA GLU ARG ILE GLY VAL SER ALA SER THR ALA SER          
SEQRES   4 B  226  GLU SER ILE ARG LYS LEU ALA GLU GLN GLY LEU VAL ASP          
SEQRES   5 B  226  HIS GLU LYS TYR GLY ALA VAL THR LEU THR ASP SER GLY          
SEQRES   6 B  226  ARG ARG ALA ALA LEU ALA MET VAL ARG ARG HIS ARG LEU          
SEQRES   7 B  226  LEU GLU THR PHE LEU VAL ASN GLU LEU GLY TYR ARG TRP          
SEQRES   8 B  226  ASP GLU VAL HIS ASP GLU ALA GLU VAL LEU GLU HIS ALA          
SEQRES   9 B  226  VAL SER ASP ARG LEU MET ALA ARG ILE ASP ALA LYS LEU          
SEQRES  10 B  226  GLY PHE PRO GLN ARG ASP PRO HIS GLY ASP PRO ILE PRO          
SEQRES  11 B  226  GLY ALA ASP GLY GLN VAL PRO THR PRO PRO ALA ARG GLN          
SEQRES  12 B  226  LEU TRP ALA CYS ARG ASP GLY ASP THR GLY THR VAL ALA          
SEQRES  13 B  226  ARG ILE SER ASP ALA ASP PRO GLN MET LEU ARG TYR PHE          
SEQRES  14 B  226  ALA SER ILE GLY ILE SER LEU ASP SER ARG LEU ARG VAL          
SEQRES  15 B  226  LEU ALA ARG ARG GLU PHE ALA GLY MET ILE SER VAL ALA          
SEQRES  16 B  226  ILE ASP SER ALA ASP GLY ALA THR VAL ASP LEU GLY SER          
SEQRES  17 B  226  PRO ALA ALA GLN ALA ILE TRP VAL VAL SER LEU GLU HIS          
SEQRES  18 B  226  HIS HIS HIS HIS HIS                                          
FORMUL   3  HOH   *9(H2 O)                                                      
HELIX    1 AA1 ALA A   14  ASP A   16  5                                   3    
HELIX    2 AA2 TYR A   17  GLN A   25  1                                   9    
HELIX    3 AA3 SER A   49  ALA A   56  1                                   8    
HELIX    4 AA4 GLU A   57  GLY A   59  5                                   3    
HELIX    5 AA5 THR A   72  GLU A   96  1                                  25    
HELIX    6 AA6 GLU A  103  GLU A  112  1                                  10    
HELIX    7 AA7 SER A  116  LEU A  127  1                                  12    
HELIX    8 AA8 ASP A  172  ILE A  182  1                                  11    
HELIX    9 AA9 PRO A  219  ALA A  223  5                                   5    
HELIX   10 AB1 ASP B   16  GLN B   25  1                                  10    
HELIX   11 AB2 ILE B   52  GLN B   58  1                                   7    
HELIX   12 AB3 THR B   72  GLU B   96  1                                  25    
HELIX   13 AB4 VAL B  104  GLU B  112  1                                   9    
HELIX   14 AB5 SER B  116  GLY B  128  1                                  13    
HELIX   15 AB6 ASP B  172  GLY B  183  1                                  12    
HELIX   16 AB7 SER B  218  GLN B  222  1                                   5    
SHEET    1 AA1 6 ARG A 152  GLN A 153  0                                        
SHEET    2 AA1 6 TRP A 225  SER A 228 -1  O  VAL A 226   N  ARG A 152           
SHEET    3 AA1 6 THR A 162  ARG A 167 -1  N  ARG A 167   O  TRP A 225           
SHEET    4 AA1 6 ARG A 189  ARG A 196 -1  O  LEU A 190   N  GLY A 163           
SHEET    5 AA1 6 MET A 201  ILE A 206 -1  O  SER A 203   N  LEU A 193           
SHEET    6 AA1 6 THR A 213  GLY A 217 -1  O  LEU A 216   N  ILE A 202           
SHEET    1 AA2 6 ARG B 152  GLN B 153  0                                        
SHEET    2 AA2 6 ILE B 224  VAL B 227 -1  O  VAL B 226   N  ARG B 152           
SHEET    3 AA2 6 THR B 162  ILE B 168 -1  N  ARG B 167   O  TRP B 225           
SHEET    4 AA2 6 ARG B 189  ARG B 196 -1  O  LEU B 190   N  GLY B 163           
SHEET    5 AA2 6 MET B 201  ALA B 205 -1  O  SER B 203   N  LEU B 193           
SHEET    6 AA2 6 THR B 213  GLY B 217 -1  O  LEU B 216   N  ILE B 202           
CISPEP   1 GLY B  128    PHE B  129          0         9.59                     
CISPEP   2 PHE B  198    ALA B  199          0         0.07                     
CRYST1   89.500  109.040  106.810  90.00  90.00  90.00 C 2 2 21     16          
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      0.011173  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009171  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009362        0.00000                         
ATOM      1  N   ALA A  14     -16.160   6.039 -15.171  1.00 87.50           N  
ANISOU    1  N   ALA A  14    10661  13407   9179   1098  -1959   -642       N  
ATOM      2  CA  ALA A  14     -16.334   6.842 -16.375  1.00104.73           C  
ANISOU    2  CA  ALA A  14    12887  15422  11483   1001  -2104   -519       C  
ATOM      3  C   ALA A  14     -16.251   5.976 -17.627  1.00131.18           C  
ANISOU    3  C   ALA A  14    16135  18910  14798    836  -1907   -317       C  
ATOM      4  O   ALA A  14     -16.943   6.225 -18.614  1.00122.47           O  
ANISOU    4  O   ALA A  14    15029  17778  13726    825  -1926   -255       O  
ATOM      5  CB  ALA A  14     -15.294   7.952 -16.427  1.00 90.61           C  
ANISOU    5  CB  ALA A  14    11195  13386   9848    872  -2377   -435       C  
ATOM      6  N   GLN A  15     -15.397   4.954 -17.578  1.00158.97           N  
ANISOU    6  N   GLN A  15    19571  22583  18248    719  -1726   -224       N  
ATOM      7  CA  GLN A  15     -15.228   4.050 -18.707  1.00167.95           C  
ANISOU    7  CA  GLN A  15    20607  23867  19339    581  -1541    -57       C  
ATOM      8  C   GLN A  15     -16.344   3.021 -18.815  1.00164.87           C  
ANISOU    8  C   GLN A  15    20138  23658  18847    693  -1328   -135       C  
ATOM      9  O   GLN A  15     -16.398   2.294 -19.813  1.00164.77           O  
ANISOU    9  O   GLN A  15    20048  23757  18799    605  -1192    -25       O  
ATOM     10  CB  GLN A  15     -13.882   3.331 -18.608  1.00182.16           C  
ANISOU   10  CB  GLN A  15    22344  25762  21107    430  -1440     59       C  
ATOM     11  CG  GLN A  15     -12.779   4.153 -17.964  1.00193.74           C  
ANISOU   11  CG  GLN A  15    23877  27079  22656    357  -1631     83       C  
ATOM     12  CD  GLN A  15     -12.356   5.343 -18.804  1.00202.75           C  
ANISOU   12  CD  GLN A  15    25074  28031  23930    217  -1857    238       C  
ATOM     13  OE1 GLN A  15     -11.465   5.237 -19.647  1.00203.20           O  
ANISOU   13  OE1 GLN A  15    25069  28134  24004     28  -1836    445       O  
ATOM     14  NE2 GLN A  15     -12.983   6.489 -18.566  1.00207.24           N  
ANISOU   14  NE2 GLN A  15    25753  28393  24595    313  -2082    142       N  
ATOM     15  N   ASP A  16     -17.229   2.938 -17.818  1.00161.12           N  
ANISOU   15  N   ASP A  16    19672  23225  18321    885  -1302   -319       N  
ATOM     16  CA  ASP A  16     -18.334   1.991 -17.884  1.00154.94           C  
ANISOU   16  CA  ASP A  16    18802  22615  17454    982  -1114   -377       C  
ATOM     17  C   ASP A  16     -19.360   2.373 -18.941  1.00146.24           C  
ANISOU   17  C   ASP A  16    17702  21475  16386   1009  -1153   -356       C  
ATOM     18  O   ASP A  16     -20.085   1.499 -19.426  1.00146.73           O  
ANISOU   18  O   ASP A  16    17678  21675  16397   1022   -995   -343       O  
ATOM     19  CB  ASP A  16     -19.012   1.875 -16.518  1.00162.27           C  
ANISOU   19  CB  ASP A  16    19723  23625  18308   1182  -1082   -560       C  
ATOM     20  CG  ASP A  16     -19.594   0.496 -16.272  1.00166.78           C  
ANISOU   20  CG  ASP A  16    20171  24418  18781   1219   -844   -566       C  
ATOM     21  OD1 ASP A  16     -18.813  -0.441 -16.007  1.00167.01           O  
ANISOU   21  OD1 ASP A  16    20145  24538  18772   1130   -720   -499       O  
ATOM     22  OD2 ASP A  16     -20.833   0.350 -16.344  1.00167.62           O  
ANISOU   22  OD2 ASP A  16    20229  24603  18854   1336   -792   -631       O  
ATOM     23  N   TYR A  17     -19.435   3.651 -19.309  1.00139.84           N  
ANISOU   23  N   TYR A  17    16988  20474  15671   1014  -1371   -350       N  
ATOM     24  CA  TYR A  17     -20.381   4.108 -20.318  1.00133.90           C  
ANISOU   24  CA  TYR A  17    16245  19673  14959   1040  -1430   -323       C  
ATOM     25  C   TYR A  17     -19.835   4.005 -21.735  1.00129.79           C  
ANISOU   25  C   TYR A  17    15698  19151  14466    843  -1417   -113       C  
ATOM     26  O   TYR A  17     -20.612   4.115 -22.690  1.00123.70           O  
ANISOU   26  O   TYR A  17    14910  18387  13702    850  -1422    -72       O  
ATOM     27  CB  TYR A  17     -20.806   5.556 -20.036  1.00132.94           C  
ANISOU   27  CB  TYR A  17    16240  19337  14933   1157  -1691   -420       C  
ATOM     28  CG  TYR A  17     -21.436   5.776 -18.673  1.00135.59           C  
ANISOU   28  CG  TYR A  17    16600  19691  15225   1387  -1724   -651       C  
ATOM     29  CD1 TYR A  17     -21.912   4.710 -17.918  1.00137.40           C  
ANISOU   29  CD1 TYR A  17    16732  20146  15328   1486  -1510   -742       C  
ATOM     30  CD2 TYR A  17     -21.563   7.055 -18.147  1.00137.79           C  
ANISOU   30  CD2 TYR A  17    16996  19771  15589   1510  -1979   -775       C  
ATOM     31  CE1 TYR A  17     -22.485   4.911 -16.676  1.00138.61           C  
ANISOU   31  CE1 TYR A  17    16890  20356  15418   1703  -1532   -941       C  
ATOM     32  CE2 TYR A  17     -22.139   7.265 -16.909  1.00141.52           C  
ANISOU   32  CE2 TYR A  17    17484  20288  16001   1744  -2011  -1003       C  
ATOM     33  CZ  TYR A  17     -22.597   6.191 -16.177  1.00141.40           C  
ANISOU   33  CZ  TYR A  17    17358  20530  15837   1840  -1778  -1081       C  
ATOM     34  OH  TYR A  17     -23.169   6.398 -14.943  1.00142.60           O  
ANISOU   34  OH  TYR A  17    17509  20766  15906   2079  -1802  -1296       O  
ATOM     35  N   LEU A  18     -18.525   3.798 -21.897  1.00133.25           N  
ANISOU   35  N   LEU A  18    16123  19597  14909    676  -1400     21       N  
ATOM     36  CA  LEU A  18     -17.963   3.612 -23.232  1.00136.14           C  
ANISOU   36  CA  LEU A  18    16441  20015  15271    499  -1367    223       C  
ATOM     37  C   LEU A  18     -18.459   2.316 -23.859  1.00130.67           C  
ANISOU   37  C   LEU A  18    15640  19531  14477    504  -1141    225       C  
ATOM     38  O   LEU A  18     -18.906   2.304 -25.012  1.00130.04           O  
ANISOU   38  O   LEU A  18    15531  19492  14384    467  -1132    305       O  
ATOM     39  CB  LEU A  18     -16.437   3.642 -23.165  1.00142.00           C  
ANISOU   39  CB  LEU A  18    17175  20749  16031    333  -1391    358       C  
ATOM     40  CG  LEU A  18     -15.871   5.022 -22.848  1.00146.41           C  
ANISOU   40  CG  LEU A  18    17837  21078  16715    282  -1653    405       C  
ATOM     41  CD1 LEU A  18     -14.360   5.031 -23.008  1.00142.80           C  
ANISOU   41  CD1 LEU A  18    17345  20635  16276     88  -1674    583       C  
ATOM     42  CD2 LEU A  18     -16.533   6.037 -23.766  1.00152.21           C  
ANISOU   42  CD2 LEU A  18    18625  21676  17531    274  -1825    481       C  
ATOM     43  N   LYS A  19     -18.401   1.215 -23.109  1.00125.89           N  
ANISOU   43  N   LYS A  19    14974  19053  13804    552   -972    138       N  
ATOM     44  CA  LYS A  19     -19.012  -0.048 -23.497  1.00123.31           C  
ANISOU   44  CA  LYS A  19    14551  18897  13405    580   -781    109       C  
ATOM     45  C   LYS A  19     -20.544   0.007 -23.465  1.00130.68           C  
ANISOU   45  C   LYS A  19    15477  19836  14338    727   -777     -6       C  
ATOM     46  O   LYS A  19     -21.195  -1.045 -23.505  1.00137.93           O  
ANISOU   46  O   LYS A  19    16314  20883  15209    770   -630    -53       O  
ATOM     47  CB  LYS A  19     -18.505  -1.171 -22.589  1.00115.53           C  
ANISOU   47  CB  LYS A  19    13508  18020  12369    588   -630     59       C  
ATOM     48  CG  LYS A  19     -18.369  -0.762 -21.142  1.00118.46           C  
ANISOU   48  CG  LYS A  19    13931  18327  12753    675   -686    -44       C  
ATOM     49  CD  LYS A  19     -17.730  -1.852 -20.317  1.00117.25           C  
ANISOU   49  CD  LYS A  19    13719  18283  12548    662   -545    -61       C  
ATOM     50  CE  LYS A  19     -17.445  -1.355 -18.918  1.00113.18           C  
ANISOU   50  CE  LYS A  19    13259  17712  12032    741   -616   -153       C  
ATOM     51  NZ  LYS A  19     -17.060  -2.449 -17.993  1.00101.14           N  
ANISOU   51  NZ  LYS A  19    11670  16309  10449    755   -475   -179       N  
ATOM     52  N   VAL A  20     -21.123   1.206 -23.381  1.00127.11           N  
ANISOU   52  N   VAL A  20    15106  19244  13945    805   -945    -49       N  
ATOM     53  CA  VAL A  20     -22.565   1.410 -23.459  1.00118.87           C  
ANISOU   53  CA  VAL A  20    14054  18206  12905    948   -962   -149       C  
ATOM     54  C   VAL A  20     -22.862   2.283 -24.672  1.00104.70           C  
ANISOU   54  C   VAL A  20    12304  16314  11163    904  -1100    -56       C  
ATOM     55  O   VAL A  20     -23.635   1.896 -25.557  1.00105.13           O  
ANISOU   55  O   VAL A  20    12304  16447  11192    910  -1042    -35       O  
ATOM     56  CB  VAL A  20     -23.116   2.045 -22.167  1.00120.75           C  
ANISOU   56  CB  VAL A  20    14342  18382  13157   1125  -1044   -313       C  
ATOM     57  CG1 VAL A  20     -24.599   2.385 -22.312  1.00119.36           C  
ANISOU   57  CG1 VAL A  20    14151  18216  12986   1282  -1080   -412       C  
ATOM     58  CG2 VAL A  20     -22.901   1.120 -20.983  1.00117.93           C  
ANISOU   58  CG2 VAL A  20    13925  18154  12729   1172   -897   -390       C  
ATOM     59  N   ILE A  21     -22.246   3.469 -24.713  1.00 96.77           N  
ANISOU   59  N   ILE A  21    11397  15134  10238    854  -1294      7       N  
ATOM     60  CA  ILE A  21     -22.396   4.356 -25.864  1.00 87.70           C  
ANISOU   60  CA  ILE A  21    10291  13882   9148    789  -1444    132       C  
ATOM     61  C   ILE A  21     -21.957   3.648 -27.140  1.00 92.05           C  
ANISOU   61  C   ILE A  21    10764  14577   9634    637  -1330    296       C  
ATOM     62  O   ILE A  21     -22.564   3.820 -28.204  1.00 89.03           O  
ANISOU   62  O   ILE A  21    10367  14217   9244    626  -1359    362       O  
ATOM     63  CB  ILE A  21     -21.607   5.660 -25.640  1.00 82.66           C  
ANISOU   63  CB  ILE A  21     9763  13024   8622    728  -1681    202       C  
ATOM     64  CG1 ILE A  21     -22.093   6.377 -24.377  1.00 87.89           C  
ANISOU   64  CG1 ILE A  21    10507  13544   9342    909  -1812      4       C  
ATOM     65  CG2 ILE A  21     -21.737   6.578 -26.848  1.00 73.12           C  
ANISOU   65  CG2 ILE A  21     8593  11707   7482    645  -1847    363       C  
ATOM     66  CD1 ILE A  21     -23.519   6.874 -24.464  1.00 95.41           C  
ANISOU   66  CD1 ILE A  21    11481  14451  10319   1090  -1889   -119       C  
ATOM     67  N   TRP A  22     -20.906   2.832 -27.053  1.00104.62           N  
ANISOU   67  N   TRP A  22    12302  16281  11169    531  -1203    355       N  
ATOM     68  CA  TRP A  22     -20.477   2.063 -28.216  1.00115.98           C  
ANISOU   68  CA  TRP A  22    13656  17886  12527    415  -1086    482       C  
ATOM     69  C   TRP A  22     -21.469   0.952 -28.541  1.00121.53           C  
ANISOU   69  C   TRP A  22    14279  18736  13160    499   -928    382       C  
ATOM     70  O   TRP A  22     -21.950   0.848 -29.675  1.00120.79           O  
ANISOU   70  O   TRP A  22    14151  18713  13030    481   -922    438       O  
ATOM     71  CB  TRP A  22     -19.083   1.481 -27.983  1.00111.87           C  
ANISOU   71  CB  TRP A  22    13093  17448  11965    299   -999    556       C  
ATOM     72  CG  TRP A  22     -18.599   0.667 -29.138  1.00111.31           C  
ANISOU   72  CG  TRP A  22    12927  17568  11795    205   -881    664       C  
ATOM     73  CD1 TRP A  22     -17.990   1.125 -30.268  1.00111.77           C  
ANISOU   73  CD1 TRP A  22    12963  17682  11823     81   -939    853       C  
ATOM     74  CD2 TRP A  22     -18.698  -0.754 -29.283  1.00111.99           C  
ANISOU   74  CD2 TRP A  22    12926  17827  11798    238   -693    586       C  
ATOM     75  NE1 TRP A  22     -17.698   0.077 -31.107  1.00112.37           N  
ANISOU   75  NE1 TRP A  22    12939  17973  11783     50   -792    881       N  
ATOM     76  CE2 TRP A  22     -18.123  -1.089 -30.524  1.00112.23           C  
ANISOU   76  CE2 TRP A  22    12887  18014  11743    147   -648    711       C  
ATOM     77  CE3 TRP A  22     -19.214  -1.777 -28.481  1.00112.88           C  
ANISOU   77  CE3 TRP A  22    13006  17978  11903    335   -569    429       C  
ATOM     78  CZ2 TRP A  22     -18.050  -2.402 -30.983  1.00113.99           C  
ANISOU   78  CZ2 TRP A  22    13020  18413  11877    166   -496    656       C  
ATOM     79  CZ3 TRP A  22     -19.141  -3.079 -28.938  1.00113.63           C  
ANISOU   79  CZ3 TRP A  22    13015  18230  11930    333   -424    398       C  
ATOM     80  CH2 TRP A  22     -18.563  -3.381 -30.177  1.00113.61           C  
ANISOU   80  CH2 TRP A  22    12955  18364  11848    257   -394    497       C  
ATOM     81  N   THR A  23     -21.795   0.116 -27.551  1.00123.27           N  
ANISOU   81  N   THR A  23    14465  19005  13365    587   -810    242       N  
ATOM     82  CA  THR A  23     -22.652  -1.041 -27.785  1.00129.46           C  
ANISOU   82  CA  THR A  23    15164  19924  14101    646   -666    161       C  
ATOM     83  C   THR A  23     -24.086  -0.658 -28.127  1.00132.56           C  
ANISOU   83  C   THR A  23    15559  20290  14518    753   -721     98       C  
ATOM     84  O   THR A  23     -24.884  -1.545 -28.453  1.00135.78           O  
ANISOU   84  O   THR A  23    15890  20802  14897    793   -624     44       O  
ATOM     85  CB  THR A  23     -22.645  -1.965 -26.562  1.00136.44           C  
ANISOU   85  CB  THR A  23    16006  20861  14975    704   -542     54       C  
ATOM     86  OG1 THR A  23     -23.034  -3.286 -26.958  1.00140.75           O  
ANISOU   86  OG1 THR A  23    16458  21540  15482    703   -403     25       O  
ATOM     87  CG2 THR A  23     -23.616  -1.463 -25.502  1.00138.60           C  
ANISOU   87  CG2 THR A  23    16307  21072  15282    850   -588    -69       C  
ATOM     88  N   ALA A  24     -24.433   0.630 -28.060  1.00133.85           N  
ANISOU   88  N   ALA A  24    15804  20311  14742    801   -887    101       N  
ATOM     89  CA  ALA A  24     -25.776   1.050 -28.444  1.00128.33           C  
ANISOU   89  CA  ALA A  24    15105  19587  14066    909   -951     45       C  
ATOM     90  C   ALA A  24     -26.018   0.830 -29.934  1.00135.57           C  
ANISOU   90  C   ALA A  24    15983  20583  14945    839   -944    143       C  
ATOM     91  O   ALA A  24     -27.088   0.353 -30.330  1.00135.70           O  
ANISOU   91  O   ALA A  24    15941  20675  14945    907   -897     82       O  
ATOM     92  CB  ALA A  24     -25.993   2.516 -28.068  1.00117.34           C  
ANISOU   92  CB  ALA A  24    13818  18007  12758    981  -1153     25       C  
ATOM     93  N   GLN A  25     -25.034   1.154 -30.772  1.00142.30           N  
ANISOU   93  N   GLN A  25    16857  21435  15775    704   -992    299       N  
ATOM     94  CA  GLN A  25     -25.153   0.980 -32.215  1.00152.18           C  
ANISOU   94  CA  GLN A  25    18067  22790  16965    639   -988    403       C  
ATOM     95  C   GLN A  25     -24.854  -0.444 -32.670  1.00159.67           C  
ANISOU   95  C   GLN A  25    18919  23928  17821    598   -816    382       C  
ATOM     96  O   GLN A  25     -24.919  -0.719 -33.874  1.00164.36           O  
ANISOU   96  O   GLN A  25    19470  24637  18343    558   -803    447       O  
ATOM     97  CB  GLN A  25     -24.224   1.962 -32.937  1.00149.23           C  
ANISOU   97  CB  GLN A  25    17741  22363  16595    512  -1117    600       C  
ATOM     98  CG  GLN A  25     -24.687   2.364 -34.333  1.00144.34           C  
ANISOU   98  CG  GLN A  25    17110  21796  15937    481  -1192    716       C  
ATOM     99  CD  GLN A  25     -25.870   3.312 -34.306  1.00134.20           C  
ANISOU   99  CD  GLN A  25    15887  20363  14740    587  -1341    671       C  
ATOM    100  OE1 GLN A  25     -26.118   3.986 -33.307  1.00133.64           O  
ANISOU  100  OE1 GLN A  25    15886  20122  14767    666  -1433    588       O  
ATOM    101  NE2 GLN A  25     -26.607   3.370 -35.410  1.00128.41           N  
ANISOU  101  NE2 GLN A  25    15125  19699  13965    601  -1373    718       N  
ATOM    102  N   GLU A  26     -24.535  -1.350 -31.752  1.00161.34           N  
ANISOU  102  N   GLU A  26    19095  24175  18030    615   -695    292       N  
ATOM    103  CA  GLU A  26     -24.237  -2.731 -32.111  1.00158.12           C  
ANISOU  103  CA  GLU A  26    18602  23922  17554    586   -551    259       C  
ATOM    104  C   GLU A  26     -25.498  -3.590 -32.085  1.00157.32           C  
ANISOU  104  C   GLU A  26    18439  23868  17469    677   -488    133       C  
ATOM    105  O   GLU A  26     -25.934  -4.104 -33.115  1.00158.53           O  
ANISOU  105  O   GLU A  26    18543  24114  17577    676   -473    127       O  
ATOM    106  CB  GLU A  26     -23.184  -3.314 -31.168  1.00153.24           C  
ANISOU  106  CB  GLU A  26    17975  23314  16937    547   -465    243       C  
ATOM    107  CG  GLU A  26     -22.561  -4.609 -31.661  1.00148.12           C  
ANISOU  107  CG  GLU A  26    17248  22812  16219    505   -345    233       C  
ATOM    108  CD  GLU A  26     -21.622  -5.228 -30.645  1.00143.89           C  
ANISOU  108  CD  GLU A  26    16700  22276  15694    480   -264    209       C  
ATOM    109  OE1 GLU A  26     -20.780  -6.060 -31.044  1.00142.81           O  
ANISOU  109  OE1 GLU A  26    16512  22249  15502    436   -191    224       O  
ATOM    110  OE2 GLU A  26     -21.728  -4.887 -29.449  1.00141.58           O  
ANISOU  110  OE2 GLU A  26    16447  21886  15461    516   -277    169       O  
ATOM    111  N   ALA A  48     -26.167  11.273 -14.305  1.00152.83           N  
ANISOU  111  N   ALA A  48    19159  21446  17464   2945  -2780  -2021       N  
ATOM    112  CA  ALA A  48     -25.327  10.345 -15.052  1.00151.41           C  
ANISOU  112  CA  ALA A  48    18924  21314  17290   2635  -2591  -1752       C  
ATOM    113  C   ALA A  48     -24.363  11.096 -15.966  1.00151.38           C  
ANISOU  113  C   ALA A  48    19036  21002  17478   2404  -2802  -1570       C  
ATOM    114  O   ALA A  48     -23.353  10.544 -16.404  1.00146.28           O  
ANISOU  114  O   ALA A  48    18368  20364  16848   2154  -2704  -1367       O  
ATOM    115  CB  ALA A  48     -26.185   9.384 -15.859  1.00148.87           C  
ANISOU  115  CB  ALA A  48    18464  21204  16895   2583  -2339  -1636       C  
ATOM    116  N   SER A  49     -24.680  12.362 -16.247  1.00155.15           N  
ANISOU  116  N   SER A  49    19631  21216  18103   2493  -3099  -1639       N  
ATOM    117  CA  SER A  49     -23.815  13.201 -17.068  1.00154.81           C  
ANISOU  117  CA  SER A  49    19698  20866  18258   2279  -3338  -1455       C  
ATOM    118  C   SER A  49     -22.488  13.515 -16.390  1.00162.82           C  
ANISOU  118  C   SER A  49    20791  21738  19337   2174  -3476  -1445       C  
ATOM    119  O   SER A  49     -21.590  14.057 -17.047  1.00164.93           O  
ANISOU  119  O   SER A  49    21123  21784  19760   1950  -3644  -1248       O  
ATOM    120  CB  SER A  49     -24.533  14.505 -17.420  1.00148.68           C  
ANISOU  120  CB  SER A  49    19031  19824  17635   2421  -3650  -1544       C  
ATOM    121  OG  SER A  49     -25.836  14.254 -17.917  1.00142.57           O  
ANISOU  121  OG  SER A  49    18181  19194  16794   2554  -3532  -1585       O  
ATOM    122  N   GLU A  50     -22.356  13.187 -15.101  1.00168.53           N  
ANISOU  122  N   GLU A  50    21499  22594  19940   2328  -3411  -1644       N  
ATOM    123  CA  GLU A  50     -21.136  13.444 -14.342  1.00175.02           C  
ANISOU  123  CA  GLU A  50    22391  23301  20809   2251  -3540  -1662       C  
ATOM    124  C   GLU A  50     -19.897  12.964 -15.088  1.00177.88           C  
ANISOU  124  C   GLU A  50    22718  23644  21225   1906  -3452  -1357       C  
ATOM    125  O   GLU A  50     -18.993  13.749 -15.394  1.00181.30           O  
ANISOU  125  O   GLU A  50    23237  23818  21829   1740  -3692  -1235       O  
ATOM    126  CB  GLU A  50     -21.240  12.763 -12.975  1.00174.02           C  
ANISOU  126  CB  GLU A  50    22206  23429  20485   2442  -3376  -1873       C  
ATOM    127  CG  GLU A  50     -19.962  12.780 -12.157  1.00172.04           C  
ANISOU  127  CG  GLU A  50    22001  23120  20247   2355  -3452  -1883       C  
ATOM    128  CD  GLU A  50     -20.030  11.841 -10.968  1.00170.38           C  
ANISOU  128  CD  GLU A  50    21700  23221  19814   2497  -3222  -2024       C  
ATOM    129  OE1 GLU A  50     -20.206  10.623 -11.182  1.00167.90           O  
ANISOU  129  OE1 GLU A  50    21252  23175  19368   2417  -2901  -1902       O  
ATOM    130  OE2 GLU A  50     -19.909  12.319  -9.820  1.00171.75           O  
ANISOU  130  OE2 GLU A  50    21937  23373  19948   2689  -3371  -2255       O  
ATOM    131  N   SER A  51     -19.840  11.667 -15.390  1.00175.59           N  
ANISOU  131  N   SER A  51    22293  23631  20792   1798  -3117  -1230       N  
ATOM    132  CA  SER A  51     -18.694  11.118 -16.101  1.00171.21           C  
ANISOU  132  CA  SER A  51    21688  23101  20264   1497  -3011   -957       C  
ATOM    133  C   SER A  51     -18.774  11.339 -17.605  1.00167.90           C  
ANISOU  133  C   SER A  51    21255  22600  19938   1314  -3037   -718       C  
ATOM    134  O   SER A  51     -17.750  11.224 -18.286  1.00166.65           O  
ANISOU  134  O   SER A  51    21072  22415  19834   1063  -3029   -480       O  
ATOM    135  CB  SER A  51     -18.555   9.625 -15.805  1.00168.74           C  
ANISOU  135  CB  SER A  51    21240  23105  19768   1464  -2662   -928       C  
ATOM    136  OG  SER A  51     -19.659   8.902 -16.316  1.00167.31           O  
ANISOU  136  OG  SER A  51    20966  23115  19489   1536  -2451   -931       O  
ATOM    137  N   ILE A  52     -19.961  11.644 -18.137  1.00165.30           N  
ANISOU  137  N   ILE A  52    20932  22254  19621   1439  -3064   -771       N  
ATOM    138  CA  ILE A  52     -20.071  11.976 -19.555  1.00156.46           C  
ANISOU  138  CA  ILE A  52    19809  21047  18591   1279  -3121   -547       C  
ATOM    139  C   ILE A  52     -19.290  13.247 -19.860  1.00160.18           C  
ANISOU  139  C   ILE A  52    20395  21196  19270   1143  -3460   -421       C  
ATOM    140  O   ILE A  52     -18.582  13.332 -20.872  1.00158.48           O  
ANISOU  140  O   ILE A  52    20154  20942  19120    896  -3482   -145       O  
ATOM    141  CB  ILE A  52     -21.549  12.103 -19.967  1.00141.95           C  
ANISOU  141  CB  ILE A  52    17959  19247  16728   1462  -3104   -650       C  
ATOM    142  CG1 ILE A  52     -22.261  10.758 -19.810  1.00134.21           C  
ANISOU  142  CG1 ILE A  52    16844  18594  15555   1547  -2763   -720       C  
ATOM    143  CG2 ILE A  52     -21.666  12.603 -21.399  1.00135.17           C  
ANISOU  143  CG2 ILE A  52    17112  18273  15972   1309  -3206   -423       C  
ATOM    144  CD1 ILE A  52     -21.649   9.646 -20.637  1.00125.40           C  
ANISOU  144  CD1 ILE A  52    15620  17663  14363   1319  -2517   -499       C  
ATOM    145  N   ARG A  53     -19.394  14.249 -18.988  1.00161.76           N  
ANISOU  145  N   ARG A  53    20717  21167  19577   1303  -3737   -617       N  
ATOM    146  CA  ARG A  53     -18.570  15.443 -19.123  1.00161.70           C  
ANISOU  146  CA  ARG A  53    20822  20827  19788   1169  -4088   -507       C  
ATOM    147  C   ARG A  53     -17.131  15.217 -18.680  1.00155.26           C  
ANISOU  147  C   ARG A  53    19992  20010  18989    977  -4085   -399       C  
ATOM    148  O   ARG A  53     -16.313  16.137 -18.789  1.00158.05           O  
ANISOU  148  O   ARG A  53    20423  20099  19529    828  -4371   -276       O  
ATOM    149  CB  ARG A  53     -19.184  16.601 -18.330  1.00168.57           C  
ANISOU  149  CB  ARG A  53    21835  21435  20778   1423  -4413   -779       C  
ATOM    150  CG  ARG A  53     -20.591  16.967 -18.774  1.00171.13           C  
ANISOU  150  CG  ARG A  53    22179  21735  21109   1622  -4457   -886       C  
ATOM    151  CD  ARG A  53     -21.336  17.753 -17.706  1.00172.29           C  
ANISOU  151  CD  ARG A  53    22431  21741  21291   1957  -4683  -1242       C  
ATOM    152  NE  ARG A  53     -21.351  17.068 -16.417  1.00167.27           N  
ANISOU  152  NE  ARG A  53    21752  21330  20471   2139  -4507  -1487       N  
ATOM    153  CZ  ARG A  53     -20.651  17.456 -15.356  1.00164.41           C  
ANISOU  153  CZ  ARG A  53    21468  20855  20144   2201  -4675  -1641       C  
ATOM    154  NH1 ARG A  53     -19.875  18.530 -15.428  1.00164.71           N  
ANISOU  154  NH1 ARG A  53    21632  20539  20411   2087  -5034  -1577       N  
ATOM    155  NH2 ARG A  53     -20.725  16.773 -14.222  1.00163.34           N  
ANISOU  155  NH2 ARG A  53    21280  20963  19819   2371  -4494  -1849       N  
ATOM    156  N   LYS A  54     -16.805  14.023 -18.185  1.00149.09           N  
ANISOU  156  N   LYS A  54    19110  19510  18026    973  -3783   -435       N  
ATOM    157  CA  LYS A  54     -15.444  13.672 -17.802  1.00146.17           C  
ANISOU  157  CA  LYS A  54    18708  19176  17653    792  -3746   -326       C  
ATOM    158  C   LYS A  54     -14.708  12.897 -18.883  1.00147.68           C  
ANISOU  158  C   LYS A  54    18775  19543  17794    521  -3534    -16       C  
ATOM    159  O   LYS A  54     -13.474  12.947 -18.937  1.00141.20           O  
ANISOU  159  O   LYS A  54    17931  18689  17031    313  -3585    158       O  
ATOM    160  CB  LYS A  54     -15.457  12.851 -16.508  1.00134.75           C  
ANISOU  160  CB  LYS A  54    17229  17928  16040    962  -3563   -559       C  
ATOM    161  CG  LYS A  54     -14.426  13.283 -15.483  1.00129.09           C  
ANISOU  161  CG  LYS A  54    16580  17077  15391    941  -3747   -634       C  
ATOM    162  CD  LYS A  54     -14.905  12.970 -14.074  1.00124.62           C  
ANISOU  162  CD  LYS A  54    16032  16632  14685   1219  -3684   -953       C  
ATOM    163  CE  LYS A  54     -14.890  11.477 -13.799  1.00118.89           C  
ANISOU  163  CE  LYS A  54    15169  16260  13743   1220  -3300   -940       C  
ATOM    164  NZ  LYS A  54     -13.502  10.973 -13.630  1.00117.36           N  
ANISOU  164  NZ  LYS A  54    14927  16120  13546   1011  -3233   -787       N  
ATOM    165  N   LEU A  55     -15.435  12.176 -19.739  1.00149.56           N  
ANISOU  165  N   LEU A  55    18927  19979  17921    527  -3303     50       N  
ATOM    166  CA  LEU A  55     -14.814  11.543 -20.896  1.00145.36           C  
ANISOU  166  CA  LEU A  55    18281  19610  17341    290  -3131    335       C  
ATOM    167  C   LEU A  55     -14.400  12.588 -21.923  1.00142.28           C  
ANISOU  167  C   LEU A  55    17925  19020  17116     94  -3375    595       C  
ATOM    168  O   LEU A  55     -13.279  12.555 -22.444  1.00142.93           O  
ANISOU  168  O   LEU A  55    17943  19137  17226   -143  -3378    845       O  
ATOM    169  CB  LEU A  55     -15.774  10.525 -21.511  1.00147.17           C  
ANISOU  169  CB  LEU A  55    18416  20089  17412    368  -2847    310       C  
ATOM    170  CG  LEU A  55     -16.024   9.267 -20.678  1.00146.40           C  
ANISOU  170  CG  LEU A  55    18248  20233  17145    500  -2567    132       C  
ATOM    171  CD1 LEU A  55     -17.195   8.482 -21.237  1.00145.92           C  
ANISOU  171  CD1 LEU A  55    18115  20358  16971    601  -2356     83       C  
ATOM    172  CD2 LEU A  55     -14.773   8.406 -20.638  1.00144.02           C  
ANISOU  172  CD2 LEU A  55    17857  20087  16777    330  -2405    264       C  
ATOM    173  N   ALA A  56     -15.294  13.537 -22.218  1.00140.77           N  
ANISOU  173  N   ALA A  56    17825  18624  17036    191  -3589    548       N  
ATOM    174  CA  ALA A  56     -14.937  14.659 -23.077  1.00139.52           C  
ANISOU  174  CA  ALA A  56    17713  18234  17062     13  -3869    794       C  
ATOM    175  C   ALA A  56     -13.811  15.495 -22.483  1.00147.43           C  
ANISOU  175  C   ALA A  56    18784  18994  18238   -116  -4146    860       C  
ATOM    176  O   ALA A  56     -13.174  16.266 -23.209  1.00152.00           O  
ANISOU  176  O   ALA A  56    19366  19420  18967   -336  -4354   1136       O  
ATOM    177  CB  ALA A  56     -16.162  15.537 -23.337  1.00132.82           C  
ANISOU  177  CB  ALA A  56    16966  17187  16315    176  -4070    692       C  
ATOM    178  N   GLU A  57     -13.557  15.361 -21.182  1.00147.55           N  
ANISOU  178  N   GLU A  57    18847  18979  18237     13  -4162    622       N  
ATOM    179  CA  GLU A  57     -12.410  15.989 -20.543  1.00150.35           C  
ANISOU  179  CA  GLU A  57    19253  19136  18736   -111  -4399    669       C  
ATOM    180  C   GLU A  57     -11.102  15.274 -20.854  1.00157.38           C  
ANISOU  180  C   GLU A  57    20010  20228  19559   -366  -4223    918       C  
ATOM    181  O   GLU A  57     -10.041  15.743 -20.430  1.00163.19           O  
ANISOU  181  O   GLU A  57    20765  20825  20417   -507  -4407   1003       O  
ATOM    182  CB  GLU A  57     -12.623  16.045 -19.027  1.00146.43           C  
ANISOU  182  CB  GLU A  57    18849  18568  18220    136  -4466    310       C  
ATOM    183  CG  GLU A  57     -12.108  17.311 -18.362  1.00147.79           C  
ANISOU  183  CG  GLU A  57    19159  18372  18624    127  -4886    248       C  
ATOM    184  CD  GLU A  57     -13.017  18.512 -18.576  1.00147.83           C  
ANISOU  184  CD  GLU A  57    19298  18065  18805    258  -5211    159       C  
ATOM    185  OE1 GLU A  57     -13.961  18.424 -19.388  1.00147.16           O  
ANISOU  185  OE1 GLU A  57    19191  18049  18675    314  -5115    199       O  
ATOM    186  OE2 GLU A  57     -12.785  19.553 -17.926  1.00148.49           O  
ANISOU  186  OE2 GLU A  57    19513  17827  19080    310  -5576     40       O  
ATOM    187  N   GLN A  58     -11.154  14.150 -21.573  1.00156.06           N  
ANISOU  187  N   GLN A  58    19706  20385  19205   -420  -3882   1027       N  
ATOM    188  CA  GLN A  58      -9.963  13.436 -22.019  1.00152.43           C  
ANISOU  188  CA  GLN A  58    19105  20147  18666   -647  -3704   1268       C  
ATOM    189  C   GLN A  58      -9.855  13.412 -23.539  1.00153.56           C  
ANISOU  189  C   GLN A  58    19144  20415  18785   -839  -3638   1588       C  
ATOM    190  O   GLN A  58      -9.126  12.582 -24.092  1.00150.94           O  
ANISOU  190  O   GLN A  58    18671  20353  18328   -978  -3415   1761       O  
ATOM    191  CB  GLN A  58      -9.952  12.006 -21.472  1.00141.44           C  
ANISOU  191  CB  GLN A  58    17628  19055  17058   -538  -3353   1108       C  
ATOM    192  CG  GLN A  58      -9.955  11.907 -19.956  1.00137.71           C  
ANISOU  192  CG  GLN A  58    17232  18517  16575   -360  -3385    818       C  
ATOM    193  CD  GLN A  58      -9.867  10.473 -19.468  1.00132.83           C  
ANISOU  193  CD  GLN A  58    16518  18198  15753   -281  -3045    707       C  
ATOM    194  OE1 GLN A  58      -9.364  10.206 -18.377  1.00135.76           O  
ANISOU  194  OE1 GLN A  58    16903  18583  16096   -226  -3034    574       O  
ATOM    195  NE2 GLN A  58     -10.361   9.541 -20.276  1.00125.63           N  
ANISOU  195  NE2 GLN A  58    15510  17520  14703   -274  -2780    762       N  
ATOM    196  N   GLY A  59     -10.564  14.306 -24.226  1.00155.23           N  
ANISOU  196  N   GLY A  59    19423  20448  19110   -839  -3833   1667       N  
ATOM    197  CA  GLY A  59     -10.641  14.237 -25.676  1.00153.92           C  
ANISOU  197  CA  GLY A  59    19159  20430  18892   -987  -3755   1949       C  
ATOM    198  C   GLY A  59     -11.264  12.957 -26.181  1.00147.84           C  
ANISOU  198  C   GLY A  59    18291  19995  17887   -883  -3392   1871       C  
ATOM    199  O   GLY A  59     -10.942  12.507 -27.286  1.00152.11           O  
ANISOU  199  O   GLY A  59    18706  20767  18321  -1023  -3243   2102       O  
ATOM    200  N   LEU A  60     -12.160  12.359 -25.399  1.00138.42           N  
ANISOU  200  N   LEU A  60    17147  18838  16608   -638  -3255   1553       N  
ATOM    201  CA  LEU A  60     -12.700  11.030 -25.658  1.00126.26           C  
ANISOU  201  CA  LEU A  60    15513  17600  14858   -535  -2914   1449       C  
ATOM    202  C   LEU A  60     -14.135  11.054 -26.161  1.00127.41           C  
ANISOU  202  C   LEU A  60    15693  17746  14971   -376  -2885   1343       C  
ATOM    203  O   LEU A  60     -14.494  10.247 -27.021  1.00128.12           O  
ANISOU  203  O   LEU A  60    15689  18068  14921   -381  -2672   1398       O  
ATOM    204  CB  LEU A  60     -12.603  10.188 -24.376  1.00118.30           C  
ANISOU  204  CB  LEU A  60    14508  16673  13767   -393  -2756   1195       C  
ATOM    205  CG  LEU A  60     -12.614   8.656 -24.335  1.00114.63           C  
ANISOU  205  CG  LEU A  60    13930  16518  13107   -340  -2411   1115       C  
ATOM    206  CD1 LEU A  60     -13.928   8.065 -24.782  1.00108.95           C  
ANISOU  206  CD1 LEU A  60    13192  15916  12288   -188  -2254    996       C  
ATOM    207  CD2 LEU A  60     -11.476   8.118 -25.184  1.00115.05           C  
ANISOU  207  CD2 LEU A  60    13851  16777  13087   -550  -2287   1367       C  
ATOM    208  N   VAL A  61     -14.967  11.957 -25.653  1.00127.17           N  
ANISOU  208  N   VAL A  61    15792  17464  15064   -226  -3102   1184       N  
ATOM    209  CA  VAL A  61     -16.340  12.080 -26.130  1.00116.61           C  
ANISOU  209  CA  VAL A  61    14483  16114  13708    -72  -3099   1089       C  
ATOM    210  C   VAL A  61     -16.658  13.537 -26.449  1.00117.52           C  
ANISOU  210  C   VAL A  61    14712  15919  14022    -87  -3446   1169       C  
ATOM    211  O   VAL A  61     -16.711  13.930 -27.614  1.00120.20           O  
ANISOU  211  O   VAL A  61    15024  16254  14392   -216  -3515   1406       O  
ATOM    212  CB  VAL A  61     -17.346  11.517 -25.109  1.00106.88           C  
ANISOU  212  CB  VAL A  61    13278  14936  12395    197  -2971    753       C  
ATOM    213  CG1 VAL A  61     -18.770  11.800 -25.562  1.00106.77           C  
ANISOU  213  CG1 VAL A  61    13295  14887  12385    359  -3006    657       C  
ATOM    214  CG2 VAL A  61     -17.135  10.023 -24.921  1.00101.11           C  
ANISOU  214  CG2 VAL A  61    12430  14510  11479    203  -2633    700       C  
ATOM    215  N   THR A  70     -21.316  11.516 -28.466  1.00134.46           N  
ANISOU  215  N   THR A  70    16697  18623  15769    431  -2865    821       N  
ATOM    216  CA  THR A  70     -20.399  11.878 -29.540  1.00137.29           C  
ANISOU  216  CA  THR A  70    17026  18982  16157    186  -2941   1140       C  
ATOM    217  C   THR A  70     -19.056  11.173 -29.377  1.00134.17           C  
ANISOU  217  C   THR A  70    16552  18739  15686     20  -2792   1249       C  
ATOM    218  O   THR A  70     -18.087  11.768 -28.907  1.00134.21           O  
ANISOU  218  O   THR A  70    16600  18597  15795    -88  -2944   1331       O  
ATOM    219  CB  THR A  70     -20.165  13.399 -29.595  1.00140.37           C  
ANISOU  219  CB  THR A  70    17532  19046  16758    122  -3301   1263       C  
ATOM    220  OG1 THR A  70     -19.253  13.784 -28.558  1.00140.73           O  
ANISOU  220  OG1 THR A  70    17637  18932  16902     85  -3425   1216       O  
ATOM    221  CG2 THR A  70     -21.476  14.148 -29.415  1.00139.28           C  
ANISOU  221  CG2 THR A  70    17489  18716  16714    336  -3476   1086       C  
ATOM    222  N   LEU A  71     -19.005   9.903 -29.768  1.00131.03           N  
ANISOU  222  N   LEU A  71    16038  18633  15114      4  -2506   1245       N  
ATOM    223  CA  LEU A  71     -17.778   9.118 -29.678  1.00135.97           C  
ANISOU  223  CA  LEU A  71    16577  19432  15654   -134  -2346   1336       C  
ATOM    224  C   LEU A  71     -16.847   9.525 -30.813  1.00140.86           C  
ANISOU  224  C   LEU A  71    17135  20112  16272   -365  -2415   1664       C  
ATOM    225  O   LEU A  71     -17.159   9.312 -31.989  1.00139.10           O  
ANISOU  225  O   LEU A  71    16845  20045  15959   -408  -2348   1793       O  
ATOM    226  CB  LEU A  71     -18.093   7.626 -29.734  1.00132.54           C  
ANISOU  226  CB  LEU A  71    16041  19272  15046    -57  -2042   1210       C  
ATOM    227  CG  LEU A  71     -18.325   6.921 -28.396  1.00128.04           C  
ANISOU  227  CG  LEU A  71    15485  18714  14451     94  -1920    952       C  
ATOM    228  CD1 LEU A  71     -18.477   5.421 -28.600  1.00125.34           C  
ANISOU  228  CD1 LEU A  71    15032  18636  13956    126  -1639    882       C  
ATOM    229  CD2 LEU A  71     -17.197   7.222 -27.421  1.00124.32           C  
ANISOU  229  CD2 LEU A  71    15050  18139  14045     26  -1998    960       C  
ATOM    230  N   THR A  72     -15.700  10.110 -30.466  1.00143.41           N  
ANISOU  230  N   THR A  72    17474  20326  16689   -514  -2551   1806       N  
ATOM    231  CA  THR A  72     -14.733  10.529 -31.474  1.00144.13           C  
ANISOU  231  CA  THR A  72    17489  20492  16781   -749  -2621   2145       C  
ATOM    232  C   THR A  72     -13.868   9.351 -31.904  1.00148.56           C  
ANISOU  232  C   THR A  72    17897  21392  17156   -835  -2355   2226       C  
ATOM    233  O   THR A  72     -14.242   8.192 -31.699  1.00144.52           O  
ANISOU  233  O   THR A  72    17343  21056  16513   -708  -2120   2031       O  
ATOM    234  CB  THR A  72     -13.858  11.671 -30.949  1.00141.51           C  
ANISOU  234  CB  THR A  72    17225  19900  16644   -887  -2897   2283       C  
ATOM    235  OG1 THR A  72     -12.865  12.003 -31.927  1.00148.87           O  
ANISOU  235  OG1 THR A  72    18056  20943  17566  -1132  -2948   2642       O  
ATOM    236  CG2 THR A  72     -13.166  11.268 -29.659  1.00133.58           C  
ANISOU  236  CG2 THR A  72    16239  18861  15655   -852  -2845   2115       C  
ATOM    237  N   ASP A  73     -12.709   9.637 -32.503  1.00155.59           N  
ANISOU  237  N   ASP A  73    18699  22381  18037  -1049  -2398   2518       N  
ATOM    238  CA  ASP A  73     -11.840   8.567 -32.981  1.00160.59           C  
ANISOU  238  CA  ASP A  73    19176  23355  18485  -1121  -2157   2601       C  
ATOM    239  C   ASP A  73     -11.208   7.790 -31.831  1.00148.23           C  
ANISOU  239  C   ASP A  73    17603  21816  16903  -1071  -2029   2420       C  
ATOM    240  O   ASP A  73     -10.959   6.587 -31.964  1.00149.57           O  
ANISOU  240  O   ASP A  73    17675  22242  16914  -1024  -1788   2342       O  
ATOM    241  CB  ASP A  73     -10.757   9.139 -33.895  1.00177.15           C  
ANISOU  241  CB  ASP A  73    21164  25574  20572  -1361  -2243   2976       C  
ATOM    242  CG  ASP A  73     -10.125  10.399 -33.334  1.00182.94           C  
ANISOU  242  CG  ASP A  73    21969  26014  21526  -1508  -2532   3132       C  
ATOM    243  OD1 ASP A  73     -10.837  11.175 -32.663  1.00186.16           O  
ANISOU  243  OD1 ASP A  73    22531  26093  22108  -1422  -2733   2996       O  
ATOM    244  OD2 ASP A  73      -8.917  10.615 -33.568  1.00184.85           O  
ANISOU  244  OD2 ASP A  73    22107  26356  21771  -1706  -2569   3389       O  
ATOM    245  N   SER A  74     -10.943   8.452 -30.703  1.00134.27           N  
ANISOU  245  N   SER A  74    15935  19783  15297  -1072  -2199   2347       N  
ATOM    246  CA  SER A  74     -10.330   7.770 -29.569  1.00118.26           C  
ANISOU  246  CA  SER A  74    13903  17777  13254  -1026  -2092   2183       C  
ATOM    247  C   SER A  74     -11.340   6.945 -28.782  1.00104.14           C  
ANISOU  247  C   SER A  74    12173  15983  11413   -795  -1945   1854       C  
ATOM    248  O   SER A  74     -10.992   5.879 -28.255  1.00 94.86           O  
ANISOU  248  O   SER A  74    10942  14956  10143   -741  -1751   1732       O  
ATOM    249  CB  SER A  74      -9.654   8.788 -28.650  1.00121.50           C  
ANISOU  249  CB  SER A  74    14397  17915  13851  -1110  -2340   2222       C  
ATOM    250  OG  SER A  74     -10.576   9.772 -28.215  1.00125.16           O  
ANISOU  250  OG  SER A  74    15014  18073  14467  -1011  -2566   2106       O  
ATOM    251  N   GLY A  75     -12.587   7.415 -28.694  1.00 98.78           N  
ANISOU  251  N   GLY A  75    11596  15143  10795   -659  -2037   1719       N  
ATOM    252  CA  GLY A  75     -13.598   6.679 -27.957  1.00 93.46           C  
ANISOU  252  CA  GLY A  75    10961  14481  10070   -445  -1903   1430       C  
ATOM    253  C   GLY A  75     -13.894   5.316 -28.547  1.00 99.10           C  
ANISOU  253  C   GLY A  75    11567  15474  10614   -395  -1631   1379       C  
ATOM    254  O   GLY A  75     -14.238   4.381 -27.817  1.00 90.82           O  
ANISOU  254  O   GLY A  75    10507  14493   9507   -270  -1475   1181       O  
ATOM    255  N   ARG A  76     -13.761   5.180 -29.867  1.00111.21           N  
ANISOU  255  N   ARG A  76    13016  17174  12065   -489  -1581   1560       N  
ATOM    256  CA  ARG A  76     -14.001   3.891 -30.505  1.00120.50           C  
ANISOU  256  CA  ARG A  76    14090  18612  13081   -437  -1346   1504       C  
ATOM    257  C   ARG A  76     -12.972   2.861 -30.056  1.00123.07           C  
ANISOU  257  C   ARG A  76    14332  19099  13328   -467  -1180   1475       C  
ATOM    258  O   ARG A  76     -13.321   1.726 -29.718  1.00122.03           O  
ANISOU  258  O   ARG A  76    14169  19068  13127   -356  -1008   1302       O  
ATOM    259  CB  ARG A  76     -13.985   4.046 -32.025  1.00128.02           C  
ANISOU  259  CB  ARG A  76    14967  19725  13948   -528  -1346   1707       C  
ATOM    260  CG  ARG A  76     -14.630   2.888 -32.765  1.00130.34           C  
ANISOU  260  CG  ARG A  76    15186  20243  14096   -433  -1154   1606       C  
ATOM    261  CD  ARG A  76     -14.387   2.984 -34.261  1.00130.86           C  
ANISOU  261  CD  ARG A  76    15160  20515  14046   -526  -1145   1815       C  
ATOM    262  NE  ARG A  76     -13.113   2.384 -34.645  1.00131.73           N  
ANISOU  262  NE  ARG A  76    15146  20869  14038   -622  -1030   1934       N  
ATOM    263  CZ  ARG A  76     -12.035   3.077 -34.996  1.00136.18           C  
ANISOU  263  CZ  ARG A  76    15654  21485  14603   -789  -1115   2189       C  
ATOM    264  NH1 ARG A  76     -12.072   4.403 -35.015  1.00137.18           N  
ANISOU  264  NH1 ARG A  76    15850  21413  14860   -890  -1330   2358       N  
ATOM    265  NH2 ARG A  76     -10.919   2.444 -35.330  1.00139.16           N  
ANISOU  265  NH2 ARG A  76    15902  22115  14857   -855   -994   2279       N  
ATOM    266  N   ARG A  77     -11.692   3.243 -30.038  1.00126.26           N  
ANISOU  266  N   ARG A  77    14696  19526  13753   -618  -1238   1651       N  
ATOM    267  CA  ARG A  77     -10.655   2.301 -29.629  1.00119.57           C  
ANISOU  267  CA  ARG A  77    13763  18836  12833   -645  -1089   1631       C  
ATOM    268  C   ARG A  77     -10.651   2.080 -28.121  1.00108.47           C  
ANISOU  268  C   ARG A  77    12430  17286  11499   -557  -1086   1439       C  
ATOM    269  O   ARG A  77     -10.295   0.988 -27.662  1.00106.95           O  
ANISOU  269  O   ARG A  77    12183  17215  11238   -506   -924   1336       O  
ATOM    270  CB  ARG A  77      -9.283   2.779 -30.103  1.00123.11           C  
ANISOU  270  CB  ARG A  77    14124  19378  13273   -836  -1151   1893       C  
ATOM    271  CG  ARG A  77      -9.086   2.681 -31.607  1.00126.65           C  
ANISOU  271  CG  ARG A  77    14455  20072  13593   -915  -1096   2088       C  
ATOM    272  CD  ARG A  77      -7.684   3.105 -32.012  1.00131.25           C  
ANISOU  272  CD  ARG A  77    14928  20785  14156  -1107  -1144   2361       C  
ATOM    273  NE  ARG A  77      -7.509   3.102 -33.461  1.00131.97           N  
ANISOU  273  NE  ARG A  77    14896  21138  14107  -1179  -1099   2566       N  
ATOM    274  CZ  ARG A  77      -7.856   4.106 -34.260  1.00129.97           C  
ANISOU  274  CZ  ARG A  77    14659  20835  13890  -1270  -1247   2764       C  
ATOM    275  NH1 ARG A  77      -8.400   5.204 -33.754  1.00123.71           N  
ANISOU  275  NH1 ARG A  77    14005  19718  13283  -1294  -1461   2774       N  
ATOM    276  NH2 ARG A  77      -7.658   4.012 -35.568  1.00133.10           N  
ANISOU  276  NH2 ARG A  77    14929  21512  14132  -1327  -1188   2951       N  
ATOM    277  N   ALA A  78     -11.034   3.089 -27.337  1.00 99.91           N  
ANISOU  277  N   ALA A  78    11467  15948  10548   -529  -1269   1385       N  
ATOM    278  CA  ALA A  78     -11.131   2.899 -25.893  1.00 88.93           C  
ANISOU  278  CA  ALA A  78    10144  14441   9204   -422  -1267   1187       C  
ATOM    279  C   ALA A  78     -12.256   1.928 -25.547  1.00 86.79           C  
ANISOU  279  C   ALA A  78     9875  14235   8866   -244  -1107    971       C  
ATOM    280  O   ALA A  78     -12.037   0.907 -24.879  1.00 79.51           O  
ANISOU  280  O   ALA A  78     8913  13411   7888   -188   -958    865       O  
ATOM    281  CB  ALA A  78     -11.340   4.246 -25.199  1.00 80.53           C  
ANISOU  281  CB  ALA A  78     9210  13099   8291   -410  -1519   1161       C  
ATOM    282  N   ALA A  79     -13.473   2.233 -26.008  1.00 83.62           N  
ANISOU  282  N   ALA A  79     9514  13781   8476   -159  -1143    917       N  
ATOM    283  CA  ALA A  79     -14.606   1.348 -25.761  1.00 72.50           C  
ANISOU  283  CA  ALA A  79     8094  12441   7013     -3  -1001    735       C  
ATOM    284  C   ALA A  79     -14.368  -0.035 -26.352  1.00 72.57           C  
ANISOU  284  C   ALA A  79     7988  12676   6908    -18   -792    743       C  
ATOM    285  O   ALA A  79     -14.757  -1.045 -25.758  1.00 71.19           O  
ANISOU  285  O   ALA A  79     7785  12567   6698     76   -657    605       O  
ATOM    286  CB  ALA A  79     -15.883   1.962 -26.333  1.00 68.01           C  
ANISOU  286  CB  ALA A  79     7572  11793   6475     74  -1086    704       C  
ATOM    287  N   LEU A  80     -13.726  -0.101 -27.521  1.00 73.33           N  
ANISOU  287  N   LEU A  80     8014  12899   6947   -132   -770    905       N  
ATOM    288  CA  LEU A  80     -13.438  -1.395 -28.131  1.00 81.41           C  
ANISOU  288  CA  LEU A  80     8931  14142   7860   -131   -590    896       C  
ATOM    289  C   LEU A  80     -12.413  -2.182 -27.325  1.00 88.04           C  
ANISOU  289  C   LEU A  80     9726  15046   8679   -148   -495    864       C  
ATOM    290  O   LEU A  80     -12.489  -3.415 -27.266  1.00 98.92           O  
ANISOU  290  O   LEU A  80    11045  16538  10002    -85   -350    768       O  
ATOM    291  CB  LEU A  80     -12.952  -1.205 -29.568  1.00 82.35           C  
ANISOU  291  CB  LEU A  80     8977  14411   7901   -234   -597   1077       C  
ATOM    292  CG  LEU A  80     -14.034  -1.224 -30.648  1.00 79.03           C  
ANISOU  292  CG  LEU A  80     8549  14044   7434   -183   -593   1067       C  
ATOM    293  CD1 LEU A  80     -13.500  -0.667 -31.958  1.00 79.91           C  
ANISOU  293  CD1 LEU A  80     8602  14284   7475   -299   -646   1283       C  
ATOM    294  CD2 LEU A  80     -14.558  -2.634 -30.839  1.00 80.17           C  
ANISOU  294  CD2 LEU A  80     8634  14323   7504    -78   -430    912       C  
ATOM    295  N   ALA A  81     -11.453  -1.496 -26.702  1.00 79.59           N  
ANISOU  295  N   ALA A  81     8683  13894   7664   -232   -589    945       N  
ATOM    296  CA  ALA A  81     -10.489  -2.184 -25.850  1.00 72.72           C  
ANISOU  296  CA  ALA A  81     7774  13075   6780   -243   -511    912       C  
ATOM    297  C   ALA A  81     -11.164  -2.734 -24.600  1.00 73.84           C  
ANISOU  297  C   ALA A  81     7965  13140   6950   -113   -457    721       C  
ATOM    298  O   ALA A  81     -10.977  -3.905 -24.244  1.00 66.26           O  
ANISOU  298  O   ALA A  81     6949  12279   5947    -67   -321    648       O  
ATOM    299  CB  ALA A  81      -9.346  -1.238 -25.480  1.00 63.86           C  
ANISOU  299  CB  ALA A  81     6669  11875   5719   -370   -644   1047       C  
ATOM    300  N   MET A  82     -11.965  -1.904 -23.924  1.00 75.98           N  
ANISOU  300  N   MET A  82     8335  13243   7292    -46   -569    644       N  
ATOM    301  CA  MET A  82     -12.664  -2.371 -22.729  1.00 84.75           C  
ANISOU  301  CA  MET A  82     9478  14315   8410     87   -517    474       C  
ATOM    302  C   MET A  82     -13.605  -3.526 -23.056  1.00 79.56           C  
ANISOU  302  C   MET A  82     8761  13767   7701    172   -366    389       C  
ATOM    303  O   MET A  82     -13.684  -4.509 -22.304  1.00 71.13           O  
ANISOU  303  O   MET A  82     7658  12756   6611    231   -256    306       O  
ATOM    304  CB  MET A  82     -13.421  -1.209 -22.088  1.00 98.81           C  
ANISOU  304  CB  MET A  82    11364  15919  10259    164   -673    397       C  
ATOM    305  CG  MET A  82     -12.525  -0.027 -21.767  1.00117.53           C  
ANISOU  305  CG  MET A  82    13802  18148  12705     78   -857    474       C  
ATOM    306  SD  MET A  82     -13.368   1.562 -21.837  1.00131.52           S  
ANISOU  306  SD  MET A  82    15695  19698  14579    127  -1095    448       S  
ATOM    307  CE  MET A  82     -11.984   2.669 -21.580  1.00133.85           C  
ANISOU  307  CE  MET A  82    16041  19842  14974    -23  -1306    580       C  
ATOM    308  N   VAL A  83     -14.317  -3.430 -24.182  1.00 76.00           N  
ANISOU  308  N   VAL A  83     8296  13345   7235    173   -369    417       N  
ATOM    309  CA  VAL A  83     -15.145  -4.544 -24.636  1.00 62.64           C  
ANISOU  309  CA  VAL A  83     6541  11755   5503    238   -243    346       C  
ATOM    310  C   VAL A  83     -14.290  -5.783 -24.866  1.00 63.37           C  
ANISOU  310  C   VAL A  83     6548  11986   5545    200   -118    362       C  
ATOM    311  O   VAL A  83     -14.664  -6.889 -24.465  1.00 56.97           O  
ANISOU  311  O   VAL A  83     5696  11221   4732    261    -17    277       O  
ATOM    312  CB  VAL A  83     -15.935  -4.152 -25.900  1.00 55.57           C  
ANISOU  312  CB  VAL A  83     5646  10874   4595    236   -285    383       C  
ATOM    313  CG1 VAL A  83     -16.586  -5.373 -26.518  1.00 57.34           C  
ANISOU  313  CG1 VAL A  83     5795  11214   4777    285   -166    318       C  
ATOM    314  CG2 VAL A  83     -17.006  -3.135 -25.550  1.00 42.56           C  
ANISOU  314  CG2 VAL A  83     4077   9090   3006    312   -397    329       C  
ATOM    315  N   ARG A  84     -13.122  -5.619 -25.493  1.00 64.00           N  
ANISOU  315  N   ARG A  84     6592  12135   5587    100   -130    478       N  
ATOM    316  CA  ARG A  84     -12.234  -6.759 -25.709  1.00 52.74           C  
ANISOU  316  CA  ARG A  84     5080  10850   4109     81    -20    484       C  
ATOM    317  C   ARG A  84     -11.889  -7.444 -24.392  1.00 53.99           C  
ANISOU  317  C   ARG A  84     5238  10977   4297    118     36    411       C  
ATOM    318  O   ARG A  84     -11.946  -8.676 -24.284  1.00 55.15           O  
ANISOU  318  O   ARG A  84     5331  11189   4435    166    134    343       O  
ATOM    319  CB  ARG A  84     -10.960  -6.314 -26.428  1.00 55.23           C  
ANISOU  319  CB  ARG A  84     5350  11262   4375    -30    -50    632       C  
ATOM    320  CG  ARG A  84     -10.144  -7.475 -26.977  1.00 64.13           C  
ANISOU  320  CG  ARG A  84     6372  12572   5424    -27     61    630       C  
ATOM    321  CD  ARG A  84      -8.958  -7.016 -27.818  1.00 72.25           C  
ANISOU  321  CD  ARG A  84     7329  13735   6389   -130     40    788       C  
ATOM    322  NE  ARG A  84      -8.124  -6.034 -27.129  1.00 77.32           N  
ANISOU  322  NE  ARG A  84     8001  14301   7074   -231    -52    903       N  
ATOM    323  CZ  ARG A  84      -8.100  -4.737 -27.417  1.00 86.03           C  
ANISOU  323  CZ  ARG A  84     9145  15330   8211   -323   -179   1036       C  
ATOM    324  NH1 ARG A  84      -8.865  -4.257 -28.389  1.00 89.53           N  
ANISOU  324  NH1 ARG A  84     9601  15783   8631   -325   -221   1080       N  
ATOM    325  NH2 ARG A  84      -7.309  -3.919 -26.736  1.00 88.53           N  
ANISOU  325  NH2 ARG A  84     9490  15554   8593   -415   -278   1128       N  
ATOM    326  N   ARG A  85     -11.540  -6.655 -23.371  1.00 53.51           N  
ANISOU  326  N   ARG A  85     5239  10814   4279     99    -39    425       N  
ATOM    327  CA  ARG A  85     -11.222  -7.229 -22.067  1.00 65.08           C  
ANISOU  327  CA  ARG A  85     6705  12261   5761    139      7    363       C  
ATOM    328  C   ARG A  85     -12.414  -7.983 -21.488  1.00 67.62           C  
ANISOU  328  C   ARG A  85     7024  12571   6097    245     75    251       C  
ATOM    329  O   ARG A  85     -12.285  -9.136 -21.059  1.00 61.90           O  
ANISOU  329  O   ARG A  85     6247  11901   5370    274    167    215       O  
ATOM    330  CB  ARG A  85     -10.764  -6.132 -21.106  1.00 77.44           C  
ANISOU  330  CB  ARG A  85     8345  13716   7364    114   -108    381       C  
ATOM    331  CG  ARG A  85      -9.726  -5.188 -21.683  1.00 90.30           C  
ANISOU  331  CG  ARG A  85     9978  15329   9002     -9   -209    515       C  
ATOM    332  CD  ARG A  85      -9.460  -4.027 -20.741  1.00 96.21           C  
ANISOU  332  CD  ARG A  85    10814  15930   9811    -25   -359    514       C  
ATOM    333  NE  ARG A  85      -8.974  -4.489 -19.446  1.00 95.87           N  
ANISOU  333  NE  ARG A  85    10775  15888   9765     14   -326    447       N  
ATOM    334  CZ  ARG A  85      -7.705  -4.784 -19.185  1.00103.03           C  
ANISOU  334  CZ  ARG A  85    11634  16850  10662    -60   -310    513       C  
ATOM    335  NH1 ARG A  85      -6.784  -4.666 -20.132  1.00109.97           N  
ANISOU  335  NH1 ARG A  85    12450  17804  11531   -177   -318    650       N  
ATOM    336  NH2 ARG A  85      -7.358  -5.198 -17.976  1.00100.61           N  
ANISOU  336  NH2 ARG A  85    11335  16544  10350    -14   -286    448       N  
ATOM    337  N   HIS A  86     -13.589  -7.347 -21.475  1.00 65.94           N  
ANISOU  337  N   HIS A  86     6859  12291   5904    304     25    203       N  
ATOM    338  CA  HIS A  86     -14.772  -7.977 -20.891  1.00 59.27           C  
ANISOU  338  CA  HIS A  86     5997  11454   5070    401     85    114       C  
ATOM    339  C   HIS A  86     -15.107  -9.291 -21.593  1.00 52.82           C  
ANISOU  339  C   HIS A  86     5099  10718   4253    404    184    100       C  
ATOM    340  O   HIS A  86     -15.236 -10.342 -20.949  1.00 48.37           O  
ANISOU  340  O   HIS A  86     4488  10187   3704    435    259     71       O  
ATOM    341  CB  HIS A  86     -15.955  -7.009 -20.960  1.00 71.95           C  
ANISOU  341  CB  HIS A  86     7655  12991   6691    466      8     70       C  
ATOM    342  CG  HIS A  86     -17.105  -7.392 -20.082  1.00 79.95           C  
ANISOU  342  CG  HIS A  86     8646  14025   7706    573     55    -14       C  
ATOM    343  ND1 HIS A  86     -17.910  -8.481 -20.340  1.00 81.34           N  
ANISOU  343  ND1 HIS A  86     8746  14270   7891    598    147    -33       N  
ATOM    344  CD2 HIS A  86     -17.593  -6.824 -18.953  1.00 81.84           C  
ANISOU  344  CD2 HIS A  86     8921  14241   7935    664     18    -79       C  
ATOM    345  CE1 HIS A  86     -18.839  -8.572 -19.405  1.00 79.82           C  
ANISOU  345  CE1 HIS A  86     8531  14103   7693    687    172    -85       C  
ATOM    346  NE2 HIS A  86     -18.669  -7.578 -18.552  1.00 80.97           N  
ANISOU  346  NE2 HIS A  86     8742  14207   7817    738    101   -120       N  
ATOM    347  N   ARG A  87     -15.244  -9.247 -22.920  1.00 49.37           N  
ANISOU  347  N   ARG A  87     4646  10313   3800    375    172    124       N  
ATOM    348  CA  ARG A  87     -15.610 -10.438 -23.680  1.00 56.14           C  
ANISOU  348  CA  ARG A  87     5434  11237   4659    390    239     90       C  
ATOM    349  C   ARG A  87     -14.567 -11.539 -23.523  1.00 64.59           C  
ANISOU  349  C   ARG A  87     6453  12343   5746    367    296     94       C  
ATOM    350  O   ARG A  87     -14.915 -12.717 -23.367  1.00 66.13           O  
ANISOU  350  O   ARG A  87     6605  12518   6005    398    334     46       O  
ATOM    351  CB  ARG A  87     -15.793 -10.075 -25.154  1.00 62.02           C  
ANISOU  351  CB  ARG A  87     6174  12026   5366    367    204    115       C  
ATOM    352  CG  ARG A  87     -16.707  -8.882 -25.395  1.00 65.83           C  
ANISOU  352  CG  ARG A  87     6714  12442   5856    384    122    125       C  
ATOM    353  CD  ARG A  87     -18.157  -9.288 -25.540  1.00 81.83           C  
ANISOU  353  CD  ARG A  87     8718  14458   7914    454    137     51       C  
ATOM    354  NE  ARG A  87     -19.031  -8.133 -25.729  1.00 88.86           N  
ANISOU  354  NE  ARG A  87     9663  15286   8814    485     53     54       N  
ATOM    355  CZ  ARG A  87     -19.261  -7.549 -26.902  1.00 78.12           C  
ANISOU  355  CZ  ARG A  87     8316  13939   7427    463     -5     94       C  
ATOM    356  NH1 ARG A  87     -18.678  -8.009 -28.001  1.00 71.84           N  
ANISOU  356  NH1 ARG A  87     7479  13238   6577    416     18    132       N  
ATOM    357  NH2 ARG A  87     -20.072  -6.503 -26.975  1.00 67.49           N  
ANISOU  357  NH2 ARG A  87     7021  12520   6102    499    -92     94       N  
ATOM    358  N   LEU A  88     -13.282 -11.174 -23.560  1.00 63.15           N  
ANISOU  358  N   LEU A  88     6275  12183   5536    310    280    155       N  
ATOM    359  CA  LEU A  88     -12.230 -12.165 -23.361  1.00 58.32           C  
ANISOU  359  CA  LEU A  88     5618  11570   4971    297    313    154       C  
ATOM    360  C   LEU A  88     -12.335 -12.814 -21.987  1.00 57.15           C  
ANISOU  360  C   LEU A  88     5473  11363   4877    328    343    126       C  
ATOM    361  O   LEU A  88     -12.116 -14.024 -21.844  1.00 62.28           O  
ANISOU  361  O   LEU A  88     6085  11997   5580    347    371     98       O  
ATOM    362  CB  LEU A  88     -10.858 -11.520 -23.547  1.00 64.72           C  
ANISOU  362  CB  LEU A  88     6422  12431   5736    227    289    238       C  
ATOM    363  CG  LEU A  88     -10.273 -11.502 -24.959  1.00 70.89           C  
ANISOU  363  CG  LEU A  88     7154  13300   6483    195    279    279       C  
ATOM    364  CD1 LEU A  88      -8.926 -10.796 -24.970  1.00 73.79           C  
ANISOU  364  CD1 LEU A  88     7499  13732   6807    112    254    388       C  
ATOM    365  CD2 LEU A  88     -10.143 -12.918 -25.496  1.00 69.67           C  
ANISOU  365  CD2 LEU A  88     6943  13162   6368    252    311    200       C  
ATOM    366  N   LEU A  89     -12.672 -12.027 -20.961  1.00 51.74           N  
ANISOU  366  N   LEU A  89     4835  10657   4168    341    329    133       N  
ATOM    367  CA  LEU A  89     -12.883 -12.602 -19.636  1.00 59.16           C  
ANISOU  367  CA  LEU A  89     5769  11560   5149    378    357    114       C  
ATOM    368  C   LEU A  89     -14.051 -13.580 -19.643  1.00 67.23           C  
ANISOU  368  C   LEU A  89     6752  12564   6229    422    391     78       C  
ATOM    369  O   LEU A  89     -13.973 -14.655 -19.034  1.00 61.31           O  
ANISOU  369  O   LEU A  89     5967  11796   5532    429    420     84       O  
ATOM    370  CB  LEU A  89     -13.113 -11.494 -18.609  1.00 60.68           C  
ANISOU  370  CB  LEU A  89     6017  11757   5281    407    327    110       C  
ATOM    371  CG  LEU A  89     -11.899 -10.634 -18.254  1.00 56.77           C  
ANISOU  371  CG  LEU A  89     5564  11268   4737    358    274    150       C  
ATOM    372  CD1 LEU A  89     -12.290  -9.513 -17.301  1.00 61.31           C  
ANISOU  372  CD1 LEU A  89     6213  11782   5301    404    197    115       C  
ATOM    373  CD2 LEU A  89     -10.789 -11.489 -17.659  1.00 49.27           C  
ANISOU  373  CD2 LEU A  89     4575  10328   3817    332    310    177       C  
ATOM    374  N   GLU A  90     -15.142 -13.227 -20.331  1.00 68.09           N  
ANISOU  374  N   GLU A  90     6861  12688   6323    446    382     50       N  
ATOM    375  CA  GLU A  90     -16.268 -14.150 -20.454  1.00 55.59           C  
ANISOU  375  CA  GLU A  90     5226  11104   4791    476    409     23       C  
ATOM    376  C   GLU A  90     -15.825 -15.473 -21.070  1.00 58.69           C  
ANISOU  376  C   GLU A  90     5569  11498   5232    458    426     10       C  
ATOM    377  O   GLU A  90     -16.095 -16.554 -20.524  1.00 58.44           O  
ANISOU  377  O   GLU A  90     5488  11460   5258    465    453     17       O  
ATOM    378  CB  GLU A  90     -17.378 -13.513 -21.291  1.00 59.16           C  
ANISOU  378  CB  GLU A  90     5681  11586   5212    503    391     -8       C  
ATOM    379  CG  GLU A  90     -17.884 -12.180 -20.762  1.00 76.72           C  
ANISOU  379  CG  GLU A  90     7956  13821   7375    543    364    -13       C  
ATOM    380  CD  GLU A  90     -19.034 -11.629 -21.584  1.00 78.90           C  
ANISOU  380  CD  GLU A  90     8239  14085   7655    574    324    -43       C  
ATOM    381  OE1 GLU A  90     -19.043 -10.412 -21.866  1.00 77.09           O  
ANISOU  381  OE1 GLU A  90     8075  13819   7396    581    256    -42       O  
ATOM    382  OE2 GLU A  90     -19.931 -12.415 -21.950  1.00 72.88           O  
ANISOU  382  OE2 GLU A  90     7415  13341   6935    588    348    -62       O  
ATOM    383  N   THR A  91     -15.122 -15.400 -22.205  1.00 57.68           N  
ANISOU  383  N   THR A  91     5446  11396   5075    439    406     -6       N  
ATOM    384  CA  THR A  91     -14.672 -16.611 -22.884  1.00 55.49           C  
ANISOU  384  CA  THR A  91     5119  11143   4822    448    415    -47       C  
ATOM    385  C   THR A  91     -13.743 -17.433 -22.000  1.00 52.57           C  
ANISOU  385  C   THR A  91     4730  10752   4490    443    435    -25       C  
ATOM    386  O   THR A  91     -13.806 -18.669 -22.000  1.00 51.81           O  
ANISOU  386  O   THR A  91     4575  10669   4441    467    452    -57       O  
ATOM    387  CB  THR A  91     -13.972 -16.249 -24.194  1.00 52.56           C  
ANISOU  387  CB  THR A  91     4752  10826   4392    440    387    -62       C  
ATOM    388  OG1 THR A  91     -14.598 -15.096 -24.770  1.00 48.98           O  
ANISOU  388  OG1 THR A  91     4331  10390   3889    429    363    -44       O  
ATOM    389  CG2 THR A  91     -14.043 -17.409 -25.176  1.00 46.25           C  
ANISOU  389  CG2 THR A  91     3895  10081   3595    485    386   -146       C  
ATOM    390  N   PHE A  92     -12.873 -16.767 -21.239  1.00 55.32           N  
ANISOU  390  N   PHE A  92     5119  11080   4820    415    430     26       N  
ATOM    391  CA  PHE A  92     -11.923 -17.496 -20.404  1.00 62.17           C  
ANISOU  391  CA  PHE A  92     5970  11937   5716    412    445     50       C  
ATOM    392  C   PHE A  92     -12.631 -18.207 -19.258  1.00 59.25           C  
ANISOU  392  C   PHE A  92     5573  11540   5397    425    473     77       C  
ATOM    393  O   PHE A  92     -12.362 -19.383 -18.985  1.00 52.29           O  
ANISOU  393  O   PHE A  92     4638  10668   4562    437    492     81       O  
ATOM    394  CB  PHE A  92     -10.853 -16.550 -19.864  1.00 70.58           C  
ANISOU  394  CB  PHE A  92     7075  13000   6743    376    429     99       C  
ATOM    395  CG  PHE A  92      -9.769 -17.246 -19.094  1.00 78.92           C  
ANISOU  395  CG  PHE A  92     8110  14057   7819    374    440    123       C  
ATOM    396  CD1 PHE A  92      -9.071 -18.301 -19.660  1.00 77.85           C  
ANISOU  396  CD1 PHE A  92     7925  13954   7699    396    447     92       C  
ATOM    397  CD2 PHE A  92      -9.450 -16.852 -17.806  1.00 81.38           C  
ANISOU  397  CD2 PHE A  92     8447  14351   8124    362    440    168       C  
ATOM    398  CE1 PHE A  92      -8.072 -18.947 -18.957  1.00 81.13           C  
ANISOU  398  CE1 PHE A  92     8316  14380   8130    401    456    114       C  
ATOM    399  CE2 PHE A  92      -8.452 -17.495 -17.097  1.00 83.50           C  
ANISOU  399  CE2 PHE A  92     8693  14628   8406    360    448    194       C  
ATOM    400  CZ  PHE A  92      -7.762 -18.544 -17.674  1.00 81.66           C  
ANISOU  400  CZ  PHE A  92     8410  14423   8195    378    457    172       C  
ATOM    401  N   LEU A  93     -13.537 -17.508 -18.570  1.00 59.12           N  
ANISOU  401  N   LEU A  93     5583  11509   5372    430    475    101       N  
ATOM    402  CA  LEU A  93     -14.238 -18.130 -17.451  1.00 58.11           C  
ANISOU  402  CA  LEU A  93     5416  11379   5282    441    502    147       C  
ATOM    403  C   LEU A  93     -15.117 -19.283 -17.919  1.00 58.81           C  
ANISOU  403  C   LEU A  93     5420  11488   5436    445    521    142       C  
ATOM    404  O   LEU A  93     -15.199 -20.319 -17.248  1.00 58.14           O  
ANISOU  404  O   LEU A  93     5266  11416   5410    438    543    197       O  
ATOM    405  CB  LEU A  93     -15.072 -17.092 -16.701  1.00 61.51           C  
ANISOU  405  CB  LEU A  93     5881  11816   5674    466    497    159       C  
ATOM    406  CG  LEU A  93     -14.353 -15.880 -16.106  1.00 57.49           C  
ANISOU  406  CG  LEU A  93     5438  11304   5101    473    472    154       C  
ATOM    407  CD1 LEU A  93     -15.362 -14.844 -15.638  1.00 60.38           C  
ANISOU  407  CD1 LEU A  93     5827  11695   5419    525    461    132       C  
ATOM    408  CD2 LEU A  93     -13.454 -16.305 -14.958  1.00 52.65           C  
ANISOU  408  CD2 LEU A  93     4822  10693   4489    467    480    199       C  
ATOM    409  N   VAL A  94     -15.777 -19.133 -19.070  1.00 59.13           N  
ANISOU  409  N   VAL A  94     5449  11543   5475    455    510     84       N  
ATOM    410  CA  VAL A  94     -16.678 -20.187 -19.531  1.00 64.06           C  
ANISOU  410  CA  VAL A  94     6000  12145   6195    454    493     71       C  
ATOM    411  C   VAL A  94     -15.891 -21.381 -20.060  1.00 67.84           C  
ANISOU  411  C   VAL A  94     6455  12570   6749    457    455     30       C  
ATOM    412  O   VAL A  94     -16.156 -22.531 -19.691  1.00 64.86           O  
ANISOU  412  O   VAL A  94     6027  12127   6490    442    424     64       O  
ATOM    413  CB  VAL A  94     -17.651 -19.642 -20.591  1.00 62.76           C  
ANISOU  413  CB  VAL A  94     5845  11986   6015    468    468     13       C  
ATOM    414  CG1 VAL A  94     -18.353 -20.790 -21.301  1.00 68.45           C  
ANISOU  414  CG1 VAL A  94     6511  12645   6854    463    414    -23       C  
ATOM    415  CG2 VAL A  94     -18.672 -18.726 -19.946  1.00 48.14           C  
ANISOU  415  CG2 VAL A  94     3995  10175   4121    480    494     53       C  
ATOM    416  N   ASN A  95     -14.909 -21.131 -20.928  1.00 76.47           N  
ANISOU  416  N   ASN A  95     7580  13697   7778    479    447    -39       N  
ATOM    417  CA  ASN A  95     -14.275 -22.230 -21.653  1.00 76.82           C  
ANISOU  417  CA  ASN A  95     7598  13710   7882    511    400   -114       C  
ATOM    418  C   ASN A  95     -13.225 -22.951 -20.813  1.00 74.65           C  
ANISOU  418  C   ASN A  95     7307  13411   7647    513    405    -76       C  
ATOM    419  O   ASN A  95     -13.122 -24.181 -20.876  1.00 80.11           O  
ANISOU  419  O   ASN A  95     7963  14024   8452    534    347   -105       O  
ATOM    420  CB  ASN A  95     -13.657 -21.712 -22.951  1.00 75.16           C  
ANISOU  420  CB  ASN A  95     7408  13584   7566    547    396   -199       C  
ATOM    421  CG  ASN A  95     -14.572 -21.902 -24.145  1.00 72.13           C  
ANISOU  421  CG  ASN A  95     7014  13193   7201    575    346   -285       C  
ATOM    422  OD1 ASN A  95     -15.292 -20.985 -24.543  1.00 61.64           O  
ANISOU  422  OD1 ASN A  95     5708  11898   5814    560    356   -275       O  
ATOM    423  ND2 ASN A  95     -14.554 -23.099 -24.721  1.00 78.65           N  
ANISOU  423  ND2 ASN A  95     7806  13966   8112    622    278   -376       N  
ATOM    424  N   GLU A  96     -12.434 -22.217 -20.032  1.00 71.93           N  
ANISOU  424  N   GLU A  96     6988  13124   7218    494    457    -15       N  
ATOM    425  CA  GLU A  96     -11.382 -22.845 -19.239  1.00 68.63           C  
ANISOU  425  CA  GLU A  96     6554  12695   6829    499    459     23       C  
ATOM    426  C   GLU A  96     -11.845 -23.199 -17.830  1.00 61.85           C  
ANISOU  426  C   GLU A  96     5676  11793   6031    464    473    134       C  
ATOM    427  O   GLU A  96     -11.633 -24.326 -17.370  1.00 71.78           O  
ANISOU  427  O   GLU A  96     6897  12984   7393    465    437    169       O  
ATOM    428  CB  GLU A  96     -10.153 -21.932 -19.175  1.00 67.12           C  
ANISOU  428  CB  GLU A  96     6390  12597   6516    494    497     32       C  
ATOM    429  CG  GLU A  96      -9.265 -21.995 -20.407  1.00 66.11           C  
ANISOU  429  CG  GLU A  96     6246  12540   6335    535    484    -53       C  
ATOM    430  CD  GLU A  96      -8.672 -23.374 -20.627  1.00 79.30           C  
ANISOU  430  CD  GLU A  96     7869  14173   8089    596    441   -116       C  
ATOM    431  OE1 GLU A  96      -8.999 -24.012 -21.650  1.00 85.22           O  
ANISOU  431  OE1 GLU A  96     8599  14906   8875    650    394   -217       O  
ATOM    432  OE2 GLU A  96      -7.878 -23.822 -19.773  1.00 85.66           O  
ANISOU  432  OE2 GLU A  96     8660  14962   8925    598    443    -71       O  
ATOM    433  N   LEU A  97     -12.477 -22.257 -17.134  1.00 51.18           N  
ANISOU  433  N   LEU A  97     4346  10487   4612    440    516    193       N  
ATOM    434  CA  LEU A  97     -12.830 -22.432 -15.733  1.00 59.78           C  
ANISOU  434  CA  LEU A  97     5410  11588   5716    420    541    303       C  
ATOM    435  C   LEU A  97     -14.233 -22.997 -15.533  1.00 67.38           C  
ANISOU  435  C   LEU A  97     6316  12520   6765    399    530    361       C  
ATOM    436  O   LEU A  97     -14.750 -22.955 -14.412  1.00 70.39           O  
ANISOU  436  O   LEU A  97     6663  12953   7129    385    562    462       O  
ATOM    437  CB  LEU A  97     -12.679 -21.101 -14.995  1.00 65.20           C  
ANISOU  437  CB  LEU A  97     6174  12307   6293    421    559    320       C  
ATOM    438  CG  LEU A  97     -11.254 -20.548 -15.082  1.00 69.20           C  
ANISOU  438  CG  LEU A  97     6742  12801   6749    420    538    287       C  
ATOM    439  CD1 LEU A  97     -11.173 -19.132 -14.548  1.00 67.12           C  
ANISOU  439  CD1 LEU A  97     6559  12527   6418    418    517    283       C  
ATOM    440  CD2 LEU A  97     -10.288 -21.458 -14.339  1.00 70.12           C  
ANISOU  440  CD2 LEU A  97     6814  12938   6890    420    549    339       C  
ATOM    441  N   GLY A  98     -14.855 -23.519 -16.586  1.00 67.02           N  
ANISOU  441  N   GLY A  98     6251  12407   6806    397    481    302       N  
ATOM    442  CA  GLY A  98     -16.109 -24.245 -16.444  1.00 65.36           C  
ANISOU  442  CA  GLY A  98     5973  12153   6709    363    450    368       C  
ATOM    443  C   GLY A  98     -17.273 -23.426 -15.929  1.00 66.15           C  
ANISOU  443  C   GLY A  98     6049  12343   6741    357    502    425       C  
ATOM    444  O   GLY A  98     -18.081 -23.931 -15.139  1.00 62.26           O  
ANISOU  444  O   GLY A  98     5479  11873   6304    323    507    545       O  
ATOM    445  N   TYR A  99     -17.379 -22.172 -16.355  1.00 69.87           N  
ANISOU  445  N   TYR A  99     6579  12875   7095    393    534    349       N  
ATOM    446  CA  TYR A  99     -18.516 -21.351 -15.975  1.00 66.77           C  
ANISOU  446  CA  TYR A  99     6166  12566   6639    410    571    376       C  
ATOM    447  C   TYR A  99     -19.701 -21.630 -16.899  1.00 68.34           C  
ANISOU  447  C   TYR A  99     6322  12727   6918    397    532    349       C  
ATOM    448  O   TYR A  99     -19.598 -22.356 -17.891  1.00 58.22           O  
ANISOU  448  O   TYR A  99     5040  11352   5730    380    471    291       O  
ATOM    449  CB  TYR A  99     -18.152 -19.867 -16.019  1.00 58.91           C  
ANISOU  449  CB  TYR A  99     5290  11569   5522    452    569    303       C  
ATOM    450  CG  TYR A  99     -17.534 -19.333 -14.746  1.00 55.90           C  
ANISOU  450  CG  TYR A  99     4968  11193   5080    469    572    342       C  
ATOM    451  CD1 TYR A  99     -16.350 -19.861 -14.250  1.00 64.67           C  
ANISOU  451  CD1 TYR A  99     6086  12289   6198    450    576    374       C  
ATOM    452  CD2 TYR A  99     -18.139 -18.303 -14.038  1.00 55.65           C  
ANISOU  452  CD2 TYR A  99     4971  11192   4981    517    567    336       C  
ATOM    453  CE1 TYR A  99     -15.781 -19.372 -13.087  1.00 65.50           C  
ANISOU  453  CE1 TYR A  99     6235  12407   6246    469    573    404       C  
ATOM    454  CE2 TYR A  99     -17.579 -17.810 -12.872  1.00 61.17           C  
ANISOU  454  CE2 TYR A  99     5710  11912   5622    546    562    353       C  
ATOM    455  CZ  TYR A  99     -16.401 -18.349 -12.401  1.00 59.71           C  
ANISOU  455  CZ  TYR A  99     5533  11707   5445    518    564    389       C  
ATOM    456  OH  TYR A  99     -15.839 -17.863 -11.242  1.00 57.73           O  
ANISOU  456  OH  TYR A  99     5314  11486   5134    549    555    402       O  
ATOM    457  N   ARG A 100     -20.842 -21.044 -16.555  1.00 74.08           N  
ANISOU  457  N   ARG A 100     7008  13535   7602    415    561    382       N  
ATOM    458  CA  ARG A 100     -22.026 -21.058 -17.399  1.00 77.73           C  
ANISOU  458  CA  ARG A 100     7431  13983   8120    410    527    352       C  
ATOM    459  C   ARG A 100     -22.214 -19.667 -17.988  1.00 75.06           C  
ANISOU  459  C   ARG A 100     7167  13683   7667    469    537    254       C  
ATOM    460  O   ARG A 100     -21.818 -18.668 -17.381  1.00 84.36           O  
ANISOU  460  O   ARG A 100     8427  14879   8746    510    553    240       O  
ATOM    461  CB  ARG A 100     -23.264 -21.477 -16.602  1.00 78.32           C  
ANISOU  461  CB  ARG A 100     7383  14135   8240    386    547    477       C  
ATOM    462  CG  ARG A 100     -22.952 -22.440 -15.470  1.00 74.56           C  
ANISOU  462  CG  ARG A 100     6836  13675   7818    336    562    620       C  
ATOM    463  CD  ARG A 100     -24.201 -22.857 -14.717  1.00 76.23           C  
ANISOU  463  CD  ARG A 100     6905  13991   8069    302    583    772       C  
ATOM    464  NE  ARG A 100     -23.887 -23.287 -13.357  1.00 83.88           N  
ANISOU  464  NE  ARG A 100     7854  15002   9016    279    610    914       N  
ATOM    465  CZ  ARG A 100     -23.828 -24.556 -12.966  1.00 80.33           C  
ANISOU  465  CZ  ARG A 100     7282  14543   8696    193    586   1066       C  
ATOM    466  NH1 ARG A 100     -24.058 -25.534 -13.833  1.00 80.98           N  
ANISOU  466  NH1 ARG A 100     7343  14461   8965    121    485   1065       N  
ATOM    467  NH2 ARG A 100     -23.534 -24.849 -11.707  1.00 68.16           N  
ANISOU  467  NH2 ARG A 100     5729  13056   7113    179    613   1201       N  
ATOM    468  N   TRP A 101     -22.819 -19.596 -19.178  1.00 54.16           N  
ANISOU  468  N   TRP A 101     4525  10995   5058    470    490    184       N  
ATOM    469  CA  TRP A 101     -22.798 -18.308 -19.863  1.00 53.42           C  
ANISOU  469  CA  TRP A 101     4514  10920   4864    519    484     99       C  
ATOM    470  C   TRP A 101     -23.755 -17.283 -19.260  1.00 58.73           C  
ANISOU  470  C   TRP A 101     5172  11680   5464    577    511    112       C  
ATOM    471  O   TRP A 101     -23.842 -16.171 -19.794  1.00 68.63           O  
ANISOU  471  O   TRP A 101     6493  12933   6649    620    489     46       O  
ATOM    472  CB  TRP A 101     -23.091 -18.465 -21.361  1.00 72.67           C  
ANISOU  472  CB  TRP A 101     6966  13303   7343    511    423     19       C  
ATOM    473  CG  TRP A 101     -24.337 -19.212 -21.745  1.00 89.58           C  
ANISOU  473  CG  TRP A 101     9019  15427   9591    490    383     32       C  
ATOM    474  CD1 TRP A 101     -25.583 -18.683 -21.913  1.00 93.88           C  
ANISOU  474  CD1 TRP A 101     9523  16018  10128    514    376     33       C  
ATOM    475  CD2 TRP A 101     -24.440 -20.596 -22.110  1.00 95.77           C  
ANISOU  475  CD2 TRP A 101     9745  16131  10513    440    326     37       C  
ATOM    476  NE1 TRP A 101     -26.466 -19.658 -22.307  1.00 93.65           N  
ANISOU  476  NE1 TRP A 101     9406  15953  10223    473    325     51       N  
ATOM    477  CE2 TRP A 101     -25.789 -20.841 -22.440  1.00 90.99           C  
ANISOU  477  CE2 TRP A 101     9061  15528   9983    425    286     52       C  
ATOM    478  CE3 TRP A 101     -23.530 -21.655 -22.167  1.00 98.65           C  
ANISOU  478  CE3 TRP A 101    10114  16417  10953    413    292     27       C  
ATOM    479  CZ2 TRP A 101     -26.249 -22.100 -22.821  1.00 83.68           C  
ANISOU  479  CZ2 TRP A 101     8064  14516   9214    372    204     62       C  
ATOM    480  CZ3 TRP A 101     -23.990 -22.907 -22.546  1.00 90.40           C  
ANISOU  480  CZ3 TRP A 101     9005  15279  10063    373    207     26       C  
ATOM    481  CH2 TRP A 101     -25.336 -23.117 -22.868  1.00 78.29           C  
ANISOU  481  CH2 TRP A 101     7397  13738   8612    347    159     45       C  
ATOM    482  N   ASP A 102     -24.454 -17.605 -18.171  1.00 71.97           N  
ANISOU  482  N   ASP A 102     6783  13401   7160    580    535    196       N  
ATOM    483  CA  ASP A 102     -25.317 -16.645 -17.489  1.00 80.61           C  
ANISOU  483  CA  ASP A 102     7887  14555   8186    652    538    195       C  
ATOM    484  C   ASP A 102     -24.642 -15.978 -16.297  1.00 91.06           C  
ANISOU  484  C   ASP A 102     9284  15885   9428    698    544    199       C  
ATOM    485  O   ASP A 102     -24.808 -14.771 -16.096  1.00 99.78           O  
ANISOU  485  O   ASP A 102    10442  17015  10454    780    525    133       O  
ATOM    486  CB  ASP A 102     -26.614 -17.319 -17.026  1.00 76.98           C  
ANISOU  486  CB  ASP A 102     7302  14168   7780    638    554    287       C  
ATOM    487  CG  ASP A 102     -26.380 -18.687 -16.418  1.00 83.46           C  
ANISOU  487  CG  ASP A 102     8040  14984   8686    555    574    410       C  
ATOM    488  OD1 ASP A 102     -25.719 -19.520 -17.071  1.00 85.53           O  
ANISOU  488  OD1 ASP A 102     8281  15186   9031    493    560    403       O  
ATOM    489  OD2 ASP A 102     -26.855 -18.929 -15.288  1.00 90.98           O  
ANISOU  489  OD2 ASP A 102     8940  16006   9623    557    597    513       O  
ATOM    490  N   GLU A 103     -23.884 -16.733 -15.497  1.00 91.15           N  
ANISOU  490  N   GLU A 103     9291  15880   9460    655    563    269       N  
ATOM    491  CA  GLU A 103     -23.164 -16.132 -14.378  1.00 92.61           C  
ANISOU  491  CA  GLU A 103     9539  16076   9572    700    561    265       C  
ATOM    492  C   GLU A 103     -21.985 -15.300 -14.865  1.00 87.11           C  
ANISOU  492  C   GLU A 103     8952  15309   8839    706    531    179       C  
ATOM    493  O   GLU A 103     -21.708 -14.220 -14.325  1.00 96.18           O  
ANISOU  493  O   GLU A 103    10158  16473   9912    772    509    126       O  
ATOM    494  CB  GLU A 103     -22.663 -17.216 -13.423  1.00101.32           C  
ANISOU  494  CB  GLU A 103    10600  17189  10708    649    587    374       C  
ATOM    495  CG  GLU A 103     -23.516 -18.469 -13.356  1.00107.47           C  
ANISOU  495  CG  GLU A 103    11255  18011  11570    588    613    492       C  
ATOM    496  CD  GLU A 103     -22.742 -19.654 -12.805  1.00102.98           C  
ANISOU  496  CD  GLU A 103    10645  17424  11059    518    629    597       C  
ATOM    497  OE1 GLU A 103     -21.523 -19.511 -12.576  1.00 96.54           O  
ANISOU  497  OE1 GLU A 103     9904  16562  10214    521    623    564       O  
ATOM    498  OE2 GLU A 103     -23.348 -20.724 -12.596  1.00102.49           O  
ANISOU  498  OE2 GLU A 103    10466  17398  11077    457    641    721       O  
ATOM    499  N   VAL A 104     -21.302 -15.781 -15.905  1.00 81.14           N  
ANISOU  499  N   VAL A 104     8212  14487   8129    642    526    164       N  
ATOM    500  CA  VAL A 104     -19.985 -15.316 -16.334  1.00 71.89           C  
ANISOU  500  CA  VAL A 104     7124  13258   6932    620    503    121       C  
ATOM    501  C   VAL A 104     -19.909 -13.798 -16.459  1.00 69.27           C  
ANISOU  501  C   VAL A 104     6867  12933   6521    674    467     53       C  
ATOM    502  O   VAL A 104     -18.822 -13.214 -16.378  1.00 72.03           O  
ANISOU  502  O   VAL A 104     7280  13255   6832    662    445     37       O  
ATOM    503  CB  VAL A 104     -19.593 -15.992 -17.662  1.00 69.46           C  
ANISOU  503  CB  VAL A 104     6805  12914   6672    565    500    101       C  
ATOM    504  CG1 VAL A 104     -20.429 -15.451 -18.815  1.00 80.27           C  
ANISOU  504  CG1 VAL A 104     8171  14303   8027    584    482     47       C  
ATOM    505  CG2 VAL A 104     -18.116 -15.814 -17.934  1.00 70.56           C  
ANISOU  505  CG2 VAL A 104     7006  13012   6791    533    483     86       C  
ATOM    506  N   HIS A 105     -21.055 -13.143 -16.645  1.00 74.82           N  
ANISOU  506  N   HIS A 105     7553  13681   7193    736    458     16       N  
ATOM    507  CA  HIS A 105     -21.048 -11.692 -16.790  1.00 80.27           C  
ANISOU  507  CA  HIS A 105     8313  14387   7798    800    416    -54       C  
ATOM    508  C   HIS A 105     -20.727 -11.010 -15.465  1.00 92.37           C  
ANISOU  508  C   HIS A 105     9880  15949   9265    871    399    -79       C  
ATOM    509  O   HIS A 105     -19.743 -10.265 -15.360  1.00 96.23           O  
ANISOU  509  O   HIS A 105    10448  16415   9701    866    359   -106       O  
ATOM    510  CB  HIS A 105     -22.390 -11.207 -17.339  1.00 75.72           C  
ANISOU  510  CB  HIS A 105     7706  13862   7203    865    406    -96       C  
ATOM    511  CG  HIS A 105     -22.340  -9.823 -17.907  1.00 83.23           C  
ANISOU  511  CG  HIS A 105     8754  14749   8122    902    317   -158       C  
ATOM    512  ND1 HIS A 105     -22.458  -9.568 -19.256  1.00 86.59           N  
ANISOU  512  ND1 HIS A 105     9210  15109   8583    859    270   -160       N  
ATOM    513  CD2 HIS A 105     -22.174  -8.619 -17.309  1.00 85.61           C  
ANISOU  513  CD2 HIS A 105     9133  15021   8374    977    245   -214       C  
ATOM    514  CE1 HIS A 105     -22.372  -8.266 -19.465  1.00 89.91           C  
ANISOU  514  CE1 HIS A 105     9719  15459   8983    894    175   -197       C  
ATOM    515  NE2 HIS A 105     -22.199  -7.668 -18.300  1.00 88.26           N  
ANISOU  515  NE2 HIS A 105     9545  15259   8733    967    150   -237       N  
ATOM    516  N   ASP A 106     -21.533 -11.278 -14.429  1.00102.49           N  
ANISOU  516  N   ASP A 106    11102  17296  10543    934    423    -65       N  
ATOM    517  CA  ASP A 106     -21.417 -10.518 -13.184  1.00109.24           C  
ANISOU  517  CA  ASP A 106    11984  18207  11317   1034    399   -114       C  
ATOM    518  C   ASP A 106     -20.023 -10.626 -12.582  1.00 85.72           C  
ANISOU  518  C   ASP A 106     9054  15188   8328    988    391    -94       C  
ATOM    519  O   ASP A 106     -19.591  -9.728 -11.849  1.00 84.54           O  
ANISOU  519  O   ASP A 106     8962  15063   8098   1061    346   -162       O  
ATOM    520  CB  ASP A 106     -22.471 -10.979 -12.174  1.00130.97           C  
ANISOU  520  CB  ASP A 106    14645  21057  14061   1099    431    -78       C  
ATOM    521  CG  ASP A 106     -22.481 -12.483 -11.978  1.00143.67           C  
ANISOU  521  CG  ASP A 106    16179  22658  15749    997    483     50       C  
ATOM    522  OD1 ASP A 106     -21.472 -13.030 -11.484  1.00149.58           O  
ANISOU  522  OD1 ASP A 106    16945  23373  16515    941    492     98       O  
ATOM    523  OD2 ASP A 106     -23.503 -13.118 -12.312  1.00145.75           O  
ANISOU  523  OD2 ASP A 106    16367  22956  16057    975    508    103       O  
ATOM    524  N   GLU A 107     -19.306 -11.709 -12.879  1.00 72.85           N  
ANISOU  524  N   GLU A 107     7404  13501   6775    876    423    -13       N  
ATOM    525  CA  GLU A 107     -17.908 -11.813 -12.479  1.00 78.11           C  
ANISOU  525  CA  GLU A 107     8113  14130   7436    827    413      6       C  
ATOM    526  C   GLU A 107     -17.054 -10.800 -13.235  1.00 81.89           C  
ANISOU  526  C   GLU A 107     8677  14567   7870    802    360    -43       C  
ATOM    527  O   GLU A 107     -16.486  -9.874 -12.640  1.00 86.30           O  
ANISOU  527  O   GLU A 107     9301  15141   8349    844    306    -93       O  
ATOM    528  CB  GLU A 107     -17.408 -13.238 -12.725  1.00 72.75           C  
ANISOU  528  CB  GLU A 107     7389  13406   6848    729    454     95       C  
ATOM    529  CG  GLU A 107     -16.154 -13.612 -11.960  1.00 65.94           C  
ANISOU  529  CG  GLU A 107     6542  12531   5983    696    454    132       C  
ATOM    530  CD  GLU A 107     -16.453 -14.414 -10.711  1.00 68.42           C  
ANISOU  530  CD  GLU A 107     6797  12901   6299    719    484    200       C  
ATOM    531  OE1 GLU A 107     -16.852 -13.808  -9.695  1.00 75.40           O  
ANISOU  531  OE1 GLU A 107     7679  13859   7111    802    473    174       O  
ATOM    532  OE2 GLU A 107     -16.293 -15.652 -10.746  1.00 66.66           O  
ANISOU  532  OE2 GLU A 107     6526  12661   6140    659    513    280       O  
ATOM    533  N   ALA A 108     -16.993 -10.936 -14.563  1.00 73.00           N  
ANISOU  533  N   ALA A 108     7555  13399   6781    735    361    -28       N  
ATOM    534  CA  ALA A 108     -16.079 -10.143 -15.379  1.00 58.95           C  
ANISOU  534  CA  ALA A 108     5845  11586   4967    681    305    -34       C  
ATOM    535  C   ALA A 108     -16.308  -8.643 -15.253  1.00 71.18           C  
ANISOU  535  C   ALA A 108     7483  13070   6493    737    192    -97       C  
ATOM    536  O   ALA A 108     -15.459  -7.866 -15.706  1.00 78.99           O  
ANISOU  536  O   ALA A 108     8538  13976   7499    677    107    -81       O  
ATOM    537  CB  ALA A 108     -16.197 -10.558 -16.847  1.00 49.08           C  
ANISOU  537  CB  ALA A 108     4572  10310   3767    615    319     -6       C  
ATOM    538  N   GLU A 109     -17.418  -8.216 -14.650  1.00 78.30           N  
ANISOU  538  N   GLU A 109     8382  14011   7360    851    181   -164       N  
ATOM    539  CA  GLU A 109     -17.671  -6.794 -14.468  1.00 86.38           C  
ANISOU  539  CA  GLU A 109     9492  14959   8367    928     54   -246       C  
ATOM    540  C   GLU A 109     -16.784  -6.163 -13.403  1.00 85.42           C  
ANISOU  540  C   GLU A 109     9435  14810   8209    958    -24   -288       C  
ATOM    541  O   GLU A 109     -16.783  -4.933 -13.280  1.00 87.17           O  
ANISOU  541  O   GLU A 109     9746  14937   8439   1010   -162   -360       O  
ATOM    542  CB  GLU A 109     -19.143  -6.563 -14.118  1.00102.84           C  
ANISOU  542  CB  GLU A 109    11543  17117  10416   1065     65   -321       C  
ATOM    543  CG  GLU A 109     -20.086  -6.642 -15.311  1.00118.76           C  
ANISOU  543  CG  GLU A 109    13530  19114  12480   1049     77   -305       C  
ATOM    544  CD  GLU A 109     -20.143  -5.350 -16.107  1.00128.04           C  
ANISOU  544  CD  GLU A 109    14802  20152  13695   1054    -63   -341       C  
ATOM    545  OE1 GLU A 109     -19.377  -4.415 -15.792  1.00131.16           O  
ANISOU  545  OE1 GLU A 109    15288  20449  14096   1053   -179   -368       O  
ATOM    546  OE2 GLU A 109     -20.958  -5.270 -17.051  1.00126.82           O  
ANISOU  546  OE2 GLU A 109    14631  19983  13572   1055    -70   -335       O  
ATOM    547  N   VAL A 110     -16.036  -6.954 -12.634  1.00 82.79           N  
ANISOU  547  N   VAL A 110     9064  14548   7845    928     46   -248       N  
ATOM    548  CA  VAL A 110     -15.121  -6.421 -11.636  1.00 86.59           C  
ANISOU  548  CA  VAL A 110     9602  15009   8290    950    -31   -286       C  
ATOM    549  C   VAL A 110     -13.666  -6.728 -11.978  1.00 89.66           C  
ANISOU  549  C   VAL A 110    10000  15345   8723    808    -37   -198       C  
ATOM    550  O   VAL A 110     -12.794  -5.873 -11.801  1.00 92.99           O  
ANISOU  550  O   VAL A 110    10494  15675   9163    775   -157   -211       O  
ATOM    551  CB  VAL A 110     -15.481  -6.923 -10.217  1.00 92.38           C  
ANISOU  551  CB  VAL A 110    10281  15895   8924   1062     38   -324       C  
ATOM    552  CG1 VAL A 110     -15.306  -8.430 -10.092  1.00 88.48           C  
ANISOU  552  CG1 VAL A 110     9684  15488   8449    991    183   -214       C  
ATOM    553  CG2 VAL A 110     -14.655  -6.192  -9.167  1.00102.48           C  
ANISOU  553  CG2 VAL A 110    11631  17152  10154   1111    -67   -394       C  
ATOM    554  N   LEU A 111     -13.385  -7.928 -12.499  1.00 83.70           N  
ANISOU  554  N   LEU A 111     9168  14642   7992    726     80   -109       N  
ATOM    555  CA  LEU A 111     -12.014  -8.272 -12.866  1.00 72.41           C  
ANISOU  555  CA  LEU A 111     7730  13187   6594    607     82    -31       C  
ATOM    556  C   LEU A 111     -11.475  -7.356 -13.955  1.00 66.77           C  
ANISOU  556  C   LEU A 111     7068  12369   5931    519    -17      4       C  
ATOM    557  O   LEU A 111     -10.257  -7.172 -14.062  1.00 74.92           O  
ANISOU  557  O   LEU A 111     8109  13376   6982    430    -61     62       O  
ATOM    558  CB  LEU A 111     -11.931  -9.731 -13.318  1.00 65.65           C  
ANISOU  558  CB  LEU A 111     6783  12402   5759    559    211     37       C  
ATOM    559  CG  LEU A 111     -12.136 -10.822 -12.266  1.00 66.11           C  
ANISOU  559  CG  LEU A 111     6778  12511   5830    601    291     52       C  
ATOM    560  CD1 LEU A 111     -13.605 -11.132 -12.069  1.00 76.60           C  
ANISOU  560  CD1 LEU A 111     8068  13855   7181    675    330     30       C  
ATOM    561  CD2 LEU A 111     -11.378 -12.072 -12.670  1.00 55.79           C  
ANISOU  561  CD2 LEU A 111     5414  11173   4611    523    342    123       C  
ATOM    562  N   GLU A 112     -12.361  -6.773 -14.765  1.00 62.14           N  
ANISOU  562  N   GLU A 112     6509  11734   5368    538    -56    -17       N  
ATOM    563  CA  GLU A 112     -11.935  -5.812 -15.776  1.00 83.45           C  
ANISOU  563  CA  GLU A 112     9256  14339   8114    453   -164     35       C  
ATOM    564  C   GLU A 112     -11.192  -4.630 -15.170  1.00 97.75           C  
ANISOU  564  C   GLU A 112    11149  16043   9948    434   -323     24       C  
ATOM    565  O   GLU A 112     -10.402  -3.985 -15.868  1.00109.52           O  
ANISOU  565  O   GLU A 112    12660  17466  11485    322   -414    111       O  
ATOM    566  CB  GLU A 112     -13.147  -5.317 -16.562  1.00 92.75           C  
ANISOU  566  CB  GLU A 112    10456  15477   9309    498   -194      5       C  
ATOM    567  CG  GLU A 112     -14.259  -4.778 -15.681  1.00106.19           C  
ANISOU  567  CG  GLU A 112    12199  17158  10990    643   -239   -115       C  
ATOM    568  CD  GLU A 112     -15.525  -4.495 -16.456  1.00113.10           C  
ANISOU  568  CD  GLU A 112    13075  18018  11880    697   -247   -144       C  
ATOM    569  OE1 GLU A 112     -16.433  -3.841 -15.901  1.00113.08           O  
ANISOU  569  OE1 GLU A 112    13109  17992  11864    822   -308   -243       O  
ATOM    570  OE2 GLU A 112     -15.612  -4.919 -17.627  1.00113.64           O  
ANISOU  570  OE2 GLU A 112    13104  18107  11968    624   -197    -75       O  
ATOM    571  N   HIS A 113     -11.427  -4.330 -13.892  1.00 95.38           N  
ANISOU  571  N   HIS A 113    10891  15734   9616    540   -367    -78       N  
ATOM    572  CA  HIS A 113     -10.712  -3.271 -13.197  1.00100.68           C  
ANISOU  572  CA  HIS A 113    11643  16299  10313    536   -535   -113       C  
ATOM    573  C   HIS A 113      -9.596  -3.816 -12.315  1.00 96.07           C  
ANISOU  573  C   HIS A 113    11031  15774   9698    502   -502    -91       C  
ATOM    574  O   HIS A 113      -9.179  -3.149 -11.362  1.00104.20           O  
ANISOU  574  O   HIS A 113    12121  16748  10724    542   -623   -158       O  
ATOM    575  CB  HIS A 113     -11.688  -2.431 -12.377  1.00113.46           C  
ANISOU  575  CB  HIS A 113    13334  17866  11908    700   -636   -266       C  
ATOM    576  CG  HIS A 113     -12.900  -2.006 -13.145  1.00128.65           C  
ANISOU  576  CG  HIS A 113    15275  19749  13855    757   -655   -298       C  
ATOM    577  ND1 HIS A 113     -12.857  -1.038 -14.126  1.00132.63           N  
ANISOU  577  ND1 HIS A 113    15837  20108  14446    685   -792   -247       N  
ATOM    578  CD2 HIS A 113     -14.186  -2.423 -13.085  1.00133.62           C  
ANISOU  578  CD2 HIS A 113    15864  20471  14434    875   -559   -364       C  
ATOM    579  CE1 HIS A 113     -14.065  -0.876 -14.635  1.00134.63           C  
ANISOU  579  CE1 HIS A 113    16092  20361  14700    764   -779   -291       C  
ATOM    580  NE2 HIS A 113     -14.891  -1.704 -14.020  1.00133.14           N  
ANISOU  580  NE2 HIS A 113    15841  20318  14429    880   -637   -365       N  
ATOM    581  N   ALA A 114      -9.105  -5.023 -12.615  1.00 85.32           N  
ANISOU  581  N   ALA A 114     9579  14522   8317    435   -353     -6       N  
ATOM    582  CA  ALA A 114      -7.993  -5.578 -11.838  1.00 81.42           C  
ANISOU  582  CA  ALA A 114     9052  14086   7800    400   -324     24       C  
ATOM    583  C   ALA A 114      -7.168  -6.581 -12.635  1.00 93.07           C  
ANISOU  583  C   ALA A 114    10438  15637   9289    291   -213    140       C  
ATOM    584  O   ALA A 114      -6.450  -7.376 -12.019  1.00101.87           O  
ANISOU  584  O   ALA A 114    11504  16824  10378    283   -151    163       O  
ATOM    585  CB  ALA A 114      -8.517  -6.227 -10.553  1.00 66.85           C  
ANISOU  585  CB  ALA A 114     7188  12339   5873    527   -247    -56       C  
ATOM    586  N   VAL A 115      -7.235  -6.577 -13.964  1.00 90.96           N  
ANISOU  586  N   VAL A 115    10142  15364   9053    219   -192    209       N  
ATOM    587  CA  VAL A 115      -6.511  -7.520 -14.810  1.00 82.88           C  
ANISOU  587  CA  VAL A 115     9027  14433   8029    141    -91    297       C  
ATOM    588  C   VAL A 115      -5.537  -6.738 -15.681  1.00 87.99           C  
ANISOU  588  C   VAL A 115     9667  15059   8709     13   -179    406       C  
ATOM    589  O   VAL A 115      -5.933  -5.788 -16.366  1.00 94.76           O  
ANISOU  589  O   VAL A 115    10568  15842   9596    -21   -268    433       O  
ATOM    590  CB  VAL A 115      -7.474  -8.355 -15.676  1.00 75.46           C  
ANISOU  590  CB  VAL A 115     8042  13549   7081    180     21    282       C  
ATOM    591  CG1 VAL A 115      -6.743  -8.978 -16.854  1.00 74.20           C  
ANISOU  591  CG1 VAL A 115     7803  13474   6918    105     83    361       C  
ATOM    592  CG2 VAL A 115      -8.136  -9.435 -14.834  1.00 75.57           C  
ANISOU  592  CG2 VAL A 115     8026  13613   7073    273    123    221       C  
ATOM    593  N   SER A 116      -4.269  -7.139 -15.657  1.00 82.82           N  
ANISOU  593  N   SER A 116     8946  14474   8047    -59   -158    480       N  
ATOM    594  CA  SER A 116      -3.241  -6.448 -16.419  1.00 73.86           C  
ANISOU  594  CA  SER A 116     7777  13351   6936   -192   -236    608       C  
ATOM    595  C   SER A 116      -3.313  -6.823 -17.898  1.00 75.30           C  
ANISOU  595  C   SER A 116     7883  13639   7088   -230   -157    680       C  
ATOM    596  O   SER A 116      -3.895  -7.842 -18.284  1.00 76.40           O  
ANISOU  596  O   SER A 116     7984  13851   7192   -157    -35    623       O  
ATOM    597  CB  SER A 116      -1.856  -6.773 -15.862  1.00 74.46           C  
ANISOU  597  CB  SER A 116     7792  13490   7008   -248   -236    663       C  
ATOM    598  OG  SER A 116      -1.648  -8.174 -15.800  1.00 76.67           O  
ANISOU  598  OG  SER A 116     7995  13892   7245   -191    -88    635       O  
ATOM    599  N   ASP A 117      -2.705  -5.975 -18.734  1.00 81.15           N  
ANISOU  599  N   ASP A 117     8597  14392   7843   -349   -240    812       N  
ATOM    600  CA  ASP A 117      -2.676  -6.242 -20.170  1.00 82.98           C  
ANISOU  600  CA  ASP A 117     8746  14758   8024   -387   -172    894       C  
ATOM    601  C   ASP A 117      -1.841  -7.471 -20.500  1.00 77.59           C  
ANISOU  601  C   ASP A 117     7941  14264   7277   -369    -39    905       C  
ATOM    602  O   ASP A 117      -2.161  -8.196 -21.447  1.00 72.83           O  
ANISOU  602  O   ASP A 117     7280  13777   6616   -322     57    884       O  
ATOM    603  CB  ASP A 117      -2.142  -5.024 -20.922  1.00 91.46           C  
ANISOU  603  CB  ASP A 117     9805  15822   9124   -529   -298   1064       C  
ATOM    604  CG  ASP A 117      -2.819  -3.737 -20.499  1.00103.50           C  
ANISOU  604  CG  ASP A 117    11458  17132  10737   -547   -467   1051       C  
ATOM    605  OD1 ASP A 117      -2.503  -3.228 -19.402  1.00111.37           O  
ANISOU  605  OD1 ASP A 117    12519  18002  11795   -554   -573   1015       O  
ATOM    606  OD2 ASP A 117      -3.667  -3.233 -21.266  1.00107.84           O  
ANISOU  606  OD2 ASP A 117    12044  17637  11294   -544   -504   1069       O  
ATOM    607  N   ARG A 118      -0.770  -7.715 -19.742  1.00 74.54           N  
ANISOU  607  N   ARG A 118     7515  13910   6898   -397    -42    928       N  
ATOM    608  CA  ARG A 118      -0.013  -8.954 -19.897  1.00 73.83           C  
ANISOU  608  CA  ARG A 118     7314  13982   6755   -354     77    913       C  
ATOM    609  C   ARG A 118      -0.911 -10.163 -19.667  1.00 68.29           C  
ANISOU  609  C   ARG A 118     6637  13248   6064   -216    177    761       C  
ATOM    610  O   ARG A 118      -1.036 -11.042 -20.531  1.00 69.63           O  
ANISOU  610  O   ARG A 118     6753  13429   6274   -154    229    708       O  
ATOM    611  CB  ARG A 118       1.167  -8.967 -18.922  1.00 83.73           C  
ANISOU  611  CB  ARG A 118     8537  15244   8031   -397     42    951       C  
ATOM    612  CG  ARG A 118       1.806 -10.336 -18.735  1.00 92.41           C  
ANISOU  612  CG  ARG A 118     9548  16466   9097   -320    153    899       C  
ATOM    613  CD  ARG A 118       2.630 -10.415 -17.452  1.00 93.43           C  
ANISOU  613  CD  ARG A 118     9683  16558   9259   -333    115    899       C  
ATOM    614  NE  ARG A 118       3.937  -9.774 -17.572  1.00101.45           N  
ANISOU  614  NE  ARG A 118    10618  17657  10274   -453     48   1037       N  
ATOM    615  CZ  ARG A 118       4.261  -8.622 -16.994  1.00107.99           C  
ANISOU  615  CZ  ARG A 118    11497  18376  11156   -555    -90   1105       C  
ATOM    616  NH1 ARG A 118       5.477  -8.118 -17.155  1.00108.80           N  
ANISOU  616  NH1 ARG A 118    11508  18563  11266   -675   -154   1246       N  
ATOM    617  NH2 ARG A 118       3.373  -7.978 -16.250  1.00110.97           N  
ANISOU  617  NH2 ARG A 118    12013  18566  11583   -531   -174   1029       N  
ATOM    618  N   LEU A 119      -1.556 -10.212 -18.498  1.00 66.96           N  
ANISOU  618  N   LEU A 119     6556  12963   5924   -161    163    679       N  
ATOM    619  CA  LEU A 119      -2.476 -11.298 -18.178  1.00 58.00           C  
ANISOU  619  CA  LEU A 119     5441  11762   4834    -48    235    559       C  
ATOM    620  C   LEU A 119      -3.551 -11.443 -19.246  1.00 55.90           C  
ANISOU  620  C   LEU A 119     5185  11466   4589    -10    257    516       C  
ATOM    621  O   LEU A 119      -3.931 -12.563 -19.612  1.00 58.49           O  
ANISOU  621  O   LEU A 119     5489  11760   4975     60    301    445       O  
ATOM    622  CB  LEU A 119      -3.111 -11.045 -16.809  1.00 44.44           C  
ANISOU  622  CB  LEU A 119     3809   9964   3112     -4    210    504       C  
ATOM    623  CG  LEU A 119      -4.318 -11.888 -16.399  1.00 44.76           C  
ANISOU  623  CG  LEU A 119     3876   9932   3201     95    266    410       C  
ATOM    624  CD1 LEU A 119      -3.949 -13.352 -16.381  1.00 42.24           C  
ANISOU  624  CD1 LEU A 119     3497   9597   2957    138    319    385       C  
ATOM    625  CD2 LEU A 119      -4.841 -11.455 -15.036  1.00 47.62           C  
ANISOU  625  CD2 LEU A 119     4307  10254   3532    140    236    370       C  
ATOM    626  N   MET A 120      -4.045 -10.318 -19.766  1.00 54.42           N  
ANISOU  626  N   MET A 120     5039  11292   4345    -60    208    565       N  
ATOM    627  CA  MET A 120      -5.090 -10.376 -20.780  1.00 58.98           C  
ANISOU  627  CA  MET A 120     5626  11851   4934    -25    224    529       C  
ATOM    628  C   MET A 120      -4.560 -10.970 -22.078  1.00 72.71           C  
ANISOU  628  C   MET A 120     7276  13665   6686    -28    253    548       C  
ATOM    629  O   MET A 120      -5.274 -11.709 -22.767  1.00 68.79           O  
ANISOU  629  O   MET A 120     6770  13147   6219     39    282    471       O  
ATOM    630  CB  MET A 120      -5.661  -8.980 -21.026  1.00 58.02           C  
ANISOU  630  CB  MET A 120     5577  11678   4790    -76    131    581       C  
ATOM    631  CG  MET A 120      -7.125  -8.972 -21.425  1.00 70.02           C  
ANISOU  631  CG  MET A 120     7142  13142   6320     -9    140    508       C  
ATOM    632  SD  MET A 120      -8.131  -9.790 -20.171  1.00 74.57           S  
ANISOU  632  SD  MET A 120     7755  13644   6933    105    196    377       S  
ATOM    633  CE  MET A 120      -8.511 -11.346 -20.966  1.00 62.59           C  
ANISOU  633  CE  MET A 120     6165  12144   5473    162    285    314       C  
ATOM    634  N   ALA A 121      -3.308 -10.662 -22.425  1.00 79.09           N  
ANISOU  634  N   ALA A 121     8013  14574   7461   -102    236    648       N  
ATOM    635  CA  ALA A 121      -2.739 -11.188 -23.660  1.00 66.72           C  
ANISOU  635  CA  ALA A 121     6355  13109   5887    -88    254    661       C  
ATOM    636  C   ALA A 121      -2.414 -12.670 -23.539  1.00 52.40           C  
ANISOU  636  C   ALA A 121     4509  11281   4118     13    294    552       C  
ATOM    637  O   ALA A 121      -2.509 -13.405 -24.529  1.00 57.20           O  
ANISOU  637  O   ALA A 121     5078  11936   4717     79    307    494       O  
ATOM    638  CB  ALA A 121      -1.492 -10.394 -24.049  1.00 42.31           C  
ANISOU  638  CB  ALA A 121     3182  10151   2744   -199    220    817       C  
ATOM    639  N   ARG A 122      -2.035 -13.132 -22.345  1.00 40.38           N  
ANISOU  639  N   ARG A 122     3005   9703   2633     30    304    523       N  
ATOM    640  CA  ARG A 122      -1.803 -14.561 -22.165  1.00 53.21           C  
ANISOU  640  CA  ARG A 122     4611  11307   4297    124    332    430       C  
ATOM    641  C   ARG A 122      -3.111 -15.339 -22.073  1.00 61.16           C  
ANISOU  641  C   ARG A 122     5675  12211   5353    200    353    325       C  
ATOM    642  O   ARG A 122      -3.158 -16.514 -22.459  1.00 66.12           O  
ANISOU  642  O   ARG A 122     6278  12847   5996    279    369    244       O  
ATOM    643  CB  ARG A 122      -0.929 -14.797 -20.932  1.00 67.66           C  
ANISOU  643  CB  ARG A 122     6435  13126   6147    112    333    451       C  
ATOM    644  CG  ARG A 122       0.225 -13.811 -20.847  1.00 67.45           C  
ANISOU  644  CG  ARG A 122     6354  13199   6072     13    304    572       C  
ATOM    645  CD  ARG A 122       1.489 -14.401 -20.253  1.00 68.58           C  
ANISOU  645  CD  ARG A 122     6440  13398   6218     24    306    588       C  
ATOM    646  NE  ARG A 122       2.533 -13.384 -20.162  1.00 77.64           N  
ANISOU  646  NE  ARG A 122     7529  14652   7321    -88    272    719       N  
ATOM    647  CZ  ARG A 122       3.798 -13.627 -19.839  1.00 79.47           C  
ANISOU  647  CZ  ARG A 122     7686  14972   7539   -104    264    765       C  
ATOM    648  NH1 ARG A 122       4.194 -14.864 -19.571  1.00 82.08           N  
ANISOU  648  NH1 ARG A 122     8000  15294   7893     -5    289    684       N  
ATOM    649  NH2 ARG A 122       4.671 -12.630 -19.786  1.00 77.63           N  
ANISOU  649  NH2 ARG A 122     7390  14840   7264   -224    226    903       N  
ATOM    650  N   ILE A 123      -4.181 -14.705 -21.583  1.00 63.17           N  
ANISOU  650  N   ILE A 123     5997  12383   5621    180    350    325       N  
ATOM    651  CA  ILE A 123      -5.505 -15.317 -21.667  1.00 65.63           C  
ANISOU  651  CA  ILE A 123     6345  12620   5970    241    367    245       C  
ATOM    652  C   ILE A 123      -5.930 -15.442 -23.123  1.00 69.72           C  
ANISOU  652  C   ILE A 123     6838  13193   6461    266    362    210       C  
ATOM    653  O   ILE A 123      -6.366 -16.508 -23.576  1.00 74.61           O  
ANISOU  653  O   ILE A 123     7439  13810   7099    336    375    125       O  
ATOM    654  CB  ILE A 123      -6.531 -14.504 -20.857  1.00 63.33           C  
ANISOU  654  CB  ILE A 123     6122  12256   5684    223    362    255       C  
ATOM    655  CG1 ILE A 123      -6.334 -14.724 -19.358  1.00 63.25           C  
ANISOU  655  CG1 ILE A 123     6134  12198   5700    231    371    261       C  
ATOM    656  CG2 ILE A 123      -7.947 -14.885 -21.264  1.00 60.56           C  
ANISOU  656  CG2 ILE A 123     5791  11860   5359    272    374    191       C  
ATOM    657  CD1 ILE A 123      -7.353 -14.012 -18.499  1.00 67.24           C  
ANISOU  657  CD1 ILE A 123     6699  12654   6196    241    364    254       C  
ATOM    658  N   ASP A 124      -5.808 -14.346 -23.879  1.00 66.12           N  
ANISOU  658  N   ASP A 124     6373  12798   5952    210    340    278       N  
ATOM    659  CA  ASP A 124      -6.148 -14.372 -25.297  1.00 64.30           C  
ANISOU  659  CA  ASP A 124     6109  12640   5681    232    333    258       C  
ATOM    660  C   ASP A 124      -5.301 -15.396 -26.044  1.00 70.21           C  
ANISOU  660  C   ASP A 124     6785  13484   6407    294    339    208       C  
ATOM    661  O   ASP A 124      -5.767 -15.998 -27.018  1.00 62.80           O  
ANISOU  661  O   ASP A 124     5823  12591   5446    361    337    131       O  
ATOM    662  CB  ASP A 124      -5.966 -12.970 -25.891  1.00 53.84           C  
ANISOU  662  CB  ASP A 124     4777  11385   4296    146    305    375       C  
ATOM    663  CG  ASP A 124      -6.588 -12.821 -27.270  1.00 64.67           C  
ANISOU  663  CG  ASP A 124     6126  12823   5622    166    295    366       C  
ATOM    664  OD1 ASP A 124      -7.118 -13.812 -27.810  1.00 70.12           O  
ANISOU  664  OD1 ASP A 124     6804  13514   6322    251    307    257       O  
ATOM    665  OD2 ASP A 124      -6.542 -11.700 -27.821  1.00 70.99           O  
ANISOU  665  OD2 ASP A 124     6918  13684   6371     93    269    474       O  
ATOM    666  N   ALA A 125      -4.068 -15.624 -25.586  1.00 75.09           N  
ANISOU  666  N   ALA A 125     7364  14146   7022    284    342    241       N  
ATOM    667  CA  ALA A 125      -3.210 -16.617 -26.222  1.00 68.06           C  
ANISOU  667  CA  ALA A 125     6401  13361   6099    360    344    184       C  
ATOM    668  C   ALA A 125      -3.677 -18.033 -25.905  1.00 64.32           C  
ANISOU  668  C   ALA A 125     5942  12826   5670    460    359     52       C  
ATOM    669  O   ALA A 125      -3.790 -18.873 -26.805  1.00 62.85           O  
ANISOU  669  O   ALA A 125     5717  12711   5453    551    354    -48       O  
ATOM    670  CB  ALA A 125      -1.759 -16.416 -25.785  1.00 66.33           C  
ANISOU  670  CB  ALA A 125     6128  13214   5860    320    341    264       C  
ATOM    671  N   LYS A 126      -3.947 -18.320 -24.629  1.00 71.02           N  
ANISOU  671  N   LYS A 126     6838  13560   6588    447    375     51       N  
ATOM    672  CA  LYS A 126      -4.456 -19.641 -24.269  1.00 67.91           C  
ANISOU  672  CA  LYS A 126     6444  13117   6242    529    390    -51       C  
ATOM    673  C   LYS A 126      -5.821 -19.911 -24.889  1.00 59.83           C  
ANISOU  673  C   LYS A 126     5437  12066   5229    564    388   -127       C  
ATOM    674  O   LYS A 126      -6.126 -21.049 -25.263  1.00 54.85           O  
ANISOU  674  O   LYS A 126     4769  11460   4609    653    389   -238       O  
ATOM    675  CB  LYS A 126      -4.525 -19.793 -22.751  1.00 58.40           C  
ANISOU  675  CB  LYS A 126     5274  11812   5102    497    409     -9       C  
ATOM    676  CG  LYS A 126      -4.880 -21.205 -22.321  1.00 52.53           C  
ANISOU  676  CG  LYS A 126     4502  11042   4415    573    427    -87       C  
ATOM    677  CD  LYS A 126      -4.021 -21.692 -21.177  1.00 66.93           C  
ANISOU  677  CD  LYS A 126     6306  12852   6271    575    440    -47       C  
ATOM    678  CE  LYS A 126      -2.937 -22.616 -21.710  1.00 87.73           C  
ANISOU  678  CE  LYS A 126     8865  15584   8883    665    432   -120       C  
ATOM    679  NZ  LYS A 126      -3.486 -23.953 -22.074  1.00 96.55           N  
ANISOU  679  NZ  LYS A 126     9920  16712  10051    774    432   -243       N  
ATOM    680  N   LEU A 127      -6.661 -18.887 -24.993  1.00 58.80           N  
ANISOU  680  N   LEU A 127     5355  11891   5096    503    383    -75       N  
ATOM    681  CA  LEU A 127      -8.006 -19.088 -25.515  1.00 63.88           C  
ANISOU  681  CA  LEU A 127     6012  12512   5749    532    381   -139       C  
ATOM    682  C   LEU A 127      -8.030 -19.396 -27.009  1.00 73.06           C  
ANISOU  682  C   LEU A 127     7129  13784   6847    597    358   -220       C  
ATOM    683  O   LEU A 127      -9.110 -19.653 -27.552  1.00 78.89           O  
ANISOU  683  O   LEU A 127     7869  14521   7585    631    350   -289       O  
ATOM    684  CB  LEU A 127      -8.855 -17.855 -25.215  1.00 56.02           C  
ANISOU  684  CB  LEU A 127     5075  11451   4758    460    378    -65       C  
ATOM    685  CG  LEU A 127      -9.491 -17.806 -23.828  1.00 44.20           C  
ANISOU  685  CG  LEU A 127     3619   9850   3323    435    397    -34       C  
ATOM    686  CD1 LEU A 127     -10.331 -16.550 -23.675  1.00 37.90           C  
ANISOU  686  CD1 LEU A 127     2874   9014   2512    391    387     16       C  
ATOM    687  CD2 LEU A 127     -10.336 -19.049 -23.592  1.00 38.25           C  
ANISOU  687  CD2 LEU A 127     2835   9073   2624    488    417   -104       C  
ATOM    688  N   GLY A 128      -6.881 -19.382 -27.679  1.00 72.62           N  
ANISOU  688  N   GLY A 128     7024  13838   6729    619    346   -213       N  
ATOM    689  CA  GLY A 128      -6.829 -19.623 -29.106  1.00 61.57           C  
ANISOU  689  CA  GLY A 128     5573  12569   5253    691    322   -286       C  
ATOM    690  C   GLY A 128      -7.084 -18.408 -29.965  1.00 59.97           C  
ANISOU  690  C   GLY A 128     5372  12421   4995    630    310   -199       C  
ATOM    691  O   GLY A 128      -7.455 -18.564 -31.135  1.00 64.08           O  
ANISOU  691  O   GLY A 128     5858  13035   5456    688    290   -261       O  
ATOM    692  N   PHE A 129      -6.888 -17.207 -29.428  1.00 59.51           N  
ANISOU  692  N   PHE A 129     5345  12318   4949    521    317    -60       N  
ATOM    693  CA  PHE A 129      -7.198 -15.961 -30.116  1.00 68.13           C  
ANISOU  693  CA  PHE A 129     6438  13454   5996    453    304     39       C  
ATOM    694  C   PHE A 129      -8.630 -15.971 -30.654  1.00 69.92           C  
ANISOU  694  C   PHE A 129     6698  13645   6222    484    294    -26       C  
ATOM    695  O   PHE A 129      -8.845 -15.909 -31.868  1.00 77.15           O  
ANISOU  695  O   PHE A 129     7574  14666   7072    519    277    -47       O  
ATOM    696  CB  PHE A 129      -6.199 -15.693 -31.236  1.00 74.38           C  
ANISOU  696  CB  PHE A 129     7139  14425   6697    458    293     94       C  
ATOM    697  CG  PHE A 129      -4.780 -15.588 -30.761  1.00 76.93           C  
ANISOU  697  CG  PHE A 129     7415  14804   7011    421    300    171       C  
ATOM    698  CD1 PHE A 129      -4.289 -14.394 -30.258  1.00 82.61           C  
ANISOU  698  CD1 PHE A 129     8139  15515   7735    299    296    326       C  
ATOM    699  CD2 PHE A 129      -3.938 -16.686 -30.808  1.00 74.77           C  
ANISOU  699  CD2 PHE A 129     7089  14601   6721    510    303     87       C  
ATOM    700  CE1 PHE A 129      -2.983 -14.297 -29.816  1.00 81.72           C  
ANISOU  700  CE1 PHE A 129     7974  15463   7611    260    297    400       C  
ATOM    701  CE2 PHE A 129      -2.631 -16.596 -30.368  1.00 74.93           C  
ANISOU  701  CE2 PHE A 129     7060  14681   6727    479    307    159       C  
ATOM    702  CZ  PHE A 129      -2.153 -15.399 -29.870  1.00 75.44           C  
ANISOU  702  CZ  PHE A 129     7126  14738   6800    351    304    318       C  
ATOM    703  N   PRO A 130      -9.634 -16.047 -29.770  1.00 74.62           N  
ANISOU  703  N   PRO A 130     7360  14108   6886    474    303    -55       N  
ATOM    704  CA  PRO A 130     -11.014 -16.224 -30.237  1.00 70.25           C  
ANISOU  704  CA  PRO A 130     6826  13532   6333    512    292   -129       C  
ATOM    705  C   PRO A 130     -11.575 -14.986 -30.912  1.00 67.10           C  
ANISOU  705  C   PRO A 130     6445  13162   5886    463    273    -48       C  
ATOM    706  O   PRO A 130     -10.935 -13.931 -30.960  1.00 77.35           O  
ANISOU  706  O   PRO A 130     7743  14494   7153    390    267     75       O  
ATOM    707  CB  PRO A 130     -11.789 -16.548 -28.950  1.00 71.99           C  
ANISOU  707  CB  PRO A 130     7094  13622   6637    505    312   -152       C  
ATOM    708  CG  PRO A 130     -10.752 -16.766 -27.892  1.00 75.37           C  
ANISOU  708  CG  PRO A 130     7525  14008   7103    480    332   -112       C  
ATOM    709  CD  PRO A 130      -9.570 -15.957 -28.305  1.00 81.05           C  
ANISOU  709  CD  PRO A 130     8221  14803   7769    432    322    -20       C  
ATOM    710  N   GLN A 131     -12.792 -15.122 -31.427  1.00 59.27           N  
ANISOU  710  N   GLN A 131     5466  12167   4887    502    258   -113       N  
ATOM    711  CA  GLN A 131     -13.466 -14.063 -32.154  1.00 64.93           C  
ANISOU  711  CA  GLN A 131     6200  12917   5554    470    234    -50       C  
ATOM    712  C   GLN A 131     -14.827 -13.715 -31.578  1.00 66.95           C  
ANISOU  712  C   GLN A 131     6513  13080   5846    467    228    -66       C  
ATOM    713  O   GLN A 131     -15.428 -12.727 -32.014  1.00 75.60           O  
ANISOU  713  O   GLN A 131     7636  14190   6900    441    200     -7       O  
ATOM    714  CB  GLN A 131     -13.639 -14.463 -33.629  1.00 84.07           C  
ANISOU  714  CB  GLN A 131     8569  15467   7906    534    211   -113       C  
ATOM    715  CG  GLN A 131     -14.533 -15.685 -33.839  1.00 96.74           C  
ANISOU  715  CG  GLN A 131    10163  17065   9528    626    200   -278       C  
ATOM    716  CD  GLN A 131     -13.851 -16.994 -33.470  1.00 91.27           C  
ANISOU  716  CD  GLN A 131     9437  16376   8866    688    211   -382       C  
ATOM    717  OE1 GLN A 131     -13.924 -17.443 -32.325  1.00 73.40           O  
ANISOU  717  OE1 GLN A 131     7197  14015   6677    675    235   -396       O  
ATOM    718  NE2 GLN A 131     -13.181 -17.609 -34.438  1.00 90.80           N  
ANISOU  718  NE2 GLN A 131     9316  16440   8744    764    193   -456       N  
ATOM    719  N   ARG A 132     -15.326 -14.485 -30.614  1.00 60.49           N  
ANISOU  719  N   ARG A 132     5706  12181   5097    494    250   -136       N  
ATOM    720  CA  ARG A 132     -16.687 -14.306 -30.133  1.00 51.75           C  
ANISOU  720  CA  ARG A 132     4627  11017   4018    505    249   -160       C  
ATOM    721  C   ARG A 132     -16.801 -14.838 -28.713  1.00 56.69           C  
ANISOU  721  C   ARG A 132     5259  11557   4726    504    287   -171       C  
ATOM    722  O   ARG A 132     -16.002 -15.667 -28.269  1.00 54.68           O  
ANISOU  722  O   ARG A 132     4981  11287   4507    509    309   -190       O  
ATOM    723  CB  ARG A 132     -17.690 -15.007 -31.054  1.00 55.99           C  
ANISOU  723  CB  ARG A 132     5129  11612   4534    565    228   -263       C  
ATOM    724  CG  ARG A 132     -17.334 -16.455 -31.347  1.00 57.88           C  
ANISOU  724  CG  ARG A 132     5313  11893   4787    623    234   -377       C  
ATOM    725  CD  ARG A 132     -18.491 -17.202 -31.983  1.00 60.69           C  
ANISOU  725  CD  ARG A 132     5644  12221   5194    674    181   -485       C  
ATOM    726  NE  ARG A 132     -18.303 -18.647 -31.905  1.00 65.16           N  
ANISOU  726  NE  ARG A 132     6170  12743   5844    721    157   -593       N  
ATOM    727  CZ  ARG A 132     -19.123 -19.539 -32.451  1.00 71.00           C  
ANISOU  727  CZ  ARG A 132     6884  13436   6658    766     85   -703       C  
ATOM    728  NH1 ARG A 132     -20.194 -19.136 -33.122  1.00 63.14           N  
ANISOU  728  NH1 ARG A 132     5892  12449   5651    770     42   -719       N  
ATOM    729  NH2 ARG A 132     -18.871 -20.835 -32.329  1.00 75.67           N  
ANISOU  729  NH2 ARG A 132     7445  13964   7344    808     43   -798       N  
ATOM    730  N   ASP A 133     -17.818 -14.345 -28.012  1.00 58.29           N  
ANISOU  730  N   ASP A 133     5484  11709   4953    505    291   -156       N  
ATOM    731  CA  ASP A 133     -18.212 -14.778 -26.678  1.00 49.19           C  
ANISOU  731  CA  ASP A 133     4326  10473   3891    509    319   -155       C  
ATOM    732  C   ASP A 133     -18.668 -16.231 -26.679  1.00 60.47           C  
ANISOU  732  C   ASP A 133     5694  11871   5410    533    322   -220       C  
ATOM    733  O   ASP A 133     -18.719 -16.870 -27.738  1.00 72.44           O  
ANISOU  733  O   ASP A 133     7181  13420   6921    558    291   -288       O  
ATOM    734  CB  ASP A 133     -19.347 -13.888 -26.165  1.00 65.70           C  
ANISOU  734  CB  ASP A 133     6446  12513   6002    522    300   -134       C  
ATOM    735  CG  ASP A 133     -18.851 -12.725 -25.349  1.00 72.87           C  
ANISOU  735  CG  ASP A 133     7416  13397   6874    506    293    -76       C  
ATOM    736  OD1 ASP A 133     -17.636 -12.460 -25.393  1.00 69.28           O  
ANISOU  736  OD1 ASP A 133     6983  12968   6374    467    296    -36       O  
ATOM    737  OD2 ASP A 133     -19.676 -12.074 -24.676  1.00 72.09           O  
ANISOU  737  OD2 ASP A 133     7340  13259   6793    538    278    -75       O  
ATOM    738  N   PRO A 134     -18.994 -16.797 -25.513  1.00 63.46           N  
ANISOU  738  N   PRO A 134     6049  12191   5874    528    346   -197       N  
ATOM    739  CA  PRO A 134     -19.906 -17.948 -25.502  1.00 61.21           C  
ANISOU  739  CA  PRO A 134     5703  11854   5700    536    323   -231       C  
ATOM    740  C   PRO A 134     -21.329 -17.557 -25.852  1.00 49.25           C  
ANISOU  740  C   PRO A 134     4172  10333   4207    548    294   -240       C  
ATOM    741  O   PRO A 134     -22.124 -18.430 -26.218  1.00 39.63           O  
ANISOU  741  O   PRO A 134     2901   9080   3078    549    253   -277       O  
ATOM    742  CB  PRO A 134     -19.801 -18.475 -24.062  1.00 54.10           C  
ANISOU  742  CB  PRO A 134     4775  10915   4867    515    362   -166       C  
ATOM    743  CG  PRO A 134     -18.553 -17.852 -23.513  1.00 41.39           C  
ANISOU  743  CG  PRO A 134     3214   9337   3176    506    401   -130       C  
ATOM    744  CD  PRO A 134     -18.453 -16.523 -24.172  1.00 47.18           C  
ANISOU  744  CD  PRO A 134     4005  10113   3809    510    389   -134       C  
ATOM    745  N   HIS A 135     -21.669 -16.270 -25.751  1.00 44.65           N  
ANISOU  745  N   HIS A 135     3633   9776   3554    558    301   -211       N  
ATOM    746  CA  HIS A 135     -22.956 -15.753 -26.195  1.00 63.97           C  
ANISOU  746  CA  HIS A 135     6069  12228   6009    581    268   -225       C  
ATOM    747  C   HIS A 135     -22.967 -15.382 -27.670  1.00 70.76           C  
ANISOU  747  C   HIS A 135     6956  13123   6809    593    217   -272       C  
ATOM    748  O   HIS A 135     -24.046 -15.158 -28.228  1.00 83.90           O  
ANISOU  748  O   HIS A 135     8602  14789   8486    614    178   -295       O  
ATOM    749  CB  HIS A 135     -23.352 -14.514 -25.383  1.00 71.30           C  
ANISOU  749  CB  HIS A 135     7034  13163   6893    607    282   -183       C  
ATOM    750  CG  HIS A 135     -23.051 -14.616 -23.922  1.00 73.75           C  
ANISOU  750  CG  HIS A 135     7333  13472   7214    607    334   -136       C  
ATOM    751  ND1 HIS A 135     -22.662 -13.531 -23.166  1.00 72.70           N  
ANISOU  751  ND1 HIS A 135     7262  13344   7018    631    341   -116       N  
ATOM    752  CD2 HIS A 135     -23.098 -15.668 -23.073  1.00 74.03           C  
ANISOU  752  CD2 HIS A 135     7304  13507   7317    589    373   -103       C  
ATOM    753  CE1 HIS A 135     -22.472 -13.914 -21.916  1.00 74.46           C  
ANISOU  753  CE1 HIS A 135     7456  13584   7253    635    388    -82       C  
ATOM    754  NE2 HIS A 135     -22.729 -15.207 -21.833  1.00 75.20           N  
ANISOU  754  NE2 HIS A 135     7472  13679   7424    606    413    -62       N  
ATOM    755  N   GLY A 136     -21.802 -15.301 -28.307  1.00 60.45           N  
ANISOU  755  N   GLY A 136     5681  11860   5428    583    218   -280       N  
ATOM    756  CA  GLY A 136     -21.707 -14.876 -29.686  1.00 62.78           C  
ANISOU  756  CA  GLY A 136     5993  12224   5638    594    177   -305       C  
ATOM    757  C   GLY A 136     -21.325 -13.427 -29.881  1.00 73.35           C  
ANISOU  757  C   GLY A 136     7393  13591   6884    575    165   -230       C  
ATOM    758  O   GLY A 136     -21.265 -12.971 -31.030  1.00 86.44           O  
ANISOU  758  O   GLY A 136     9061  15320   8464    577    128   -222       O  
ATOM    759  N   ASP A 137     -21.074 -12.690 -28.807  1.00 73.84           N  
ANISOU  759  N   ASP A 137     7496  13603   6957    557    183   -170       N  
ATOM    760  CA  ASP A 137     -20.656 -11.301 -28.936  1.00 80.09           C  
ANISOU  760  CA  ASP A 137     8352  14393   7686    532    145    -95       C  
ATOM    761  C   ASP A 137     -19.254 -11.240 -29.532  1.00 81.69           C  
ANISOU  761  C   ASP A 137     8554  14677   7807    484    155    -44       C  
ATOM    762  O   ASP A 137     -18.336 -11.881 -29.007  1.00 81.45           O  
ANISOU  762  O   ASP A 137     8504  14663   7782    469    203    -48       O  
ATOM    763  CB  ASP A 137     -20.682 -10.605 -27.579  1.00 79.71           C  
ANISOU  763  CB  ASP A 137     8347  14264   7674    537    146    -68       C  
ATOM    764  CG  ASP A 137     -22.047 -10.643 -26.930  1.00 75.50           C  
ANISOU  764  CG  ASP A 137     7796  13689   7203    597    146   -113       C  
ATOM    765  OD1 ASP A 137     -22.504 -11.748 -26.575  1.00 72.60           O  
ANISOU  765  OD1 ASP A 137     7363  13332   6888    611    193   -150       O  
ATOM    766  OD2 ASP A 137     -22.660  -9.567 -26.769  1.00 77.89           O  
ANISOU  766  OD2 ASP A 137     8141  13951   7503    632     92   -106       O  
ATOM    767  N   PRO A 138     -19.045 -10.483 -30.608  1.00 80.16           N  
ANISOU  767  N   PRO A 138     8374  14549   7534    460    109     15       N  
ATOM    768  CA  PRO A 138     -17.741 -10.505 -31.280  1.00 79.25           C  
ANISOU  768  CA  PRO A 138     8231  14543   7338    416    124     75       C  
ATOM    769  C   PRO A 138     -16.640  -9.924 -30.407  1.00 79.61           C  
ANISOU  769  C   PRO A 138     8305  14552   7392    354    129    161       C  
ATOM    770  O   PRO A 138     -16.818  -8.897 -29.747  1.00 89.23           O  
ANISOU  770  O   PRO A 138     9586  15681   8637    329     79    215       O  
ATOM    771  CB  PRO A 138     -17.980  -9.649 -32.528  1.00 78.69           C  
ANISOU  771  CB  PRO A 138     8166  14541   7192    396     63    147       C  
ATOM    772  CG  PRO A 138     -19.059  -8.701 -32.105  1.00 76.22           C  
ANISOU  772  CG  PRO A 138     7919  14113   6930    407     -1    163       C  
ATOM    773  CD  PRO A 138     -19.974  -9.536 -31.248  1.00 78.83           C  
ANISOU  773  CD  PRO A 138     8238  14359   7354    469     37     44       C  
ATOM    774  N   ILE A 139     -15.496 -10.603 -30.404  1.00 71.39           N  
ANISOU  774  N   ILE A 139     7218  13538   6372    336    170    162       N  
ATOM    775  CA  ILE A 139     -14.309 -10.161 -29.678  1.00 71.38           C  
ANISOU  775  CA  ILE A 139     7226  13521   6374    274    174    245       C  
ATOM    776  C   ILE A 139     -13.419  -9.413 -30.662  1.00 81.46           C  
ANISOU  776  C   ILE A 139     8472  14897   7583    204    144    371       C  
ATOM    777  O   ILE A 139     -12.800 -10.052 -31.532  1.00 88.09           O  
ANISOU  777  O   ILE A 139     9236  15827   8405    218    169    358       O  
ATOM    778  CB  ILE A 139     -13.562 -11.339 -29.041  1.00 70.74           C  
ANISOU  778  CB  ILE A 139     7106  13416   6355    297    227    181       C  
ATOM    779  CG1 ILE A 139     -14.497 -12.136 -28.129  1.00 66.78           C  
ANISOU  779  CG1 ILE A 139     6621  12830   5923    355    255     82       C  
ATOM    780  CG2 ILE A 139     -12.345 -10.843 -28.272  1.00 71.87           C  
ANISOU  780  CG2 ILE A 139     7256  13551   6498    232    227    267       C  
ATOM    781  CD1 ILE A 139     -13.786 -13.165 -27.280  1.00 59.91           C  
ANISOU  781  CD1 ILE A 139     5728  11921   5116    368    293     45       C  
ATOM    782  N   PRO A 140     -13.324  -8.087 -30.583  1.00 74.25           N  
ANISOU  782  N   PRO A 140     7607  13978   6625    130     75    498       N  
ATOM    783  CA  PRO A 140     -12.496  -7.343 -31.536  1.00 76.76           C  
ANISOU  783  CA  PRO A 140     7884  14399   6884     45     39    653       C  
ATOM    784  C   PRO A 140     -11.024  -7.706 -31.404  1.00 85.88           C  
ANISOU  784  C   PRO A 140     8963  15621   8044     -1     82    702       C  
ATOM    785  O   PRO A 140     -10.576  -8.264 -30.400  1.00 95.98           O  
ANISOU  785  O   PRO A 140    10248  16846   9374     16    118    641       O  
ATOM    786  CB  PRO A 140     -12.735  -5.874 -31.157  1.00 66.25           C  
ANISOU  786  CB  PRO A 140     6637  12996   5537    -28    -82    779       C  
ATOM    787  CG  PRO A 140     -13.370  -5.907 -29.800  1.00 53.84           C  
ANISOU  787  CG  PRO A 140     5147  11231   4080     28    -92    661       C  
ATOM    788  CD  PRO A 140     -14.109  -7.197 -29.711  1.00 59.19           C  
ANISOU  788  CD  PRO A 140     5795  11937   4758    132      4    500       C  
ATOM    789  N   GLY A 141     -10.269  -7.383 -32.449  1.00 88.88           N  
ANISOU  789  N   GLY A 141     9265  16133   8372    -58     74    821       N  
ATOM    790  CA  GLY A 141      -8.830  -7.505 -32.404  1.00 90.93           C  
ANISOU  790  CA  GLY A 141     9441  16484   8626   -113     97    900       C  
ATOM    791  C   GLY A 141      -8.186  -6.285 -31.778  1.00 96.23           C  
ANISOU  791  C   GLY A 141    10144  17128   9289   -248     24   1081       C  
ATOM    792  O   GLY A 141      -8.840  -5.307 -31.418  1.00 92.86           O  
ANISOU  792  O   GLY A 141     9815  16606   8861   -293    -68   1145       O  
ATOM    793  N   ALA A 142      -6.860  -6.350 -31.650  1.00107.82           N  
ANISOU  793  N   ALA A 142    11529  18683  10756   -309     41   1164       N  
ATOM    794  CA  ALA A 142      -6.112  -5.232 -31.087  1.00118.06           C  
ANISOU  794  CA  ALA A 142    12844  19964  12051   -454    -45   1352       C  
ATOM    795  C   ALA A 142      -6.075  -4.021 -32.010  1.00127.43           C  
ANISOU  795  C   ALA A 142    14011  21208  13200   -577   -142   1574       C  
ATOM    796  O   ALA A 142      -5.559  -2.973 -31.608  1.00135.64           O  
ANISOU  796  O   ALA A 142    15077  22204  14256   -712   -260   1756       O  
ATOM    797  CB  ALA A 142      -4.685  -5.669 -30.752  1.00116.82           C  
ANISOU  797  CB  ALA A 142    12584  19898  11903   -489     -2   1388       C  
ATOM    798  N   ASP A 143      -6.612  -4.136 -33.227  1.00124.42           N  
ANISOU  798  N   ASP A 143    13586  20913  12777   -535   -114   1570       N  
ATOM    799  CA  ASP A 143      -6.596  -3.052 -34.197  1.00120.36           C  
ANISOU  799  CA  ASP A 143    13040  20461  12229   -649   -199   1790       C  
ATOM    800  C   ASP A 143      -7.952  -2.399 -34.414  1.00113.44           C  
ANISOU  800  C   ASP A 143    12284  19462  11357   -629   -290   1787       C  
ATOM    801  O   ASP A 143      -8.003  -1.293 -34.960  1.00110.79           O  
ANISOU  801  O   ASP A 143    11957  19116  11023   -739   -408   1991       O  
ATOM    802  CB  ASP A 143      -6.076  -3.563 -35.549  1.00119.99           C  
ANISOU  802  CB  ASP A 143    12831  20641  12118   -620   -117   1815       C  
ATOM    803  CG  ASP A 143      -6.628  -4.932 -35.903  1.00115.89           C  
ANISOU  803  CG  ASP A 143    12294  20159  11580   -436    -13   1559       C  
ATOM    804  OD1 ASP A 143      -7.821  -5.021 -36.260  1.00112.30           O  
ANISOU  804  OD1 ASP A 143    11909  19642  11116   -364    -19   1466       O  
ATOM    805  OD2 ASP A 143      -5.869  -5.919 -35.816  1.00113.48           O  
ANISOU  805  OD2 ASP A 143    11908  19934  11275   -363     54   1455       O  
ATOM    806  N   GLY A 144      -9.041  -3.044 -34.002  1.00108.90           N  
ANISOU  806  N   GLY A 144    11793  18790  10796   -493   -251   1571       N  
ATOM    807  CA  GLY A 144     -10.373  -2.539 -34.271  1.00102.39           C  
ANISOU  807  CA  GLY A 144    11062  17869   9972   -451   -332   1545       C  
ATOM    808  C   GLY A 144     -11.098  -3.394 -35.289  1.00 99.47           C  
ANISOU  808  C   GLY A 144    10643  17593   9558   -338   -233   1413       C  
ATOM    809  O   GLY A 144     -11.886  -2.890 -36.096  1.00 99.42           O  
ANISOU  809  O   GLY A 144    10658  17591   9525   -335   -290   1463       O  
ATOM    810  N   GLN A 145     -10.834  -4.701 -35.249  1.00 98.59           N  
ANISOU  810  N   GLN A 145    10468  17546   9448   -242   -107   1242       N  
ATOM    811  CA  GLN A 145     -11.367  -5.609 -36.259  1.00 99.22           C  
ANISOU  811  CA  GLN A 145    10489  17718   9491   -133    -40   1112       C  
ATOM    812  C   GLN A 145     -12.878  -5.754 -36.132  1.00 92.56           C  
ANISOU  812  C   GLN A 145     9738  16762   8668    -46    -63    979       C  
ATOM    813  O   GLN A 145     -13.601  -5.679 -37.133  1.00101.97           O  
ANISOU  813  O   GLN A 145    10919  18009   9817    -12    -80    974       O  
ATOM    814  CB  GLN A 145     -10.679  -6.969 -36.141  1.00107.35           C  
ANISOU  814  CB  GLN A 145    11440  18811  10539    -47     54    962       C  
ATOM    815  CG  GLN A 145     -11.115  -7.995 -37.170  1.00110.33           C  
ANISOU  815  CG  GLN A 145    11757  19284  10878     75     94    818       C  
ATOM    816  CD  GLN A 145     -10.338  -9.293 -37.056  1.00109.21           C  
ANISOU  816  CD  GLN A 145    11545  19197  10752    161    148    683       C  
ATOM    817  OE1 GLN A 145     -10.399 -10.147 -37.941  1.00107.93           O  
ANISOU  817  OE1 GLN A 145    11321  19142  10547    261    164    576       O  
ATOM    818  NE2 GLN A 145      -9.597  -9.446 -35.964  1.00103.56           N  
ANISOU  818  NE2 GLN A 145    10844  18410  10094    128    164    687       N  
ATOM    819  N   VAL A 146     -13.365  -5.927 -34.903  1.00 81.76           N  
ANISOU  819  N   VAL A 146     8453  15249   7362    -11    -68    877       N  
ATOM    820  CA  VAL A 146     -14.759  -6.215 -34.544  1.00 76.09           C  
ANISOU  820  CA  VAL A 146     7805  14431   6675     80    -81    734       C  
ATOM    821  C   VAL A 146     -15.423  -7.077 -35.618  1.00 79.99           C  
ANISOU  821  C   VAL A 146     8246  15004   7144    167    -39    622       C  
ATOM    822  O   VAL A 146     -16.115  -6.558 -36.508  1.00 71.18           O  
ANISOU  822  O   VAL A 146     7139  13924   5984    169    -90    668       O  
ATOM    823  CB  VAL A 146     -15.543  -4.916 -34.242  1.00 68.69           C  
ANISOU  823  CB  VAL A 146     6964  13395   5739     47   -210    822       C  
ATOM    824  CG1 VAL A 146     -15.469  -3.886 -35.380  1.00 77.78           C  
ANISOU  824  CG1 VAL A 146     8104  14607   6841    -30   -297   1005       C  
ATOM    825  CG2 VAL A 146     -16.994  -5.222 -33.869  1.00 56.89           C  
ANISOU  825  CG2 VAL A 146     5521  11778   4315    151   -215    662       C  
ATOM    826  N   PRO A 147     -15.244  -8.403 -35.573  1.00 88.52           N  
ANISOU  826  N   PRO A 147     9274  16109   8252    242     35    474       N  
ATOM    827  CA  PRO A 147     -15.799  -9.262 -36.629  1.00 92.09           C  
ANISOU  827  CA  PRO A 147     9675  16642   8675    329     50    361       C  
ATOM    828  C   PRO A 147     -17.306  -9.445 -36.504  1.00 88.96           C  
ANISOU  828  C   PRO A 147     9329  16168   8303    390     21    255       C  
ATOM    829  O   PRO A 147     -17.774 -10.492 -36.048  1.00 83.60           O  
ANISOU  829  O   PRO A 147     8647  15444   7676    457     47    110       O  
ATOM    830  CB  PRO A 147     -15.042 -10.581 -36.426  1.00 96.99           C  
ANISOU  830  CB  PRO A 147    10235  17291   9325    387    106    243       C  
ATOM    831  CG  PRO A 147     -14.780 -10.594 -34.957  1.00 92.27           C  
ANISOU  831  CG  PRO A 147     9688  16566   8806    354    126    242       C  
ATOM    832  CD  PRO A 147     -14.513  -9.174 -34.554  1.00 88.33           C  
ANISOU  832  CD  PRO A 147     9238  16034   8289    252     89    408       C  
ATOM    833  N   THR A 148     -18.069  -8.433 -36.895  1.00 94.08           N  
ANISOU  833  N   THR A 148    10023  16805   8919    367    -44    335       N  
ATOM    834  CA  THR A 148     -19.524  -8.526 -36.818  1.00 86.36           C  
ANISOU  834  CA  THR A 148     9083  15768   7962    429    -83    242       C  
ATOM    835  C   THR A 148     -20.044  -9.489 -37.881  1.00 91.40           C  
ANISOU  835  C   THR A 148     9664  16494   8571    506    -74    121       C  
ATOM    836  O   THR A 148     -19.716  -9.333 -39.064  1.00 92.99           O  
ANISOU  836  O   THR A 148     9822  16809   8701    504    -82    170       O  
ATOM    837  CB  THR A 148     -20.159  -7.144 -37.002  1.00 76.85           C  
ANISOU  837  CB  THR A 148     7939  14526   6733    393   -180    362       C  
ATOM    838  OG1 THR A 148     -19.501  -6.199 -36.149  1.00 76.86           O  
ANISOU  838  OG1 THR A 148     7993  14458   6752    319   -216    482       O  
ATOM    839  CG2 THR A 148     -21.640  -7.173 -36.662  1.00 76.56           C  
ANISOU  839  CG2 THR A 148     7937  14407   6744    463   -225    263       C  
ATOM    840  N   PRO A 149     -20.857 -10.477 -37.514  1.00 91.45           N  
ANISOU  840  N   PRO A 149     9662  16460   8623    574    -66    -31       N  
ATOM    841  CA  PRO A 149     -21.382 -11.418 -38.511  1.00 93.77           C  
ANISOU  841  CA  PRO A 149     9907  16834   8889    650    -82   -159       C  
ATOM    842  C   PRO A 149     -22.635 -10.870 -39.170  1.00 92.61           C  
ANISOU  842  C   PRO A 149     9778  16694   8715    672   -154   -156       C  
ATOM    843  O   PRO A 149     -23.345 -10.040 -38.582  1.00 92.59           O  
ANISOU  843  O   PRO A 149     9825  16613   8740    650   -193    -99       O  
ATOM    844  CB  PRO A 149     -21.691 -12.679 -37.686  1.00 90.52           C  
ANISOU  844  CB  PRO A 149     9479  16370   8544    696    -61   -306       C  
ATOM    845  CG  PRO A 149     -21.638 -12.258 -36.233  1.00 86.49           C  
ANISOU  845  CG  PRO A 149     9014  15750   8098    647    -29   -247       C  
ATOM    846  CD  PRO A 149     -21.305 -10.799 -36.150  1.00 85.59           C  
ANISOU  846  CD  PRO A 149     8950  15613   7958    582    -48    -89       C  
ATOM    847  N   PRO A 150     -22.946 -11.308 -40.394  1.00 88.22           N  
ANISOU  847  N   PRO A 150     9181  16234   8104    727   -181   -224       N  
ATOM    848  CA  PRO A 150     -24.157 -10.823 -41.090  1.00 88.04           C  
ANISOU  848  CA  PRO A 150     9172  16220   8058    752   -255   -224       C  
ATOM    849  C   PRO A 150     -25.422 -11.523 -40.598  1.00 86.06           C  
ANISOU  849  C   PRO A 150     8915  15907   7875    801   -302   -360       C  
ATOM    850  O   PRO A 150     -25.984 -12.419 -41.227  1.00 97.07           O  
ANISOU  850  O   PRO A 150    10270  17344   9267    862   -342   -494       O  
ATOM    851  CB  PRO A 150     -23.847 -11.144 -42.553  1.00 88.89           C  
ANISOU  851  CB  PRO A 150     9229  16469   8076    796   -260   -254       C  
ATOM    852  CG  PRO A 150     -23.039 -12.406 -42.470  1.00 83.75           C  
ANISOU  852  CG  PRO A 150     8528  15861   7431    845   -214   -381       C  
ATOM    853  CD  PRO A 150     -22.224 -12.316 -41.192  1.00 85.17           C  
ANISOU  853  CD  PRO A 150     8731  15958   7673    784   -155   -320       C  
ATOM    854  N   ALA A 151     -25.894 -11.096 -39.431  1.00 82.00           N  
ANISOU  854  N   ALA A 151     8435  15261   7460    771   -298   -323       N  
ATOM    855  CA  ALA A 151     -27.021 -11.728 -38.763  1.00 77.36           C  
ANISOU  855  CA  ALA A 151     7826  14543   7025    796   -310   -418       C  
ATOM    856  C   ALA A 151     -28.123 -10.713 -38.500  1.00 77.39           C  
ANISOU  856  C   ALA A 151     7857  14461   7087    798   -357   -358       C  
ATOM    857  O   ALA A 151     -27.850  -9.550 -38.184  1.00 78.51           O  
ANISOU  857  O   ALA A 151     8054  14568   7210    770   -362   -245       O  
ATOM    858  CB  ALA A 151     -26.588 -12.373 -37.443  1.00 76.94           C  
ANISOU  858  CB  ALA A 151     7767  14385   7080    771   -240   -440       C  
ATOM    859  N   ARG A 152     -29.367 -11.160 -38.638  1.00 79.33           N  
ANISOU  859  N   ARG A 152     8060  14672   7410    835   -402   -438       N  
ATOM    860  CA  ARG A 152     -30.530 -10.394 -38.225  1.00 90.28           C  
ANISOU  860  CA  ARG A 152     9452  15979   8872    855   -439   -406       C  
ATOM    861  C   ARG A 152     -31.304 -11.182 -37.175  1.00 86.00           C  
ANISOU  861  C   ARG A 152     8850  15349   8476    861   -408   -466       C  
ATOM    862  O   ARG A 152     -31.108 -12.388 -37.001  1.00 80.09           O  
ANISOU  862  O   ARG A 152     8056  14594   7781    846   -384   -536       O  
ATOM    863  CB  ARG A 152     -31.433 -10.042 -39.416  1.00105.13           C  
ANISOU  863  CB  ARG A 152    11320  17923  10703    893   -531   -418       C  
ATOM    864  CG  ARG A 152     -31.565 -11.126 -40.471  1.00113.98           C  
ANISOU  864  CG  ARG A 152    12388  19137  11782    917   -570   -528       C  
ATOM    865  CD  ARG A 152     -32.522 -10.678 -41.565  1.00124.42           C  
ANISOU  865  CD  ARG A 152    13698  20522  13052    957   -666   -533       C  
ATOM    866  NE  ARG A 152     -32.423 -11.493 -42.773  1.00136.71           N  
ANISOU  866  NE  ARG A 152    15222  22204  14519    991   -715   -632       N  
ATOM    867  CZ  ARG A 152     -33.028 -12.664 -42.939  1.00140.43           C  
ANISOU  867  CZ  ARG A 152    15632  22653  15070   1016   -759   -771       C  
ATOM    868  NH1 ARG A 152     -33.783 -13.170 -41.973  1.00137.77           N  
ANISOU  868  NH1 ARG A 152    15253  22185  14908    995   -750   -801       N  
ATOM    869  NH2 ARG A 152     -32.881 -13.329 -44.076  1.00143.19           N  
ANISOU  869  NH2 ARG A 152    15961  23121  15325   1063   -820   -876       N  
ATOM    870  N   GLN A 153     -32.184 -10.479 -36.471  1.00 82.20           N  
ANISOU  870  N   GLN A 153     8365  14808   8059    887   -416   -433       N  
ATOM    871  CA  GLN A 153     -32.857 -11.054 -35.317  1.00 75.77           C  
ANISOU  871  CA  GLN A 153     7483  13940   7364    892   -373   -456       C  
ATOM    872  C   GLN A 153     -33.865 -12.115 -35.745  1.00 74.88           C  
ANISOU  872  C   GLN A 153     7274  13843   7334    892   -416   -527       C  
ATOM    873  O   GLN A 153     -34.439 -12.055 -36.835  1.00 81.91           O  
ANISOU  873  O   GLN A 153     8153  14775   8195    914   -493   -563       O  
ATOM    874  CB  GLN A 153     -33.547  -9.950 -34.518  1.00 75.14           C  
ANISOU  874  CB  GLN A 153     7415  13825   7309    943   -376   -412       C  
ATOM    875  CG  GLN A 153     -32.800  -8.626 -34.597  1.00 82.63           C  
ANISOU  875  CG  GLN A 153     8472  14746   8178    951   -400   -347       C  
ATOM    876  CD  GLN A 153     -33.513  -7.496 -33.890  1.00 89.37           C  
ANISOU  876  CD  GLN A 153     9346  15550   9060   1024   -433   -329       C  
ATOM    877  OE1 GLN A 153     -33.500  -6.354 -34.351  1.00 98.83           O  
ANISOU  877  OE1 GLN A 153    10616  16716  10220   1050   -511   -287       O  
ATOM    878  NE2 GLN A 153     -34.115  -7.799 -32.753  1.00 85.31           N  
ANISOU  878  NE2 GLN A 153     8767  15036   8611   1063   -381   -358       N  
ATOM    879  N   LEU A 154     -34.073 -13.102 -34.868  1.00 68.53           N  
ANISOU  879  N   LEU A 154     6397  13002   6638    862   -374   -539       N  
ATOM    880  CA  LEU A 154     -35.046 -14.154 -35.147  1.00 64.43           C  
ANISOU  880  CA  LEU A 154     5777  12477   6227    844   -430   -589       C  
ATOM    881  C   LEU A 154     -36.455 -13.600 -35.300  1.00 68.14           C  
ANISOU  881  C   LEU A 154     6185  12975   6729    885   -479   -578       C  
ATOM    882  O   LEU A 154     -37.300 -14.244 -35.933  1.00 74.05           O  
ANISOU  882  O   LEU A 154     6861  13731   7543    876   -556   -624       O  
ATOM    883  CB  LEU A 154     -35.013 -15.213 -34.041  1.00 58.30           C  
ANISOU  883  CB  LEU A 154     4928  11653   5573    791   -381   -565       C  
ATOM    884  CG  LEU A 154     -35.792 -16.507 -34.299  1.00 61.05           C  
ANISOU  884  CG  LEU A 154     5170  11965   6060    747   -456   -605       C  
ATOM    885  CD1 LEU A 154     -35.276 -17.202 -35.549  1.00 60.81           C  
ANISOU  885  CD1 LEU A 154     5179  11919   6006    750   -542   -717       C  
ATOM    886  CD2 LEU A 154     -35.720 -17.439 -33.101  1.00 71.54           C  
ANISOU  886  CD2 LEU A 154     6426  13245   7512    684   -409   -543       C  
ATOM    887  N   TRP A 155     -36.727 -12.419 -34.743  1.00 66.57           N  
ANISOU  887  N   TRP A 155     6013  12791   6489    937   -449   -525       N  
ATOM    888  CA  TRP A 155     -38.023 -11.785 -34.938  1.00 68.14           C  
ANISOU  888  CA  TRP A 155     6157  13026   6707    996   -501   -521       C  
ATOM    889  C   TRP A 155     -38.165 -11.190 -36.333  1.00 85.28           C  
ANISOU  889  C   TRP A 155     8385  15218   8798   1026   -594   -550       C  
ATOM    890  O   TRP A 155     -39.285 -11.073 -36.839  1.00 88.86           O  
ANISOU  890  O   TRP A 155     8777  15703   9282   1060   -663   -569       O  
ATOM    891  CB  TRP A 155     -38.244 -10.700 -33.886  1.00 64.16           C  
ANISOU  891  CB  TRP A 155     5668  12529   6182   1065   -454   -475       C  
ATOM    892  CG  TRP A 155     -39.645 -10.178 -33.849  1.00 77.35           C  
ANISOU  892  CG  TRP A 155     7255  14249   7885   1140   -497   -476       C  
ATOM    893  CD1 TRP A 155     -40.039  -8.882 -34.009  1.00 82.24           C  
ANISOU  893  CD1 TRP A 155     7925  14869   8454   1233   -546   -476       C  
ATOM    894  CD2 TRP A 155     -40.842 -10.938 -33.636  1.00 79.85           C  
ANISOU  894  CD2 TRP A 155     7415  14624   8299   1130   -504   -473       C  
ATOM    895  NE1 TRP A 155     -41.405  -8.787 -33.911  1.00 86.59           N  
ANISOU  895  NE1 TRP A 155     8361  15486   9056   1295   -577   -485       N  
ATOM    896  CE2 TRP A 155     -41.922 -10.035 -33.681  1.00 85.37           C  
ANISOU  896  CE2 TRP A 155     8072  15377   8990   1228   -547   -477       C  
ATOM    897  CE3 TRP A 155     -41.104 -12.293 -33.410  1.00 78.58           C  
ANISOU  897  CE3 TRP A 155     7141  14472   8242   1044   -490   -459       C  
ATOM    898  CZ2 TRP A 155     -43.243 -10.443 -33.510  1.00 91.63           C  
ANISOU  898  CZ2 TRP A 155     8702  16252   9861   1242   -563   -464       C  
ATOM    899  CZ3 TRP A 155     -42.417 -12.695 -33.241  1.00 79.46           C  
ANISOU  899  CZ3 TRP A 155     7095  14653   8445   1044   -515   -434       C  
ATOM    900  CH2 TRP A 155     -43.469 -11.774 -33.292  1.00 90.28           C  
ANISOU  900  CH2 TRP A 155     8415  16096   9791   1142   -545   -435       C  
ATOM    901  N   ALA A 156     -37.055 -10.807 -36.964  1.00 87.81           N  
ANISOU  901  N   ALA A 156     8813  15538   9013   1014   -598   -543       N  
ATOM    902  CA  ALA A 156     -37.105 -10.245 -38.306  1.00 82.61           C  
ANISOU  902  CA  ALA A 156     8203  14924   8259   1038   -683   -549       C  
ATOM    903  C   ALA A 156     -37.319 -11.298 -39.386  1.00 86.37           C  
ANISOU  903  C   ALA A 156     8633  15450   8735   1020   -746   -633       C  
ATOM    904  O   ALA A 156     -37.625 -10.936 -40.527  1.00 87.97           O  
ANISOU  904  O   ALA A 156     8851  15712   8861   1050   -827   -647       O  
ATOM    905  CB  ALA A 156     -35.822  -9.462 -38.598  1.00 80.33           C  
ANISOU  905  CB  ALA A 156     8027  14642   7851   1022   -666   -487       C  
ATOM    906  N   CYS A 157     -37.171 -12.579 -39.058  1.00 86.44           N  
ANISOU  906  N   CYS A 157     8585  15431   8827    977   -725   -691       N  
ATOM    907  CA  CYS A 157     -37.354 -13.646 -40.028  1.00 93.11           C  
ANISOU  907  CA  CYS A 157     9389  16301   9687    970   -806   -794       C  
ATOM    908  C   CYS A 157     -38.841 -13.858 -40.311  1.00109.70           C  
ANISOU  908  C   CYS A 157    11395  18403  11885    983   -895   -823       C  
ATOM    909  O   CYS A 157     -39.716 -13.243 -39.695  1.00120.31           O  
ANISOU  909  O   CYS A 157    12693  19738  13282   1000   -879   -762       O  
ATOM    910  CB  CYS A 157     -36.702 -14.933 -39.526  1.00 95.62           C  
ANISOU  910  CB  CYS A 157     9683  16562  10088    921   -777   -845       C  
ATOM    911  SG  CYS A 157     -34.899 -14.870 -39.427  1.00102.82           S  
ANISOU  911  SG  CYS A 157    10693  17496  10878    914   -690   -833       S  
ATOM    912  N   ARG A 158     -39.130 -14.744 -41.261  1.00110.69           N  
ANISOU  912  N   ARG A 158    11485  18544  12029    983   -996   -926       N  
ATOM    913  CA  ARG A 158     -40.493 -15.106 -41.628  1.00 98.81           C  
ANISOU  913  CA  ARG A 158     9881  17036  10626    984  -1100   -964       C  
ATOM    914  C   ARG A 158     -40.592 -16.624 -41.743  1.00 90.16           C  
ANISOU  914  C   ARG A 158     8720  15874   9662    936  -1179  -1062       C  
ATOM    915  O   ARG A 158     -39.622 -17.351 -41.508  1.00 95.25           O  
ANISOU  915  O   ARG A 158     9400  16473  10318    913  -1151  -1102       O  
ATOM    916  CB  ARG A 158     -40.917 -14.422 -42.934  1.00106.39           C  
ANISOU  916  CB  ARG A 158    10871  18088  11464   1047  -1191   -997       C  
ATOM    917  CG  ARG A 158     -42.022 -13.391 -42.757  1.00120.18           C  
ANISOU  917  CG  ARG A 158    12580  19856  13229   1082  -1203   -919       C  
ATOM    918  CD  ARG A 158     -41.459 -12.003 -42.486  1.00123.87           C  
ANISOU  918  CD  ARG A 158    13143  20341  13580   1120  -1129   -820       C  
ATOM    919  NE  ARG A 158     -42.496 -11.056 -42.081  1.00126.26           N  
ANISOU  919  NE  ARG A 158    13407  20643  13924   1167  -1140   -756       N  
ATOM    920  CZ  ARG A 158     -43.403 -10.535 -42.902  1.00122.99           C  
ANISOU  920  CZ  ARG A 158    12969  20277  13484   1219  -1237   -762       C  
ATOM    921  NH1 ARG A 158     -43.408 -10.861 -44.188  1.00120.57           N  
ANISOU  921  NH1 ARG A 158    12677  20032  13103   1225  -1332   -825       N  
ATOM    922  NH2 ARG A 158     -44.306  -9.683 -42.438  1.00118.05           N  
ANISOU  922  NH2 ARG A 158    12305  19648  12901   1275  -1245   -711       N  
ATOM    923  N   ASP A 159     -41.779 -17.102 -42.111  1.00 90.59           N  
ANISOU  923  N   ASP A 159     8679  15915   9828    923  -1293  -1101       N  
ATOM    924  CA  ASP A 159     -42.014 -18.536 -42.209  1.00 96.27           C  
ANISOU  924  CA  ASP A 159     9327  16543  10707    868  -1403  -1187       C  
ATOM    925  C   ASP A 159     -41.124 -19.160 -43.276  1.00 92.52           C  
ANISOU  925  C   ASP A 159     8932  16080  10141    916  -1483  -1344       C  
ATOM    926  O   ASP A 159     -40.831 -18.541 -44.302  1.00 96.36           O  
ANISOU  926  O   ASP A 159     9489  16679  10446    993  -1503  -1397       O  
ATOM    927  CB  ASP A 159     -43.485 -18.807 -42.529  1.00106.65           C  
ANISOU  927  CB  ASP A 159    10521  17851  12149    845  -1528  -1195       C  
ATOM    928  CG  ASP A 159     -44.427 -17.953 -41.703  1.00117.11           C  
ANISOU  928  CG  ASP A 159    11763  19221  13510    836  -1449  -1053       C  
ATOM    929  OD1 ASP A 159     -44.315 -17.974 -40.458  1.00121.84           O  
ANISOU  929  OD1 ASP A 159    12322  19795  14179    790  -1339   -945       O  
ATOM    930  OD2 ASP A 159     -45.280 -17.262 -42.297  1.00122.02           O  
ANISOU  930  OD2 ASP A 159    12359  19917  14087    885  -1501  -1052       O  
ATOM    931  N   GLY A 160     -40.690 -20.396 -43.025  1.00 85.39           N  
ANISOU  931  N   GLY A 160     8013  15069   9361    876  -1536  -1416       N  
ATOM    932  CA  GLY A 160     -39.867 -21.126 -43.961  1.00 82.26           C  
ANISOU  932  CA  GLY A 160     7680  14680   8894    939  -1627  -1589       C  
ATOM    933  C   GLY A 160     -38.394 -20.788 -43.935  1.00 80.99           C  
ANISOU  933  C   GLY A 160     7623  14591   8560    989  -1506  -1594       C  
ATOM    934  O   GLY A 160     -37.605 -21.492 -44.578  1.00 86.59           O  
ANISOU  934  O   GLY A 160     8372  15315   9211   1051  -1570  -1741       O  
ATOM    935  N   ASP A 161     -37.991 -19.743 -43.218  1.00 74.35           N  
ANISOU  935  N   ASP A 161     6819  13797   7634    972  -1345  -1445       N  
ATOM    936  CA  ASP A 161     -36.590 -19.360 -43.162  1.00 70.30           C  
ANISOU  936  CA  ASP A 161     6394  13354   6963   1006  -1233  -1430       C  
ATOM    937  C   ASP A 161     -35.822 -20.254 -42.196  1.00 74.16           C  
ANISOU  937  C   ASP A 161     6881  13728   7569    961  -1188  -1430       C  
ATOM    938  O   ASP A 161     -36.365 -20.749 -41.204  1.00 77.04           O  
ANISOU  938  O   ASP A 161     7181  13968   8123    882  -1186  -1364       O  
ATOM    939  CB  ASP A 161     -36.448 -17.897 -42.738  1.00 67.29           C  
ANISOU  939  CB  ASP A 161     6057  13043   6468    998  -1102  -1270       C  
ATOM    940  CG  ASP A 161     -36.670 -16.932 -43.887  1.00 68.34           C  
ANISOU  940  CG  ASP A 161     6225  13317   6424   1060  -1138  -1267       C  
ATOM    941  OD1 ASP A 161     -36.465 -17.333 -45.053  1.00 80.35           O  
ANISOU  941  OD1 ASP A 161     7757  14931   7841   1123  -1225  -1389       O  
ATOM    942  OD2 ASP A 161     -37.046 -15.771 -43.625  1.00 63.43           O  
ANISOU  942  OD2 ASP A 161     5620  12717   5764   1053  -1087  -1145       O  
ATOM    943  N   THR A 162     -34.545 -20.465 -42.505  1.00 78.41           N  
ANISOU  943  N   THR A 162     7481  14324   7988   1012  -1154  -1497       N  
ATOM    944  CA  THR A 162     -33.640 -21.221 -41.655  1.00 74.86           C  
ANISOU  944  CA  THR A 162     7040  13782   7621    984  -1106  -1499       C  
ATOM    945  C   THR A 162     -32.397 -20.384 -41.392  1.00 74.77           C  
ANISOU  945  C   THR A 162     7098  13874   7438   1000   -957  -1417       C  
ATOM    946  O   THR A 162     -32.125 -19.405 -42.091  1.00 64.16           O  
ANISOU  946  O   THR A 162     5795  12678   5906   1041   -918  -1386       O  
ATOM    947  CB  THR A 162     -33.242 -22.561 -42.290  1.00 73.73           C  
ANISOU  947  CB  THR A 162     6893  13591   7531   1044  -1242  -1694       C  
ATOM    948  OG1 THR A 162     -32.589 -22.322 -43.543  1.00 75.74           O  
ANISOU  948  OG1 THR A 162     7192  14024   7562   1158  -1265  -1814       O  
ATOM    949  CG2 THR A 162     -34.468 -23.428 -42.524  1.00 85.22           C  
ANISOU  949  CG2 THR A 162     8279  14919   9183   1014  -1415  -1771       C  
ATOM    950  N   GLY A 163     -31.641 -20.777 -40.374  1.00 90.66           N  
ANISOU  950  N   GLY A 163     9118  15806   9522    960   -883  -1370       N  
ATOM    951  CA  GLY A 163     -30.418 -20.056 -40.071  1.00 96.97           C  
ANISOU  951  CA  GLY A 163     9976  16694  10176    967   -752  -1292       C  
ATOM    952  C   GLY A 163     -29.650 -20.725 -38.955  1.00 92.21           C  
ANISOU  952  C   GLY A 163     9372  15987   9678    927   -695  -1263       C  
ATOM    953  O   GLY A 163     -30.018 -21.799 -38.468  1.00 92.97           O  
ANISOU  953  O   GLY A 163     9424  15943   9958    896   -763  -1302       O  
ATOM    954  N   THR A 164     -28.564 -20.067 -38.556  1.00 84.32           N  
ANISOU  954  N   THR A 164     8419  15056   8563    923   -578  -1183       N  
ATOM    955  CA  THR A 164     -27.693 -20.543 -37.491  1.00 72.38           C  
ANISOU  955  CA  THR A 164     6912  13469   7120    889   -511  -1142       C  
ATOM    956  C   THR A 164     -27.623 -19.491 -36.393  1.00 67.77           C  
ANISOU  956  C   THR A 164     6352  12874   6523    825   -392   -974       C  
ATOM    957  O   THR A 164     -27.431 -18.303 -36.678  1.00 68.77           O  
ANISOU  957  O   THR A 164     6520  13096   6513    830   -342   -905       O  
ATOM    958  CB  THR A 164     -26.288 -20.853 -38.023  1.00 73.19           C  
ANISOU  958  CB  THR A 164     7041  13673   7094    957   -493  -1223       C  
ATOM    959  OG1 THR A 164     -26.351 -21.951 -38.940  1.00 82.75           O  
ANISOU  959  OG1 THR A 164     8229  14884   8329   1038   -619  -1407       O  
ATOM    960  CG2 THR A 164     -25.342 -21.205 -36.886  1.00 75.99           C  
ANISOU  960  CG2 THR A 164     7404  13958   7510    922   -417  -1165       C  
ATOM    961  N   VAL A 165     -27.787 -19.928 -35.145  1.00 66.75           N  
ANISOU  961  N   VAL A 165     6195  12630   6536    768   -358   -908       N  
ATOM    962  CA  VAL A 165     -27.694 -19.034 -33.994  1.00 60.12           C  
ANISOU  962  CA  VAL A 165     5375  11783   5685    723   -252   -769       C  
ATOM    963  C   VAL A 165     -26.251 -18.552 -33.879  1.00 64.62           C  
ANISOU  963  C   VAL A 165     6005  12419   6129    732   -176   -740       C  
ATOM    964  O   VAL A 165     -25.357 -19.320 -33.512  1.00 76.83           O  
ANISOU  964  O   VAL A 165     7549  13937   7705    732   -159   -765       O  
ATOM    965  CB  VAL A 165     -28.155 -19.724 -32.704  1.00 52.17           C  
ANISOU  965  CB  VAL A 165     4310  10669   4843    666   -235   -703       C  
ATOM    966  CG1 VAL A 165     -27.998 -18.788 -31.517  1.00 42.58           C  
ANISOU  966  CG1 VAL A 165     3117   9471   3590    642   -128   -580       C  
ATOM    967  CG2 VAL A 165     -29.600 -20.181 -32.833  1.00 59.67           C  
ANISOU  967  CG2 VAL A 165     5182  11569   5922    644   -315   -710       C  
ATOM    968  N   ALA A 166     -26.019 -17.278 -34.199  1.00 56.87           N  
ANISOU  968  N   ALA A 166     5073  11522   5014    738   -140   -679       N  
ATOM    969  CA  ALA A 166     -24.688 -16.695 -34.141  1.00 59.27           C  
ANISOU  969  CA  ALA A 166     5425  11896   5200    732    -77   -628       C  
ATOM    970  C   ALA A 166     -24.485 -15.740 -32.975  1.00 64.44           C  
ANISOU  970  C   ALA A 166     6118  12509   5859    690    -10   -510       C  
ATOM    971  O   ALA A 166     -23.336 -15.424 -32.653  1.00 73.30           O  
ANISOU  971  O   ALA A 166     7271  13661   6919    670     39   -462       O  
ATOM    972  CB  ALA A 166     -24.376 -15.949 -35.448  1.00 56.50           C  
ANISOU  972  CB  ALA A 166     5097  11682   4687    761   -102   -628       C  
ATOM    973  N   ARG A 167     -25.559 -15.285 -32.334  1.00 60.89           N  
ANISOU  973  N   ARG A 167     5660  11998   5477    682    -12   -470       N  
ATOM    974  CA  ARG A 167     -25.453 -14.267 -31.301  1.00 56.63           C  
ANISOU  974  CA  ARG A 167     5162  11428   4927    667     33   -383       C  
ATOM    975  C   ARG A 167     -26.678 -14.346 -30.403  1.00 62.59           C  
ANISOU  975  C   ARG A 167     5870  12131   5781    677     39   -370       C  
ATOM    976  O   ARG A 167     -27.801 -14.484 -30.892  1.00 60.43           O  
ANISOU  976  O   ARG A 167     5553  11860   5549    696     -8   -401       O  
ATOM    977  CB  ARG A 167     -25.332 -12.871 -31.925  1.00 58.26           C  
ANISOU  977  CB  ARG A 167     5431  11674   5031    672      2   -331       C  
ATOM    978  CG  ARG A 167     -25.506 -11.715 -30.956  1.00 59.94           C  
ANISOU  978  CG  ARG A 167     5691  11832   5250    676     10   -265       C  
ATOM    979  CD  ARG A 167     -24.262 -11.503 -30.116  1.00 64.90           C  
ANISOU  979  CD  ARG A 167     6359  12444   5856    642     56   -216       C  
ATOM    980  NE  ARG A 167     -24.277 -10.201 -29.457  1.00 80.51           N  
ANISOU  980  NE  ARG A 167     8400  14369   7821    652     30   -163       N  
ATOM    981  CZ  ARG A 167     -23.889  -9.070 -30.038  1.00 88.94           C  
ANISOU  981  CZ  ARG A 167     9530  15433   8832    633    -30   -103       C  
ATOM    982  NH1 ARG A 167     -23.456  -9.082 -31.291  1.00 86.57           N  
ANISOU  982  NH1 ARG A 167     9225  15206   8461    601    -53    -75       N  
ATOM    983  NH2 ARG A 167     -23.934  -7.927 -29.368  1.00 97.95           N  
ANISOU  983  NH2 ARG A 167    10733  16499   9985    648    -77    -69       N  
ATOM    984  N   ILE A 168     -26.451 -14.266 -29.094  1.00 68.64           N  
ANISOU  984  N   ILE A 168     6636  12869   6577    668     96   -321       N  
ATOM    985  CA  ILE A 168     -27.517 -14.239 -28.101  1.00 57.69           C  
ANISOU  985  CA  ILE A 168     5192  11472   5254    687    116   -293       C  
ATOM    986  C   ILE A 168     -27.232 -13.095 -27.139  1.00 66.14           C  
ANISOU  986  C   ILE A 168     6318  12544   6267    718    147   -251       C  
ATOM    987  O   ILE A 168     -26.110 -12.973 -26.633  1.00 74.79           O  
ANISOU  987  O   ILE A 168     7462  13627   7327    697    179   -228       O  
ATOM    988  CB  ILE A 168     -27.629 -15.572 -27.336  1.00 45.10           C  
ANISOU  988  CB  ILE A 168     3515   9857   3764    651    147   -275       C  
ATOM    989  CG1 ILE A 168     -27.982 -16.715 -28.291  1.00 45.94           C  
ANISOU  989  CG1 ILE A 168     3570   9936   3951    626     85   -330       C  
ATOM    990  CG2 ILE A 168     -28.666 -15.463 -26.228  1.00 45.57           C  
ANISOU  990  CG2 ILE A 168     3500   9948   3865    670    181   -219       C  
ATOM    991  CD1 ILE A 168     -28.315 -18.020 -27.592  1.00 45.08           C  
ANISOU  991  CD1 ILE A 168     3369   9782   3976    580     84   -296       C  
ATOM    992  N   SER A 169     -28.237 -12.257 -26.894  1.00 60.42           N  
ANISOU  992  N   SER A 169     5585  11835   5536    776    126   -251       N  
ATOM    993  CA  SER A 169     -28.059 -11.132 -25.988  1.00 63.50           C  
ANISOU  993  CA  SER A 169     6031  12219   5876    827    132   -238       C  
ATOM    994  C   SER A 169     -27.764 -11.624 -24.576  1.00 73.53           C  
ANISOU  994  C   SER A 169     7264  13516   7159    829    205   -209       C  
ATOM    995  O   SER A 169     -28.269 -12.659 -24.134  1.00 68.96           O  
ANISOU  995  O   SER A 169     6587  12976   6639    809    248   -185       O  
ATOM    996  CB  SER A 169     -29.303 -10.243 -25.984  1.00 67.80           C  
ANISOU  996  CB  SER A 169     6561  12782   6416    912     87   -261       C  
ATOM    997  OG  SER A 169     -29.125  -9.121 -25.138  1.00 74.14           O  
ANISOU  997  OG  SER A 169     7427  13569   7174    981     70   -272       O  
ATOM    998  N   ASP A 170     -26.929 -10.866 -23.867  1.00 93.28           N  
ANISOU  998  N   ASP A 170     9841  15997   9606    847    208   -204       N  
ATOM    999  CA  ASP A 170     -26.498 -11.216 -22.522  1.00 99.12           C  
ANISOU  999  CA  ASP A 170    10556  16769  10335    854    271   -178       C  
ATOM   1000  C   ASP A 170     -27.036 -10.270 -21.459  1.00 91.78           C  
ANISOU 1000  C   ASP A 170     9634  15884   9356    959    265   -205       C  
ATOM   1001  O   ASP A 170     -26.721 -10.447 -20.277  1.00 91.61           O  
ANISOU 1001  O   ASP A 170     9592  15912   9305    982    314   -189       O  
ATOM   1002  CB  ASP A 170     -24.966 -11.248 -22.453  1.00102.94           C  
ANISOU 1002  CB  ASP A 170    11113  17205  10794    794    278   -159       C  
ATOM   1003  CG  ASP A 170     -24.333  -9.937 -22.891  1.00104.95           C  
ANISOU 1003  CG  ASP A 170    11478  17397  10999    800    203   -171       C  
ATOM   1004  OD1 ASP A 170     -24.476  -8.929 -22.167  1.00107.45           O  
ANISOU 1004  OD1 ASP A 170    11842  17698  11286    867    165   -195       O  
ATOM   1005  OD2 ASP A 170     -23.695  -9.914 -23.964  1.00107.16           O  
ANISOU 1005  OD2 ASP A 170    11794  17651  11272    739    174   -154       O  
ATOM   1006  N   ALA A 171     -27.842  -9.277 -21.844  1.00 88.34           N  
ANISOU 1006  N   ALA A 171     9223  15438   8905   1036    200   -252       N  
ATOM   1007  CA  ALA A 171     -28.301  -8.257 -20.908  1.00 75.02           C  
ANISOU 1007  CA  ALA A 171     7555  13784   7165   1162    171   -305       C  
ATOM   1008  C   ALA A 171     -29.149  -8.821 -19.776  1.00 76.76           C  
ANISOU 1008  C   ALA A 171     7648  14154   7363   1229    253   -294       C  
ATOM   1009  O   ALA A 171     -29.406  -8.103 -18.804  1.00 92.66           O  
ANISOU 1009  O   ALA A 171     9665  16230   9309   1349    243   -347       O  
ATOM   1010  CB  ALA A 171     -29.090  -7.180 -21.655  1.00 64.68           C  
ANISOU 1010  CB  ALA A 171     6288  12429   5860   1235     74   -358       C  
ATOM   1011  N   ASP A 172     -29.585 -10.073 -19.872  1.00 69.16           N  
ANISOU 1011  N   ASP A 172     6570  13256   6452   1159    322   -225       N  
ATOM   1012  CA  ASP A 172     -30.374 -10.686 -18.814  1.00 66.84           C  
ANISOU 1012  CA  ASP A 172     6134  13121   6140   1200    401   -177       C  
ATOM   1013  C   ASP A 172     -30.022 -12.164 -18.690  1.00 71.39           C  
ANISOU 1013  C   ASP A 172     6658  13670   6800   1065    446    -71       C  
ATOM   1014  O   ASP A 172     -30.167 -12.920 -19.660  1.00 73.13           O  
ANISOU 1014  O   ASP A 172     6830  13856   7098    982    443    -48       O  
ATOM   1015  CB  ASP A 172     -31.867 -10.503 -19.088  1.00 65.42           C  
ANISOU 1015  CB  ASP A 172     5852  13033   5971   1272    390   -190       C  
ATOM   1016  CG  ASP A 172     -32.730 -11.336 -18.169  1.00 76.63           C  
ANISOU 1016  CG  ASP A 172     7164  14538   7414   1253    429    -94       C  
ATOM   1017  OD1 ASP A 172     -33.039 -10.861 -17.056  1.00 84.81           O  
ANISOU 1017  OD1 ASP A 172     8195  15658   8372   1351    436   -105       O  
ATOM   1018  OD2 ASP A 172     -33.102 -12.460 -18.562  1.00 77.31           O  
ANISOU 1018  OD2 ASP A 172     7171  14610   7594   1141    446     -7       O  
ATOM   1019  N   PRO A 173     -29.566 -12.615 -17.517  1.00 77.09           N  
ANISOU 1019  N   PRO A 173     7384  14396   7511   1044    475    -10       N  
ATOM   1020  CA  PRO A 173     -29.158 -14.021 -17.386  1.00 76.21           C  
ANISOU 1020  CA  PRO A 173     7229  14242   7485    919    505     93       C  
ATOM   1021  C   PRO A 173     -30.321 -15.000 -17.381  1.00 75.12           C  
ANISOU 1021  C   PRO A 173     6957  14161   7425    869    521    188       C  
ATOM   1022  O   PRO A 173     -30.108 -16.178 -17.697  1.00 77.70           O  
ANISOU 1022  O   PRO A 173     7229  14442   7851    762    528    257       O  
ATOM   1023  CB  PRO A 173     -28.400 -14.035 -16.055  1.00 75.02           C  
ANISOU 1023  CB  PRO A 173     7120  14100   7285    933    524    130       C  
ATOM   1024  CG  PRO A 173     -29.104 -12.998 -15.243  1.00 78.08           C  
ANISOU 1024  CG  PRO A 173     7503  14588   7574   1068    513     82       C  
ATOM   1025  CD  PRO A 173     -29.524 -11.911 -16.223  1.00 80.44           C  
ANISOU 1025  CD  PRO A 173     7835  14884   7844   1146    475    -32       C  
ATOM   1026  N   GLN A 174     -31.539 -14.562 -17.043  1.00 68.00           N  
ANISOU 1026  N   GLN A 174     5991  13360   6487    943    521    194       N  
ATOM   1027  CA  GLN A 174     -32.684 -15.465 -17.114  1.00 60.49           C  
ANISOU 1027  CA  GLN A 174     4902  12465   5615    882    531    297       C  
ATOM   1028  C   GLN A 174     -32.921 -15.933 -18.544  1.00 67.83           C  
ANISOU 1028  C   GLN A 174     5790  13328   6653    813    493    268       C  
ATOM   1029  O   GLN A 174     -33.316 -17.083 -18.773  1.00 73.88           O  
ANISOU 1029  O   GLN A 174     6451  14082   7538    712    484    358       O  
ATOM   1030  CB  GLN A 174     -33.940 -14.786 -16.566  1.00 67.13           C  
ANISOU 1030  CB  GLN A 174     5683  13440   6382    987    535    296       C  
ATOM   1031  CG  GLN A 174     -33.697 -13.689 -15.543  1.00 78.68           C  
ANISOU 1031  CG  GLN A 174     7216  14972   7705   1124    537    227       C  
ATOM   1032  CD  GLN A 174     -34.977 -12.961 -15.167  1.00 90.51           C  
ANISOU 1032  CD  GLN A 174     8650  16615   9126   1251    531    199       C  
ATOM   1033  OE1 GLN A 174     -35.168 -11.795 -15.513  1.00100.10           O  
ANISOU 1033  OE1 GLN A 174     9914  17840  10281   1376    493     67       O  
ATOM   1034  NE2 GLN A 174     -35.863 -13.650 -14.457  1.00 79.57           N  
ANISOU 1034  NE2 GLN A 174     7145  15347   7739   1222    565    327       N  
ATOM   1035  N   MET A 175     -32.689 -15.052 -19.520  1.00 66.88           N  
ANISOU 1035  N   MET A 175     5742  13173   6498    870    459    145       N  
ATOM   1036  CA  MET A 175     -32.837 -15.433 -20.921  1.00 63.30           C  
ANISOU 1036  CA  MET A 175     5250  12672   6128    819    413    103       C  
ATOM   1037  C   MET A 175     -31.857 -16.539 -21.293  1.00 64.14           C  
ANISOU 1037  C   MET A 175     5391  12657   6324    706    394    125       C  
ATOM   1038  O   MET A 175     -32.231 -17.530 -21.933  1.00 67.47           O  
ANISOU 1038  O   MET A 175     5750  13019   6866    626    343    150       O  
ATOM   1039  CB  MET A 175     -32.636 -14.209 -21.816  1.00 65.47           C  
ANISOU 1039  CB  MET A 175     5656  12885   6337    891    360    -18       C  
ATOM   1040  CG  MET A 175     -33.188 -14.368 -23.222  1.00 75.72           C  
ANISOU 1040  CG  MET A 175     6954  14113   7702    858    282    -62       C  
ATOM   1041  SD  MET A 175     -34.986 -14.492 -23.264  1.00 79.83           S  
ANISOU 1041  SD  MET A 175     7306  14752   8275    889    268    -24       S  
ATOM   1042  CE  MET A 175     -35.446 -12.807 -22.870  1.00 81.47           C  
ANISOU 1042  CE  MET A 175     7561  15044   8352   1057    271    -97       C  
ATOM   1043  N   LEU A 176     -30.591 -16.385 -20.896  1.00 59.96           N  
ANISOU 1043  N   LEU A 176     4960  12082   5739    705    422    109       N  
ATOM   1044  CA  LEU A 176     -29.601 -17.422 -21.162  1.00 63.32           C  
ANISOU 1044  CA  LEU A 176     5417  12400   6240    616    404    123       C  
ATOM   1045  C   LEU A 176     -29.936 -18.714 -20.429  1.00 70.47           C  
ANISOU 1045  C   LEU A 176     6193  13327   7254    538    418    249       C  
ATOM   1046  O   LEU A 176     -29.654 -19.807 -20.937  1.00 63.12           O  
ANISOU 1046  O   LEU A 176     5250  12289   6445    459    362    259       O  
ATOM   1047  CB  LEU A 176     -28.210 -16.923 -20.773  1.00 55.42           C  
ANISOU 1047  CB  LEU A 176     4535  11370   5153    636    435     92       C  
ATOM   1048  CG  LEU A 176     -27.854 -15.525 -21.285  1.00 51.35           C  
ANISOU 1048  CG  LEU A 176     4140  10838   4533    704    414      0       C  
ATOM   1049  CD1 LEU A 176     -26.788 -14.879 -20.416  1.00 47.48           C  
ANISOU 1049  CD1 LEU A 176     3730  10357   3953    734    449     -2       C  
ATOM   1050  CD2 LEU A 176     -27.402 -15.588 -22.736  1.00 46.18           C  
ANISOU 1050  CD2 LEU A 176     3555  10093   3900    671    353    -69       C  
ATOM   1051  N   ARG A 177     -30.540 -18.612 -19.242  1.00 75.72           N  
ANISOU 1051  N   ARG A 177     6777  14113   7881    560    476    348       N  
ATOM   1052  CA  ARG A 177     -30.987 -19.807 -18.534  1.00 73.74           C  
ANISOU 1052  CA  ARG A 177     6402  13882   7736    472    479    502       C  
ATOM   1053  C   ARG A 177     -32.107 -20.508 -19.293  1.00 69.12           C  
ANISOU 1053  C   ARG A 177     5677  13298   7289    409    416    540       C  
ATOM   1054  O   ARG A 177     -32.153 -21.743 -19.343  1.00 64.80           O  
ANISOU 1054  O   ARG A 177     5051  12675   6895    302    361    629       O  
ATOM   1055  CB  ARG A 177     -31.438 -19.439 -17.120  1.00 82.21           C  
ANISOU 1055  CB  ARG A 177     7472  15052   8713    515    535    596       C  
ATOM   1056  CG  ARG A 177     -30.312 -18.947 -16.219  1.00 90.58           C  
ANISOU 1056  CG  ARG A 177     8650  16104   9661    564    571    574       C  
ATOM   1057  CD  ARG A 177     -30.728 -18.920 -14.757  1.00 95.67           C  
ANISOU 1057  CD  ARG A 177     9258  16860  10231    594    609    685       C  
ATOM   1058  NE  ARG A 177     -29.857 -18.058 -13.962  1.00 91.97           N  
ANISOU 1058  NE  ARG A 177     8907  16401   9635    680    623    618       N  
ATOM   1059  CZ  ARG A 177     -30.255 -16.939 -13.365  1.00 94.00           C  
ANISOU 1059  CZ  ARG A 177     9200  16746   9769    801    623    554       C  
ATOM   1060  NH1 ARG A 177     -31.515 -16.539 -13.472  1.00 92.84           N  
ANISOU 1060  NH1 ARG A 177     8986  16693   9596    857    621    549       N  
ATOM   1061  NH2 ARG A 177     -29.392 -16.217 -12.662  1.00 94.54           N  
ANISOU 1061  NH2 ARG A 177     9363  16812   9746    872    619    489       N  
ATOM   1062  N   TYR A 178     -33.015 -19.737 -19.896  1.00 65.93           N  
ANISOU 1062  N   TYR A 178     5269  12936   6846    469    400    472       N  
ATOM   1063  CA  TYR A 178     -34.091 -20.327 -20.688  1.00 66.56           C  
ANISOU 1063  CA  TYR A 178     5232  13001   7056    410    323    494       C  
ATOM   1064  C   TYR A 178     -33.541 -21.008 -21.935  1.00 71.28           C  
ANISOU 1064  C   TYR A 178     5918  13399   7765    352    216    397       C  
ATOM   1065  O   TYR A 178     -33.884 -22.159 -22.230  1.00 73.52           O  
ANISOU 1065  O   TYR A 178     6124  13594   8215    254    130    452       O  
ATOM   1066  CB  TYR A 178     -35.110 -19.250 -21.065  1.00 73.82           C  
ANISOU 1066  CB  TYR A 178     6150  14003   7895    503    327    429       C  
ATOM   1067  CG  TYR A 178     -36.371 -19.781 -21.714  1.00 83.52           C  
ANISOU 1067  CG  TYR A 178     7244  15242   9247    447    254    469       C  
ATOM   1068  CD1 TYR A 178     -36.780 -21.095 -21.521  1.00 84.81           C  
ANISOU 1068  CD1 TYR A 178     7272  15374   9578    318    204    606       C  
ATOM   1069  CD2 TYR A 178     -37.148 -18.968 -22.529  1.00 85.64           C  
ANISOU 1069  CD2 TYR A 178     7518  15545   9477    520    221    376       C  
ATOM   1070  CE1 TYR A 178     -37.929 -21.582 -22.116  1.00 84.07           C  
ANISOU 1070  CE1 TYR A 178     7054  15277   9611    257    120    647       C  
ATOM   1071  CE2 TYR A 178     -38.298 -19.445 -23.129  1.00 84.55           C  
ANISOU 1071  CE2 TYR A 178     7259  15412   9452    468    146    410       C  
ATOM   1072  CZ  TYR A 178     -38.684 -20.752 -22.919  1.00 86.42           C  
ANISOU 1072  CZ  TYR A 178     7366  15613   9858    334     95    544       C  
ATOM   1073  OH  TYR A 178     -39.828 -21.232 -23.514  1.00 88.31           O  
ANISOU 1073  OH  TYR A 178     7483  15847  10224    273      6    582       O  
ATOM   1074  N   PHE A 179     -32.685 -20.306 -22.683  1.00 73.80           N  
ANISOU 1074  N   PHE A 179     6396  13651   7995    414    210    252       N  
ATOM   1075  CA  PHE A 179     -32.104 -20.894 -23.885  1.00 63.58           C  
ANISOU 1075  CA  PHE A 179     5180  12205   6772    382    115    146       C  
ATOM   1076  C   PHE A 179     -31.272 -22.125 -23.557  1.00 57.74           C  
ANISOU 1076  C   PHE A 179     4437  11358   6142    308     84    189       C  
ATOM   1077  O   PHE A 179     -31.209 -23.064 -24.359  1.00 53.11           O  
ANISOU 1077  O   PHE A 179     3851  10647   5680    264    -24    136       O  
ATOM   1078  CB  PHE A 179     -31.264 -19.855 -24.626  1.00 59.34           C  
ANISOU 1078  CB  PHE A 179     4796  11655   6095    460    130     15       C  
ATOM   1079  CG  PHE A 179     -32.065 -18.702 -25.161  1.00 71.44           C  
ANISOU 1079  CG  PHE A 179     6343  13257   7543    531    128    -37       C  
ATOM   1080  CD1 PHE A 179     -33.415 -18.851 -25.439  1.00 74.41           C  
ANISOU 1080  CD1 PHE A 179     6612  13673   7988    522     84    -12       C  
ATOM   1081  CD2 PHE A 179     -31.470 -17.473 -25.390  1.00 75.41           C  
ANISOU 1081  CD2 PHE A 179     6964  13781   7907    603    157   -101       C  
ATOM   1082  CE1 PHE A 179     -34.156 -17.795 -25.932  1.00 73.95           C  
ANISOU 1082  CE1 PHE A 179     6566  13675   7856    595     74    -61       C  
ATOM   1083  CE2 PHE A 179     -32.207 -16.413 -25.885  1.00 79.49           C  
ANISOU 1083  CE2 PHE A 179     7498  14344   8359    669    137   -143       C  
ATOM   1084  CZ  PHE A 179     -33.552 -16.574 -26.155  1.00 77.87           C  
ANISOU 1084  CZ  PHE A 179     7188  14180   8218    672     98   -128       C  
ATOM   1085  N   ALA A 180     -30.632 -22.143 -22.386  1.00 63.33           N  
ANISOU 1085  N   ALA A 180     5144  12111   6807    302    165    278       N  
ATOM   1086  CA  ALA A 180     -29.982 -23.365 -21.928  1.00 69.94           C  
ANISOU 1086  CA  ALA A 180     5957  12851   7764    227    129    349       C  
ATOM   1087  C   ALA A 180     -31.003 -24.438 -21.575  1.00 79.80           C  
ANISOU 1087  C   ALA A 180     7050  14080   9191    126     63    494       C  
ATOM   1088  O   ALA A 180     -30.715 -25.633 -21.709  1.00 71.46           O  
ANISOU 1088  O   ALA A 180     5974  12880   8297     53    -36    521       O  
ATOM   1089  CB  ALA A 180     -29.084 -23.068 -20.727  1.00 69.53           C  
ANISOU 1089  CB  ALA A 180     5937  12867   7613    247    230    418       C  
ATOM   1090  N   SER A 181     -32.196 -24.035 -21.128  1.00 90.17           N  
ANISOU 1090  N   SER A 181     8245  15535  10482    122    106    592       N  
ATOM   1091  CA  SER A 181     -33.227 -25.011 -20.789  1.00 88.94           C  
ANISOU 1091  CA  SER A 181     7918  15381  10494     12     42    758       C  
ATOM   1092  C   SER A 181     -33.753 -25.713 -22.034  1.00 96.17           C  
ANISOU 1092  C   SER A 181     8823  16141  11578    -40   -115    677       C  
ATOM   1093  O   SER A 181     -33.914 -26.939 -22.039  1.00 97.15           O  
ANISOU 1093  O   SER A 181     8874  16134  11902   -147   -232    761       O  
ATOM   1094  CB  SER A 181     -34.372 -24.333 -20.035  1.00 86.62           C  
ANISOU 1094  CB  SER A 181     7486  15314  10111     36    135    876       C  
ATOM   1095  OG  SER A 181     -33.887 -23.312 -19.182  1.00 98.69           O  
ANISOU 1095  OG  SER A 181     9067  16994  11438    138    271    865       O  
ATOM   1096  N   ILE A 182     -34.027 -24.958 -23.097  1.00104.78           N  
ANISOU 1096  N   ILE A 182     9984  17235  12594     36   -133    516       N  
ATOM   1097  CA  ILE A 182     -34.487 -25.552 -24.348  1.00107.15           C  
ANISOU 1097  CA  ILE A 182    10284  17399  13029      5   -286    414       C  
ATOM   1098  C   ILE A 182     -33.332 -26.287 -25.014  1.00104.62           C  
ANISOU 1098  C   ILE A 182    10084  16896  12770     13   -379    281       C  
ATOM   1099  O   ILE A 182     -33.073 -27.461 -24.726  1.00119.79           O  
ANISOU 1099  O   ILE A 182    11967  18684  14861    -67   -471    346       O  
ATOM   1100  CB  ILE A 182     -35.069 -24.491 -25.299  1.00110.47           C  
ANISOU 1100  CB  ILE A 182    10748  17893  13333     93   -277    283       C  
ATOM   1101  CG1 ILE A 182     -35.747 -23.369 -24.511  1.00109.05           C  
ANISOU 1101  CG1 ILE A 182    10505  17918  13011    148   -144    367       C  
ATOM   1102  CG2 ILE A 182     -36.029 -25.134 -26.287  1.00119.78           C  
ANISOU 1102  CG2 ILE A 182    11858  18986  14666     42   -432    242       C  
ATOM   1103  CD1 ILE A 182     -36.218 -22.220 -25.374  1.00111.56           C  
ANISOU 1103  CD1 ILE A 182    10880  18300  13209    246   -136    242       C  
ATOM   1104  N   GLY A 183     -32.640 -25.595 -25.912  1.00 88.37           N  
ANISOU 1104  N   GLY A 183     8164  14838  10574    113   -362    100       N  
ATOM   1105  CA  GLY A 183     -31.514 -26.150 -26.633  1.00 69.51           C  
ANISOU 1105  CA  GLY A 183     5885  12322   8202    149   -435    -47       C  
ATOM   1106  C   GLY A 183     -30.866 -25.081 -27.484  1.00 68.59           C  
ANISOU 1106  C   GLY A 183     5896  12281   7885    258   -376   -200       C  
ATOM   1107  O   GLY A 183     -30.020 -25.369 -28.336  1.00 84.56           O  
ANISOU 1107  O   GLY A 183     8003  14245   9882    311   -433   -345       O  
ATOM   1108  N   ILE A 184     -31.269 -23.832 -27.255  1.00 57.15           N  
ANISOU 1108  N   ILE A 184     4453  10969   6292    297   -268   -164       N  
ATOM   1109  CA  ILE A 184     -30.749 -22.692 -27.998  1.00 60.41           C  
ANISOU 1109  CA  ILE A 184     4978  11455   6521    385   -219   -273       C  
ATOM   1110  C   ILE A 184     -29.360 -22.349 -27.478  1.00 70.81           C  
ANISOU 1110  C   ILE A 184     6383  12790   7731    414   -129   -272       C  
ATOM   1111  O   ILE A 184     -29.207 -21.533 -26.562  1.00 76.16           O  
ANISOU 1111  O   ILE A 184     7073  13547   8319    425    -23   -192       O  
ATOM   1112  CB  ILE A 184     -31.693 -21.479 -27.899  1.00 63.38           C  
ANISOU 1112  CB  ILE A 184     5331  11948   6803    419   -159   -234       C  
ATOM   1113  CG1 ILE A 184     -33.084 -21.843 -28.417  1.00 66.17           C  
ANISOU 1113  CG1 ILE A 184     5582  12292   7265    389   -251   -230       C  
ATOM   1114  CG2 ILE A 184     -31.145 -20.306 -28.698  1.00 67.40           C  
ANISOU 1114  CG2 ILE A 184     5956  12513   7141    498   -129   -327       C  
ATOM   1115  CD1 ILE A 184     -33.095 -22.252 -29.866  1.00 64.60           C  
ANISOU 1115  CD1 ILE A 184     5425  12027   7094    410   -375   -377       C  
ATOM   1116  N   SER A 185     -28.345 -22.985 -28.044  1.00 77.59           N  
ANISOU 1116  N   SER A 185     7299  13583   8599    432   -177   -367       N  
ATOM   1117  CA  SER A 185     -26.955 -22.644 -27.794  1.00 83.89           C  
ANISOU 1117  CA  SER A 185     8180  14410   9286    465   -104   -383       C  
ATOM   1118  C   SER A 185     -26.395 -21.933 -29.020  1.00 83.74           C  
ANISOU 1118  C   SER A 185     8242  14456   9119    535   -109   -501       C  
ATOM   1119  O   SER A 185     -27.107 -21.669 -29.994  1.00 84.81           O  
ANISOU 1119  O   SER A 185     8375  14618   9232    560   -165   -566       O  
ATOM   1120  CB  SER A 185     -26.142 -23.895 -27.454  1.00 89.98           C  
ANISOU 1120  CB  SER A 185     8942  15079  10169    444   -150   -391       C  
ATOM   1121  OG  SER A 185     -26.282 -24.881 -28.462  1.00 94.63           O  
ANISOU 1121  OG  SER A 185     9519  15577  10859    461   -286   -513       O  
ATOM   1122  N   LEU A 186     -25.106 -21.616 -28.969  1.00 82.11           N  
ANISOU 1122  N   LEU A 186     8100  14290   8807    562    -53   -517       N  
ATOM   1123  CA  LEU A 186     -24.453 -21.053 -30.139  1.00 74.02           C  
ANISOU 1123  CA  LEU A 186     7136  13350   7640    619    -59   -607       C  
ATOM   1124  C   LEU A 186     -24.320 -22.109 -31.228  1.00 74.84           C  
ANISOU 1124  C   LEU A 186     7224  13426   7786    666   -165   -750       C  
ATOM   1125  O   LEU A 186     -24.237 -23.310 -30.955  1.00 71.71           O  
ANISOU 1125  O   LEU A 186     6794  12925   7528    658   -230   -784       O  
ATOM   1126  CB  LEU A 186     -23.079 -20.492 -29.778  1.00 71.38           C  
ANISOU 1126  CB  LEU A 186     6855  13077   7190    628     24   -573       C  
ATOM   1127  CG  LEU A 186     -22.993 -18.965 -29.817  1.00 73.44           C  
ANISOU 1127  CG  LEU A 186     7168  13422   7313    626     83   -509       C  
ATOM   1128  CD1 LEU A 186     -24.087 -18.341 -28.962  1.00 77.63           C  
ANISOU 1128  CD1 LEU A 186     7685  13925   7888    600    108   -428       C  
ATOM   1129  CD2 LEU A 186     -21.616 -18.492 -29.380  1.00 72.26           C  
ANISOU 1129  CD2 LEU A 186     7063  13319   7074    618    149   -463       C  
ATOM   1130  N   ASP A 187     -24.324 -21.645 -32.474  1.00 80.78           N  
ANISOU 1130  N   ASP A 187     8002  14274   8419    721   -196   -834       N  
ATOM   1131  CA  ASP A 187     -24.214 -22.474 -33.671  1.00 87.03           C  
ANISOU 1131  CA  ASP A 187     8783  15079   9207    793   -301   -994       C  
ATOM   1132  C   ASP A 187     -25.403 -23.412 -33.857  1.00 90.12           C  
ANISOU 1132  C   ASP A 187     9122  15346   9772    777   -427  -1052       C  
ATOM   1133  O   ASP A 187     -25.379 -24.263 -34.754  1.00 98.82           O  
ANISOU 1133  O   ASP A 187    10216  16427  10905    841   -543  -1204       O  
ATOM   1134  CB  ASP A 187     -22.901 -23.276 -33.681  1.00 93.53           C  
ANISOU 1134  CB  ASP A 187     9615  15906  10017    846   -307  -1071       C  
ATOM   1135  CG  ASP A 187     -21.675 -22.385 -33.767  1.00 91.10           C  
ANISOU 1135  CG  ASP A 187     9343  15749   9521    866   -201  -1025       C  
ATOM   1136  OD1 ASP A 187     -21.749 -21.341 -34.446  1.00 88.77           O  
ANISOU 1136  OD1 ASP A 187     9069  15581   9079    874   -167   -996       O  
ATOM   1137  OD2 ASP A 187     -20.637 -22.727 -33.161  1.00 83.40           O  
ANISOU 1137  OD2 ASP A 187     8371  14764   8552    870   -158  -1009       O  
ATOM   1138  N   SER A 188     -26.445 -23.282 -33.039  1.00 88.32           N  
ANISOU 1138  N   SER A 188     8853  15045   9659    699   -414   -939       N  
ATOM   1139  CA  SER A 188     -27.655 -24.064 -33.248  1.00 90.73           C  
ANISOU 1139  CA  SER A 188     9094  15247  10131    668   -537   -970       C  
ATOM   1140  C   SER A 188     -28.366 -23.592 -34.510  1.00 84.80           C  
ANISOU 1140  C   SER A 188     8349  14574   9297    717   -599  -1060       C  
ATOM   1141  O   SER A 188     -28.404 -22.396 -34.810  1.00 81.99           O  
ANISOU 1141  O   SER A 188     8028  14339   8786    736   -523  -1021       O  
ATOM   1142  CB  SER A 188     -28.584 -23.949 -32.040  1.00 93.69           C  
ANISOU 1142  CB  SER A 188     9403  15570  10624    573   -492   -803       C  
ATOM   1143  OG  SER A 188     -28.017 -24.571 -30.899  1.00 95.08           O  
ANISOU 1143  OG  SER A 188     9561  15671  10893    524   -457   -717       O  
ATOM   1144  N   ARG A 189     -28.918 -24.540 -35.261  1.00 87.13           N  
ANISOU 1144  N   ARG A 189     8612  14794   9700    738   -752  -1183       N  
ATOM   1145  CA  ARG A 189     -29.603 -24.241 -36.512  1.00 86.17           C  
ANISOU 1145  CA  ARG A 189     8490  14744   9504    791   -833  -1286       C  
ATOM   1146  C   ARG A 189     -31.108 -24.263 -36.277  1.00 76.53           C  
ANISOU 1146  C   ARG A 189     7195  13457   8426    717   -890  -1214       C  
ATOM   1147  O   ARG A 189     -31.653 -25.262 -35.796  1.00 76.32           O  
ANISOU 1147  O   ARG A 189     7102  13286   8609    651   -983  -1192       O  
ATOM   1148  CB  ARG A 189     -29.200 -25.229 -37.607  1.00 90.29           C  
ANISOU 1148  CB  ARG A 189     9027  15248  10030    885   -979  -1497       C  
ATOM   1149  CG  ARG A 189     -27.982 -24.773 -38.401  1.00 98.54           C  
ANISOU 1149  CG  ARG A 189    10133  16468  10839    994   -919  -1586       C  
ATOM   1150  CD  ARG A 189     -26.980 -25.894 -38.626  1.00111.44           C  
ANISOU 1150  CD  ARG A 189    11779  18060  12504   1078   -996  -1741       C  
ATOM   1151  NE  ARG A 189     -27.528 -26.973 -39.441  1.00122.42           N  
ANISOU 1151  NE  ARG A 189    13149  19359  14008   1140  -1198  -1931       N  
ATOM   1152  CZ  ARG A 189     -27.589 -28.243 -39.055  1.00131.88           C  
ANISOU 1152  CZ  ARG A 189    14325  20353  15430   1127  -1335  -1998       C  
ATOM   1153  NH1 ARG A 189     -27.132 -28.598 -37.862  1.00132.18           N  
ANISOU 1153  NH1 ARG A 189    14356  20273  15592   1053  -1279  -1880       N  
ATOM   1154  NH2 ARG A 189     -28.105 -29.159 -39.863  1.00137.75           N  
ANISOU 1154  NH2 ARG A 189    15055  21006  16279   1188  -1541  -2182       N  
ATOM   1155  N   LEU A 190     -31.769 -23.159 -36.615  1.00 67.26           N  
ANISOU 1155  N   LEU A 190     6023  12389   7143    725   -842  -1166       N  
ATOM   1156  CA  LEU A 190     -33.193 -22.979 -36.384  1.00 73.70           C  
ANISOU 1156  CA  LEU A 190     6760  13180   8064    667   -876  -1088       C  
ATOM   1157  C   LEU A 190     -33.940 -22.938 -37.709  1.00 86.06           C  
ANISOU 1157  C   LEU A 190     8318  14787   9594    718   -999  -1208       C  
ATOM   1158  O   LEU A 190     -33.446 -22.380 -38.697  1.00 96.15           O  
ANISOU 1158  O   LEU A 190     9662  16181  10691    801   -994  -1294       O  
ATOM   1159  CB  LEU A 190     -33.461 -21.688 -35.605  1.00 64.20           C  
ANISOU 1159  CB  LEU A 190     5560  12062   6773    648   -731   -937       C  
ATOM   1160  CG  LEU A 190     -32.832 -21.592 -34.216  1.00 56.92           C  
ANISOU 1160  CG  LEU A 190     4641  11118   5870    604   -606   -813       C  
ATOM   1161  CD1 LEU A 190     -33.345 -20.365 -33.476  1.00 52.05           C  
ANISOU 1161  CD1 LEU A 190     4013  10580   5184    601   -497   -690       C  
ATOM   1162  CD2 LEU A 190     -33.106 -22.859 -33.427  1.00 51.66           C  
ANISOU 1162  CD2 LEU A 190     3890  10327   5413    524   -661   -764       C  
ATOM   1163  N   ARG A 191     -35.134 -23.531 -37.720  1.00 83.13           N  
ANISOU 1163  N   ARG A 191     7857  14334   9395    664  -1113  -1202       N  
ATOM   1164  CA  ARG A 191     -36.046 -23.459 -38.859  1.00 83.29           C  
ANISOU 1164  CA  ARG A 191     7853  14390   9402    700  -1236  -1298       C  
ATOM   1165  C   ARG A 191     -37.343 -22.811 -38.393  1.00 80.68           C  
ANISOU 1165  C   ARG A 191     7438  14091   9127    644  -1205  -1162       C  
ATOM   1166  O   ARG A 191     -38.123 -23.430 -37.660  1.00 85.07           O  
ANISOU 1166  O   ARG A 191     7888  14561   9874    553  -1245  -1073       O  
ATOM   1167  CB  ARG A 191     -36.312 -24.842 -39.452  1.00 84.51           C  
ANISOU 1167  CB  ARG A 191     7973  14414   9724    696  -1440  -1442       C  
ATOM   1168  CG  ARG A 191     -37.279 -24.818 -40.629  1.00 82.09           C  
ANISOU 1168  CG  ARG A 191     7639  14143   9408    735  -1584  -1552       C  
ATOM   1169  CD  ARG A 191     -38.015 -26.140 -40.790  1.00 87.86           C  
ANISOU 1169  CD  ARG A 191     8293  14701  10389    679  -1798  -1627       C  
ATOM   1170  NE  ARG A 191     -37.106 -27.276 -40.920  1.00 91.79           N  
ANISOU 1170  NE  ARG A 191     8835  15077  10965    715  -1903  -1765       N  
ATOM   1171  CZ  ARG A 191     -36.438 -27.577 -42.029  1.00101.98           C  
ANISOU 1171  CZ  ARG A 191    10200  16411  12135    845  -1995  -1986       C  
ATOM   1172  NH1 ARG A 191     -36.577 -26.830 -43.116  1.00100.24           N  
ANISOU 1172  NH1 ARG A 191    10016  16363  11707    941  -1992  -2077       N  
ATOM   1173  NH2 ARG A 191     -35.633 -28.631 -42.054  1.00110.34           N  
ANISOU 1173  NH2 ARG A 191    11294  17353  13278    889  -2095  -2116       N  
ATOM   1174  N   VAL A 192     -37.578 -21.570 -38.820  1.00 66.70           N  
ANISOU 1174  N   VAL A 192     5703  12450   7191    699  -1139  -1140       N  
ATOM   1175  CA  VAL A 192     -38.784 -20.855 -38.420  1.00 63.52           C  
ANISOU 1175  CA  VAL A 192     5221  12092   6821    672  -1109  -1027       C  
ATOM   1176  C   VAL A 192     -40.004 -21.547 -39.011  1.00 78.38           C  
ANISOU 1176  C   VAL A 192     7003  13929   8848    639  -1273  -1077       C  
ATOM   1177  O   VAL A 192     -40.080 -21.782 -40.225  1.00 94.69           O  
ANISOU 1177  O   VAL A 192     9100  16006  10872    691  -1396  -1219       O  
ATOM   1178  CB  VAL A 192     -38.710 -19.385 -38.857  1.00 62.44           C  
ANISOU 1178  CB  VAL A 192     5157  12083   6484    748  -1032  -1006       C  
ATOM   1179  CG1 VAL A 192     -40.000 -18.661 -38.498  1.00 69.03           C  
ANISOU 1179  CG1 VAL A 192     5908  12965   7356    743  -1019   -912       C  
ATOM   1180  CG2 VAL A 192     -37.512 -18.701 -38.217  1.00 58.39           C  
ANISOU 1180  CG2 VAL A 192     4737  11600   5849    766   -888   -945       C  
ATOM   1181  N   LEU A 193     -40.968 -21.878 -38.153  1.00 70.36           N  
ANISOU 1181  N   LEU A 193     5857  12875   8000    554  -1278   -957       N  
ATOM   1182  CA  LEU A 193     -42.192 -22.556 -38.564  1.00 68.24           C  
ANISOU 1182  CA  LEU A 193     5471  12560   7899    500  -1436   -972       C  
ATOM   1183  C   LEU A 193     -43.392 -21.620 -38.622  1.00 78.57           C  
ANISOU 1183  C   LEU A 193     6699  13984   9171    520  -1413   -899       C  
ATOM   1184  O   LEU A 193     -44.074 -21.549 -39.649  1.00 86.45           O  
ANISOU 1184  O   LEU A 193     7682  15006  10160    552  -1533   -986       O  
ATOM   1185  CB  LEU A 193     -42.491 -23.724 -37.617  1.00 61.42           C  
ANISOU 1185  CB  LEU A 193     4489  11575   7272    373  -1484   -868       C  
ATOM   1186  CG  LEU A 193     -41.433 -24.825 -37.536  1.00 59.59           C  
ANISOU 1186  CG  LEU A 193     4319  11197   7124    347  -1545   -940       C  
ATOM   1187  CD1 LEU A 193     -41.941 -25.995 -36.711  1.00 57.56           C  
ANISOU 1187  CD1 LEU A 193     3930  10808   7132    207  -1633   -818       C  
ATOM   1188  CD2 LEU A 193     -41.042 -25.282 -38.930  1.00 60.50           C  
ANISOU 1188  CD2 LEU A 193     4525  11263   7200    427  -1702  -1167       C  
ATOM   1189  N   ALA A 194     -43.667 -20.898 -37.539  1.00 76.12           N  
ANISOU 1189  N   ALA A 194     6336  13752   8834    513  -1268   -751       N  
ATOM   1190  CA  ALA A 194     -44.829 -20.025 -37.457  1.00 67.52           C  
ANISOU 1190  CA  ALA A 194     5157  12779   7718    545  -1244   -681       C  
ATOM   1191  C   ALA A 194     -44.392 -18.632 -37.033  1.00 70.90           C  
ANISOU 1191  C   ALA A 194     5673  13305   7961    640  -1090   -643       C  
ATOM   1192  O   ALA A 194     -43.590 -18.486 -36.105  1.00 79.61           O  
ANISOU 1192  O   ALA A 194     6820  14404   9024    636   -969   -584       O  
ATOM   1193  CB  ALA A 194     -45.867 -20.576 -36.474  1.00 81.22           C  
ANISOU 1193  CB  ALA A 194     6696  14535   9630    449  -1243   -529       C  
ATOM   1194  N   ARG A 195     -44.915 -17.618 -37.717  1.00 74.67           N  
ANISOU 1194  N   ARG A 195     6177  13861   8333    726  -1111   -677       N  
ATOM   1195  CA  ARG A 195     -44.712 -16.212 -37.368  1.00 82.27           C  
ANISOU 1195  CA  ARG A 195     7213  14901   9145    821  -1002   -639       C  
ATOM   1196  C   ARG A 195     -46.075 -15.636 -36.997  1.00 89.40           C  
ANISOU 1196  C   ARG A 195     7981  15903  10084    861  -1000   -571       C  
ATOM   1197  O   ARG A 195     -46.765 -15.035 -37.824  1.00 86.85           O  
ANISOU 1197  O   ARG A 195     7655  15624   9719    922  -1075   -611       O  
ATOM   1198  CB  ARG A 195     -44.055 -15.438 -38.523  1.00 88.29           C  
ANISOU 1198  CB  ARG A 195     8131  15669   9746    895  -1037   -727       C  
ATOM   1199  CG  ARG A 195     -43.880 -13.950 -38.255  1.00 88.24           C  
ANISOU 1199  CG  ARG A 195     8205  15715   9607    986   -961   -682       C  
ATOM   1200  CD  ARG A 195     -42.683 -13.653 -37.373  1.00 81.18           C  
ANISOU 1200  CD  ARG A 195     7404  14789   8651    983   -840   -642       C  
ATOM   1201  NE  ARG A 195     -42.628 -12.237 -37.023  1.00 88.07           N  
ANISOU 1201  NE  ARG A 195     8344  15692   9426   1070   -793   -601       N  
ATOM   1202  CZ  ARG A 195     -42.059 -11.302 -37.776  1.00 99.82           C  
ANISOU 1202  CZ  ARG A 195     9959  17174  10793   1116   -822   -614       C  
ATOM   1203  NH1 ARG A 195     -41.490 -11.630 -38.928  1.00 98.71           N  
ANISOU 1203  NH1 ARG A 195     9882  17032  10589   1090   -881   -665       N  
ATOM   1204  NH2 ARG A 195     -42.056 -10.037 -37.377  1.00107.81           N  
ANISOU 1204  NH2 ARG A 195    11029  18187  11746   1191   -801   -573       N  
ATOM   1205  N   ARG A 196     -46.467 -15.837 -35.741  1.00 91.30           N  
ANISOU 1205  N   ARG A 196     8100  16194  10396    832   -915   -464       N  
ATOM   1206  CA  ARG A 196     -47.743 -15.347 -35.227  1.00 87.92           C  
ANISOU 1206  CA  ARG A 196     7516  15894   9994    879   -897   -391       C  
ATOM   1207  C   ARG A 196     -47.488 -14.010 -34.540  1.00 88.88           C  
ANISOU 1207  C   ARG A 196     7708  16085   9976   1007   -788   -379       C  
ATOM   1208  O   ARG A 196     -47.275 -13.940 -33.329  1.00 90.82           O  
ANISOU 1208  O   ARG A 196     7914  16386  10207   1018   -676   -309       O  
ATOM   1209  CB  ARG A 196     -48.379 -16.364 -34.286  1.00 82.83           C  
ANISOU 1209  CB  ARG A 196     6688  15283   9502    774   -871   -268       C  
ATOM   1210  CG  ARG A 196     -48.400 -17.782 -34.836  1.00 80.99           C  
ANISOU 1210  CG  ARG A 196     6394  14947   9432    635   -999   -279       C  
ATOM   1211  CD  ARG A 196     -49.131 -18.732 -33.902  1.00 84.45           C  
ANISOU 1211  CD  ARG A 196     6656  15393  10038    513   -984   -122       C  
ATOM   1212  NE  ARG A 196     -48.670 -20.109 -34.056  1.00 86.14           N  
ANISOU 1212  NE  ARG A 196     6832  15490  10407    378  -1089   -119       N  
ATOM   1213  CZ  ARG A 196     -49.353 -21.058 -34.688  1.00 95.37           C  
ANISOU 1213  CZ  ARG A 196     7903  16583  11750    278  -1255   -123       C  
ATOM   1214  NH1 ARG A 196     -48.859 -22.285 -34.782  1.00 96.49           N  
ANISOU 1214  NH1 ARG A 196     8059  16561  12043    164  -1355   -131       N  
ATOM   1215  NH2 ARG A 196     -50.531 -20.778 -35.229  1.00101.25           N  
ANISOU 1215  NH2 ARG A 196     8578  17363  12530    294  -1321   -123       N  
ATOM   1216  N   GLU A 197     -47.508 -12.937 -35.333  1.00 91.81           N  
ANISOU 1216  N   GLU A 197     8188  16453  10245   1107   -834   -448       N  
ATOM   1217  CA  GLU A 197     -47.344 -11.600 -34.776  1.00 95.76           C  
ANISOU 1217  CA  GLU A 197     8760  16992  10630   1237   -769   -448       C  
ATOM   1218  C   GLU A 197     -48.537 -11.207 -33.914  1.00 96.56           C  
ANISOU 1218  C   GLU A 197     8707  17225  10755   1317   -726   -397       C  
ATOM   1219  O   GLU A 197     -48.381 -10.452 -32.947  1.00 87.15           O  
ANISOU 1219  O   GLU A 197     7538  16080   9493   1411   -643   -386       O  
ATOM   1220  CB  GLU A 197     -47.135 -10.591 -35.908  1.00 99.34           C  
ANISOU 1220  CB  GLU A 197     9360  17394  10989   1311   -854   -515       C  
ATOM   1221  CG  GLU A 197     -47.109  -9.136 -35.471  1.00111.93           C  
ANISOU 1221  CG  GLU A 197    11032  19004  12493   1451   -832   -520       C  
ATOM   1222  CD  GLU A 197     -46.031  -8.336 -36.176  1.00124.42           C  
ANISOU 1222  CD  GLU A 197    12816  20483  13976   1466   -869   -546       C  
ATOM   1223  OE1 GLU A 197     -45.334  -7.549 -35.502  1.00128.34           O  
ANISOU 1223  OE1 GLU A 197    13408  20939  14415   1518   -822   -537       O  
ATOM   1224  OE2 GLU A 197     -45.881  -8.496 -37.406  1.00128.53           O  
ANISOU 1224  OE2 GLU A 197    13392  20972  14472   1425   -952   -570       O  
ATOM   1225  N   PHE A 198     -49.728 -11.717 -34.239  1.00 96.91           N  
ANISOU 1225  N   PHE A 198     8632  17294  10896   1273   -775   -368       N  
ATOM   1226  CA  PHE A 198     -50.903 -11.437 -33.420  1.00 92.77           C  
ANISOU 1226  CA  PHE A 198     7988  16867  10392   1329   -717   -308       C  
ATOM   1227  C   PHE A 198     -50.744 -12.008 -32.017  1.00 93.94           C  
ANISOU 1227  C   PHE A 198     8066  17068  10560   1276   -588   -210       C  
ATOM   1228  O   PHE A 198     -51.108 -11.360 -31.029  1.00103.15           O  
ANISOU 1228  O   PHE A 198     9207  18329  11657   1377   -501   -187       O  
ATOM   1229  CB  PHE A 198     -52.162 -11.992 -34.094  1.00 87.76           C  
ANISOU 1229  CB  PHE A 198     7228  16247   9870   1269   -804   -282       C  
ATOM   1230  CG  PHE A 198     -52.086 -13.461 -34.424  1.00 73.27           C  
ANISOU 1230  CG  PHE A 198     5320  14344   8176   1092   -860   -239       C  
ATOM   1231  CD1 PHE A 198     -51.520 -13.890 -35.615  1.00 68.10           C  
ANISOU 1231  CD1 PHE A 198     4744  13592   7540   1039   -977   -324       C  
ATOM   1232  CD2 PHE A 198     -52.589 -14.412 -33.549  1.00 63.50           C  
ANISOU 1232  CD2 PHE A 198     3935  13139   7051    984   -810   -115       C  
ATOM   1233  CE1 PHE A 198     -51.450 -15.236 -35.923  1.00 63.45           C  
ANISOU 1233  CE1 PHE A 198     4091  12928   7088    892  -1054   -309       C  
ATOM   1234  CE2 PHE A 198     -52.522 -15.761 -33.853  1.00 60.38           C  
ANISOU 1234  CE2 PHE A 198     3471  12661   6810    821   -890    -75       C  
ATOM   1235  CZ  PHE A 198     -51.951 -16.173 -35.042  1.00 59.83           C  
ANISOU 1235  CZ  PHE A 198     3484  12483   6767    780  -1019   -183       C  
ATOM   1236  N   ALA A 199     -50.195 -13.216 -31.909  1.00 83.97           N  
ANISOU 1236  N   ALA A 199     6773  15745   9385   1127   -583   -156       N  
ATOM   1237  CA  ALA A 199     -49.950 -13.836 -30.614  1.00 77.07           C  
ANISOU 1237  CA  ALA A 199     5840  14908   8532   1062   -470    -48       C  
ATOM   1238  C   ALA A 199     -48.629 -13.404 -29.995  1.00 82.00           C  
ANISOU 1238  C   ALA A 199     6596  15513   9049   1111   -389    -82       C  
ATOM   1239  O   ALA A 199     -48.311 -13.844 -28.885  1.00 83.47           O  
ANISOU 1239  O   ALA A 199     6753  15730   9233   1067   -293      3       O  
ATOM   1240  CB  ALA A 199     -49.984 -15.361 -30.745  1.00 57.69           C  
ANISOU 1240  CB  ALA A 199     3288  12386   6247    876   -522     37       C  
ATOM   1241  N   GLY A 200     -47.861 -12.555 -30.677  1.00 85.77           N  
ANISOU 1241  N   GLY A 200     7211  15940   9436   1195   -431   -194       N  
ATOM   1242  CA  GLY A 200     -46.565 -12.145 -30.172  1.00 76.87           C  
ANISOU 1242  CA  GLY A 200     6203  14786   8217   1233   -370   -225       C  
ATOM   1243  C   GLY A 200     -45.570 -13.269 -30.029  1.00 73.50           C  
ANISOU 1243  C   GLY A 200     5789  14289   7850   1097   -348   -187       C  
ATOM   1244  O   GLY A 200     -44.628 -13.157 -29.240  1.00 86.85           O  
ANISOU 1244  O   GLY A 200     7547  15971   9483   1106   -267   -175       O  
ATOM   1245  N   MET A 201     -45.749 -14.355 -30.773  1.00 67.86           N  
ANISOU 1245  N   MET A 201     5017  13513   7255    976   -430   -176       N  
ATOM   1246  CA  MET A 201     -44.897 -15.529 -30.676  1.00 80.04           C  
ANISOU 1246  CA  MET A 201     6586  14948   8877    845   -429   -147       C  
ATOM   1247  C   MET A 201     -44.317 -15.882 -32.038  1.00 82.44           C  
ANISOU 1247  C   MET A 201     7018  15106   9199    801   -536   -253       C  
ATOM   1248  O   MET A 201     -44.655 -15.290 -33.066  1.00 78.58           O  
ANISOU 1248  O   MET A 201     6582  14611   8665    858   -611   -332       O  
ATOM   1249  CB  MET A 201     -45.670 -16.731 -30.120  1.00 89.07           C  
ANISOU 1249  CB  MET A 201     7542  16123  10175    724   -438    -21       C  
ATOM   1250  CG  MET A 201     -46.046 -16.615 -28.659  1.00113.95           C  
ANISOU 1250  CG  MET A 201    10630  19368  13300    736   -308    107       C  
ATOM   1251  SD  MET A 201     -46.363 -18.228 -27.922  1.00134.84           S  
ANISOU 1251  SD  MET A 201    13119  21985  16129    551   -313    287       S  
ATOM   1252  CE  MET A 201     -47.554 -18.892 -29.082  1.00134.33           C  
ANISOU 1252  CE  MET A 201    12931  21874  16234    467   -477    282       C  
ATOM   1253  N   ILE A 202     -43.428 -16.873 -32.019  1.00 80.27           N  
ANISOU 1253  N   ILE A 202     6788  14724   8985    707   -545   -255       N  
ATOM   1254  CA  ILE A 202     -42.832 -17.438 -33.222  1.00 75.71           C  
ANISOU 1254  CA  ILE A 202     6311  14025   8429    670   -648   -363       C  
ATOM   1255  C   ILE A 202     -42.255 -18.803 -32.872  1.00 80.09           C  
ANISOU 1255  C   ILE A 202     6840  14479   9111    558   -670   -335       C  
ATOM   1256  O   ILE A 202     -41.444 -18.932 -31.946  1.00 77.90           O  
ANISOU 1256  O   ILE A 202     6593  14190   8814    540   -576   -279       O  
ATOM   1257  CB  ILE A 202     -41.761 -16.506 -33.819  1.00 74.01           C  
ANISOU 1257  CB  ILE A 202     6286  13787   8050    748   -621   -451       C  
ATOM   1258  CG1 ILE A 202     -40.899 -17.257 -34.836  1.00 73.30           C  
ANISOU 1258  CG1 ILE A 202     6288  13601   7963    712   -701   -553       C  
ATOM   1259  CG2 ILE A 202     -40.910 -15.893 -32.723  1.00 79.84           C  
ANISOU 1259  CG2 ILE A 202     7089  14545   8701    781   -491   -399       C  
ATOM   1260  CD1 ILE A 202     -39.880 -16.383 -35.533  1.00 75.44           C  
ANISOU 1260  CD1 ILE A 202     6720  13879   8065    779   -680   -618       C  
ATOM   1261  N   SER A 203     -42.689 -19.833 -33.592  1.00 89.13           N  
ANISOU 1261  N   SER A 203     7927  15544  10395    487   -808   -374       N  
ATOM   1262  CA  SER A 203     -42.231 -21.193 -33.351  1.00 96.96           C  
ANISOU 1262  CA  SER A 203     8892  16412  11538    383   -869   -356       C  
ATOM   1263  C   SER A 203     -41.023 -21.498 -34.225  1.00 82.96           C  
ANISOU 1263  C   SER A 203     7277  14535   9707    415   -920   -508       C  
ATOM   1264  O   SER A 203     -40.945 -21.053 -35.374  1.00 79.61           O  
ANISOU 1264  O   SER A 203     6936  14126   9185    485   -977   -634       O  
ATOM   1265  CB  SER A 203     -43.351 -22.196 -33.633  1.00118.51           C  
ANISOU 1265  CB  SER A 203    11467  19090  14472    285  -1018   -319       C  
ATOM   1266  OG  SER A 203     -42.897 -23.528 -33.476  1.00132.70           O  
ANISOU 1266  OG  SER A 203    13249  20736  16436    185  -1109   -309       O  
ATOM   1267  N   VAL A 204     -40.077 -22.259 -33.671  1.00 77.43           N  
ANISOU 1267  N   VAL A 204     6612  13747   9062    368   -900   -491       N  
ATOM   1268  CA  VAL A 204     -38.860 -22.630 -34.382  1.00 82.51           C  
ANISOU 1268  CA  VAL A 204     7390  14310   9651    407   -941   -632       C  
ATOM   1269  C   VAL A 204     -38.564 -24.105 -34.147  1.00 91.14           C  
ANISOU 1269  C   VAL A 204     8444  15248  10937    324  -1047   -635       C  
ATOM   1270  O   VAL A 204     -38.999 -24.706 -33.162  1.00 91.18           O  
ANISOU 1270  O   VAL A 204     8337  15215  11093    226  -1044   -489       O  
ATOM   1271  CB  VAL A 204     -37.642 -21.774 -33.959  1.00 70.21           C  
ANISOU 1271  CB  VAL A 204     5953  12810   7912    470   -789   -626       C  
ATOM   1272  CG1 VAL A 204     -37.787 -20.344 -34.464  1.00 64.05           C  
ANISOU 1272  CG1 VAL A 204     5239  12148   6949    558   -729   -650       C  
ATOM   1273  CG2 VAL A 204     -37.470 -21.798 -32.449  1.00 62.01           C  
ANISOU 1273  CG2 VAL A 204     4863  11787   6912    419   -670   -471       C  
ATOM   1274  N   ALA A 205     -37.812 -24.682 -35.081  1.00 91.84           N  
ANISOU 1274  N   ALA A 205     8623  15255  11017    370  -1149   -803       N  
ATOM   1275  CA  ALA A 205     -37.333 -26.053 -34.995  1.00 94.50           C  
ANISOU 1275  CA  ALA A 205     8954  15426  11527    321  -1271   -847       C  
ATOM   1276  C   ALA A 205     -35.833 -26.045 -34.735  1.00 98.54           C  
ANISOU 1276  C   ALA A 205     9578  15932  11931    376  -1181   -893       C  
ATOM   1277  O   ALA A 205     -35.094 -25.249 -35.328  1.00100.88           O  
ANISOU 1277  O   ALA A 205     9978  16332  12022    473  -1106   -984       O  
ATOM   1278  CB  ALA A 205     -37.643 -26.830 -36.277  1.00 92.48           C  
ANISOU 1278  CB  ALA A 205     8707  15077  11353    352  -1485  -1033       C  
ATOM   1279  N   ILE A 206     -35.392 -26.943 -33.856  1.00 95.89           N  
ANISOU 1279  N   ILE A 206     9213  15480  11739    307  -1196   -816       N  
ATOM   1280  CA  ILE A 206     -34.037 -26.950 -33.321  1.00 89.14           C  
ANISOU 1280  CA  ILE A 206     8441  14622  10804    341  -1096   -817       C  
ATOM   1281  C   ILE A 206     -33.364 -28.261 -33.703  1.00101.34           C  
ANISOU 1281  C   ILE A 206    10018  16002  12486    356  -1256   -946       C  
ATOM   1282  O   ILE A 206     -34.015 -29.310 -33.755  1.00107.94           O  
ANISOU 1282  O   ILE A 206    10782  16684  13547    286  -1428   -944       O  
ATOM   1283  CB  ILE A 206     -34.050 -26.770 -31.787  1.00 84.47           C  
ANISOU 1283  CB  ILE A 206     7788  14058  10246    258   -959   -598       C  
ATOM   1284  CG1 ILE A 206     -34.705 -25.442 -31.411  1.00 85.06           C  
ANISOU 1284  CG1 ILE A 206     7836  14302  10179    271   -814   -498       C  
ATOM   1285  CG2 ILE A 206     -32.642 -26.821 -31.214  1.00 84.74           C  
ANISOU 1285  CG2 ILE A 206     7906  14084  10208    289   -868   -598       C  
ATOM   1286  CD1 ILE A 206     -34.973 -25.299 -29.930  1.00 84.79           C  
ANISOU 1286  CD1 ILE A 206     7716  14323  10178    200   -697   -291       C  
ATOM   1287  N   ASP A 207     -32.059 -28.196 -33.969  1.00107.46           N  
ANISOU 1287  N   ASP A 207    10895  16806  13130    450  -1208  -1057       N  
ATOM   1288  CA  ASP A 207     -31.259 -29.384 -34.243  1.00115.92           C  
ANISOU 1288  CA  ASP A 207    12001  17733  14311    492  -1346  -1191       C  
ATOM   1289  C   ASP A 207     -31.213 -30.330 -33.047  1.00123.13           C  
ANISOU 1289  C   ASP A 207    12854  18483  15447    381  -1386  -1041       C  
ATOM   1290  O   ASP A 207     -30.245 -30.331 -32.280  1.00117.22           O  
ANISOU 1290  O   ASP A 207    12140  17741  14658    385  -1285   -979       O  
ATOM   1291  CB  ASP A 207     -29.843 -28.976 -34.661  1.00115.61           C  
ANISOU 1291  CB  ASP A 207    12066  17804  14057    618  -1254  -1314       C  
ATOM   1292  CG  ASP A 207     -29.304 -27.805 -33.853  1.00115.19           C  
ANISOU 1292  CG  ASP A 207    12041  17897  13830    601  -1027  -1165       C  
ATOM   1293  OD1 ASP A 207     -29.416 -27.816 -32.609  1.00114.85           O  
ANISOU 1293  OD1 ASP A 207    11955  17814  13869    508   -950   -986       O  
ATOM   1294  OD2 ASP A 207     -28.764 -26.864 -34.472  1.00115.12           O  
ANISOU 1294  OD2 ASP A 207    12094  18047  13598    681   -935  -1225       O  
ATOM   1295  N   SER A 208     -32.247 -31.149 -32.887  1.00134.54           N  
ANISOU 1295  N   SER A 208    14205  19783  17132    277  -1540   -971       N  
ATOM   1296  CA  SER A 208     -32.290 -32.115 -31.795  1.00139.40           C  
ANISOU 1296  CA  SER A 208    14749  20239  17979    155  -1602   -802       C  
ATOM   1297  C   SER A 208     -32.638 -33.507 -32.310  1.00143.14           C  
ANISOU 1297  C   SER A 208    15193  20467  18726    123  -1886   -898       C  
ATOM   1298  O   SER A 208     -33.356 -33.652 -33.299  1.00140.56           O  
ANISOU 1298  O   SER A 208    14856  20107  18444    148  -2029  -1030       O  
ATOM   1299  CB  SER A 208     -33.300 -31.679 -30.731  1.00140.87           C  
ANISOU 1299  CB  SER A 208    14811  20507  18207     18  -1493   -532       C  
ATOM   1300  OG  SER A 208     -34.625 -31.767 -31.223  1.00144.89           O  
ANISOU 1300  OG  SER A 208    15229  20999  18823    -43  -1604   -515       O  
ATOM   1301  N   ALA A 212     -36.236 -30.496 -32.306  1.00119.32           N  
ANISOU 1301  N   ALA A 212    11935  17960  15441    -10  -1577   -570       N  
ATOM   1302  CA  ALA A 212     -37.603 -30.390 -31.810  1.00112.00           C  
ANISOU 1302  CA  ALA A 212    10850  17085  14619   -128  -1577   -378       C  
ATOM   1303  C   ALA A 212     -38.096 -28.950 -31.883  1.00109.04           C  
ANISOU 1303  C   ALA A 212    10473  16938  14018    -64  -1402   -357       C  
ATOM   1304  O   ALA A 212     -37.301 -28.016 -31.967  1.00112.56           O  
ANISOU 1304  O   ALA A 212    11032  17497  14240     42  -1253   -428       O  
ATOM   1305  CB  ALA A 212     -37.694 -30.911 -30.385  1.00112.46           C  
ANISOU 1305  CB  ALA A 212    10798  17118  14816   -261  -1530   -118       C  
ATOM   1306  N   THR A 213     -39.412 -28.777 -31.846  1.00108.87           N  
ANISOU 1306  N   THR A 213    10318  16981  14066   -130  -1430   -252       N  
ATOM   1307  CA  THR A 213     -40.020 -27.462 -31.957  1.00106.03           C  
ANISOU 1307  CA  THR A 213     9945  16824  13518    -63  -1294   -238       C  
ATOM   1308  C   THR A 213     -40.103 -26.786 -30.592  1.00 98.19           C  
ANISOU 1308  C   THR A 213     8882  15989  12436    -84  -1092    -37       C  
ATOM   1309  O   THR A 213     -40.069 -27.436 -29.545  1.00 99.07           O  
ANISOU 1309  O   THR A 213     8904  16074  12663   -182  -1074    136       O  
ATOM   1310  CB  THR A 213     -41.418 -27.564 -32.568  1.00106.72           C  
ANISOU 1310  CB  THR A 213     9912  16924  13713   -110  -1420   -229       C  
ATOM   1311  OG1 THR A 213     -42.267 -28.315 -31.692  1.00101.72           O  
ANISOU 1311  OG1 THR A 213     9094  16266  13291   -262  -1471    -10       O  
ATOM   1312  CG2 THR A 213     -41.356 -28.261 -33.916  1.00111.66           C  
ANISOU 1312  CG2 THR A 213    10605  17395  14424    -80  -1637   -444       C  
ATOM   1313  N   VAL A 214     -40.213 -25.458 -30.620  1.00 89.90           N  
ANISOU 1313  N   VAL A 214     7874  15108  11175     17   -950    -63       N  
ATOM   1314  CA  VAL A 214     -40.405 -24.675 -29.406  1.00 82.21           C  
ANISOU 1314  CA  VAL A 214     6836  14305  10096     30   -771     95       C  
ATOM   1315  C   VAL A 214     -41.006 -23.336 -29.802  1.00 85.21           C  
ANISOU 1315  C   VAL A 214     7232  14836  10308    138   -699     39       C  
ATOM   1316  O   VAL A 214     -40.784 -22.842 -30.912  1.00 90.80           O  
ANISOU 1316  O   VAL A 214     8055  15518  10928    216   -744   -124       O  
ATOM   1317  CB  VAL A 214     -39.079 -24.506 -28.620  1.00 75.45           C  
ANISOU 1317  CB  VAL A 214     6086  13445   9135     63   -647    108       C  
ATOM   1318  CG1 VAL A 214     -38.164 -23.508 -29.308  1.00 68.88           C  
ANISOU 1318  CG1 VAL A 214     5436  12633   8103    189   -586    -61       C  
ATOM   1319  CG2 VAL A 214     -39.359 -24.085 -27.185  1.00 84.60           C  
ANISOU 1319  CG2 VAL A 214     7143  14766  10236     50   -496    294       C  
ATOM   1320  N   ASP A 215     -41.786 -22.755 -28.895  1.00 86.98           N  
ANISOU 1320  N   ASP A 215     7334  15229  10486    147   -595    176       N  
ATOM   1321  CA  ASP A 215     -42.418 -21.460 -29.107  1.00 87.90           C  
ANISOU 1321  CA  ASP A 215     7453  15492  10454    261   -530    134       C  
ATOM   1322  C   ASP A 215     -41.623 -20.397 -28.359  1.00 77.78           C  
ANISOU 1322  C   ASP A 215     6273  14297   8981    364   -374    125       C  
ATOM   1323  O   ASP A 215     -41.435 -20.500 -27.141  1.00 81.37           O  
ANISOU 1323  O   ASP A 215     6667  14829   9420    346   -276    246       O  
ATOM   1324  CB  ASP A 215     -43.871 -21.477 -28.633  1.00 92.38           C  
ANISOU 1324  CB  ASP A 215     7803  16205  11089    227   -529    274       C  
ATOM   1325  CG  ASP A 215     -44.652 -22.652 -29.186  1.00 96.33           C  
ANISOU 1325  CG  ASP A 215     8180  16611  11811     95   -695    318       C  
ATOM   1326  OD1 ASP A 215     -44.510 -22.948 -30.391  1.00 94.94           O  
ANISOU 1326  OD1 ASP A 215     8094  16294  11685     94   -829    170       O  
ATOM   1327  OD2 ASP A 215     -45.406 -23.282 -28.415  1.00101.24           O  
ANISOU 1327  OD2 ASP A 215     8608  17304  12556     -7   -699    504       O  
ATOM   1328  N   LEU A 216     -41.155 -19.386 -29.084  1.00 63.83           N  
ANISOU 1328  N   LEU A 216     4659  12519   7073    469   -363    -11       N  
ATOM   1329  CA  LEU A 216     -40.395 -18.287 -28.505  1.00 64.02           C  
ANISOU 1329  CA  LEU A 216     4795  12602   6929    567   -246    -33       C  
ATOM   1330  C   LEU A 216     -41.207 -17.004 -28.601  1.00 61.25           C  
ANISOU 1330  C   LEU A 216     4431  12369   6473    684   -223    -62       C  
ATOM   1331  O   LEU A 216     -41.790 -16.710 -29.649  1.00 66.86           O  
ANISOU 1331  O   LEU A 216     5152  13064   7188    712   -307   -133       O  
ATOM   1332  CB  LEU A 216     -39.047 -18.118 -29.210  1.00 60.32           C  
ANISOU 1332  CB  LEU A 216     4516  12017   6387    587   -260   -149       C  
ATOM   1333  CG  LEU A 216     -38.155 -19.359 -29.295  1.00 55.94           C  
ANISOU 1333  CG  LEU A 216     3991  11336   5928    496   -301   -157       C  
ATOM   1334  CD1 LEU A 216     -36.809 -19.014 -29.913  1.00 65.63           C  
ANISOU 1334  CD1 LEU A 216     5390  12498   7046    538   -293   -266       C  
ATOM   1335  CD2 LEU A 216     -37.968 -19.975 -27.919  1.00 48.92           C  
ANISOU 1335  CD2 LEU A 216     3018  10469   5099    435   -227    -20       C  
ATOM   1336  N   GLY A 217     -41.245 -16.248 -27.508  1.00 54.69           N  
ANISOU 1336  N   GLY A 217     3577  11655   5546    763   -118    -14       N  
ATOM   1337  CA  GLY A 217     -41.960 -14.990 -27.502  1.00 60.70           C  
ANISOU 1337  CA  GLY A 217     4333  12520   6208    896   -105    -55       C  
ATOM   1338  C   GLY A 217     -41.283 -13.941 -28.361  1.00 65.12           C  
ANISOU 1338  C   GLY A 217     5084  12989   6668    972   -144   -174       C  
ATOM   1339  O   GLY A 217     -40.178 -14.120 -28.877  1.00 67.92           O  
ANISOU 1339  O   GLY A 217     5572  13226   7007    927   -162   -220       O  
ATOM   1340  N   SER A 218     -41.976 -12.813 -28.519  1.00 71.59           N  
ANISOU 1340  N   SER A 218     5907  13872   7420   1092   -164   -217       N  
ATOM   1341  CA  SER A 218     -41.419 -11.719 -29.311  1.00 73.53           C  
ANISOU 1341  CA  SER A 218     6326  14034   7579   1161   -217   -305       C  
ATOM   1342  C   SER A 218     -40.128 -11.170 -28.717  1.00 77.27           C  
ANISOU 1342  C   SER A 218     6942  14450   7969   1183   -162   -319       C  
ATOM   1343  O   SER A 218     -39.120 -11.127 -29.441  1.00 87.42           O  
ANISOU 1343  O   SER A 218     8359  15629   9228   1135   -193   -349       O  
ATOM   1344  CB  SER A 218     -42.473 -10.622 -29.501  1.00 90.52           C  
ANISOU 1344  CB  SER A 218     8446  16255   9691   1292   -263   -341       C  
ATOM   1345  OG  SER A 218     -41.869  -9.410 -29.919  1.00 96.45           O  
ANISOU 1345  OG  SER A 218     9363  16924  10357   1368   -309   -401       O  
ATOM   1346  N   PRO A 219     -40.062 -10.759 -27.442  1.00 84.16           N  
ANISOU 1346  N   PRO A 219     7789  15396   8790   1253    -87   -298       N  
ATOM   1347  CA  PRO A 219     -38.762 -10.338 -26.896  1.00 87.75           C  
ANISOU 1347  CA  PRO A 219     8380  15785   9177   1259    -48   -312       C  
ATOM   1348  C   PRO A 219     -37.784 -11.487 -26.737  1.00 86.80           C  
ANISOU 1348  C   PRO A 219     8270  15610   9098   1130      0   -266       C  
ATOM   1349  O   PRO A 219     -36.573 -11.243 -26.668  1.00 73.25           O  
ANISOU 1349  O   PRO A 219     6680  13816   7337   1110     13   -281       O  
ATOM   1350  CB  PRO A 219     -39.128  -9.721 -25.541  1.00 76.03           C  
ANISOU 1350  CB  PRO A 219     6840  14420   7629   1381     11   -312       C  
ATOM   1351  CG  PRO A 219     -40.360 -10.426 -25.143  1.00 70.31           C  
ANISOU 1351  CG  PRO A 219     5912  13848   6953   1379     50   -250       C  
ATOM   1352  CD  PRO A 219     -41.121 -10.688 -26.415  1.00 81.57           C  
ANISOU 1352  CD  PRO A 219     7302  15236   8456   1334    -33   -260       C  
ATOM   1353  N   ALA A 220     -38.271 -12.728 -26.676  1.00 91.15           N  
ANISOU 1353  N   ALA A 220     8690  16196   9745   1042     15   -205       N  
ATOM   1354  CA  ALA A 220     -37.380 -13.882 -26.639  1.00 88.16           C  
ANISOU 1354  CA  ALA A 220     8325  15744   9428    924     35   -170       C  
ATOM   1355  C   ALA A 220     -36.638 -14.028 -27.958  1.00 82.90           C  
ANISOU 1355  C   ALA A 220     7776  14957   8765    877    -36   -240       C  
ATOM   1356  O   ALA A 220     -35.407 -13.940 -28.005  1.00 82.73           O  
ANISOU 1356  O   ALA A 220     7868  14872   8695    858    -18   -260       O  
ATOM   1357  CB  ALA A 220     -38.169 -15.153 -26.319  1.00 95.49           C  
ANISOU 1357  CB  ALA A 220     9082  16719  10480    838     38    -81       C  
ATOM   1358  N   ALA A 221     -37.377 -14.071 -29.018  1.00 87.18           N  
ANISOU 1358  N   ALA A 221     8285  15486   9353    866   -119   -277       N  
ATOM   1359  CA  ALA A 221     -36.761 -14.289 -30.266  1.00 88.28           C  
ANISOU 1359  CA  ALA A 221     8519  15548   9476    837   -192   -350       C  
ATOM   1360  C   ALA A 221     -36.408 -13.035 -30.891  1.00 86.02           C  
ANISOU 1360  C   ALA A 221     8363  15252   9067    906   -210   -388       C  
ATOM   1361  O   ALA A 221     -36.487 -12.928 -32.054  1.00100.63           O  
ANISOU 1361  O   ALA A 221    10265  17088  10884    910   -283   -435       O  
ATOM   1362  CB  ALA A 221     -37.699 -15.058 -31.141  1.00 93.80           C  
ANISOU 1362  CB  ALA A 221     9134  16245  10261    808   -286   -382       C  
ATOM   1363  N   GLN A 222     -36.033 -12.107 -30.093  1.00 77.58           N  
ANISOU 1363  N   GLN A 222     7349  14195   7934    959   -156   -363       N  
ATOM   1364  CA  GLN A 222     -35.705 -10.868 -30.623  1.00 80.72           C  
ANISOU 1364  CA  GLN A 222     7870  14564   8238   1018   -191   -381       C  
ATOM   1365  C   GLN A 222     -34.454 -10.373 -30.003  1.00 99.35           C  
ANISOU 1365  C   GLN A 222    10289  16908  10551   1047   -132   -358       C  
ATOM   1366  O   GLN A 222     -34.210  -9.220 -30.002  1.00117.04           O  
ANISOU 1366  O   GLN A 222    12509  19186  12777   1134   -121   -361       O  
ATOM   1367  CB  GLN A 222     -36.809 -10.013 -30.195  1.00 79.84           C  
ANISOU 1367  CB  GLN A 222     7728  14485   8121   1104   -257   -399       C  
ATOM   1368  CG  GLN A 222     -36.773  -8.594 -30.594  1.00 84.63           C  
ANISOU 1368  CG  GLN A 222     8447  15051   8657   1184   -308   -406       C  
ATOM   1369  CD  GLN A 222     -37.934  -7.886 -30.001  1.00 89.96           C  
ANISOU 1369  CD  GLN A 222     9065  15774   9343   1304   -337   -428       C  
ATOM   1370  OE1 GLN A 222     -38.813  -8.492 -29.429  1.00 84.88           O  
ANISOU 1370  OE1 GLN A 222     8289  15219   8742   1330   -288   -425       O  
ATOM   1371  NE2 GLN A 222     -37.936  -6.608 -30.113  1.00 99.18           N  
ANISOU 1371  NE2 GLN A 222    10323  16888  10473   1380   -422   -443       N  
ATOM   1372  N   ALA A 223     -33.652 -11.267 -29.471  1.00 95.57           N  
ANISOU 1372  N   ALA A 223     9879  16387  10048    985    -95   -343       N  
ATOM   1373  CA  ALA A 223     -32.400 -10.993 -28.848  1.00 93.27           C  
ANISOU 1373  CA  ALA A 223     9600  16072   9767    901    -99   -353       C  
ATOM   1374  C   ALA A 223     -31.529 -11.794 -29.672  1.00 85.51           C  
ANISOU 1374  C   ALA A 223     8626  15072   8792    857    -22   -325       C  
ATOM   1375  O   ALA A 223     -30.683 -11.298 -30.362  1.00 89.47           O  
ANISOU 1375  O   ALA A 223     9151  15578   9265    895     16   -302       O  
ATOM   1376  CB  ALA A 223     -32.391 -11.601 -27.487  1.00100.24           C  
ANISOU 1376  CB  ALA A 223    10583  16935  10570    894   -158   -361       C  
ATOM   1377  N   ILE A 224     -31.750 -13.072 -29.566  1.00 84.77           N  
ANISOU 1377  N   ILE A 224     8516  14959   8735    790     -4   -332       N  
ATOM   1378  CA  ILE A 224     -31.067 -14.050 -30.311  1.00 76.69           C  
ANISOU 1378  CA  ILE A 224     7471  13923   7744    750    -52   -382       C  
ATOM   1379  C   ILE A 224     -30.934 -13.724 -31.768  1.00 66.56           C  
ANISOU 1379  C   ILE A 224     6237  12663   6390    770   -124   -427       C  
ATOM   1380  O   ILE A 224     -31.927 -13.692 -32.394  1.00 60.58           O  
ANISOU 1380  O   ILE A 224     5441  11924   5652    795   -182   -452       O  
ATOM   1381  CB  ILE A 224     -31.785 -15.361 -30.126  1.00 63.51           C  
ANISOU 1381  CB  ILE A 224     5680  12247   6206    721    -73   -383       C  
ATOM   1382  CG1 ILE A 224     -31.809 -16.164 -31.332  1.00 64.68           C  
ANISOU 1382  CG1 ILE A 224     5814  12360   6402    689   -145   -457       C  
ATOM   1383  CG2 ILE A 224     -33.238 -15.189 -29.972  1.00 68.65           C  
ANISOU 1383  CG2 ILE A 224     6262  12941   6883    761    -99   -368       C  
ATOM   1384  CD1 ILE A 224     -32.327 -17.475 -30.912  1.00 75.64           C  
ANISOU 1384  CD1 ILE A 224     7086  13712   7942    646   -195   -453       C  
ATOM   1385  N   TRP A 225     -29.707 -13.441 -32.273  1.00 65.63           N  
ANISOU 1385  N   TRP A 225     6195  12559   6182    757   -118   -429       N  
ATOM   1386  CA  TRP A 225     -29.493 -13.137 -33.679  1.00 53.66           C  
ANISOU 1386  CA  TRP A 225     4715  11096   4576    769   -177   -458       C  
ATOM   1387  C   TRP A 225     -29.097 -14.408 -34.420  1.00 54.45           C  
ANISOU 1387  C   TRP A 225     4781  11221   4686    759   -200   -542       C  
ATOM   1388  O   TRP A 225     -28.527 -15.335 -33.838  1.00 49.76           O  
ANISOU 1388  O   TRP A 225     4166  10590   4151    736   -166   -562       O  
ATOM   1389  CB  TRP A 225     -28.411 -12.068 -33.858  1.00 43.59           C  
ANISOU 1389  CB  TRP A 225     3527   9849   3188    758   -163   -393       C  
ATOM   1390  CG  TRP A 225     -28.736 -10.765 -33.193  1.00 53.28           C  
ANISOU 1390  CG  TRP A 225     4801  11030   4413    777   -170   -326       C  
ATOM   1391  CD1 TRP A 225     -28.824 -10.527 -31.852  1.00 64.10           C  
ANISOU 1391  CD1 TRP A 225     6173  12345   5835    788   -127   -305       C  
ATOM   1392  CD2 TRP A 225     -29.036  -9.524 -33.841  1.00 51.82           C  
ANISOU 1392  CD2 TRP A 225     4668  10849   4171    798   -240   -280       C  
ATOM   1393  NE1 TRP A 225     -29.154  -9.212 -31.625  1.00 62.81           N  
ANISOU 1393  NE1 TRP A 225     6064  12146   5653    827   -171   -269       N  
ATOM   1394  CE2 TRP A 225     -29.290  -8.575 -32.830  1.00 57.82           C  
ANISOU 1394  CE2 TRP A 225     5466  11537   4965    829   -245   -246       C  
ATOM   1395  CE3 TRP A 225     -29.111  -9.121 -35.178  1.00 53.10           C  
ANISOU 1395  CE3 TRP A 225     4848  11073   4256    799   -307   -261       C  
ATOM   1396  CZ2 TRP A 225     -29.613  -7.249 -33.115  1.00 59.47           C  
ANISOU 1396  CZ2 TRP A 225     5735  11708   5152    860   -327   -201       C  
ATOM   1397  CZ3 TRP A 225     -29.431  -7.804 -35.458  1.00 58.47           C  
ANISOU 1397  CZ3 TRP A 225     5583  11724   4909    817   -379   -193       C  
ATOM   1398  CH2 TRP A 225     -29.678  -6.884 -34.431  1.00 61.24           C  
ANISOU 1398  CH2 TRP A 225     5976  11977   5314    847   -395   -166       C  
ATOM   1399  N   VAL A 226     -29.396 -14.440 -35.715  1.00 64.74           N  
ANISOU 1399  N   VAL A 226     6081  12587   5930    787   -270   -598       N  
ATOM   1400  CA  VAL A 226     -29.258 -15.647 -36.522  1.00 66.00           C  
ANISOU 1400  CA  VAL A 226     6204  12771   6103    805   -323   -710       C  
ATOM   1401  C   VAL A 226     -28.797 -15.256 -37.920  1.00 67.86           C  
ANISOU 1401  C   VAL A 226     6470  13137   6177    844   -362   -741       C  
ATOM   1402  O   VAL A 226     -29.199 -14.213 -38.448  1.00 78.80           O  
ANISOU 1402  O   VAL A 226     7882  14573   7485    854   -386   -683       O  
ATOM   1403  CB  VAL A 226     -30.590 -16.430 -36.564  1.00 67.18           C  
ANISOU 1403  CB  VAL A 226     6278  12858   6391    805   -396   -770       C  
ATOM   1404  CG1 VAL A 226     -31.722 -15.540 -37.060  1.00 58.15           C  
ANISOU 1404  CG1 VAL A 226     5127  11746   5223    828   -442   -744       C  
ATOM   1405  CG2 VAL A 226     -30.473 -17.670 -37.423  1.00 68.33           C  
ANISOU 1405  CG2 VAL A 226     6393  13005   6563    830   -480   -905       C  
ATOM   1406  N   VAL A 227     -27.936 -16.082 -38.514  1.00 58.02           N  
ANISOU 1406  N   VAL A 227     5216  11956   4873    874   -373   -829       N  
ATOM   1407  CA  VAL A 227     -27.517 -15.898 -39.900  1.00 61.09           C  
ANISOU 1407  CA  VAL A 227     5612  12508   5091    927   -412   -873       C  
ATOM   1408  C   VAL A 227     -28.423 -16.730 -40.797  1.00 65.66           C  
ANISOU 1408  C   VAL A 227     6148  13095   5704    983   -523  -1016       C  
ATOM   1409  O   VAL A 227     -28.684 -17.907 -40.515  1.00 72.33           O  
ANISOU 1409  O   VAL A 227     6957  13841   6685    991   -570  -1122       O  
ATOM   1410  CB  VAL A 227     -26.039 -16.278 -40.091  1.00 71.67           C  
ANISOU 1410  CB  VAL A 227     6955  13951   6323    951   -363   -897       C  
ATOM   1411  CG1 VAL A 227     -25.137 -15.157 -39.597  1.00 71.64           C  
ANISOU 1411  CG1 VAL A 227     6993  13987   6240    894   -276   -736       C  
ATOM   1412  CG2 VAL A 227     -25.721 -17.572 -39.368  1.00 76.33           C  
ANISOU 1412  CG2 VAL A 227     7522  14433   7049    957   -361   -993       C  
ATOM   1413  N   SER A 228     -28.901 -16.120 -41.880  1.00 69.35           N  
ANISOU 1413  N   SER A 228     6618  13675   6056   1018   -577  -1015       N  
ATOM   1414  CA  SER A 228     -29.937 -16.724 -42.706  1.00 75.49           C  
ANISOU 1414  CA  SER A 228     7357  14455   6869   1066   -694  -1140       C  
ATOM   1415  C   SER A 228     -29.367 -17.800 -43.621  1.00 75.84           C  
ANISOU 1415  C   SER A 228     7380  14595   6839   1152   -759  -1316       C  
ATOM   1416  O   SER A 228     -28.282 -17.644 -44.189  1.00 76.80           O  
ANISOU 1416  O   SER A 228     7514  14877   6789   1198   -716  -1318       O  
ATOM   1417  CB  SER A 228     -30.637 -15.654 -43.543  1.00 79.03           C  
ANISOU 1417  CB  SER A 228     7817  14999   7211   1080   -734  -1073       C  
ATOM   1418  OG  SER A 228     -29.696 -14.838 -44.220  1.00 89.71           O  
ANISOU 1418  OG  SER A 228     9206  16499   8380   1090   -679   -985       O  
ATOM   1419  N   LEU A 229     -30.121 -18.890 -43.765  1.00 77.41           N  
ANISOU 1419  N   LEU A 229     7542  14694   7177   1178   -870  -1461       N  
ATOM   1420  CA  LEU A 229     -29.771 -20.009 -44.641  1.00 79.89           C  
ANISOU 1420  CA  LEU A 229     7836  15068   7450   1279   -972  -1667       C  
ATOM   1421  C   LEU A 229     -28.349 -20.509 -44.401  1.00 88.45           C  
ANISOU 1421  C   LEU A 229     8932  16201   8473   1319   -909  -1710       C  
ATOM   1422  O   LEU A 229     -28.022 -20.975 -43.310  1.00 88.65           O  
ANISOU 1422  O   LEU A 229     8959  16075   8647   1264   -866  -1677       O  
ATOM   1423  CB  LEU A 229     -29.947 -19.616 -46.112  1.00 81.40           C  
ANISOU 1423  CB  LEU A 229     8036  15426   7466   1362  -1013  -1720       C  
ATOM   1424  CG  LEU A 229     -31.344 -19.777 -46.725  1.00 89.16           C  
ANISOU 1424  CG  LEU A 229     8996  16357   8523   1374  -1144  -1793       C  
ATOM   1425  CD1 LEU A 229     -31.844 -21.207 -46.566  1.00 89.03           C  
ANISOU 1425  CD1 LEU A 229     8934  16206   8687   1397  -1306  -1984       C  
ATOM   1426  CD2 LEU A 229     -32.344 -18.785 -46.139  1.00 89.44           C  
ANISOU 1426  CD2 LEU A 229     9019  16348   8616   1284  -1128  -1632       C  
TER    1427      LEU A 229                                                      
ATOM   1428  N   GLN B  15      -4.711  -4.553   4.819  1.00108.38           N  
ANISOU 1428  N   GLN B  15    12665  18315  10202   1624   -862   -963       N  
ATOM   1429  CA  GLN B  15      -5.391  -5.839   4.734  1.00113.55           C  
ANISOU 1429  CA  GLN B  15    13188  19104  10853   1603   -620   -803       C  
ATOM   1430  C   GLN B  15      -4.420  -6.909   4.242  1.00107.24           C  
ANISOU 1430  C   GLN B  15    12327  18298  10123   1418   -529   -610       C  
ATOM   1431  O   GLN B  15      -4.573  -8.094   4.547  1.00 98.16           O  
ANISOU 1431  O   GLN B  15    11069  17251   8976   1395   -369   -473       O  
ATOM   1432  CB  GLN B  15      -6.609  -5.741   3.809  1.00120.39           C  
ANISOU 1432  CB  GLN B  15    14038  19950  11756   1622   -552   -803       C  
ATOM   1433  CG  GLN B  15      -7.336  -7.056   3.573  1.00123.78           C  
ANISOU 1433  CG  GLN B  15    14332  20483  12218   1575   -333   -630       C  
ATOM   1434  CD  GLN B  15      -8.481  -6.920   2.591  1.00127.60           C  
ANISOU 1434  CD  GLN B  15    14803  20934  12746   1583   -283   -633       C  
ATOM   1435  OE1 GLN B  15      -8.603  -5.911   1.897  1.00129.09           O  
ANISOU 1435  OE1 GLN B  15    15087  21013  12949   1595   -402   -742       O  
ATOM   1436  NE2 GLN B  15      -9.336  -7.934   2.536  1.00128.50           N  
ANISOU 1436  NE2 GLN B  15    14797  21136  12890   1571   -126   -508       N  
ATOM   1437  N   ASP B  16      -3.407  -6.477   3.487  1.00111.65           N  
ANISOU 1437  N   ASP B  16    12944  18734  10744   1288   -649   -597       N  
ATOM   1438  CA  ASP B  16      -2.385  -7.399   3.006  1.00117.40           C  
ANISOU 1438  CA  ASP B  16    13609  19462  11535   1125   -579   -429       C  
ATOM   1439  C   ASP B  16      -1.501  -7.921   4.129  1.00124.14           C  
ANISOU 1439  C   ASP B  16    14429  20394  12343   1136   -576   -394       C  
ATOM   1440  O   ASP B  16      -0.792  -8.914   3.933  1.00119.13           O  
ANISOU 1440  O   ASP B  16    13721  19789  11752   1032   -488   -249       O  
ATOM   1441  CB  ASP B  16      -1.521  -6.721   1.943  1.00119.53           C  
ANISOU 1441  CB  ASP B  16    13928  19607  11881    983   -722   -415       C  
ATOM   1442  CG  ASP B  16      -1.803  -7.242   0.555  1.00129.27           C  
ANISOU 1442  CG  ASP B  16    15111  20817  13189    871   -610   -296       C  
ATOM   1443  OD1 ASP B  16      -2.329  -8.368   0.451  1.00134.35           O  
ANISOU 1443  OD1 ASP B  16    15673  21527  13845    874   -422   -202       O  
ATOM   1444  OD2 ASP B  16      -1.500  -6.533  -0.428  1.00133.53           O  
ANISOU 1444  OD2 ASP B  16    15691  21197  13847    767   -700   -287       O  
ATOM   1445  N   TYR B  17      -1.526  -7.273   5.295  1.00133.03           N  
ANISOU 1445  N   TYR B  17    15607  21555  13384   1268   -677   -530       N  
ATOM   1446  CA  TYR B  17      -0.710  -7.722   6.417  1.00136.35           C  
ANISOU 1446  CA  TYR B  17    15997  22058  13751   1288   -681   -503       C  
ATOM   1447  C   TYR B  17      -1.151  -9.094   6.914  1.00132.46           C  
ANISOU 1447  C   TYR B  17    15382  21710  13237   1307   -479   -357       C  
ATOM   1448  O   TYR B  17      -0.349  -9.825   7.510  1.00134.68           O  
ANISOU 1448  O   TYR B  17    15612  22053  13507   1271   -449   -266       O  
ATOM   1449  CB  TYR B  17      -0.760  -6.686   7.545  1.00147.21           C  
ANISOU 1449  CB  TYR B  17    17457  23442  15036   1443   -837   -697       C  
ATOM   1450  CG  TYR B  17      -0.766  -5.246   7.060  1.00158.39           C  
ANISOU 1450  CG  TYR B  17    18998  24694  16490   1459  -1056   -865       C  
ATOM   1451  CD1 TYR B  17      -1.943  -4.628   6.647  1.00165.25           C  
ANISOU 1451  CD1 TYR B  17    19906  25527  17356   1553  -1063   -966       C  
ATOM   1452  CD2 TYR B  17       0.411  -4.510   7.001  1.00162.46           C  
ANISOU 1452  CD2 TYR B  17    19586  25082  17060   1374  -1271   -912       C  
ATOM   1453  CE1 TYR B  17      -1.947  -3.319   6.198  1.00169.24           C  
ANISOU 1453  CE1 TYR B  17    20527  25863  17913   1567  -1285  -1115       C  
ATOM   1454  CE2 TYR B  17       0.416  -3.199   6.554  1.00167.55           C  
ANISOU 1454  CE2 TYR B  17    20338  25554  17769   1374  -1501  -1050       C  
ATOM   1455  CZ  TYR B  17      -0.766  -2.610   6.153  1.00170.26           C  
ANISOU 1455  CZ  TYR B  17    20727  25853  18110   1474  -1510  -1153       C  
ATOM   1456  OH  TYR B  17      -0.766  -1.307   5.708  1.00171.37           O  
ANISOU 1456  OH  TYR B  17    20978  25803  18333   1476  -1759  -1287       O  
ATOM   1457  N   LEU B  18      -2.413  -9.461   6.661  1.00130.71           N  
ANISOU 1457  N   LEU B  18    15106  21537  13022   1356   -355   -326       N  
ATOM   1458  CA  LEU B  18      -2.914 -10.787   7.015  1.00126.98           C  
ANISOU 1458  CA  LEU B  18    14506  21181  12560   1351   -191   -166       C  
ATOM   1459  C   LEU B  18      -2.025 -11.896   6.471  1.00118.29           C  
ANISOU 1459  C   LEU B  18    13350  20045  11551   1200   -128      4       C  
ATOM   1460  O   LEU B  18      -1.889 -12.952   7.100  1.00113.17           O  
ANISOU 1460  O   LEU B  18    12614  19485  10899   1192    -53    131       O  
ATOM   1461  CB  LEU B  18      -4.339 -10.961   6.483  1.00133.75           C  
ANISOU 1461  CB  LEU B  18    15316  22055  13448   1386    -97   -145       C  
ATOM   1462  CG  LEU B  18      -5.484 -10.985   7.494  1.00138.91           C  
ANISOU 1462  CG  LEU B  18    15901  22865  14013   1537    -50   -170       C  
ATOM   1463  CD1 LEU B  18      -5.444 -12.238   8.338  1.00143.35           C  
ANISOU 1463  CD1 LEU B  18    16343  23562  14562   1521     40      0       C  
ATOM   1464  CD2 LEU B  18      -5.401  -9.776   8.372  1.00140.40           C  
ANISOU 1464  CD2 LEU B  18    16169  23091  14085   1689   -173   -368       C  
ATOM   1465  N   LYS B  19      -1.411 -11.674   5.310  1.00114.44           N  
ANISOU 1465  N   LYS B  19    12904  19436  11141   1084   -166     12       N  
ATOM   1466  CA  LYS B  19      -0.574 -12.695   4.693  1.00103.16           C  
ANISOU 1466  CA  LYS B  19    11416  17980   9800    955   -108    158       C  
ATOM   1467  C   LYS B  19       0.788 -12.786   5.371  1.00101.83           C  
ANISOU 1467  C   LYS B  19    11249  17841   9601    927   -180    178       C  
ATOM   1468  O   LYS B  19       1.217 -13.874   5.771  1.00103.66           O  
ANISOU 1468  O   LYS B  19    11405  18132   9850    902   -116    300       O  
ATOM   1469  CB  LYS B  19      -0.410 -12.398   3.205  1.00 98.13           C  
ANISOU 1469  CB  LYS B  19    10807  17231   9247    851   -121    160       C  
ATOM   1470  CG  LYS B  19      -1.710 -12.073   2.494  1.00 95.88           C  
ANISOU 1470  CG  LYS B  19    10539  16906   8985    882    -77    116       C  
ATOM   1471  CD  LYS B  19      -1.455 -11.374   1.169  1.00 94.51           C  
ANISOU 1471  CD  LYS B  19    10417  16630   8861    794   -134     85       C  
ATOM   1472  CE  LYS B  19      -0.778 -12.299   0.168  1.00 84.39           C  
ANISOU 1472  CE  LYS B  19     9071  15322   7673    670    -63    211       C  
ATOM   1473  NZ  LYS B  19       0.710 -12.293   0.262  1.00 82.46           N  
ANISOU 1473  NZ  LYS B  19     8816  15088   7427    595   -135    250       N  
ATOM   1474  N   VAL B  20       1.480 -11.652   5.510  1.00 99.95           N  
ANISOU 1474  N   VAL B  20    11096  17555   9325    928   -331     62       N  
ATOM   1475  CA  VAL B  20       2.828 -11.677   6.069  1.00 97.87           C  
ANISOU 1475  CA  VAL B  20    10832  17308   9047    887   -418     81       C  
ATOM   1476  C   VAL B  20       2.802 -12.096   7.535  1.00107.47           C  
ANISOU 1476  C   VAL B  20    12019  18642  10172    991   -396     84       C  
ATOM   1477  O   VAL B  20       3.747 -12.731   8.021  1.00109.44           O  
ANISOU 1477  O   VAL B  20    12224  18938  10421    956   -397    166       O  
ATOM   1478  CB  VAL B  20       3.514 -10.310   5.866  1.00 92.18           C  
ANISOU 1478  CB  VAL B  20    10204  16491   8328    853   -617    -40       C  
ATOM   1479  CG1 VAL B  20       2.641  -9.183   6.394  1.00100.77           C  
ANISOU 1479  CG1 VAL B  20    11387  17554   9345    983   -712   -218       C  
ATOM   1480  CG2 VAL B  20       4.897 -10.286   6.510  1.00 89.98           C  
ANISOU 1480  CG2 VAL B  20     9918  16227   8042    809   -724    -24       C  
ATOM   1481  N   ILE B  21       1.724 -11.781   8.262  1.00107.80           N  
ANISOU 1481  N   ILE B  21    12076  18749  10135   1123   -373      3       N  
ATOM   1482  CA  ILE B  21       1.632 -12.260   9.638  1.00 96.51           C  
ANISOU 1482  CA  ILE B  21    10597  17460   8612   1221   -338     28       C  
ATOM   1483  C   ILE B  21       1.326 -13.752   9.688  1.00 95.99           C  
ANISOU 1483  C   ILE B  21    10409  17474   8589   1182   -186    224       C  
ATOM   1484  O   ILE B  21       1.519 -14.385  10.733  1.00 93.61           O  
ANISOU 1484  O   ILE B  21    10048  17290   8229   1225   -159    298       O  
ATOM   1485  CB  ILE B  21       0.581 -11.470  10.442  1.00 89.22           C  
ANISOU 1485  CB  ILE B  21     9706  16611   7582   1386   -362   -116       C  
ATOM   1486  CG1 ILE B  21      -0.827 -11.742   9.909  1.00 84.56           C  
ANISOU 1486  CG1 ILE B  21     9065  16043   7023   1414   -246    -79       C  
ATOM   1487  CG2 ILE B  21       0.902  -9.981  10.429  1.00 88.42           C  
ANISOU 1487  CG2 ILE B  21     9737  16408   7450   1434   -547   -323       C  
ATOM   1488  CD1 ILE B  21      -1.922 -11.071  10.705  1.00 83.60           C  
ANISOU 1488  CD1 ILE B  21     8945  16023   6793   1588   -256   -206       C  
ATOM   1489  N   TRP B  22       0.857 -14.334   8.583  1.00101.13           N  
ANISOU 1489  N   TRP B  22    11022  18059   9343   1102   -101    313       N  
ATOM   1490  CA  TRP B  22       0.610 -15.769   8.513  1.00112.58           C  
ANISOU 1490  CA  TRP B  22    12366  19552  10856   1053     10    498       C  
ATOM   1491  C   TRP B  22       1.831 -16.553   8.053  1.00134.74           C  
ANISOU 1491  C   TRP B  22    15145  22313  13738    946      7    604       C  
ATOM   1492  O   TRP B  22       2.038 -17.684   8.508  1.00140.20           O  
ANISOU 1492  O   TRP B  22    15759  23067  14444    932     53    747       O  
ATOM   1493  CB  TRP B  22      -0.565 -16.060   7.571  1.00104.96           C  
ANISOU 1493  CB  TRP B  22    11375  18536   9970   1029     90    534       C  
ATOM   1494  CG  TRP B  22      -1.017 -17.498   7.579  1.00105.46           C  
ANISOU 1494  CG  TRP B  22    11336  18639  10097    989    178    719       C  
ATOM   1495  CD1 TRP B  22      -2.041 -18.029   8.309  1.00111.92           C  
ANISOU 1495  CD1 TRP B  22    12078  19568  10879   1044    231    804       C  
ATOM   1496  CD2 TRP B  22      -0.467 -18.581   6.814  1.00101.49           C  
ANISOU 1496  CD2 TRP B  22    10793  18069   9700    887    210    847       C  
ATOM   1497  NE1 TRP B  22      -2.159 -19.374   8.052  1.00111.57           N  
ANISOU 1497  NE1 TRP B  22    11957  19519  10918    971    283    985       N  
ATOM   1498  CE2 TRP B  22      -1.205 -19.737   7.138  1.00102.54           C  
ANISOU 1498  CE2 TRP B  22    10837  18262   9860    883    271   1005       C  
ATOM   1499  CE3 TRP B  22       0.577 -18.685   5.889  1.00105.65           C  
ANISOU 1499  CE3 TRP B  22    11344  18504  10296    805    187    844       C  
ATOM   1500  CZ2 TRP B  22      -0.932 -20.981   6.571  1.00 95.22           C  
ANISOU 1500  CZ2 TRP B  22     9860  17291   9030    805    301   1151       C  
ATOM   1501  CZ3 TRP B  22       0.848 -19.922   5.329  1.00107.09           C  
ANISOU 1501  CZ3 TRP B  22    11467  18656  10567    741    228    977       C  
ATOM   1502  CH2 TRP B  22       0.096 -21.052   5.671  1.00 99.31           C  
ANISOU 1502  CH2 TRP B  22    10408  17717   9609    744    280   1124       C  
ATOM   1503  N   THR B  23       2.642 -15.976   7.162  1.00147.55           N  
ANISOU 1503  N   THR B  23    16821  23837  15404    874    -55    543       N  
ATOM   1504  CA  THR B  23       3.794 -16.693   6.623  1.00154.30           C  
ANISOU 1504  CA  THR B  23    17633  24664  16329    780    -58    639       C  
ATOM   1505  C   THR B  23       4.795 -17.038   7.719  1.00148.16           C  
ANISOU 1505  C   THR B  23    16830  23968  15497    799   -105    685       C  
ATOM   1506  O   THR B  23       5.254 -18.182   7.819  1.00150.64           O  
ANISOU 1506  O   THR B  23    17070  24317  15848    772    -63    819       O  
ATOM   1507  CB  THR B  23       4.464 -15.864   5.526  1.00164.37           C  
ANISOU 1507  CB  THR B  23    18957  25847  17647    700   -127    567       C  
ATOM   1508  OG1 THR B  23       4.851 -14.590   6.055  1.00169.52           O  
ANISOU 1508  OG1 THR B  23    19691  26489  18230    727   -257    439       O  
ATOM   1509  CG2 THR B  23       3.511 -15.653   4.357  1.00166.39           C  
ANISOU 1509  CG2 THR B  23    19231  26028  17963    675    -73    540       C  
ATOM   1510  N   ALA B  24       5.151 -16.056   8.550  1.00141.66           N  
ANISOU 1510  N   ALA B  24    16069  23170  14586    851   -203    571       N  
ATOM   1511  CA  ALA B  24       6.074 -16.319   9.650  1.00126.66           C  
ANISOU 1511  CA  ALA B  24    14150  21349  12627    876   -255    603       C  
ATOM   1512  C   ALA B  24       5.465 -17.279  10.664  1.00120.92           C  
ANISOU 1512  C   ALA B  24    13353  20742  11850    946   -171    711       C  
ATOM   1513  O   ALA B  24       6.132 -18.215  11.118  1.00125.54           O  
ANISOU 1513  O   ALA B  24    13875  21382  12442    927   -158    835       O  
ATOM   1514  CB  ALA B  24       6.475 -15.008  10.323  1.00118.75           C  
ANISOU 1514  CB  ALA B  24    13238  20339  11542    927   -395    440       C  
ATOM   1515  N   GLN B  25       4.202 -17.073  11.018  1.00115.09           N  
ANISOU 1515  N   GLN B  25    12614  20052  11061   1024   -120    676       N  
ATOM   1516  CA  GLN B  25       3.514 -17.945  11.962  1.00113.73           C  
ANISOU 1516  CA  GLN B  25    12358  20013  10842   1082    -44    796       C  
ATOM   1517  C   GLN B  25       3.172 -19.287  11.322  1.00112.27           C  
ANISOU 1517  C   GLN B  25    12088  19805  10764   1007     45    982       C  
ATOM   1518  O   GLN B  25       3.961 -20.230  11.374  1.00110.02           O  
ANISOU 1518  O   GLN B  25    11755  19528  10521    956     46   1112       O  
ATOM   1519  CB  GLN B  25       2.243 -17.272  12.480  1.00112.35           C  
ANISOU 1519  CB  GLN B  25    12192  19913  10582   1192    -23    703       C  
ATOM   1520  CG  GLN B  25       1.371 -18.168  13.347  1.00121.15           C  
ANISOU 1520  CG  GLN B  25    13197  21183  11651   1242     59    847       C  
ATOM   1521  CD  GLN B  25       0.206 -17.418  13.964  1.00133.33           C  
ANISOU 1521  CD  GLN B  25    14735  22835  13090   1369     70    743       C  
ATOM   1522  OE1 GLN B  25       0.173 -16.188  13.954  1.00138.41           O  
ANISOU 1522  OE1 GLN B  25    15469  23443  13677   1440      3    547       O  
ATOM   1523  NE2 GLN B  25      -0.757 -18.157  14.502  1.00132.61           N  
ANISOU 1523  NE2 GLN B  25    14532  22881  12971   1400    145    879       N  
ATOM   1524  N   SER B  49       3.518  -1.018  11.747  1.00126.40           N  
ANISOU 1524  N   SER B  49    15373  20279  12374   1705  -2234  -1604       N  
ATOM   1525  CA  SER B  49       2.994   0.107  12.512  1.00130.34           C  
ANISOU 1525  CA  SER B  49    15978  20706  12837   1902  -2413  -1861       C  
ATOM   1526  C   SER B  49       1.641  -0.234  13.125  1.00143.89           C  
ANISOU 1526  C   SER B  49    17646  22624  14400   2125  -2210  -1928       C  
ATOM   1527  O   SER B  49       1.380  -1.384  13.478  1.00134.21           O  
ANISOU 1527  O   SER B  49    16303  21618  13074   2141  -1961  -1786       O  
ATOM   1528  CB  SER B  49       2.873   1.348  11.625  1.00118.73           C  
ANISOU 1528  CB  SER B  49    14618  18969  11524   1853  -2659  -1969       C  
ATOM   1529  OG  SER B  49       2.049   1.095  10.499  1.00106.55           O  
ANISOU 1529  OG  SER B  49    13041  17426  10017   1805  -2522  -1876       O  
ATOM   1530  N   GLU B  50       0.778   0.776  13.245  1.00165.96           N  
ANISOU 1530  N   GLU B  50    20520  25342  17193   2296  -2328  -2138       N  
ATOM   1531  CA  GLU B  50      -0.569   0.578  13.768  1.00169.43           C  
ANISOU 1531  CA  GLU B  50    20898  25978  17498   2518  -2154  -2209       C  
ATOM   1532  C   GLU B  50      -1.473  -0.170  12.803  1.00159.78           C  
ANISOU 1532  C   GLU B  50    19587  24834  16287   2455  -1921  -2047       C  
ATOM   1533  O   GLU B  50      -2.667  -0.317  13.089  1.00158.61           O  
ANISOU 1533  O   GLU B  50    19374  24842  16050   2620  -1782  -2087       O  
ATOM   1534  CB  GLU B  50      -1.200   1.926  14.118  1.00176.02           C  
ANISOU 1534  CB  GLU B  50    21839  26698  18341   2730  -2364  -2491       C  
ATOM   1535  CG  GLU B  50      -0.353   2.797  15.030  1.00183.21           C  
ANISOU 1535  CG  GLU B  50    22850  27495  19264   2803  -2629  -2679       C  
ATOM   1536  CD  GLU B  50      -0.080   2.148  16.375  1.00187.92           C  
ANISOU 1536  CD  GLU B  50    23365  28343  19691   2913  -2518  -2672       C  
ATOM   1537  OE1 GLU B  50       0.857   1.327  16.470  1.00188.04           O  
ANISOU 1537  OE1 GLU B  50    23330  28415  19700   2750  -2446  -2496       O  
ATOM   1538  OE2 GLU B  50      -0.810   2.456  17.339  1.00190.77           O  
ANISOU 1538  OE2 GLU B  50    23703  28855  19925   3170  -2506  -2839       O  
ATOM   1539  N   SER B  51      -0.940  -0.640  11.673  1.00153.76           N  
ANISOU 1539  N   SER B  51    18812  23976  15635   2224  -1881  -1864       N  
ATOM   1540  CA  SER B  51      -1.763  -1.364  10.715  1.00144.86           C  
ANISOU 1540  CA  SER B  51    17602  22912  14527   2158  -1668  -1711       C  
ATOM   1541  C   SER B  51      -2.284  -2.671  11.299  1.00145.39           C  
ANISOU 1541  C   SER B  51    17517  23240  14483   2202  -1387  -1561       C  
ATOM   1542  O   SER B  51      -3.327  -3.166  10.864  1.00145.49           O  
ANISOU 1542  O   SER B  51    17452  23342  14487   2226  -1214  -1484       O  
ATOM   1543  CB  SER B  51      -0.971  -1.629   9.434  1.00136.06           C  
ANISOU 1543  CB  SER B  51    16490  21659  13547   1907  -1687  -1545       C  
ATOM   1544  OG  SER B  51       0.279  -2.230   9.723  1.00131.26           O  
ANISOU 1544  OG  SER B  51    15845  21077  12949   1777  -1687  -1424       O  
ATOM   1545  N   ILE B  52      -1.582  -3.241  12.281  1.00145.86           N  
ANISOU 1545  N   ILE B  52    17530  23420  14472   2208  -1351  -1508       N  
ATOM   1546  CA  ILE B  52      -2.016  -4.511  12.857  1.00143.77           C  
ANISOU 1546  CA  ILE B  52    17113  23391  14123   2233  -1109  -1342       C  
ATOM   1547  C   ILE B  52      -3.151  -4.309  13.857  1.00140.53           C  
ANISOU 1547  C   ILE B  52    16642  23172  13582   2470  -1055  -1453       C  
ATOM   1548  O   ILE B  52      -3.978  -5.207  14.048  1.00143.20           O  
ANISOU 1548  O   ILE B  52    16841  23694  13875   2498   -858  -1315       O  
ATOM   1549  CB  ILE B  52      -0.827  -5.240  13.504  1.00145.81           C  
ANISOU 1549  CB  ILE B  52    17334  23709  14358   2146  -1095  -1228       C  
ATOM   1550  CG1 ILE B  52      -0.072  -4.302  14.448  1.00142.40           C  
ANISOU 1550  CG1 ILE B  52    17002  23231  13874   2240  -1314  -1420       C  
ATOM   1551  CG2 ILE B  52       0.099  -5.794  12.429  1.00146.72           C  
ANISOU 1551  CG2 ILE B  52    17449  23698  14601   1911  -1078  -1060       C  
ATOM   1552  CD1 ILE B  52       1.100  -4.956  15.145  1.00136.55           C  
ANISOU 1552  CD1 ILE B  52    16227  22554  13104   2166  -1314  -1319       C  
ATOM   1553  N   ARG B  53      -3.209  -3.145  14.510  1.00136.87           N  
ANISOU 1553  N   ARG B  53    16271  22670  13063   2643  -1238  -1696       N  
ATOM   1554  CA  ARG B  53      -4.305  -2.863  15.432  1.00133.73           C  
ANISOU 1554  CA  ARG B  53    15805  22468  12537   2891  -1198  -1818       C  
ATOM   1555  C   ARG B  53      -5.649  -2.838  14.715  1.00131.29           C  
ANISOU 1555  C   ARG B  53    15442  22191  12252   2942  -1095  -1805       C  
ATOM   1556  O   ARG B  53      -6.665  -3.265  15.280  1.00133.31           O  
ANISOU 1556  O   ARG B  53    15558  22680  12414   3072   -956  -1763       O  
ATOM   1557  CB  ARG B  53      -4.034  -1.539  16.151  1.00130.23           C  
ANISOU 1557  CB  ARG B  53    15487  21940  12054   3070  -1444  -2104       C  
ATOM   1558  CG  ARG B  53      -5.265  -0.715  16.487  1.00130.68           C  
ANISOU 1558  CG  ARG B  53    15535  22074  12044   3327  -1485  -2306       C  
ATOM   1559  CD  ARG B  53      -4.908   0.762  16.543  1.00130.79           C  
ANISOU 1559  CD  ARG B  53    15726  21853  12116   3433  -1783  -2589       C  
ATOM   1560  NE  ARG B  53      -6.029   1.616  16.165  1.00131.28           N  
ANISOU 1560  NE  ARG B  53    15817  21863  12199   3600  -1846  -2755       N  
ATOM   1561  CZ  ARG B  53      -5.897   2.868  15.740  1.00130.39           C  
ANISOU 1561  CZ  ARG B  53    15866  21478  12199   3645  -2104  -2964       C  
ATOM   1562  NH1 ARG B  53      -4.690   3.411  15.637  1.00128.33           N  
ANISOU 1562  NH1 ARG B  53    15745  20972  12044   3520  -2327  -3020       N  
ATOM   1563  NH2 ARG B  53      -6.968   3.580  15.415  1.00131.33           N  
ANISOU 1563  NH2 ARG B  53    16002  21561  12336   3809  -2153  -3108       N  
ATOM   1564  N   LYS B  54      -5.671  -2.375  13.463  1.00123.43           N  
ANISOU 1564  N   LYS B  54    14541  20973  11384   2833  -1164  -1824       N  
ATOM   1565  CA  LYS B  54      -6.910  -2.351  12.697  1.00123.08           C  
ANISOU 1565  CA  LYS B  54    14451  20945  11370   2869  -1071  -1807       C  
ATOM   1566  C   LYS B  54      -7.426  -3.748  12.374  1.00124.61           C  
ANISOU 1566  C   LYS B  54    14482  21293  11573   2752   -819  -1542       C  
ATOM   1567  O   LYS B  54      -8.593  -3.884  11.991  1.00136.94           O  
ANISOU 1567  O   LYS B  54    15966  22928  13137   2804   -721  -1510       O  
ATOM   1568  CB  LYS B  54      -6.717  -1.553  11.406  1.00125.19           C  
ANISOU 1568  CB  LYS B  54    14860  20935  11774   2763  -1216  -1875       C  
ATOM   1569  CG  LYS B  54      -6.269  -2.378  10.214  1.00123.94           C  
ANISOU 1569  CG  LYS B  54    14681  20688  11723   2506  -1111  -1652       C  
ATOM   1570  CD  LYS B  54      -6.062  -1.503   8.990  1.00123.70           C  
ANISOU 1570  CD  LYS B  54    14780  20402  11818   2409  -1278  -1719       C  
ATOM   1571  CE  LYS B  54      -5.703  -2.332   7.769  1.00121.71           C  
ANISOU 1571  CE  LYS B  54    14489  20095  11662   2172  -1162  -1498       C  
ATOM   1572  NZ  LYS B  54      -4.552  -3.234   8.044  1.00116.58           N  
ANISOU 1572  NZ  LYS B  54    13790  19490  11016   2027  -1099  -1340       N  
ATOM   1573  N   LEU B  55      -6.597  -4.784  12.513  1.00112.30           N  
ANISOU 1573  N   LEU B  55    12868  19772  10029   2597   -727  -1351       N  
ATOM   1574  CA  LEU B  55      -7.107  -6.145  12.410  1.00109.03           C  
ANISOU 1574  CA  LEU B  55    12293  19505   9628   2507   -513  -1106       C  
ATOM   1575  C   LEU B  55      -7.658  -6.655  13.730  1.00118.72           C  
ANISOU 1575  C   LEU B  55    13375  21008  10724   2648   -428  -1059       C  
ATOM   1576  O   LEU B  55      -8.595  -7.461  13.729  1.00119.74           O  
ANISOU 1576  O   LEU B  55    13361  21284  10850   2641   -288   -905       O  
ATOM   1577  CB  LEU B  55      -6.032  -7.111  11.901  1.00 96.03           C  
ANISOU 1577  CB  LEU B  55    10641  17773   8072   2281   -456   -911       C  
ATOM   1578  CG  LEU B  55      -5.580  -6.942  10.452  1.00 91.31           C  
ANISOU 1578  CG  LEU B  55    10135  16950   7611   2109   -494   -884       C  
ATOM   1579  CD1 LEU B  55      -6.797  -6.894   9.516  1.00 94.92           C  
ANISOU 1579  CD1 LEU B  55    10561  17382   8120   2114   -421   -869       C  
ATOM   1580  CD2 LEU B  55      -4.655  -5.765  10.227  1.00 86.21           C  
ANISOU 1580  CD2 LEU B  55     9651  16117   6987   2097   -710  -1056       C  
ATOM   1581  N   ALA B  56      -7.097  -6.211  14.856  1.00123.95           N  
ANISOU 1581  N   ALA B  56    14067  21748  11279   2771   -522  -1181       N  
ATOM   1582  CA  ALA B  56      -7.775  -6.409  16.128  1.00134.98           C  
ANISOU 1582  CA  ALA B  56    15330  23429  12528   2952   -467  -1184       C  
ATOM   1583  C   ALA B  56      -9.114  -5.690  16.152  1.00152.07           C  
ANISOU 1583  C   ALA B  56    17453  25687  14639   3145   -480  -1321       C  
ATOM   1584  O   ALA B  56     -10.008  -6.090  16.906  1.00160.14           O  
ANISOU 1584  O   ALA B  56    18315  26972  15558   3263   -393  -1255       O  
ATOM   1585  CB  ALA B  56      -6.900  -5.928  17.288  1.00132.05           C  
ANISOU 1585  CB  ALA B  56    15012  23111  12048   3064   -586  -1323       C  
ATOM   1586  N   GLU B  57      -9.267  -4.638  15.343  1.00155.87           N  
ANISOU 1586  N   GLU B  57    18071  25966  15189   3180   -598  -1502       N  
ATOM   1587  CA  GLU B  57     -10.575  -4.007  15.194  1.00157.76           C  
ANISOU 1587  CA  GLU B  57    18270  26275  15396   3352   -606  -1619       C  
ATOM   1588  C   GLU B  57     -11.559  -4.932  14.486  1.00152.78           C  
ANISOU 1588  C   GLU B  57    17504  25722  14822   3244   -435  -1401       C  
ATOM   1589  O   GLU B  57     -12.735  -5.001  14.863  1.00155.02           O  
ANISOU 1589  O   GLU B  57    17654  26216  15031   3379   -376  -1388       O  
ATOM   1590  CB  GLU B  57     -10.437  -2.683  14.442  1.00158.81           C  
ANISOU 1590  CB  GLU B  57    18591  26143  15606   3400   -791  -1856       C  
ATOM   1591  CG  GLU B  57      -9.592  -1.654  15.172  1.00160.48           C  
ANISOU 1591  CG  GLU B  57    18941  26261  15775   3525  -1002  -2095       C  
ATOM   1592  CD  GLU B  57     -10.114  -1.355  16.564  1.00159.31           C  
ANISOU 1592  CD  GLU B  57    18697  26373  15460   3796  -1023  -2225       C  
ATOM   1593  OE1 GLU B  57     -11.350  -1.285  16.737  1.00158.31           O  
ANISOU 1593  OE1 GLU B  57    18451  26430  15268   3956   -959  -2248       O  
ATOM   1594  OE2 GLU B  57      -9.289  -1.195  17.487  1.00157.88           O  
ANISOU 1594  OE2 GLU B  57    18553  26225  15210   3851  -1107  -2303       O  
ATOM   1595  N   GLN B  58     -11.102  -5.647  13.459  1.00144.90           N  
ANISOU 1595  N   GLN B  58    16536  24562  13958   3004   -365  -1230       N  
ATOM   1596  CA  GLN B  58     -11.940  -6.642  12.800  1.00136.96           C  
ANISOU 1596  CA  GLN B  58    15406  23612  13020   2883   -214  -1012       C  
ATOM   1597  C   GLN B  58     -12.030  -7.945  13.581  1.00130.78           C  
ANISOU 1597  C   GLN B  58    14455  23043  12192   2825    -89   -776       C  
ATOM   1598  O   GLN B  58     -12.734  -8.862  13.143  1.00128.58           O  
ANISOU 1598  O   GLN B  58    14068  22815  11971   2720     19   -580       O  
ATOM   1599  CB  GLN B  58     -11.421  -6.931  11.388  1.00131.47           C  
ANISOU 1599  CB  GLN B  58    14802  22664  12485   2660   -196   -925       C  
ATOM   1600  CG  GLN B  58     -11.242  -5.702  10.513  1.00128.77           C  
ANISOU 1600  CG  GLN B  58    14630  22097  12198   2684   -332  -1127       C  
ATOM   1601  CD  GLN B  58     -10.579  -6.026   9.187  1.00128.76           C  
ANISOU 1601  CD  GLN B  58    14707  21876  12338   2457   -318  -1026       C  
ATOM   1602  OE1 GLN B  58     -10.481  -7.190   8.797  1.00128.77           O  
ANISOU 1602  OE1 GLN B  58    14626  21892  12407   2297   -192   -812       O  
ATOM   1603  NE2 GLN B  58     -10.121  -4.996   8.486  1.00128.70           N  
ANISOU 1603  NE2 GLN B  58    14858  21665  12378   2445   -464  -1178       N  
ATOM   1604  N   GLY B  59     -11.344  -8.049  14.717  1.00125.37           N  
ANISOU 1604  N   GLY B  59    13749  22477  11406   2887   -113   -788       N  
ATOM   1605  CA  GLY B  59     -11.342  -9.269  15.498  1.00122.84           C  
ANISOU 1605  CA  GLY B  59    13276  22358  11041   2830    -11   -561       C  
ATOM   1606  C   GLY B  59     -10.535 -10.371  14.847  1.00126.05           C  
ANISOU 1606  C   GLY B  59    13695  22617  11580   2585     54   -351       C  
ATOM   1607  O   GLY B  59     -10.990 -11.516  14.757  1.00128.65           O  
ANISOU 1607  O   GLY B  59    13902  23024  11953   2478    153   -122       O  
ATOM   1608  N   LEU B  60      -9.331 -10.038  14.388  1.00125.95           N  
ANISOU 1608  N   LEU B  60    13830  22392  11634   2496    -15   -428       N  
ATOM   1609  CA  LEU B  60      -8.480 -10.985  13.682  1.00126.25           C  
ANISOU 1609  CA  LEU B  60    13887  22282  11800   2277     32   -254       C  
ATOM   1610  C   LEU B  60      -7.166 -11.281  14.387  1.00128.52           C  
ANISOU 1610  C   LEU B  60    14204  22574  12053   2237     -4   -225       C  
ATOM   1611  O   LEU B  60      -6.676 -12.408  14.292  1.00129.43           O  
ANISOU 1611  O   LEU B  60    14263  22679  12234   2095     61    -27       O  
ATOM   1612  CB  LEU B  60      -8.175 -10.476  12.264  1.00125.68           C  
ANISOU 1612  CB  LEU B  60    13948  21949  11857   2170    -12   -328       C  
ATOM   1613  CG  LEU B  60      -9.375 -10.291  11.330  1.00120.31           C  
ANISOU 1613  CG  LEU B  60    13249  21227  11237   2173     28   -335       C  
ATOM   1614  CD1 LEU B  60      -8.920  -9.833   9.953  1.00118.87           C  
ANISOU 1614  CD1 LEU B  60    13195  20796  11172   2057    -18   -395       C  
ATOM   1615  CD2 LEU B  60     -10.199 -11.566  11.231  1.00115.09           C  
ANISOU 1615  CD2 LEU B  60    12437  20669  10623   2090    150   -102       C  
ATOM   1616  N   VAL B  61      -6.582 -10.314  15.086  1.00130.61           N  
ANISOU 1616  N   VAL B  61    14556  22847  12221   2360   -116   -420       N  
ATOM   1617  CA  VAL B  61      -5.313 -10.538  15.769  1.00131.57           C  
ANISOU 1617  CA  VAL B  61    14711  22972  12306   2324   -164   -402       C  
ATOM   1618  C   VAL B  61      -5.440 -10.227  17.257  1.00131.24           C  
ANISOU 1618  C   VAL B  61    14615  23158  12090   2515   -197   -489       C  
ATOM   1619  O   VAL B  61      -6.305  -9.455  17.670  1.00132.21           O  
ANISOU 1619  O   VAL B  61    14723  23388  12122   2696   -229   -638       O  
ATOM   1620  CB  VAL B  61      -4.184  -9.703  15.136  1.00132.08           C  
ANISOU 1620  CB  VAL B  61    14951  22799  12434   2257   -301   -547       C  
ATOM   1621  CG1 VAL B  61      -3.939 -10.142  13.700  1.00124.04           C  
ANISOU 1621  CG1 VAL B  61    13964  21588  11577   2061   -259   -435       C  
ATOM   1622  CG2 VAL B  61      -4.516  -8.224  15.200  1.00137.82           C  
ANISOU 1622  CG2 VAL B  61    15793  23466  13108   2415   -441   -817       C  
ATOM   1623  N   THR B  70       0.376 -13.937  17.084  1.00112.08           N  
ANISOU 1623  N   THR B  70    12222  20422   9941   1831   -195    149       N  
ATOM   1624  CA  THR B  70      -0.717 -13.039  17.436  1.00112.83           C  
ANISOU 1624  CA  THR B  70    12325  20602   9942   1991   -208     -8       C  
ATOM   1625  C   THR B  70      -1.850 -13.137  16.420  1.00119.72           C  
ANISOU 1625  C   THR B  70    13168  21417  10904   1956   -128     31       C  
ATOM   1626  O   THR B  70      -2.180 -12.159  15.750  1.00125.14           O  
ANISOU 1626  O   THR B  70    13946  21986  11616   1988   -187   -130       O  
ATOM   1627  CB  THR B  70      -0.242 -11.577  17.525  1.00108.15           C  
ANISOU 1627  CB  THR B  70    11883  19907   9301   2078   -373   -274       C  
ATOM   1628  OG1 THR B  70       0.123 -11.110  16.220  1.00 96.03           O  
ANISOU 1628  OG1 THR B  70    10453  18139   7896   1961   -432   -325       O  
ATOM   1629  CG2 THR B  70       0.957 -11.462  18.453  1.00112.98           C  
ANISOU 1629  CG2 THR B  70    12536  20552   9840   2098   -473   -317       C  
ATOM   1630  N   LEU B  71      -2.442 -14.324  16.310  1.00120.53           N  
ANISOU 1630  N   LEU B  71    13142  21597  11056   1887     -8    248       N  
ATOM   1631  CA  LEU B  71      -3.527 -14.580  15.372  1.00115.94           C  
ANISOU 1631  CA  LEU B  71    12520  20967  10566   1841     66    310       C  
ATOM   1632  C   LEU B  71      -4.653 -15.300  16.095  1.00120.01           C  
ANISOU 1632  C   LEU B  71    12878  21702  11019   1900    153    456       C  
ATOM   1633  O   LEU B  71      -4.406 -16.248  16.848  1.00122.63           O  
ANISOU 1633  O   LEU B  71    13113  22161  11319   1872    191    626       O  
ATOM   1634  CB  LEU B  71      -3.047 -15.415  14.180  1.00109.52           C  
ANISOU 1634  CB  LEU B  71    11718  19977   9919   1654    103    450       C  
ATOM   1635  CG  LEU B  71      -2.708 -14.660  12.893  1.00103.43           C  
ANISOU 1635  CG  LEU B  71    11070  18988   9242   1587     51    325       C  
ATOM   1636  CD1 LEU B  71      -2.361 -15.633  11.777  1.00 92.64           C  
ANISOU 1636  CD1 LEU B  71     9684  17489   8028   1421    103    479       C  
ATOM   1637  CD2 LEU B  71      -3.859 -13.756  12.481  1.00108.20           C  
ANISOU 1637  CD2 LEU B  71    11704  19576   9829   1674     46    189       C  
ATOM   1638  N   THR B  72      -5.884 -14.850  15.866  1.00125.59           N  
ANISOU 1638  N   THR B  72    13553  22458  11706   1978    177    396       N  
ATOM   1639  CA  THR B  72      -7.056 -15.483  16.446  1.00135.36           C  
ANISOU 1639  CA  THR B  72    14632  23911  12888   2027    251    540       C  
ATOM   1640  C   THR B  72      -7.511 -16.643  15.563  1.00140.16           C  
ANISOU 1640  C   THR B  72    15176  24437  13642   1863    322    760       C  
ATOM   1641  O   THR B  72      -6.873 -16.987  14.565  1.00140.91           O  
ANISOU 1641  O   THR B  72    15345  24323  13872   1725    319    794       O  
ATOM   1642  CB  THR B  72      -8.181 -14.464  16.629  1.00136.10           C  
ANISOU 1642  CB  THR B  72    14712  24112  12887   2197    234    375       C  
ATOM   1643  OG1 THR B  72      -8.671 -14.054  15.346  1.00129.17           O  
ANISOU 1643  OG1 THR B  72    13908  23048  12122   2144    232    306       O  
ATOM   1644  CG2 THR B  72      -7.675 -13.244  17.384  1.00139.26           C  
ANISOU 1644  CG2 THR B  72    15201  24554  13158   2366    140    128       C  
ATOM   1645  N   ASP B  73      -8.632 -17.261  15.937  1.00145.26           N  
ANISOU 1645  N   ASP B  73    15679  25260  14255   1881    378    911       N  
ATOM   1646  CA  ASP B  73      -9.197 -18.324  15.111  1.00144.76           C  
ANISOU 1646  CA  ASP B  73    15558  25118  14325   1734    430   1112       C  
ATOM   1647  C   ASP B  73      -9.740 -17.764  13.802  1.00141.56           C  
ANISOU 1647  C   ASP B  73    15238  24528  14019   1703    426    999       C  
ATOM   1648  O   ASP B  73      -9.429 -18.274  12.720  1.00138.04           O  
ANISOU 1648  O   ASP B  73    14847  23884  13719   1563    435   1058       O  
ATOM   1649  CB  ASP B  73     -10.291 -19.064  15.879  1.00146.37           C  
ANISOU 1649  CB  ASP B  73    15583  25570  14460   1760    477   1309       C  
ATOM   1650  CG  ASP B  73     -11.073 -20.022  15.003  1.00140.63           C  
ANISOU 1650  CG  ASP B  73    14802  24765  13866   1622    516   1498       C  
ATOM   1651  OD1 ASP B  73     -10.444 -20.871  14.336  1.00137.60           O  
ANISOU 1651  OD1 ASP B  73    14455  24210  13617   1474    519   1613       O  
ATOM   1652  OD2 ASP B  73     -12.318 -19.926  14.982  1.00138.61           O  
ANISOU 1652  OD2 ASP B  73    14465  24625  13574   1666    538   1528       O  
ATOM   1653  N   SER B  74     -10.556 -16.710  13.883  1.00141.02           N  
ANISOU 1653  N   SER B  74    15181  24531  13870   1840    410    832       N  
ATOM   1654  CA  SER B  74     -11.061 -16.074  12.670  1.00128.44           C  
ANISOU 1654  CA  SER B  74    13672  22768  12361   1822    400    713       C  
ATOM   1655  C   SER B  74      -9.955 -15.344  11.920  1.00117.85           C  
ANISOU 1655  C   SER B  74    12495  21198  11084   1783    345    548       C  
ATOM   1656  O   SER B  74     -10.019 -15.220  10.691  1.00113.58           O  
ANISOU 1656  O   SER B  74    12026  20471  10658   1698    345    517       O  
ATOM   1657  CB  SER B  74     -12.195 -15.110  13.015  1.00125.74           C  
ANISOU 1657  CB  SER B  74    13295  22573  11908   1994    387    575       C  
ATOM   1658  OG  SER B  74     -13.266 -15.789  13.648  1.00126.20           O  
ANISOU 1658  OG  SER B  74    13188  22860  11902   2023    436    742       O  
ATOM   1659  N   GLY B  75      -8.941 -14.855  12.635  1.00117.02           N  
ANISOU 1659  N   GLY B  75    12448  21112  10903   1842    292    447       N  
ATOM   1660  CA  GLY B  75      -7.824 -14.208  11.964  1.00114.77           C  
ANISOU 1660  CA  GLY B  75    12311  20623  10674   1791    228    313       C  
ATOM   1661  C   GLY B  75      -7.008 -15.182  11.137  1.00105.85           C  
ANISOU 1661  C   GLY B  75    11196  19339   9682   1607    255    459       C  
ATOM   1662  O   GLY B  75      -6.737 -14.940   9.958  1.00102.91           O  
ANISOU 1662  O   GLY B  75    10906  18784   9411   1522    241    412       O  
ATOM   1663  N   ARG B  76      -6.606 -16.300  11.744  1.00103.33           N  
ANISOU 1663  N   ARG B  76    10793  19102   9366   1550    291    640       N  
ATOM   1664  CA  ARG B  76      -5.898 -17.338  11.007  1.00105.91           C  
ANISOU 1664  CA  ARG B  76    11120  19299   9823   1392    314    787       C  
ATOM   1665  C   ARG B  76      -6.791 -18.047   9.997  1.00110.37           C  
ANISOU 1665  C   ARG B  76    11643  19787  10504   1303    367    899       C  
ATOM   1666  O   ARG B  76      -6.272 -18.760   9.132  1.00121.25           O  
ANISOU 1666  O   ARG B  76    13040  21029  12000   1182    378    982       O  
ATOM   1667  CB  ARG B  76      -5.295 -18.354  11.979  1.00114.60           C  
ANISOU 1667  CB  ARG B  76    12138  20514  10891   1367    328    955       C  
ATOM   1668  CG  ARG B  76      -6.271 -19.406  12.475  1.00125.19           C  
ANISOU 1668  CG  ARG B  76    13338  22003  12227   1355    387   1163       C  
ATOM   1669  CD  ARG B  76      -5.565 -20.486  13.284  1.00131.53           C  
ANISOU 1669  CD  ARG B  76    14066  22893  13018   1309    394   1350       C  
ATOM   1670  NE  ARG B  76      -4.557 -21.196  12.502  1.00129.89           N  
ANISOU 1670  NE  ARG B  76    13903  22517  12934   1184    383   1423       N  
ATOM   1671  CZ  ARG B  76      -3.245 -21.029  12.642  1.00127.59           C  
ANISOU 1671  CZ  ARG B  76    13673  22172  12633   1173    341   1366       C  
ATOM   1672  NH1 ARG B  76      -2.778 -20.172  13.539  1.00127.28           N  
ANISOU 1672  NH1 ARG B  76    13670  22221  12470   1272    300   1235       N  
ATOM   1673  NH2 ARG B  76      -2.401 -21.719  11.887  1.00125.33           N  
ANISOU 1673  NH2 ARG B  76    13411  21752  12456   1068    332   1439       N  
ATOM   1674  N   ARG B  77      -8.109 -17.870  10.086  1.00106.06           N  
ANISOU 1674  N   ARG B  77    11040  19332   9924   1364    396    901       N  
ATOM   1675  CA  ARG B  77      -9.024 -18.382   9.075  1.00100.12           C  
ANISOU 1675  CA  ARG B  77    10264  18500   9278   1286    435    982       C  
ATOM   1676  C   ARG B  77      -9.263 -17.387   7.949  1.00101.19           C  
ANISOU 1676  C   ARG B  77    10502  18486   9461   1293    414    808       C  
ATOM   1677  O   ARG B  77      -9.682 -17.793   6.859  1.00103.29           O  
ANISOU 1677  O   ARG B  77    10776  18635   9836   1206    439    855       O  
ATOM   1678  CB  ARG B  77     -10.361 -18.768   9.718  1.00104.52           C  
ANISOU 1678  CB  ARG B  77    10693  19243   9775   1338    472   1095       C  
ATOM   1679  CG  ARG B  77     -11.125 -19.849   8.973  1.00116.66           C  
ANISOU 1679  CG  ARG B  77    12170  20730  11425   1222    512   1274       C  
ATOM   1680  CD  ARG B  77     -12.625 -19.687   9.154  1.00130.67           C  
ANISOU 1680  CD  ARG B  77    13859  22644  13147   1284    537   1302       C  
ATOM   1681  NE  ARG B  77     -13.096 -18.380   8.707  1.00135.38           N  
ANISOU 1681  NE  ARG B  77    14530  23202  13707   1382    517   1084       N  
ATOM   1682  CZ  ARG B  77     -14.372 -18.006   8.709  1.00136.52           C  
ANISOU 1682  CZ  ARG B  77    14618  23451  13804   1453    530   1062       C  
ATOM   1683  NH1 ARG B  77     -15.308 -18.842   9.137  1.00136.59           N  
ANISOU 1683  NH1 ARG B  77    14493  23615  13792   1431    564   1252       N  
ATOM   1684  NH2 ARG B  77     -14.712 -16.797   8.284  1.00137.40           N  
ANISOU 1684  NH2 ARG B  77    14802  23518  13886   1547    504    859       N  
ATOM   1685  N   ALA B  78      -9.010 -16.099   8.188  1.00100.30           N  
ANISOU 1685  N   ALA B  78    10467  18376   9267   1397    364    611       N  
ATOM   1686  CA  ALA B  78      -9.047 -15.100   7.129  1.00100.23           C  
ANISOU 1686  CA  ALA B  78    10564  18218   9300   1397    330    450       C  
ATOM   1687  C   ALA B  78      -7.724 -15.001   6.385  1.00100.35           C  
ANISOU 1687  C   ALA B  78    10673  18069   9387   1297    294    416       C  
ATOM   1688  O   ALA B  78      -7.717 -14.719   5.181  1.00106.78           O  
ANISOU 1688  O   ALA B  78    11547  18743  10283   1232    288    372       O  
ATOM   1689  CB  ALA B  78      -9.420 -13.730   7.702  1.00105.97           C  
ANISOU 1689  CB  ALA B  78    11338  19020   9907   1561    274    252       C  
ATOM   1690  N   ALA B  79      -6.603 -15.222   7.078  1.00 93.53           N  
ANISOU 1690  N   ALA B  79     9815  17235   8486   1285    267    441       N  
ATOM   1691  CA  ALA B  79      -5.319 -15.328   6.396  1.00 78.10           C  
ANISOU 1691  CA  ALA B  79     7923  15151   6601   1180    237    444       C  
ATOM   1692  C   ALA B  79      -5.279 -16.541   5.480  1.00 78.12           C  
ANISOU 1692  C   ALA B  79     7879  15071   6734   1053    295    597       C  
ATOM   1693  O   ALA B  79      -4.631 -16.501   4.430  1.00 79.74           O  
ANISOU 1693  O   ALA B  79     8132  15151   7017    969    282    578       O  
ATOM   1694  CB  ALA B  79      -4.183 -15.402   7.415  1.00 70.86           C  
ANISOU 1694  CB  ALA B  79     7009  14301   5614   1198    195    451       C  
ATOM   1695  N   LEU B  80      -5.964 -17.621   5.862  1.00 77.87           N  
ANISOU 1695  N   LEU B  80     7751  15116   6721   1042    350    750       N  
ATOM   1696  CA  LEU B  80      -6.052 -18.796   5.003  1.00 75.43           C  
ANISOU 1696  CA  LEU B  80     7402  14725   6533    934    392    888       C  
ATOM   1697  C   LEU B  80      -6.638 -18.440   3.642  1.00 72.30           C  
ANISOU 1697  C   LEU B  80     7053  14202   6218    895    403    818       C  
ATOM   1698  O   LEU B  80      -6.219 -18.986   2.615  1.00 74.32           O  
ANISOU 1698  O   LEU B  80     7321  14346   6571    808    414    853       O  
ATOM   1699  CB  LEU B  80      -6.897 -19.869   5.685  1.00 81.11           C  
ANISOU 1699  CB  LEU B  80     8011  15558   7247    934    434   1065       C  
ATOM   1700  CG  LEU B  80      -6.742 -21.313   5.214  1.00 91.24           C  
ANISOU 1700  CG  LEU B  80     9240  16792   8635    830    462   1247       C  
ATOM   1701  CD1 LEU B  80      -5.610 -21.997   5.961  1.00 99.30           C  
ANISOU 1701  CD1 LEU B  80    10230  17863   9636    811    446   1348       C  
ATOM   1702  CD2 LEU B  80      -8.051 -22.065   5.399  1.00 99.51           C  
ANISOU 1702  CD2 LEU B  80    10194  17915   9699    816    499   1395       C  
ATOM   1703  N   ALA B  81      -7.603 -17.522   3.617  1.00 78.42           N  
ANISOU 1703  N   ALA B  81     7849  15001   6946    967    399    715       N  
ATOM   1704  CA  ALA B  81      -8.224 -17.082   2.375  1.00 87.92           C  
ANISOU 1704  CA  ALA B  81     9096  16095   8215    940    405    643       C  
ATOM   1705  C   ALA B  81      -7.207 -16.408   1.464  1.00 94.21           C  
ANISOU 1705  C   ALA B  81     9981  16771   9045    892    366    543       C  
ATOM   1706  O   ALA B  81      -6.869 -16.945   0.405  1.00102.82           O  
ANISOU 1706  O   ALA B  81    11075  17761  10230    802    383    583       O  
ATOM   1707  CB  ALA B  81      -9.387 -16.131   2.665  1.00 91.65           C  
ANISOU 1707  CB  ALA B  81     9572  16637   8614   1047    398    544       C  
ATOM   1708  N   MET B  82      -6.711 -15.236   1.876  1.00 92.45           N  
ANISOU 1708  N   MET B  82     9823  16565   8737    952    307    415       N  
ATOM   1709  CA  MET B  82      -5.770 -14.485   1.048  1.00 87.58           C  
ANISOU 1709  CA  MET B  82     9288  15852   8137    899    254    332       C  
ATOM   1710  C   MET B  82      -4.530 -15.302   0.709  1.00 80.12           C  
ANISOU 1710  C   MET B  82     8321  14868   7253    800    261    421       C  
ATOM   1711  O   MET B  82      -3.951 -15.132  -0.370  1.00 80.47           O  
ANISOU 1711  O   MET B  82     8394  14830   7351    724    249    406       O  
ATOM   1712  CB  MET B  82      -5.367 -13.190   1.754  1.00 91.42           C  
ANISOU 1712  CB  MET B  82     9850  16373   8511    980    163    193       C  
ATOM   1713  CG  MET B  82      -6.447 -12.123   1.766  1.00 96.77           C  
ANISOU 1713  CG  MET B  82    10574  17062   9133   1084    130     65       C  
ATOM   1714  SD  MET B  82      -6.817 -11.505   0.114  1.00109.43           S  
ANISOU 1714  SD  MET B  82    12236  18537  10805   1019    114     17       S  
ATOM   1715  CE  MET B  82      -7.861 -10.104   0.505  1.00108.28           C  
ANISOU 1715  CE  MET B  82    12158  18422  10563   1177     37   -160       C  
ATOM   1716  N   VAL B  83      -4.110 -16.192   1.610  1.00 77.60           N  
ANISOU 1716  N   VAL B  83     7945  14620   6921    804    280    517       N  
ATOM   1717  CA  VAL B  83      -2.937 -17.016   1.340  1.00 69.29           C  
ANISOU 1717  CA  VAL B  83     6864  13541   5921    726    283    600       C  
ATOM   1718  C   VAL B  83      -3.258 -18.072   0.287  1.00 60.29           C  
ANISOU 1718  C   VAL B  83     5683  12331   4895    660    339    684       C  
ATOM   1719  O   VAL B  83      -2.417 -18.393  -0.560  1.00 66.22           O  
ANISOU 1719  O   VAL B  83     6430  13026   5703    597    338    696       O  
ATOM   1720  CB  VAL B  83      -2.410 -17.637   2.647  1.00 65.60           C  
ANISOU 1720  CB  VAL B  83     6350  13176   5398    758    278    681       C  
ATOM   1721  CG1 VAL B  83      -1.493 -18.808   2.358  1.00 68.93           C  
ANISOU 1721  CG1 VAL B  83     6721  13581   5886    689    296    797       C  
ATOM   1722  CG2 VAL B  83      -1.667 -16.588   3.463  1.00 50.34           C  
ANISOU 1722  CG2 VAL B  83     4473  11292   3363    807    204    580       C  
ATOM   1723  N   ARG B  84      -4.479 -18.616   0.305  1.00 54.44           N  
ANISOU 1723  N   ARG B  84     4904  11597   4182    677    382    739       N  
ATOM   1724  CA  ARG B  84      -4.881 -19.514  -0.776  1.00 61.82           C  
ANISOU 1724  CA  ARG B  84     5811  12457   5222    618    422    797       C  
ATOM   1725  C   ARG B  84      -4.981 -18.769  -2.103  1.00 74.65           C  
ANISOU 1725  C   ARG B  84     7490  13985   6889    589    415    692       C  
ATOM   1726  O   ARG B  84      -4.606 -19.309  -3.152  1.00 74.64           O  
ANISOU 1726  O   ARG B  84     7479  13918   6964    537    429    703       O  
ATOM   1727  CB  ARG B  84      -6.206 -20.198  -0.443  1.00 59.82           C  
ANISOU 1727  CB  ARG B  84     5501  12244   4983    634    461    888       C  
ATOM   1728  CG  ARG B  84      -6.074 -21.391   0.489  1.00 68.69           C  
ANISOU 1728  CG  ARG B  84     6545  13451   6102    625    478   1052       C  
ATOM   1729  CD  ARG B  84      -7.438 -21.935   0.889  1.00 86.35           C  
ANISOU 1729  CD  ARG B  84     8715  15753   8342    633    510   1159       C  
ATOM   1730  NE  ARG B  84      -8.272 -22.240  -0.272  1.00 92.79           N  
ANISOU 1730  NE  ARG B  84     9526  16485   9246    590    536   1157       N  
ATOM   1731  CZ  ARG B  84      -8.172 -23.349  -0.998  1.00 94.67           C  
ANISOU 1731  CZ  ARG B  84     9720  16668   9582    524    557   1245       C  
ATOM   1732  NH1 ARG B  84      -7.269 -24.270  -0.689  1.00 90.67           N  
ANISOU 1732  NH1 ARG B  84     9169  16182   9101    496    556   1350       N  
ATOM   1733  NH2 ARG B  84      -8.975 -23.538  -2.036  1.00 97.25           N  
ANISOU 1733  NH2 ARG B  84    10038  16927   9984    492    577   1226       N  
ATOM   1734  N   ARG B  85      -5.482 -17.532  -2.077  1.00 81.35           N  
ANISOU 1734  N   ARG B  85     8392  14835   7683    631    390    588       N  
ATOM   1735  CA  ARG B  85      -5.513 -16.693  -3.270  1.00 91.56           C  
ANISOU 1735  CA  ARG B  85     9738  16052   9001    602    373    500       C  
ATOM   1736  C   ARG B  85      -4.109 -16.504  -3.827  1.00101.67           C  
ANISOU 1736  C   ARG B  85    11033  17306  10290    541    344    488       C  
ATOM   1737  O   ARG B  85      -3.768 -17.071  -4.869  1.00100.43           O  
ANISOU 1737  O   ARG B  85    10853  17099  10207    487    365    511       O  
ATOM   1738  CB  ARG B  85      -6.141 -15.327  -2.975  1.00 89.33           C  
ANISOU 1738  CB  ARG B  85     9512  15792   8637    668    335    393       C  
ATOM   1739  CG  ARG B  85      -7.422 -15.364  -2.166  1.00 84.43           C  
ANISOU 1739  CG  ARG B  85     8863  15237   7977    751    358    396       C  
ATOM   1740  CD  ARG B  85      -8.637 -15.575  -3.051  1.00 87.71           C  
ANISOU 1740  CD  ARG B  85     9262  15608   8455    742    395    403       C  
ATOM   1741  NE  ARG B  85      -9.865 -15.143  -2.394  1.00 98.69           N  
ANISOU 1741  NE  ARG B  85    10636  17076   9786    834    400    372       N  
ATOM   1742  CZ  ARG B  85     -10.248 -13.874  -2.283  1.00104.86           C  
ANISOU 1742  CZ  ARG B  85    11469  17879  10494    915    359    249       C  
ATOM   1743  NH1 ARG B  85     -11.383 -13.575  -1.667  1.00107.28           N  
ANISOU 1743  NH1 ARG B  85    11745  18273  10744   1014    366    220       N  
ATOM   1744  NH2 ARG B  85      -9.499 -12.905  -2.791  1.00105.59           N  
ANISOU 1744  NH2 ARG B  85    11642  17914  10562    901    302    158       N  
ATOM   1745  N   HIS B  86      -3.282 -15.721  -3.133  1.00105.66           N  
ANISOU 1745  N   HIS B  86    11571  17859  10716    553    289    450       N  
ATOM   1746  CA  HIS B  86      -1.930 -15.444  -3.603  1.00109.42           C  
ANISOU 1746  CA  HIS B  86    12052  18333  11188    487    251    451       C  
ATOM   1747  C   HIS B  86      -1.058 -16.688  -3.454  1.00103.75           C  
ANISOU 1747  C   HIS B  86    11265  17638  10516    462    282    540       C  
ATOM   1748  O   HIS B  86      -0.055 -16.676  -2.734  1.00118.02           O  
ANISOU 1748  O   HIS B  86    13061  19503  12276    458    246    562       O  
ATOM   1749  CB  HIS B  86      -1.337 -14.254  -2.842  1.00123.39           C  
ANISOU 1749  CB  HIS B  86    13881  20146  12854    505    158    388       C  
ATOM   1750  CG  HIS B  86       0.021 -13.837  -3.319  1.00139.47           C  
ANISOU 1750  CG  HIS B  86    15920  22192  14881    422     95    404       C  
ATOM   1751  ND1 HIS B  86       0.766 -12.869  -2.682  1.00145.47           N  
ANISOU 1751  ND1 HIS B  86    16729  22978  15565    416    -24    362       N  
ATOM   1752  CD2 HIS B  86       0.766 -14.252  -4.371  1.00143.57           C  
ANISOU 1752  CD2 HIS B  86    16388  22704  15457    343    122    459       C  
ATOM   1753  CE1 HIS B  86       1.912 -12.707  -3.319  1.00146.17           C  
ANISOU 1753  CE1 HIS B  86    16790  23026  15722    319    -68    404       C  
ATOM   1754  NE2 HIS B  86       1.937 -13.535  -4.347  1.00144.13           N  
ANISOU 1754  NE2 HIS B  86    16466  22767  15528    279     26    464       N  
ATOM   1755  N   ARG B  87      -1.452 -17.766  -4.131  1.00 88.95           N  
ANISOU 1755  N   ARG B  87     9346  15723   8728    450    337    587       N  
ATOM   1756  CA  ARG B  87      -0.714 -19.022  -4.177  1.00 83.44           C  
ANISOU 1756  CA  ARG B  87     8584  15042   8078    437    362    663       C  
ATOM   1757  C   ARG B  87      -1.335 -19.875  -5.275  1.00 86.81           C  
ANISOU 1757  C   ARG B  87     8982  15406   8595    427    406    671       C  
ATOM   1758  O   ARG B  87      -0.646 -20.296  -6.212  1.00 93.69           O  
ANISOU 1758  O   ARG B  87     9821  16264   9512    406    414    660       O  
ATOM   1759  CB  ARG B  87      -0.747 -19.738  -2.822  1.00 79.90           C  
ANISOU 1759  CB  ARG B  87     8104  14658   7595    476    368    745       C  
ATOM   1760  CG  ARG B  87       0.566 -19.646  -2.048  1.00 77.06           C  
ANISOU 1760  CG  ARG B  87     7730  14371   7177    475    329    768       C  
ATOM   1761  CD  ARG B  87       0.510 -20.354  -0.701  1.00 73.77           C  
ANISOU 1761  CD  ARG B  87     7281  14030   6721    516    332    859       C  
ATOM   1762  NE  ARG B  87       1.182 -19.568   0.334  1.00 68.23           N  
ANISOU 1762  NE  ARG B  87     6606  13395   5925    538    276    828       N  
ATOM   1763  CZ  ARG B  87       1.642 -20.063   1.479  1.00 64.19           C  
ANISOU 1763  CZ  ARG B  87     6063  12964   5364    567    261    901       C  
ATOM   1764  NH1 ARG B  87       1.512 -21.353   1.750  1.00 65.60           N  
ANISOU 1764  NH1 ARG B  87     6177  13170   5576    572    299   1027       N  
ATOM   1765  NH2 ARG B  87       2.238 -19.266   2.356  1.00 54.84           N  
ANISOU 1765  NH2 ARG B  87     4910  11834   4094    592    201    852       N  
ATOM   1766  N   LEU B  88      -2.648 -20.109  -5.174  1.00 79.14           N  
ANISOU 1766  N   LEU B  88     8018  14408   7644    448    432    684       N  
ATOM   1767  CA  LEU B  88      -3.383 -20.682  -6.297  1.00 60.73           C  
ANISOU 1767  CA  LEU B  88     5670  12016   5389    436    463    672       C  
ATOM   1768  C   LEU B  88      -3.290 -19.793  -7.528  1.00 53.85           C  
ANISOU 1768  C   LEU B  88     4838  11095   4526    411    447    581       C  
ATOM   1769  O   LEU B  88      -3.291 -20.291  -8.660  1.00 52.08           O  
ANISOU 1769  O   LEU B  88     4592  10839   4357    401    463    556       O  
ATOM   1770  CB  LEU B  88      -4.847 -20.902  -5.913  1.00 60.33           C  
ANISOU 1770  CB  LEU B  88     5615  11962   5347    455    487    709       C  
ATOM   1771  CG  LEU B  88      -5.161 -22.134  -5.064  1.00 59.72           C  
ANISOU 1771  CG  LEU B  88     5466  11936   5289    462    514    838       C  
ATOM   1772  CD1 LEU B  88      -6.588 -22.080  -4.546  1.00 46.92           C  
ANISOU 1772  CD1 LEU B  88     3835  10340   3654    477    530    883       C  
ATOM   1773  CD2 LEU B  88      -4.935 -23.393  -5.876  1.00 65.14           C  
ANISOU 1773  CD2 LEU B  88     6080  12601   6069    443    540    877       C  
ATOM   1774  N   LEU B  89      -3.204 -18.477  -7.326  1.00 56.15           N  
ANISOU 1774  N   LEU B  89     5182  11395   4756    404    413    533       N  
ATOM   1775  CA  LEU B  89      -3.078 -17.554  -8.447  1.00 61.38           C  
ANISOU 1775  CA  LEU B  89     5875  12031   5417    369    394    474       C  
ATOM   1776  C   LEU B  89      -1.703 -17.655  -9.093  1.00 61.19           C  
ANISOU 1776  C   LEU B  89     5813  12035   5399    328    382    484       C  
ATOM   1777  O   LEU B  89      -1.588 -17.639 -10.323  1.00 61.26           O  
ANISOU 1777  O   LEU B  89     5808  12028   5439    305    387    461       O  
ATOM   1778  CB  LEU B  89      -3.353 -16.129  -7.972  1.00 69.61           C  
ANISOU 1778  CB  LEU B  89     6978  13091   6380    376    354    430       C  
ATOM   1779  CG  LEU B  89      -4.814 -15.831  -7.628  1.00 67.81           C  
ANISOU 1779  CG  LEU B  89     6781  12844   6139    429    365    399       C  
ATOM   1780  CD1 LEU B  89      -4.977 -14.383  -7.214  1.00 68.15           C  
ANISOU 1780  CD1 LEU B  89     6889  12913   6091    455    311    334       C  
ATOM   1781  CD2 LEU B  89      -5.713 -16.156  -8.809  1.00 55.77           C  
ANISOU 1781  CD2 LEU B  89     5249  11261   4681    418    395    385       C  
ATOM   1782  N   GLU B  90      -0.647 -17.762  -8.282  1.00 72.35           N  
ANISOU 1782  N   GLU B  90     7203  13508   6780    323    365    520       N  
ATOM   1783  CA  GLU B  90       0.693 -17.912  -8.839  1.00 74.03           C  
ANISOU 1783  CA  GLU B  90     7361  13769   6996    289    355    538       C  
ATOM   1784  C   GLU B  90       0.833 -19.235  -9.583  1.00 68.64           C  
ANISOU 1784  C   GLU B  90     6622  13075   6384    322    391    537       C  
ATOM   1785  O   GLU B  90       1.307 -19.269 -10.726  1.00 71.49           O  
ANISOU 1785  O   GLU B  90     6950  13451   6763    310    391    512       O  
ATOM   1786  CB  GLU B  90       1.744 -17.799  -7.734  1.00 83.64           C  
ANISOU 1786  CB  GLU B  90     8560  15062   8159    283    326    579       C  
ATOM   1787  CG  GLU B  90       1.878 -16.405  -7.140  1.00 89.81           C  
ANISOU 1787  CG  GLU B  90     9397  15875   8851    250    267    565       C  
ATOM   1788  CD  GLU B  90       3.060 -16.285  -6.196  1.00 86.30           C  
ANISOU 1788  CD  GLU B  90     8933  15508   8349    235    220    602       C  
ATOM   1789  OE1 GLU B  90       3.698 -17.318  -5.906  1.00 80.59           O  
ANISOU 1789  OE1 GLU B  90     8147  14824   7650    258    248    644       O  
ATOM   1790  OE2 GLU B  90       3.354 -15.158  -5.745  1.00 82.89           O  
ANISOU 1790  OE2 GLU B  90     8553  15063   7881    203    132    581       O  
ATOM   1791  N   THR B  91       0.414 -20.340  -8.955  1.00 58.54           N  
ANISOU 1791  N   THR B  91     5323  11784   5137    367    418    567       N  
ATOM   1792  CA  THR B  91       0.516 -21.634  -9.621  1.00 61.25           C  
ANISOU 1792  CA  THR B  91     5602  12126   5544    408    447    559       C  
ATOM   1793  C   THR B  91      -0.419 -21.742 -10.819  1.00 64.67           C  
ANISOU 1793  C   THR B  91     6048  12506   6018    415    462    498       C  
ATOM   1794  O   THR B  91      -0.153 -22.541 -11.725  1.00 65.76           O  
ANISOU 1794  O   THR B  91     6131  12659   6195    454    473    455       O  
ATOM   1795  CB  THR B  91       0.251 -22.773  -8.630  1.00 57.73           C  
ANISOU 1795  CB  THR B  91     5111  11695   5127    444    470    630       C  
ATOM   1796  OG1 THR B  91       0.528 -24.031  -9.257  1.00 70.07           O  
ANISOU 1796  OG1 THR B  91     6612  13222   6788    489    463    611       O  
ATOM   1797  CG2 THR B  91      -1.182 -22.760  -8.156  1.00 78.41           C  
ANISOU 1797  CG2 THR B  91     7767  14272   7754    439    487    662       C  
ATOM   1798  N   PHE B  92      -1.496 -20.952 -10.854  1.00 66.93           N  
ANISOU 1798  N   PHE B  92     6398  12741   6290    392    460    484       N  
ATOM   1799  CA  PHE B  92      -2.332 -20.907 -12.049  1.00 63.26           C  
ANISOU 1799  CA  PHE B  92     5947  12236   5854    394    468    427       C  
ATOM   1800  C   PHE B  92      -1.653 -20.126 -13.165  1.00 62.39           C  
ANISOU 1800  C   PHE B  92     5842  12149   5716    368    446    386       C  
ATOM   1801  O   PHE B  92      -1.687 -20.539 -14.330  1.00 59.60           O  
ANISOU 1801  O   PHE B  92     5461  11804   5379    391    452    335       O  
ATOM   1802  CB  PHE B  92      -3.693 -20.292 -11.726  1.00 56.59           C  
ANISOU 1802  CB  PHE B  92     5157  11341   5002    384    472    429       C  
ATOM   1803  CG  PHE B  92      -4.664 -20.341 -12.872  1.00 63.12           C  
ANISOU 1803  CG  PHE B  92     5991  12133   5859    390    482    377       C  
ATOM   1804  CD1 PHE B  92      -5.262 -21.534 -13.241  1.00 64.92           C  
ANISOU 1804  CD1 PHE B  92     6164  12357   6146    420    508    369       C  
ATOM   1805  CD2 PHE B  92      -4.972 -19.195 -13.587  1.00 67.89           C  
ANISOU 1805  CD2 PHE B  92     6642  12720   6433    364    462    339       C  
ATOM   1806  CE1 PHE B  92      -6.154 -21.583 -14.297  1.00 68.12           C  
ANISOU 1806  CE1 PHE B  92     6567  12741   6573    428    513    314       C  
ATOM   1807  CE2 PHE B  92      -5.862 -19.238 -14.645  1.00 63.02           C  
ANISOU 1807  CE2 PHE B  92     6029  12080   5837    372    468    294       C  
ATOM   1808  CZ  PHE B  92      -6.453 -20.434 -15.000  1.00 68.13           C  
ANISOU 1808  CZ  PHE B  92     6628  12724   6536    405    494    276       C  
ATOM   1809  N   LEU B  93      -1.039 -18.989 -12.828  1.00 57.99           N  
ANISOU 1809  N   LEU B  93     5308  11618   5108    319    417    413       N  
ATOM   1810  CA  LEU B  93      -0.334 -18.204 -13.835  1.00 59.24           C  
ANISOU 1810  CA  LEU B  93     5449  11823   5235    276    396    410       C  
ATOM   1811  C   LEU B  93       0.814 -18.998 -14.444  1.00 63.97           C  
ANISOU 1811  C   LEU B  93     5973  12494   5841    303    400    403       C  
ATOM   1812  O   LEU B  93       0.996 -19.001 -15.667  1.00 67.59           O  
ANISOU 1812  O   LEU B  93     6403  12989   6289    309    398    375       O  
ATOM   1813  CB  LEU B  93       0.175 -16.901 -13.220  1.00 60.80           C  
ANISOU 1813  CB  LEU B  93     5668  12059   5376    211    362    456       C  
ATOM   1814  CG  LEU B  93      -0.895 -15.858 -12.885  1.00 55.21           C  
ANISOU 1814  CG  LEU B  93     5034  11306   4639    195    346    443       C  
ATOM   1815  CD1 LEU B  93      -0.282 -14.653 -12.183  1.00 49.58           C  
ANISOU 1815  CD1 LEU B  93     4345  10647   3848    140    298    479       C  
ATOM   1816  CD2 LEU B  93      -1.649 -15.436 -14.138  1.00 56.88           C  
ANISOU 1816  CD2 LEU B  93     5261  11493   4859    182    349    418       C  
ATOM   1817  N   VAL B  94       1.591 -19.691 -13.609  1.00 66.45           N  
ANISOU 1817  N   VAL B  94     6249  12839   6160    329    404    427       N  
ATOM   1818  CA  VAL B  94       2.703 -20.486 -14.123  1.00 63.86           C  
ANISOU 1818  CA  VAL B  94     5842  12590   5833    373    406    411       C  
ATOM   1819  C   VAL B  94       2.189 -21.702 -14.883  1.00 72.43           C  
ANISOU 1819  C   VAL B  94     6900  13660   6961    460    430    334       C  
ATOM   1820  O   VAL B  94       2.561 -21.936 -16.039  1.00 84.67           O  
ANISOU 1820  O   VAL B  94     8410  15268   8493    499    427    280       O  
ATOM   1821  CB  VAL B  94       3.644 -20.903 -12.979  1.00 57.26           C  
ANISOU 1821  CB  VAL B  94     4966  11798   4994    384    402    459       C  
ATOM   1822  CG1 VAL B  94       4.725 -21.832 -13.504  1.00 49.11           C  
ANISOU 1822  CG1 VAL B  94     3845  10849   3967    452    405    430       C  
ATOM   1823  CG2 VAL B  94       4.270 -19.684 -12.330  1.00 46.38           C  
ANISOU 1823  CG2 VAL B  94     3598  10461   3563    301    371    524       C  
ATOM   1824  N   ASN B  95       1.322 -22.492 -14.247  1.00 76.35           N  
ANISOU 1824  N   ASN B  95     7405  14096   7509    494    452    330       N  
ATOM   1825  CA  ASN B  95       0.989 -23.805 -14.786  1.00 77.92           C  
ANISOU 1825  CA  ASN B  95     7541  14299   7767    584    467    261       C  
ATOM   1826  C   ASN B  95       0.038 -23.725 -15.972  1.00 76.98           C  
ANISOU 1826  C   ASN B  95     7443  14156   7649    598    470    186       C  
ATOM   1827  O   ASN B  95       0.162 -24.511 -16.918  1.00 78.97           O  
ANISOU 1827  O   ASN B  95     7636  14452   7918    682    465     93       O  
ATOM   1828  CB  ASN B  95       0.388 -24.680 -13.689  1.00 80.45           C  
ANISOU 1828  CB  ASN B  95     7851  14547   8170    599    468    311       C  
ATOM   1829  CG  ASN B  95       1.439 -25.456 -12.931  1.00 78.84           C  
ANISOU 1829  CG  ASN B  95     7603  14343   8008    637    436    346       C  
ATOM   1830  OD1 ASN B  95       2.143 -24.905 -12.085  1.00 62.81           O  
ANISOU 1830  OD1 ASN B  95     5574  12369   5921    598    444    414       O  
ATOM   1831  ND2 ASN B  95       1.557 -26.743 -13.232  1.00 89.46           N  
ANISOU 1831  ND2 ASN B  95     8912  15619   9462    719    386    294       N  
ATOM   1832  N   GLU B  96      -0.920 -22.800 -15.946  1.00 76.34           N  
ANISOU 1832  N   GLU B  96     7440  14013   7552    531    471    213       N  
ATOM   1833  CA  GLU B  96      -1.897 -22.698 -17.026  1.00 65.62           C  
ANISOU 1833  CA  GLU B  96     6101  12636   6196    542    472    150       C  
ATOM   1834  C   GLU B  96      -1.550 -21.599 -18.025  1.00 65.65           C  
ANISOU 1834  C   GLU B  96     6133  12676   6134    502    450    144       C  
ATOM   1835  O   GLU B  96      -1.363 -21.880 -19.211  1.00 69.37           O  
ANISOU 1835  O   GLU B  96     6569  13210   6580    549    443     76       O  
ATOM   1836  CB  GLU B  96      -3.304 -22.489 -16.454  1.00 59.51           C  
ANISOU 1836  CB  GLU B  96     5374  11782   5455    507    486    182       C  
ATOM   1837  CG  GLU B  96      -3.934 -23.770 -15.914  1.00 59.70           C  
ANISOU 1837  CG  GLU B  96     5340  11776   5569    548    499    189       C  
ATOM   1838  CD  GLU B  96      -4.179 -24.818 -16.987  1.00 69.58           C  
ANISOU 1838  CD  GLU B  96     6557  12979   6900    618    455     87       C  
ATOM   1839  OE1 GLU B  96      -4.377 -24.439 -18.160  1.00 81.26           O  
ANISOU 1839  OE1 GLU B  96     8035  14515   8326    637    462     10       O  
ATOM   1840  OE2 GLU B  96      -4.166 -26.024 -16.656  1.00 70.02           O  
ANISOU 1840  OE2 GLU B  96     6589  12940   7076    656    402     83       O  
ATOM   1841  N   LEU B  97      -1.444 -20.352 -17.572  1.00 63.35           N  
ANISOU 1841  N   LEU B  97     5891  12364   5815    420    436    215       N  
ATOM   1842  CA  LEU B  97      -1.238 -19.237 -18.490  1.00 67.06           C  
ANISOU 1842  CA  LEU B  97     6368  12876   6235    370    414    235       C  
ATOM   1843  C   LEU B  97       0.228 -19.023 -18.864  1.00 73.26           C  
ANISOU 1843  C   LEU B  97     7090  13771   6974    355    398    270       C  
ATOM   1844  O   LEU B  97       0.585 -17.950 -19.371  1.00 73.22           O  
ANISOU 1844  O   LEU B  97     7073  13819   6926    288    378    329       O  
ATOM   1845  CB  LEU B  97      -1.841 -17.962 -17.901  1.00 68.29           C  
ANISOU 1845  CB  LEU B  97     6587  12977   6382    297    401    289       C  
ATOM   1846  CG  LEU B  97      -3.369 -18.005 -17.857  1.00 83.40           C  
ANISOU 1846  CG  LEU B  97     8553  14809   8327    315    414    253       C  
ATOM   1847  CD1 LEU B  97      -3.922 -16.639 -17.560  1.00 91.09           C  
ANISOU 1847  CD1 LEU B  97     9582  15756   9273    261    396    288       C  
ATOM   1848  CD2 LEU B  97      -3.930 -18.515 -19.177  1.00 84.49           C  
ANISOU 1848  CD2 LEU B  97     8671  14965   8468    357    420    187       C  
ATOM   1849  N   GLY B  98       1.075 -20.024 -18.638  1.00 70.68           N  
ANISOU 1849  N   GLY B  98     6710  13492   6653    416    406    245       N  
ATOM   1850  CA  GLY B  98       2.421 -20.009 -19.174  1.00 72.80           C  
ANISOU 1850  CA  GLY B  98     6902  13886   6871    425    393    264       C  
ATOM   1851  C   GLY B  98       3.334 -18.946 -18.611  1.00 80.54           C  
ANISOU 1851  C   GLY B  98     7866  14914   7822    328    372    372       C  
ATOM   1852  O   GLY B  98       4.270 -18.518 -19.296  1.00 90.39           O  
ANISOU 1852  O   GLY B  98     9047  16281   9016    301    356    419       O  
ATOM   1853  N   TYR B  99       3.091 -18.499 -17.383  1.00 83.39           N  
ANISOU 1853  N   TYR B  99     8275  15202   8209    277    368    416       N  
ATOM   1854  CA  TYR B  99       4.038 -17.600 -16.744  1.00 85.81           C  
ANISOU 1854  CA  TYR B  99     8553  15569   8483    193    343    509       C  
ATOM   1855  C   TYR B  99       5.319 -18.361 -16.403  1.00 77.02           C  
ANISOU 1855  C   TYR B  99     7364  14539   7360    233    343    518       C  
ATOM   1856  O   TYR B  99       5.442 -19.569 -16.625  1.00 69.59           O  
ANISOU 1856  O   TYR B  99     6398  13605   6437    332    363    448       O  
ATOM   1857  CB  TYR B  99       3.418 -16.954 -15.508  1.00 88.27           C  
ANISOU 1857  CB  TYR B  99     8935  15800   8804    148    335    534       C  
ATOM   1858  CG  TYR B  99       2.564 -15.740 -15.808  1.00 79.91           C  
ANISOU 1858  CG  TYR B  99     7931  14706   7723     82    319    555       C  
ATOM   1859  CD1 TYR B  99       1.406 -15.847 -16.568  1.00 75.84           C  
ANISOU 1859  CD1 TYR B  99     7460  14126   7231    115    335    500       C  
ATOM   1860  CD2 TYR B  99       2.913 -14.487 -15.320  1.00 73.58           C  
ANISOU 1860  CD2 TYR B  99     7137  13948   6871    -12    281    630       C  
ATOM   1861  CE1 TYR B  99       0.625 -14.738 -16.839  1.00 80.42           C  
ANISOU 1861  CE1 TYR B  99     8088  14682   7786     63    318    520       C  
ATOM   1862  CE2 TYR B  99       2.139 -13.375 -15.584  1.00 73.46           C  
ANISOU 1862  CE2 TYR B  99     7181  13909   6822    -65    256    650       C  
ATOM   1863  CZ  TYR B  99       0.997 -13.506 -16.345  1.00 83.05           C  
ANISOU 1863  CZ  TYR B  99     8435  15056   8064    -24    278    595       C  
ATOM   1864  OH  TYR B  99       0.222 -12.402 -16.612  1.00 88.90           O  
ANISOU 1864  OH  TYR B  99     9236  15778   8765    -70    247    615       O  
ATOM   1865  N   ARG B 100       6.288 -17.642 -15.846  1.00 83.92           N  
ANISOU 1865  N   ARG B 100     8195  15488   8203    157    317    605       N  
ATOM   1866  CA  ARG B 100       7.636 -18.173 -15.669  1.00 97.30           C  
ANISOU 1866  CA  ARG B 100     9803  17289   9877    183    311    630       C  
ATOM   1867  C   ARG B 100       8.237 -17.716 -14.348  1.00102.52           C  
ANISOU 1867  C   ARG B 100    10453  17969  10532    121    289    699       C  
ATOM   1868  O   ARG B 100       9.355 -17.204 -14.311  1.00118.86           O  
ANISOU 1868  O   ARG B 100    12443  20154  12564     56    262    780       O  
ATOM   1869  CB  ARG B 100       8.543 -17.723 -16.809  1.00 97.24           C  
ANISOU 1869  CB  ARG B 100     9708  17426   9812    148    295    685       C  
ATOM   1870  CG  ARG B 100       8.506 -18.557 -18.064  1.00 96.88           C  
ANISOU 1870  CG  ARG B 100     9634  17432   9746    251    315    605       C  
ATOM   1871  CD  ARG B 100       9.562 -18.034 -19.018  1.00106.77           C  
ANISOU 1871  CD  ARG B 100    10785  18861  10921    212    296    685       C  
ATOM   1872  NE  ARG B 100       9.448 -18.596 -20.358  1.00117.24           N  
ANISOU 1872  NE  ARG B 100    12078  20266  12201    305    309    612       N  
ATOM   1873  CZ  ARG B 100      10.314 -19.461 -20.875  1.00119.15           C  
ANISOU 1873  CZ  ARG B 100    12244  20638  12391    412    317    560       C  
ATOM   1874  NH1 ARG B 100      11.362 -19.861 -20.165  1.00125.46           N  
ANISOU 1874  NH1 ARG B 100    12993  21491  13184    433    315    580       N  
ATOM   1875  NH2 ARG B 100      10.136 -19.920 -22.105  1.00112.88           N  
ANISOU 1875  NH2 ARG B 100    11419  19929  11542    504    324    484       N  
ATOM   1876  N   TRP B 101       7.498 -17.915 -13.249  1.00 99.32           N  
ANISOU 1876  N   TRP B 101    10119  17465  10154    141    298    671       N  
ATOM   1877  CA  TRP B 101       7.778 -17.390 -11.907  1.00 96.51           C  
ANISOU 1877  CA  TRP B 101     9774  17123   9772     91    275    722       C  
ATOM   1878  C   TRP B 101       8.437 -16.009 -11.941  1.00 90.24           C  
ANISOU 1878  C   TRP B 101     8942  16426   8920    -38    231    815       C  
ATOM   1879  O   TRP B 101       8.281 -15.277 -12.924  1.00 81.35           O  
ANISOU 1879  O   TRP B 101     7806  15321   7781   -100    220    848       O  
ATOM   1880  CB  TRP B 101       8.577 -18.425 -11.081  1.00 94.45           C  
ANISOU 1880  CB  TRP B 101     9462  16901   9525    157    282    723       C  
ATOM   1881  CG  TRP B 101      10.082 -18.604 -11.294  1.00101.96           C  
ANISOU 1881  CG  TRP B 101    10298  17983  10458    149    265    770       C  
ATOM   1882  CD1 TRP B 101      10.860 -18.079 -12.284  1.00106.37           C  
ANISOU 1882  CD1 TRP B 101    10787  18642  10987     96    247    815       C  
ATOM   1883  CD2 TRP B 101      10.951 -19.443 -10.515  1.00107.29           C  
ANISOU 1883  CD2 TRP B 101    10913  18710  11144    205    262    780       C  
ATOM   1884  NE1 TRP B 101      12.161 -18.508 -12.151  1.00112.46           N  
ANISOU 1884  NE1 TRP B 101    11464  19522  11743    116    235    849       N  
ATOM   1885  CE2 TRP B 101      12.242 -19.348 -11.072  1.00110.88           C  
ANISOU 1885  CE2 TRP B 101    11268  19288  11572    186    242    822       C  
ATOM   1886  CE3 TRP B 101      10.763 -20.251  -9.388  1.00102.54           C  
ANISOU 1886  CE3 TRP B 101    10326  18069  10566    269    273    769       C  
ATOM   1887  CZ2 TRP B 101      13.339 -20.030 -10.541  1.00108.37           C  
ANISOU 1887  CZ2 TRP B 101    10872  19045  11258    234    231    839       C  
ATOM   1888  CZ3 TRP B 101      11.852 -20.928  -8.863  1.00 95.89           C  
ANISOU 1888  CZ3 TRP B 101     9397  17304   9734    314    259    794       C  
ATOM   1889  CH2 TRP B 101      13.123 -20.813  -9.439  1.00103.68           C  
ANISOU 1889  CH2 TRP B 101    10293  18401  10701    300    237    821       C  
ATOM   1890  N   ASP B 102       9.082 -15.598 -10.846  1.00 93.85           N  
ANISOU 1890  N   ASP B 102     9400  16896   9363    -84    175    859       N  
ATOM   1891  CA  ASP B 102       9.735 -14.292 -10.699  1.00 99.44           C  
ANISOU 1891  CA  ASP B 102    10107  17605  10071   -212     70    939       C  
ATOM   1892  C   ASP B 102       8.944 -13.080 -11.210  1.00 99.78           C  
ANISOU 1892  C   ASP B 102    10230  17560  10120   -291     15    953       C  
ATOM   1893  O   ASP B 102       9.379 -11.940 -11.021  1.00 94.75           O  
ANISOU 1893  O   ASP B 102     9610  16885   9504   -401   -100   1017       O  
ATOM   1894  CB  ASP B 102      11.120 -14.311 -11.363  1.00 99.12           C  
ANISOU 1894  CB  ASP B 102     9908  17738  10016   -271     72   1035       C  
ATOM   1895  CG  ASP B 102      11.068 -14.070 -12.861  1.00105.43           C  
ANISOU 1895  CG  ASP B 102    10629  18647  10781   -308    121   1083       C  
ATOM   1896  OD1 ASP B 102      10.891 -15.046 -13.619  1.00109.60           O  
ANISOU 1896  OD1 ASP B 102    11153  19171  11320   -198    175   1011       O  
ATOM   1897  OD2 ASP B 102      11.256 -12.912 -13.286  1.00109.41           O  
ANISOU 1897  OD2 ASP B 102    11124  19157  11290   -436     48   1181       O  
ATOM   1898  N   GLU B 103       7.793 -13.299 -11.858  1.00106.49           N  
ANISOU 1898  N   GLU B 103    11131  18369  10961   -237     81    895       N  
ATOM   1899  CA  GLU B 103       6.897 -12.206 -12.225  1.00111.23           C  
ANISOU 1899  CA  GLU B 103    11822  18867  11571   -291     25    893       C  
ATOM   1900  C   GLU B 103       5.438 -12.589 -11.992  1.00100.36           C  
ANISOU 1900  C   GLU B 103    10548  17391  10194   -192     77    787       C  
ATOM   1901  O   GLU B 103       4.536 -11.950 -12.548  1.00102.32           O  
ANISOU 1901  O   GLU B 103    10857  17575  10446   -207     61    772       O  
ATOM   1902  CB  GLU B 103       7.111 -11.768 -13.684  1.00122.66           C  
ANISOU 1902  CB  GLU B 103    13192  20411  13002   -367     39    979       C  
ATOM   1903  CG  GLU B 103       6.665 -10.333 -13.998  1.00134.57           C  
ANISOU 1903  CG  GLU B 103    14774  21817  14539   -471    -72   1032       C  
ATOM   1904  CD  GLU B 103       6.981  -9.344 -12.886  1.00145.96           C  
ANISOU 1904  CD  GLU B 103    16294  23131  16033   -537   -224   1044       C  
ATOM   1905  OE1 GLU B 103       8.124  -9.346 -12.382  1.00150.99           O  
ANISOU 1905  OE1 GLU B 103    16865  23822  16681   -589   -271   1101       O  
ATOM   1906  OE2 GLU B 103       6.077  -8.566 -12.511  1.00149.27           O  
ANISOU 1906  OE2 GLU B 103    16840  23396  16481   -528   -306    984       O  
ATOM   1907  N   VAL B 104       5.186 -13.623 -11.185  1.00 90.55           N  
ANISOU 1907  N   VAL B 104     9316  16140   8949    -95    134    727       N  
ATOM   1908  CA  VAL B 104       3.828 -13.958 -10.769  1.00 74.05           C  
ANISOU 1908  CA  VAL B 104     7310  13966   6859    -12    173    648       C  
ATOM   1909  C   VAL B 104       3.451 -13.298  -9.454  1.00 76.48           C  
ANISOU 1909  C   VAL B 104     7713  14195   7151      5     97    612       C  
ATOM   1910  O   VAL B 104       2.266 -13.302  -9.086  1.00 87.03           O  
ANISOU 1910  O   VAL B 104     9117  15477   8472     68    117    553       O  
ATOM   1911  CB  VAL B 104       3.656 -15.485 -10.646  1.00 65.51           C  
ANISOU 1911  CB  VAL B 104     6185  12896   5810     80    260    617       C  
ATOM   1912  CG1 VAL B 104       3.940 -16.151 -11.977  1.00 64.44           C  
ANISOU 1912  CG1 VAL B 104     5980  12774   5729     93    293    610       C  
ATOM   1913  CG2 VAL B 104       4.575 -16.035  -9.566  1.00 59.20           C  
ANISOU 1913  CG2 VAL B 104     5349  12153   4993    100    251    646       C  
ATOM   1914  N   HIS B 105       4.417 -12.726  -8.734  1.00 83.27           N  
ANISOU 1914  N   HIS B 105     8573  15058   8006    -44      5    641       N  
ATOM   1915  CA  HIS B 105       4.130 -12.096  -7.450  1.00 90.26           C  
ANISOU 1915  CA  HIS B 105     9548  15883   8862    -11    -81    588       C  
ATOM   1916  C   HIS B 105       3.347 -10.802  -7.635  1.00 88.40           C  
ANISOU 1916  C   HIS B 105     9409  15545   8634    -29   -173    540       C  
ATOM   1917  O   HIS B 105       2.265 -10.626  -7.063  1.00 92.04           O  
ANISOU 1917  O   HIS B 105     9945  15965   9060     56   -174    460       O  
ATOM   1918  CB  HIS B 105       5.438 -11.830  -6.701  1.00 87.86           C  
ANISOU 1918  CB  HIS B 105     9215  15607   8559    -60   -171    626       C  
ATOM   1919  CG  HIS B 105       5.277 -11.732  -5.217  1.00 79.30           C  
ANISOU 1919  CG  HIS B 105     8196  14510   7424     12   -227    565       C  
ATOM   1920  ND1 HIS B 105       5.265 -12.838  -4.395  1.00 80.50           N  
ANISOU 1920  ND1 HIS B 105     8319  14733   7536     93   -151    566       N  
ATOM   1921  CD2 HIS B 105       5.116 -10.659  -4.407  1.00 80.11           C  
ANISOU 1921  CD2 HIS B 105     8389  14546   7503     24   -360    497       C  
ATOM   1922  CE1 HIS B 105       5.110 -12.449  -3.141  1.00 86.52           C  
ANISOU 1922  CE1 HIS B 105     9144  15495   8236    150   -223    512       C  
ATOM   1923  NE2 HIS B 105       5.014 -11.132  -3.122  1.00 84.31           N  
ANISOU 1923  NE2 HIS B 105     8939  15132   7962    118   -351    456       N  
ATOM   1924  N   ASP B 106       3.882  -9.882  -8.443  1.00 90.96           N  
ANISOU 1924  N   ASP B 106     9724  15833   9004   -139   -257    598       N  
ATOM   1925  CA  ASP B 106       3.255  -8.577  -8.619  1.00 99.92           C  
ANISOU 1925  CA  ASP B 106    10953  16847  10166   -165   -377    563       C  
ATOM   1926  C   ASP B 106       1.877  -8.673  -9.259  1.00102.78           C  
ANISOU 1926  C   ASP B 106    11355  17180  10516   -102   -302    512       C  
ATOM   1927  O   ASP B 106       1.104  -7.712  -9.184  1.00105.34           O  
ANISOU 1927  O   ASP B 106    11770  17402  10852    -81   -393    453       O  
ATOM   1928  CB  ASP B 106       4.160  -7.672  -9.458  1.00109.58           C  
ANISOU 1928  CB  ASP B 106    12138  18044  11452   -316   -483    673       C  
ATOM   1929  CG  ASP B 106       5.330  -7.123  -8.664  1.00116.11           C  
ANISOU 1929  CG  ASP B 106    12959  18850  12309   -386   -622    707       C  
ATOM   1930  OD1 ASP B 106       5.458  -7.474  -7.472  1.00117.88           O  
ANISOU 1930  OD1 ASP B 106    13209  19085  12493   -309   -631    635       O  
ATOM   1931  OD2 ASP B 106       6.123  -6.341  -9.232  1.00118.34           O  
ANISOU 1931  OD2 ASP B 106    13201  19109  12654   -524   -728    816       O  
ATOM   1932  N   GLU B 107       1.551  -9.804  -9.885  1.00100.44           N  
ANISOU 1932  N   GLU B 107    10992  16966  10204    -67   -152    528       N  
ATOM   1933  CA  GLU B 107       0.225 -10.010 -10.455  1.00 93.07           C  
ANISOU 1933  CA  GLU B 107    10088  16011   9263     -6    -80    480       C  
ATOM   1934  C   GLU B 107      -0.751 -10.586  -9.435  1.00 86.45           C  
ANISOU 1934  C   GLU B 107     9286  15180   8382    115    -23    398       C  
ATOM   1935  O   GLU B 107      -1.833 -10.030  -9.226  1.00 75.70           O  
ANISOU 1935  O   GLU B 107     7993  13766   7004    175    -51    329       O  
ATOM   1936  CB  GLU B 107       0.311 -10.927 -11.678  1.00 89.95           C  
ANISOU 1936  CB  GLU B 107     9603  15696   8877    -25     35    529       C  
ATOM   1937  CG  GLU B 107       1.221 -10.412 -12.778  1.00 99.55           C  
ANISOU 1937  CG  GLU B 107    10760  16955  10110   -136     -2    624       C  
ATOM   1938  CD  GLU B 107       0.448  -9.725 -13.887  1.00103.61           C  
ANISOU 1938  CD  GLU B 107    11302  17430  10634   -167    -21    638       C  
ATOM   1939  OE1 GLU B 107      -0.208 -10.430 -14.681  1.00103.31           O  
ANISOU 1939  OE1 GLU B 107    11235  17438  10581   -121     76    613       O  
ATOM   1940  OE2 GLU B 107       0.493  -8.479 -13.961  1.00106.46           O  
ANISOU 1940  OE2 GLU B 107    11718  17708  11024   -237   -145    673       O  
ATOM   1941  N   ALA B 108      -0.381 -11.697  -8.791  1.00 85.30           N  
ANISOU 1941  N   ALA B 108     9086  15107   8217    153     52    415       N  
ATOM   1942  CA  ALA B 108      -1.272 -12.320  -7.818  1.00 78.66           C  
ANISOU 1942  CA  ALA B 108     8258  14296   7331    255    109    372       C  
ATOM   1943  C   ALA B 108      -1.503 -11.423  -6.608  1.00 94.23           C  
ANISOU 1943  C   ALA B 108    10307  16253   9242    313     15    303       C  
ATOM   1944  O   ALA B 108      -2.557 -11.509  -5.966  1.00108.65           O  
ANISOU 1944  O   ALA B 108    12158  18111  11015    407     46    252       O  
ATOM   1945  CB  ALA B 108      -0.706 -13.670  -7.380  1.00 65.86           C  
ANISOU 1945  CB  ALA B 108     6562  12743   5719    272    186    424       C  
ATOM   1946  N   GLU B 109      -0.538 -10.557  -6.284  1.00 90.88           N  
ANISOU 1946  N   GLU B 109     9916  15790   8824    263   -107    298       N  
ATOM   1947  CA  GLU B 109      -0.715  -9.620  -5.180  1.00 97.46           C  
ANISOU 1947  CA  GLU B 109    10831  16596   9603    329   -224    207       C  
ATOM   1948  C   GLU B 109      -1.801  -8.588  -5.470  1.00108.57           C  
ANISOU 1948  C   GLU B 109    12319  17921  11012    377   -292    120       C  
ATOM   1949  O   GLU B 109      -2.268  -7.918  -4.543  1.00118.30           O  
ANISOU 1949  O   GLU B 109    13618  19147  12183    476   -375     15       O  
ATOM   1950  CB  GLU B 109       0.610  -8.918  -4.868  1.00101.48           C  
ANISOU 1950  CB  GLU B 109    11355  17061  10143    251   -363    224       C  
ATOM   1951  CG  GLU B 109       0.659  -8.207  -3.517  1.00117.59           C  
ANISOU 1951  CG  GLU B 109    13469  19094  12117    333   -491    122       C  
ATOM   1952  CD  GLU B 109       0.906  -9.150  -2.350  1.00129.75           C  
ANISOU 1952  CD  GLU B 109    14965  20765  13568    407   -421    129       C  
ATOM   1953  OE1 GLU B 109       0.079 -10.056  -2.120  1.00132.19           O  
ANISOU 1953  OE1 GLU B 109    15238  21168  13821    483   -287    142       O  
ATOM   1954  OE2 GLU B 109       1.930  -8.981  -1.655  1.00134.65           O  
ANISOU 1954  OE2 GLU B 109    15585  21397  14178    383   -510    132       O  
ATOM   1955  N   VAL B 110      -2.209  -8.444  -6.729  1.00101.42           N  
ANISOU 1955  N   VAL B 110    11407  16961  10168    321   -263    154       N  
ATOM   1956  CA  VAL B 110      -3.289  -7.547  -7.106  1.00 96.24           C  
ANISOU 1956  CA  VAL B 110    10821  16225   9520    368   -321     80       C  
ATOM   1957  C   VAL B 110      -4.564  -8.312  -7.442  1.00 98.53           C  
ANISOU 1957  C   VAL B 110    11077  16579   9783    439   -180     69       C  
ATOM   1958  O   VAL B 110      -5.663  -7.872  -7.098  1.00103.11           O  
ANISOU 1958  O   VAL B 110    11699  17156  10321    543   -198    -18       O  
ATOM   1959  CB  VAL B 110      -2.860  -6.642  -8.281  1.00 91.91           C  
ANISOU 1959  CB  VAL B 110    10296  15561   9063    247   -420    136       C  
ATOM   1960  CG1 VAL B 110      -3.979  -5.684  -8.655  1.00 95.73           C  
ANISOU 1960  CG1 VAL B 110    10858  15949   9566    300   -497     61       C  
ATOM   1961  CG2 VAL B 110      -1.592  -5.881  -7.924  1.00 88.34           C  
ANISOU 1961  CG2 VAL B 110     9867  15045   8654    160   -574    165       C  
ATOM   1962  N   LEU B 111      -4.436  -9.464  -8.107  1.00 94.70           N  
ANISOU 1962  N   LEU B 111    10508  16151   9323    391    -50    153       N  
ATOM   1963  CA  LEU B 111      -5.599 -10.304  -8.372  1.00 87.10           C  
ANISOU 1963  CA  LEU B 111     9504  15241   8348    448     72    152       C  
ATOM   1964  C   LEU B 111      -6.231 -10.811  -7.083  1.00 92.58           C  
ANISOU 1964  C   LEU B 111    10181  16018   8978    555    121    121       C  
ATOM   1965  O   LEU B 111      -7.449 -11.018  -7.031  1.00101.66           O  
ANISOU 1965  O   LEU B 111    11316  17166  10146    621    171     96       O  
ATOM   1966  CB  LEU B 111      -5.206 -11.482  -9.264  1.00 84.08           C  
ANISOU 1966  CB  LEU B 111     9039  14890   8018    382    174    235       C  
ATOM   1967  CG  LEU B 111      -5.181 -11.254 -10.775  1.00 78.55           C  
ANISOU 1967  CG  LEU B 111     8330  14144   7373    309    173    261       C  
ATOM   1968  CD1 LEU B 111      -5.136 -12.584 -11.503  1.00 76.04           C  
ANISOU 1968  CD1 LEU B 111     7932  13833   7126    292    270    301       C  
ATOM   1969  CD2 LEU B 111      -6.401 -10.462 -11.199  1.00 76.58           C  
ANISOU 1969  CD2 LEU B 111     8134  13840   7122    349    141    205       C  
ATOM   1970  N   GLU B 112      -5.426 -11.001  -6.034  1.00 94.64           N  
ANISOU 1970  N   GLU B 112    10435  16320   9205    567     99    131       N  
ATOM   1971  CA  GLU B 112      -5.937 -11.476  -4.751  1.00 97.68           C  
ANISOU 1971  CA  GLU B 112    10794  16756   9566    661    136    119       C  
ATOM   1972  C   GLU B 112      -7.061 -10.604  -4.204  1.00100.14           C  
ANISOU 1972  C   GLU B 112    11151  17090   9806    780     96     14       C  
ATOM   1973  O   GLU B 112      -7.835 -11.070  -3.360  1.00105.80           O  
ANISOU 1973  O   GLU B 112    11822  17866  10511    861    150     19       O  
ATOM   1974  CB  GLU B 112      -4.795 -11.545  -3.739  1.00 97.84           C  
ANISOU 1974  CB  GLU B 112    10815  16822   9538    658     92    133       C  
ATOM   1975  CG  GLU B 112      -4.354 -10.180  -3.246  1.00 99.10           C  
ANISOU 1975  CG  GLU B 112    11066  16982   9606    693    -57     31       C  
ATOM   1976  CD  GLU B 112      -3.040 -10.223  -2.503  1.00 91.71           C  
ANISOU 1976  CD  GLU B 112    10129  16076   8640    661   -121     53       C  
ATOM   1977  OE1 GLU B 112      -2.563  -9.149  -2.085  1.00 85.30           O  
ANISOU 1977  OE1 GLU B 112     9389  15227   7792    676   -272    -29       O  
ATOM   1978  OE2 GLU B 112      -2.484 -11.327  -2.340  1.00 86.19           O  
ANISOU 1978  OE2 GLU B 112     9357  15411   7982    620    -37    149       O  
ATOM   1979  N   HIS B 113      -7.167  -9.354  -4.657  1.00 99.16           N  
ANISOU 1979  N   HIS B 113    11111  16928   9635    796    -11    -75       N  
ATOM   1980  CA  HIS B 113      -8.225  -8.447  -4.232  1.00100.57           C  
ANISOU 1980  CA  HIS B 113    11341  17121   9751    927    -70   -198       C  
ATOM   1981  C   HIS B 113      -9.322  -8.308  -5.282  1.00 96.69           C  
ANISOU 1981  C   HIS B 113    10845  16597   9296    931    -33   -206       C  
ATOM   1982  O   HIS B 113      -9.934  -7.241  -5.404  1.00100.91           O  
ANISOU 1982  O   HIS B 113    11448  17096   9799   1008   -130   -312       O  
ATOM   1983  CB  HIS B 113      -7.638  -7.077  -3.890  1.00107.50           C  
ANISOU 1983  CB  HIS B 113    12326  17930  10589    959   -263   -313       C  
ATOM   1984  CG  HIS B 113      -6.537  -7.127  -2.877  1.00111.33           C  
ANISOU 1984  CG  HIS B 113    12819  18453  11027    957   -320   -316       C  
ATOM   1985  ND1 HIS B 113      -6.745  -7.516  -1.571  1.00111.93           N  
ANISOU 1985  ND1 HIS B 113    12863  18630  11036   1065   -272   -347       N  
ATOM   1986  CD2 HIS B 113      -5.219  -6.834  -2.977  1.00113.12           C  
ANISOU 1986  CD2 HIS B 113    13075  18586  11321    848   -417   -281       C  
ATOM   1987  CE1 HIS B 113      -5.602  -7.463  -0.911  1.00112.30           C  
ANISOU 1987  CE1 HIS B 113    12927  18681  11059   1036   -344   -344       C  
ATOM   1988  NE2 HIS B 113      -4.660  -7.052  -1.741  1.00112.98           N  
ANISOU 1988  NE2 HIS B 113    13049  18666  11212    906   -439   -307       N  
ATOM   1989  N   ALA B 114      -9.584  -9.370  -6.045  1.00 90.93           N  
ANISOU 1989  N   ALA B 114    10039  15854   8656    854     88   -101       N  
ATOM   1990  CA  ALA B 114     -10.613  -9.331  -7.077  1.00 77.55           C  
ANISOU 1990  CA  ALA B 114     8333  14129   7003    851    124   -104       C  
ATOM   1991  C   ALA B 114     -11.092 -10.732  -7.437  1.00 69.80           C  
ANISOU 1991  C   ALA B 114     7254  13141   6126    802    245     -2       C  
ATOM   1992  O   ALA B 114     -11.942 -10.894  -8.318  1.00 74.79           O  
ANISOU 1992  O   ALA B 114     7865  13746   6806    790    278      6       O  
ATOM   1993  CB  ALA B 114     -10.095  -8.616  -8.327  1.00 70.35           C  
ANISOU 1993  CB  ALA B 114     7480  13117   6131    758     47   -100       C  
ATOM   1994  N   VAL B 115     -10.555 -11.747  -6.768  1.00 66.08           N  
ANISOU 1994  N   VAL B 115     6728  12689   5688    773    290     74       N  
ATOM   1995  CA  VAL B 115     -10.968 -13.128  -6.986  1.00 66.96           C  
ANISOU 1995  CA  VAL B 115     6762  12786   5894    729    365    170       C  
ATOM   1996  C   VAL B 115     -12.063 -13.481  -5.989  1.00 71.56           C  
ANISOU 1996  C   VAL B 115     7291  13447   6451    809    393    192       C  
ATOM   1997  O   VAL B 115     -11.928 -13.227  -4.786  1.00 78.39           O  
ANISOU 1997  O   VAL B 115     8153  14391   7242    878    376    175       O  
ATOM   1998  CB  VAL B 115      -9.776 -14.091  -6.858  1.00 65.47           C  
ANISOU 1998  CB  VAL B 115     6545  12579   5750    656    381    249       C  
ATOM   1999  CG1 VAL B 115     -10.231 -15.527  -7.059  1.00 63.71           C  
ANISOU 1999  CG1 VAL B 115     6254  12339   5613    620    436    341       C  
ATOM   2000  CG2 VAL B 115      -8.705 -13.744  -7.872  1.00 71.79           C  
ANISOU 2000  CG2 VAL B 115     7380  13329   6570    579    355    237       C  
ATOM   2001  N   SER B 116     -13.150 -14.059  -6.488  1.00 71.53           N  
ANISOU 2001  N   SER B 116     7240  13437   6502    799    432    232       N  
ATOM   2002  CA  SER B 116     -14.220 -14.552  -5.638  1.00 71.12           C  
ANISOU 2002  CA  SER B 116     7118  13476   6431    853    462    287       C  
ATOM   2003  C   SER B 116     -13.910 -15.973  -5.176  1.00 63.46           C  
ANISOU 2003  C   SER B 116     6082  12520   5508    790    498    423       C  
ATOM   2004  O   SER B 116     -13.037 -16.653  -5.719  1.00 57.93           O  
ANISOU 2004  O   SER B 116     5391  11748   4873    711    504    463       O  
ATOM   2005  CB  SER B 116     -15.560 -14.515  -6.375  1.00 72.34           C  
ANISOU 2005  CB  SER B 116     7244  13629   6614    867    480    279       C  
ATOM   2006  OG  SER B 116     -15.560 -15.394  -7.487  1.00 77.36           O  
ANISOU 2006  OG  SER B 116     7863  14180   7349    770    505    334       O  
ATOM   2007  N   ASP B 117     -14.642 -16.414  -4.149  1.00 61.77           N  
ANISOU 2007  N   ASP B 117     5797  12417   5253    833    519    499       N  
ATOM   2008  CA  ASP B 117     -14.455 -17.769  -3.639  1.00 71.31           C  
ANISOU 2008  CA  ASP B 117     6936  13659   6500    774    549    650       C  
ATOM   2009  C   ASP B 117     -14.784 -18.807  -4.705  1.00 69.00           C  
ANISOU 2009  C   ASP B 117     6611  13289   6318    682    577    724       C  
ATOM   2010  O   ASP B 117     -14.135 -19.857  -4.783  1.00 60.33           O  
ANISOU 2010  O   ASP B 117     5484  12159   5278    615    589    812       O  
ATOM   2011  CB  ASP B 117     -15.315 -17.983  -2.394  1.00 88.33           C  
ANISOU 2011  CB  ASP B 117     9008  15972   8581    835    564    733       C  
ATOM   2012  CG  ASP B 117     -14.985 -17.006  -1.282  1.00 97.74           C  
ANISOU 2012  CG  ASP B 117    10222  17261   9655    944    535    647       C  
ATOM   2013  OD1 ASP B 117     -15.331 -15.812  -1.415  1.00101.68           O  
ANISOU 2013  OD1 ASP B 117    10767  17767  10100   1029    508    509       O  
ATOM   2014  OD2 ASP B 117     -14.380 -17.431  -0.276  1.00 99.52           O  
ANISOU 2014  OD2 ASP B 117    10416  17558   9837    951    534    716       O  
ATOM   2015  N   ARG B 118     -15.790 -18.527  -5.536  1.00 81.39           N  
ANISOU 2015  N   ARG B 118     8176  14834   7913    685    583    683       N  
ATOM   2016  CA  ARG B 118     -16.128 -19.430  -6.632  1.00 82.60           C  
ANISOU 2016  CA  ARG B 118     8296  14918   8170    607    604    731       C  
ATOM   2017  C   ARG B 118     -15.008 -19.487  -7.664  1.00 82.15           C  
ANISOU 2017  C   ARG B 118     8298  14747   8167    560    591    663       C  
ATOM   2018  O   ARG B 118     -14.630 -20.573  -8.124  1.00 85.65           O  
ANISOU 2018  O   ARG B 118     8701  15154   8688    499    605    724       O  
ATOM   2019  CB  ARG B 118     -17.443 -18.982  -7.272  1.00 80.66           C  
ANISOU 2019  CB  ARG B 118     8035  14684   7930    630    609    689       C  
ATOM   2020  CG  ARG B 118     -17.642 -19.410  -8.715  1.00 88.80           C  
ANISOU 2020  CG  ARG B 118     9062  15624   9054    569    615    664       C  
ATOM   2021  CD  ARG B 118     -18.665 -18.512  -9.399  1.00 82.60           C  
ANISOU 2021  CD  ARG B 118     8295  14841   8250    612    606    576       C  
ATOM   2022  NE  ARG B 118     -19.989 -19.126  -9.455  1.00 86.61           N  
ANISOU 2022  NE  ARG B 118     8706  15408   8793    595    629    660       N  
ATOM   2023  CZ  ARG B 118     -21.113 -18.455  -9.687  1.00 91.03           C  
ANISOU 2023  CZ  ARG B 118     9251  16013   9322    645    626    616       C  
ATOM   2024  NH1 ARG B 118     -22.274 -19.093  -9.719  1.00 91.21           N  
ANISOU 2024  NH1 ARG B 118     9174  16097   9385    618    647    708       N  
ATOM   2025  NH2 ARG B 118     -21.076 -17.144  -9.888  1.00 90.67           N  
ANISOU 2025  NH2 ARG B 118     9283  15958   9211    721    599    487       N  
ATOM   2026  N   LEU B 119     -14.459 -18.326  -8.028  1.00 76.46           N  
ANISOU 2026  N   LEU B 119     7662  13983   7405    591    560    542       N  
ATOM   2027  CA  LEU B 119     -13.353 -18.282  -8.978  1.00 70.96           C  
ANISOU 2027  CA  LEU B 119     7013  13203   6744    547    544    488       C  
ATOM   2028  C   LEU B 119     -12.134 -19.018  -8.434  1.00 74.33           C  
ANISOU 2028  C   LEU B 119     7427  13633   7182    519    546    546       C  
ATOM   2029  O   LEU B 119     -11.493 -19.797  -9.149  1.00 70.30           O  
ANISOU 2029  O   LEU B 119     6898  13081   6731    476    553    558       O  
ATOM   2030  CB  LEU B 119     -13.004 -16.829  -9.301  1.00 61.00           C  
ANISOU 2030  CB  LEU B 119     5831  11920   5428    578    507    379       C  
ATOM   2031  CG  LEU B 119     -11.877 -16.579 -10.305  1.00 59.64           C  
ANISOU 2031  CG  LEU B 119     5701  11685   5276    529    487    335       C  
ATOM   2032  CD1 LEU B 119     -12.008 -17.500 -11.504  1.00 46.95           C  
ANISOU 2032  CD1 LEU B 119     4060  10033   3744    484    506    346       C  
ATOM   2033  CD2 LEU B 119     -11.862 -15.123 -10.743  1.00 66.41           C  
ANISOU 2033  CD2 LEU B 119     6620  12536   6076    549    450    253       C  
ATOM   2034  N   MET B 120     -11.798 -18.778  -7.165  1.00 71.62           N  
ANISOU 2034  N   MET B 120     7086  13353   6775    554    537    575       N  
ATOM   2035  CA  MET B 120     -10.649 -19.447  -6.561  1.00 77.15           C  
ANISOU 2035  CA  MET B 120     7768  14068   7476    532    536    636       C  
ATOM   2036  C   MET B 120     -10.859 -20.955  -6.500  1.00 70.64           C  
ANISOU 2036  C   MET B 120     6860  13260   6721    491    570    762       C  
ATOM   2037  O   MET B 120      -9.939 -21.732  -6.791  1.00 67.94           O  
ANISOU 2037  O   MET B 120     6496  12895   6425    459    573    791       O  
ATOM   2038  CB  MET B 120     -10.393 -18.873  -5.167  1.00 92.88           C  
ANISOU 2038  CB  MET B 120     9770  16142   9377    586    519    641       C  
ATOM   2039  CG  MET B 120      -9.401 -19.661  -4.329  1.00106.87           C  
ANISOU 2039  CG  MET B 120    11509  17955  11140    570    519    728       C  
ATOM   2040  SD  MET B 120      -9.682 -19.451  -2.558  1.00117.02           S  
ANISOU 2040  SD  MET B 120    12763  19379  12322    641    514    781       S  
ATOM   2041  CE  MET B 120     -11.095 -20.522  -2.301  1.00112.09           C  
ANISOU 2041  CE  MET B 120    12041  18818  11731    626    556    928       C  
ATOM   2042  N   ALA B 121     -12.069 -21.389  -6.137  1.00 65.94           N  
ANISOU 2042  N   ALA B 121     6203  12716   6136    493    592    844       N  
ATOM   2043  CA  ALA B 121     -12.354 -22.818  -6.072  1.00 57.81           C  
ANISOU 2043  CA  ALA B 121     5072  11708   5184    440    619    989       C  
ATOM   2044  C   ALA B 121     -12.273 -23.463  -7.449  1.00 56.99           C  
ANISOU 2044  C   ALA B 121     4938  11527   5187    398    626    953       C  
ATOM   2045  O   ALA B 121     -11.830 -24.611  -7.577  1.00 62.14           O  
ANISOU 2045  O   ALA B 121     5507  12178   5926    362    633   1032       O  
ATOM   2046  CB  ALA B 121     -13.730 -23.051  -5.448  1.00 51.36           C  
ANISOU 2046  CB  ALA B 121     4183  10974   4358    441    637   1096       C  
ATOM   2047  N   ARG B 122     -12.688 -22.743  -8.494  1.00 64.45           N  
ANISOU 2047  N   ARG B 122     5936  12418   6133    410    619    831       N  
ATOM   2048  CA  ARG B 122     -12.621 -23.308  -9.837  1.00 65.27           C  
ANISOU 2048  CA  ARG B 122     6005  12468   6327    386    620    777       C  
ATOM   2049  C   ARG B 122     -11.204 -23.299 -10.397  1.00 70.23           C  
ANISOU 2049  C   ARG B 122     6672  13060   6952    395    605    697       C  
ATOM   2050  O   ARG B 122     -10.858 -24.175 -11.198  1.00 70.78           O  
ANISOU 2050  O   ARG B 122     6712  13056   7126    386    574    669       O  
ATOM   2051  CB  ARG B 122     -13.577 -22.563 -10.769  1.00 61.89           C  
ANISOU 2051  CB  ARG B 122     5613  12010   5890    397    615    685       C  
ATOM   2052  CG  ARG B 122     -14.949 -23.206 -10.831  1.00 63.09           C  
ANISOU 2052  CG  ARG B 122     5665  12193   6112    370    630    766       C  
ATOM   2053  CD  ARG B 122     -16.044 -22.208 -11.148  1.00 71.46           C  
ANISOU 2053  CD  ARG B 122     6771  13259   7123    398    628    703       C  
ATOM   2054  NE  ARG B 122     -17.357 -22.848 -11.168  1.00 81.74           N  
ANISOU 2054  NE  ARG B 122     7964  14600   8493    367    639    793       N  
ATOM   2055  CZ  ARG B 122     -18.494 -22.217 -11.439  1.00 90.92           C  
ANISOU 2055  CZ  ARG B 122     9131  15784   9630    389    640    761       C  
ATOM   2056  NH1 ARG B 122     -18.487 -20.921 -11.715  1.00 92.69           N  
ANISOU 2056  NH1 ARG B 122     9459  15991   9767    446    627    640       N  
ATOM   2057  NH2 ARG B 122     -19.641 -22.884 -11.430  1.00 99.70           N  
ANISOU 2057  NH2 ARG B 122    10129  16938  10815    350    646    859       N  
ATOM   2058  N   ILE B 123     -10.376 -22.331  -9.999  1.00 73.22           N  
ANISOU 2058  N   ILE B 123     7142  13433   7247    414    586    647       N  
ATOM   2059  CA  ILE B 123      -8.957 -22.384 -10.344  1.00 61.72           C  
ANISOU 2059  CA  ILE B 123     5703  11962   5785    416    571    601       C  
ATOM   2060  C   ILE B 123      -8.305 -23.591  -9.681  1.00 59.25           C  
ANISOU 2060  C   ILE B 123     5307  11691   5517    412    584    697       C  
ATOM   2061  O   ILE B 123      -7.558 -24.351 -10.317  1.00 63.44           O  
ANISOU 2061  O   ILE B 123     5820  12155   6129    418    550    663       O  
ATOM   2062  CB  ILE B 123      -8.258 -21.072  -9.942  1.00 49.99           C  
ANISOU 2062  CB  ILE B 123     4306  10472   4215    424    540    552       C  
ATOM   2063  CG1 ILE B 123      -8.737 -19.916 -10.822  1.00 48.24           C  
ANISOU 2063  CG1 ILE B 123     4145  10213   3971    424    521    462       C  
ATOM   2064  CG2 ILE B 123      -6.747 -21.225 -10.012  1.00 41.75           C  
ANISOU 2064  CG2 ILE B 123     3259   9439   3163    418    526    540       C  
ATOM   2065  CD1 ILE B 123      -8.032 -18.605 -10.543  1.00 49.97           C  
ANISOU 2065  CD1 ILE B 123     4427  10437   4123    423    486    420       C  
ATOM   2066  N   ASP B 124      -8.587 -23.789  -8.389  1.00 55.78           N  
ANISOU 2066  N   ASP B 124     4845  11298   5051    408    592    809       N  
ATOM   2067  CA  ASP B 124      -8.080 -24.965  -7.691  1.00 63.01           C  
ANISOU 2067  CA  ASP B 124     5695  12210   6035    396    576    924       C  
ATOM   2068  C   ASP B 124      -8.549 -26.246  -8.369  1.00 59.93           C  
ANISOU 2068  C   ASP B 124     5258  11689   5825    371    522    953       C  
ATOM   2069  O   ASP B 124      -7.792 -27.219  -8.464  1.00 61.25           O  
ANISOU 2069  O   ASP B 124     5407  11768   6099    375    465    968       O  
ATOM   2070  CB  ASP B 124      -8.525 -24.937  -6.229  1.00 72.21           C  
ANISOU 2070  CB  ASP B 124     6823  13495   7120    394    607   1061       C  
ATOM   2071  CG  ASP B 124      -7.913 -26.057  -5.410  1.00 79.93           C  
ANISOU 2071  CG  ASP B 124     7749  14455   8166    376    572   1195       C  
ATOM   2072  OD1 ASP B 124      -8.471 -27.175  -5.409  1.00 79.11           O  
ANISOU 2072  OD1 ASP B 124     7583  14278   8199    337    536   1305       O  
ATOM   2073  OD2 ASP B 124      -6.868 -25.818  -4.770  1.00 85.72           O  
ANISOU 2073  OD2 ASP B 124     8505  15239   8827    399    569   1196       O  
ATOM   2074  N   ALA B 125      -9.793 -26.262  -8.854  1.00 68.73           N  
ANISOU 2074  N   ALA B 125     6350  12782   6982    350    528    953       N  
ATOM   2075  CA  ALA B 125     -10.289 -27.433  -9.570  1.00 73.59           C  
ANISOU 2075  CA  ALA B 125     6924  13256   7779    324    456    966       C  
ATOM   2076  C   ALA B 125      -9.590 -27.610 -10.912  1.00 68.25           C  
ANISOU 2076  C   ALA B 125     6289  12482   7161    364    408    802       C  
ATOM   2077  O   ALA B 125      -9.427 -28.743 -11.379  1.00 57.16           O  
ANISOU 2077  O   ALA B 125     4861  10947   5910    370    322    787       O  
ATOM   2078  CB  ALA B 125     -11.801 -27.329  -9.767  1.00 75.45           C  
ANISOU 2078  CB  ALA B 125     7120  13508   8041    289    470   1007       C  
ATOM   2079  N   LYS B 126      -9.086 -26.539 -11.497  1.00 76.34           N  
ANISOU 2079  N   LYS B 126     7370  13573   8062    395    454    679       N  
ATOM   2080  CA  LYS B 126      -8.337 -26.620 -12.765  1.00 71.17           C  
ANISOU 2080  CA  LYS B 126     6739  12873   7428    439    421    534       C  
ATOM   2081  C   LYS B 126      -7.036 -27.364 -12.540  1.00 74.21           C  
ANISOU 2081  C   LYS B 126     7115  13241   7840    475    387    525       C  
ATOM   2082  O   LYS B 126      -6.807 -28.389 -13.116  1.00 71.49           O  
ANISOU 2082  O   LYS B 126     6753  12815   7594    521    319    446       O  
ATOM   2083  CB  LYS B 126      -8.000 -25.227 -13.268  1.00 63.17           C  
ANISOU 2083  CB  LYS B 126     5776  11952   6272    449    476    443       C  
ATOM   2084  CG  LYS B 126      -8.325 -24.918 -14.714  1.00 68.40           C  
ANISOU 2084  CG  LYS B 126     6448  12585   6957    467    456    331       C  
ATOM   2085  CD  LYS B 126      -8.281 -26.177 -15.554  1.00 54.00           C  
ANISOU 2085  CD  LYS B 126     4602  10701   5215    522    392    234       C  
ATOM   2086  CE  LYS B 126      -8.407 -25.935 -17.035  1.00 52.27           C  
ANISOU 2086  CE  LYS B 126     4385  10455   5018    548    361    122       C  
ATOM   2087  NZ  LYS B 126      -8.467 -27.276 -17.646  1.00 63.07           N  
ANISOU 2087  NZ  LYS B 126     5730  11775   6460    625    286      4       N  
ATOM   2088  N   LEU B 127      -6.196 -26.822 -11.674  1.00 74.22           N  
ANISOU 2088  N   LEU B 127     7125  13323   7753    465    425    594       N  
ATOM   2089  CA  LEU B 127      -4.927 -27.367 -11.294  1.00 62.28           C  
ANISOU 2089  CA  LEU B 127     5599  11812   6253    499    397    592       C  
ATOM   2090  C   LEU B 127      -5.043 -28.745 -10.657  1.00 76.12           C  
ANISOU 2090  C   LEU B 127     7310  13482   8130    493    338    709       C  
ATOM   2091  O   LEU B 127      -4.299 -29.628 -10.930  1.00 83.20           O  
ANISOU 2091  O   LEU B 127     8193  14379   9040    523    310    725       O  
ATOM   2092  CB  LEU B 127      -4.262 -26.364 -10.393  1.00 57.16           C  
ANISOU 2092  CB  LEU B 127     4979  11287   5453    488    452    610       C  
ATOM   2093  CG  LEU B 127      -4.525 -24.960 -10.884  1.00 55.45           C  
ANISOU 2093  CG  LEU B 127     4809  11146   5116    471    500    540       C  
ATOM   2094  CD1 LEU B 127      -4.114 -23.839 -10.004  1.00 53.63           C  
ANISOU 2094  CD1 LEU B 127     4609  11006   4763    451    526    579       C  
ATOM   2095  CD2 LEU B 127      -3.866 -24.746 -12.180  1.00 53.87           C  
ANISOU 2095  CD2 LEU B 127     4602  10959   4909    502    489    426       C  
ATOM   2096  N   GLY B 128      -5.981 -28.918  -9.773  1.00 82.08           N  
ANISOU 2096  N   GLY B 128     8037  14167   8981    450    311    804       N  
ATOM   2097  CA  GLY B 128      -6.244 -30.190  -9.145  1.00 89.77           C  
ANISOU 2097  CA  GLY B 128     8968  15110  10032    414    275    978       C  
ATOM   2098  C   GLY B 128      -5.210 -31.140  -8.656  1.00 97.20           C  
ANISOU 2098  C   GLY B 128     9875  15878  11180    428    151   1003       C  
ATOM   2099  O   GLY B 128      -4.925 -32.102  -9.284  1.00106.66           O  
ANISOU 2099  O   GLY B 128    11069  16954  12504    441     80    922       O  
ATOM   2100  N   PHE B 129      -4.713 -30.924  -7.471  1.00 94.84           N  
ANISOU 2100  N   PHE B 129     9552  15561  10921    431    110   1111       N  
ATOM   2101  CA  PHE B 129      -5.265 -29.963  -6.596  1.00105.73           C  
ANISOU 2101  CA  PHE B 129    10940  17076  12158    441    170   1166       C  
ATOM   2102  C   PHE B 129      -4.087 -29.580  -5.819  1.00106.76           C  
ANISOU 2102  C   PHE B 129    11082  17385  12099    400    281   1239       C  
ATOM   2103  O   PHE B 129      -3.858 -30.056  -4.755  1.00116.96           O  
ANISOU 2103  O   PHE B 129    12340  18700  13400    348    299   1352       O  
ATOM   2104  CB  PHE B 129      -6.268 -30.630  -5.685  1.00122.52           C  
ANISOU 2104  CB  PHE B 129    13095  19225  14231    518    173    996       C  
ATOM   2105  CG  PHE B 129      -7.696 -30.249  -5.971  1.00127.93           C  
ANISOU 2105  CG  PHE B 129    13755  19816  15037    575     76    995       C  
ATOM   2106  CD1 PHE B 129      -8.131 -28.971  -5.756  1.00129.74           C  
ANISOU 2106  CD1 PHE B 129    13961  19862  15474    594    -47   1002       C  
ATOM   2107  CD2 PHE B 129      -8.585 -31.179  -6.470  1.00126.22           C  
ANISOU 2107  CD2 PHE B 129    13536  19688  14736    613     94    986       C  
ATOM   2108  CE1 PHE B 129      -9.415 -28.642  -6.031  1.00132.24           C  
ANISOU 2108  CE1 PHE B 129    14255  20078  15910    661   -152    991       C  
ATOM   2109  CE2 PHE B 129      -9.870 -30.851  -6.749  1.00130.79           C  
ANISOU 2109  CE2 PHE B 129    14086  20184  15425    677      1    982       C  
ATOM   2110  CZ  PHE B 129     -10.281 -29.581  -6.535  1.00133.88           C  
ANISOU 2110  CZ  PHE B 129    14458  20387  16022    707   -123    981       C  
ATOM   2111  N   PRO B 130      -3.364 -28.667  -6.357  1.00103.49           N  
ANISOU 2111  N   PRO B 130    10705  17099  11518    425    344   1181       N  
ATOM   2112  CA  PRO B 130      -2.119 -28.028  -6.051  1.00 94.09           C  
ANISOU 2112  CA  PRO B 130     9539  15965  10247    465    348   1113       C  
ATOM   2113  C   PRO B 130      -1.887 -27.999  -4.596  1.00 95.53           C  
ANISOU 2113  C   PRO B 130     9707  16248  10341    456    359   1242       C  
ATOM   2114  O   PRO B 130      -2.652 -27.437  -3.843  1.00101.48           O  
ANISOU 2114  O   PRO B 130    10440  17070  11049    425    385   1367       O  
ATOM   2115  CB  PRO B 130      -2.321 -26.629  -6.567  1.00 87.75           C  
ANISOU 2115  CB  PRO B 130     8787  15242   9314    469    411    982       C  
ATOM   2116  CG  PRO B 130      -3.745 -26.418  -6.483  1.00100.14           C  
ANISOU 2116  CG  PRO B 130    10363  16864  10820    436    459   1035       C  
ATOM   2117  CD  PRO B 130      -4.351 -27.717  -6.819  1.00106.30           C  
ANISOU 2117  CD  PRO B 130    11091  17555  11743    408    423   1142       C  
ATOM   2118  N   GLN B 131      -0.776 -28.583  -4.212  1.00 91.29           N  
ANISOU 2118  N   GLN B 131     9174  15741   9772    488    337   1214       N  
ATOM   2119  CA  GLN B 131      -0.378 -28.611  -2.854  1.00 83.50           C  
ANISOU 2119  CA  GLN B 131     8172  14846   8707    486    333   1334       C  
ATOM   2120  C   GLN B 131       0.712 -27.622  -2.565  1.00 84.55           C  
ANISOU 2120  C   GLN B 131     8335  15081   8708    506    347   1261       C  
ATOM   2121  O   GLN B 131       0.890 -27.317  -1.439  1.00 88.42           O  
ANISOU 2121  O   GLN B 131     8824  15673   9100    506    348   1342       O  
ATOM   2122  CB  GLN B 131       0.071 -29.991  -2.515  1.00 81.61           C  
ANISOU 2122  CB  GLN B 131     7882  14511   8614    496    251   1449       C  
ATOM   2123  CG  GLN B 131      -0.679 -31.035  -3.294  1.00 90.45           C  
ANISOU 2123  CG  GLN B 131     8964  15512   9889    460    208   1556       C  
ATOM   2124  CD  GLN B 131      -0.670 -32.380  -2.629  1.00 97.12           C  
ANISOU 2124  CD  GLN B 131     9770  16211  10920    476     95   1637       C  
ATOM   2125  OE1 GLN B 131      -0.613 -33.411  -3.286  1.00102.99           O  
ANISOU 2125  OE1 GLN B 131    10483  16990  11657    468     63   1784       O  
ATOM   2126  NE2 GLN B 131      -0.730 -32.383  -1.323  1.00 92.20           N  
ANISOU 2126  NE2 GLN B 131     9147  15422  10463    505     24   1537       N  
ATOM   2127  N   ARG B 132       1.378 -27.032  -3.559  1.00 81.80           N  
ANISOU 2127  N   ARG B 132     8007  14722   8351    519    352   1121       N  
ATOM   2128  CA  ARG B 132       2.491 -26.138  -3.275  1.00 69.99           C  
ANISOU 2128  CA  ARG B 132     6527  13318   6748    521    349   1074       C  
ATOM   2129  C   ARG B 132       2.640 -25.091  -4.373  1.00 51.16           C  
ANISOU 2129  C   ARG B 132     4172  10948   4317    505    374    945       C  
ATOM   2130  O   ARG B 132       2.341 -25.339  -5.544  1.00 45.33           O  
ANISOU 2130  O   ARG B 132     3425  10150   3647    514    385    875       O  
ATOM   2131  CB  ARG B 132       3.802 -26.918  -3.094  1.00 74.75           C  
ANISOU 2131  CB  ARG B 132     7081  13910   7412    556    295   1097       C  
ATOM   2132  CG  ARG B 132       4.487 -27.339  -4.381  1.00 80.87           C  
ANISOU 2132  CG  ARG B 132     7821  14631   8274    594    278    993       C  
ATOM   2133  CD  ARG B 132       5.961 -27.617  -4.133  1.00 81.94           C  
ANISOU 2133  CD  ARG B 132     7907  14813   8415    630    235    995       C  
ATOM   2134  NE  ARG B 132       6.244 -29.045  -4.029  1.00 90.74           N  
ANISOU 2134  NE  ARG B 132     8976  15834   9667    690    172   1037       N  
ATOM   2135  CZ  ARG B 132       7.464 -29.570  -4.083  1.00107.62           C  
ANISOU 2135  CZ  ARG B 132    11058  17987  11845    750    124   1016       C  
ATOM   2136  NH1 ARG B 132       8.519 -28.784  -4.241  1.00109.45           N  
ANISOU 2136  NH1 ARG B 132    11262  18338  11985    747    141    966       N  
ATOM   2137  NH2 ARG B 132       7.630 -30.882  -3.979  1.00116.33           N  
ANISOU 2137  NH2 ARG B 132    12129  18983  13089    812     49   1051       N  
ATOM   2138  N   ASP B 133       3.103 -23.907  -3.956  1.00 59.38           N  
ANISOU 2138  N   ASP B 133     5247  12072   5242    481    371    919       N  
ATOM   2139  CA  ASP B 133       3.394 -22.782  -4.834  1.00 41.40           C  
ANISOU 2139  CA  ASP B 133     2995   9816   2918    449    376    827       C  
ATOM   2140  C   ASP B 133       4.435 -23.172  -5.882  1.00 63.03           C  
ANISOU 2140  C   ASP B 133     5675  12558   5717    459    367    783       C  
ATOM   2141  O   ASP B 133       5.197 -24.121  -5.688  1.00 66.57           O  
ANISOU 2141  O   ASP B 133     6068  13003   6223    499    344    812       O  
ATOM   2142  CB  ASP B 133       3.905 -21.611  -3.985  1.00 60.48           C  
ANISOU 2142  CB  ASP B 133     5451  12303   5225    421    339    826       C  
ATOM   2143  CG  ASP B 133       3.737 -20.265  -4.654  1.00 58.36           C  
ANISOU 2143  CG  ASP B 133     5231  12034   4908    376    329    753       C  
ATOM   2144  OD1 ASP B 133       4.653 -19.858  -5.400  1.00 66.78           O  
ANISOU 2144  OD1 ASP B 133     6268  13118   5986    338    307    731       O  
ATOM   2145  OD2 ASP B 133       2.714 -19.594  -4.402  1.00 65.47           O  
ANISOU 2145  OD2 ASP B 133     6199  12890   5787    378    321    721       O  
ATOM   2146  N   PRO B 134       4.480 -22.461  -7.013  1.00 65.89           N  
ANISOU 2146  N   PRO B 134     6039  12936   6060    432    383    716       N  
ATOM   2147  CA  PRO B 134       5.639 -22.605  -7.909  1.00 68.33           C  
ANISOU 2147  CA  PRO B 134     6273  13304   6383    442    376    683       C  
ATOM   2148  C   PRO B 134       6.949 -22.200  -7.253  1.00 70.87           C  
ANISOU 2148  C   PRO B 134     6560  13707   6662    416    336    725       C  
ATOM   2149  O   PRO B 134       8.015 -22.615  -7.724  1.00 72.50           O  
ANISOU 2149  O   PRO B 134     6682  13979   6886    443    329    717       O  
ATOM   2150  CB  PRO B 134       5.297 -21.694  -9.097  1.00 69.55           C  
ANISOU 2150  CB  PRO B 134     6458  13454   6515    399    385    628       C  
ATOM   2151  CG  PRO B 134       4.137 -20.865  -8.669  1.00 62.60           C  
ANISOU 2151  CG  PRO B 134     5673  12505   5609    361    381    629       C  
ATOM   2152  CD  PRO B 134       3.429 -21.609  -7.589  1.00 72.78           C  
ANISOU 2152  CD  PRO B 134     6975  13769   6908    399    400    671       C  
ATOM   2153  N   HIS B 135       6.904 -21.403  -6.185  1.00 68.78           N  
ANISOU 2153  N   HIS B 135     6350  13447   6336    373    303    761       N  
ATOM   2154  CA  HIS B 135       8.087 -21.066  -5.406  1.00 64.40           C  
ANISOU 2154  CA  HIS B 135     5766  12958   5746    349    248    802       C  
ATOM   2155  C   HIS B 135       8.333 -22.035  -4.257  1.00 68.42           C  
ANISOU 2155  C   HIS B 135     6261  13462   6274    403    230    857       C  
ATOM   2156  O   HIS B 135       9.422 -22.016  -3.673  1.00 79.26           O  
ANISOU 2156  O   HIS B 135     7593  14893   7630    398    184    890       O  
ATOM   2157  CB  HIS B 135       7.964 -19.644  -4.853  1.00 66.49           C  
ANISOU 2157  CB  HIS B 135     6103  13226   5936    282    197    797       C  
ATOM   2158  CG  HIS B 135       7.629 -18.620  -5.891  1.00 69.03           C  
ANISOU 2158  CG  HIS B 135     6448  13533   6246    220    197    762       C  
ATOM   2159  ND1 HIS B 135       6.826 -17.531  -5.629  1.00 70.65           N  
ANISOU 2159  ND1 HIS B 135     6747  13688   6410    188    162    731       N  
ATOM   2160  CD2 HIS B 135       7.997 -18.512  -7.190  1.00 75.71           C  
ANISOU 2160  CD2 HIS B 135     7235  14419   7113    190    222    756       C  
ATOM   2161  CE1 HIS B 135       6.705 -16.802  -6.724  1.00 81.70           C  
ANISOU 2161  CE1 HIS B 135     8147  15077   7819    132    160    718       C  
ATOM   2162  NE2 HIS B 135       7.408 -17.374  -7.685  1.00 80.47           N  
ANISOU 2162  NE2 HIS B 135     7896  14987   7694    128    201    739       N  
ATOM   2163  N   GLY B 136       7.355 -22.868  -3.917  1.00 64.40           N  
ANISOU 2163  N   GLY B 136     5777  12889   5802    448    258    879       N  
ATOM   2164  CA  GLY B 136       7.493 -23.849  -2.855  1.00 72.03           C  
ANISOU 2164  CA  GLY B 136     6726  13848   6795    492    237    958       C  
ATOM   2165  C   GLY B 136       6.561 -23.651  -1.680  1.00 81.66           C  
ANISOU 2165  C   GLY B 136     8003  15078   7945    491    240   1014       C  
ATOM   2166  O   GLY B 136       6.432 -24.568  -0.855  1.00102.40           O  
ANISOU 2166  O   GLY B 136    10610  17701  10597    523    230   1104       O  
ATOM   2167  N   ASP B 137       5.910 -22.497  -1.560  1.00 65.87           N  
ANISOU 2167  N   ASP B 137     6069  13101   5858    462    248    970       N  
ATOM   2168  CA  ASP B 137       4.992 -22.269  -0.454  1.00 61.68           C  
ANISOU 2168  CA  ASP B 137     5583  12613   5239    482    255   1008       C  
ATOM   2169  C   ASP B 137       3.852 -23.281  -0.515  1.00 70.86           C  
ANISOU 2169  C   ASP B 137     6726  13732   6464    503    307   1075       C  
ATOM   2170  O   ASP B 137       3.246 -23.462  -1.579  1.00 74.20           O  
ANISOU 2170  O   ASP B 137     7150  14080   6962    492    341   1033       O  
ATOM   2171  CB  ASP B 137       4.432 -20.847  -0.497  1.00 67.72           C  
ANISOU 2171  CB  ASP B 137     6422  13396   5913    464    245    922       C  
ATOM   2172  CG  ASP B 137       5.475 -19.816  -0.886  1.00 83.78           C  
ANISOU 2172  CG  ASP B 137     8470  15429   7933    416    182    856       C  
ATOM   2173  OD1 ASP B 137       6.571 -19.820  -0.288  1.00 98.23           O  
ANISOU 2173  OD1 ASP B 137    10274  17304   9745    410    127    881       O  
ATOM   2174  OD2 ASP B 137       5.195 -18.999  -1.789  1.00 90.18           O  
ANISOU 2174  OD2 ASP B 137     9312  16195   8755    378    181    791       O  
ATOM   2175  N   PRO B 138       3.533 -23.958   0.585  1.00 75.90           N  
ANISOU 2175  N   PRO B 138     7343  14420   7077    529    307   1187       N  
ATOM   2176  CA  PRO B 138       2.473 -24.970   0.536  1.00 75.72           C  
ANISOU 2176  CA  PRO B 138     7287  14351   7132    531    341   1280       C  
ATOM   2177  C   PRO B 138       1.104 -24.327   0.378  1.00 72.88           C  
ANISOU 2177  C   PRO B 138     6960  14017   6712    527    393   1247       C  
ATOM   2178  O   PRO B 138       0.783 -23.338   1.040  1.00 73.99           O  
ANISOU 2178  O   PRO B 138     7149  14201   6761    546    377   1195       O  
ATOM   2179  CB  PRO B 138       2.605 -25.686   1.884  1.00 72.46           C  
ANISOU 2179  CB  PRO B 138     6834  14017   6681    549    320   1431       C  
ATOM   2180  CG  PRO B 138       3.217 -24.667   2.791  1.00 65.60           C  
ANISOU 2180  CG  PRO B 138     6000  13274   5651    571    295   1389       C  
ATOM   2181  CD  PRO B 138       4.096 -23.794   1.937  1.00 64.36           C  
ANISOU 2181  CD  PRO B 138     5879  13068   5506    552    268   1245       C  
ATOM   2182  N   ILE B 139       0.301 -24.893  -0.518  1.00 74.57           N  
ANISOU 2182  N   ILE B 139     7158  14138   7039    509    420   1249       N  
ATOM   2183  CA  ILE B 139      -1.081 -24.449  -0.686  1.00 76.73           C  
ANISOU 2183  CA  ILE B 139     7450  14425   7280    505    464   1233       C  
ATOM   2184  C   ILE B 139      -1.864 -24.928   0.530  1.00 73.08           C  
ANISOU 2184  C   ILE B 139     6948  14039   6778    516    470   1376       C  
ATOM   2185  O   ILE B 139      -1.919 -26.138   0.798  1.00 71.13           O  
ANISOU 2185  O   ILE B 139     6629  13797   6602    496    473   1528       O  
ATOM   2186  CB  ILE B 139      -1.692 -24.958  -2.004  1.00 78.87           C  
ANISOU 2186  CB  ILE B 139     7708  14576   7683    481    481   1196       C  
ATOM   2187  CG1 ILE B 139      -1.543 -23.912  -3.114  1.00 79.98           C  
ANISOU 2187  CG1 ILE B 139     7906  14679   7805    476    487   1038       C  
ATOM   2188  CG2 ILE B 139      -3.172 -25.283  -1.838  1.00 71.92           C  
ANISOU 2188  CG2 ILE B 139     6796  13714   6818    469    518   1277       C  
ATOM   2189  CD1 ILE B 139      -0.134 -23.420  -3.332  1.00 75.97           C  
ANISOU 2189  CD1 ILE B 139     7415  14182   7270    475    455    970       C  
ATOM   2190  N   PRO B 140      -2.442 -24.021   1.315  1.00 77.76           N  
ANISOU 2190  N   PRO B 140     7582  14673   7292    551    453   1329       N  
ATOM   2191  CA  PRO B 140      -3.266 -24.454   2.447  1.00 87.15           C  
ANISOU 2191  CA  PRO B 140     8715  15958   8439    568    463   1464       C  
ATOM   2192  C   PRO B 140      -4.513 -25.163   1.948  1.00 95.40           C  
ANISOU 2192  C   PRO B 140     9709  16979   9562    530    502   1557       C  
ATOM   2193  O   PRO B 140      -5.235 -24.649   1.087  1.00 93.06           O  
ANISOU 2193  O   PRO B 140     9449  16610   9298    526    515   1455       O  
ATOM   2194  CB  PRO B 140      -3.608 -23.142   3.161  1.00 78.94           C  
ANISOU 2194  CB  PRO B 140     7726  14968   7299    633    441   1339       C  
ATOM   2195  CG  PRO B 140      -2.524 -22.206   2.751  1.00 71.09           C  
ANISOU 2195  CG  PRO B 140     6806  13920   6284    638    404   1188       C  
ATOM   2196  CD  PRO B 140      -2.254 -22.564   1.316  1.00 74.64           C  
ANISOU 2196  CD  PRO B 140     7268  14260   6834    582    421   1161       C  
ATOM   2197  N   GLY B 141      -4.740 -26.366   2.472  1.00 97.39           N  
ANISOU 2197  N   GLY B 141     9866  17291   9848    495    514   1768       N  
ATOM   2198  CA  GLY B 141      -5.945 -27.095   2.126  1.00 94.91           C  
ANISOU 2198  CA  GLY B 141     9480  16966   9614    445    544   1891       C  
ATOM   2199  C   GLY B 141      -7.194 -26.285   2.413  1.00100.13           C  
ANISOU 2199  C   GLY B 141    10159  17670  10216    480    551   1831       C  
ATOM   2200  O   GLY B 141      -7.219 -25.436   3.306  1.00101.36           O  
ANISOU 2200  O   GLY B 141    10342  17909  10261    548    536   1762       O  
ATOM   2201  N   ALA B 142      -8.232 -26.523   1.602  1.00102.45           N  
ANISOU 2201  N   ALA B 142    10427  17911  10589    441    575   1847       N  
ATOM   2202  CA  ALA B 142      -9.488 -25.794   1.761  1.00 97.24           C  
ANISOU 2202  CA  ALA B 142     9774  17296   9877    477    585   1794       C  
ATOM   2203  C   ALA B 142     -10.038 -25.916   3.179  1.00108.76           C  
ANISOU 2203  C   ALA B 142    11155  18924  11246    509    582   1930       C  
ATOM   2204  O   ALA B 142     -10.689 -24.990   3.679  1.00108.96           O  
ANISOU 2204  O   ALA B 142    11194  19032  11175    585    582   1838       O  
ATOM   2205  CB  ALA B 142     -10.510 -26.291   0.741  1.00 80.91           C  
ANISOU 2205  CB  ALA B 142     7663  15159   7919    415    608   1836       C  
ATOM   2206  N   ASP B 143      -9.785 -27.045   3.841  1.00113.59           N  
ANISOU 2206  N   ASP B 143    11674  19599  11886    456    576   2154       N  
ATOM   2207  CA  ASP B 143     -10.169 -27.187   5.240  1.00126.19           C  
ANISOU 2207  CA  ASP B 143    13185  21373  13388    488    569   2292       C  
ATOM   2208  C   ASP B 143      -9.316 -26.311   6.149  1.00126.25           C  
ANISOU 2208  C   ASP B 143    13245  21458  13265    586    552   2161       C  
ATOM   2209  O   ASP B 143      -9.774 -25.908   7.225  1.00125.36           O  
ANISOU 2209  O   ASP B 143    13083  21508  13041    656    553   2174       O  
ATOM   2210  CB  ASP B 143     -10.057 -28.651   5.663  1.00136.95           C  
ANISOU 2210  CB  ASP B 143    14431  22770  14832    393    557   2589       C  
ATOM   2211  CG  ASP B 143      -8.796 -29.316   5.137  1.00142.88           C  
ANISOU 2211  CG  ASP B 143    15210  23405  15672    343    542   2620       C  
ATOM   2212  OD1 ASP B 143      -7.706 -28.723   5.268  1.00144.36           O  
ANISOU 2212  OD1 ASP B 143    15480  23578  15791    404    531   2470       O  
ATOM   2213  OD2 ASP B 143      -8.898 -30.435   4.592  1.00146.15           O  
ANISOU 2213  OD2 ASP B 143    15550  23746  16235    243    538   2798       O  
ATOM   2214  N   GLY B 144      -8.094 -26.002   5.736  1.00126.66           N  
ANISOU 2214  N   GLY B 144    13387  21410  13330    593    535   2034       N  
ATOM   2215  CA  GLY B 144      -7.142 -25.303   6.565  1.00126.04           C  
ANISOU 2215  CA  GLY B 144    13351  21392  13148    666    510   1931       C  
ATOM   2216  C   GLY B 144      -6.016 -26.157   7.122  1.00124.55           C  
ANISOU 2216  C   GLY B 144    13126  21230  12966    634    489   2069       C  
ATOM   2217  O   GLY B 144      -5.347 -25.721   8.068  1.00121.22           O  
ANISOU 2217  O   GLY B 144    12714  20896  12449    694    468   2024       O  
ATOM   2218  N   GLN B 145      -5.790 -27.350   6.570  1.00126.91           N  
ANISOU 2218  N   GLN B 145    13384  21460  13378    546    491   2235       N  
ATOM   2219  CA  GLN B 145      -4.769 -28.244   7.108  1.00132.14           C  
ANISOU 2219  CA  GLN B 145    14004  22152  14052    517    465   2393       C  
ATOM   2220  C   GLN B 145      -3.379 -27.630   6.995  1.00136.50           C  
ANISOU 2220  C   GLN B 145    14644  22660  14560    560    439   2227       C  
ATOM   2221  O   GLN B 145      -2.623 -27.604   7.972  1.00138.82           O  
ANISOU 2221  O   GLN B 145    14926  23038  14780    594    411   2257       O  
ATOM   2222  CB  GLN B 145      -4.821 -29.592   6.386  1.00133.67           C  
ANISOU 2222  CB  GLN B 145    14134  22265  14390    417    467   2599       C  
ATOM   2223  CG  GLN B 145      -3.816 -30.616   6.887  1.00134.63           C  
ANISOU 2223  CG  GLN B 145    14209  22406  14537    384    428   2799       C  
ATOM   2224  CD  GLN B 145      -3.068 -31.291   5.752  1.00135.10           C  
ANISOU 2224  CD  GLN B 145    14316  22183  14833    353    352   2718       C  
ATOM   2225  OE1 GLN B 145      -2.808 -30.678   4.717  1.00137.13           O  
ANISOU 2225  OE1 GLN B 145    14651  22329  15125    379    363   2491       O  
ATOM   2226  NE2 GLN B 145      -2.727 -32.562   5.937  1.00133.34           N  
ANISOU 2226  NE2 GLN B 145    14044  21835  14784    304    260   2895       N  
ATOM   2227  N   VAL B 146      -3.038 -27.122   5.811  1.00136.82           N  
ANISOU 2227  N   VAL B 146    14764  22575  14646    555    444   2055       N  
ATOM   2228  CA  VAL B 146      -1.699 -26.634   5.473  1.00134.45           C  
ANISOU 2228  CA  VAL B 146    14533  22226  14326    576    416   1917       C  
ATOM   2229  C   VAL B 146      -0.714 -27.791   5.594  1.00145.02           C  
ANISOU 2229  C   VAL B 146    15823  23580  15700    545    396   2084       C  
ATOM   2230  O   VAL B 146      -0.403 -28.225   6.713  1.00145.42           O  
ANISOU 2230  O   VAL B 146    15828  23724  15700    557    367   2221       O  
ATOM   2231  CB  VAL B 146      -1.280 -25.443   6.353  1.00117.00           C  
ANISOU 2231  CB  VAL B 146    12375  20081  12000    645    386   1773       C  
ATOM   2232  CG1 VAL B 146       0.060 -24.886   5.891  1.00 95.36           C  
ANISOU 2232  CG1 VAL B 146     9699  17283   9252    648    350   1638       C  
ATOM   2233  CG2 VAL B 146      -2.351 -24.362   6.336  1.00118.03           C  
ANISOU 2233  CG2 VAL B 146    12543  20214  12089    688    402   1635       C  
ATOM   2234  N   PRO B 147      -0.204 -28.327   4.472  1.00155.85           N  
ANISOU 2234  N   PRO B 147    17210  24760  17247    515    363   2028       N  
ATOM   2235  CA  PRO B 147       0.732 -29.460   4.538  1.00169.11           C  
ANISOU 2235  CA  PRO B 147    18856  26326  19072    503    285   2121       C  
ATOM   2236  C   PRO B 147       1.891 -29.220   5.492  1.00180.86           C  
ANISOU 2236  C   PRO B 147    20351  27921  20447    542    250   2134       C  
ATOM   2237  O   PRO B 147       2.231 -28.070   5.783  1.00178.03           O  
ANISOU 2237  O   PRO B 147    20041  27676  19927    577    271   2012       O  
ATOM   2238  CB  PRO B 147       1.214 -29.594   3.089  1.00166.29           C  
ANISOU 2238  CB  PRO B 147    18534  25772  18876    502    258   1959       C  
ATOM   2239  CG  PRO B 147       0.074 -29.075   2.276  1.00158.61           C  
ANISOU 2239  CG  PRO B 147    17585  24776  17905    482    317   1875       C  
ATOM   2240  CD  PRO B 147      -0.533 -27.958   3.084  1.00153.83           C  
ANISOU 2240  CD  PRO B 147    16997  24367  17083    501    383   1866       C  
ATOM   2241  N   THR B 148       2.498 -30.301   5.989  1.00197.71           N  
ANISOU 2241  N   THR B 148    22437  30010  22673    536    182   2283       N  
ATOM   2242  CA  THR B 148       3.483 -30.223   7.059  1.00207.38           C  
ANISOU 2242  CA  THR B 148    23652  31354  23787    571    143   2338       C  
ATOM   2243  C   THR B 148       4.891 -30.360   6.494  1.00206.84           C  
ANISOU 2243  C   THR B 148    23603  31168  23819    596     79   2224       C  
ATOM   2244  O   THR B 148       5.309 -31.476   6.150  1.00216.27           O  
ANISOU 2244  O   THR B 148    24763  32213  25195    594     13   2288       O  
ATOM   2245  CB  THR B 148       3.217 -31.312   8.103  1.00213.93           C  
ANISOU 2245  CB  THR B 148    24406  32240  24638    549    105   2606       C  
ATOM   2246  OG1 THR B 148       3.443 -32.601   7.518  1.00216.50           O  
ANISOU 2246  OG1 THR B 148    24701  32346  25214    520     25   2688       O  
ATOM   2247  CG2 THR B 148       1.781 -31.235   8.599  1.00216.35           C  
ANISOU 2247  CG2 THR B 148    24668  32687  24847    520    175   2739       C  
ATOM   2248  N   PRO B 149       5.655 -29.279   6.371  1.00179.96           N  
ANISOU 2248  N   PRO B 149    20245  27823  20308    621     87   2058       N  
ATOM   2249  CA  PRO B 149       7.035 -29.398   5.931  1.00158.13           C  
ANISOU 2249  CA  PRO B 149    17476  24987  17621    643     29   1973       C  
ATOM   2250  C   PRO B 149       7.994 -28.995   7.036  1.00139.27           C  
ANISOU 2250  C   PRO B 149    15082  22737  15096    670    -14   1999       C  
ATOM   2251  O   PRO B 149       8.224 -27.797   7.261  1.00143.84           O  
ANISOU 2251  O   PRO B 149    15705  23418  15531    675     -4   1886       O  
ATOM   2252  CB  PRO B 149       7.103 -28.414   4.754  1.00159.69           C  
ANISOU 2252  CB  PRO B 149    17719  25140  17816    632     69   1771       C  
ATOM   2253  CG  PRO B 149       5.955 -27.404   5.027  1.00165.98           C  
ANISOU 2253  CG  PRO B 149    18564  26033  18467    617    134   1737       C  
ATOM   2254  CD  PRO B 149       5.203 -27.886   6.254  1.00174.98           C  
ANISOU 2254  CD  PRO B 149    19674  27286  19526    625    144   1915       C  
ATOM   2255  N   PRO B 150       8.569 -29.960   7.758  1.00116.58           N  
ANISOU 2255  N   PRO B 150    12160  19867  12270    688    -77   2145       N  
ATOM   2256  CA  PRO B 150       9.630 -29.619   8.716  1.00 98.65           C  
ANISOU 2256  CA  PRO B 150     9880  17720   9882    718   -131   2157       C  
ATOM   2257  C   PRO B 150      10.832 -29.025   8.000  1.00 85.15           C  
ANISOU 2257  C   PRO B 150     8178  15972   8204    726   -160   1989       C  
ATOM   2258  O   PRO B 150      11.785 -29.739   7.671  1.00 80.27           O  
ANISOU 2258  O   PRO B 150     7512  15276   7709    749   -214   1997       O  
ATOM   2259  CB  PRO B 150       9.964 -30.965   9.374  1.00 96.52           C  
ANISOU 2259  CB  PRO B 150     9550  17418   9706    734   -199   2355       C  
ATOM   2260  CG  PRO B 150       8.770 -31.831   9.112  1.00102.58           C  
ANISOU 2260  CG  PRO B 150    10298  18090  10587    700   -175   2483       C  
ATOM   2261  CD  PRO B 150       8.247 -31.396   7.778  1.00108.80           C  
ANISOU 2261  CD  PRO B 150    11123  18764  11450    681   -118   2314       C  
ATOM   2262  N   ALA B 151      10.791 -27.719   7.745  1.00 77.35           N  
ANISOU 2262  N   ALA B 151     7240  15040   7108    707   -132   1842       N  
ATOM   2263  CA  ALA B 151      11.766 -27.048   6.898  1.00 81.99           C  
ANISOU 2263  CA  ALA B 151     7827  15594   7733    691   -152   1696       C  
ATOM   2264  C   ALA B 151      12.538 -26.014   7.702  1.00 94.12           C  
ANISOU 2264  C   ALA B 151     9383  17253   9126    687   -211   1645       C  
ATOM   2265  O   ALA B 151      11.939 -25.174   8.381  1.00 94.36           O  
ANISOU 2265  O   ALA B 151     9469  17372   9010    689   -208   1615       O  
ATOM   2266  CB  ALA B 151      11.080 -26.380   5.703  1.00 80.56           C  
ANISOU 2266  CB  ALA B 151     7685  15340   7582    655    -89   1573       C  
ATOM   2267  N   ARG B 152      13.863 -26.076   7.617  1.00102.45           N  
ANISOU 2267  N   ARG B 152    10386  18314  10225    688   -273   1626       N  
ATOM   2268  CA  ARG B 152      14.740 -25.087   8.221  1.00104.84           C  
ANISOU 2268  CA  ARG B 152    10698  18712  10423    671   -348   1568       C  
ATOM   2269  C   ARG B 152      15.280 -24.144   7.151  1.00 93.96           C  
ANISOU 2269  C   ARG B 152     9316  17295   9089    611   -355   1442       C  
ATOM   2270  O   ARG B 152      15.230 -24.432   5.953  1.00 84.54           O  
ANISOU 2270  O   ARG B 152     8093  16023   8007    597   -302   1410       O  
ATOM   2271  CB  ARG B 152      15.909 -25.757   8.951  1.00114.86           C  
ANISOU 2271  CB  ARG B 152    11900  20037  11706    705   -425   1652       C  
ATOM   2272  CG  ARG B 152      15.538 -26.967   9.792  1.00124.94           C  
ANISOU 2272  CG  ARG B 152    13156  21329  12988    758   -425   1813       C  
ATOM   2273  CD  ARG B 152      15.996 -28.255   9.125  1.00126.69           C  
ANISOU 2273  CD  ARG B 152    13306  21438  13394    788   -428   1873       C  
ATOM   2274  NE  ARG B 152      15.403 -29.435   9.745  1.00125.84           N  
ANISOU 2274  NE  ARG B 152    13185  21301  13326    822   -432   2039       N  
ATOM   2275  CZ  ARG B 152      15.893 -30.031  10.827  1.00122.32           C  
ANISOU 2275  CZ  ARG B 152    12706  20923  12846    856   -500   2173       C  
ATOM   2276  NH1 ARG B 152      16.988 -29.559  11.407  1.00113.00           N  
ANISOU 2276  NH1 ARG B 152    11503  19843  11587    868   -568   2144       N  
ATOM   2277  NH2 ARG B 152      15.291 -31.101  11.328  1.00122.98           N  
ANISOU 2277  NH2 ARG B 152    12774  20972  12980    872   -509   2347       N  
ATOM   2278  N   GLN B 153      15.802 -23.007   7.604  1.00 92.67           N  
ANISOU 2278  N   GLN B 153     9180  17194   8837    576   -432   1377       N  
ATOM   2279  CA  GLN B 153      16.496 -22.095   6.710  1.00 83.96           C  
ANISOU 2279  CA  GLN B 153     8055  16065   7781    501   -465   1292       C  
ATOM   2280  C   GLN B 153      17.763 -22.754   6.165  1.00 92.18           C  
ANISOU 2280  C   GLN B 153     8978  17121   8926    498   -479   1332       C  
ATOM   2281  O   GLN B 153      18.224 -23.787   6.656  1.00102.77           O  
ANISOU 2281  O   GLN B 153    10265  18487  10295    559   -490   1410       O  
ATOM   2282  CB  GLN B 153      16.849 -20.799   7.440  1.00 78.92           C  
ANISOU 2282  CB  GLN B 153     7479  15440   7067    457   -561   1216       C  
ATOM   2283  CG  GLN B 153      15.699 -19.819   7.592  1.00 74.72           C  
ANISOU 2283  CG  GLN B 153     7064  14857   6468    453   -551   1123       C  
ATOM   2284  CD  GLN B 153      15.971 -18.502   6.893  1.00 69.38           C  
ANISOU 2284  CD  GLN B 153     6414  14128   5819    363   -623   1035       C  
ATOM   2285  OE1 GLN B 153      16.512 -17.570   7.488  1.00 66.74           O  
ANISOU 2285  OE1 GLN B 153     6119  13777   5462    330   -737    975       O  
ATOM   2286  NE2 GLN B 153      15.603 -18.421   5.619  1.00 67.47           N  
ANISOU 2286  NE2 GLN B 153     6148  13859   5628    320   -569   1032       N  
ATOM   2287  N   LEU B 154      18.332 -22.138   5.128  1.00 85.18           N  
ANISOU 2287  N   LEU B 154     8042  16227   8094    431   -482   1283       N  
ATOM   2288  CA  LEU B 154      19.598 -22.633   4.597  1.00 74.84           C  
ANISOU 2288  CA  LEU B 154     6602  14971   6864    434   -496   1313       C  
ATOM   2289  C   LEU B 154      20.770 -22.141   5.437  1.00 79.04           C  
ANISOU 2289  C   LEU B 154     7091  15581   7359    399   -610   1335       C  
ATOM   2290  O   LEU B 154      21.672 -22.917   5.774  1.00 78.23           O  
ANISOU 2290  O   LEU B 154     6914  15515   7295    446   -630   1384       O  
ATOM   2291  CB  LEU B 154      19.763 -22.213   3.136  1.00 68.00           C  
ANISOU 2291  CB  LEU B 154     5678  14102   6056    378   -446   1271       C  
ATOM   2292  CG  LEU B 154      21.006 -22.761   2.433  1.00 72.76           C  
ANISOU 2292  CG  LEU B 154     6125  14794   6728    399   -442   1295       C  
ATOM   2293  CD1 LEU B 154      21.045 -24.279   2.526  1.00 72.61           C  
ANISOU 2293  CD1 LEU B 154     6065  14753   6769    528   -407   1320       C  
ATOM   2294  CD2 LEU B 154      21.043 -22.310   0.982  1.00 69.08           C  
ANISOU 2294  CD2 LEU B 154     5599  14356   6292    348   -383   1261       C  
ATOM   2295  N   TRP B 155      20.771 -20.851   5.784  1.00 79.47           N  
ANISOU 2295  N   TRP B 155     7218  15611   7366    314   -678   1284       N  
ATOM   2296  CA  TRP B 155      21.793 -20.328   6.684  1.00 80.19           C  
ANISOU 2296  CA  TRP B 155     7305  15719   7443    274   -786   1285       C  
ATOM   2297  C   TRP B 155      21.686 -20.950   8.069  1.00 79.45           C  
ANISOU 2297  C   TRP B 155     7262  15639   7284    359   -809   1312       C  
ATOM   2298  O   TRP B 155      22.702 -21.122   8.752  1.00 85.94           O  
ANISOU 2298  O   TRP B 155     8042  16498   8114    364   -876   1343       O  
ATOM   2299  CB  TRP B 155      21.683 -18.805   6.777  1.00 89.46           C  
ANISOU 2299  CB  TRP B 155     8559  16839   8594    174   -880   1213       C  
ATOM   2300  CG  TRP B 155      22.979 -18.121   7.103  1.00106.02           C  
ANISOU 2300  CG  TRP B 155    10607  18949  10727     90  -1003   1221       C  
ATOM   2301  CD1 TRP B 155      24.226 -18.483   6.685  1.00116.81           C  
ANISOU 2301  CD1 TRP B 155    11837  20379  12166     56  -1005   1288       C  
ATOM   2302  CD2 TRP B 155      23.152 -16.957   7.921  1.00116.95           C  
ANISOU 2302  CD2 TRP B 155    12075  20277  12082     35  -1151   1157       C  
ATOM   2303  NE1 TRP B 155      25.166 -17.616   7.190  1.00123.31           N  
ANISOU 2303  NE1 TRP B 155    12651  21192  13011    -31  -1142   1284       N  
ATOM   2304  CE2 TRP B 155      24.532 -16.670   7.952  1.00126.46           C  
ANISOU 2304  CE2 TRP B 155    13187  21511  13353    -46  -1244   1201       C  
ATOM   2305  CE3 TRP B 155      22.276 -16.129   8.630  1.00117.38           C  
ANISOU 2305  CE3 TRP B 155    12275  20261  12062     55  -1222   1058       C  
ATOM   2306  CZ2 TRP B 155      25.055 -15.591   8.664  1.00129.42           C  
ANISOU 2306  CZ2 TRP B 155    13609  21832  13731   -116  -1418   1155       C  
ATOM   2307  CZ3 TRP B 155      22.796 -15.058   9.335  1.00119.39           C  
ANISOU 2307  CZ3 TRP B 155    12583  20465  12314      2  -1397    995       C  
ATOM   2308  CH2 TRP B 155      24.173 -14.799   9.347  1.00124.69           C  
ANISOU 2308  CH2 TRP B 155    13161  21154  13063    -89  -1501   1046       C  
ATOM   2309  N   ALA B 156      20.470 -21.295   8.501  1.00 80.12           N  
ANISOU 2309  N   ALA B 156     7432  15703   7305    425   -753   1312       N  
ATOM   2310  CA  ALA B 156      20.293 -21.924   9.804  1.00 77.14           C  
ANISOU 2310  CA  ALA B 156     7095  15355   6861    502   -762   1360       C  
ATOM   2311  C   ALA B 156      20.775 -23.367   9.818  1.00 80.27           C  
ANISOU 2311  C   ALA B 156     7398  15783   7318    569   -734   1472       C  
ATOM   2312  O   ALA B 156      20.974 -23.929  10.900  1.00 88.34           O  
ANISOU 2312  O   ALA B 156     8428  16838   8301    621   -762   1536       O  
ATOM   2313  CB  ALA B 156      18.826 -21.859  10.231  1.00 72.78           C  
ANISOU 2313  CB  ALA B 156     6644  14784   6225    547   -701   1341       C  
ATOM   2314  N   CYS B 157      20.954 -23.981   8.651  1.00 78.78           N  
ANISOU 2314  N   CYS B 157     7122  15584   7227    577   -686   1493       N  
ATOM   2315  CA  CYS B 157      21.575 -25.293   8.594  1.00 85.71           C  
ANISOU 2315  CA  CYS B 157     7905  16472   8187    651   -685   1576       C  
ATOM   2316  C   CYS B 157      23.045 -25.188   8.986  1.00 94.72           C  
ANISOU 2316  C   CYS B 157     8978  17659   9352    636   -759   1581       C  
ATOM   2317  O   CYS B 157      23.672 -24.134   8.868  1.00106.13           O  
ANISOU 2317  O   CYS B 157    10418  19124  10784    554   -803   1523       O  
ATOM   2318  CB  CYS B 157      21.446 -25.893   7.193  1.00 90.63           C  
ANISOU 2318  CB  CYS B 157     8451  17069   8917    679   -622   1560       C  
ATOM   2319  SG  CYS B 157      19.834 -26.628   6.834  1.00 97.81           S  
ANISOU 2319  SG  CYS B 157     9441  17860   9863    720   -525   1577       S  
ATOM   2320  N   ARG B 158      23.593 -26.298   9.462  1.00 94.76           N  
ANISOU 2320  N   ARG B 158     8930  17672   9403    713   -785   1661       N  
ATOM   2321  CA  ARG B 158      24.985 -26.357   9.876  1.00 97.89           C  
ANISOU 2321  CA  ARG B 158     9255  18112   9825    714   -855   1676       C  
ATOM   2322  C   ARG B 158      25.783 -27.224   8.912  1.00101.50           C  
ANISOU 2322  C   ARG B 158     9590  18570  10406    773   -834   1679       C  
ATOM   2323  O   ARG B 158      25.228 -27.941   8.074  1.00110.06           O  
ANISOU 2323  O   ARG B 158    10651  19608  11559    831   -777   1674       O  
ATOM   2324  CB  ARG B 158      25.098 -26.870  11.316  1.00101.14           C  
ANISOU 2324  CB  ARG B 158     9706  18540  10182    762   -914   1758       C  
ATOM   2325  CG  ARG B 158      24.405 -25.955  12.315  1.00111.29           C  
ANISOU 2325  CG  ARG B 158    11109  19842  11333    721   -934   1729       C  
ATOM   2326  CD  ARG B 158      24.145 -26.632  13.650  1.00122.65           C  
ANISOU 2326  CD  ARG B 158    12591  21307  12705    782   -958   1826       C  
ATOM   2327  NE  ARG B 158      22.812 -26.316  14.158  1.00128.82           N  
ANISOU 2327  NE  ARG B 158    13474  22091  13382    785   -907   1823       N  
ATOM   2328  CZ  ARG B 158      22.478 -25.162  14.727  1.00129.46           C  
ANISOU 2328  CZ  ARG B 158    13640  22194  13353    752   -928   1725       C  
ATOM   2329  NH1 ARG B 158      23.379 -24.198  14.866  1.00136.53           N  
ANISOU 2329  NH1 ARG B 158    14537  23099  14238    703  -1015   1632       N  
ATOM   2330  NH2 ARG B 158      21.238 -24.969  15.156  1.00122.16           N  
ANISOU 2330  NH2 ARG B 158    12796  21281  12340    773   -871   1719       N  
ATOM   2331  N   ASP B 159      27.106 -27.137   9.038  1.00 98.54           N  
ANISOU 2331  N   ASP B 159     9135  18246  10058    763   -886   1678       N  
ATOM   2332  CA  ASP B 159      28.001 -27.774   8.081  1.00 97.38           C  
ANISOU 2332  CA  ASP B 159     8867  18121  10013    821   -862   1657       C  
ATOM   2333  C   ASP B 159      27.766 -29.279   8.031  1.00 97.00           C  
ANISOU 2333  C   ASP B 159     8796  18009  10053    960   -860   1698       C  
ATOM   2334  O   ASP B 159      27.592 -29.935   9.061  1.00100.67           O  
ANISOU 2334  O   ASP B 159     9298  18439  10511   1009   -915   1783       O  
ATOM   2335  CB  ASP B 159      29.456 -27.478   8.448  1.00104.83           C  
ANISOU 2335  CB  ASP B 159     9730  19138  10963    792   -928   1666       C  
ATOM   2336  CG  ASP B 159      29.690 -26.013   8.768  1.00111.86           C  
ANISOU 2336  CG  ASP B 159    10654  20065  11782    649   -973   1642       C  
ATOM   2337  OD1 ASP B 159      29.028 -25.492   9.690  1.00113.07           O  
ANISOU 2337  OD1 ASP B 159    10917  20190  11856    612  -1014   1646       O  
ATOM   2338  OD2 ASP B 159      30.535 -25.383   8.098  1.00116.07           O  
ANISOU 2338  OD2 ASP B 159    11105  20656  12342    577   -973   1621       O  
ATOM   2339  N   GLY B 160      27.750 -29.822   6.813  1.00 95.69           N  
ANISOU 2339  N   GLY B 160     8567  17820   9970   1026   -804   1638       N  
ATOM   2340  CA  GLY B 160      27.550 -31.235   6.594  1.00 93.38           C  
ANISOU 2340  CA  GLY B 160     8249  17444   9789   1167   -821   1653       C  
ATOM   2341  C   GLY B 160      26.116 -31.650   6.338  1.00 87.33           C  
ANISOU 2341  C   GLY B 160     7552  16580   9049   1189   -788   1668       C  
ATOM   2342  O   GLY B 160      25.886 -32.766   5.858  1.00 83.77           O  
ANISOU 2342  O   GLY B 160     7072  16041   8714   1302   -805   1658       O  
ATOM   2343  N   ASP B 161      25.150 -30.785   6.636  1.00 89.52           N  
ANISOU 2343  N   ASP B 161     7918  16867   9228   1088   -752   1686       N  
ATOM   2344  CA  ASP B 161      23.748 -31.149   6.487  1.00 86.73           C  
ANISOU 2344  CA  ASP B 161     7628  16433   8892   1100   -722   1716       C  
ATOM   2345  C   ASP B 161      23.373 -31.287   5.018  1.00 84.62           C  
ANISOU 2345  C   ASP B 161     7331  16123   8699   1133   -651   1607       C  
ATOM   2346  O   ASP B 161      23.793 -30.492   4.172  1.00 90.56           O  
ANISOU 2346  O   ASP B 161     8045  16948   9416   1086   -598   1515       O  
ATOM   2347  CB  ASP B 161      22.852 -30.108   7.157  1.00 80.61           C  
ANISOU 2347  CB  ASP B 161     6958  15692   7979    993   -696   1744       C  
ATOM   2348  CG  ASP B 161      22.905 -30.183   8.668  1.00 79.94           C  
ANISOU 2348  CG  ASP B 161     6926  15632   7814    983   -758   1854       C  
ATOM   2349  OD1 ASP B 161      23.040 -31.304   9.201  1.00 80.96           O  
ANISOU 2349  OD1 ASP B 161     7033  15715   8012   1058   -811   1955       O  
ATOM   2350  OD2 ASP B 161      22.805 -29.124   9.323  1.00 76.88           O  
ANISOU 2350  OD2 ASP B 161     6606  15305   7301    905   -757   1835       O  
ATOM   2351  N   THR B 162      22.574 -32.307   4.720  1.00 81.06           N  
ANISOU 2351  N   THR B 162     6921  15521   8356   1199   -646   1615       N  
ATOM   2352  CA  THR B 162      22.032 -32.534   3.391  1.00 88.29           C  
ANISOU 2352  CA  THR B 162     7837  16365   9345   1236   -584   1503       C  
ATOM   2353  C   THR B 162      20.511 -32.488   3.448  1.00 86.95           C  
ANISOU 2353  C   THR B 162     7790  16071   9174   1173   -535   1534       C  
ATOM   2354  O   THR B 162      19.907 -32.732   4.498  1.00 89.18           O  
ANISOU 2354  O   THR B 162     8141  16303   9441   1141   -563   1657       O  
ATOM   2355  CB  THR B 162      22.495 -33.882   2.823  1.00 93.96           C  
ANISOU 2355  CB  THR B 162     8481  17000  10218   1393   -646   1457       C  
ATOM   2356  OG1 THR B 162      22.097 -33.988   1.450  1.00107.26           O  
ANISOU 2356  OG1 THR B 162    10153  18650  11950   1440   -590   1321       O  
ATOM   2357  CG2 THR B 162      21.893 -35.036   3.615  1.00 84.34           C  
ANISOU 2357  CG2 THR B 162     7326  15606   9115   1434   -729   1574       C  
ATOM   2358  N   GLY B 163      19.890 -32.158   2.317  1.00 85.12           N  
ANISOU 2358  N   GLY B 163     7578  15812   8950   1157   -459   1430       N  
ATOM   2359  CA  GLY B 163      18.442 -32.080   2.288  1.00 82.80           C  
ANISOU 2359  CA  GLY B 163     7391  15411   8658   1099   -410   1452       C  
ATOM   2360  C   GLY B 163      17.820 -31.463   1.051  1.00 74.41           C  
ANISOU 2360  C   GLY B 163     6349  14345   7576   1066   -323   1333       C  
ATOM   2361  O   GLY B 163      18.416 -30.604   0.395  1.00 63.99           O  
ANISOU 2361  O   GLY B 163     4981  13147   6187   1037   -283   1255       O  
ATOM   2362  N   THR B 164      16.596 -31.886   0.747  1.00 75.78           N  
ANISOU 2362  N   THR B 164     6593  14387   7813   1061   -300   1335       N  
ATOM   2363  CA  THR B 164      15.856 -31.392  -0.406  1.00 80.47           C  
ANISOU 2363  CA  THR B 164     7216  14964   8396   1034   -224   1228       C  
ATOM   2364  C   THR B 164      15.301 -29.995  -0.144  1.00 74.22           C  
ANISOU 2364  C   THR B 164     6490  14247   7461    912   -156   1239       C  
ATOM   2365  O   THR B 164      14.620 -29.767   0.859  1.00 77.16           O  
ANISOU 2365  O   THR B 164     6932  14605   7781    858   -157   1330       O  
ATOM   2366  CB  THR B 164      14.721 -32.362  -0.739  1.00 87.55           C  
ANISOU 2366  CB  THR B 164     8161  15685   9421   1068   -240   1234       C  
ATOM   2367  OG1 THR B 164      15.253 -33.527  -1.384  1.00 98.78           O  
ANISOU 2367  OG1 THR B 164     9520  17027  10984   1197   -311   1164       O  
ATOM   2368  CG2 THR B 164      13.681 -31.709  -1.626  1.00 89.11           C  
ANISOU 2368  CG2 THR B 164     8412  15864   9581   1013   -158   1156       C  
ATOM   2369  N   VAL B 165      15.588 -29.060  -1.054  1.00 73.05           N  
ANISOU 2369  N   VAL B 165     6317  14188   7250    876   -106   1147       N  
ATOM   2370  CA  VAL B 165      15.026 -27.717  -0.959  1.00 71.27           C  
ANISOU 2370  CA  VAL B 165     6160  14007   6911    766    -59   1142       C  
ATOM   2371  C   VAL B 165      13.538 -27.765  -1.283  1.00 69.58           C  
ANISOU 2371  C   VAL B 165     6031  13687   6717    747     -9   1127       C  
ATOM   2372  O   VAL B 165      13.104 -28.481  -2.196  1.00 65.24           O  
ANISOU 2372  O   VAL B 165     5470  13060   6257    800      8   1072       O  
ATOM   2373  CB  VAL B 165      15.776 -26.755  -1.898  1.00 59.99           C  
ANISOU 2373  CB  VAL B 165     4669  12695   5428    723    -34   1072       C  
ATOM   2374  CG1 VAL B 165      15.951 -27.383  -3.257  1.00 53.67           C  
ANISOU 2374  CG1 VAL B 165     3795  11902   4693    803     -1    985       C  
ATOM   2375  CG2 VAL B 165      15.035 -25.433  -2.029  1.00 51.26           C  
ANISOU 2375  CG2 VAL B 165     3644  11594   4238    616      1   1055       C  
ATOM   2376  N   ALA B 166      12.740 -27.003  -0.529  1.00 69.53           N  
ANISOU 2376  N   ALA B 166     6109  13684   6626    678      7   1169       N  
ATOM   2377  CA  ALA B 166      11.292 -27.062  -0.693  1.00 63.70           C  
ANISOU 2377  CA  ALA B 166     5441  12862   5900    661     53   1171       C  
ATOM   2378  C   ALA B 166      10.585 -25.715  -0.721  1.00 71.54           C  
ANISOU 2378  C   ALA B 166     6507  13891   6786    588     92   1131       C  
ATOM   2379  O   ALA B 166       9.385 -25.694  -1.006  1.00 85.92           O  
ANISOU 2379  O   ALA B 166     8378  15653   8615    578    135   1120       O  
ATOM   2380  CB  ALA B 166      10.670 -27.916   0.421  1.00 59.15           C  
ANISOU 2380  CB  ALA B 166     4888  12236   5350    681     28   1293       C  
ATOM   2381  N   ARG B 167      11.258 -24.599  -0.443  1.00 67.33           N  
ANISOU 2381  N   ARG B 167     5980  13441   6162    539     66   1108       N  
ATOM   2382  CA  ARG B 167      10.580 -23.308  -0.405  1.00 67.73           C  
ANISOU 2382  CA  ARG B 167     6107  13503   6123    479     76   1063       C  
ATOM   2383  C   ARG B 167      11.599 -22.204  -0.643  1.00 59.75           C  
ANISOU 2383  C   ARG B 167     5075  12555   5070    417     28   1026       C  
ATOM   2384  O   ARG B 167      12.661 -22.191  -0.013  1.00 59.08           O  
ANISOU 2384  O   ARG B 167     4947  12532   4968    414    -31   1059       O  
ATOM   2385  CB  ARG B 167       9.859 -23.113   0.936  1.00 73.67           C  
ANISOU 2385  CB  ARG B 167     6925  14279   6786    491     62   1111       C  
ATOM   2386  CG  ARG B 167       9.294 -21.721   1.169  1.00 68.69           C  
ANISOU 2386  CG  ARG B 167     6376  13670   6054    454     46   1047       C  
ATOM   2387  CD  ARG B 167       8.002 -21.786   1.974  1.00 87.46           C  
ANISOU 2387  CD  ARG B 167     8808  16063   8358    492     79   1074       C  
ATOM   2388  NE  ARG B 167       8.195 -21.441   3.381  1.00 99.88           N  
ANISOU 2388  NE  ARG B 167    10405  17734   9811    522     24   1099       N  
ATOM   2389  CZ  ARG B 167       7.969 -22.274   4.393  1.00 96.63           C  
ANISOU 2389  CZ  ARG B 167     9970  17386   9360    570     33   1202       C  
ATOM   2390  NH1 ARG B 167       7.541 -23.506   4.157  1.00 96.26           N  
ANISOU 2390  NH1 ARG B 167     9876  17292   9405    582     84   1297       N  
ATOM   2391  NH2 ARG B 167       8.169 -21.875   5.642  1.00 87.00           N  
ANISOU 2391  NH2 ARG B 167     8771  16246   8040    602    -16   1205       N  
ATOM   2392  N   ILE B 168      11.273 -21.285  -1.551  1.00 56.71           N  
ANISOU 2392  N   ILE B 168     4716  12155   4676    361     45    969       N  
ATOM   2393  CA  ILE B 168      12.164 -20.200  -1.940  1.00 61.24           C  
ANISOU 2393  CA  ILE B 168     5262  12778   5228    281     -8    954       C  
ATOM   2394  C   ILE B 168      11.408 -18.882  -1.846  1.00 73.89           C  
ANISOU 2394  C   ILE B 168     6963  14335   6777    223    -43    911       C  
ATOM   2395  O   ILE B 168      10.260 -18.780  -2.294  1.00 83.68           O  
ANISOU 2395  O   ILE B 168     8261  15517   8016    236      8    874       O  
ATOM   2396  CB  ILE B 168      12.724 -20.407  -3.364  1.00 66.86           C  
ANISOU 2396  CB  ILE B 168     5878  13532   5992    267     34    945       C  
ATOM   2397  CG1 ILE B 168      13.547 -21.695  -3.432  1.00 63.30           C  
ANISOU 2397  CG1 ILE B 168     5326  13130   5595    348     51    966       C  
ATOM   2398  CG2 ILE B 168      13.561 -19.212  -3.794  1.00 68.18           C  
ANISOU 2398  CG2 ILE B 168     6006  13762   6139    163    -23    962       C  
ATOM   2399  CD1 ILE B 168      14.207 -21.928  -4.773  1.00 54.37           C  
ANISOU 2399  CD1 ILE B 168     4084  12081   4493    361     90    944       C  
ATOM   2400  N   SER B 169      12.055 -17.874  -1.265  1.00 74.53           N  
ANISOU 2400  N   SER B 169     7062  14435   6819    164   -144    910       N  
ATOM   2401  CA  SER B 169      11.437 -16.563  -1.121  1.00 81.71           C  
ANISOU 2401  CA  SER B 169     8071  15286   7690    118   -211    855       C  
ATOM   2402  C   SER B 169      11.291 -15.884  -2.478  1.00 89.97           C  
ANISOU 2402  C   SER B 169     9105  16298   8781     41   -198    849       C  
ATOM   2403  O   SER B 169      12.220 -15.889  -3.292  1.00 91.05           O  
ANISOU 2403  O   SER B 169     9145  16491   8960    -19   -197    900       O  
ATOM   2404  CB  SER B 169      12.267 -15.689  -0.182  1.00 80.59           C  
ANISOU 2404  CB  SER B 169     7948  15159   7514     75   -350    849       C  
ATOM   2405  OG  SER B 169      11.953 -14.317  -0.350  1.00 83.70           O  
ANISOU 2405  OG  SER B 169     8419  15478   7906     10   -446    798       O  
ATOM   2406  N   ASP B 170      10.119 -15.297  -2.717  1.00 99.35           N  
ANISOU 2406  N   ASP B 170    10385  17411   9954     47   -188    794       N  
ATOM   2407  CA  ASP B 170       9.850 -14.539  -3.931  1.00109.61           C  
ANISOU 2407  CA  ASP B 170    11688  18669  11288    -27   -189    793       C  
ATOM   2408  C   ASP B 170       9.861 -13.034  -3.689  1.00110.55           C  
ANISOU 2408  C   ASP B 170    11884  18714  11407   -102   -331    766       C  
ATOM   2409  O   ASP B 170       9.286 -12.280  -4.481  1.00103.62           O  
ANISOU 2409  O   ASP B 170    11046  17772  10552   -148   -348    754       O  
ATOM   2410  CB  ASP B 170       8.512 -14.964  -4.537  1.00109.93           C  
ANISOU 2410  CB  ASP B 170    11771  18669  11330     32    -86    752       C  
ATOM   2411  CG  ASP B 170       7.429 -15.149  -3.491  1.00112.05           C  
ANISOU 2411  CG  ASP B 170    12125  18905  11544    121    -72    698       C  
ATOM   2412  OD1 ASP B 170       7.680 -14.836  -2.309  1.00113.76           O  
ANISOU 2412  OD1 ASP B 170    12379  19134  11709    145   -146    681       O  
ATOM   2413  OD2 ASP B 170       6.326 -15.610  -3.854  1.00113.06           O  
ANISOU 2413  OD2 ASP B 170    12276  19008  11675    171     12    676       O  
ATOM   2414  N   ALA B 171      10.499 -12.585  -2.605  1.00110.26           N  
ANISOU 2414  N   ALA B 171    11870  18674  11348   -111   -447    754       N  
ATOM   2415  CA  ALA B 171      10.558 -11.156  -2.321  1.00104.33           C  
ANISOU 2415  CA  ALA B 171    11197  17830  10612   -177   -614    716       C  
ATOM   2416  C   ALA B 171      11.363 -10.415  -3.380  1.00109.88           C  
ANISOU 2416  C   ALA B 171    11833  18519  11397   -326   -681    807       C  
ATOM   2417  O   ALA B 171      11.036  -9.276  -3.733  1.00118.35           O  
ANISOU 2417  O   ALA B 171    12970  19486  12512   -394   -789    795       O  
ATOM   2418  CB  ALA B 171      11.150 -10.921  -0.932  1.00 99.59           C  
ANISOU 2418  CB  ALA B 171    10629  17240   9970   -148   -734    676       C  
ATOM   2419  N   ASP B 172      12.410 -11.043  -3.899  1.00107.19           N  
ANISOU 2419  N   ASP B 172    11355  18292  11080   -377   -625    907       N  
ATOM   2420  CA  ASP B 172      13.252 -10.436  -4.930  1.00 95.74           C  
ANISOU 2420  CA  ASP B 172     9807  16879   9692   -521   -672   1023       C  
ATOM   2421  C   ASP B 172      13.224 -11.287  -6.189  1.00 86.48           C  
ANISOU 2421  C   ASP B 172     8527  15821   8509   -505   -508   1077       C  
ATOM   2422  O   ASP B 172      13.701 -12.438  -6.165  1.00 76.09           O  
ANISOU 2422  O   ASP B 172     7123  14619   7171   -434   -406   1086       O  
ATOM   2423  CB  ASP B 172      14.687 -10.275  -4.429  1.00 95.83           C  
ANISOU 2423  CB  ASP B 172     9725  16956   9732   -602   -775   1099       C  
ATOM   2424  CG  ASP B 172      15.544  -9.450  -5.369  1.00103.70           C  
ANISOU 2424  CG  ASP B 172    10615  17990  10795   -773   -854   1240       C  
ATOM   2425  OD1 ASP B 172      14.976  -8.737  -6.225  1.00103.18           O  
ANISOU 2425  OD1 ASP B 172    10582  17862  10760   -839   -873   1271       O  
ATOM   2426  OD2 ASP B 172      16.786  -9.514  -5.254  1.00110.58           O  
ANISOU 2426  OD2 ASP B 172    11362  18963  11688   -845   -900   1332       O  
ATOM   2427  N   PRO B 173      12.679 -10.786  -7.301  1.00 91.18           N  
ANISOU 2427  N   PRO B 173     9128  16395   9121   -558   -485   1108       N  
ATOM   2428  CA  PRO B 173      12.744 -11.560  -8.550  1.00 96.61           C  
ANISOU 2428  CA  PRO B 173     9703  17217   9786   -537   -340   1153       C  
ATOM   2429  C   PRO B 173      14.155 -11.695  -9.091  1.00101.02           C  
ANISOU 2429  C   PRO B 173    10084  17952  10348   -614   -337   1277       C  
ATOM   2430  O   PRO B 173      14.463 -12.703  -9.742  1.00102.84           O  
ANISOU 2430  O   PRO B 173    10205  18329  10542   -542   -213   1281       O  
ATOM   2431  CB  PRO B 173      11.843 -10.762  -9.501  1.00 97.49           C  
ANISOU 2431  CB  PRO B 173     9872  17259   9909   -589   -349   1164       C  
ATOM   2432  CG  PRO B 173      11.900  -9.366  -8.976  1.00 97.71           C  
ANISOU 2432  CG  PRO B 173     9985  17147   9993   -697   -535   1188       C  
ATOM   2433  CD  PRO B 173      11.976  -9.504  -7.480  1.00 93.38           C  
ANISOU 2433  CD  PRO B 173     9516  16529   9438   -628   -600   1096       C  
ATOM   2434  N   GLN B 174      15.020 -10.705  -8.849  1.00 99.84           N  
ANISOU 2434  N   GLN B 174     9896  17795  10243   -753   -480   1375       N  
ATOM   2435  CA  GLN B 174      16.422 -10.836  -9.232  1.00 99.58           C  
ANISOU 2435  CA  GLN B 174     9677  17950  10211   -830   -483   1505       C  
ATOM   2436  C   GLN B 174      17.061 -12.035  -8.546  1.00 90.78           C  
ANISOU 2436  C   GLN B 174     8497  16929   9066   -713   -414   1455       C  
ATOM   2437  O   GLN B 174      17.823 -12.786  -9.166  1.00 89.26           O  
ANISOU 2437  O   GLN B 174     8146  16928   8840   -677   -323   1502       O  
ATOM   2438  CB  GLN B 174      17.182  -9.557  -8.880  1.00112.45           C  
ANISOU 2438  CB  GLN B 174    11290  19523  11913  -1008   -676   1619       C  
ATOM   2439  CG  GLN B 174      16.459  -8.273  -9.248  1.00124.79           C  
ANISOU 2439  CG  GLN B 174    12959  20924  13533  -1117   -793   1651       C  
ATOM   2440  CD  GLN B 174      16.792  -7.135  -8.303  1.00132.69           C  
ANISOU 2440  CD  GLN B 174    14039  21754  14622  -1227  -1024   1663       C  
ATOM   2441  OE1 GLN B 174      16.326  -6.009  -8.478  1.00140.29           O  
ANISOU 2441  OE1 GLN B 174    15090  22559  15653  -1321  -1162   1688       O  
ATOM   2442  NE2 GLN B 174      17.600  -7.426  -7.290  1.00127.68           N  
ANISOU 2442  NE2 GLN B 174    13376  21144  13992  -1209  -1079   1640       N  
ATOM   2443  N   MET B 175      16.757 -12.228  -7.260  1.00 85.63           N  
ANISOU 2443  N   MET B 175     7963  16152   8420   -644   -463   1358       N  
ATOM   2444  CA  MET B 175      17.251 -13.396  -6.540  1.00 76.60           C  
ANISOU 2444  CA  MET B 175     6774  15078   7253   -528   -406   1314       C  
ATOM   2445  C   MET B 175      16.735 -14.683  -7.171  1.00 83.92           C  
ANISOU 2445  C   MET B 175     7672  16066   8146   -385   -241   1252       C  
ATOM   2446  O   MET B 175      17.457 -15.686  -7.239  1.00 88.19           O  
ANISOU 2446  O   MET B 175     8100  16730   8676   -306   -179   1256       O  
ATOM   2447  CB  MET B 175      16.834 -13.308  -5.072  1.00 68.37           C  
ANISOU 2447  CB  MET B 175     5874  13898   6207   -477   -487   1228       C  
ATOM   2448  CG  MET B 175      17.387 -14.409  -4.193  1.00 81.64           C  
ANISOU 2448  CG  MET B 175     7512  15640   7866   -373   -454   1205       C  
ATOM   2449  SD  MET B 175      19.186 -14.367  -4.085  1.00106.61           S  
ANISOU 2449  SD  MET B 175    10494  18961  11054   -453   -528   1317       S  
ATOM   2450  CE  MET B 175      19.465 -12.637  -3.714  1.00113.04           C  
ANISOU 2450  CE  MET B 175    11363  19673  11915   -633   -734   1367       C  
ATOM   2451  N   LEU B 176      15.487 -14.669  -7.644  1.00 81.14           N  
ANISOU 2451  N   LEU B 176     7421  15624   7785   -346   -182   1187       N  
ATOM   2452  CA  LEU B 176      14.932 -15.843  -8.308  1.00 72.68           C  
ANISOU 2452  CA  LEU B 176     6328  14592   6697   -219    -47   1123       C  
ATOM   2453  C   LEU B 176      15.663 -16.135  -9.612  1.00 68.42           C  
ANISOU 2453  C   LEU B 176     5622  14241   6131   -221     22   1176       C  
ATOM   2454  O   LEU B 176      15.927 -17.299  -9.934  1.00 65.63           O  
ANISOU 2454  O   LEU B 176     5254  13912   5770    -97     86   1121       O  
ATOM   2455  CB  LEU B 176      13.436 -15.647  -8.559  1.00 73.93           C  
ANISOU 2455  CB  LEU B 176     6622  14616   6853   -192    -12   1051       C  
ATOM   2456  CG  LEU B 176      12.527 -15.923  -7.360  1.00 76.51           C  
ANISOU 2456  CG  LEU B 176     7086  14802   7182   -120    -25    974       C  
ATOM   2457  CD1 LEU B 176      11.198 -15.200  -7.506  1.00 80.23           C  
ANISOU 2457  CD1 LEU B 176     7685  15151   7648   -136    -33    926       C  
ATOM   2458  CD2 LEU B 176      12.309 -17.419  -7.197  1.00 72.24           C  
ANISOU 2458  CD2 LEU B 176     6523  14274   6652     12     64    928       C  
ATOM   2459  N   ARG B 177      16.000 -15.092 -10.376  1.00 72.88           N  
ANISOU 2459  N   ARG B 177     6128  14877   6685   -352    -17   1275       N  
ATOM   2460  CA  ARG B 177      16.776 -15.299 -11.596  1.00 77.23           C  
ANISOU 2460  CA  ARG B 177     6623  15531   7190   -345     25   1324       C  
ATOM   2461  C   ARG B 177      18.173 -15.817 -11.278  1.00 79.26           C  
ANISOU 2461  C   ARG B 177     6794  15883   7437   -318     15   1362       C  
ATOM   2462  O   ARG B 177      18.721 -16.638 -12.025  1.00 71.48           O  
ANISOU 2462  O   ARG B 177     5773  14975   6411   -216     66   1331       O  
ATOM   2463  CB  ARG B 177      16.846 -14.003 -12.403  1.00 76.23           C  
ANISOU 2463  CB  ARG B 177     6458  15452   7053   -507    -22   1454       C  
ATOM   2464  CG  ARG B 177      15.848 -13.944 -13.550  1.00 78.03           C  
ANISOU 2464  CG  ARG B 177     6745  15652   7251   -475     28   1416       C  
ATOM   2465  CD  ARG B 177      14.946 -12.722 -13.466  1.00 84.28           C  
ANISOU 2465  CD  ARG B 177     7567  16377   8078   -608    -26   1468       C  
ATOM   2466  NE  ARG B 177      15.705 -11.477 -13.392  1.00 94.13           N  
ANISOU 2466  NE  ARG B 177     8735  17664   9365   -800   -151   1635       N  
ATOM   2467  CZ  ARG B 177      15.154 -10.275 -13.263  1.00 96.35           C  
ANISOU 2467  CZ  ARG B 177     9126  17776   9705   -918   -272   1678       C  
ATOM   2468  NH1 ARG B 177      13.835 -10.154 -13.198  1.00 92.18           N  
ANISOU 2468  NH1 ARG B 177     8762  17074   9187   -859   -263   1567       N  
ATOM   2469  NH2 ARG B 177      15.919  -9.194 -13.204  1.00 99.08           N  
ANISOU 2469  NH2 ARG B 177     9418  18122  10107  -1094   -413   1832       N  
ATOM   2470  N   TYR B 178      18.768 -15.343 -10.180  1.00 83.96           N  
ANISOU 2470  N   TYR B 178     7354  16474   8073   -401    -66   1419       N  
ATOM   2471  CA  TYR B 178      20.013 -15.926  -9.689  1.00 78.45           C  
ANISOU 2471  CA  TYR B 178     6584  15848   7374   -362    -74   1441       C  
ATOM   2472  C   TYR B 178      19.859 -17.423  -9.455  1.00 82.75           C  
ANISOU 2472  C   TYR B 178     7157  16371   7913   -169     -3   1317       C  
ATOM   2473  O   TYR B 178      20.665 -18.230  -9.934  1.00 51.87           O  
ANISOU 2473  O   TYR B 178     3189  12546   3974    -77     37   1299       O  
ATOM   2474  CB  TYR B 178      20.441 -15.219  -8.400  1.00 81.23           C  
ANISOU 2474  CB  TYR B 178     6930  16150   7782   -466   -198   1492       C  
ATOM   2475  CG  TYR B 178      21.801 -15.624  -7.868  1.00 91.35           C  
ANISOU 2475  CG  TYR B 178     8131  17507   9071   -454   -220   1535       C  
ATOM   2476  CD1 TYR B 178      21.940 -16.719  -7.022  1.00 91.00           C  
ANISOU 2476  CD1 TYR B 178     8098  17446   9031   -317   -199   1453       C  
ATOM   2477  CD2 TYR B 178      22.943 -14.904  -8.196  1.00 92.48           C  
ANISOU 2477  CD2 TYR B 178     8181  17738   9221   -583   -269   1668       C  
ATOM   2478  CE1 TYR B 178      23.175 -17.090  -6.528  1.00 86.28           C  
ANISOU 2478  CE1 TYR B 178     7423  16917   8441   -302   -224   1491       C  
ATOM   2479  CE2 TYR B 178      24.185 -15.269  -7.706  1.00 91.11           C  
ANISOU 2479  CE2 TYR B 178     7927  17638   9053   -570   -290   1706       C  
ATOM   2480  CZ  TYR B 178      24.294 -16.363  -6.872  1.00 95.65           C  
ANISOU 2480  CZ  TYR B 178     8518  18195   9631   -426   -267   1611       C  
ATOM   2481  OH  TYR B 178      25.525 -16.733  -6.379  1.00109.76           O  
ANISOU 2481  OH  TYR B 178    10222  20056  11426   -408   -291   1648       O  
ATOM   2482  N   PHE B 179      18.811 -17.810  -8.723  1.00 80.52           N  
ANISOU 2482  N   PHE B 179     6956  15975   7661   -105      3   1232       N  
ATOM   2483  CA  PHE B 179      18.602 -19.220  -8.412  1.00 77.13           C  
ANISOU 2483  CA  PHE B 179     6553  15502   7251     61     53   1135       C  
ATOM   2484  C   PHE B 179      18.333 -20.040  -9.666  1.00 71.81           C  
ANISOU 2484  C   PHE B 179     5893  14829   6560    173    124   1057       C  
ATOM   2485  O   PHE B 179      18.678 -21.226  -9.719  1.00 70.21           O  
ANISOU 2485  O   PHE B 179     5667  14635   6376    309    149    991       O  
ATOM   2486  CB  PHE B 179      17.452 -19.367  -7.418  1.00 77.58           C  
ANISOU 2486  CB  PHE B 179     6690  15448   7339     90     43   1088       C  
ATOM   2487  CG  PHE B 179      17.741 -18.775  -6.068  1.00 84.08           C  
ANISOU 2487  CG  PHE B 179     7539  16240   8170     22    -58   1132       C  
ATOM   2488  CD1 PHE B 179      19.044 -18.517  -5.673  1.00 81.71           C  
ANISOU 2488  CD1 PHE B 179     7137  16039   7869    -32   -126   1203       C  
ATOM   2489  CD2 PHE B 179      16.710 -18.478  -5.193  1.00 86.36           C  
ANISOU 2489  CD2 PHE B 179     7988  16368   8456     19    -89   1092       C  
ATOM   2490  CE1 PHE B 179      19.313 -17.975  -4.433  1.00 79.57           C  
ANISOU 2490  CE1 PHE B 179     6921  15710   7600    -88   -235   1227       C  
ATOM   2491  CE2 PHE B 179      16.973 -17.936  -3.950  1.00 86.43           C  
ANISOU 2491  CE2 PHE B 179     8057  16331   8454    -25   -190   1110       C  
ATOM   2492  CZ  PHE B 179      18.277 -17.684  -3.570  1.00 84.09           C  
ANISOU 2492  CZ  PHE B 179     7662  16128   8162    -79   -268   1173       C  
ATOM   2493  N   ALA B 180      17.727 -19.431 -10.686  1.00 65.76           N  
ANISOU 2493  N   ALA B 180     5161  14058   5766    124    143   1058       N  
ATOM   2494  CA  ALA B 180      17.478 -20.158 -11.925  1.00 75.52           C  
ANISOU 2494  CA  ALA B 180     6405  15306   6982    233    192    975       C  
ATOM   2495  C   ALA B 180      18.761 -20.326 -12.730  1.00 82.73           C  
ANISOU 2495  C   ALA B 180     7214  16386   7835    260    196   1007       C  
ATOM   2496  O   ALA B 180      18.978 -21.373 -13.351  1.00 89.01           O  
ANISOU 2496  O   ALA B 180     7981  17222   8616    405    227    913       O  
ATOM   2497  CB  ALA B 180      16.412 -19.440 -12.753  1.00 82.65           C  
ANISOU 2497  CB  ALA B 180     7374  16155   7873    174    202    970       C  
ATOM   2498  N   SER B 181      19.624 -19.307 -12.728  1.00 83.42           N  
ANISOU 2498  N   SER B 181     7232  16580   7885    125    161   1140       N  
ATOM   2499  CA  SER B 181      20.839 -19.363 -13.534  1.00 86.99           C  
ANISOU 2499  CA  SER B 181     7573  17213   8265    140    168   1193       C  
ATOM   2500  C   SER B 181      21.898 -20.263 -12.905  1.00 95.49           C  
ANISOU 2500  C   SER B 181     8581  18350   9351    236    170   1166       C  
ATOM   2501  O   SER B 181      22.584 -21.004 -13.619  1.00 99.85           O  
ANISOU 2501  O   SER B 181     9063  19024   9851    354    198   1116       O  
ATOM   2502  CB  SER B 181      21.392 -17.955 -13.752  1.00 87.74           C  
ANISOU 2502  CB  SER B 181     7609  17401   8329    -52    124   1369       C  
ATOM   2503  OG  SER B 181      21.266 -17.171 -12.579  1.00 96.36           O  
ANISOU 2503  OG  SER B 181     8727  18400   9485   -183     70   1438       O  
ATOM   2504  N   ILE B 182      22.053 -20.217 -11.579  1.00 93.53           N  
ANISOU 2504  N   ILE B 182     8345  18027   9165    195    135   1192       N  
ATOM   2505  CA  ILE B 182      23.013 -21.104 -10.929  1.00 82.73           C  
ANISOU 2505  CA  ILE B 182     6913  16705   7817    291    129   1166       C  
ATOM   2506  C   ILE B 182      22.523 -22.542 -10.866  1.00 77.69           C  
ANISOU 2506  C   ILE B 182     6312  15985   7222    483    160   1018       C  
ATOM   2507  O   ILE B 182      23.321 -23.447 -10.597  1.00 79.07           O  
ANISOU 2507  O   ILE B 182     6424  16208   7412    596    157    977       O  
ATOM   2508  CB  ILE B 182      23.369 -20.611  -9.511  1.00 77.10           C  
ANISOU 2508  CB  ILE B 182     6195  15944   7157    191     66   1244       C  
ATOM   2509  CG1 ILE B 182      22.218 -20.877  -8.538  1.00 76.96           C  
ANISOU 2509  CG1 ILE B 182     6280  15762   7202    218     52   1183       C  
ATOM   2510  CG2 ILE B 182      23.744 -19.135  -9.537  1.00 69.54           C  
ANISOU 2510  CG2 ILE B 182     5202  15036   6183    -11     16   1388       C  
ATOM   2511  CD1 ILE B 182      22.565 -20.582  -7.096  1.00 65.06           C  
ANISOU 2511  CD1 ILE B 182     4767  14219   5735    156    -22   1236       C  
ATOM   2512  N   GLY B 183      21.239 -22.777 -11.106  1.00 80.49           N  
ANISOU 2512  N   GLY B 183     6761  16217   7606    520    182    940       N  
ATOM   2513  CA  GLY B 183      20.715 -24.114 -11.253  1.00 85.16           C  
ANISOU 2513  CA  GLY B 183     7377  16731   8247    693    205    804       C  
ATOM   2514  C   GLY B 183      20.073 -24.732 -10.032  1.00 84.31           C  
ANISOU 2514  C   GLY B 183     7321  16477   8234    732    183    784       C  
ATOM   2515  O   GLY B 183      20.066 -25.963  -9.920  1.00 95.16           O  
ANISOU 2515  O   GLY B 183     8676  17808   9671    881    178    700       O  
ATOM   2516  N   ILE B 184      19.529 -23.932  -9.118  1.00 75.30           N  
ANISOU 2516  N   ILE B 184     6237  15268   7107    611    160    860       N  
ATOM   2517  CA  ILE B 184      18.843 -24.447  -7.940  1.00 87.86           C  
ANISOU 2517  CA  ILE B 184     7872  16743   8767    643    136    859       C  
ATOM   2518  C   ILE B 184      17.352 -24.163  -8.078  1.00 94.25           C  
ANISOU 2518  C   ILE B 184     8778  17444   9588    609    164    832       C  
ATOM   2519  O   ILE B 184      16.946 -23.041  -8.411  1.00 94.68           O  
ANISOU 2519  O   ILE B 184     8875  17505   9596    495    172    864       O  
ATOM   2520  CB  ILE B 184      19.425 -23.869  -6.634  1.00 96.06           C  
ANISOU 2520  CB  ILE B 184     8890  17810   9800    555     77    956       C  
ATOM   2521  CG1 ILE B 184      19.056 -22.398  -6.436  1.00 95.14           C  
ANISOU 2521  CG1 ILE B 184     8812  17701   9637    392     55   1021       C  
ATOM   2522  CG2 ILE B 184      20.936 -24.035  -6.608  1.00102.77           C  
ANISOU 2522  CG2 ILE B 184     9641  18773  10634    574     52    988       C  
ATOM   2523  CD1 ILE B 184      19.217 -21.924  -5.008  1.00 96.37           C  
ANISOU 2523  CD1 ILE B 184     8972  17851   9793    329    -24   1085       C  
ATOM   2524  N   SER B 185      16.545 -25.198  -7.871  1.00 94.94           N  
ANISOU 2524  N   SER B 185     8893  17432   9747    710    173    778       N  
ATOM   2525  CA  SER B 185      15.096 -25.088  -7.867  1.00101.22           C  
ANISOU 2525  CA  SER B 185     9774  18122  10564    688    201    759       C  
ATOM   2526  C   SER B 185      14.564 -26.125  -6.888  1.00104.80           C  
ANISOU 2526  C   SER B 185    10263  18453  11102    758    170    773       C  
ATOM   2527  O   SER B 185      15.332 -26.846  -6.247  1.00111.83           O  
ANISOU 2527  O   SER B 185    11104  19352  12034    821    123    799       O  
ATOM   2528  CB  SER B 185      14.516 -25.276  -9.273  1.00105.50           C  
ANISOU 2528  CB  SER B 185    10345  18636  11105    731    244    666       C  
ATOM   2529  OG  SER B 185      14.775 -26.580  -9.764  1.00106.69           O  
ANISOU 2529  OG  SER B 185    10438  18780  11317    883    235    578       O  
ATOM   2530  N   LEU B 186      13.240 -26.201  -6.780  1.00 90.72           N  
ANISOU 2530  N   LEU B 186     8589  16533   9348    739    188    764       N  
ATOM   2531  CA  LEU B 186      12.623 -27.088  -5.804  1.00 78.11           C  
ANISOU 2531  CA  LEU B 186     7056  14797   7828    774    152    809       C  
ATOM   2532  C   LEU B 186      13.002 -28.542  -6.065  1.00 86.50           C  
ANISOU 2532  C   LEU B 186     8058  15805   9003    907    108    768       C  
ATOM   2533  O   LEU B 186      13.204 -28.962  -7.210  1.00106.61           O  
ANISOU 2533  O   LEU B 186    10547  18384  11578    989    117    666       O  
ATOM   2534  CB  LEU B 186      11.102 -26.925  -5.830  1.00 73.93           C  
ANISOU 2534  CB  LEU B 186     6629  14152   7308    732    184    809       C  
ATOM   2535  CG  LEU B 186      10.577 -25.499  -5.638  1.00 66.33           C  
ANISOU 2535  CG  LEU B 186     5736  13224   6243    622    217    828       C  
ATOM   2536  CD1 LEU B 186       9.079 -25.428  -5.893  1.00 63.94           C  
ANISOU 2536  CD1 LEU B 186     5515  12825   5955    603    253    809       C  
ATOM   2537  CD2 LEU B 186      10.907 -24.983  -4.245  1.00 62.84           C  
ANISOU 2537  CD2 LEU B 186     5326  12810   5740    573    178    909       C  
ATOM   2538  N   ASP B 187      13.126 -29.301  -4.973  1.00 83.90           N  
ANISOU 2538  N   ASP B 187     7742  15399   8737    934     48    847       N  
ATOM   2539  CA  ASP B 187      13.363 -30.744  -4.939  1.00 96.49           C  
ANISOU 2539  CA  ASP B 187     9301  16895  10467   1052    -25    834       C  
ATOM   2540  C   ASP B 187      14.798 -31.150  -5.265  1.00 93.30           C  
ANISOU 2540  C   ASP B 187     8780  16597  10072   1155    -61    778       C  
ATOM   2541  O   ASP B 187      15.076 -32.351  -5.383  1.00 93.30           O  
ANISOU 2541  O   ASP B 187     8745  16514  10191   1277   -135    739       O  
ATOM   2542  CB  ASP B 187      12.397 -31.507  -5.855  1.00111.53           C  
ANISOU 2542  CB  ASP B 187    11235  18665  12475   1111    -35    750       C  
ATOM   2543  CG  ASP B 187      10.942 -31.230  -5.529  1.00120.79           C  
ANISOU 2543  CG  ASP B 187    12507  19735  13652   1017     -4    813       C  
ATOM   2544  OD1 ASP B 187      10.425 -30.172  -5.943  1.00124.37           O  
ANISOU 2544  OD1 ASP B 187    12996  20250  14007    941     71    786       O  
ATOM   2545  OD2 ASP B 187      10.315 -32.069  -4.853  1.00122.44           O  
ANISOU 2545  OD2 ASP B 187    12751  19805  13964   1017    -59    899       O  
ATOM   2546  N   SER B 188      15.723 -30.203  -5.403  1.00 92.50           N  
ANISOU 2546  N   SER B 188     8612  16675   9857   1112    -23    777       N  
ATOM   2547  CA  SER B 188      17.120 -30.530  -5.669  1.00 94.23           C  
ANISOU 2547  CA  SER B 188     8701  17030  10072   1205    -51    738       C  
ATOM   2548  C   SER B 188      17.860 -30.684  -4.344  1.00 87.54           C  
ANISOU 2548  C   SER B 188     7841  16188   9233   1190   -114    847       C  
ATOM   2549  O   SER B 188      17.905 -29.746  -3.541  1.00 85.75           O  
ANISOU 2549  O   SER B 188     7652  16007   8923   1071   -102    934       O  
ATOM   2550  CB  SER B 188      17.776 -29.455  -6.535  1.00 93.36           C  
ANISOU 2550  CB  SER B 188     8514  17119   9840   1153     16    703       C  
ATOM   2551  OG  SER B 188      17.497 -28.157  -6.040  1.00 85.34           O  
ANISOU 2551  OG  SER B 188     7552  16138   8736    992     47    788       O  
ATOM   2552  N   ARG B 189      18.433 -31.863  -4.114  1.00 84.03           N  
ANISOU 2552  N   ARG B 189     7345  15693   8890   1319   -191    835       N  
ATOM   2553  CA  ARG B 189      19.105 -32.118  -2.848  1.00 81.96           C  
ANISOU 2553  CA  ARG B 189     7071  15429   8642   1314   -260    945       C  
ATOM   2554  C   ARG B 189      20.333 -31.223  -2.716  1.00 80.57           C  
ANISOU 2554  C   ARG B 189     6796  15461   8356   1268   -243    966       C  
ATOM   2555  O   ARG B 189      21.033 -30.947  -3.695  1.00 74.48           O  
ANISOU 2555  O   ARG B 189     5951  14805   7541   1296   -200    882       O  
ATOM   2556  CB  ARG B 189      19.484 -33.600  -2.725  1.00 83.32           C  
ANISOU 2556  CB  ARG B 189     7204  15493   8961   1471   -361    925       C  
ATOM   2557  CG  ARG B 189      20.684 -34.070  -3.551  1.00 89.19           C  
ANISOU 2557  CG  ARG B 189     7805  16361   9722   1626   -387    806       C  
ATOM   2558  CD  ARG B 189      21.995 -33.971  -2.771  1.00 97.75           C  
ANISOU 2558  CD  ARG B 189     8796  17576  10770   1639   -429    875       C  
ATOM   2559  NE  ARG B 189      23.114 -34.587  -3.477  1.00102.21           N  
ANISOU 2559  NE  ARG B 189     9278  18192  11364   1784   -449    755       N  
ATOM   2560  CZ  ARG B 189      24.378 -34.525  -3.068  1.00 98.13           C  
ANISOU 2560  CZ  ARG B 189     8700  17768  10816   1797   -467    780       C  
ATOM   2561  NH1 ARG B 189      24.686 -33.871  -1.955  1.00102.18           N  
ANISOU 2561  NH1 ARG B 189     9231  18324  11270   1672   -475    916       N  
ATOM   2562  NH2 ARG B 189      25.334 -35.115  -3.771  1.00 88.65           N  
ANISOU 2562  NH2 ARG B 189     7421  16625   9639   1941   -482    662       N  
ATOM   2563  N   LEU B 190      20.581 -30.760  -1.496  1.00 80.80           N  
ANISOU 2563  N   LEU B 190     6857  15508   8336   1183   -275   1078       N  
ATOM   2564  CA  LEU B 190      21.689 -29.871  -1.192  1.00 71.69           C  
ANISOU 2564  CA  LEU B 190     5632  14515   7090   1114   -280   1113       C  
ATOM   2565  C   LEU B 190      22.556 -30.481  -0.100  1.00 82.84           C  
ANISOU 2565  C   LEU B 190     7009  15929   8535   1165   -367   1187       C  
ATOM   2566  O   LEU B 190      22.133 -31.381   0.631  1.00 98.13           O  
ANISOU 2566  O   LEU B 190     8987  17752  10545   1222   -426   1245       O  
ATOM   2567  CB  LEU B 190      21.191 -28.490  -0.746  1.00 65.72           C  
ANISOU 2567  CB  LEU B 190     4951  13792   6229    952   -255   1164       C  
ATOM   2568  CG  LEU B 190      20.305 -27.712  -1.721  1.00 69.92           C  
ANISOU 2568  CG  LEU B 190     5535  14312   6722    881   -175   1105       C  
ATOM   2569  CD1 LEU B 190      20.019 -26.319  -1.183  1.00 71.92           C  
ANISOU 2569  CD1 LEU B 190     5862  14584   6880    731   -178   1149       C  
ATOM   2570  CD2 LEU B 190      20.953 -27.638  -3.093  1.00 72.06           C  
ANISOU 2570  CD2 LEU B 190     5733  14662   6985    910   -120   1022       C  
ATOM   2571  N   ARG B 191      23.781 -29.970   0.005  1.00 80.62           N  
ANISOU 2571  N   ARG B 191     6674  15753   8205   1127   -373   1192       N  
ATOM   2572  CA  ARG B 191      24.734 -30.420   1.015  1.00 77.91           C  
ANISOU 2572  CA  ARG B 191     6292  15427   7883   1166   -453   1258       C  
ATOM   2573  C   ARG B 191      25.505 -29.204   1.507  1.00 72.96           C  
ANISOU 2573  C   ARG B 191     5656  14906   7158   1031   -459   1303       C  
ATOM   2574  O   ARG B 191      26.328 -28.653   0.770  1.00 73.07           O  
ANISOU 2574  O   ARG B 191     5605  15016   7141    993   -422   1265       O  
ATOM   2575  CB  ARG B 191      25.682 -31.479   0.453  1.00 88.19           C  
ANISOU 2575  CB  ARG B 191     7501  16737   9269   1318   -476   1189       C  
ATOM   2576  CG  ARG B 191      26.725 -31.974   1.445  1.00106.48           C  
ANISOU 2576  CG  ARG B 191     9771  19071  11616   1366   -563   1254       C  
ATOM   2577  CD  ARG B 191      26.182 -33.112   2.294  1.00121.64           C  
ANISOU 2577  CD  ARG B 191    11728  20856  13633   1455   -654   1325       C  
ATOM   2578  NE  ARG B 191      25.798 -34.264   1.484  1.00134.07           N  
ANISOU 2578  NE  ARG B 191    13281  22327  15334   1607   -676   1243       N  
ATOM   2579  CZ  ARG B 191      25.475 -35.453   1.982  1.00137.86           C  
ANISOU 2579  CZ  ARG B 191    13771  22672  15939   1712   -778   1297       C  
ATOM   2580  NH1 ARG B 191      25.488 -35.650   3.293  1.00133.25           N  
ANISOU 2580  NH1 ARG B 191    13220  22055  15355   1677   -853   1447       N  
ATOM   2581  NH2 ARG B 191      25.136 -36.445   1.170  1.00140.60           N  
ANISOU 2581  NH2 ARG B 191    14097  22912  16412   1853   -817   1205       N  
ATOM   2582  N   VAL B 192      25.232 -28.783   2.741  1.00 72.96           N  
ANISOU 2582  N   VAL B 192     5721  14892   7108    961   -514   1386       N  
ATOM   2583  CA  VAL B 192      25.945 -27.665   3.348  1.00 77.81           C  
ANISOU 2583  CA  VAL B 192     6334  15585   7645    841   -550   1421       C  
ATOM   2584  C   VAL B 192      27.416 -28.034   3.481  1.00 82.16           C  
ANISOU 2584  C   VAL B 192     6784  16205   8230    885   -590   1432       C  
ATOM   2585  O   VAL B 192      27.784 -28.881   4.303  1.00 90.23           O  
ANISOU 2585  O   VAL B 192     7795  17199   9289    967   -653   1476       O  
ATOM   2586  CB  VAL B 192      25.342 -27.291   4.714  1.00 74.30           C  
ANISOU 2586  CB  VAL B 192     5990  15108   7133    789   -611   1487       C  
ATOM   2587  CG1 VAL B 192      26.033 -26.060   5.279  1.00 57.04           C  
ANISOU 2587  CG1 VAL B 192     3812  12982   4877    668   -665   1497       C  
ATOM   2588  CG2 VAL B 192      23.846 -27.058   4.584  1.00 72.04           C  
ANISOU 2588  CG2 VAL B 192     5799  14762   6813    766   -568   1477       C  
ATOM   2589  N   LEU B 193      28.265 -27.408   2.669  1.00 75.23           N  
ANISOU 2589  N   LEU B 193     5828  15420   7335    829   -556   1402       N  
ATOM   2590  CA  LEU B 193      29.687 -27.723   2.650  1.00 73.71           C  
ANISOU 2590  CA  LEU B 193     5524  15315   7168    872   -583   1410       C  
ATOM   2591  C   LEU B 193      30.517 -26.803   3.533  1.00 78.55           C  
ANISOU 2591  C   LEU B 193     6121  15986   7740    751   -657   1476       C  
ATOM   2592  O   LEU B 193      31.434 -27.275   4.212  1.00 78.80           O  
ANISOU 2592  O   LEU B 193     6100  16046   7795    801   -718   1508       O  
ATOM   2593  CB  LEU B 193      30.222 -27.675   1.216  1.00 71.26           C  
ANISOU 2593  CB  LEU B 193     5124  15097   6856    894   -503   1351       C  
ATOM   2594  CG  LEU B 193      29.921 -28.906   0.359  1.00 74.04           C  
ANISOU 2594  CG  LEU B 193     5455  15410   7267   1068   -457   1259       C  
ATOM   2595  CD1 LEU B 193      30.670 -28.838  -0.960  1.00 68.56           C  
ANISOU 2595  CD1 LEU B 193     4663  14844   6542   1101   -388   1199       C  
ATOM   2596  CD2 LEU B 193      30.272 -30.181   1.111  1.00 80.66           C  
ANISOU 2596  CD2 LEU B 193     6273  16185   8190   1216   -533   1262       C  
ATOM   2597  N   ALA B 194      30.225 -25.500   3.552  1.00 81.04           N  
ANISOU 2597  N   ALA B 194     6480  16308   8002    597   -666   1493       N  
ATOM   2598  CA  ALA B 194      31.021 -24.583   4.370  1.00 79.07           C  
ANISOU 2598  CA  ALA B 194     6217  16096   7729    480   -759   1544       C  
ATOM   2599  C   ALA B 194      30.152 -23.394   4.771  1.00 80.07           C  
ANISOU 2599  C   ALA B 194     6456  16159   7807    352   -802   1541       C  
ATOM   2600  O   ALA B 194      30.040 -22.424   4.017  1.00 87.35           O  
ANISOU 2600  O   ALA B 194     7370  17094   8723    239   -785   1540       O  
ATOM   2601  CB  ALA B 194      32.269 -24.130   3.624  1.00 84.23           C  
ANISOU 2601  CB  ALA B 194     6740  16867   8398    416   -749   1571       C  
ATOM   2602  N   ARG B 195      29.563 -23.465   5.963  1.00 75.41           N  
ANISOU 2602  N   ARG B 195     5971  15502   7179    375   -864   1542       N  
ATOM   2603  CA  ARG B 195      28.809 -22.341   6.508  1.00 88.35           C  
ANISOU 2603  CA  ARG B 195     7727  17081   8761    277   -923   1519       C  
ATOM   2604  C   ARG B 195      29.790 -21.393   7.186  1.00 91.75           C  
ANISOU 2604  C   ARG B 195     8140  17529   9191    171  -1049   1536       C  
ATOM   2605  O   ARG B 195      30.297 -21.685   8.275  1.00104.39           O  
ANISOU 2605  O   ARG B 195     9751  19139  10775    210  -1124   1552       O  
ATOM   2606  CB  ARG B 195      27.740 -22.822   7.484  1.00 94.55           C  
ANISOU 2606  CB  ARG B 195     8635  17804   9487    358   -928   1509       C  
ATOM   2607  CG  ARG B 195      27.127 -21.714   8.333  1.00 93.90           C  
ANISOU 2607  CG  ARG B 195     8681  17670   9327    288  -1009   1468       C  
ATOM   2608  CD  ARG B 195      26.074 -22.271   9.275  1.00 96.32           C  
ANISOU 2608  CD  ARG B 195     9097  17942   9557    380   -991   1469       C  
ATOM   2609  NE  ARG B 195      25.975 -21.528  10.529  1.00101.23           N  
ANISOU 2609  NE  ARG B 195     9820  18548  10094    360  -1090   1432       N  
ATOM   2610  CZ  ARG B 195      25.360 -20.357  10.660  1.00 91.88           C  
ANISOU 2610  CZ  ARG B 195     8736  17314   8861    299  -1139   1352       C  
ATOM   2611  NH1 ARG B 195      24.782 -19.789   9.611  1.00 76.24           N  
ANISOU 2611  NH1 ARG B 195     6766  15293   6909    240  -1094   1317       N  
ATOM   2612  NH2 ARG B 195      25.319 -19.755  11.841  1.00 92.44           N  
ANISOU 2612  NH2 ARG B 195     8898  17373   8853    307  -1238   1301       N  
ATOM   2613  N   ARG B 196      30.067 -20.265   6.540  1.00 86.28           N  
ANISOU 2613  N   ARG B 196     7419  16840   8526     34  -1081   1539       N  
ATOM   2614  CA  ARG B 196      31.033 -19.287   7.031  1.00 85.79           C  
ANISOU 2614  CA  ARG B 196     7327  16780   8488    -86  -1218   1563       C  
ATOM   2615  C   ARG B 196      30.252 -18.172   7.718  1.00100.73           C  
ANISOU 2615  C   ARG B 196     9366  18565  10341   -155  -1331   1501       C  
ATOM   2616  O   ARG B 196      29.665 -17.312   7.057  1.00102.30           O  
ANISOU 2616  O   ARG B 196     9605  18710  10553   -242  -1336   1482       O  
ATOM   2617  CB  ARG B 196      31.893 -18.767   5.884  1.00 86.93           C  
ANISOU 2617  CB  ARG B 196     7339  16992   8697   -198  -1197   1626       C  
ATOM   2618  CG  ARG B 196      32.629 -19.880   5.151  1.00102.75           C  
ANISOU 2618  CG  ARG B 196     9205  19113  10721   -103  -1080   1663       C  
ATOM   2619  CD  ARG B 196      33.750 -19.363   4.267  1.00112.17           C  
ANISOU 2619  CD  ARG B 196    10254  20407  11958   -209  -1075   1741       C  
ATOM   2620  NE  ARG B 196      34.400 -20.458   3.550  1.00111.28           N  
ANISOU 2620  NE  ARG B 196    10022  20415  11846    -90   -960   1753       N  
ATOM   2621  CZ  ARG B 196      35.504 -20.329   2.822  1.00113.71           C  
ANISOU 2621  CZ  ARG B 196    10186  20849  12169   -134   -934   1820       C  
ATOM   2622  NH1 ARG B 196      36.019 -21.384   2.206  1.00115.54           N  
ANISOU 2622  NH1 ARG B 196    10325  21187  12387      4   -835   1804       N  
ATOM   2623  NH2 ARG B 196      36.092 -19.146   2.707  1.00118.54           N  
ANISOU 2623  NH2 ARG B 196    10749  21480  12812   -313  -1016   1903       N  
ATOM   2624  N   GLU B 197      30.244 -18.200   9.055  1.00116.76           N  
ANISOU 2624  N   GLU B 197    11481  20566  12319   -105  -1426   1463       N  
ATOM   2625  CA  GLU B 197      29.457 -17.241   9.826  1.00127.03           C  
ANISOU 2625  CA  GLU B 197    12935  21770  13561   -130  -1535   1377       C  
ATOM   2626  C   GLU B 197      29.842 -15.803   9.502  1.00142.91           C  
ANISOU 2626  C   GLU B 197    14947  23713  15638   -291  -1677   1364       C  
ATOM   2627  O   GLU B 197      28.985 -14.912   9.518  1.00135.36           O  
ANISOU 2627  O   GLU B 197    14107  22663  14662   -326  -1739   1290       O  
ATOM   2628  CB  GLU B 197      29.614 -17.509  11.326  1.00126.28           C  
ANISOU 2628  CB  GLU B 197    12910  21680  13392    -46  -1621   1342       C  
ATOM   2629  CG  GLU B 197      29.454 -18.972  11.744  1.00125.62           C  
ANISOU 2629  CG  GLU B 197    12807  21662  13262     98  -1508   1389       C  
ATOM   2630  CD  GLU B 197      30.703 -19.804  11.501  1.00128.15           C  
ANISOU 2630  CD  GLU B 197    12975  22063  13653    114  -1484   1474       C  
ATOM   2631  OE1 GLU B 197      31.805 -19.221  11.429  1.00125.76           O  
ANISOU 2631  OE1 GLU B 197    12593  21781  13410     22  -1578   1494       O  
ATOM   2632  OE2 GLU B 197      30.581 -21.041  11.378  1.00129.26           O  
ANISOU 2632  OE2 GLU B 197    13075  22243  13795    221  -1381   1521       O  
ATOM   2633  N   PHE B 198      31.117 -15.556   9.209  1.00168.28           N  
ANISOU 2633  N   PHE B 198    18032  26970  18937   -389  -1737   1439       N  
ATOM   2634  CA  PHE B 198      31.576 -14.259   8.733  1.00177.61           C  
ANISOU 2634  CA  PHE B 198    19187  28090  20209   -562  -1869   1465       C  
ATOM   2635  C   PHE B 198      32.425 -14.461   7.486  1.00177.13           C  
ANISOU 2635  C   PHE B 198    18947  28128  20226   -644  -1772   1590       C  
ATOM   2636  O   PHE B 198      33.294 -15.338   7.458  1.00185.59           O  
ANISOU 2636  O   PHE B 198    19901  29313  21303   -589  -1700   1648       O  
ATOM   2637  CB  PHE B 198      32.355 -13.499   9.820  1.00187.48           C  
ANISOU 2637  CB  PHE B 198    20465  29281  21485   -621  -2091   1432       C  
ATOM   2638  CG  PHE B 198      33.129 -14.384  10.764  1.00194.03           C  
ANISOU 2638  CG  PHE B 198    21251  30194  22277   -523  -2094   1443       C  
ATOM   2639  CD1 PHE B 198      34.134 -15.217  10.302  1.00197.92           C  
ANISOU 2639  CD1 PHE B 198    21580  30810  22812   -514  -1997   1546       C  
ATOM   2640  CD2 PHE B 198      32.849 -14.372  12.121  1.00195.30           C  
ANISOU 2640  CD2 PHE B 198    21536  30316  22353   -432  -2197   1346       C  
ATOM   2641  CE1 PHE B 198      34.842 -16.024  11.173  1.00199.50           C  
ANISOU 2641  CE1 PHE B 198    21741  31078  22982   -423  -2010   1556       C  
ATOM   2642  CE2 PHE B 198      33.554 -15.177  12.998  1.00195.87           C  
ANISOU 2642  CE2 PHE B 198    21568  30465  22389   -346  -2204   1366       C  
ATOM   2643  CZ  PHE B 198      34.551 -16.004  12.523  1.00197.44           C  
ANISOU 2643  CZ  PHE B 198    21604  30772  22643   -345  -2115   1473       C  
ATOM   2644  N   ALA B 199      32.160 -13.667   6.451  1.00169.59           N  
ANISOU 2644  N   ALA B 199    17974  27139  19324   -765  -1766   1633       N  
ATOM   2645  CA  ALA B 199      31.114 -12.651   6.497  1.00158.17           C  
ANISOU 2645  CA  ALA B 199    16672  25548  17876   -818  -1862   1558       C  
ATOM   2646  C   ALA B 199      29.967 -12.978   5.546  1.00149.20           C  
ANISOU 2646  C   ALA B 199    15571  24422  16699   -768  -1697   1544       C  
ATOM   2647  O   ALA B 199      30.002 -12.615   4.369  1.00149.83           O  
ANISOU 2647  O   ALA B 199    15577  24524  16828   -865  -1642   1623       O  
ATOM   2648  CB  ALA B 199      31.694 -11.283   6.173  1.00157.56           C  
ANISOU 2648  CB  ALA B 199    16566  25387  17915  -1017  -2039   1621       C  
ATOM   2649  N   GLY B 200      28.955 -13.667   6.068  1.00139.74           N  
ANISOU 2649  N   GLY B 200    14480  23210  15405   -618  -1619   1450       N  
ATOM   2650  CA  GLY B 200      27.749 -13.953   5.316  1.00122.47           C  
ANISOU 2650  CA  GLY B 200    12344  21014  13176   -562  -1482   1419       C  
ATOM   2651  C   GLY B 200      27.959 -14.767   4.057  1.00109.50           C  
ANISOU 2651  C   GLY B 200    10567  19487  11551   -543  -1301   1498       C  
ATOM   2652  O   GLY B 200      27.648 -14.307   2.955  1.00101.43           O  
ANISOU 2652  O   GLY B 200     9517  18464  10557   -620  -1254   1536       O  
ATOM   2653  N   MET B 201      28.485 -15.981   4.204  1.00103.86           N  
ANISOU 2653  N   MET B 201     9773  18872  10816   -431  -1205   1518       N  
ATOM   2654  CA  MET B 201      28.706 -16.866   3.073  1.00 98.43           C  
ANISOU 2654  CA  MET B 201     8969  18294  10137   -376  -1042   1564       C  
ATOM   2655  C   MET B 201      28.445 -18.302   3.503  1.00 89.62           C  
ANISOU 2655  C   MET B 201     7861  17209   8980   -196   -950   1524       C  
ATOM   2656  O   MET B 201      28.545 -18.647   4.683  1.00 94.18           O  
ANISOU 2656  O   MET B 201     8489  17762   9532   -134  -1013   1502       O  
ATOM   2657  CB  MET B 201      30.130 -16.733   2.512  1.00112.01           C  
ANISOU 2657  CB  MET B 201    10529  20122  11909   -456  -1046   1663       C  
ATOM   2658  CG  MET B 201      30.271 -17.180   1.064  1.00123.67           C  
ANISOU 2658  CG  MET B 201    11900  21709  13379   -434   -894   1705       C  
ATOM   2659  SD  MET B 201      31.981 -17.209   0.493  1.00128.52           S  
ANISOU 2659  SD  MET B 201    12325  22485  14022   -490   -882   1820       S  
ATOM   2660  CE  MET B 201      32.430 -18.904   0.858  1.00121.94           C  
ANISOU 2660  CE  MET B 201    11443  21728  13159   -270   -796   1760       C  
ATOM   2661  N   ILE B 202      28.108 -19.138   2.523  1.00 83.72           N  
ANISOU 2661  N   ILE B 202     7068  16513   8231   -111   -810   1517       N  
ATOM   2662  CA  ILE B 202      27.889 -20.561   2.748  1.00 81.57           C  
ANISOU 2662  CA  ILE B 202     6792  16254   7948     58   -734   1487       C  
ATOM   2663  C   ILE B 202      28.022 -21.297   1.420  1.00 77.30           C  
ANISOU 2663  C   ILE B 202     6161  15783   7425    129   -607   1479       C  
ATOM   2664  O   ILE B 202      27.380 -20.940   0.425  1.00 77.81           O  
ANISOU 2664  O   ILE B 202     6239  15844   7479     95   -542   1462       O  
ATOM   2665  CB  ILE B 202      26.523 -20.822   3.412  1.00 80.23           C  
ANISOU 2665  CB  ILE B 202     6759  15990   7733    126   -730   1436       C  
ATOM   2666  CG1 ILE B 202      26.274 -22.325   3.568  1.00 85.48           C  
ANISOU 2666  CG1 ILE B 202     7412  16656   8409    288   -664   1429       C  
ATOM   2667  CG2 ILE B 202      25.401 -20.150   2.637  1.00 77.61           C  
ANISOU 2667  CG2 ILE B 202     6494  15610   7385     71   -688   1400       C  
ATOM   2668  CD1 ILE B 202      25.035 -22.651   4.369  1.00 88.23           C  
ANISOU 2668  CD1 ILE B 202     7883  16929   8712    349   -668   1412       C  
ATOM   2669  N   SER B 203      28.879 -22.312   1.390  1.00 77.33           N  
ANISOU 2669  N   SER B 203     6079  15852   7452    236   -580   1484       N  
ATOM   2670  CA  SER B 203      29.120 -23.111   0.197  1.00 77.80           C  
ANISOU 2670  CA  SER B 203     6060  15978   7521    335   -476   1451       C  
ATOM   2671  C   SER B 203      28.295 -24.387   0.274  1.00 69.75           C  
ANISOU 2671  C   SER B 203     5092  14882   6527    499   -434   1385       C  
ATOM   2672  O   SER B 203      28.388 -25.134   1.257  1.00 69.86           O  
ANISOU 2672  O   SER B 203     5123  14853   6567    580   -486   1394       O  
ATOM   2673  CB  SER B 203      30.605 -23.444   0.052  1.00 86.50           C  
ANISOU 2673  CB  SER B 203     7030  17198   8636    365   -484   1485       C  
ATOM   2674  OG  SER B 203      31.378 -22.266  -0.102  1.00 89.69           O  
ANISOU 2674  OG  SER B 203     7374  17675   9028    202   -526   1564       O  
ATOM   2675  N   VAL B 204      27.488 -24.626  -0.761  1.00 73.33           N  
ANISOU 2675  N   VAL B 204     5570  15314   6978    543   -351   1328       N  
ATOM   2676  CA  VAL B 204      26.568 -25.754  -0.816  1.00 79.72           C  
ANISOU 2676  CA  VAL B 204     6430  16031   7828    682   -320   1266       C  
ATOM   2677  C   VAL B 204      26.831 -26.547  -2.090  1.00 81.16           C  
ANISOU 2677  C   VAL B 204     6550  16257   8031    802   -249   1186       C  
ATOM   2678  O   VAL B 204      27.237 -25.993  -3.116  1.00 77.76           O  
ANISOU 2678  O   VAL B 204     6071  15922   7552    755   -198   1177       O  
ATOM   2679  CB  VAL B 204      25.093 -25.291  -0.761  1.00 77.96           C  
ANISOU 2679  CB  VAL B 204     6318  15717   7586    629   -302   1254       C  
ATOM   2680  CG1 VAL B 204      24.168 -26.466  -0.489  1.00 77.32           C  
ANISOU 2680  CG1 VAL B 204     6286  15532   7560    756   -297   1224       C  
ATOM   2681  CG2 VAL B 204      24.907 -24.205   0.290  1.00 79.95           C  
ANISOU 2681  CG2 VAL B 204     6633  15952   7792    499   -376   1312       C  
ATOM   2682  N   ALA B 205      26.594 -27.854  -2.019  1.00 80.57           N  
ANISOU 2682  N   ALA B 205     6475  16110   8027    962   -259   1130       N  
ATOM   2683  CA  ALA B 205      26.762 -28.756  -3.151  1.00 78.47           C  
ANISOU 2683  CA  ALA B 205     6159  15866   7792   1109   -215   1025       C  
ATOM   2684  C   ALA B 205      25.396 -29.151  -3.696  1.00 90.01           C  
ANISOU 2684  C   ALA B 205     7696  17214   9288   1158   -181    957       C  
ATOM   2685  O   ALA B 205      24.523 -29.587  -2.938  1.00102.57           O  
ANISOU 2685  O   ALA B 205     9351  18683  10938   1176   -221    984       O  
ATOM   2686  CB  ALA B 205      27.550 -30.004  -2.747  1.00 80.03           C  
ANISOU 2686  CB  ALA B 205     6290  16050   8068   1271   -276    996       C  
ATOM   2687  N   ILE B 206      25.219 -29.005  -5.008  1.00 91.40           N  
ANISOU 2687  N   ILE B 206     7863  17441   9423   1178   -112    877       N  
ATOM   2688  CA  ILE B 206      23.955 -29.319  -5.666  1.00 86.00           C  
ANISOU 2688  CA  ILE B 206     7247  16661   8770   1221    -78    801       C  
ATOM   2689  C   ILE B 206      24.029 -30.741  -6.208  1.00 93.57           C  
ANISOU 2689  C   ILE B 206     8165  17572   9816   1429   -106    678       C  
ATOM   2690  O   ILE B 206      25.073 -31.397  -6.116  1.00111.06           O  
ANISOU 2690  O   ILE B 206    10301  19839  12057   1536   -145    649       O  
ATOM   2691  CB  ILE B 206      23.647 -28.311  -6.791  1.00 83.35           C  
ANISOU 2691  CB  ILE B 206     6933  16399   8336   1124     -1    785       C  
ATOM   2692  CG1 ILE B 206      24.236 -26.936  -6.466  1.00 83.71           C  
ANISOU 2692  CG1 ILE B 206     6967  16541   8300    942      0    902       C  
ATOM   2693  CG2 ILE B 206      22.145 -28.176  -7.005  1.00 81.25           C  
ANISOU 2693  CG2 ILE B 206     6765  16014   8091   1092     25    759       C  
ATOM   2694  CD1 ILE B 206      23.576 -26.238  -5.295  1.00 82.92           C  
ANISOU 2694  CD1 ILE B 206     6940  16356   8211    818    -39    988       C  
ATOM   2695  N   ASP B 207      22.923 -31.232  -6.769  1.00 94.04           N  
ANISOU 2695  N   ASP B 207     8275  17528   9927   1492    -97    598       N  
ATOM   2696  CA  ASP B 207      22.891 -32.520  -7.450  1.00108.79           C  
ANISOU 2696  CA  ASP B 207    10108  19341  11885   1694   -139    456       C  
ATOM   2697  C   ASP B 207      22.740 -32.374  -8.959  1.00119.96           C  
ANISOU 2697  C   ASP B 207    11518  20839  13224   1742    -72    329       C  
ATOM   2698  O   ASP B 207      22.523 -33.374  -9.652  1.00120.91           O  
ANISOU 2698  O   ASP B 207    11622  20907  13411   1913   -110    185       O  
ATOM   2699  CB  ASP B 207      21.763 -33.394  -6.892  1.00108.11           C  
ANISOU 2699  CB  ASP B 207    10073  19060  11943   1753   -215    463       C  
ATOM   2700  CG  ASP B 207      20.413 -32.698  -6.915  1.00110.32           C  
ANISOU 2700  CG  ASP B 207    10440  19279  12198   1623   -163    510       C  
ATOM   2701  OD1 ASP B 207      20.335 -31.547  -7.394  1.00109.21           O  
ANISOU 2701  OD1 ASP B 207    10329  19232  11936   1495    -75    526       O  
ATOM   2702  OD2 ASP B 207      19.424 -33.308  -6.457  1.00109.72           O  
ANISOU 2702  OD2 ASP B 207    10404  19056  12229   1647   -220    540       O  
ATOM   2703  N   SER B 208      22.846 -31.157  -9.482  1.00119.99           N  
ANISOU 2703  N   SER B 208    11535  20965  13091   1598     10    379       N  
ATOM   2704  CA  SER B 208      22.693 -30.912 -10.911  1.00112.63           C  
ANISOU 2704  CA  SER B 208    10601  20128  12064   1626     69    285       C  
ATOM   2705  C   SER B 208      23.898 -31.427 -11.693  1.00117.43           C  
ANISOU 2705  C   SER B 208    11108  20899  12611   1770     69    192       C  
ATOM   2706  O   SER B 208      25.042 -31.257 -11.274  1.00123.90           O  
ANISOU 2706  O   SER B 208    11855  21826  13394   1752     62    258       O  
ATOM   2707  CB  SER B 208      22.491 -29.419 -11.177  1.00104.20           C  
ANISOU 2707  CB  SER B 208     9575  19137  10878   1422    133    397       C  
ATOM   2708  OG  SER B 208      23.656 -28.680 -10.855  1.00105.71           O  
ANISOU 2708  OG  SER B 208     9703  19467  10996   1326    138    507       O  
ATOM   2709  N   ALA B 212      27.353 -29.709  -8.561  1.00115.42           N  
ANISOU 2709  N   ALA B 212    10675  20884  12295   1445     10    632       N  
ATOM   2710  CA  ALA B 212      27.957 -28.387  -8.601  1.00109.60           C  
ANISOU 2710  CA  ALA B 212     9907  20281  11457   1261     39    763       C  
ATOM   2711  C   ALA B 212      28.311 -27.920  -7.191  1.00109.69           C  
ANISOU 2711  C   ALA B 212     9922  20243  11512   1144    -17    886       C  
ATOM   2712  O   ALA B 212      28.153 -28.644  -6.204  1.00113.79           O  
ANISOU 2712  O   ALA B 212    10466  20646  12124   1211    -74    877       O  
ATOM   2713  CB  ALA B 212      27.020 -27.395  -9.285  1.00104.91           C  
ANISOU 2713  CB  ALA B 212     9387  19674  10801   1130     86    795       C  
ATOM   2714  N   THR B 213      28.797 -26.684  -7.098  1.00101.98           N  
ANISOU 2714  N   THR B 213     8920  19359  10470    967    -14   1008       N  
ATOM   2715  CA  THR B 213      29.184 -26.092  -5.822  1.00 84.73           C  
ANISOU 2715  CA  THR B 213     6735  17141   8315    845    -78   1118       C  
ATOM   2716  C   THR B 213      28.996 -24.587  -5.915  1.00 73.67           C  
ANISOU 2716  C   THR B 213     5359  15767   6864    632    -79   1227       C  
ATOM   2717  O   THR B 213      29.614 -23.938  -6.765  1.00 83.02           O  
ANISOU 2717  O   THR B 213     6473  17090   7980    561    -51   1283       O  
ATOM   2718  CB  THR B 213      30.631 -26.431  -5.472  1.00 78.92           C  
ANISOU 2718  CB  THR B 213     5881  16522   7581    892   -111   1150       C  
ATOM   2719  OG1 THR B 213      30.801 -27.854  -5.463  1.00 81.79           O  
ANISOU 2719  OG1 THR B 213     6218  16854   8002   1102   -121   1040       O  
ATOM   2720  CG2 THR B 213      30.984 -25.878  -4.106  1.00 71.37           C  
ANISOU 2720  CG2 THR B 213     4934  15522   6662    774   -191   1251       C  
ATOM   2721  N   VAL B 214      28.151 -24.036  -5.048  1.00 68.46           N  
ANISOU 2721  N   VAL B 214     4793  14980   6238    536   -121   1260       N  
ATOM   2722  CA  VAL B 214      27.787 -22.626  -5.085  1.00 73.14           C  
ANISOU 2722  CA  VAL B 214     5422  15563   6804    345   -141   1344       C  
ATOM   2723  C   VAL B 214      28.239 -21.957  -3.796  1.00 78.25           C  
ANISOU 2723  C   VAL B 214     6069  16178   7483    231   -240   1423       C  
ATOM   2724  O   VAL B 214      28.060 -22.504  -2.701  1.00 84.14           O  
ANISOU 2724  O   VAL B 214     6858  16846   8267    292   -288   1399       O  
ATOM   2725  CB  VAL B 214      26.270 -22.435  -5.287  1.00 64.65           C  
ANISOU 2725  CB  VAL B 214     4465  14366   5733    333   -113   1293       C  
ATOM   2726  CG1 VAL B 214      25.949 -20.969  -5.530  1.00 64.91           C  
ANISOU 2726  CG1 VAL B 214     4523  14399   5742    146   -138   1373       C  
ATOM   2727  CG2 VAL B 214      25.774 -23.297  -6.440  1.00 56.15           C  
ANISOU 2727  CG2 VAL B 214     3399  13295   4639    471    -32   1192       C  
ATOM   2728  N   ASP B 215      28.829 -20.769  -3.936  1.00 82.21           N  
ANISOU 2728  N   ASP B 215     6523  16740   7972     64   -283   1524       N  
ATOM   2729  CA  ASP B 215      29.139 -19.887  -2.814  1.00 90.50           C  
ANISOU 2729  CA  ASP B 215     7589  17739   9060    -70   -402   1591       C  
ATOM   2730  C   ASP B 215      28.010 -18.867  -2.720  1.00 85.44           C  
ANISOU 2730  C   ASP B 215     7054  16985   8425   -185   -444   1591       C  
ATOM   2731  O   ASP B 215      27.976 -17.891  -3.474  1.00 84.92           O  
ANISOU 2731  O   ASP B 215     6971  16941   8356   -315   -450   1656       O  
ATOM   2732  CB  ASP B 215      30.491 -19.207  -3.006  1.00 96.70           C  
ANISOU 2732  CB  ASP B 215     8253  18638   9849   -189   -447   1704       C  
ATOM   2733  CG  ASP B 215      31.644 -20.189  -3.000  1.00 99.13           C  
ANISOU 2733  CG  ASP B 215     8453  19065  10148    -69   -415   1698       C  
ATOM   2734  OD1 ASP B 215      31.397 -21.398  -2.813  1.00100.11           O  
ANISOU 2734  OD1 ASP B 215     8600  19164  10273    106   -372   1604       O  
ATOM   2735  OD2 ASP B 215      32.799 -19.750  -3.185  1.00105.21           O  
ANISOU 2735  OD2 ASP B 215     9109  19950  10915   -150   -443   1793       O  
ATOM   2736  N   LEU B 216      27.082 -19.097  -1.798  1.00 85.94           N  
ANISOU 2736  N   LEU B 216     7227  16932   8494   -133   -479   1524       N  
ATOM   2737  CA  LEU B 216      25.909 -18.251  -1.641  1.00 79.86           C  
ANISOU 2737  CA  LEU B 216     6570  16054   7719   -207   -522   1499       C  
ATOM   2738  C   LEU B 216      26.109 -17.273  -0.493  1.00 73.48           C  
ANISOU 2738  C   LEU B 216     5821  15167   6930   -315   -679   1520       C  
ATOM   2739  O   LEU B 216      26.580 -17.649   0.584  1.00 82.78           O  
ANISOU 2739  O   LEU B 216     7009  16336   8109   -268   -739   1509       O  
ATOM   2740  CB  LEU B 216      24.659 -19.097  -1.387  1.00 80.61           C  
ANISOU 2740  CB  LEU B 216     6759  16077   7793    -73   -464   1410       C  
ATOM   2741  CG  LEU B 216      24.026 -19.772  -2.604  1.00 79.11           C  
ANISOU 2741  CG  LEU B 216     6556  15909   7593     13   -335   1365       C  
ATOM   2742  CD1 LEU B 216      23.195 -20.974  -2.182  1.00 79.17           C  
ANISOU 2742  CD1 LEU B 216     6620  15853   7607    166   -292   1295       C  
ATOM   2743  CD2 LEU B 216      23.180 -18.778  -3.381  1.00 72.62           C  
ANISOU 2743  CD2 LEU B 216     5780  15055   6757    -88   -324   1369       C  
ATOM   2744  N   GLY B 217      25.745 -16.017  -0.726  1.00 69.29           N  
ANISOU 2744  N   GLY B 217     5338  14571   6418   -454   -756   1543       N  
ATOM   2745  CA  GLY B 217      25.801 -15.025   0.324  1.00 82.94           C  
ANISOU 2745  CA  GLY B 217     7152  16194   8169   -545   -928   1533       C  
ATOM   2746  C   GLY B 217      24.722 -15.241   1.368  1.00 86.21           C  
ANISOU 2746  C   GLY B 217     7718  16511   8526   -444   -958   1425       C  
ATOM   2747  O   GLY B 217      23.825 -16.074   1.231  1.00 83.24           O  
ANISOU 2747  O   GLY B 217     7382  16141   8105   -325   -848   1375       O  
ATOM   2748  N   SER B 218      24.822 -14.464   2.452  1.00 92.85           N  
ANISOU 2748  N   SER B 218     8648  17263   9367   -489  -1116   1389       N  
ATOM   2749  CA  SER B 218      23.796 -14.539   3.492  1.00 99.49           C  
ANISOU 2749  CA  SER B 218     9644  18024  10133   -389  -1147   1283       C  
ATOM   2750  C   SER B 218      22.448 -14.020   3.009  1.00111.08           C  
ANISOU 2750  C   SER B 218    11220  19414  11573   -388  -1123   1223       C  
ATOM   2751  O   SER B 218      21.430 -14.689   3.262  1.00119.77           O  
ANISOU 2751  O   SER B 218    12394  20510  12604   -268  -1032   1167       O  
ATOM   2752  CB  SER B 218      24.272 -13.808   4.752  1.00107.29           C  
ANISOU 2752  CB  SER B 218    10704  18946  11117   -420  -1328   1240       C  
ATOM   2753  OG  SER B 218      23.185 -13.209   5.436  1.00109.31           O  
ANISOU 2753  OG  SER B 218    11124  19100  11307   -374  -1398   1127       O  
ATOM   2754  N   PRO B 219      22.347 -12.866   2.333  1.00113.83           N  
ANISOU 2754  N   PRO B 219    11581  19695  11973   -517  -1205   1240       N  
ATOM   2755  CA  PRO B 219      21.028 -12.452   1.823  1.00108.33           C  
ANISOU 2755  CA  PRO B 219    10985  18927  11249   -504  -1174   1182       C  
ATOM   2756  C   PRO B 219      20.416 -13.450   0.858  1.00 98.27           C  
ANISOU 2756  C   PRO B 219     9657  17733   9949   -429   -981   1202       C  
ATOM   2757  O   PRO B 219      19.185 -13.531   0.761  1.00100.69           O  
ANISOU 2757  O   PRO B 219    10073  17966  10218   -360   -912   1130       O  
ATOM   2758  CB  PRO B 219      21.320 -11.109   1.137  1.00108.89           C  
ANISOU 2758  CB  PRO B 219    11043  18924  11407   -676  -1306   1236       C  
ATOM   2759  CG  PRO B 219      22.549 -10.608   1.796  1.00113.50           C  
ANISOU 2759  CG  PRO B 219    11583  19490  12051   -764  -1459   1276       C  
ATOM   2760  CD  PRO B 219      23.366 -11.827   2.088  1.00114.52           C  
ANISOU 2760  CD  PRO B 219    11604  19752  12154   -685  -1348   1316       C  
ATOM   2761  N   ALA B 220      21.239 -14.218   0.142  1.00 94.17           N  
ANISOU 2761  N   ALA B 220     8988  17331   9462   -429   -882   1283       N  
ATOM   2762  CA  ALA B 220      20.711 -15.255  -0.736  1.00 87.61           C  
ANISOU 2762  CA  ALA B 220     8105  16572   8612   -336   -715   1280       C  
ATOM   2763  C   ALA B 220      20.293 -16.487   0.057  1.00 90.20           C  
ANISOU 2763  C   ALA B 220     8479  16893   8899   -180   -640   1228       C  
ATOM   2764  O   ALA B 220      19.155 -16.953  -0.063  1.00 98.98           O  
ANISOU 2764  O   ALA B 220     9681  17937   9991   -100   -548   1173       O  
ATOM   2765  CB  ALA B 220      21.749 -15.622  -1.799  1.00 86.71           C  
ANISOU 2765  CB  ALA B 220     7825  16579   8540   -371   -636   1365       C  
ATOM   2766  N   ALA B 221      21.197 -17.015   0.888  1.00 89.15           N  
ANISOU 2766  N   ALA B 221     8292  16817   8763   -142   -680   1255       N  
ATOM   2767  CA  ALA B 221      20.914 -18.220   1.660  1.00 86.90           C  
ANISOU 2767  CA  ALA B 221     8029  16544   8445     -3   -631   1238       C  
ATOM   2768  C   ALA B 221      19.788 -18.029   2.668  1.00 83.51           C  
ANISOU 2768  C   ALA B 221     7763  16019   7949     46   -652   1176       C  
ATOM   2769  O   ALA B 221      19.243 -19.022   3.160  1.00 72.25           O  
ANISOU 2769  O   ALA B 221     6370  14583   6499    153   -587   1175       O  
ATOM   2770  CB  ALA B 221      22.176 -18.687   2.385  1.00 83.75           C  
ANISOU 2770  CB  ALA B 221     7555  16198   8066     16   -676   1281       C  
ATOM   2771  N   GLN B 222      19.432 -16.787   2.992  1.00 88.14           N  
ANISOU 2771  N   GLN B 222     8444  16539   8504    -24   -751   1128       N  
ATOM   2772  CA  GLN B 222      18.272 -16.513   3.830  1.00100.29           C  
ANISOU 2772  CA  GLN B 222    10132  18010   9965     37   -764   1052       C  
ATOM   2773  C   GLN B 222      16.961 -16.568   3.051  1.00110.53           C  
ANISOU 2773  C   GLN B 222    11496  19233  11265     63   -651   1013       C  
ATOM   2774  O   GLN B 222      15.948 -16.029   3.516  1.00116.73           O  
ANISOU 2774  O   GLN B 222    12399  19963  11991     94   -671    943       O  
ATOM   2775  CB  GLN B 222      18.426 -15.152   4.514  1.00101.55           C  
ANISOU 2775  CB  GLN B 222    10379  18102  10105    -26   -925    986       C  
ATOM   2776  CG  GLN B 222      19.403 -15.162   5.680  1.00100.35           C  
ANISOU 2776  CG  GLN B 222    10217  17972   9939    -16  -1025    989       C  
ATOM   2777  CD  GLN B 222      19.525 -13.811   6.355  1.00102.47           C  
ANISOU 2777  CD  GLN B 222    10580  18156  10197    -67  -1206    904       C  
ATOM   2778  OE1 GLN B 222      19.446 -12.770   5.704  1.00101.67           O  
ANISOU 2778  OE1 GLN B 222    10501  17981  10149   -165  -1291    884       O  
ATOM   2779  NE2 GLN B 222      19.725 -13.822   7.669  1.00104.38           N  
ANISOU 2779  NE2 GLN B 222    10880  18405  10375      2  -1280    854       N  
ATOM   2780  N   ALA B 223      16.962 -17.212   1.880  1.00106.75           N  
ANISOU 2780  N   ALA B 223    10941  18767  10852     60   -539   1050       N  
ATOM   2781  CA  ALA B 223      15.773 -17.330   1.048  1.00 89.26           C  
ANISOU 2781  CA  ALA B 223     8778  16487   8649     81   -435   1016       C  
ATOM   2782  C   ALA B 223      15.515 -18.762   0.592  1.00 82.10           C  
ANISOU 2782  C   ALA B 223     7817  15598   7779    169   -310   1043       C  
ATOM   2783  O   ALA B 223      14.675 -18.973  -0.291  1.00 91.12           O  
ANISOU 2783  O   ALA B 223     8978  16695   8948    183   -224   1018       O  
ATOM   2784  CB  ALA B 223      15.880 -16.410  -0.174  1.00 84.79           C  
ANISOU 2784  CB  ALA B 223     8188  15899   8131    -25   -447   1017       C  
ATOM   2785  N   ILE B 224      16.209 -19.746   1.158  1.00 74.04           N  
ANISOU 2785  N   ILE B 224     6730  14633   6770    230   -310   1090       N  
ATOM   2786  CA  ILE B 224      16.024 -21.152   0.812  1.00 65.05           C  
ANISOU 2786  CA  ILE B 224     5543  13487   5686    320   -223   1113       C  
ATOM   2787  C   ILE B 224      15.646 -21.910   2.076  1.00 72.93           C  
ANISOU 2787  C   ILE B 224     6586  14474   6651    395   -235   1155       C  
ATOM   2788  O   ILE B 224      16.386 -21.882   3.068  1.00 86.67           O  
ANISOU 2788  O   ILE B 224     8309  16271   8351    401   -309   1191       O  
ATOM   2789  CB  ILE B 224      17.280 -21.768   0.171  1.00 65.04           C  
ANISOU 2789  CB  ILE B 224     5399  13567   5746    338   -220   1141       C  
ATOM   2790  CG1 ILE B 224      17.657 -21.054  -1.131  1.00 59.22           C  
ANISOU 2790  CG1 ILE B 224     4596  12881   5026    265   -199   1122       C  
ATOM   2791  CG2 ILE B 224      17.086 -23.257  -0.065  1.00 68.95           C  
ANISOU 2791  CG2 ILE B 224     5857  14031   6309    451   -161   1148       C  
ATOM   2792  CD1 ILE B 224      18.612 -19.908  -0.946  1.00 62.60           C  
ANISOU 2792  CD1 ILE B 224     4981  13376   5429    153   -292   1157       C  
ATOM   2793  N   TRP B 225      14.500 -22.583   2.041  1.00 70.29           N  
ANISOU 2793  N   TRP B 225     6301  14075   6332    446   -166   1161       N  
ATOM   2794  CA  TRP B 225      14.091 -23.508   3.086  1.00 72.28           C  
ANISOU 2794  CA  TRP B 225     6572  14324   6569    513   -165   1234       C  
ATOM   2795  C   TRP B 225      14.204 -24.939   2.573  1.00 70.94           C  
ANISOU 2795  C   TRP B 225     6335  14101   6517    577   -131   1277       C  
ATOM   2796  O   TRP B 225      14.004 -25.208   1.385  1.00 74.18           O  
ANISOU 2796  O   TRP B 225     6721  14460   7005    584    -82   1226       O  
ATOM   2797  CB  TRP B 225      12.665 -23.219   3.561  1.00 71.84           C  
ANISOU 2797  CB  TRP B 225     6611  14244   6441    519   -128   1232       C  
ATOM   2798  CG  TRP B 225      12.592 -22.150   4.615  1.00 79.60           C  
ANISOU 2798  CG  TRP B 225     7659  15297   7289    506   -190   1204       C  
ATOM   2799  CD1 TRP B 225      12.603 -22.334   5.969  1.00 82.82           C  
ANISOU 2799  CD1 TRP B 225     8081  15786   7600    551   -231   1261       C  
ATOM   2800  CD2 TRP B 225      12.506 -20.734   4.405  1.00 76.67           C  
ANISOU 2800  CD2 TRP B 225     7348  14920   6864    453   -234   1106       C  
ATOM   2801  NE1 TRP B 225      12.524 -21.123   6.613  1.00 83.57           N  
ANISOU 2801  NE1 TRP B 225     8244  15923   7584    541   -294   1181       N  
ATOM   2802  CE2 TRP B 225      12.463 -20.125   5.676  1.00 80.47           C  
ANISOU 2802  CE2 TRP B 225     7882  15473   7218    481   -308   1087       C  
ATOM   2803  CE3 TRP B 225      12.458 -19.923   3.266  1.00 67.29           C  
ANISOU 2803  CE3 TRP B 225     6172  13673   5724    387   -227   1036       C  
ATOM   2804  CZ2 TRP B 225      12.375 -18.744   5.840  1.00 73.80           C  
ANISOU 2804  CZ2 TRP B 225     7115  14595   6332    448   -380    978       C  
ATOM   2805  CZ3 TRP B 225      12.371 -18.551   3.432  1.00 68.69           C  
ANISOU 2805  CZ3 TRP B 225     6418  13839   5843    343   -305    958       C  
ATOM   2806  CH2 TRP B 225      12.330 -17.976   4.709  1.00 70.79           C  
ANISOU 2806  CH2 TRP B 225     6744  14157   5998    378   -392    925       C  
ATOM   2807  N   VAL B 226      14.526 -25.859   3.480  1.00 67.74           N  
ANISOU 2807  N   VAL B 226     5903  13707   6129    629   -170   1367       N  
ATOM   2808  CA  VAL B 226      14.953 -27.198   3.089  1.00 68.70           C  
ANISOU 2808  CA  VAL B 226     5953  13772   6379    699   -178   1402       C  
ATOM   2809  C   VAL B 226      14.452 -28.210   4.113  1.00 61.42           C  
ANISOU 2809  C   VAL B 226     5047  12812   5478    740   -203   1529       C  
ATOM   2810  O   VAL B 226      14.542 -27.988   5.324  1.00 50.86           O  
ANISOU 2810  O   VAL B 226     3730  11552   4043    733   -240   1604       O  
ATOM   2811  CB  VAL B 226      16.491 -27.251   2.936  1.00 71.77           C  
ANISOU 2811  CB  VAL B 226     6245  14234   6792    721   -231   1385       C  
ATOM   2812  CG1 VAL B 226      17.170 -26.613   4.139  1.00 50.88           C  
ANISOU 2812  CG1 VAL B 226     3604  11688   4042    689   -299   1430       C  
ATOM   2813  CG2 VAL B 226      16.971 -28.673   2.752  1.00 60.01           C  
ANISOU 2813  CG2 VAL B 226     4684  12689   5429    817   -262   1418       C  
ATOM   2814  N   VAL B 227      13.911 -29.321   3.614  1.00 57.42           N  
ANISOU 2814  N   VAL B 227     4529  12188   5102    782   -193   1558       N  
ATOM   2815  CA  VAL B 227      13.583 -30.479   4.430  1.00 64.78           C  
ANISOU 2815  CA  VAL B 227     5454  13062   6099    816   -239   1703       C  
ATOM   2816  C   VAL B 227      14.721 -31.484   4.307  1.00 71.92           C  
ANISOU 2816  C   VAL B 227     6280  13922   7124    894   -317   1717       C  
ATOM   2817  O   VAL B 227      15.540 -31.427   3.387  1.00 85.43           O  
ANISOU 2817  O   VAL B 227     7939  15640   8882    932   -319   1602       O  
ATOM   2818  CB  VAL B 227      12.230 -31.109   4.024  1.00 75.83           C  
ANISOU 2818  CB  VAL B 227     6886  14338   7588    806   -206   1742       C  
ATOM   2819  CG1 VAL B 227      11.193 -30.024   3.775  1.00 71.47           C  
ANISOU 2819  CG1 VAL B 227     6399  13829   6928    745   -121   1680       C  
ATOM   2820  CG2 VAL B 227      12.396 -31.986   2.791  1.00 78.81           C  
ANISOU 2820  CG2 VAL B 227     7227  14576   8141    864   -229   1660       C  
ATOM   2821  N   SER B 228      14.782 -32.426   5.246  1.00 79.05           N  
ANISOU 2821  N   SER B 228     7167  14791   8076    923   -386   1865       N  
ATOM   2822  CA  SER B 228      15.920 -33.341   5.348  1.00 96.58           C  
ANISOU 2822  CA  SER B 228     9316  16978  10401   1004   -478   1891       C  
ATOM   2823  C   SER B 228      15.453 -34.782   5.157  1.00106.60           C  
ANISOU 2823  C   SER B 228    10576  18062  11865   1056   -548   1969       C  
ATOM   2824  O   SER B 228      14.979 -35.419   6.103  1.00106.37           O  
ANISOU 2824  O   SER B 228    10559  17995  11861   1035   -596   2148       O  
ATOM   2825  CB  SER B 228      16.634 -33.169   6.686  1.00 92.99           C  
ANISOU 2825  CB  SER B 228     8844  16647   9841    998   -530   2001       C  
ATOM   2826  OG  SER B 228      17.788 -33.989   6.755  1.00 84.98           O  
ANISOU 2826  OG  SER B 228     7755  15607   8926   1082   -622   2019       O  
ATOM   2827  N   LEU B 229      15.602 -35.291   3.936  1.00108.25           N  
ANISOU 2827  N   LEU B 229    10759  18161  12210   1124   -564   1838       N  
ATOM   2828  CA  LEU B 229      15.410 -36.710   3.637  1.00109.03           C  
ANISOU 2828  CA  LEU B 229    10843  18061  12523   1198   -667   1874       C  
ATOM   2829  C   LEU B 229      15.966 -37.051   2.258  1.00115.72           C  
ANISOU 2829  C   LEU B 229    11646  18850  13474   1310   -687   1671       C  
ATOM   2830  O   LEU B 229      17.035 -36.575   1.874  1.00116.10           O  
ANISOU 2830  O   LEU B 229    11632  19027  13452   1361   -664   1558       O  
ATOM   2831  CB  LEU B 229      13.932 -37.102   3.714  1.00102.55           C  
ANISOU 2831  CB  LEU B 229    10080  17113  11771   1127   -662   1978       C  
ATOM   2832  CG  LEU B 229      13.579 -38.081   4.838  1.00100.29           C  
ANISOU 2832  CG  LEU B 229     9792  16740  11573   1101   -760   2219       C  
ATOM   2833  CD1 LEU B 229      12.150 -38.586   4.697  1.00 97.86           C  
ANISOU 2833  CD1 LEU B 229     9520  16293  11370   1032   -768   2319       C  
ATOM   2834  CD2 LEU B 229      14.563 -39.243   4.867  1.00 96.91           C  
ANISOU 2834  CD2 LEU B 229     9314  16189  11320   1212   -910   2234       C  
TER    2835      LEU B 229                                                      
HETATM 2836  O   HOH A 301     -21.329 -10.907 -23.731  1.00 45.94           O  
ANISOU 2836  O   HOH A 301     4054   9903   3498    625    239    -98       O  
HETATM 2837  O   HOH A 302     -17.500  -2.727 -14.072  1.00100.63           O  
ANISOU 2837  O   HOH A 302    11598  16419  10219   1089   -425   -463       O  
HETATM 2838  O   HOH A 303     -20.500  -8.025 -23.243  1.00 78.60           O  
ANISOU 2838  O   HOH A 303     8370  13920   7575    638     79    -63       O  
HETATM 2839  O   HOH B 301       4.379 -17.494  -3.683  1.00 41.61           O  
ANISOU 2839  O   HOH B 301     3224   9952   2635    305    185    685       O  
HETATM 2840  O   HOH B 302       4.036 -15.297  -3.472  1.00 66.13           O  
ANISOU 2840  O   HOH B 302     6449  13009   5670    265     60    592       O  
HETATM 2841  O   HOH B 303      30.843 -23.284  10.226  1.00 67.28           O  
ANISOU 2841  O   HOH B 303     5067  14461   6037    391  -1192   1609       O  
HETATM 2842  O   HOH B 304       4.114 -16.645  -1.506  1.00 67.70           O  
ANISOU 2842  O   HOH B 304     6614  13316   5794    370     94    654       O  
HETATM 2843  O   HOH B 305       6.620 -14.721 -14.908  1.00104.72           O  
ANISOU 2843  O   HOH B 305    10839  18190  10760   -102    241    801       O  
HETATM 2844  O   HOH B 306      -4.491 -29.944   2.763  1.00 66.61           O  
ANISOU 2844  O   HOH B 306     5760  13263   6285    350    435   2271       O  
MASTER      389    0    0   16   12    0    0    6 2842    2    0   36          
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.