CNRS Nantes University UFIP UFIP
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***  11111111111  ***

elNémo ID: 20053001484328695

Job options:

ID        	=	 20053001484328695
JOBID     	=	 11111111111
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 11111111111

HEADER    HYDROLASE                               22-MAR-20   6W9C              
TITLE     THE CRYSTAL STRUCTURE OF PAPAIN-LIKE PROTEASE OF SARS COV-2           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PAPAIN-LIKE PROTEINASE;                                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 3.4.22.-;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: TWO C-TERMINAL ALANINE RESIDUES ARE CLONING ARTIFACTS 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCPD                                      
KEYWDS    COVID-19, CORONAVIRUS, SARS, COV-2 IN PAPAIN-LIKE PROTEASE, IDP51000, 
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID,        
KEYWDS   3 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.OSIPIUK,R.JEDRZEJCZAK,C.TESAR,M.ENDRES,L.STOLS,G.BABNIGG,Y.KIM,     
AUTHOR   2 K.MICHALSKA,A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF           
AUTHOR   3 INFECTIOUS DISEASES (CSGID)                                          
REVDAT   2   06-MAY-20 6W9C    1       COMPND SOURCE REMARK DBREF               
REVDAT   2 2                   1       SEQADV LINK   SITE   ATOM                
REVDAT   1   01-APR-20 6W9C    0                                                
JRNL        AUTH   J.OSIPIUK,R.JEDRZEJCZAK,C.TESAR,M.ENDRES,L.STOLS,G.BABNIGG,  
JRNL        AUTH 2 Y.KIM,K.MICHALSKA,A.JOACHIMIAK,                              
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 4 (CSGID)                                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF PAPAIN-LIKE PROTEASE OF SARS COV-2  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0232                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 57.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 19766                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.235                           
REMARK   3   FREE R VALUE                     : 0.309                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1031                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 977                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 37.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.3920                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7392                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.65000                                              
REMARK   3    B22 (A**2) : -3.86000                                             
REMARK   3    B33 (A**2) : 3.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.37000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.625         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.436         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 51.587        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.917                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.843                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7569 ; 0.004 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  6770 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10271 ; 1.316 ; 1.656       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15799 ; 1.082 ; 1.571       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   927 ; 7.279 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   359 ;39.685 ;24.039       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1282 ;19.235 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;23.142 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1006 ; 0.044 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8397 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1532 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   315                          
REMARK   3    RESIDUE RANGE :   C   401        C   401                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.447   33.990   25.598              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0356 T22:   0.1518                                     
REMARK   3      T33:   0.4976 T12:   0.0079                                     
REMARK   3      T13:  -0.0121 T23:   0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8900 L22:   1.2663                                     
REMARK   3      L33:   1.5720 L12:  -0.1311                                     
REMARK   3      L13:   0.8310 L23:  -0.4614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0762 S12:   0.0720 S13:   0.0152                       
REMARK   3      S21:  -0.1356 S22:  -0.0624 S23:  -0.0960                       
REMARK   3      S31:   0.0688 S32:   0.2085 S33:  -0.0138                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B   314                          
REMARK   3    RESIDUE RANGE :   B   501        B   502                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.217    0.640   25.589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0060 T22:   0.1933                                     
REMARK   3      T33:   0.5296 T12:   0.0003                                     
REMARK   3      T13:  -0.0282 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0743 L22:   0.6710                                     
REMARK   3      L33:   1.5263 L12:  -0.1626                                     
REMARK   3      L13:  -0.3044 L23:  -0.1700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0300 S12:   0.1133 S13:  -0.1094                       
REMARK   3      S21:   0.0031 S22:  -0.0847 S23:   0.0934                       
REMARK   3      S31:   0.0667 S32:  -0.0274 S33:   0.1147                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     4        C   315                          
REMARK   3    RESIDUE RANGE :   C   402        C   402                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -54.839    4.940   25.572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0313 T22:   0.1141                                     
REMARK   3      T33:   0.5453 T12:  -0.0228                                     
REMARK   3      T13:  -0.0854 T23:   0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0778 L22:   0.5132                                     
REMARK   3      L33:   1.8231 L12:  -0.0287                                     
REMARK   3      L13:  -0.2627 L23:   0.5821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0277 S12:   0.0049 S13:   0.1609                       
REMARK   3      S21:  -0.0584 S22:  -0.0426 S23:   0.1068                       
REMARK   3      S31:  -0.0455 S32:  -0.1209 S33:   0.0149                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6W9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000247849.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20799                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 57.3                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 38.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.140                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5Y3Q                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THIN PLATES                                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM ACETATE, 10% PEG 8000,   
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       95.39300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.14000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       95.39300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       55.14000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     GLU A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ALA A   316                                                      
REMARK 465     ALA A   317                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     CYS B   224                                                      
REMARK 465     THR B   225                                                      
REMARK 465     CYS B   226                                                      
REMARK 465     GLY B   227                                                      
REMARK 465     LYS B   228                                                      
REMARK 465     LYS B   315                                                      
REMARK 465     ALA B   316                                                      
REMARK 465     ALA B   317                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     ALA C   316                                                      
REMARK 465     ALA C   317                                                      
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   OH   TYR B    83     ND2  ASN B   146              2.16            
REMARK 500   OE1  GLN A   122     OG1  THR A   277              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   ND2  ASN B   308     ND2  ASN B   308     2556     1.90            
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    ASP A  76   CB  -  CG  -  OD1 ANGL. DEV. =  -5.4 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    ASN A  13       20.53     80.39                                   
REMARK 500    ILE A  14      -71.63   -121.15                                   
REMARK 500    ASN A  15       94.68    -69.40                                   
REMARK 500    PRO A  46      151.44    -44.86                                   
REMARK 500    GLU A  51      117.17    -32.47                                   
REMARK 500    PRO A  59      105.90    -56.43                                   
REMARK 500    ASP A  76      106.12    -44.11                                   
REMARK 500    ALA A 107      122.49   -174.13                                   
REMARK 500    ALA A 145      -71.02    -63.99                                   
REMARK 500    ASN A 177       60.83   -114.39                                   
REMARK 500    THR A 191      -72.35    -82.02                                   
REMARK 500    LYS A 228     -141.17   -109.74                                   
REMARK 500    ALA A 246      147.58   -176.73                                   
REMARK 500    GLN A 250      104.06    -57.04                                   
REMARK 500    PHE A 258      160.95    172.51                                   
REMARK 500    THR A 259      -79.04    -80.84                                   
REMARK 500    ASN A 267      -55.60   -120.40                                   
REMARK 500    TYR A 268     -107.10   -109.86                                   
REMARK 500    LYS A 279     -138.87   -120.08                                   
REMARK 500    THR A 281     -153.71   -128.31                                   
REMARK 500    ASP A 286       62.60   -100.21                                   
REMARK 500    ASN A 308      -62.63   -133.61                                   
REMARK 500    THR A 313       51.70    -93.74                                   
REMARK 500    ASN B  13       39.74     70.94                                   
REMARK 500    ILE B  14      -54.88   -139.56                                   
REMARK 500    ALA B  39       94.28    -55.76                                   
REMARK 500    PRO B  46      108.12    -53.19                                   
REMARK 500    GLU B  51      121.39    -34.89                                   
REMARK 500    ASP B  61     -168.20   -173.03                                   
REMARK 500    ASP B  76       98.86    -57.75                                   
REMARK 500    PRO B  77        5.83    -69.99                                   
REMARK 500    TYR B  95       79.27   -107.28                                   
REMARK 500    SER B 103     -167.69   -102.13                                   
REMARK 500    ALA B 107      136.69   -170.46                                   
REMARK 500    SER B 170      -71.46    -53.28                                   
REMARK 500    THR B 191      -61.34    -95.52                                   
REMARK 500    VAL B 235      -64.57    -93.78                                   
REMARK 500    TYR B 251      105.72   -165.09                                   
REMARK 500    THR B 259      -74.79    -74.56                                   
REMARK 500    TYR B 268      -79.75   -113.27                                   
REMARK 500    LYS B 279     -128.80   -123.28                                   
REMARK 500    VAL C   7     -168.44   -128.90                                   
REMARK 500    GLN C  29      -52.38    -26.06                                   
REMARK 500    GLU C  51      113.14    -36.18                                   
REMARK 500    PRO C  59       87.14    -50.42                                   
REMARK 500    ASP C  61      146.13    176.04                                   
REMARK 500    ASN C  99       51.81     38.00                                   
REMARK 500    SER C 103     -169.69   -106.59                                   
REMARK 500    ALA C 107      129.75   -177.69                                   
REMARK 500    ASN C 109       43.15     34.28                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 270   SG                                                     
REMARK 620 2 CYS B 270   SG   88.0                                              
REMARK 620 3 CYS C 270   SG   99.8 117.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 189   SG                                                     
REMARK 620 2 CYS B 192   SG   91.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 189   SG                                                     
REMARK 620 2 CYS C 224   SG  133.9                                              
REMARK 620 3 CYS C 226   SG  118.4  96.3                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP51000   RELATED DB: TARGETTRACK                       
DBREF  6W9C A    1   315  UNP    P0DTC1   R1A_SARS2     1564   1878             
DBREF  6W9C B    1   315  UNP    P0DTC1   R1A_SARS2     1564   1878             
DBREF  6W9C C    1   315  UNP    P0DTC1   R1A_SARS2     1564   1878             
SEQADV 6W9C ALA A  316  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA A  317  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA B  316  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA B  317  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA C  316  UNP  P0DTC1              EXPRESSION TAG                 
SEQADV 6W9C ALA C  317  UNP  P0DTC1              EXPRESSION TAG                 
SEQRES   1 A  317  GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL ASP ASN          
SEQRES   2 A  317  ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER MET THR          
SEQRES   3 A  317  TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP GLY ALA          
SEQRES   4 A  317  ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS GLU GLY          
SEQRES   5 A  317  LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR LEU ARG          
SEQRES   6 A  317  VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP PRO SER          
SEQRES   7 A  317  PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS THR LYS          
SEQRES   8 A  317  LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR SER ILE          
SEQRES   9 A  317  LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR ALA LEU          
SEQRES  10 A  317  LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN PRO PRO          
SEQRES  11 A  317  ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA GLY GLU          
SEQRES  12 A  317  ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR CYS ASN          
SEQRES  13 A  317  LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU THR MET          
SEQRES  14 A  317  SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER CYS LYS          
SEQRES  15 A  317  ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY GLN GLN          
SEQRES  16 A  317  GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET TYR MET          
SEQRES  17 A  317  GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY VAL GLN          
SEQRES  18 A  317  ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS TYR LEU          
SEQRES  19 A  317  VAL GLN GLN GLU SER PRO PHE VAL MET MET SER ALA PRO          
SEQRES  20 A  317  PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE THR CYS          
SEQRES  21 A  317  ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY HIS TYR          
SEQRES  22 A  317  LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS ILE ASP          
SEQRES  23 A  317  GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS GLY PRO          
SEQRES  24 A  317  ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR THR THR          
SEQRES  25 A  317  THR ILE LYS ALA ALA                                          
SEQRES   1 B  317  GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL ASP ASN          
SEQRES   2 B  317  ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER MET THR          
SEQRES   3 B  317  TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP GLY ALA          
SEQRES   4 B  317  ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS GLU GLY          
SEQRES   5 B  317  LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR LEU ARG          
SEQRES   6 B  317  VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP PRO SER          
SEQRES   7 B  317  PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS THR LYS          
SEQRES   8 B  317  LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR SER ILE          
SEQRES   9 B  317  LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR ALA LEU          
SEQRES  10 B  317  LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN PRO PRO          
SEQRES  11 B  317  ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA GLY GLU          
SEQRES  12 B  317  ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR CYS ASN          
SEQRES  13 B  317  LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU THR MET          
SEQRES  14 B  317  SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER CYS LYS          
SEQRES  15 B  317  ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY GLN GLN          
SEQRES  16 B  317  GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET TYR MET          
SEQRES  17 B  317  GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY VAL GLN          
SEQRES  18 B  317  ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS TYR LEU          
SEQRES  19 B  317  VAL GLN GLN GLU SER PRO PHE VAL MET MET SER ALA PRO          
SEQRES  20 B  317  PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE THR CYS          
SEQRES  21 B  317  ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY HIS TYR          
SEQRES  22 B  317  LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS ILE ASP          
SEQRES  23 B  317  GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS GLY PRO          
SEQRES  24 B  317  ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR THR THR          
SEQRES  25 B  317  THR ILE LYS ALA ALA                                          
SEQRES   1 C  317  GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL ASP ASN          
SEQRES   2 C  317  ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER MET THR          
SEQRES   3 C  317  TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP GLY ALA          
SEQRES   4 C  317  ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS GLU GLY          
SEQRES   5 C  317  LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR LEU ARG          
SEQRES   6 C  317  VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP PRO SER          
SEQRES   7 C  317  PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS THR LYS          
SEQRES   8 C  317  LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR SER ILE          
SEQRES   9 C  317  LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR ALA LEU          
SEQRES  10 C  317  LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN PRO PRO          
SEQRES  11 C  317  ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA GLY GLU          
SEQRES  12 C  317  ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR CYS ASN          
SEQRES  13 C  317  LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU THR MET          
SEQRES  14 C  317  SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER CYS LYS          
SEQRES  15 C  317  ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY GLN GLN          
SEQRES  16 C  317  GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET TYR MET          
SEQRES  17 C  317  GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY VAL GLN          
SEQRES  18 C  317  ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS TYR LEU          
SEQRES  19 C  317  VAL GLN GLN GLU SER PRO PHE VAL MET MET SER ALA PRO          
SEQRES  20 C  317  PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE THR CYS          
SEQRES  21 C  317  ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY HIS TYR          
SEQRES  22 C  317  LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS ILE ASP          
SEQRES  23 C  317  GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS GLY PRO          
SEQRES  24 C  317  ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR THR THR          
SEQRES  25 C  317  THR ILE LYS ALA ALA                                          
HET     ZN  A 401       1                                                       
HET     ZN  B 501       1                                                       
HET     CL  B 502       1                                                       
HET     ZN  C 401       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4   ZN    3(ZN 2+)                                                     
FORMUL   6   CL    CL 1-                                                        
FORMUL   8  HOH   *(H2 O)                                                       
HELIX    1 AA1 THR A   26  PHE A   31  1                                   6    
HELIX    2 AA2 HIS A   47  GLU A   51  5                                   5    
HELIX    3 AA3 ASP A   61  HIS A   73  1                                  13    
HELIX    4 AA4 SER A   78  LYS A   91  1                                  14    
HELIX    5 AA5 ASN A  110  GLN A  121  1                                  12    
HELIX    6 AA6 PRO A  129  ALA A  141  1                                  13    
HELIX    7 AA7 ALA A  144  CYS A  155  1                                  12    
HELIX    8 AA8 ASP A  164  HIS A  175  1                                  12    
HELIX    9 AA9 VAL A  202  ALA A  204  5                                   3    
HELIX   10 AB1 GLU A  214  GLY A  219  1                                   6    
HELIX   11 AB2 TYR B   27  GLY B   32  1                                   6    
HELIX   12 AB3 THR B   63  HIS B   73  1                                  11    
HELIX   13 AB4 SER B   78  LYS B   91  1                                  14    
HELIX   14 AB5 ASN B  110  GLN B  121  1                                  12    
HELIX   15 AB6 PRO B  129  GLY B  142  1                                  14    
HELIX   16 AB7 ALA B  144  CYS B  155  1                                  12    
HELIX   17 AB8 ASP B  164  HIS B  175  1                                  12    
HELIX   18 AB9 VAL B  202  ALA B  204  5                                   3    
HELIX   19 AC1 SER B  212  LYS B  217  1                                   6    
HELIX   20 AC2 THR C   26  GLY C   32  1                                   7    
HELIX   21 AC3 HIS C   47  GLU C   51  5                                   5    
HELIX   22 AC4 ASP C   61  HIS C   73  1                                  13    
HELIX   23 AC5 SER C   78  LYS C   91  1                                  14    
HELIX   24 AC6 ASN C  110  GLN C  122  1                                  13    
HELIX   25 AC7 PRO C  129  ALA C  141  1                                  13    
HELIX   26 AC8 ALA C  144  CYS C  155  1                                  12    
HELIX   27 AC9 ASP C  164  GLN C  174  1                                  11    
HELIX   28 AD1 GLY C  201  MET C  206  1                                   6    
HELIX   29 AD2 SER C  212  GLY C  219  1                                   8    
SHEET    1 AA1 5 HIS A  17  ASP A  22  0                                        
SHEET    2 AA1 5 THR A   4  THR A  10 -1  N  VAL A   7   O  GLN A  19           
SHEET    3 AA1 5 THR A  54  VAL A  57  1  O  PHE A  55   N  THR A  10           
SHEET    4 AA1 5 THR A  34  LEU A  36 -1  N  TYR A  35   O  TYR A  56           
SHEET    5 AA1 5 ALA A  39  ASP A  40 -1  O  ALA A  39   N  LEU A  36           
SHEET    1 AA2 4 GLY A 193  LYS A 200  0                                        
SHEET    2 AA2 4 LYS A 182  CYS A 189 -1  N  LEU A 185   O  THR A 197           
SHEET    3 AA2 4 GLN A 229  GLU A 238 -1  O  VAL A 235   N  VAL A 184           
SHEET    4 AA2 4 VAL A 220  PRO A 223 -1  N  VAL A 220   O  LYS A 232           
SHEET    1 AA3 4 GLY A 193  LYS A 200  0                                        
SHEET    2 AA3 4 LYS A 182  CYS A 189 -1  N  LEU A 185   O  THR A 197           
SHEET    3 AA3 4 GLN A 229  GLU A 238 -1  O  VAL A 235   N  VAL A 184           
SHEET    4 AA3 4 SER A 309  THR A 311 -1  O  TYR A 310   N  GLN A 237           
SHEET    1 AA4 7 MET A 206  MET A 208  0                                        
SHEET    2 AA4 7 PHE A 241  LEU A 253  1  O  SER A 245   N  TYR A 207           
SHEET    3 AA4 7 TYR A 296  LYS A 306 -1  O  TYR A 296   N  LEU A 253           
SHEET    4 AA4 7 ALA A 261  THR A 265 -1  N  SER A 262   O  THR A 301           
SHEET    5 AA4 7 HIS A 272  SER A 278 -1  O  ILE A 276   N  ALA A 261           
SHEET    6 AA4 7 LEU A 282  ILE A 285 -1  O  ILE A 285   N  HIS A 275           
SHEET    7 AA4 7 LYS A 292  SER A 293 -1  O  SER A 293   N  LEU A 282           
SHEET    1 AA5 5 HIS B  17  VAL B  21  0                                        
SHEET    2 AA5 5 ILE B   5  THR B  10 -1  N  VAL B   7   O  GLN B  19           
SHEET    3 AA5 5 THR B  54  VAL B  57  1  O  PHE B  55   N  PHE B   8           
SHEET    4 AA5 5 THR B  34  LEU B  36 -1  N  TYR B  35   O  TYR B  56           
SHEET    5 AA5 5 ALA B  39  ASP B  40 -1  O  ALA B  39   N  LEU B  36           
SHEET    1 AA6 2 GLN B  97  VAL B  98  0                                        
SHEET    2 AA6 2 LEU B 101  THR B 102 -1  O  LEU B 101   N  VAL B  98           
SHEET    1 AA7 4 GLN B 194  LYS B 200  0                                        
SHEET    2 AA7 4 LYS B 182  VAL B 188 -1  N  ARG B 183   O  LEU B 199           
SHEET    3 AA7 4 THR B 231  GLU B 238 -1  O  GLU B 238   N  LYS B 182           
SHEET    4 AA7 4 TYR B 310  THR B 311 -1  O  TYR B 310   N  GLN B 237           
SHEET    1 AA8 7 MET B 206  MET B 208  0                                        
SHEET    2 AA8 7 PHE B 241  GLN B 250  1  O  SER B 245   N  TYR B 207           
SHEET    3 AA8 7 PRO B 299  LYS B 306 -1  O  VAL B 303   N  MET B 244           
SHEET    4 AA8 7 CYS B 260  THR B 265 -1  N  CYS B 260   O  PHE B 304           
SHEET    5 AA8 7 HIS B 272  SER B 278 -1  O  LYS B 274   N  GLU B 263           
SHEET    6 AA8 7 LEU B 282  ASP B 286 -1  O  ILE B 285   N  HIS B 275           
SHEET    7 AA8 7 LEU B 289  SER B 293 -1  O  SER B 293   N  LEU B 282           
SHEET    1 AA9 5 HIS C  17  VAL C  21  0                                        
SHEET    2 AA9 5 ILE C   5  THR C  10 -1  N  THR C   9   O  HIS C  17           
SHEET    3 AA9 5 THR C  54  VAL C  57  1  O  PHE C  55   N  PHE C   8           
SHEET    4 AA9 5 THR C  34  LEU C  36 -1  N  TYR C  35   O  TYR C  56           
SHEET    5 AA9 5 ALA C  39  ASP C  40 -1  O  ALA C  39   N  LEU C  36           
SHEET    1 AB1 2 GLN C  97  VAL C  98  0                                        
SHEET    2 AB1 2 LEU C 101  THR C 102 -1  O  LEU C 101   N  VAL C  98           
SHEET    1 AB2 4 GLN C 194  LYS C 200  0                                        
SHEET    2 AB2 4 LYS C 182  VAL C 188 -1  N  VAL C 187   O  GLN C 195           
SHEET    3 AB2 4 THR C 231  GLU C 238 -1  O  THR C 231   N  VAL C 188           
SHEET    4 AB2 4 TYR C 310  THR C 311 -1  O  TYR C 310   N  GLN C 237           
SHEET    1 AB3 2 PRO C 223  CYS C 224  0                                        
SHEET    2 AB3 2 LYS C 228  GLN C 229 -1  O  LYS C 228   N  CYS C 224           
SHEET    1 AB4 6 PHE C 241  LEU C 253  0                                        
SHEET    2 AB4 6 TYR C 296  LYS C 306 -1  O  VAL C 303   N  MET C 244           
SHEET    3 AB4 6 CYS C 260  THR C 265 -1  N  CYS C 260   O  PHE C 304           
SHEET    4 AB4 6 HIS C 272  SER C 278 -1  O  LYS C 274   N  GLU C 263           
SHEET    5 AB4 6 LEU C 282  ASP C 286 -1  O  ILE C 285   N  HIS C 275           
SHEET    6 AB4 6 LEU C 289  SER C 293 -1  O  THR C 291   N  CYS C 284           
SSBOND   1 CYS A  189    CYS A  226                          1555   1555  2.04  
LINK         SG  CYS A 270                ZN    ZN A 401     1555   1555  2.75  
LINK         SG  CYS B 189                ZN    ZN B 501     1555   1555  2.79  
LINK         SG  CYS B 192                ZN    ZN B 501     1555   1555  2.66  
LINK         SG  CYS B 270                ZN    ZN A 401     1555   1555  2.41  
LINK         SG  CYS C 189                ZN    ZN C 401     1555   1555  2.78  
LINK         SG  CYS C 224                ZN    ZN C 401     1555   1555  2.22  
LINK         SG  CYS C 226                ZN    ZN C 401     1555   1555  2.85  
LINK         SG  CYS C 270                ZN    ZN A 401     1555   1555  2.40  
SITE     1 AC1  3 CYS A 270  CYS B 270  CYS C 270                               
SITE     1 AC2  2 CYS B 189  CYS B 192                                          
SITE     1 AC3  3 ILE B 285  ASP B 286  GLY B 287                               
SITE     1 AC4  3 CYS C 189  CYS C 224  CYS C 226                               
CRYST1  190.786  110.280   64.069  90.00  96.22  90.00 C 1 2 1      12          
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      0.005241  0.000000  0.000571        0.00000                         
SCALE2      0.000000  0.009068  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015700        0.00000                         
ATOM      1  N   ARG A   3     -59.695  23.876  -8.802  1.00 95.58           N  
ANISOU    1  N   ARG A   3    14348   8506  13459   -331  -4749    441       N  
ATOM      2  CA  ARG A   3     -58.479  23.235  -9.374  1.00 96.07           C  
ANISOU    2  CA  ARG A   3    14682   8537  13281   -175  -4668    299       C  
ATOM      3  C   ARG A   3     -57.240  23.786  -8.653  1.00 94.76           C  
ANISOU    3  C   ARG A   3    14371   8541  13089    -70  -4329    254       C  
ATOM      4  O   ARG A   3     -56.457  22.963  -8.141  1.00 94.76           O  
ANISOU    4  O   ARG A   3    14411   8538  13053     -1  -4250    180       O  
ATOM      5  CB  ARG A   3     -58.431  23.454 -10.891  1.00 97.64           C  
ANISOU    5  CB  ARG A   3    15168   8670  13257   -104  -4767    249       C  
ATOM      6  CG  ARG A   3     -57.639  22.401 -11.658  1.00 99.15           C  
ANISOU    6  CG  ARG A   3    15700   8762  13207     30  -4818    109       C  
ATOM      7  CD  ARG A   3     -56.165  22.742 -11.797  1.00 98.72           C  
ANISOU    7  CD  ARG A   3    15697   8844  12966    207  -4517     12       C  
ATOM      8  NE  ARG A   3     -55.290  21.592 -11.571  1.00 99.21           N  
ANISOU    8  NE  ARG A   3    15901   8863  12929    324  -4480   -104       N  
ATOM      9  CZ  ARG A   3     -54.509  21.007 -12.481  1.00100.30           C  
ANISOU    9  CZ  ARG A   3    16339   8957  12811    486  -4476   -231       C  
ATOM     10  NH1 ARG A   3     -54.464  21.448 -13.729  1.00101.51           N  
ANISOU   10  NH1 ARG A   3    16698   9108  12763    549  -4503   -258       N  
ATOM     11  NH2 ARG A   3     -53.765  19.972 -12.128  1.00100.16           N  
ANISOU   11  NH2 ARG A   3    16419   8900  12735    592  -4444   -332       N  
ATOM     12  N   THR A   4     -57.076  25.117  -8.609  1.00 93.94           N  
ANISOU   12  N   THR A   4    14109   8573  13009    -60  -4148    301       N  
ATOM     13  CA  THR A   4     -55.946  25.825  -7.937  1.00 92.47           C  
ANISOU   13  CA  THR A   4    13767   8555  12811     21  -3831    276       C  
ATOM     14  C   THR A   4     -56.486  26.917  -6.998  1.00 90.88           C  
ANISOU   14  C   THR A   4    13246   8459  12825    -70  -3735    382       C  
ATOM     15  O   THR A   4     -57.403  27.648  -7.424  1.00 91.46           O  
ANISOU   15  O   THR A   4    13274   8513  12960   -140  -3845    459       O  
ATOM     16  CB  THR A   4     -54.975  26.431  -8.962  1.00 92.81           C  
ANISOU   16  CB  THR A   4    13979   8664  12621    148  -3685    215       C  
ATOM     17  OG1 THR A   4     -55.609  27.540  -9.601  1.00 93.13           O  
ANISOU   17  OG1 THR A   4    13996   8719  12670     95  -3731    291       O  
ATOM     18  CG2 THR A   4     -54.519  25.443 -10.014  1.00 94.44           C  
ANISOU   18  CG2 THR A   4    14517   8771  12592    255  -3785    107       C  
ATOM     19  N   ILE A   5     -55.925  27.034  -5.784  1.00 88.87           N  
ANISOU   19  N   ILE A   5    12785   8309  12672    -61  -3541    383       N  
ATOM     20  CA  ILE A   5     -56.296  28.070  -4.767  1.00 87.52           C  
ANISOU   20  CA  ILE A   5    12311   8248  12693   -127  -3422    468       C  
ATOM     21  C   ILE A   5     -55.129  29.053  -4.582  1.00 86.22           C  
ANISOU   21  C   ILE A   5    12080   8221  12458    -40  -3149    439       C  
ATOM     22  O   ILE A   5     -53.973  28.653  -4.825  1.00 85.97           O  
ANISOU   22  O   ILE A   5    12175   8216  12271     61  -3029    355       O  
ATOM     23  CB  ILE A   5     -56.721  27.425  -3.430  1.00 87.03           C  
ANISOU   23  CB  ILE A   5    12054   8193  12819   -205  -3440    506       C  
ATOM     24  CG1 ILE A   5     -55.559  26.734  -2.711  1.00 87.21           C  
ANISOU   24  CG1 ILE A   5    12083   8257  12792   -131  -3282    429       C  
ATOM     25  CG2 ILE A   5     -57.890  26.477  -3.647  1.00 88.32           C  
ANISOU   25  CG2 ILE A   5    12278   8223  13057   -308  -3721    552       C  
ATOM     26  CD1 ILE A   5     -55.739  26.625  -1.213  1.00 86.09           C  
ANISOU   26  CD1 ILE A   5    11691   8183  12835   -195  -3205    477       C  
ATOM     27  N   LYS A   6     -55.438  30.284  -4.153  1.00 84.93           N  
ANISOU   27  N   LYS A   6    11721   8138  12408    -78  -3062    508       N  
ATOM     28  CA  LYS A   6     -54.484  31.420  -4.010  1.00 83.41           C  
ANISOU   28  CA  LYS A   6    11456   8066  12170    -20  -2830    502       C  
ATOM     29  C   LYS A   6     -54.077  31.557  -2.533  1.00 81.69           C  
ANISOU   29  C   LYS A   6    11007   7943  12089    -28  -2663    507       C  
ATOM     30  O   LYS A   6     -54.975  31.729  -1.685  1.00 79.68           O  
ANISOU   30  O   LYS A   6    10564   7694  12015   -102  -2713    566       O  
ATOM     31  CB  LYS A   6     -55.127  32.696  -4.568  1.00 83.28           C  
ANISOU   31  CB  LYS A   6    11405   8054  12184    -55  -2873    574       C  
ATOM     32  CG  LYS A   6     -54.186  33.637  -5.312  1.00 83.06           C  
ANISOU   32  CG  LYS A   6    11470   8089  12001      7  -2731    563       C  
ATOM     33  CD  LYS A   6     -54.900  34.759  -6.045  1.00 83.33           C  
ANISOU   33  CD  LYS A   6    11518   8096  12046    -30  -2818    634       C  
ATOM     34  CE  LYS A   6     -53.980  35.898  -6.435  1.00 82.96           C  
ANISOU   34  CE  LYS A   6    11494   8130  11894      8  -2652    648       C  
ATOM     35  NZ  LYS A   6     -54.725  37.158  -6.672  1.00 82.74           N  
ANISOU   35  NZ  LYS A   6    11403   8085  11950    -37  -2716    729       N  
ATOM     36  N   VAL A   7     -52.768  31.477  -2.249  1.00 81.77           N  
ANISOU   36  N   VAL A   7    11029   8030  12009     47  -2473    448       N  
ATOM     37  CA  VAL A   7     -52.166  31.501  -0.878  1.00 80.76           C  
ANISOU   37  CA  VAL A   7    10711   7990  11982     51  -2308    439       C  
ATOM     38  C   VAL A   7     -50.915  32.395  -0.884  1.00 80.66           C  
ANISOU   38  C   VAL A   7    10674   8087  11885    115  -2091    422       C  
ATOM     39  O   VAL A   7     -50.544  32.898  -1.970  1.00 81.92           O  
ANISOU   39  O   VAL A   7    10967   8254  11904    152  -2072    419       O  
ATOM     40  CB  VAL A   7     -51.830  30.078  -0.381  1.00 80.73           C  
ANISOU   40  CB  VAL A   7    10753   7951  11969     73  -2334    383       C  
ATOM     41  CG1 VAL A   7     -53.079  29.226  -0.209  1.00 81.19           C  
ANISOU   41  CG1 VAL A   7    10808   7906  12134    -12  -2550    419       C  
ATOM     42  CG2 VAL A   7     -50.824  29.371  -1.281  1.00 81.67           C  
ANISOU   42  CG2 VAL A   7    11096   8049  11883    179  -2306    297       C  
ATOM     43  N   PHE A   8     -50.295  32.578   0.289  1.00 79.22           N  
ANISOU   43  N   PHE A   8    10327   7988  11783    119  -1939    416       N  
ATOM     44  CA  PHE A   8     -49.060  33.379   0.511  1.00 77.98           C  
ANISOU   44  CA  PHE A   8    10113   7940  11573    165  -1732    408       C  
ATOM     45  C   PHE A   8     -47.956  32.489   1.098  1.00 77.38           C  
ANISOU   45  C   PHE A   8    10034   7913  11454    228  -1620    344       C  
ATOM     46  O   PHE A   8     -48.275  31.632   1.945  1.00 77.14           O  
ANISOU   46  O   PHE A   8     9943   7850  11514    207  -1669    329       O  
ATOM     47  CB  PHE A   8     -49.330  34.535   1.477  1.00 76.94           C  
ANISOU   47  CB  PHE A   8     9778   7861  11591    111  -1661    462       C  
ATOM     48  CG  PHE A   8     -50.394  35.514   1.045  1.00 77.15           C  
ANISOU   48  CG  PHE A   8     9784   7846  11681     60  -1763    525       C  
ATOM     49  CD1 PHE A   8     -50.273  36.218  -0.143  1.00 77.67           C  
ANISOU   49  CD1 PHE A   8     9976   7899  11635     71  -1780    547       C  
ATOM     50  CD2 PHE A   8     -51.499  35.759   1.848  1.00 76.56           C  
ANISOU   50  CD2 PHE A   8     9558   7752  11777      5  -1835    566       C  
ATOM     51  CE1 PHE A   8     -51.247  37.127  -0.529  1.00 78.28           C  
ANISOU   51  CE1 PHE A   8    10036   7931  11774     29  -1883    607       C  
ATOM     52  CE2 PHE A   8     -52.471  36.669   1.461  1.00 76.73           C  
ANISOU   52  CE2 PHE A   8     9553   7738  11862    -27  -1930    622       C  
ATOM     53  CZ  PHE A   8     -52.344  37.350   0.273  1.00 77.74           C  
ANISOU   53  CZ  PHE A   8     9814   7840  11882    -16  -1959    641       C  
ATOM     54  N   THR A   9     -46.702  32.702   0.674  1.00 76.63           N  
ANISOU   54  N   THR A   9     9992   7896  11226    300  -1474    316       N  
ATOM     55  CA  THR A   9     -45.480  32.076   1.253  1.00 75.50           C  
ANISOU   55  CA  THR A   9     9818   7824  11043    370  -1338    263       C  
ATOM     56  C   THR A   9     -44.492  33.178   1.656  1.00 74.10           C  
ANISOU   56  C   THR A   9     9513   7767  10873    369  -1153    296       C  
ATOM     57  O   THR A   9     -44.520  34.246   1.023  1.00 75.01           O  
ANISOU   57  O   THR A   9     9642   7907  10950    342  -1129    346       O  
ATOM     58  CB  THR A   9     -44.840  31.074   0.283  1.00 76.80           C  
ANISOU   58  CB  THR A   9    10180   7972  11026    478  -1348    191       C  
ATOM     59  OG1 THR A   9     -44.528  31.773  -0.922  1.00 78.04           O  
ANISOU   59  OG1 THR A   9    10446   8168  11037    507  -1307    210       O  
ATOM     60  CG2 THR A   9     -45.729  29.890  -0.025  1.00 77.21           C  
ANISOU   60  CG2 THR A   9    10369   7890  11073    478  -1544    153       C  
ATOM     61  N   THR A  10     -43.651  32.922   2.664  1.00 72.40           N  
ANISOU   61  N   THR A  10     9184   7618  10706    392  -1039    274       N  
ATOM     62  CA  THR A  10     -42.748  33.927   3.292  1.00 71.37           C  
ANISOU   62  CA  THR A  10     8909   7595  10613    374   -880    310       C  
ATOM     63  C   THR A  10     -41.698  33.213   4.155  1.00 70.60           C  
ANISOU   63  C   THR A  10     8738   7560  10524    428   -776    267       C  
ATOM     64  O   THR A  10     -42.031  32.150   4.702  1.00 71.85           O  
ANISOU   64  O   THR A  10     8905   7663  10731    442   -848    225       O  
ATOM     65  CB  THR A  10     -43.568  34.934   4.111  1.00 70.16           C  
ANISOU   65  CB  THR A  10     8617   7421  10618    278   -910    365       C  
ATOM     66  OG1 THR A  10     -42.724  35.997   4.553  1.00 70.27           O  
ANISOU   66  OG1 THR A  10     8523   7520  10655    257   -779    402       O  
ATOM     67  CG2 THR A  10     -44.239  34.310   5.314  1.00 69.40           C  
ANISOU   67  CG2 THR A  10     8422   7284  10660    246   -970    350       C  
ATOM     68  N   VAL A  11     -40.488  33.778   4.266  1.00 69.23           N  
ANISOU   68  N   VAL A  11     8493   7498  10311    450   -623    284       N  
ATOM     69  CA  VAL A  11     -39.399  33.301   5.178  1.00 67.97           C  
ANISOU   69  CA  VAL A  11     8234   7413  10176    494   -515    256       C  
ATOM     70  C   VAL A  11     -39.412  34.122   6.475  1.00 66.09           C  
ANISOU   70  C   VAL A  11     7821   7200  10090    410   -475    297       C  
ATOM     71  O   VAL A  11     -38.820  33.656   7.468  1.00 65.23           O  
ANISOU   71  O   VAL A  11     7622   7125  10034    427   -425    274       O  
ATOM     72  CB  VAL A  11     -38.008  33.372   4.516  1.00 68.52           C  
ANISOU   72  CB  VAL A  11     8321   7602  10110    574   -372    255       C  
ATOM     73  CG1 VAL A  11     -37.873  32.378   3.376  1.00 69.80           C  
ANISOU   73  CG1 VAL A  11     8661   7747  10110    687   -401    195       C  
ATOM     74  CG2 VAL A  11     -37.654  34.779   4.055  1.00 68.47           C  
ANISOU   74  CG2 VAL A  11     8269   7667  10076    513   -292    336       C  
ATOM     75  N   ASP A  12     -40.045  35.300   6.455  1.00 64.71           N  
ANISOU   75  N   ASP A  12     7607   7005   9973    329   -501    353       N  
ATOM     76  CA  ASP A  12     -39.909  36.358   7.495  1.00 63.10           C  
ANISOU   76  CA  ASP A  12     7257   6831   9885    258   -450    394       C  
ATOM     77  C   ASP A  12     -41.263  36.662   8.147  1.00 62.19           C  
ANISOU   77  C   ASP A  12     7097   6634   9896    198   -555    404       C  
ATOM     78  O   ASP A  12     -41.262  37.051   9.331  1.00 60.92           O  
ANISOU   78  O   ASP A  12     6817   6488   9840    163   -528    409       O  
ATOM     79  CB  ASP A  12     -39.329  37.635   6.887  1.00 62.91           C  
ANISOU   79  CB  ASP A  12     7227   6861   9814    223   -381    458       C  
ATOM     80  CG  ASP A  12     -40.143  38.148   5.713  1.00 63.12           C  
ANISOU   80  CG  ASP A  12     7367   6832   9784    203   -461    489       C  
ATOM     81  OD1 ASP A  12     -40.707  39.239   5.840  1.00 62.29           O  
ANISOU   81  OD1 ASP A  12     7229   6689   9748    139   -500    534       O  
ATOM     82  OD2 ASP A  12     -40.222  37.438   4.689  1.00 63.32           O  
ANISOU   82  OD2 ASP A  12     7520   6845   9694    258   -491    464       O  
ATOM     83  N   ASN A  13     -42.360  36.522   7.395  1.00 63.07           N  
ANISOU   83  N   ASN A  13     7298   6670   9995    191   -669    407       N  
ATOM     84  CA  ASN A  13     -43.749  36.808   7.848  1.00 63.06           C  
ANISOU   84  CA  ASN A  13     7249   6599  10109    140   -776    425       C  
ATOM     85  C   ASN A  13     -43.998  38.321   7.772  1.00 63.84           C  
ANISOU   85  C   ASN A  13     7308   6697  10251     96   -768    476       C  
ATOM     86  O   ASN A  13     -44.913  38.794   8.470  1.00 63.38           O  
ANISOU   86  O   ASN A  13     7169   6606  10304     65   -819    489       O  
ATOM     87  CB  ASN A  13     -44.002  36.259   9.256  1.00 61.59           C  
ANISOU   87  CB  ASN A  13     6949   6419  10033    126   -775    404       C  
ATOM     88  CG  ASN A  13     -45.407  35.742   9.475  1.00 60.74           C  
ANISOU   88  CG  ASN A  13     6829   6245  10003     97   -901    411       C  
ATOM     89  OD1 ASN A  13     -46.125  35.432   8.528  1.00 60.29           O  
ANISOU   89  OD1 ASN A  13     6867   6128   9910     96  -1004    418       O  
ATOM     90  ND2 ASN A  13     -45.790  35.613  10.733  1.00 59.90           N  
ANISOU   90  ND2 ASN A  13     6604   6154  10001     72   -894    412       N  
ATOM     91  N   ILE A  14     -43.197  39.037   6.972  1.00 65.21           N  
ANISOU   91  N   ILE A  14     7534   6906  10336     96   -707    506       N  
ATOM     92  CA  ILE A  14     -43.364  40.483   6.634  1.00 66.55           C  
ANISOU   92  CA  ILE A  14     7703   7059  10524     51   -716    563       C  
ATOM     93  C   ILE A  14     -43.501  40.573   5.105  1.00 69.00           C  
ANISOU   93  C   ILE A  14     8157   7346  10712     59   -763    590       C  
ATOM     94  O   ILE A  14     -44.627  40.809   4.641  1.00 69.30           O  
ANISOU   94  O   ILE A  14     8242   7309  10779     44   -880    606       O  
ATOM     95  CB  ILE A  14     -42.206  41.339   7.206  1.00 66.26           C  
ANISOU   95  CB  ILE A  14     7587   7088  10498     24   -603    589       C  
ATOM     96  CG1 ILE A  14     -42.302  41.496   8.728  1.00 65.06           C  
ANISOU   96  CG1 ILE A  14     7306   6939  10474      9   -583    566       C  
ATOM     97  CG2 ILE A  14     -42.122  42.698   6.523  1.00 66.49           C  
ANISOU   97  CG2 ILE A  14     7657   7101  10505    -23   -613    657       C  
ATOM     98  CD1 ILE A  14     -41.916  40.268   9.516  1.00 64.44           C  
ANISOU   98  CD1 ILE A  14     7176   6900  10405     44   -540    514       C  
ATOM     99  N   ASN A  15     -42.409  40.346   4.359  1.00 71.84           N  
ANISOU   99  N   ASN A  15     8583   7774  10938     86   -677    596       N  
ATOM    100  CA  ASN A  15     -42.389  40.271   2.869  1.00 74.29           C  
ANISOU  100  CA  ASN A  15     9046   8080  11099    107   -703    617       C  
ATOM    101  C   ASN A  15     -43.116  39.001   2.404  1.00 76.62           C  
ANISOU  101  C   ASN A  15     9443   8316  11351    159   -803    559       C  
ATOM    102  O   ASN A  15     -42.461  37.939   2.338  1.00 78.10           O  
ANISOU  102  O   ASN A  15     9669   8544  11462    223   -752    507       O  
ATOM    103  CB  ASN A  15     -40.965  40.277   2.299  1.00 74.27           C  
ANISOU  103  CB  ASN A  15     9070   8189  10959    135   -565    637       C  
ATOM    104  CG  ASN A  15     -40.187  41.536   2.615  1.00 74.15           C  
ANISOU  104  CG  ASN A  15     8966   8230  10976     69   -480    710       C  
ATOM    105  OD1 ASN A  15     -40.204  42.013   3.746  1.00 72.54           O  
ANISOU  105  OD1 ASN A  15     8643   8014  10903     29   -472    712       O  
ATOM    106  ND2 ASN A  15     -39.482  42.068   1.629  1.00 75.79           N  
ANISOU  106  ND2 ASN A  15     9234   8502  11059     55   -417    773       N  
ATOM    107  N   LEU A  16     -44.411  39.106   2.079  1.00 78.31           N  
ANISOU  107  N   LEU A  16     9704   8436  11614    132   -947    569       N  
ATOM    108  CA  LEU A  16     -45.232  37.987   1.532  1.00 80.03           C  
ANISOU  108  CA  LEU A  16    10032   8580  11795    162  -1075    528       C  
ATOM    109  C   LEU A  16     -44.890  37.778   0.052  1.00 82.03           C  
ANISOU  109  C   LEU A  16    10470   8837  11859    204  -1085    527       C  
ATOM    110  O   LEU A  16     -44.313  38.705  -0.554  1.00 84.57           O  
ANISOU  110  O   LEU A  16    10819   9209  12103    190  -1015    579       O  
ATOM    111  CB  LEU A  16     -46.722  38.306   1.684  1.00 80.72           C  
ANISOU  111  CB  LEU A  16    10088   8576  12006    112  -1227    555       C  
ATOM    112  CG  LEU A  16     -47.213  38.672   3.085  1.00 80.25           C  
ANISOU  112  CG  LEU A  16     9846   8517  12125     76  -1218    562       C  
ATOM    113  CD1 LEU A  16     -48.734  38.639   3.133  1.00 79.66           C  
ANISOU  113  CD1 LEU A  16     9746   8364  12158     43  -1375    582       C  
ATOM    114  CD2 LEU A  16     -46.625  37.750   4.146  1.00 79.69           C  
ANISOU  114  CD2 LEU A  16     9694   8492  12089     98  -1140    513       C  
ATOM    115  N   HIS A  17     -45.235  36.607  -0.501  1.00 82.46           N  
ANISOU  115  N   HIS A  17    10652   8838  11839    252  -1176    475       N  
ATOM    116  CA  HIS A  17     -45.043  36.235  -1.932  1.00 83.34           C  
ANISOU  116  CA  HIS A  17    10967   8939  11757    306  -1209    459       C  
ATOM    117  C   HIS A  17     -46.243  35.407  -2.411  1.00 83.73           C  
ANISOU  117  C   HIS A  17    11138   8865  11811    303  -1408    430       C  
ATOM    118  O   HIS A  17     -46.329  34.220  -2.036  1.00 83.15           O  
ANISOU  118  O   HIS A  17    11086   8753  11753    338  -1456    369       O  
ATOM    119  CB  HIS A  17     -43.699  35.518  -2.130  1.00 83.06           C  
ANISOU  119  CB  HIS A  17    10981   8998  11580    403  -1067    406       C  
ATOM    120  CG  HIS A  17     -42.528  36.368  -1.771  1.00 82.54           C  
ANISOU  120  CG  HIS A  17    10795   9059  11506    395   -882    449       C  
ATOM    121  ND1 HIS A  17     -41.804  37.065  -2.715  1.00 83.78           N  
ANISOU  121  ND1 HIS A  17    11014   9299  11519    405   -790    499       N  
ATOM    122  CD2 HIS A  17     -41.973  36.662  -0.575  1.00 81.57           C  
ANISOU  122  CD2 HIS A  17    10494   8994  11503    369   -782    459       C  
ATOM    123  CE1 HIS A  17     -40.841  37.739  -2.118  1.00 83.74           C  
ANISOU  123  CE1 HIS A  17    10868   9397  11551    380   -644    542       C  
ATOM    124  NE2 HIS A  17     -40.929  37.514  -0.803  1.00 82.20           N  
ANISOU  124  NE2 HIS A  17    10528   9184  11518    359   -640    515       N  
ATOM    125  N   THR A  18     -47.127  36.029  -3.203  1.00 84.73           N  
ANISOU  125  N   THR A  18    11338   8927  11927    257  -1530    479       N  
ATOM    126  CA  THR A  18     -48.416  35.462  -3.689  1.00 85.64           C  
ANISOU  126  CA  THR A  18    11552   8918  12067    231  -1744    474       C  
ATOM    127  C   THR A  18     -48.153  34.291  -4.641  1.00 86.46           C  
ANISOU  127  C   THR A  18    11874   8982  11991    308  -1803    404       C  
ATOM    128  O   THR A  18     -47.371  34.469  -5.597  1.00 87.97           O  
ANISOU  128  O   THR A  18    12198   9227  11997    368  -1724    396       O  
ATOM    129  CB  THR A  18     -49.261  36.519  -4.412  1.00 86.88           C  
ANISOU  129  CB  THR A  18    11745   9027  12238    173  -1849    547       C  
ATOM    130  OG1 THR A  18     -49.526  37.599  -3.516  1.00 86.32           O  
ANISOU  130  OG1 THR A  18    11482   8981  12332    116  -1803    602       O  
ATOM    131  CG2 THR A  18     -50.568  35.965  -4.936  1.00 88.15           C  
ANISOU  131  CG2 THR A  18    11999   9064  12428    142  -2077    550       C  
ATOM    132  N   GLN A  19     -48.797  33.148  -4.392  1.00 85.18           N  
ANISOU  132  N   GLN A  19    11753   8731  11881    307  -1941    361       N  
ATOM    133  CA  GLN A  19     -48.742  31.946  -5.264  1.00 85.82           C  
ANISOU  133  CA  GLN A  19    12062   8740  11806    378  -2044    288       C  
ATOM    134  C   GLN A  19     -50.170  31.424  -5.459  1.00 86.20           C  
ANISOU  134  C   GLN A  19    12168   8645  11938    307  -2296    305       C  
ATOM    135  O   GLN A  19     -51.060  31.840  -4.691  1.00 84.60           O  
ANISOU  135  O   GLN A  19    11792   8423  11929    214  -2356    366       O  
ATOM    136  CB  GLN A  19     -47.838  30.875  -4.648  1.00 85.16           C  
ANISOU  136  CB  GLN A  19    11975   8688  11695    459  -1953    207       C  
ATOM    137  CG  GLN A  19     -46.439  31.361  -4.279  1.00 83.58           C  
ANISOU  137  CG  GLN A  19    11676   8637  11443    521  -1706    200       C  
ATOM    138  CD  GLN A  19     -45.514  31.502  -5.463  1.00 84.13           C  
ANISOU  138  CD  GLN A  19    11907   8779  11279    619  -1607    175       C  
ATOM    139  OE1 GLN A  19     -45.451  30.640  -6.339  1.00 85.15           O  
ANISOU  139  OE1 GLN A  19    12247   8856  11250    703  -1681    108       O  
ATOM    140  NE2 GLN A  19     -44.760  32.588  -5.483  1.00 83.35           N  
ANISOU  140  NE2 GLN A  19    11712   8803  11153    610  -1436    230       N  
ATOM    141  N   VAL A  20     -50.373  30.565  -6.461  1.00 87.85           N  
ANISOU  141  N   VAL A  20    12612   8761  12004    351  -2439    254       N  
ATOM    142  CA  VAL A  20     -51.655  29.840  -6.715  1.00 89.10           C  
ANISOU  142  CA  VAL A  20    12856   8771  12228    284  -2703    264       C  
ATOM    143  C   VAL A  20     -51.326  28.344  -6.812  1.00 90.45           C  
ANISOU  143  C   VAL A  20    13193   8864  12309    354  -2777    169       C  
ATOM    144  O   VAL A  20     -50.827  27.909  -7.867  1.00 91.49           O  
ANISOU  144  O   VAL A  20    13562   8968  12228    452  -2795    101       O  
ATOM    145  CB  VAL A  20     -52.393  30.387  -7.956  1.00 90.33           C  
ANISOU  145  CB  VAL A  20    13159   8862  12300    253  -2851    305       C  
ATOM    146  CG1 VAL A  20     -51.457  30.673  -9.122  1.00 91.37           C  
ANISOU  146  CG1 VAL A  20    13489   9047  12179    355  -2750    265       C  
ATOM    147  CG2 VAL A  20     -53.534  29.482  -8.394  1.00 91.45           C  
ANISOU  147  CG2 VAL A  20    13433   8845  12467    199  -3133    303       C  
ATOM    148  N   VAL A  21     -51.588  27.598  -5.732  1.00 90.99           N  
ANISOU  148  N   VAL A  21    13144   8898  12529    310  -2818    167       N  
ATOM    149  CA  VAL A  21     -51.036  26.228  -5.492  1.00 92.44           C  
ANISOU  149  CA  VAL A  21    13440   9026  12655    384  -2843     77       C  
ATOM    150  C   VAL A  21     -51.910  25.176  -6.189  1.00 95.00           C  
ANISOU  150  C   VAL A  21    13981   9173  12938    357  -3124     52       C  
ATOM    151  O   VAL A  21     -53.147  25.223  -6.040  1.00 95.33           O  
ANISOU  151  O   VAL A  21    13956   9139  13125    227  -3305    130       O  
ATOM    152  CB  VAL A  21     -50.868  25.921  -3.988  1.00 90.81           C  
ANISOU  152  CB  VAL A  21    13014   8864  12625    343  -2759     93       C  
ATOM    153  CG1 VAL A  21     -49.658  26.633  -3.412  1.00 89.65           C  
ANISOU  153  CG1 VAL A  21    12722   8878  12462    410  -2484     81       C  
ATOM    154  CG2 VAL A  21     -52.111  26.239  -3.169  1.00 89.76           C  
ANISOU  154  CG2 VAL A  21    12677   8707  12719    191  -2863    195       C  
ATOM    155  N   ASP A  22     -51.259  24.267  -6.923  1.00 97.16           N  
ANISOU  155  N   ASP A  22    14507   9388  13019    481  -3157    -52       N  
ATOM    156  CA  ASP A  22     -51.855  23.066  -7.570  1.00 99.26           C  
ANISOU  156  CA  ASP A  22    15026   9470  13218    482  -3424   -102       C  
ATOM    157  C   ASP A  22     -52.328  22.100  -6.473  1.00100.20           C  
ANISOU  157  C   ASP A  22    15050   9504  13517    397  -3543    -83       C  
ATOM    158  O   ASP A  22     -51.467  21.593  -5.722  1.00 99.48           O  
ANISOU  158  O   ASP A  22    14907   9456  13433    468  -3414   -134       O  
ATOM    159  CB  ASP A  22     -50.835  22.428  -8.518  1.00 99.87           C  
ANISOU  159  CB  ASP A  22    15383   9532  13032    668  -3381   -232       C  
ATOM    160  CG  ASP A  22     -51.378  21.293  -9.366  1.00101.18           C  
ANISOU  160  CG  ASP A  22    15854   9501  13089    690  -3659   -298       C  
ATOM    161  OD1 ASP A  22     -52.580  21.322  -9.691  1.00101.12           O  
ANISOU  161  OD1 ASP A  22    15881   9381  13159    561  -3889   -232       O  
ATOM    162  OD2 ASP A  22     -50.589  20.393  -9.699  1.00101.70           O  
ANISOU  162  OD2 ASP A  22    16122   9525  12993    841  -3649   -416       O  
ATOM    163  N   MET A  23     -53.644  21.864  -6.389  1.00102.08           N  
ANISOU  163  N   MET A  23    15260   9629  13896    246  -3781     -3       N  
ATOM    164  CA  MET A  23     -54.311  21.059  -5.325  1.00102.56           C  
ANISOU  164  CA  MET A  23    15198   9617  14153    125  -3912     52       C  
ATOM    165  C   MET A  23     -53.816  19.607  -5.370  1.00103.75           C  
ANISOU  165  C   MET A  23    15570   9638  14212    204  -4020    -47       C  
ATOM    166  O   MET A  23     -53.572  19.042  -4.291  1.00103.84           O  
ANISOU  166  O   MET A  23    15465   9657  14331    181  -3978    -40       O  
ATOM    167  CB  MET A  23     -55.836  21.061  -5.492  1.00104.07           C  
ANISOU  167  CB  MET A  23    15350   9709  14482    -45  -4170    160       C  
ATOM    168  CG  MET A  23     -56.484  22.422  -5.298  1.00103.61           C  
ANISOU  168  CG  MET A  23    15050   9766  14549   -130  -4091    267       C  
ATOM    169  SD  MET A  23     -56.923  22.785  -3.576  1.00103.74           S  
ANISOU  169  SD  MET A  23    14679   9900  14837   -250  -3976    378       S  
ATOM    170  CE  MET A  23     -58.484  21.918  -3.425  1.00104.26           C  
ANISOU  170  CE  MET A  23    14719   9824  15068   -435  -4306    485       C  
ATOM    171  N   SER A  24     -53.702  19.027  -6.570  1.00105.29           N  
ANISOU  171  N   SER A  24    16080   9711  14213    294  -4164   -136       N  
ATOM    172  CA  SER A  24     -53.271  17.623  -6.807  1.00106.64           C  
ANISOU  172  CA  SER A  24    16515   9732  14271    390  -4300   -246       C  
ATOM    173  C   SER A  24     -51.951  17.356  -6.076  1.00105.73           C  
ANISOU  173  C   SER A  24    16337   9715  14118    529  -4063   -325       C  
ATOM    174  O   SER A  24     -51.947  16.518  -5.155  1.00106.89           O  
ANISOU  174  O   SER A  24    16432   9801  14378    488  -4121   -318       O  
ATOM    175  CB  SER A  24     -53.146  17.334  -8.280  1.00108.66           C  
ANISOU  175  CB  SER A  24    17112   9886  14285    506  -4422   -345       C  
ATOM    176  OG  SER A  24     -52.194  18.197  -8.885  1.00108.74           O  
ANISOU  176  OG  SER A  24    17140  10052  14122    654  -4172   -400       O  
ATOM    177  N   MET A  25     -50.886  18.065  -6.461  1.00104.05           N  
ANISOU  177  N   MET A  25    16120   9654  13758    679  -3809   -386       N  
ATOM    178  CA  MET A  25     -49.516  17.898  -5.905  1.00102.38           C  
ANISOU  178  CA  MET A  25    15853   9557  13490    830  -3568   -463       C  
ATOM    179  C   MET A  25     -49.517  18.355  -4.444  1.00 99.13           C  
ANISOU  179  C   MET A  25    15106   9256  13302    720  -3427   -370       C  
ATOM    180  O   MET A  25     -50.379  19.180  -4.088  1.00 98.68           O  
ANISOU  180  O   MET A  25    14854   9244  13395    566  -3438   -255       O  
ATOM    181  CB  MET A  25     -48.495  18.735  -6.684  1.00103.08           C  
ANISOU  181  CB  MET A  25    15975   9803  13384    985  -3328   -517       C  
ATOM    182  CG  MET A  25     -48.430  18.423  -8.169  1.00105.79           C  
ANISOU  182  CG  MET A  25    16646  10067  13481   1106  -3433   -608       C  
ATOM    183  SD  MET A  25     -47.578  19.721  -9.107  1.00106.32           S  
ANISOU  183  SD  MET A  25    16704  10341  13351   1219  -3164   -615       S  
ATOM    184  CE  MET A  25     -46.015  18.918  -9.460  1.00107.59           C  
ANISOU  184  CE  MET A  25    17037  10563  13277   1493  -3000   -773       C  
ATOM    185  N   THR A  26     -48.579  17.852  -3.636  1.00 97.45           N  
ANISOU  185  N   THR A  26    14833   9089  13103    806  -3299   -420       N  
ATOM    186  CA  THR A  26     -48.307  18.354  -2.262  1.00 94.65           C  
ANISOU  186  CA  THR A  26    14170   8866  12924    736  -3121   -348       C  
ATOM    187  C   THR A  26     -47.799  19.795  -2.373  1.00 92.22           C  
ANISOU  187  C   THR A  26    13694   8753  12590    758  -2870   -314       C  
ATOM    188  O   THR A  26     -47.586  20.255  -3.512  1.00 92.56           O  
ANISOU  188  O   THR A  26    13873   8824  12471    837  -2837   -350       O  
ATOM    189  CB  THR A  26     -47.291  17.481  -1.510  1.00 95.16           C  
ANISOU  189  CB  THR A  26    14238   8934  12981    845  -3043   -420       C  
ATOM    190  OG1 THR A  26     -46.013  17.621  -2.135  1.00 96.57           O  
ANISOU  190  OG1 THR A  26    14510   9211  12971   1047  -2857   -522       O  
ATOM    191  CG2 THR A  26     -47.674  16.017  -1.466  1.00 96.83           C  
ANISOU  191  CG2 THR A  26    14649   8941  13201    839  -3296   -463       C  
ATOM    192  N   TYR A  27     -47.612  20.477  -1.242  1.00 89.68           N  
ANISOU  192  N   TYR A  27    13099   8557  12417    690  -2708   -246       N  
ATOM    193  CA  TYR A  27     -46.913  21.788  -1.169  1.00 87.99           C  
ANISOU  193  CA  TYR A  27    12717   8528  12185    720  -2456   -219       C  
ATOM    194  C   TYR A  27     -45.425  21.564  -1.464  1.00 87.05           C  
ANISOU  194  C   TYR A  27    12675   8497  11902    908  -2277   -316       C  
ATOM    195  O   TYR A  27     -44.819  22.383  -2.183  1.00 86.73           O  
ANISOU  195  O   TYR A  27    12645   8568  11738    979  -2128   -325       O  
ATOM    196  CB  TYR A  27     -47.140  22.457   0.189  1.00 86.71           C  
ANISOU  196  CB  TYR A  27    12262   8456  12226    601  -2356   -128       C  
ATOM    197  CG  TYR A  27     -48.487  23.115   0.348  1.00 86.50           C  
ANISOU  197  CG  TYR A  27    12119   8404  12343    438  -2465    -24       C  
ATOM    198  CD1 TYR A  27     -49.486  22.524   1.102  1.00 86.72           C  
ANISOU  198  CD1 TYR A  27    12075   8347  12527    313  -2624     35       C  
ATOM    199  CD2 TYR A  27     -48.767  24.331  -0.256  1.00 86.37           C  
ANISOU  199  CD2 TYR A  27    12058   8451  12304    411  -2411     21       C  
ATOM    200  CE1 TYR A  27     -50.726  23.123   1.255  1.00 86.62           C  
ANISOU  200  CE1 TYR A  27    11938   8326  12647    174  -2717    135       C  
ATOM    201  CE2 TYR A  27     -50.001  24.944  -0.113  1.00 86.12           C  
ANISOU  201  CE2 TYR A  27    11916   8399  12407    277  -2512    114       C  
ATOM    202  CZ  TYR A  27     -50.986  24.337   0.646  1.00 85.89           C  
ANISOU  202  CZ  TYR A  27    11803   8296  12534    163  -2661    170       C  
ATOM    203  OH  TYR A  27     -52.205  24.930   0.795  1.00 85.50           O  
ANISOU  203  OH  TYR A  27    11626   8240  12618     40  -2755    265       O  
ATOM    204  N   GLY A  28     -44.869  20.476  -0.920  1.00 86.53           N  
ANISOU  204  N   GLY A  28    12654   8382  11837    984  -2295   -381       N  
ATOM    205  CA  GLY A  28     -43.516  19.977  -1.226  1.00 86.93           C  
ANISOU  205  CA  GLY A  28    12806   8492  11731   1184  -2164   -487       C  
ATOM    206  C   GLY A  28     -43.267  19.970  -2.721  1.00 88.35           C  
ANISOU  206  C   GLY A  28    13221   8663  11682   1313  -2174   -558       C  
ATOM    207  O   GLY A  28     -42.491  20.821  -3.190  1.00 88.37           O  
ANISOU  207  O   GLY A  28    13173   8822  11581   1385  -1975   -556       O  
ATOM    208  N   GLN A  29     -43.941  19.072  -3.446  1.00 89.60           N  
ANISOU  208  N   GLN A  29    13631   8645  11767   1330  -2406   -611       N  
ATOM    209  CA  GLN A  29     -43.864  18.945  -4.927  1.00 91.78           C  
ANISOU  209  CA  GLN A  29    14176   8884  11812   1450  -2458   -686       C  
ATOM    210  C   GLN A  29     -43.688  20.326  -5.575  1.00 91.41           C  
ANISOU  210  C   GLN A  29    14045   8994  11689   1434  -2290   -628       C  
ATOM    211  O   GLN A  29     -42.854  20.440  -6.493  1.00 92.89           O  
ANISOU  211  O   GLN A  29    14356   9269  11666   1591  -2167   -692       O  
ATOM    212  CB  GLN A  29     -45.126  18.275  -5.474  1.00 93.22           C  
ANISOU  212  CB  GLN A  29    14566   8851  12000   1364  -2767   -688       C  
ATOM    213  CG  GLN A  29     -45.089  16.753  -5.446  1.00 95.07           C  
ANISOU  213  CG  GLN A  29    15021   8906  12195   1450  -2957   -788       C  
ATOM    214  CD  GLN A  29     -45.963  16.141  -6.516  1.00 97.00           C  
ANISOU  214  CD  GLN A  29    15563   8958  12334   1441  -3232   -829       C  
ATOM    215  OE1 GLN A  29     -47.016  15.572  -6.237  1.00 97.16           O  
ANISOU  215  OE1 GLN A  29    15624   8810  12480   1297  -3481   -783       O  
ATOM    216  NE2 GLN A  29     -45.534  16.267  -7.762  1.00 98.31           N  
ANISOU  216  NE2 GLN A  29    15940   9151  12261   1591  -3191   -910       N  
ATOM    217  N   GLN A  30     -44.448  21.327  -5.119  1.00 89.68           N  
ANISOU  217  N   GLN A  30    13629   8812  11633   1254  -2286   -509       N  
ATOM    218  CA  GLN A  30     -44.510  22.682  -5.731  1.00 89.22           C  
ANISOU  218  CA  GLN A  30    13502   8869  11527   1208  -2174   -438       C  
ATOM    219  C   GLN A  30     -43.368  23.553  -5.197  1.00 88.03           C  
ANISOU  219  C   GLN A  30    13134   8923  11389   1247  -1889   -407       C  
ATOM    220  O   GLN A  30     -42.461  23.880  -5.990  1.00 89.21           O  
ANISOU  220  O   GLN A  30    13352   9189  11354   1368  -1736   -438       O  
ATOM    221  CB  GLN A  30     -45.873  23.314  -5.457  1.00 88.62           C  
ANISOU  221  CB  GLN A  30    13317   8725  11626   1010  -2317   -330       C  
ATOM    222  CG  GLN A  30     -47.021  22.553  -6.101  1.00 90.20           C  
ANISOU  222  CG  GLN A  30    13728   8731  11810    959  -2607   -345       C  
ATOM    223  CD  GLN A  30     -48.365  23.028  -5.610  1.00 89.74           C  
ANISOU  223  CD  GLN A  30    13522   8614  11959    763  -2749   -233       C  
ATOM    224  OE1 GLN A  30     -48.998  23.883  -6.221  1.00 90.05           O  
ANISOU  224  OE1 GLN A  30    13561   8661  11993    695  -2792   -172       O  
ATOM    225  NE2 GLN A  30     -48.805  22.482  -4.488  1.00 89.59           N  
ANISOU  225  NE2 GLN A  30    13372   8543  12125    674  -2821   -201       N  
ATOM    226  N   PHE A  31     -43.414  23.912  -3.909  1.00 85.82           N  
ANISOU  226  N   PHE A  31    12605   8689  11312   1144  -1824   -343       N  
ATOM    227  CA  PHE A  31     -42.455  24.836  -3.246  1.00 84.16           C  
ANISOU  227  CA  PHE A  31    12165   8659  11150   1146  -1578   -297       C  
ATOM    228  C   PHE A  31     -41.284  24.055  -2.644  1.00 83.96           C  
ANISOU  228  C   PHE A  31    12105   8692  11102   1275  -1461   -368       C  
ATOM    229  O   PHE A  31     -40.127  24.490  -2.805  1.00 85.07           O  
ANISOU  229  O   PHE A  31    12182   8988  11150   1369  -1256   -375       O  
ATOM    230  CB  PHE A  31     -43.146  25.649  -2.148  1.00 82.15           C  
ANISOU  230  CB  PHE A  31    11671   8416  11123    974  -1579   -196       C  
ATOM    231  CG  PHE A  31     -44.372  26.401  -2.599  1.00 82.00           C  
ANISOU  231  CG  PHE A  31    11661   8336  11157    847  -1705   -122       C  
ATOM    232  CD1 PHE A  31     -44.422  26.999  -3.851  1.00 82.80           C  
ANISOU  232  CD1 PHE A  31    11894   8457  11108    873  -1705   -112       C  
ATOM    233  CD2 PHE A  31     -45.470  26.526  -1.763  1.00 80.93           C  
ANISOU  233  CD2 PHE A  31    11395   8132  11220    706  -1822    -58       C  
ATOM    234  CE1 PHE A  31     -45.551  27.689  -4.262  1.00 82.60           C  
ANISOU  234  CE1 PHE A  31    11876   8370  11137    760  -1831    -42       C  
ATOM    235  CE2 PHE A  31     -46.597  27.222  -2.174  1.00 80.80           C  
ANISOU  235  CE2 PHE A  31    11375   8065  11259    600  -1938     10       C  
ATOM    236  CZ  PHE A  31     -46.634  27.802  -3.421  1.00 81.72           C  
ANISOU  236  CZ  PHE A  31    11628   8190  11232    628  -1948     17       C  
ATOM    237  N   GLY A  32     -41.585  22.941  -1.973  1.00 82.90           N  
ANISOU  237  N   GLY A  32    12006   8437  11052   1275  -1593   -412       N  
ATOM    238  CA  GLY A  32     -40.644  22.216  -1.100  1.00 82.22           C  
ANISOU  238  CA  GLY A  32    11849   8388  11001   1366  -1509   -463       C  
ATOM    239  C   GLY A  32     -41.076  22.369   0.353  1.00 80.04           C  
ANISOU  239  C   GLY A  32    11356   8101  10955   1220  -1525   -391       C  
ATOM    240  O   GLY A  32     -42.245  22.646   0.610  1.00 79.62           O  
ANISOU  240  O   GLY A  32    11258   7970  11021   1069  -1652   -324       O  
ATOM    241  N   PRO A  33     -40.168  22.217   1.343  1.00 78.86           N  
ANISOU  241  N   PRO A  33    11059   8034  10870   1261  -1397   -399       N  
ATOM    242  CA  PRO A  33     -40.554  22.332   2.750  1.00 77.09           C  
ANISOU  242  CA  PRO A  33    10639   7802  10849   1129  -1411   -334       C  
ATOM    243  C   PRO A  33     -41.478  23.540   2.990  1.00 75.13           C  
ANISOU  243  C   PRO A  33    10247   7582  10716    961  -1411   -231       C  
ATOM    244  O   PRO A  33     -41.029  24.658   2.799  1.00 74.91           O  
ANISOU  244  O   PRO A  33    10119   7677  10663    955  -1261   -193       O  
ATOM    245  CB  PRO A  33     -39.217  22.445   3.512  1.00 76.78           C  
ANISOU  245  CB  PRO A  33    10449   7899  10823   1208  -1218   -348       C  
ATOM    246  CG  PRO A  33     -38.125  22.480   2.446  1.00 77.81           C  
ANISOU  246  CG  PRO A  33    10678   8127  10759   1381  -1089   -411       C  
ATOM    247  CD  PRO A  33     -38.737  21.930   1.175  1.00 79.28           C  
ANISOU  247  CD  PRO A  33    11121   8197  10804   1438  -1235   -467       C  
ATOM    248  N   THR A  34     -42.740  23.277   3.368  1.00 73.54           N  
ANISOU  248  N   THR A  34    10041   7266  10632    834  -1584   -187       N  
ATOM    249  CA  THR A  34     -43.825  24.278   3.595  1.00 71.06           C  
ANISOU  249  CA  THR A  34     9602   6959  10438    681  -1619    -93       C  
ATOM    250  C   THR A  34     -44.387  24.106   5.014  1.00 69.37           C  
ANISOU  250  C   THR A  34     9218   6729  10409    567  -1656    -37       C  
ATOM    251  O   THR A  34     -44.571  22.947   5.430  1.00 69.60           O  
ANISOU  251  O   THR A  34     9309   6665  10470    565  -1773    -59       O  
ATOM    252  CB  THR A  34     -44.919  24.138   2.528  1.00 71.31           C  
ANISOU  252  CB  THR A  34     9795   6875  10421    641  -1803    -85       C  
ATOM    253  OG1 THR A  34     -44.299  24.230   1.246  1.00 71.77           O  
ANISOU  253  OG1 THR A  34    10024   6955  10289    760  -1759   -143       O  
ATOM    254  CG2 THR A  34     -45.997  25.193   2.631  1.00 70.77           C  
ANISOU  254  CG2 THR A  34     9604   6819  10465    506  -1840      7       C  
ATOM    255  N   TYR A  35     -44.667  25.213   5.715  1.00 67.88           N  
ANISOU  255  N   TYR A  35     8833   6625  10332    477  -1568     34       N  
ATOM    256  CA  TYR A  35     -45.038  25.236   7.157  1.00 66.76           C  
ANISOU  256  CA  TYR A  35     8508   6506  10351    383  -1557     88       C  
ATOM    257  C   TYR A  35     -46.228  26.173   7.413  1.00 66.34           C  
ANISOU  257  C   TYR A  35     8327   6464  10413    262  -1595    171       C  
ATOM    258  O   TYR A  35     -46.062  27.407   7.348  1.00 65.71           O  
ANISOU  258  O   TYR A  35     8157   6468  10339    255  -1483    197       O  
ATOM    259  CB  TYR A  35     -43.836  25.656   8.005  1.00 65.99           C  
ANISOU  259  CB  TYR A  35     8278   6527  10265    430  -1367     74       C  
ATOM    260  CG  TYR A  35     -42.654  24.721   7.934  1.00 66.65           C  
ANISOU  260  CG  TYR A  35     8451   6612  10257    554  -1323     -1       C  
ATOM    261  CD1 TYR A  35     -42.565  23.618   8.770  1.00 66.62           C  
ANISOU  261  CD1 TYR A  35     8453   6553  10306    555  -1388    -18       C  
ATOM    262  CD2 TYR A  35     -41.618  24.938   7.037  1.00 67.00           C  
ANISOU  262  CD2 TYR A  35     8573   6720  10162    673  -1217    -52       C  
ATOM    263  CE1 TYR A  35     -41.483  22.755   8.716  1.00 67.31           C  
ANISOU  263  CE1 TYR A  35     8623   6637  10313    681  -1355    -91       C  
ATOM    264  CE2 TYR A  35     -40.529  24.084   6.969  1.00 67.49           C  
ANISOU  264  CE2 TYR A  35     8708   6794  10140    804  -1171   -125       C  
ATOM    265  CZ  TYR A  35     -40.460  22.989   7.813  1.00 67.70           C  
ANISOU  265  CZ  TYR A  35     8742   6755  10226    813  -1243   -148       C  
ATOM    266  OH  TYR A  35     -39.394  22.139   7.760  1.00 68.49           O  
ANISOU  266  OH  TYR A  35     8914   6861  10248    952  -1206   -222       O  
ATOM    267  N   LEU A  36     -47.390  25.591   7.729  1.00 67.15           N  
ANISOU  267  N   LEU A  36     8419   6486  10608    169  -1752    217       N  
ATOM    268  CA  LEU A  36     -48.624  26.316   8.138  1.00 67.10           C  
ANISOU  268  CA  LEU A  36     8268   6496  10729     56  -1798    303       C  
ATOM    269  C   LEU A  36     -48.514  26.685   9.620  1.00 65.85           C  
ANISOU  269  C   LEU A  36     7906   6429  10684     13  -1685    339       C  
ATOM    270  O   LEU A  36     -49.184  26.032  10.445  1.00 65.34           O  
ANISOU  270  O   LEU A  36     7773   6341  10713    -62  -1762    385       O  
ATOM    271  CB  LEU A  36     -49.850  25.431   7.876  1.00 68.44           C  
ANISOU  271  CB  LEU A  36     8504   6552  10949    -26  -2015    344       C  
ATOM    272  CG  LEU A  36     -51.195  25.985   8.353  1.00 68.46           C  
ANISOU  272  CG  LEU A  36     8343   6576  11092   -141  -2077    441       C  
ATOM    273  CD1 LEU A  36     -51.420  27.407   7.856  1.00 68.15           C  
ANISOU  273  CD1 LEU A  36     8244   6596  11052   -129  -2007    458       C  
ATOM    274  CD2 LEU A  36     -52.336  25.080   7.916  1.00 69.77           C  
ANISOU  274  CD2 LEU A  36     8586   6626  11296   -226  -2305    487       C  
ATOM    275  N   ASP A  37     -47.696  27.692   9.937  1.00 65.24           N  
ANISOU  275  N   ASP A  37     7741   6451  10593     56  -1514    324       N  
ATOM    276  CA  ASP A  37     -47.496  28.202  11.321  1.00 64.60           C  
ANISOU  276  CA  ASP A  37     7479   6460  10604     26  -1398    350       C  
ATOM    277  C   ASP A  37     -47.080  27.028  12.219  1.00 65.21           C  
ANISOU  277  C   ASP A  37     7553   6521  10700     25  -1411    336       C  
ATOM    278  O   ASP A  37     -47.845  26.679  13.141  1.00 65.56           O  
ANISOU  278  O   ASP A  37     7502   6566  10842    -54  -1461    389       O  
ATOM    279  CB  ASP A  37     -48.753  28.915  11.830  1.00 64.03           C  
ANISOU  279  CB  ASP A  37     7265   6412  10649    -57  -1431    423       C  
ATOM    280  CG  ASP A  37     -48.553  29.670  13.133  1.00 62.60           C  
ANISOU  280  CG  ASP A  37     6912   6328  10543    -72  -1302    441       C  
ATOM    281  OD1 ASP A  37     -47.827  30.684  13.117  1.00 61.21           O  
ANISOU  281  OD1 ASP A  37     6708   6208  10339    -29  -1184    418       O  
ATOM    282  OD2 ASP A  37     -49.124  29.235  14.156  1.00 62.68           O  
ANISOU  282  OD2 ASP A  37     6822   6357  10634   -128  -1325    481       O  
ATOM    283  N   GLY A  38     -45.918  26.431  11.935  1.00 66.06           N  
ANISOU  283  N   GLY A  38     7764   6619  10717    113  -1369    270       N  
ATOM    284  CA  GLY A  38     -45.323  25.342  12.734  1.00 66.26           C  
ANISOU  284  CA  GLY A  38     7800   6626  10748    132  -1375    247       C  
ATOM    285  C   GLY A  38     -45.576  23.982  12.111  1.00 67.32           C  
ANISOU  285  C   GLY A  38     8107   6634  10836    148  -1538    221       C  
ATOM    286  O   GLY A  38     -44.622  23.185  12.031  1.00 68.19           O  
ANISOU  286  O   GLY A  38     8312   6718  10877    237  -1528    159       O  
ATOM    287  N   ALA A  39     -46.817  23.724  11.689  1.00 68.07           N  
ANISOU  287  N   ALA A  39     8241   6651  10969     68  -1691    267       N  
ATOM    288  CA  ALA A  39     -47.256  22.457  11.058  1.00 69.19           C  
ANISOU  288  CA  ALA A  39     8559   6653  11077     61  -1883    252       C  
ATOM    289  C   ALA A  39     -46.469  22.240   9.761  1.00 69.45           C  
ANISOU  289  C   ALA A  39     8789   6642  10958    192  -1884    160       C  
ATOM    290  O   ALA A  39     -46.564  23.102   8.871  1.00 69.49           O  
ANISOU  290  O   ALA A  39     8817   6677  10907    215  -1846    153       O  
ATOM    291  CB  ALA A  39     -48.744  22.494  10.803  1.00 69.54           C  
ANISOU  291  CB  ALA A  39     8582   6643  11196    -57  -2035    331       C  
ATOM    292  N   ASP A  40     -45.712  21.143   9.673  1.00 69.45           N  
ANISOU  292  N   ASP A  40     8924   6576  10888    279  -1924     92       N  
ATOM    293  CA  ASP A  40     -44.979  20.735   8.445  1.00 70.82           C  
ANISOU  293  CA  ASP A  40     9303   6700  10903    421  -1937     -3       C  
ATOM    294  C   ASP A  40     -45.988  20.126   7.460  1.00 72.61           C  
ANISOU  294  C   ASP A  40     9710   6781  11094    384  -2154     -3       C  
ATOM    295  O   ASP A  40     -46.398  18.966   7.676  1.00 72.51           O  
ANISOU  295  O   ASP A  40     9795   6643  11113    347  -2325      0       O  
ATOM    296  CB  ASP A  40     -43.830  19.778   8.781  1.00 70.76           C  
ANISOU  296  CB  ASP A  40     9368   6675  10841    541  -1904    -78       C  
ATOM    297  CG  ASP A  40     -42.904  19.495   7.611  1.00 71.54           C  
ANISOU  297  CG  ASP A  40     9649   6764  10768    715  -1869   -183       C  
ATOM    298  OD1 ASP A  40     -43.392  19.509   6.466  1.00 71.94           O  
ANISOU  298  OD1 ASP A  40     9847   6751  10733    732  -1959   -204       O  
ATOM    299  OD2 ASP A  40     -41.697  19.269   7.854  1.00 71.54           O  
ANISOU  299  OD2 ASP A  40     9639   6826  10718    837  -1751   -240       O  
ATOM    300  N   VAL A  41     -46.363  20.884   6.421  1.00 73.64           N  
ANISOU  300  N   VAL A  41     9890   6924  11163    387  -2156     -1       N  
ATOM    301  CA  VAL A  41     -47.397  20.501   5.408  1.00 75.44           C  
ANISOU  301  CA  VAL A  41    10282   7022  11358    341  -2365      7       C  
ATOM    302  C   VAL A  41     -46.702  20.086   4.100  1.00 78.14           C  
ANISOU  302  C   VAL A  41    10871   7310  11506    495  -2386    -99       C  
ATOM    303  O   VAL A  41     -47.367  20.128   3.044  1.00 79.40           O  
ANISOU  303  O   VAL A  41    11171   7394  11602    481  -2514   -101       O  
ATOM    304  CB  VAL A  41     -48.427  21.632   5.192  1.00 74.30           C  
ANISOU  304  CB  VAL A  41    10020   6923  11287    231  -2374     92       C  
ATOM    305  CG1 VAL A  41     -49.073  22.060   6.501  1.00 72.71           C  
ANISOU  305  CG1 VAL A  41     9571   6789  11263    102  -2337    190       C  
ATOM    306  CG2 VAL A  41     -47.845  22.844   4.477  1.00 73.86           C  
ANISOU  306  CG2 VAL A  41     9949   6975  11138    306  -2211     69       C  
ATOM    307  N   THR A  42     -45.433  19.662   4.179  1.00 79.90           N  
ANISOU  307  N   THR A  42    11146   7571  11638    641  -2271   -183       N  
ATOM    308  CA  THR A  42     -44.564  19.279   3.029  1.00 82.23           C  
ANISOU  308  CA  THR A  42    11659   7850  11735    821  -2247   -295       C  
ATOM    309  C   THR A  42     -45.210  18.141   2.226  1.00 85.09           C  
ANISOU  309  C   THR A  42    12285   8018  12026    836  -2499   -343       C  
ATOM    310  O   THR A  42     -45.145  18.200   0.982  1.00 86.98           O  
ANISOU  310  O   THR A  42    12709   8229  12110    923  -2531   -400       O  
ATOM    311  CB  THR A  42     -43.158  18.879   3.503  1.00 82.46           C  
ANISOU  311  CB  THR A  42    11664   7953  11713    967  -2093   -366       C  
ATOM    312  OG1 THR A  42     -42.535  20.025   4.083  1.00 81.01           O  
ANISOU  312  OG1 THR A  42    11253   7947  11578    952  -1867   -321       O  
ATOM    313  CG2 THR A  42     -42.273  18.342   2.397  1.00 84.06           C  
ANISOU  313  CG2 THR A  42    12086   8140  11710   1169  -2071   -484       C  
ATOM    314  N   LYS A  43     -45.797  17.148   2.905  1.00 86.46           N  
ANISOU  314  N   LYS A  43    12482   8061  12305    751  -2677   -317       N  
ATOM    315  CA  LYS A  43     -46.244  15.864   2.295  1.00 88.77           C  
ANISOU  315  CA  LYS A  43    13043   8148  12536    773  -2934   -371       C  
ATOM    316  C   LYS A  43     -47.774  15.823   2.135  1.00 89.90           C  
ANISOU  316  C   LYS A  43    13196   8180  12781    584  -3160   -275       C  
ATOM    317  O   LYS A  43     -48.242  14.966   1.361  1.00 91.51           O  
ANISOU  317  O   LYS A  43    13641   8212  12915    593  -3387   -315       O  
ATOM    318  CB  LYS A  43     -45.717  14.688   3.127  1.00 89.43           C  
ANISOU  318  CB  LYS A  43    13167   8152  12656    820  -2988   -410       C  
ATOM    319  CG  LYS A  43     -44.203  14.507   3.087  1.00 89.92           C  
ANISOU  319  CG  LYS A  43    13268   8297  12598   1035  -2807   -521       C  
ATOM    320  CD  LYS A  43     -43.664  13.455   4.042  1.00 90.19           C  
ANISOU  320  CD  LYS A  43    13310   8266  12689   1076  -2849   -548       C  
ATOM    321  CE  LYS A  43     -42.164  13.269   3.918  1.00 90.55           C  
ANISOU  321  CE  LYS A  43    13394   8397  12612   1305  -2675   -660       C  
ATOM    322  NZ  LYS A  43     -41.636  12.289   4.897  1.00 90.78           N  
ANISOU  322  NZ  LYS A  43    13420   8364  12707   1345  -2718   -681       N  
ATOM    323  N   ILE A  44     -48.534  16.691   2.819  1.00 89.19           N  
ANISOU  323  N   ILE A  44    12861   8179  12846    424  -3111   -155       N  
ATOM    324  CA  ILE A  44     -50.014  16.804   2.624  1.00 89.98           C  
ANISOU  324  CA  ILE A  44    12936   8201  13048    247  -3308    -53       C  
ATOM    325  C   ILE A  44     -50.263  17.666   1.381  1.00 91.42           C  
ANISOU  325  C   ILE A  44    13198   8410  13126    281  -3299    -69       C  
ATOM    326  O   ILE A  44     -49.312  18.334   0.922  1.00 91.26           O  
ANISOU  326  O   ILE A  44    13190   8499  12983    415  -3104   -135       O  
ATOM    327  CB  ILE A  44     -50.752  17.346   3.871  1.00 87.87           C  
ANISOU  327  CB  ILE A  44    12372   8026  12986     77  -3260     80       C  
ATOM    328  CG1 ILE A  44     -50.552  18.850   4.077  1.00 85.69           C  
ANISOU  328  CG1 ILE A  44    11881   7937  12737     83  -3025    113       C  
ATOM    329  CG2 ILE A  44     -50.380  16.552   5.118  1.00 87.28           C  
ANISOU  329  CG2 ILE A  44    12221   7944  12996     52  -3245     96       C  
ATOM    330  CD1 ILE A  44     -51.493  19.454   5.095  1.00 84.49           C  
ANISOU  330  CD1 ILE A  44    11464   7864  12772    -76  -3006    241       C  
ATOM    331  N   LYS A  45     -51.494  17.644   0.865  1.00 93.48           N  
ANISOU  331  N   LYS A  45    13506   8575  13435    158  -3507     -3       N  
ATOM    332  CA  LYS A  45     -51.902  18.348  -0.380  1.00 94.97           C  
ANISOU  332  CA  LYS A  45    13798   8758  13528    174  -3551     -9       C  
ATOM    333  C   LYS A  45     -52.856  19.483  -0.021  1.00 94.49           C  
ANISOU  333  C   LYS A  45    13490   8792  13618     32  -3517    115       C  
ATOM    334  O   LYS A  45     -53.633  19.358   0.924  1.00 93.12           O  
ANISOU  334  O   LYS A  45    13136   8622  13621   -107  -3577    214       O  
ATOM    335  CB  LYS A  45     -52.526  17.349  -1.358  1.00 97.63           C  
ANISOU  335  CB  LYS A  45    14418   8890  13784    161  -3843    -43       C  
ATOM    336  CG  LYS A  45     -51.548  16.321  -1.912  1.00 99.37           C  
ANISOU  336  CG  LYS A  45    14919   9014  13822    336  -3875   -187       C  
ATOM    337  CD  LYS A  45     -52.200  15.042  -2.380  1.00102.04           C  
ANISOU  337  CD  LYS A  45    15510   9122  14138    294  -4196   -209       C  
ATOM    338  CE  LYS A  45     -51.193  14.015  -2.850  1.00103.93           C  
ANISOU  338  CE  LYS A  45    16029   9262  14195    488  -4222   -361       C  
ATOM    339  NZ  LYS A  45     -51.856  12.865  -3.506  1.00106.55           N  
ANISOU  339  NZ  LYS A  45    16649   9353  14480    456  -4555   -393       N  
ATOM    340  N   PRO A  46     -52.811  20.625  -0.750  1.00 95.76           N  
ANISOU  340  N   PRO A  46    13634   9036  13711     70  -3416    116       N  
ATOM    341  CA  PRO A  46     -53.646  21.786  -0.437  1.00 95.41           C  
ANISOU  341  CA  PRO A  46    13361   9084  13804    -40  -3375    225       C  
ATOM    342  C   PRO A  46     -55.117  21.459  -0.126  1.00 96.77           C  
ANISOU  342  C   PRO A  46    13445   9177  14145   -214  -3598    337       C  
ATOM    343  O   PRO A  46     -55.635  20.476  -0.632  1.00 98.16           O  
ANISOU  343  O   PRO A  46    13797   9201  14298   -255  -3833    332       O  
ATOM    344  CB  PRO A  46     -53.541  22.636  -1.713  1.00 95.57           C  
ANISOU  344  CB  PRO A  46    13505   9123  13684     26  -3350    196       C  
ATOM    345  CG  PRO A  46     -52.159  22.331  -2.246  1.00 95.56           C  
ANISOU  345  CG  PRO A  46    13683   9142  13480    200  -3218     73       C  
ATOM    346  CD  PRO A  46     -51.926  20.874  -1.902  1.00 96.34           C  
ANISOU  346  CD  PRO A  46    13907   9126  13568    226  -3332     15       C  
ATOM    347  N   HIS A  47     -55.740  22.306   0.699  1.00 96.39           N  
ANISOU  347  N   HIS A  47    13125   9238  14261   -306  -3520    437       N  
ATOM    348  CA  HIS A  47     -57.144  22.209   1.183  1.00 96.76           C  
ANISOU  348  CA  HIS A  47    13010   9261  14491   -472  -3683    564       C  
ATOM    349  C   HIS A  47     -57.856  23.527   0.852  1.00 94.99           C  
ANISOU  349  C   HIS A  47    12649   9115  14326   -502  -3652    630       C  
ATOM    350  O   HIS A  47     -57.157  24.542   0.660  1.00 94.81           O  
ANISOU  350  O   HIS A  47    12602   9187  14232   -409  -3462    586       O  
ATOM    351  CB  HIS A  47     -57.148  21.885   2.688  1.00 96.94           C  
ANISOU  351  CB  HIS A  47    12819   9357  14656   -537  -3597    620       C  
ATOM    352  CG  HIS A  47     -58.298  21.054   3.159  1.00 99.16           C  
ANISOU  352  CG  HIS A  47    13027   9568  15079   -697  -3807    729       C  
ATOM    353  ND1 HIS A  47     -58.745  19.937   2.471  1.00101.99           N  
ANISOU  353  ND1 HIS A  47    13594   9752  15403   -753  -4072    729       N  
ATOM    354  CD2 HIS A  47     -59.066  21.146   4.268  1.00 99.04           C  
ANISOU  354  CD2 HIS A  47    12756   9636  15237   -816  -3793    845       C  
ATOM    355  CE1 HIS A  47     -59.753  19.394   3.124  1.00102.29           C  
ANISOU  355  CE1 HIS A  47    13500   9767  15595   -912  -4218    851       C  
ATOM    356  NE2 HIS A  47     -59.968  20.116   4.232  1.00100.87           N  
ANISOU  356  NE2 HIS A  47    13029   9753  15542   -951  -4043    926       N  
ATOM    357  N   ASN A  48     -59.189  23.515   0.782  1.00 93.76           N  
ANISOU  357  N   ASN A  48    12405   8921  14296   -630  -3838    736       N  
ATOM    358  CA  ASN A  48     -60.007  24.713   0.452  1.00 92.18           C  
ANISOU  358  CA  ASN A  48    12072   8783  14167   -660  -3841    806       C  
ATOM    359  C   ASN A  48     -59.925  25.701   1.624  1.00 89.18           C  
ANISOU  359  C   ASN A  48    11407   8572  13905   -652  -3614    846       C  
ATOM    360  O   ASN A  48     -59.978  26.919   1.370  1.00 87.69           O  
ANISOU  360  O   ASN A  48    11145   8454  13718   -609  -3519    853       O  
ATOM    361  CB  ASN A  48     -61.450  24.331   0.106  1.00 93.80           C  
ANISOU  361  CB  ASN A  48    12250   8904  14484   -798  -4112    913       C  
ATOM    362  CG  ASN A  48     -61.914  24.897  -1.220  1.00 94.83           C  
ANISOU  362  CG  ASN A  48    12515   8970  14544   -783  -4243    913       C  
ATOM    363  OD1 ASN A  48     -61.589  26.029  -1.569  1.00 94.34           O  
ANISOU  363  OD1 ASN A  48    12433   8980  14432   -704  -4107    887       O  
ATOM    364  ND2 ASN A  48     -62.677  24.116  -1.967  1.00 96.54           N  
ANISOU  364  ND2 ASN A  48    12878   9045  14756   -865  -4519    946       N  
ATOM    365  N   SER A  49     -59.782  25.182   2.851  1.00 87.76           N  
ANISOU  365  N   SER A  49    11088   8446  13811   -690  -3539    870       N  
ATOM    366  CA  SER A  49     -59.641  25.942   4.124  1.00 86.02           C  
ANISOU  366  CA  SER A  49    10608   8381  13693   -681  -3324    901       C  
ATOM    367  C   SER A  49     -58.451  26.906   4.054  1.00 84.20           C  
ANISOU  367  C   SER A  49    10405   8227  13359   -551  -3095    811       C  
ATOM    368  O   SER A  49     -58.560  28.011   4.624  1.00 82.42           O  
ANISOU  368  O   SER A  49     9996   8113  13205   -533  -2954    838       O  
ATOM    369  CB  SER A  49     -59.485  25.005   5.302  1.00 85.79           C  
ANISOU  369  CB  SER A  49    10493   8372  13728   -735  -3297    924       C  
ATOM    370  OG  SER A  49     -60.440  23.955   5.260  1.00 86.96           O  
ANISOU  370  OG  SER A  49    10658   8430  13952   -862  -3528   1006       O  
ATOM    371  N   HIS A  50     -57.364  26.485   3.395  1.00 84.29           N  
ANISOU  371  N   HIS A  50    10636   8180  13208   -463  -3063    711       N  
ATOM    372  CA  HIS A  50     -56.041  27.170   3.353  1.00 82.74           C  
ANISOU  372  CA  HIS A  50    10479   8058  12900   -343  -2843    626       C  
ATOM    373  C   HIS A  50     -56.124  28.484   2.560  1.00 82.15           C  
ANISOU  373  C   HIS A  50    10410   8018  12785   -304  -2797    631       C  
ATOM    374  O   HIS A  50     -55.404  29.431   2.932  1.00 80.28           O  
ANISOU  374  O   HIS A  50    10089   7878  12535   -247  -2604    610       O  
ATOM    375  CB  HIS A  50     -54.963  26.243   2.761  1.00 83.46           C  
ANISOU  375  CB  HIS A  50    10807   8079  12826   -258  -2844    525       C  
ATOM    376  CG  HIS A  50     -54.689  24.998   3.543  1.00 83.24           C  
ANISOU  376  CG  HIS A  50    10791   8011  12825   -277  -2876    509       C  
ATOM    377  ND1 HIS A  50     -54.084  23.889   2.975  1.00 83.74           N  
ANISOU  377  ND1 HIS A  50    11082   7970  12763   -217  -2958    430       N  
ATOM    378  CD2 HIS A  50     -54.930  24.672   4.832  1.00 82.48           C  
ANISOU  378  CD2 HIS A  50    10517   7961  12858   -346  -2844    561       C  
ATOM    379  CE1 HIS A  50     -53.963  22.940   3.880  1.00 83.11           C  
ANISOU  379  CE1 HIS A  50    10967   7867  12743   -250  -2982    436       C  
ATOM    380  NE2 HIS A  50     -54.475  23.394   5.027  1.00 82.42           N  
ANISOU  380  NE2 HIS A  50    10632   7874  12810   -335  -2911    519       N  
ATOM    381  N   GLU A  51     -56.948  28.532   1.504  1.00 83.27           N  
ANISOU  381  N   GLU A  51    10656   8077  12906   -338  -2976    661       N  
ATOM    382  CA  GLU A  51     -57.068  29.684   0.564  1.00 83.07           C  
ANISOU  382  CA  GLU A  51    10676   8059  12825   -304  -2968    669       C  
ATOM    383  C   GLU A  51     -56.818  30.994   1.321  1.00 80.78           C  
ANISOU  383  C   GLU A  51    10189   7892  12609   -278  -2775    690       C  
ATOM    384  O   GLU A  51     -57.600  31.299   2.243  1.00 79.12           O  
ANISOU  384  O   GLU A  51     9767   7734  12559   -332  -2772    754       O  
ATOM    385  CB  GLU A  51     -58.448  29.694  -0.101  1.00 85.36           C  
ANISOU  385  CB  GLU A  51    10977   8271  13184   -385  -3199    744       C  
ATOM    386  CG  GLU A  51     -58.747  30.947  -0.920  1.00 86.41           C  
ANISOU  386  CG  GLU A  51    11124   8414  13292   -362  -3205    770       C  
ATOM    387  CD  GLU A  51     -58.385  30.890  -2.397  1.00 87.96           C  
ANISOU  387  CD  GLU A  51    11592   8527  13299   -314  -3288    723       C  
ATOM    388  OE1 GLU A  51     -57.717  31.831  -2.881  1.00 87.20           O  
ANISOU  388  OE1 GLU A  51    11548   8476  13106   -249  -3165    700       O  
ATOM    389  OE2 GLU A  51     -58.791  29.919  -3.070  1.00 89.64           O  
ANISOU  389  OE2 GLU A  51    11969   8629  13460   -346  -3481    714       O  
ATOM    390  N   GLY A  52     -55.760  31.721   0.939  1.00 79.86           N  
ANISOU  390  N   GLY A  52    10144   7821  12375   -198  -2623    640       N  
ATOM    391  CA  GLY A  52     -55.446  33.081   1.421  1.00 78.21           C  
ANISOU  391  CA  GLY A  52     9795   7706  12213   -171  -2460    656       C  
ATOM    392  C   GLY A  52     -54.833  33.086   2.812  1.00 76.20           C  
ANISOU  392  C   GLY A  52     9377   7543  12030   -159  -2290    639       C  
ATOM    393  O   GLY A  52     -55.121  34.031   3.570  1.00 74.82           O  
ANISOU  393  O   GLY A  52     9030   7433  11962   -167  -2213    674       O  
ATOM    394  N   LYS A  53     -54.010  32.082   3.134  1.00 76.09           N  
ANISOU  394  N   LYS A  53     9424   7530  11954   -134  -2238    585       N  
ATOM    395  CA  LYS A  53     -53.249  31.997   4.411  1.00 75.15           C  
ANISOU  395  CA  LYS A  53     9176   7494  11881   -116  -2075    561       C  
ATOM    396  C   LYS A  53     -51.741  31.968   4.127  1.00 74.07           C  
ANISOU  396  C   LYS A  53     9146   7393  11602    -34  -1930    491       C  
ATOM    397  O   LYS A  53     -51.344  31.628   2.993  1.00 74.01           O  
ANISOU  397  O   LYS A  53     9327   7339  11455     10  -1972    454       O  
ATOM    398  CB  LYS A  53     -53.660  30.768   5.228  1.00 75.40           C  
ANISOU  398  CB  LYS A  53     9156   7502  11991   -167  -2148    573       C  
ATOM    399  CG  LYS A  53     -54.894  30.946   6.105  1.00 75.72           C  
ANISOU  399  CG  LYS A  53     8998   7571  12201   -247  -2204    653       C  
ATOM    400  CD  LYS A  53     -54.770  30.270   7.463  1.00 75.38           C  
ANISOU  400  CD  LYS A  53     8828   7577  12235   -278  -2144    662       C  
ATOM    401  CE  LYS A  53     -56.101  29.946   8.113  1.00 76.02           C  
ANISOU  401  CE  LYS A  53     8755   7668  12460   -372  -2251    751       C  
ATOM    402  NZ  LYS A  53     -56.711  31.132   8.761  1.00 75.47           N  
ANISOU  402  NZ  LYS A  53     8487   7692  12494   -371  -2171    796       N  
ATOM    403  N   THR A  54     -50.945  32.311   5.144  1.00 72.70           N  
ANISOU  403  N   THR A  54     8851   7306  11463    -13  -1766    476       N  
ATOM    404  CA  THR A  54     -49.463  32.416   5.090  1.00 72.60           C  
ANISOU  404  CA  THR A  54     8888   7354  11342     59  -1608    422       C  
ATOM    405  C   THR A  54     -48.852  31.017   5.252  1.00 73.24           C  
ANISOU  405  C   THR A  54     9053   7409  11365     98  -1618    366       C  
ATOM    406  O   THR A  54     -49.421  30.206   6.011  1.00 72.23           O  
ANISOU  406  O   THR A  54     8868   7248  11326     53  -1693    378       O  
ATOM    407  CB  THR A  54     -48.959  33.420   6.138  1.00 70.96           C  
ANISOU  407  CB  THR A  54     8512   7239  11208     55  -1453    437       C  
ATOM    408  OG1 THR A  54     -49.489  34.703   5.799  1.00 69.50           O  
ANISOU  408  OG1 THR A  54     8289   7058  11059     32  -1462    482       O  
ATOM    409  CG2 THR A  54     -47.449  33.488   6.222  1.00 70.20           C  
ANISOU  409  CG2 THR A  54     8438   7213  11022    116  -1296    395       C  
ATOM    410  N   PHE A  55     -47.744  30.758   4.546  1.00 74.89           N  
ANISOU  410  N   PHE A  55     9390   7635  11427    182  -1546    310       N  
ATOM    411  CA  PHE A  55     -47.030  29.454   4.490  1.00 76.64           C  
ANISOU  411  CA  PHE A  55     9723   7828  11566    251  -1554    243       C  
ATOM    412  C   PHE A  55     -45.513  29.703   4.477  1.00 76.44           C  
ANISOU  412  C   PHE A  55     9697   7903  11444    340  -1370    201       C  
ATOM    413  O   PHE A  55     -45.003  30.206   3.459  1.00 77.26           O  
ANISOU  413  O   PHE A  55     9892   8039  11423    391  -1315    192       O  
ATOM    414  CB  PHE A  55     -47.476  28.655   3.259  1.00 78.97           C  
ANISOU  414  CB  PHE A  55    10234   8017  11754    278  -1714    212       C  
ATOM    415  CG  PHE A  55     -48.824  27.982   3.375  1.00 80.41           C  
ANISOU  415  CG  PHE A  55    10430   8089  12031    191  -1917    247       C  
ATOM    416  CD1 PHE A  55     -48.968  26.795   4.081  1.00 81.02           C  
ANISOU  416  CD1 PHE A  55    10507   8110  12164    171  -1996    233       C  
ATOM    417  CD2 PHE A  55     -49.949  28.521   2.766  1.00 81.21           C  
ANISOU  417  CD2 PHE A  55    10542   8144  12169    125  -2040    302       C  
ATOM    418  CE1 PHE A  55     -50.203  26.172   4.188  1.00 81.23           C  
ANISOU  418  CE1 PHE A  55    10539   8042  12283     76  -2188    281       C  
ATOM    419  CE2 PHE A  55     -51.184  27.897   2.874  1.00 82.04           C  
ANISOU  419  CE2 PHE A  55    10644   8158  12369     37  -2232    346       C  
ATOM    420  CZ  PHE A  55     -51.309  26.723   3.584  1.00 81.78           C  
ANISOU  420  CZ  PHE A  55    10606   8075  12392      8  -2305    339       C  
ATOM    421  N   TYR A  56     -44.820  29.369   5.574  1.00 74.60           N  
ANISOU  421  N   TYR A  56     9357   7720  11265    355  -1278    184       N  
ATOM    422  CA  TYR A  56     -43.340  29.455   5.711  1.00 73.66           C  
ANISOU  422  CA  TYR A  56     9215   7700  11071    440  -1110    148       C  
ATOM    423  C   TYR A  56     -42.687  28.425   4.780  1.00 76.07           C  
ANISOU  423  C   TYR A  56     9704   7977  11221    556  -1129     75       C  
ATOM    424  O   TYR A  56     -42.959  27.226   4.954  1.00 76.64           O  
ANISOU  424  O   TYR A  56     9856   7962  11300    577  -1239     35       O  
ATOM    425  CB  TYR A  56     -42.903  29.200   7.156  1.00 71.85           C  
ANISOU  425  CB  TYR A  56     8838   7514  10949    423  -1042    148       C  
ATOM    426  CG  TYR A  56     -42.696  30.417   8.026  1.00 70.04           C  
ANISOU  426  CG  TYR A  56     8430   7369  10811    365   -929    197       C  
ATOM    427  CD1 TYR A  56     -41.468  31.058   8.079  1.00 69.23           C  
ANISOU  427  CD1 TYR A  56     8271   7369  10662    405   -776    196       C  
ATOM    428  CD2 TYR A  56     -43.707  30.892   8.850  1.00 68.76           C  
ANISOU  428  CD2 TYR A  56     8154   7189  10783    273   -977    245       C  
ATOM    429  CE1 TYR A  56     -41.259  32.157   8.898  1.00 68.10           C  
ANISOU  429  CE1 TYR A  56     7980   7290  10604    349   -690    239       C  
ATOM    430  CE2 TYR A  56     -43.516  31.991   9.674  1.00 67.55           C  
ANISOU  430  CE2 TYR A  56     7855   7104  10706    232   -881    279       C  
ATOM    431  CZ  TYR A  56     -42.286  32.626   9.701  1.00 67.39           C  
ANISOU  431  CZ  TYR A  56     7796   7168  10639    267   -744    274       C  
ATOM    432  OH  TYR A  56     -42.079  33.706  10.509  1.00 65.67           O  
ANISOU  432  OH  TYR A  56     7451   7005  10496    223   -667    306       O  
ATOM    433  N   VAL A  57     -41.855  28.880   3.833  1.00 78.71           N  
ANISOU  433  N   VAL A  57    10105   8383  11416    631  -1027     61       N  
ATOM    434  CA  VAL A  57     -41.110  28.026   2.854  1.00 81.16           C  
ANISOU  434  CA  VAL A  57    10592   8692  11551    768  -1015    -13       C  
ATOM    435  C   VAL A  57     -39.604  28.290   3.006  1.00 82.87           C  
ANISOU  435  C   VAL A  57    10728   9054  11704    854   -816    -26       C  
ATOM    436  O   VAL A  57     -39.234  29.418   3.396  1.00 81.60           O  
ANISOU  436  O   VAL A  57    10416   8988  11597    794   -700     36       O  
ATOM    437  CB  VAL A  57     -41.585  28.254   1.402  1.00 81.71           C  
ANISOU  437  CB  VAL A  57    10837   8721  11485    787  -1087    -15       C  
ATOM    438  CG1 VAL A  57     -43.076  27.991   1.247  1.00 81.42           C  
ANISOU  438  CG1 VAL A  57    10871   8543  11521    696  -1296      4       C  
ATOM    439  CG2 VAL A  57     -41.228  29.639   0.880  1.00 81.14           C  
ANISOU  439  CG2 VAL A  57    10707   8754  11365    758   -965     47       C  
ATOM    440  N   LEU A  58     -38.771  27.288   2.696  1.00 86.08           N  
ANISOU  440  N   LEU A  58    11231   9474  11999    993   -785   -103       N  
ATOM    441  CA  LEU A  58     -37.298  27.305   2.929  1.00 88.50           C  
ANISOU  441  CA  LEU A  58    11449   9921  12254   1091   -604   -120       C  
ATOM    442  C   LEU A  58     -36.618  28.223   1.916  1.00 90.47           C  
ANISOU  442  C   LEU A  58    11707  10298  12368   1127   -467    -84       C  
ATOM    443  O   LEU A  58     -37.071  28.338   0.778  1.00 91.73           O  
ANISOU  443  O   LEU A  58    12019  10425  12410   1144   -520    -89       O  
ATOM    444  CB  LEU A  58     -36.746  25.878   2.821  1.00 89.79           C  
ANISOU  444  CB  LEU A  58    11734  10046  12336   1244   -636   -219       C  
ATOM    445  CG  LEU A  58     -35.232  25.727   2.986  1.00 90.52           C  
ANISOU  445  CG  LEU A  58    11743  10282  12366   1372   -460   -245       C  
ATOM    446  CD1 LEU A  58     -34.847  25.635   4.456  1.00 89.09           C  
ANISOU  446  CD1 LEU A  58    11379  10124  12346   1324   -426   -225       C  
ATOM    447  CD2 LEU A  58     -34.720  24.512   2.226  1.00 92.73           C  
ANISOU  447  CD2 LEU A  58    12208  10535  12489   1563   -483   -351       C  
ATOM    448  N   PRO A  59     -35.516  28.909   2.300  1.00 91.52           N  
ANISOU  448  N   PRO A  59    11678  10582  12512   1132   -293    -40       N  
ATOM    449  CA  PRO A  59     -34.646  29.573   1.332  1.00 93.50           C  
ANISOU  449  CA  PRO A  59    11934  10974  12615   1185   -147     -5       C  
ATOM    450  C   PRO A  59     -34.137  28.572   0.286  1.00 96.06           C  
ANISOU  450  C   PRO A  59    12436  11319  12743   1367   -129    -92       C  
ATOM    451  O   PRO A  59     -33.303  27.741   0.623  1.00 95.59           O  
ANISOU  451  O   PRO A  59    12353  11302  12661   1489    -72   -152       O  
ATOM    452  CB  PRO A  59     -33.493  30.128   2.184  1.00 93.57           C  
ANISOU  452  CB  PRO A  59    11727  11127  12698   1167     11     46       C  
ATOM    453  CG  PRO A  59     -34.086  30.267   3.570  1.00 91.60           C  
ANISOU  453  CG  PRO A  59    11355  10796  12653   1049    -65     64       C  
ATOM    454  CD  PRO A  59     -35.068  29.121   3.686  1.00 90.92           C  
ANISOU  454  CD  PRO A  59    11403  10549  12591   1075   -234    -11       C  
ATOM    455  N   ASN A  60     -34.685  28.653  -0.931  1.00 98.24           N  
ANISOU  455  N   ASN A  60    12891  11555  12881   1387   -188   -101       N  
ATOM    456  CA  ASN A  60     -34.234  27.872  -2.115  1.00101.39           C  
ANISOU  456  CA  ASN A  60    13484  11981  13057   1565   -164   -181       C  
ATOM    457  C   ASN A  60     -33.851  28.840  -3.245  1.00102.71           C  
ANISOU  457  C   ASN A  60    13678  12279  13066   1564    -45   -113       C  
ATOM    458  O   ASN A  60     -32.765  28.641  -3.833  1.00103.40           O  
ANISOU  458  O   ASN A  60    13777  12514  12995   1705    106   -133       O  
ATOM    459  CB  ASN A  60     -35.282  26.844  -2.553  1.00102.27           C  
ANISOU  459  CB  ASN A  60    13826  11901  13128   1603   -375   -269       C  
ATOM    460  CG  ASN A  60     -34.688  25.693  -3.340  1.00104.73           C  
ANISOU  460  CG  ASN A  60    14328  12216  13247   1816   -366   -384       C  
ATOM    461  OD1 ASN A  60     -33.600  25.211  -3.028  1.00105.27           O  
ANISOU  461  OD1 ASN A  60    14329  12384  13284   1946   -243   -426       O  
ATOM    462  ND2 ASN A  60     -35.398  25.239  -4.359  1.00106.65           N  
ANISOU  462  ND2 ASN A  60    14814  12347  13357   1861   -502   -439       N  
ATOM    463  N   ASP A  61     -34.691  29.847  -3.534  1.00101.85           N  
ANISOU  463  N   ASP A  61    13574  12125  12997   1416   -108    -32       N  
ATOM    464  CA  ASP A  61     -34.417  30.900  -4.555  1.00102.08           C  
ANISOU  464  CA  ASP A  61    13625  12267  12892   1384    -10     53       C  
ATOM    465  C   ASP A  61     -33.911  32.170  -3.855  1.00100.32           C  
ANISOU  465  C   ASP A  61    13165  12154  12795   1249    108    174       C  
ATOM    466  O   ASP A  61     -34.287  32.393  -2.687  1.00 97.97           O  
ANISOU  466  O   ASP A  61    12731  11789  12701   1146     54    192       O  
ATOM    467  CB  ASP A  61     -35.636  31.158  -5.445  1.00101.38           C  
ANISOU  467  CB  ASP A  61    13720  12050  12747   1320   -171     63       C  
ATOM    468  CG  ASP A  61     -36.813  31.779  -4.719  1.00100.03           C  
ANISOU  468  CG  ASP A  61    13474  11747  12785   1145   -314    116       C  
ATOM    469  OD1 ASP A  61     -36.850  33.019  -4.621  1.00 99.72           O  
ANISOU  469  OD1 ASP A  61    13323  11756  12809   1024   -267    220       O  
ATOM    470  OD2 ASP A  61     -37.676  31.014  -4.253  1.00100.13           O  
ANISOU  470  OD2 ASP A  61    13537  11611  12894   1134   -473     56       O  
ATOM    471  N   ASP A  62     -33.113  32.973  -4.573  1.00100.75           N  
ANISOU  471  N   ASP A  62    13184  12369  12727   1248    259    257       N  
ATOM    472  CA  ASP A  62     -32.206  34.025  -4.028  1.00 99.91           C  
ANISOU  472  CA  ASP A  62    12853  12408  12697   1155    409    371       C  
ATOM    473  C   ASP A  62     -32.990  35.060  -3.209  1.00 97.27           C  
ANISOU  473  C   ASP A  62    12415  11975  12568    965    315    445       C  
ATOM    474  O   ASP A  62     -32.471  35.492  -2.157  1.00 96.43           O  
ANISOU  474  O   ASP A  62    12116  11916  12607    897    375    489       O  
ATOM    475  CB  ASP A  62     -31.414  34.704  -5.150  1.00101.24           C  
ANISOU  475  CB  ASP A  62    13038  12751  12677   1172    558    459       C  
ATOM    476  CG  ASP A  62     -30.449  33.779  -5.875  1.00102.95           C  
ANISOU  476  CG  ASP A  62    13321  13107  12688   1375    690    393       C  
ATOM    477  OD1 ASP A  62     -29.881  32.881  -5.216  1.00102.62           O  
ANISOU  477  OD1 ASP A  62    13211  13090  12688   1486    730    314       O  
ATOM    478  OD2 ASP A  62     -30.272  33.962  -7.094  1.00103.95           O  
ANISOU  478  OD2 ASP A  62    13569  13317  12607   1426    751    421       O  
ATOM    479  N   THR A  63     -34.185  35.440  -3.673  1.00 95.55           N  
ANISOU  479  N   THR A  63    12320  11624  12359    889    169    458       N  
ATOM    480  CA  THR A  63     -35.101  36.407  -3.007  1.00 92.62           C  
ANISOU  480  CA  THR A  63    11875  11145  12172    727     62    518       C  
ATOM    481  C   THR A  63     -35.328  36.003  -1.545  1.00 89.15           C  
ANISOU  481  C   THR A  63    11303  10634  11932    702     14    471       C  
ATOM    482  O   THR A  63     -35.378  36.905  -0.688  1.00 86.17           O  
ANISOU  482  O   THR A  63    10783  10251  11705    588     19    533       O  
ATOM    483  CB  THR A  63     -36.440  36.494  -3.749  1.00 93.28           C  
ANISOU  483  CB  THR A  63    12131  11083  12226    691   -109    509       C  
ATOM    484  OG1 THR A  63     -36.161  36.574  -5.148  1.00 94.88           O  
ANISOU  484  OG1 THR A  63    12486  11353  12211    746    -65    531       O  
ATOM    485  CG2 THR A  63     -37.282  37.676  -3.317  1.00 92.66           C  
ANISOU  485  CG2 THR A  63    11982  10919  12302    539   -199    587       C  
ATOM    486  N   LEU A  64     -35.464  34.698  -1.285  1.00 88.31           N  
ANISOU  486  N   LEU A  64    11256  10474  11821    804    -34    365       N  
ATOM    487  CA  LEU A  64     -35.754  34.123   0.056  1.00 87.05           C  
ANISOU  487  CA  LEU A  64    10997  10240  11836    788    -93    315       C  
ATOM    488  C   LEU A  64     -34.485  34.101   0.918  1.00 86.67           C  
ANISOU  488  C   LEU A  64    10775  10317  11836    814     52    326       C  
ATOM    489  O   LEU A  64     -34.634  34.101   2.155  1.00 85.54           O  
ANISOU  489  O   LEU A  64    10509  10134  11855    758     24    322       O  
ATOM    490  CB  LEU A  64     -36.319  32.708  -0.107  1.00 87.98           C  
ANISOU  490  CB  LEU A  64    11262  10250  11915    885   -210    208       C  
ATOM    491  CG  LEU A  64     -37.631  32.595  -0.882  1.00 88.74           C  
ANISOU  491  CG  LEU A  64    11529  10209  11978    854   -381    194       C  
ATOM    492  CD1 LEU A  64     -38.013  31.136  -1.082  1.00 89.16           C  
ANISOU  492  CD1 LEU A  64    11736  10159  11979    954   -497     90       C  
ATOM    493  CD2 LEU A  64     -38.752  33.350  -0.182  1.00 87.73           C  
ANISOU  493  CD2 LEU A  64    11315   9987  12031    710   -489    247       C  
ATOM    494  N   ARG A  65     -33.295  34.055   0.306  1.00 87.34           N  
ANISOU  494  N   ARG A  65    10846  10553  11783    900    201    341       N  
ATOM    495  CA  ARG A  65     -31.998  34.001   1.038  1.00 87.26           C  
ANISOU  495  CA  ARG A  65    10663  10678  11811    934    343    358       C  
ATOM    496  C   ARG A  65     -31.641  35.402   1.554  1.00 85.68           C  
ANISOU  496  C   ARG A  65    10298  10542  11713    786    404    476       C  
ATOM    497  O   ARG A  65     -30.955  35.484   2.593  1.00 85.19           O  
ANISOU  497  O   ARG A  65    10074  10533  11760    761    460    492       O  
ATOM    498  CB  ARG A  65     -30.883  33.401   0.172  1.00 89.78           C  
ANISOU  498  CB  ARG A  65    11020  11145  11944   1091    480    334       C  
ATOM    499  CG  ARG A  65     -30.515  31.974   0.553  1.00 91.16           C  
ANISOU  499  CG  ARG A  65    11224  11305  12106   1246    474    219       C  
ATOM    500  CD  ARG A  65     -29.305  31.456  -0.199  1.00 94.19           C  
ANISOU  500  CD  ARG A  65    11618  11855  12315   1416    626    196       C  
ATOM    501  NE  ARG A  65     -29.513  31.508  -1.641  1.00 97.09           N  
ANISOU  501  NE  ARG A  65    12161  12247  12480   1478    641    192       N  
ATOM    502  CZ  ARG A  65     -30.224  30.631  -2.349  1.00 98.43           C  
ANISOU  502  CZ  ARG A  65    12554  12301  12541   1577    530     93       C  
ATOM    503  NH1 ARG A  65     -30.813  29.604  -1.757  1.00 97.55           N  
ANISOU  503  NH1 ARG A  65    12517  12037  12510   1620    392     -6       N  
ATOM    504  NH2 ARG A  65     -30.343  30.788  -3.657  1.00100.06           N  
ANISOU  504  NH2 ARG A  65    12918  12545  12555   1626    551     99       N  
ATOM    505  N   VAL A  66     -32.102  36.458   0.875  1.00 84.62           N  
ANISOU  505  N   VAL A  66    10211  10394  11547    689    380    555       N  
ATOM    506  CA  VAL A  66     -31.868  37.876   1.288  1.00 83.84           C  
ANISOU  506  CA  VAL A  66     9983  10329  11543    539    411    670       C  
ATOM    507  C   VAL A  66     -32.758  38.188   2.500  1.00 81.66           C  
ANISOU  507  C   VAL A  66     9647   9915  11464    445    292    652       C  
ATOM    508  O   VAL A  66     -32.211  38.603   3.545  1.00 80.34           O  
ANISOU  508  O   VAL A  66     9328   9781  11415    386    331    683       O  
ATOM    509  CB  VAL A  66     -32.126  38.860   0.129  1.00 84.56           C  
ANISOU  509  CB  VAL A  66    10164  10434  11531    471    408    759       C  
ATOM    510  CG1 VAL A  66     -31.928  40.304   0.572  1.00 84.12           C  
ANISOU  510  CG1 VAL A  66     9992  10390  11579    314    417    876       C  
ATOM    511  CG2 VAL A  66     -31.263  38.546  -1.085  1.00 85.89           C  
ANISOU  511  CG2 VAL A  66    10394  10751  11486    568    535    780       C  
ATOM    512  N   GLU A  67     -34.075  37.994   2.352  1.00 80.84           N  
ANISOU  512  N   GLU A  67     9657   9667  11389    434    152    607       N  
ATOM    513  CA  GLU A  67     -35.111  38.192   3.407  1.00 78.83           C  
ANISOU  513  CA  GLU A  67     9360   9284  11308    362     33    584       C  
ATOM    514  C   GLU A  67     -34.783  37.323   4.631  1.00 76.27           C  
ANISOU  514  C   GLU A  67     8938   8962  11078    404     48    520       C  
ATOM    515  O   GLU A  67     -35.000  37.798   5.765  1.00 74.19           O  
ANISOU  515  O   GLU A  67     8568   8662  10958    331     22    532       O  
ATOM    516  CB  GLU A  67     -36.504  37.838   2.875  1.00 79.67           C  
ANISOU  516  CB  GLU A  67     9608   9258  11404    370   -112    542       C  
ATOM    517  CG  GLU A  67     -37.013  38.765   1.781  1.00 80.81           C  
ANISOU  517  CG  GLU A  67     9851   9375  11478    317   -156    607       C  
ATOM    518  CD  GLU A  67     -38.345  38.362   1.161  1.00 81.30           C  
ANISOU  518  CD  GLU A  67    10056   9312  11520    329   -308    569       C  
ATOM    519  OE1 GLU A  67     -38.918  37.333   1.594  1.00 80.93           O  
ANISOU  519  OE1 GLU A  67    10032   9195  11521    373   -384    494       O  
ATOM    520  OE2 GLU A  67     -38.812  39.079   0.248  1.00 81.34           O  
ANISOU  520  OE2 GLU A  67    10150   9286  11466    289   -358    621       O  
ATOM    521  N   ALA A  68     -34.303  36.094   4.405  1.00 75.61           N  
ANISOU  521  N   ALA A  68     8902   8915  10912    523     83    451       N  
ATOM    522  CA  ALA A  68     -33.826  35.160   5.453  1.00 74.81           C  
ANISOU  522  CA  ALA A  68     8719   8824  10878    578    102    392       C  
ATOM    523  C   ALA A  68     -32.778  35.866   6.322  1.00 74.56           C  
ANISOU  523  C   ALA A  68     8511   8893  10924    524    204    450       C  
ATOM    524  O   ALA A  68     -33.066  36.099   7.514  1.00 72.41           O  
ANISOU  524  O   ALA A  68     8149   8571  10792    457    162    449       O  
ATOM    525  CB  ALA A  68     -33.269  33.901   4.831  1.00 75.54           C  
ANISOU  525  CB  ALA A  68     8902   8957  10843    727    139    320       C  
ATOM    526  N   PHE A  69     -31.629  36.223   5.734  1.00 75.98           N  
ANISOU  526  N   PHE A  69     8644   9211  11013    548    331    504       N  
ATOM    527  CA  PHE A  69     -30.474  36.841   6.441  1.00 75.98           C  
ANISOU  527  CA  PHE A  69     8471   9323  11074    497    430    570       C  
ATOM    528  C   PHE A  69     -30.872  38.198   7.042  1.00 74.03           C  
ANISOU  528  C   PHE A  69     8159   9024  10946    343    382    643       C  
ATOM    529  O   PHE A  69     -30.486  38.442   8.202  1.00 72.26           O  
ANISOU  529  O   PHE A  69     7813   8805  10837    292    386    654       O  
ATOM    530  CB  PHE A  69     -29.254  36.989   5.527  1.00 78.29           C  
ANISOU  530  CB  PHE A  69     8726   9784  11234    547    572    629       C  
ATOM    531  CG  PHE A  69     -28.087  37.665   6.203  1.00 79.79           C  
ANISOU  531  CG  PHE A  69     8730  10090  11494    479    662    713       C  
ATOM    532  CD1 PHE A  69     -27.360  37.006   7.185  1.00 80.48           C  
ANISOU  532  CD1 PHE A  69     8704  10222  11653    529    693    677       C  
ATOM    533  CD2 PHE A  69     -27.741  38.973   5.895  1.00 80.54           C  
ANISOU  533  CD2 PHE A  69     8767  10241  11590    355    699    832       C  
ATOM    534  CE1 PHE A  69     -26.297  37.631   7.823  1.00 80.94           C  
ANISOU  534  CE1 PHE A  69     8590  10383  11781    459    761    758       C  
ATOM    535  CE2 PHE A  69     -26.679  39.596   6.535  1.00 81.20           C  
ANISOU  535  CE2 PHE A  69     8682  10423  11745    280    764    916       C  
ATOM    536  CZ  PHE A  69     -25.959  38.926   7.498  1.00 81.06           C  
ANISOU  536  CZ  PHE A  69     8547  10452  11797    332    794    878       C  
ATOM    537  N   GLU A  70     -31.608  39.041   6.300  1.00 73.11           N  
ANISOU  537  N   GLU A  70     8126   8852  10800    277    331    688       N  
ATOM    538  CA  GLU A  70     -31.942  40.438   6.709  1.00 71.64           C  
ANISOU  538  CA  GLU A  70     7895   8613  10710    139    283    762       C  
ATOM    539  C   GLU A  70     -32.836  40.431   7.956  1.00 67.73           C  
ANISOU  539  C   GLU A  70     7371   7998  10364    106    183    708       C  
ATOM    540  O   GLU A  70     -32.740  41.395   8.740  1.00 66.81           O  
ANISOU  540  O   GLU A  70     7177   7859  10346     15    165    750       O  
ATOM    541  CB  GLU A  70     -32.604  41.229   5.574  1.00 73.62           C  
ANISOU  541  CB  GLU A  70     8259   8820  10890     92    238    816       C  
ATOM    542  CG  GLU A  70     -31.622  41.818   4.566  1.00 76.62           C  
ANISOU  542  CG  GLU A  70     8632   9328  11151     66    341    916       C  
ATOM    543  CD  GLU A  70     -30.800  43.022   5.020  1.00 77.92           C  
ANISOU  543  CD  GLU A  70     8675   9547  11383    -56    381   1025       C  
ATOM    544  OE1 GLU A  70     -30.529  43.144   6.235  1.00 78.09           O  
ANISOU  544  OE1 GLU A  70     8587   9551  11530    -92    369   1012       O  
ATOM    545  OE2 GLU A  70     -30.419  43.839   4.150  1.00 78.92           O  
ANISOU  545  OE2 GLU A  70     8821   9732  11432   -121    419   1128       O  
ATOM    546  N   TYR A  71     -33.654  39.389   8.140  1.00 65.25           N  
ANISOU  546  N   TYR A  71     7119   7611  10060    175    119    621       N  
ATOM    547  CA  TYR A  71     -34.578  39.225   9.295  1.00 62.70           C  
ANISOU  547  CA  TYR A  71     6769   7189   9866    152     29    571       C  
ATOM    548  C   TYR A  71     -33.875  38.487  10.441  1.00 60.74           C  
ANISOU  548  C   TYR A  71     6421   6982   9674    184     70    531       C  
ATOM    549  O   TYR A  71     -34.063  38.882  11.605  1.00 59.51           O  
ANISOU  549  O   TYR A  71     6189   6791   9628    131     42    529       O  
ATOM    550  CB  TYR A  71     -35.852  38.483   8.874  1.00 62.57           C  
ANISOU  550  CB  TYR A  71     6864   7075   9833    194    -70    514       C  
ATOM    551  CG  TYR A  71     -37.036  38.698   9.787  1.00 61.66           C  
ANISOU  551  CG  TYR A  71     6722   6862   9841    148   -167    494       C  
ATOM    552  CD1 TYR A  71     -37.499  39.976  10.054  1.00 61.48           C  
ANISOU  552  CD1 TYR A  71     6670   6800   9890     72   -200    538       C  
ATOM    553  CD2 TYR A  71     -37.709  37.635  10.373  1.00 60.99           C  
ANISOU  553  CD2 TYR A  71     6644   6726   9800    183   -227    434       C  
ATOM    554  CE1 TYR A  71     -38.586  40.198  10.883  1.00 60.72           C  
ANISOU  554  CE1 TYR A  71     6543   6627   9899     46   -278    517       C  
ATOM    555  CE2 TYR A  71     -38.798  37.840  11.208  1.00 60.09           C  
ANISOU  555  CE2 TYR A  71     6493   6543   9795    142   -303    425       C  
ATOM    556  CZ  TYR A  71     -39.239  39.128  11.463  1.00 59.77           C  
ANISOU  556  CZ  TYR A  71     6415   6476   9818     81   -323    464       C  
ATOM    557  OH  TYR A  71     -40.303  39.372  12.280  1.00 58.76           O  
ANISOU  557  OH  TYR A  71     6243   6292   9789     56   -388    453       O  
ATOM    558  N   TYR A  72     -33.096  37.448  10.122  1.00 60.43           N  
ANISOU  558  N   TYR A  72     6388   7012   9557    277    132    499       N  
ATOM    559  CA  TYR A  72     -32.567  36.455  11.096  1.00 59.40           C  
ANISOU  559  CA  TYR A  72     6192   6904   9471    331    150    448       C  
ATOM    560  C   TYR A  72     -31.098  36.733  11.448  1.00 59.64           C  
ANISOU  560  C   TYR A  72     6097   7057   9504    329    255    492       C  
ATOM    561  O   TYR A  72     -30.736  36.499  12.618  1.00 60.10           O  
ANISOU  561  O   TYR A  72     6067   7120   9647    318    252    477       O  
ATOM    562  CB  TYR A  72     -32.761  35.036  10.554  1.00 59.45           C  
ANISOU  562  CB  TYR A  72     6301   6887   9398    447    125    374       C  
ATOM    563  CG  TYR A  72     -34.203  34.613  10.425  1.00 58.72           C  
ANISOU  563  CG  TYR A  72     6315   6668   9326    438      2    334       C  
ATOM    564  CD1 TYR A  72     -34.715  34.141   9.228  1.00 59.51           C  
ANISOU  564  CD1 TYR A  72     6556   6730   9323    493    -40    308       C  
ATOM    565  CD2 TYR A  72     -35.067  34.698  11.505  1.00 57.41           C  
ANISOU  565  CD2 TYR A  72     6107   6425   9279    374    -73    325       C  
ATOM    566  CE1 TYR A  72     -36.043  33.762   9.110  1.00 59.22           C  
ANISOU  566  CE1 TYR A  72     6609   6577   9313    474   -165    281       C  
ATOM    567  CE2 TYR A  72     -36.394  34.320  11.405  1.00 57.03           C  
ANISOU  567  CE2 TYR A  72     6136   6275   9256    359   -184    301       C  
ATOM    568  CZ  TYR A  72     -36.886  33.849  10.203  1.00 58.06           C  
ANISOU  568  CZ  TYR A  72     6400   6363   9294    404   -236    282       C  
ATOM    569  OH  TYR A  72     -38.197  33.475  10.108  1.00 58.51           O  
ANISOU  569  OH  TYR A  72     6524   6320   9385    380   -357    267       O  
ATOM    570  N   HIS A  73     -30.289  37.216  10.496  1.00 59.59           N  
ANISOU  570  N   HIS A  73     6078   7151   9409    333    342    552       N  
ATOM    571  CA  HIS A  73     -28.810  37.344  10.616  1.00 59.72           C  
ANISOU  571  CA  HIS A  73     5967   7311   9411    344    453    604       C  
ATOM    572  C   HIS A  73     -28.222  35.959  10.884  1.00 59.95           C  
ANISOU  572  C   HIS A  73     5979   7383   9416    475    485    533       C  
ATOM    573  O   HIS A  73     -27.476  35.811  11.874  1.00 59.96           O  
ANISOU  573  O   HIS A  73     5863   7427   9493    469    506    538       O  
ATOM    574  CB  HIS A  73     -28.411  38.351  11.703  1.00 58.75           C  
ANISOU  574  CB  HIS A  73     5721   7192   9409    223    443    664       C  
ATOM    575  CG  HIS A  73     -28.955  39.719  11.470  1.00 58.53           C  
ANISOU  575  CG  HIS A  73     5720   7109   9409    103    399    730       C  
ATOM    576  ND1 HIS A  73     -29.215  40.596  12.501  1.00 57.35           N  
ANISOU  576  ND1 HIS A  73     5524   6891   9375      1    335    749       N  
ATOM    577  CD2 HIS A  73     -29.302  40.355  10.331  1.00 58.90           C  
ANISOU  577  CD2 HIS A  73     5845   7152   9379     73    402    778       C  
ATOM    578  CE1 HIS A  73     -29.691  41.719  12.004  1.00 57.51           C  
ANISOU  578  CE1 HIS A  73     5593   6862   9393    -81    298    805       C  
ATOM    579  NE2 HIS A  73     -29.760  41.594  10.675  1.00 58.29           N  
ANISOU  579  NE2 HIS A  73     5768   7000   9378    -43    336    827       N  
ATOM    580  N   THR A  74     -28.601  34.984  10.050  1.00 60.08           N  
ANISOU  580  N   THR A  74     6120   7375   9331    588    474    467       N  
ATOM    581  CA  THR A  74     -28.028  33.613  10.016  1.00 60.21           C  
ANISOU  581  CA  THR A  74     6153   7428   9293    739    503    393       C  
ATOM    582  C   THR A  74     -28.057  33.085   8.578  1.00 61.33           C  
ANISOU  582  C   THR A  74     6428   7600   9272    855    538    360       C  
ATOM    583  O   THR A  74     -28.970  33.453   7.814  1.00 60.39           O  
ANISOU  583  O   THR A  74     6427   7414   9104    817    486    365       O  
ATOM    584  CB  THR A  74     -28.746  32.662  10.980  1.00 59.10           C  
ANISOU  584  CB  THR A  74     6057   7163   9236    760    393    313       C  
ATOM    585  OG1 THR A  74     -27.994  31.448  11.031  1.00 58.90           O  
ANISOU  585  OG1 THR A  74     6031   7178   9168    901    423    253       O  
ATOM    586  CG2 THR A  74     -30.175  32.371  10.574  1.00 58.97           C  
ANISOU  586  CG2 THR A  74     6194   7007   9205    746    279    268       C  
ATOM    587  N   THR A  75     -27.058  32.268   8.249  1.00 63.30           N  
ANISOU  587  N   THR A  75     6657   7953   9439    998    624    328       N  
ATOM    588  CA  THR A  75     -26.865  31.572   6.950  1.00 64.79           C  
ANISOU  588  CA  THR A  75     6972   8190   9455   1149    672    279       C  
ATOM    589  C   THR A  75     -27.453  30.158   7.041  1.00 64.72           C  
ANISOU  589  C   THR A  75     7109   8053   9428   1267    566    158       C  
ATOM    590  O   THR A  75     -27.906  29.631   6.000  1.00 65.12           O  
ANISOU  590  O   THR A  75     7331   8061   9350   1356    534    103       O  
ATOM    591  CB  THR A  75     -25.370  31.537   6.618  1.00 65.95           C  
ANISOU  591  CB  THR A  75     6993   8536   9526   1246    834    317       C  
ATOM    592  OG1 THR A  75     -24.734  30.824   7.679  1.00 65.35           O  
ANISOU  592  OG1 THR A  75     6814   8472   9543   1303    831    280       O  
ATOM    593  CG2 THR A  75     -24.763  32.916   6.493  1.00 66.31           C  
ANISOU  593  CG2 THR A  75     6895   8710   9590   1116    930    451       C  
ATOM    594  N   ASP A  76     -27.445  29.586   8.251  1.00 63.60           N  
ANISOU  594  N   ASP A  76     6908   7849   9409   1260    504    124       N  
ATOM    595  CA  ASP A  76     -27.774  28.167   8.544  1.00 63.99           C  
ANISOU  595  CA  ASP A  76     7068   7784   9458   1369    403     20       C  
ATOM    596  C   ASP A  76     -29.020  27.746   7.771  1.00 64.51           C  
ANISOU  596  C   ASP A  76     7342   7709   9459   1376    282    -32       C  
ATOM    597  O   ASP A  76     -30.135  28.114   8.143  1.00 64.77           O  
ANISOU  597  O   ASP A  76     7401   7630   9575   1246    179    -12       O  
ATOM    598  CB  ASP A  76     -27.980  27.957  10.043  1.00 62.28           C  
ANISOU  598  CB  ASP A  76     6765   7493   9404   1289    326     21       C  
ATOM    599  CG  ASP A  76     -28.393  26.527  10.412  1.00 61.93           C  
ANISOU  599  CG  ASP A  76     6838   7319   9372   1377    205    -70       C  
ATOM    600  OD1 ASP A  76     -27.892  25.602   9.567  1.00 62.34           O  
ANISOU  600  OD1 ASP A  76     6995   7391   9298   1555    226   -142       O  
ATOM    601  OD2 ASP A  76     -28.769  26.366  11.533  1.00 61.17           O  
ANISOU  601  OD2 ASP A  76     6695   7149   9394   1298    130    -64       O  
ATOM    602  N   PRO A  77     -28.878  26.934   6.700  1.00 65.82           N  
ANISOU  602  N   PRO A  77     7661   7873   9473   1531    285   -104       N  
ATOM    603  CA  PRO A  77     -30.036  26.440   5.954  1.00 66.26           C  
ANISOU  603  CA  PRO A  77     7928   7783   9462   1541    150   -158       C  
ATOM    604  C   PRO A  77     -30.859  25.405   6.737  1.00 65.87           C  
ANISOU  604  C   PRO A  77     7959   7559   9507   1526    -19   -217       C  
ATOM    605  O   PRO A  77     -31.772  24.840   6.154  1.00 66.05           O  
ANISOU  605  O   PRO A  77     8161   7455   9480   1540   -147   -265       O  
ATOM    606  CB  PRO A  77     -29.411  25.802   4.705  1.00 68.30           C  
ANISOU  606  CB  PRO A  77     8320   8105   9525   1734    213   -225       C  
ATOM    607  CG  PRO A  77     -28.032  25.378   5.161  1.00 68.99           C  
ANISOU  607  CG  PRO A  77     8278   8322   9611   1861    333   -242       C  
ATOM    608  CD  PRO A  77     -27.605  26.438   6.156  1.00 67.62           C  
ANISOU  608  CD  PRO A  77     7870   8240   9583   1712    411   -137       C  
ATOM    609  N   SER A  78     -30.510  25.178   8.011  1.00 65.51           N  
ANISOU  609  N   SER A  78     7785   7514   9591   1494    -22   -207       N  
ATOM    610  CA  SER A  78     -31.242  24.307   8.968  1.00 65.26           C  
ANISOU  610  CA  SER A  78     7794   7332   9666   1450   -174   -238       C  
ATOM    611  C   SER A  78     -32.008  25.152   9.993  1.00 64.29           C  
ANISOU  611  C   SER A  78     7550   7180   9696   1258   -209   -162       C  
ATOM    612  O   SER A  78     -32.620  24.541  10.896  1.00 64.70           O  
ANISOU  612  O   SER A  78     7610   7127   9843   1203   -321   -170       O  
ATOM    613  CB  SER A  78     -30.302  23.376   9.677  1.00 65.79           C  
ANISOU  613  CB  SER A  78     7819   7419   9760   1562   -159   -284       C  
ATOM    614  OG  SER A  78     -29.918  23.915  10.934  1.00 64.68           O  
ANISOU  614  OG  SER A  78     7486   7335   9751   1465   -111   -222       O  
ATOM    615  N   PHE A  79     -31.968  26.487   9.883  1.00 63.53           N  
ANISOU  615  N   PHE A  79     7348   7171   9618   1163   -120    -89       N  
ATOM    616  CA  PHE A  79     -32.531  27.411  10.903  1.00 61.65           C  
ANISOU  616  CA  PHE A  79     6984   6922   9518    999   -134    -21       C  
ATOM    617  C   PHE A  79     -34.050  27.232  10.977  1.00 61.20           C  
ANISOU  617  C   PHE A  79     7014   6724   9512    910   -281    -21       C  
ATOM    618  O   PHE A  79     -34.543  26.850  12.055  1.00 60.61           O  
ANISOU  618  O   PHE A  79     6899   6587   9542    848   -354    -16       O  
ATOM    619  CB  PHE A  79     -32.186  28.876  10.621  1.00 61.00           C  
ANISOU  619  CB  PHE A  79     6798   6946   9433    926    -24     52       C  
ATOM    620  CG  PHE A  79     -32.650  29.813  11.710  1.00 59.13           C  
ANISOU  620  CG  PHE A  79     6439   6695   9330    780    -38    110       C  
ATOM    621  CD1 PHE A  79     -31.858  30.065  12.819  1.00 58.64           C  
ANISOU  621  CD1 PHE A  79     6233   6697   9350    752     18    135       C  
ATOM    622  CD2 PHE A  79     -33.896  30.411  11.653  1.00 57.94           C  
ANISOU  622  CD2 PHE A  79     6323   6466   9225    680   -115    136       C  
ATOM    623  CE1 PHE A  79     -32.292  30.908  13.831  1.00 57.04           C  
ANISOU  623  CE1 PHE A  79     5937   6478   9259    630      0    179       C  
ATOM    624  CE2 PHE A  79     -34.327  31.256  12.665  1.00 56.66           C  
ANISOU  624  CE2 PHE A  79     6055   6294   9178    566   -126    180       C  
ATOM    625  CZ  PHE A  79     -33.526  31.502  13.752  1.00 55.98           C  
ANISOU  625  CZ  PHE A  79     5840   6268   9160    543    -68    198       C  
ATOM    626  N   LEU A  80     -34.750  27.497   9.868  1.00 61.99           N  
ANISOU  626  N   LEU A  80     7228   6786   9539    903   -322    -20       N  
ATOM    627  CA  LEU A  80     -36.237  27.563   9.797  1.00 61.83           C  
ANISOU  627  CA  LEU A  80     7272   6649   9569    806   -457     -3       C  
ATOM    628  C   LEU A  80     -36.845  26.236  10.258  1.00 61.50           C  
ANISOU  628  C   LEU A  80     7312   6486   9567    816   -598    -45       C  
ATOM    629  O   LEU A  80     -37.750  26.271  11.113  1.00 60.85           O  
ANISOU  629  O   LEU A  80     7173   6348   9598    710   -674     -9       O  
ATOM    630  CB  LEU A  80     -36.679  27.903   8.370  1.00 63.17           C  
ANISOU  630  CB  LEU A  80     7571   6800   9628    825   -481     -5       C  
ATOM    631  CG  LEU A  80     -36.725  29.397   8.048  1.00 63.28           C  
ANISOU  631  CG  LEU A  80     7508   6885   9647    747   -403     63       C  
ATOM    632  CD1 LEU A  80     -35.453  29.849   7.342  1.00 64.25           C  
ANISOU  632  CD1 LEU A  80     7613   7140   9658    823   -254     72       C  
ATOM    633  CD2 LEU A  80     -37.950  29.728   7.212  1.00 63.96           C  
ANISOU  633  CD2 LEU A  80     7699   6888   9713    692   -511     82       C  
ATOM    634  N   GLY A  81     -36.367  25.120   9.706  1.00 62.22           N  
ANISOU  634  N   GLY A  81     7534   6540   9564    943   -631   -115       N  
ATOM    635  CA  GLY A  81     -36.742  23.763  10.141  1.00 61.71           C  
ANISOU  635  CA  GLY A  81     7561   6354   9529    966   -770   -157       C  
ATOM    636  C   GLY A  81     -36.881  23.696  11.649  1.00 60.19           C  
ANISOU  636  C   GLY A  81     7230   6159   9478    873   -782   -116       C  
ATOM    637  O   GLY A  81     -37.951  23.287  12.118  1.00 60.27           O  
ANISOU  637  O   GLY A  81     7261   6073   9565    780   -910    -89       O  
ATOM    638  N   ARG A  82     -35.854  24.132  12.384  1.00 59.55           N  
ANISOU  638  N   ARG A  82     7008   6188   9430    892   -654   -103       N  
ATOM    639  CA  ARG A  82     -35.740  23.951  13.860  1.00 58.91           C  
ANISOU  639  CA  ARG A  82     6807   6112   9464    829   -658    -74       C  
ATOM    640  C   ARG A  82     -36.596  24.998  14.587  1.00 57.16           C  
ANISOU  640  C   ARG A  82     6463   5909   9342    679   -649     -2       C  
ATOM    641  O   ARG A  82     -37.174  24.659  15.641  1.00 56.09           O  
ANISOU  641  O   ARG A  82     6282   5731   9296    600   -714     25       O  
ATOM    642  CB  ARG A  82     -34.269  24.005  14.286  1.00 59.12           C  
ANISOU  642  CB  ARG A  82     6738   6246   9479    915   -534    -90       C  
ATOM    643  CG  ARG A  82     -33.421  22.890  13.688  1.00 60.33           C  
ANISOU  643  CG  ARG A  82     7001   6383   9537   1083   -543   -165       C  
ATOM    644  CD  ARG A  82     -32.023  22.812  14.272  1.00 60.63           C  
ANISOU  644  CD  ARG A  82     6927   6524   9585   1166   -438   -175       C  
ATOM    645  NE  ARG A  82     -31.184  23.880  13.738  1.00 60.55           N  
ANISOU  645  NE  ARG A  82     6817   6660   9526   1191   -282   -149       N  
ATOM    646  CZ  ARG A  82     -31.058  25.097  14.261  1.00 59.19           C  
ANISOU  646  CZ  ARG A  82     6495   6572   9419   1081   -200    -80       C  
ATOM    647  NH1 ARG A  82     -31.712  25.437  15.361  1.00 57.89           N  
ANISOU  647  NH1 ARG A  82     6261   6368   9366    951   -249    -39       N  
ATOM    648  NH2 ARG A  82     -30.299  25.997  13.645  1.00 59.58           N  
ANISOU  648  NH2 ARG A  82     6472   6747   9417   1102    -72    -51       N  
ATOM    649  N   TYR A  83     -36.657  26.219  14.045  1.00 56.55           N  
ANISOU  649  N   TYR A  83     6340   5897   9247    646   -571     26       N  
ATOM    650  CA  TYR A  83     -37.553  27.319  14.492  1.00 55.00           C  
ANISOU  650  CA  TYR A  83     6053   5712   9133    523   -569     86       C  
ATOM    651  C   TYR A  83     -39.012  26.882  14.286  1.00 54.91           C  
ANISOU  651  C   TYR A  83     6116   5594   9151    459   -710    100       C  
ATOM    652  O   TYR A  83     -39.818  26.997  15.235  1.00 54.36           O  
ANISOU  652  O   TYR A  83     5968   5507   9177    368   -751    141       O  
ATOM    653  CB  TYR A  83     -37.185  28.617  13.762  1.00 54.87           C  
ANISOU  653  CB  TYR A  83     6002   5773   9073    520   -470    109       C  
ATOM    654  CG  TYR A  83     -38.214  29.713  13.852  1.00 53.82           C  
ANISOU  654  CG  TYR A  83     5819   5627   9001    419   -490    158       C  
ATOM    655  CD1 TYR A  83     -38.842  29.993  15.052  1.00 53.08           C  
ANISOU  655  CD1 TYR A  83     5626   5525   9014    337   -512    189       C  
ATOM    656  CD2 TYR A  83     -38.561  30.468  12.743  1.00 53.89           C  
ANISOU  656  CD2 TYR A  83     5883   5635   8958    412   -488    175       C  
ATOM    657  CE1 TYR A  83     -39.798  30.987  15.148  1.00 52.86           C  
ANISOU  657  CE1 TYR A  83     5552   5488   9042    262   -530    228       C  
ATOM    658  CE2 TYR A  83     -39.516  31.467  12.821  1.00 53.64           C  
ANISOU  658  CE2 TYR A  83     5808   5585   8987    330   -516    218       C  
ATOM    659  CZ  TYR A  83     -40.138  31.726  14.030  1.00 53.20           C  
ANISOU  659  CZ  TYR A  83     5650   5522   9041    260   -536    242       C  
ATOM    660  OH  TYR A  83     -41.084  32.702  14.151  1.00 53.34           O  
ANISOU  660  OH  TYR A  83     5620   5525   9118    197   -561    278       O  
ATOM    661  N   MET A  84     -39.334  26.364  13.097  1.00 55.47           N  
ANISOU  661  N   MET A  84     6334   5599   9142    508   -786     70       N  
ATOM    662  CA  MET A  84     -40.694  25.869  12.740  1.00 56.11           C  
ANISOU  662  CA  MET A  84     6501   5572   9245    447   -940     86       C  
ATOM    663  C   MET A  84     -41.019  24.567  13.491  1.00 55.83           C  
ANISOU  663  C   MET A  84     6498   5454   9260    427  -1053     82       C  
ATOM    664  O   MET A  84     -42.218  24.321  13.728  1.00 55.97           O  
ANISOU  664  O   MET A  84     6513   5406   9344    332  -1168    127       O  
ATOM    665  CB  MET A  84     -40.829  25.628  11.231  1.00 57.64           C  
ANISOU  665  CB  MET A  84     6862   5712   9324    512   -998     48       C  
ATOM    666  CG  MET A  84     -41.093  26.894  10.422  1.00 58.00           C  
ANISOU  666  CG  MET A  84     6893   5804   9339    487   -946     78       C  
ATOM    667  SD  MET A  84     -42.679  27.697  10.819  1.00 57.78           S  
ANISOU  667  SD  MET A  84     6772   5744   9435    344  -1026    155       S  
ATOM    668  CE  MET A  84     -42.106  29.125  11.737  1.00 56.71           C  
ANISOU  668  CE  MET A  84     6450   5730   9365    310   -863    192       C  
ATOM    669  N   SER A  85     -40.011  23.757  13.838  1.00 55.29           N  
ANISOU  669  N   SER A  85     6458   5388   9162    509  -1029     37       N  
ATOM    670  CA  SER A  85     -40.171  22.476  14.580  1.00 54.83           C  
ANISOU  670  CA  SER A  85     6442   5244   9145    496  -1139     34       C  
ATOM    671  C   SER A  85     -40.307  22.752  16.077  1.00 53.02           C  
ANISOU  671  C   SER A  85     6052   5068   9025    403  -1099     92       C  
ATOM    672  O   SER A  85     -40.935  21.929  16.769  1.00 53.33           O  
ANISOU  672  O   SER A  85     6100   5039   9122    335  -1207    126       O  
ATOM    673  CB  SER A  85     -39.029  21.542  14.318  1.00 55.98           C  
ANISOU  673  CB  SER A  85     6687   5369   9213    635  -1133    -39       C  
ATOM    674  OG  SER A  85     -39.025  21.139  12.958  1.00 57.64           O  
ANISOU  674  OG  SER A  85     7069   5519   9313    727  -1189    -98       O  
ATOM    675  N   ALA A  86     -39.708  23.847  16.550  1.00 51.22           N  
ANISOU  675  N   ALA A  86     5689   4954   8816    400   -955    104       N  
ATOM    676  CA  ALA A  86     -39.770  24.305  17.957  1.00 49.59           C  
ANISOU  676  CA  ALA A  86     5333   4809   8698    321   -901    152       C  
ATOM    677  C   ALA A  86     -41.076  25.073  18.172  1.00 48.41           C  
ANISOU  677  C   ALA A  86     5111   4668   8614    211   -924    213       C  
ATOM    678  O   ALA A  86     -41.735  24.803  19.194  1.00 47.44           O  
ANISOU  678  O   ALA A  86     4922   4541   8561    130   -964    261       O  
ATOM    679  CB  ALA A  86     -38.560  25.141  18.294  1.00 49.21           C  
ANISOU  679  CB  ALA A  86     5191   4868   8639    367   -754    137       C  
ATOM    680  N   LEU A  87     -41.429  25.971  17.238  1.00 47.91           N  
ANISOU  680  N   LEU A  87     5059   4618   8524    212   -900    213       N  
ATOM    681  CA  LEU A  87     -42.683  26.780  17.253  1.00 47.69           C  
ANISOU  681  CA  LEU A  87     4967   4597   8556    127   -925    266       C  
ATOM    682  C   LEU A  87     -43.892  25.859  17.436  1.00 48.34           C  
ANISOU  682  C   LEU A  87     5075   4603   8687     53  -1068    309       C  
ATOM    683  O   LEU A  87     -44.729  26.147  18.315  1.00 47.47           O  
ANISOU  683  O   LEU A  87     4854   4525   8654    -27  -1072    366       O  
ATOM    684  CB  LEU A  87     -42.806  27.565  15.942  1.00 47.95           C  
ANISOU  684  CB  LEU A  87     5059   4626   8534    157   -914    252       C  
ATOM    685  CG  LEU A  87     -44.126  28.310  15.730  1.00 47.47           C  
ANISOU  685  CG  LEU A  87     4952   4555   8527     85   -963    301       C  
ATOM    686  CD1 LEU A  87     -44.396  29.280  16.871  1.00 46.66           C  
ANISOU  686  CD1 LEU A  87     4695   4527   8504     37   -885    337       C  
ATOM    687  CD2 LEU A  87     -44.127  29.040  14.396  1.00 47.56           C  
ANISOU  687  CD2 LEU A  87     5039   4557   8474    120   -958    288       C  
ATOM    688  N   ASN A  88     -43.940  24.794  16.629  1.00 49.77           N  
ANISOU  688  N   ASN A  88     5402   4689   8819     83  -1180    283       N  
ATOM    689  CA  ASN A  88     -44.990  23.740  16.590  1.00 51.01           C  
ANISOU  689  CA  ASN A  88     5619   4748   9011     11  -1347    324       C  
ATOM    690  C   ASN A  88     -45.322  23.214  17.995  1.00 51.39           C  
ANISOU  690  C   ASN A  88     5571   4814   9140    -70  -1367    383       C  
ATOM    691  O   ASN A  88     -46.434  22.676  18.152  1.00 52.18           O  
ANISOU  691  O   ASN A  88     5663   4866   9295   -165  -1487    449       O  
ATOM    692  CB  ASN A  88     -44.563  22.588  15.676  1.00 52.15           C  
ANISOU  692  CB  ASN A  88     5955   4782   9075     84  -1453    266       C  
ATOM    693  CG  ASN A  88     -45.720  21.727  15.217  1.00 53.25           C  
ANISOU  693  CG  ASN A  88     6190   4805   9238      9  -1646    304       C  
ATOM    694  OD1 ASN A  88     -45.816  21.394  14.040  1.00 54.39           O  
ANISOU  694  OD1 ASN A  88     6486   4867   9312     55  -1734    264       O  
ATOM    695  ND2 ASN A  88     -46.604  21.362  16.132  1.00 53.15           N  
ANISOU  695  ND2 ASN A  88     6089   4786   9319   -107  -1715    387       N  
ATOM    696  N   HIS A  89     -44.408  23.317  18.969  1.00 51.71           N  
ANISOU  696  N   HIS A  89     5542   4919   9184    -41  -1262    367       N  
ATOM    697  CA  HIS A  89     -44.647  22.930  20.389  1.00 52.32           C  
ANISOU  697  CA  HIS A  89     5524   5029   9326   -117  -1264    425       C  
ATOM    698  C   HIS A  89     -44.923  24.174  21.246  1.00 51.65           C  
ANISOU  698  C   HIS A  89     5274   5062   9287   -154  -1140    458       C  
ATOM    699  O   HIS A  89     -45.843  24.113  22.094  1.00 51.93           O  
ANISOU  699  O   HIS A  89     5216   5131   9383   -244  -1162    530       O  
ATOM    700  CB  HIS A  89     -43.470  22.125  20.964  1.00 52.84           C  
ANISOU  700  CB  HIS A  89     5636   5077   9363    -59  -1250    386       C  
ATOM    701  CG  HIS A  89     -43.137  20.878  20.211  1.00 54.48           C  
ANISOU  701  CG  HIS A  89     6014   5164   9522     -3  -1372    344       C  
ATOM    702  ND1 HIS A  89     -42.263  20.873  19.134  1.00 54.90           N  
ANISOU  702  ND1 HIS A  89     6174   5193   9492    120  -1346    259       N  
ATOM    703  CD2 HIS A  89     -43.531  19.596  20.383  1.00 55.71           C  
ANISOU  703  CD2 HIS A  89     6258   5214   9694    -48  -1524    373       C  
ATOM    704  CE1 HIS A  89     -42.148  19.645  18.667  1.00 56.18           C  
ANISOU  704  CE1 HIS A  89     6489   5237   9618    162  -1475    228       C  
ATOM    705  NE2 HIS A  89     -42.915  18.841  19.419  1.00 56.70           N  
ANISOU  705  NE2 HIS A  89     6551   5242   9747     56  -1594    297       N  
ATOM    706  N   THR A  90     -44.163  25.257  21.046  1.00 50.95           N  
ANISOU  706  N   THR A  90     5151   5036   9169    -89  -1018    410       N  
ATOM    707  CA  THR A  90     -44.128  26.429  21.966  1.00 50.39           C  
ANISOU  707  CA  THR A  90     4945   5067   9131   -105   -899    424       C  
ATOM    708  C   THR A  90     -45.477  27.150  21.939  1.00 50.86           C  
ANISOU  708  C   THR A  90     4925   5155   9242   -164   -913    475       C  
ATOM    709  O   THR A  90     -45.787  27.826  22.943  1.00 50.51           O  
ANISOU  709  O   THR A  90     4768   5189   9235   -191   -844    500       O  
ATOM    710  CB  THR A  90     -42.975  27.391  21.650  1.00 49.59           C  
ANISOU  710  CB  THR A  90     4842   5012   8988    -30   -786    367       C  
ATOM    711  OG1 THR A  90     -43.123  27.857  20.308  1.00 49.67           O  
ANISOU  711  OG1 THR A  90     4916   4993   8963      2   -799    346       O  
ATOM    712  CG2 THR A  90     -41.615  26.758  21.852  1.00 49.37           C  
ANISOU  712  CG2 THR A  90     4856   4980   8919     31   -758    324       C  
ATOM    713  N   LYS A  91     -46.239  26.994  20.847  1.00 51.68           N  
ANISOU  713  N   LYS A  91     5089   5199   9346   -177  -1003    487       N  
ATOM    714  CA  LYS A  91     -47.587  27.599  20.646  1.00 51.66           C  
ANISOU  714  CA  LYS A  91     5014   5216   9398   -228  -1038    540       C  
ATOM    715  C   LYS A  91     -48.664  26.781  21.381  1.00 52.09           C  
ANISOU  715  C   LYS A  91     5002   5275   9514   -322  -1119    623       C  
ATOM    716  O   LYS A  91     -49.844  27.177  21.292  1.00 52.95           O  
ANISOU  716  O   LYS A  91     5030   5411   9676   -368  -1152    678       O  
ATOM    717  CB  LYS A  91     -47.912  27.700  19.151  1.00 52.19           C  
ANISOU  717  CB  LYS A  91     5181   5212   9437   -207  -1115    524       C  
ATOM    718  CG  LYS A  91     -48.106  26.363  18.447  1.00 53.50           C  
ANISOU  718  CG  LYS A  91     5474   5272   9578   -228  -1260    529       C  
ATOM    719  CD  LYS A  91     -48.905  26.426  17.166  1.00 54.78           C  
ANISOU  719  CD  LYS A  91     5713   5368   9733   -240  -1369    539       C  
ATOM    720  CE  LYS A  91     -49.419  25.063  16.743  1.00 56.19           C  
ANISOU  720  CE  LYS A  91     5999   5439   9911   -290  -1540    565       C  
ATOM    721  NZ  LYS A  91     -50.054  25.098  15.403  1.00 57.19           N  
ANISOU  721  NZ  LYS A  91     6225   5489  10014   -292  -1655    565       N  
ATOM    722  N   LYS A  92     -48.290  25.679  22.049  1.00 51.57           N  
ANISOU  722  N   LYS A  92     4965   5185   9442   -352  -1156    638       N  
ATOM    723  CA  LYS A  92     -49.195  24.868  22.912  1.00 51.85           C  
ANISOU  723  CA  LYS A  92     4932   5236   9531   -454  -1224    731       C  
ATOM    724  C   LYS A  92     -48.858  25.101  24.387  1.00 50.64           C  
ANISOU  724  C   LYS A  92     4675   5181   9383   -463  -1115    747       C  
ATOM    725  O   LYS A  92     -49.741  24.862  25.229  1.00 50.89           O  
ANISOU  725  O   LYS A  92     4605   5273   9458   -543  -1126    832       O  
ATOM    726  CB  LYS A  92     -49.086  23.373  22.593  1.00 53.12           C  
ANISOU  726  CB  LYS A  92     5220   5282   9680   -493  -1370    747       C  
ATOM    727  CG  LYS A  92     -49.784  22.920  21.318  1.00 53.93           C  
ANISOU  727  CG  LYS A  92     5420   5282   9787   -518  -1519    759       C  
ATOM    728  CD  LYS A  92     -49.116  21.726  20.672  1.00 54.54           C  
ANISOU  728  CD  LYS A  92     5684   5226   9812   -486  -1635    713       C  
ATOM    729  CE  LYS A  92     -49.810  21.273  19.407  1.00 55.51           C  
ANISOU  729  CE  LYS A  92     5923   5238   9930   -510  -1794    720       C  
ATOM    730  NZ  LYS A  92     -48.901  20.484  18.547  1.00 55.89           N  
ANISOU  730  NZ  LYS A  92     6173   5167   9896   -422  -1864    632       N  
ATOM    731  N   TRP A  93     -47.626  25.517  24.690  1.00 49.49           N  
ANISOU  731  N   TRP A  93     4554   5055   9193   -387  -1017    674       N  
ATOM    732  CA  TRP A  93     -47.230  25.963  26.052  1.00 48.77           C  
ANISOU  732  CA  TRP A  93     4373   5058   9098   -384   -907    677       C  
ATOM    733  C   TRP A  93     -48.173  27.090  26.476  1.00 47.61           C  
ANISOU  733  C   TRP A  93     4096   5009   8984   -394   -834    706       C  
ATOM    734  O   TRP A  93     -48.626  27.847  25.593  1.00 46.98           O  
ANISOU  734  O   TRP A  93     4011   4920   8920   -366   -836    689       O  
ATOM    735  CB  TRP A  93     -45.768  26.434  26.114  1.00 48.68           C  
ANISOU  735  CB  TRP A  93     4406   5050   9040   -300   -822    592       C  
ATOM    736  CG  TRP A  93     -44.720  25.375  25.927  1.00 49.19           C  
ANISOU  736  CG  TRP A  93     4578   5042   9069   -270   -872    559       C  
ATOM    737  CD1 TRP A  93     -44.886  24.019  25.891  1.00 49.65           C  
ANISOU  737  CD1 TRP A  93     4708   5023   9131   -310   -988    593       C  
ATOM    738  CD2 TRP A  93     -43.306  25.608  25.779  1.00 48.75           C  
ANISOU  738  CD2 TRP A  93     4566   4983   8972   -187   -810    487       C  
ATOM    739  NE1 TRP A  93     -43.679  23.398  25.709  1.00 49.52           N  
ANISOU  739  NE1 TRP A  93     4785   4954   9076   -243  -1001    538       N  
ATOM    740  CE2 TRP A  93     -42.693  24.347  25.638  1.00 48.84           C  
ANISOU  740  CE2 TRP A  93     4674   4920   8962   -167   -888    475       C  
ATOM    741  CE3 TRP A  93     -42.508  26.759  25.737  1.00 48.23           C  
ANISOU  741  CE3 TRP A  93     4466   4970   8887   -130   -704    437       C  
ATOM    742  CZ2 TRP A  93     -41.318  24.211  25.468  1.00 48.82           C  
ANISOU  742  CZ2 TRP A  93     4720   4908   8921    -81   -851    413       C  
ATOM    743  CZ3 TRP A  93     -41.149  26.623  25.568  1.00 47.93           C  
ANISOU  743  CZ3 TRP A  93     4472   4923   8813    -62   -671    386       C  
ATOM    744  CH2 TRP A  93     -40.565  25.363  25.436  1.00 48.54           C  
ANISOU  744  CH2 TRP A  93     4631   4940   8871    -33   -738    373       C  
ATOM    745  N   LYS A  94     -48.447  27.185  27.777  1.00 46.93           N  
ANISOU  745  N   LYS A  94     3914   5013   8904   -425   -773    747       N  
ATOM    746  CA  LYS A  94     -49.243  28.279  28.386  1.00 46.64           C  
ANISOU  746  CA  LYS A  94     3751   5083   8885   -412   -685    764       C  
ATOM    747  C   LYS A  94     -48.263  29.322  28.927  1.00 45.04           C  
ANISOU  747  C   LYS A  94     3552   4916   8643   -335   -574    684       C  
ATOM    748  O   LYS A  94     -47.258  28.911  29.548  1.00 44.18           O  
ANISOU  748  O   LYS A  94     3487   4798   8498   -331   -555    661       O  
ATOM    749  CB  LYS A  94     -50.181  27.730  29.469  1.00 47.92           C  
ANISOU  749  CB  LYS A  94     3808   5332   9065   -489   -685    861       C  
ATOM    750  CG  LYS A  94     -51.430  27.031  28.946  1.00 49.18           C  
ANISOU  750  CG  LYS A  94     3924   5480   9281   -573   -789    956       C  
ATOM    751  CD  LYS A  94     -52.549  27.981  28.548  1.00 49.59           C  
ANISOU  751  CD  LYS A  94     3870   5592   9377   -550   -766    976       C  
ATOM    752  CE  LYS A  94     -53.128  27.683  27.178  1.00 50.33           C  
ANISOU  752  CE  LYS A  94     4008   5597   9515   -580   -890    997       C  
ATOM    753  NZ  LYS A  94     -52.445  28.454  26.108  1.00 49.65           N  
ANISOU  753  NZ  LYS A  94     4022   5434   9408   -494   -882    898       N  
ATOM    754  N   TYR A  95     -48.553  30.604  28.678  1.00 44.07           N  
ANISOU  754  N   TYR A  95     3389   4823   8530   -279   -517    647       N  
ATOM    755  CA  TYR A  95     -47.714  31.773  29.049  1.00 42.95           C  
ANISOU  755  CA  TYR A  95     3259   4700   8357   -209   -429    573       C  
ATOM    756  C   TYR A  95     -48.491  32.723  29.948  1.00 42.19           C  
ANISOU  756  C   TYR A  95     3065   4698   8265   -177   -355    577       C  
ATOM    757  O   TYR A  95     -48.822  33.832  29.543  1.00 41.54           O  
ANISOU  757  O   TYR A  95     2968   4616   8199   -123   -331    544       O  
ATOM    758  CB  TYR A  95     -47.255  32.517  27.798  1.00 43.09           C  
ANISOU  758  CB  TYR A  95     3343   4649   8378   -162   -441    519       C  
ATOM    759  CG  TYR A  95     -46.463  31.669  26.843  1.00 43.37           C  
ANISOU  759  CG  TYR A  95     3479   4603   8396   -172   -501    506       C  
ATOM    760  CD1 TYR A  95     -45.093  31.517  26.985  1.00 42.95           C  
ANISOU  760  CD1 TYR A  95     3483   4529   8304   -148   -473    462       C  
ATOM    761  CD2 TYR A  95     -47.092  31.015  25.799  1.00 44.00           C  
ANISOU  761  CD2 TYR A  95     3597   4627   8494   -198   -590    536       C  
ATOM    762  CE1 TYR A  95     -44.364  30.732  26.107  1.00 43.18           C  
ANISOU  762  CE1 TYR A  95     3601   4493   8311   -138   -520    445       C  
ATOM    763  CE2 TYR A  95     -46.373  30.239  24.906  1.00 44.21           C  
ANISOU  763  CE2 TYR A  95     3728   4576   8491   -191   -645    515       C  
ATOM    764  CZ  TYR A  95     -45.008  30.094  25.062  1.00 43.61           C  
ANISOU  764  CZ  TYR A  95     3704   4489   8373   -154   -604    467       C  
ATOM    765  OH  TYR A  95     -44.316  29.314  24.187  1.00 44.14           O  
ANISOU  765  OH  TYR A  95     3872   4491   8407   -130   -652    442       O  
ATOM    766  N   PRO A  96     -48.787  32.329  31.203  1.00 42.05           N  
ANISOU  766  N   PRO A  96     2986   4762   8226   -204   -316    615       N  
ATOM    767  CA  PRO A  96     -49.485  33.217  32.127  1.00 42.48           C  
ANISOU  767  CA  PRO A  96     2953   4917   8268   -157   -235    612       C  
ATOM    768  C   PRO A  96     -48.613  34.410  32.541  1.00 42.03           C  
ANISOU  768  C   PRO A  96     2945   4850   8173    -80   -172    521       C  
ATOM    769  O   PRO A  96     -47.415  34.253  32.674  1.00 41.64           O  
ANISOU  769  O   PRO A  96     2972   4754   8096    -88   -176    484       O  
ATOM    770  CB  PRO A  96     -49.793  32.311  33.328  1.00 42.98           C  
ANISOU  770  CB  PRO A  96     2961   5066   8301   -214   -213    681       C  
ATOM    771  CG  PRO A  96     -48.699  31.265  33.284  1.00 42.48           C  
ANISOU  771  CG  PRO A  96     2991   4928   8221   -268   -268    682       C  
ATOM    772  CD  PRO A  96     -48.453  31.031  31.809  1.00 42.04           C  
ANISOU  772  CD  PRO A  96     3003   4763   8205   -273   -348    664       C  
ATOM    773  N   GLN A  97     -49.240  35.573  32.704  1.00 42.41           N  
ANISOU  773  N   GLN A  97     2949   4938   8225     -7   -126    489       N  
ATOM    774  CA  GLN A  97     -48.683  36.701  33.489  1.00 42.79           C  
ANISOU  774  CA  GLN A  97     3032   4997   8227     64    -66    412       C  
ATOM    775  C   GLN A  97     -48.484  36.193  34.916  1.00 43.16           C  
ANISOU  775  C   GLN A  97     3061   5123   8211     47    -16    427       C  
ATOM    776  O   GLN A  97     -49.384  35.478  35.412  1.00 43.93           O  
ANISOU  776  O   GLN A  97     3074   5310   8305     14      1    499       O  
ATOM    777  CB  GLN A  97     -49.623  37.909  33.499  1.00 43.67           C  
ANISOU  777  CB  GLN A  97     3094   5143   8353    156    -31    381       C  
ATOM    778  CG  GLN A  97     -50.081  38.347  32.116  1.00 43.65           C  
ANISOU  778  CG  GLN A  97     3094   5073   8415    169    -87    383       C  
ATOM    779  CD  GLN A  97     -48.912  38.667  31.222  1.00 42.85           C  
ANISOU  779  CD  GLN A  97     3104   4856   8318    153   -132    340       C  
ATOM    780  OE1 GLN A  97     -48.662  37.992  30.221  1.00 41.97           O  
ANISOU  780  OE1 GLN A  97     3024   4690   8232     98   -187    370       O  
ATOM    781  NE2 GLN A  97     -48.171  39.693  31.611  1.00 43.21           N  
ANISOU  781  NE2 GLN A  97     3212   4869   8336    201   -109    272       N  
ATOM    782  N   VAL A  98     -47.352  36.519  35.533  1.00 42.40           N  
ANISOU  782  N   VAL A  98     3041   4999   8069     59     -2    371       N  
ATOM    783  CA  VAL A  98     -47.061  36.170  36.953  1.00 42.90           C  
ANISOU  783  CA  VAL A  98     3106   5132   8060     49     39    376       C  
ATOM    784  C   VAL A  98     -46.315  37.360  37.562  1.00 43.12           C  
ANISOU  784  C   VAL A  98     3206   5134   8042    117     63    286       C  
ATOM    785  O   VAL A  98     -45.081  37.471  37.339  1.00 42.58           O  
ANISOU  785  O   VAL A  98     3214   4985   7978     94     24    251       O  
ATOM    786  CB  VAL A  98     -46.265  34.851  37.073  1.00 42.49           C  
ANISOU  786  CB  VAL A  98     3087   5054   8003    -37     -4    422       C  
ATOM    787  CG1 VAL A  98     -46.024  34.459  38.527  1.00 42.82           C  
ANISOU  787  CG1 VAL A  98     3134   5167   7968    -54     31    437       C  
ATOM    788  CG2 VAL A  98     -46.929  33.704  36.321  1.00 42.36           C  
ANISOU  788  CG2 VAL A  98     3026   5032   8037   -106    -54    505       C  
ATOM    789  N   ASN A  99     -47.040  38.227  38.275  1.00 43.59           N  
ANISOU  789  N   ASN A  99     3241   5260   8061    199    121    251       N  
ATOM    790  CA  ASN A  99     -46.476  39.430  38.942  1.00 43.64           C  
ANISOU  790  CA  ASN A  99     3329   5237   8016    273    133    159       C  
ATOM    791  C   ASN A  99     -45.925  40.372  37.862  1.00 42.70           C  
ANISOU  791  C   ASN A  99     3272   4997   7955    291     78    109       C  
ATOM    792  O   ASN A  99     -44.839  40.940  38.064  1.00 42.65           O  
ANISOU  792  O   ASN A  99     3352   4920   7931    287     45     58       O  
ATOM    793  CB  ASN A  99     -45.420  39.031  39.980  1.00 43.67           C  
ANISOU  793  CB  ASN A  99     3397   5242   7953    233    128    148       C  
ATOM    794  CG  ASN A  99     -45.256  40.046  41.091  1.00 44.60           C  
ANISOU  794  CG  ASN A  99     3580   5375   7987    314    155     70       C  
ATOM    795  OD1 ASN A  99     -46.238  40.605  41.584  1.00 45.83           O  
ANISOU  795  OD1 ASN A  99     3705   5604   8101    402    213     46       O  
ATOM    796  ND2 ASN A  99     -44.020  40.276  41.503  1.00 44.07           N  
ANISOU  796  ND2 ASN A  99     3605   5242   7895    288    109     29       N  
ATOM    797  N   GLY A 100     -46.651  40.505  36.749  1.00 42.30           N  
ANISOU  797  N   GLY A 100     3175   4925   7970    301     62    132       N  
ATOM    798  CA  GLY A 100     -46.410  41.501  35.688  1.00 41.70           C  
ANISOU  798  CA  GLY A 100     3150   4747   7945    327     14     93       C  
ATOM    799  C   GLY A 100     -45.539  40.960  34.574  1.00 40.64           C  
ANISOU  799  C   GLY A 100     3046   4536   7858    244    -38    124       C  
ATOM    800  O   GLY A 100     -45.214  41.752  33.663  1.00 40.69           O  
ANISOU  800  O   GLY A 100     3099   4460   7899    252    -77    102       O  
ATOM    801  N   LEU A 101     -45.186  39.669  34.627  1.00 40.06           N  
ANISOU  801  N   LEU A 101     2950   4489   7780    171    -41    175       N  
ATOM    802  CA  LEU A 101     -44.143  39.054  33.761  1.00 38.95           C  
ANISOU  802  CA  LEU A 101     2848   4284   7665    106    -85    195       C  
ATOM    803  C   LEU A 101     -44.660  37.770  33.114  1.00 38.83           C  
ANISOU  803  C   LEU A 101     2789   4285   7678     58   -105    260       C  
ATOM    804  O   LEU A 101     -45.315  36.960  33.808  1.00 39.02           O  
ANISOU  804  O   LEU A 101     2760   4378   7686     38    -87    303       O  
ATOM    805  CB  LEU A 101     -42.901  38.749  34.600  1.00 38.53           C  
ANISOU  805  CB  LEU A 101     2836   4229   7574     74    -86    180       C  
ATOM    806  CG  LEU A 101     -42.236  39.953  35.253  1.00 38.55           C  
ANISOU  806  CG  LEU A 101     2896   4201   7548    106    -87    119       C  
ATOM    807  CD1 LEU A 101     -41.193  39.491  36.252  1.00 38.61           C  
ANISOU  807  CD1 LEU A 101     2931   4223   7515     71    -93    115       C  
ATOM    808  CD2 LEU A 101     -41.623  40.867  34.207  1.00 38.23           C  
ANISOU  808  CD2 LEU A 101     2901   4076   7547    103   -124     99       C  
ATOM    809  N   THR A 102     -44.321  37.590  31.836  1.00 38.56           N  
ANISOU  809  N   THR A 102     2785   4188   7678     36   -146    271       N  
ATOM    810  CA  THR A 102     -44.621  36.381  31.037  1.00 38.49           C  
ANISOU  810  CA  THR A 102     2765   4166   7691     -8   -186    322       C  
ATOM    811  C   THR A 102     -43.634  35.283  31.442  1.00 38.39           C  
ANISOU  811  C   THR A 102     2779   4150   7654    -49   -198    335       C  
ATOM    812  O   THR A 102     -42.486  35.292  30.957  1.00 37.60           O  
ANISOU  812  O   THR A 102     2729   4005   7549    -50   -209    312       O  
ATOM    813  CB  THR A 102     -44.595  36.675  29.532  1.00 38.25           C  
ANISOU  813  CB  THR A 102     2772   4069   7690     -2   -224    320       C  
ATOM    814  OG1 THR A 102     -45.541  37.705  29.245  1.00 38.60           O  
ANISOU  814  OG1 THR A 102     2792   4115   7760     38   -221    310       O  
ATOM    815  CG2 THR A 102     -44.930  35.456  28.703  1.00 38.32           C  
ANISOU  815  CG2 THR A 102     2790   4056   7714    -41   -277    364       C  
ATOM    816  N   SER A 103     -44.082  34.392  32.326  1.00 39.10           N  
ANISOU  816  N   SER A 103     2834   4292   7730    -80   -196    375       N  
ATOM    817  CA  SER A 103     -43.448  33.085  32.619  1.00 39.24           C  
ANISOU  817  CA  SER A 103     2875   4299   7734   -125   -229    404       C  
ATOM    818  C   SER A 103     -43.926  32.072  31.573  1.00 39.86           C  
ANISOU  818  C   SER A 103     2967   4332   7843   -156   -294    446       C  
ATOM    819  O   SER A 103     -44.399  32.500  30.502  1.00 40.19           O  
ANISOU  819  O   SER A 103     3014   4342   7911   -140   -311    440       O  
ATOM    820  CB  SER A 103     -43.770  32.646  34.016  1.00 39.48           C  
ANISOU  820  CB  SER A 103     2868   4399   7730   -150   -205    436       C  
ATOM    821  OG  SER A 103     -42.941  31.568  34.404  1.00 39.46           O  
ANISOU  821  OG  SER A 103     2903   4377   7712   -186   -240    455       O  
ATOM    822  N   ILE A 104     -43.781  30.779  31.856  1.00 40.59           N  
ANISOU  822  N   ILE A 104     3079   4414   7930   -200   -340    486       N  
ATOM    823  CA  ILE A 104     -44.413  29.672  31.078  1.00 41.59           C  
ANISOU  823  CA  ILE A 104     3225   4494   8083   -242   -421    536       C  
ATOM    824  C   ILE A 104     -44.924  28.627  32.082  1.00 42.60           C  
ANISOU  824  C   ILE A 104     3323   4659   8205   -309   -450    608       C  
ATOM    825  O   ILE A 104     -44.373  28.553  33.199  1.00 42.91           O  
ANISOU  825  O   ILE A 104     3356   4737   8210   -314   -416    607       O  
ATOM    826  CB  ILE A 104     -43.423  29.063  30.062  1.00 41.60           C  
ANISOU  826  CB  ILE A 104     3317   4409   8080   -218   -473    503       C  
ATOM    827  CG1 ILE A 104     -42.295  30.028  29.684  1.00 41.46           C  
ANISOU  827  CG1 ILE A 104     3323   4383   8045   -157   -418    435       C  
ATOM    828  CG2 ILE A 104     -44.164  28.560  28.834  1.00 42.01           C  
ANISOU  828  CG2 ILE A 104     3405   4401   8155   -233   -549    525       C  
ATOM    829  CD1 ILE A 104     -41.162  29.387  28.895  1.00 41.39           C  
ANISOU  829  CD1 ILE A 104     3389   4317   8020   -123   -448    404       C  
ATOM    830  N   LYS A 105     -45.961  27.866  31.732  1.00 43.29           N  
ANISOU  830  N   LYS A 105     3390   4735   8322   -368   -516    677       N  
ATOM    831  CA  LYS A 105     -46.325  26.649  32.503  1.00 44.00           C  
ANISOU  831  CA  LYS A 105     3471   4837   8409   -449   -570    760       C  
ATOM    832  C   LYS A 105     -45.186  25.647  32.285  1.00 43.59           C  
ANISOU  832  C   LYS A 105     3527   4691   8343   -444   -640    736       C  
ATOM    833  O   LYS A 105     -44.678  25.589  31.139  1.00 42.91           O  
ANISOU  833  O   LYS A 105     3513   4524   8265   -398   -678    684       O  
ATOM    834  CB  LYS A 105     -47.677  26.089  32.050  1.00 44.89           C  
ANISOU  834  CB  LYS A 105     3538   4950   8566   -522   -641    847       C  
ATOM    835  CG  LYS A 105     -48.372  25.166  33.045  1.00 46.01           C  
ANISOU  835  CG  LYS A 105     3627   5146   8707   -621   -672    956       C  
ATOM    836  CD  LYS A 105     -49.311  24.163  32.386  1.00 47.13           C  
ANISOU  836  CD  LYS A 105     3771   5234   8899   -712   -797   1045       C  
ATOM    837  CE  LYS A 105     -50.611  23.949  33.135  1.00 48.34           C  
ANISOU  837  CE  LYS A 105     3795   5499   9072   -805   -788   1169       C  
ATOM    838  NZ  LYS A 105     -50.410  23.328  34.466  1.00 48.88           N  
ANISOU  838  NZ  LYS A 105     3848   5626   9098   -863   -767   1232       N  
ATOM    839  N   TRP A 106     -44.768  24.914  33.323  1.00 43.44           N  
ANISOU  839  N   TRP A 106     3521   4683   8299   -480   -655    770       N  
ATOM    840  CA  TRP A 106     -43.697  23.901  33.156  1.00 43.41           C  
ANISOU  840  CA  TRP A 106     3620   4586   8287   -465   -731    748       C  
ATOM    841  C   TRP A 106     -44.150  22.900  32.097  1.00 43.98           C  
ANISOU  841  C   TRP A 106     3762   4557   8390   -494   -853    775       C  
ATOM    842  O   TRP A 106     -45.290  22.448  32.191  1.00 45.63           O  
ANISOU  842  O   TRP A 106     3936   4777   8624   -580   -905    860       O  
ATOM    843  CB  TRP A 106     -43.318  23.181  34.448  1.00 43.58           C  
ANISOU  843  CB  TRP A 106     3648   4629   8280   -510   -748    794       C  
ATOM    844  CG  TRP A 106     -42.100  22.346  34.215  1.00 43.78           C  
ANISOU  844  CG  TRP A 106     3774   4560   8301   -466   -817    754       C  
ATOM    845  CD1 TRP A 106     -40.801  22.728  34.391  1.00 43.44           C  
ANISOU  845  CD1 TRP A 106     3750   4517   8238   -390   -773    682       C  
ATOM    846  CD2 TRP A 106     -42.051  21.020  33.655  1.00 44.54           C  
ANISOU  846  CD2 TRP A 106     3965   4543   8414   -485   -948    777       C  
ATOM    847  NE1 TRP A 106     -39.952  21.720  34.023  1.00 43.58           N  
ANISOU  847  NE1 TRP A 106     3856   4442   8259   -353   -858    662       N  
ATOM    848  CE2 TRP A 106     -40.688  20.662  33.564  1.00 44.36           C  
ANISOU  848  CE2 TRP A 106     4012   4463   8377   -404   -967    713       C  
ATOM    849  CE3 TRP A 106     -43.017  20.097  33.239  1.00 45.14           C  
ANISOU  849  CE3 TRP A 106     4076   4555   8517   -561  -1058    848       C  
ATOM    850  CZ2 TRP A 106     -40.276  19.417  33.089  1.00 44.99           C  
ANISOU  850  CZ2 TRP A 106     4202   4426   8464   -383  -1089    709       C  
ATOM    851  CZ3 TRP A 106     -42.608  18.868  32.770  1.00 45.65           C  
ANISOU  851  CZ3 TRP A 106     4261   4493   8589   -553  -1190    846       C  
ATOM    852  CH2 TRP A 106     -41.257  18.534  32.699  1.00 45.70           C  
ANISOU  852  CH2 TRP A 106     4342   4444   8576   -457  -1202    773       C  
ATOM    853  N   ALA A 107     -43.274  22.566  31.150  1.00 43.75           N  
ANISOU  853  N   ALA A 107     3830   4437   8355   -425   -897    708       N  
ATOM    854  CA  ALA A 107     -43.548  21.662  30.011  1.00 44.16           C  
ANISOU  854  CA  ALA A 107     3979   4376   8422   -428  -1018    710       C  
ATOM    855  C   ALA A 107     -42.251  21.420  29.237  1.00 44.28           C  
ANISOU  855  C   ALA A 107     4095   4320   8409   -319  -1029    619       C  
ATOM    856  O   ALA A 107     -41.650  22.408  28.789  1.00 43.32           O  
ANISOU  856  O   ALA A 107     3949   4238   8270   -245   -935    553       O  
ATOM    857  CB  ALA A 107     -44.599  22.263  29.118  1.00 43.96           C  
ANISOU  857  CB  ALA A 107     3920   4361   8422   -446  -1019    722       C  
ATOM    858  N   ASP A 108     -41.845  20.155  29.099  1.00 45.31           N  
ANISOU  858  N   ASP A 108     4331   4350   8533   -308  -1140    619       N  
ATOM    859  CA  ASP A 108     -40.705  19.720  28.246  1.00 45.80           C  
ANISOU  859  CA  ASP A 108     4500   4337   8564   -190  -1167    533       C  
ATOM    860  C   ASP A 108     -39.403  20.371  28.740  1.00 45.33           C  
ANISOU  860  C   ASP A 108     4388   4350   8484   -111  -1053    478       C  
ATOM    861  O   ASP A 108     -38.648  20.910  27.889  1.00 45.39           O  
ANISOU  861  O   ASP A 108     4408   4370   8467    -16   -992    407       O  
ATOM    862  CB  ASP A 108     -40.979  20.040  26.771  1.00 45.85           C  
ANISOU  862  CB  ASP A 108     4561   4305   8554   -140  -1176    485       C  
ATOM    863  CG  ASP A 108     -42.181  19.302  26.210  1.00 46.76           C  
ANISOU  863  CG  ASP A 108     4742   4333   8691   -216  -1313    537       C  
ATOM    864  OD1 ASP A 108     -42.293  18.093  26.477  1.00 47.53           O  
ANISOU  864  OD1 ASP A 108     4921   4341   8798   -253  -1439    572       O  
ATOM    865  OD2 ASP A 108     -42.997  19.943  25.516  1.00 47.01           O  
ANISOU  865  OD2 ASP A 108     4747   4382   8733   -241  -1301    546       O  
ATOM    866  N   ASN A 109     -39.144  20.323  30.054  1.00 44.78           N  
ANISOU  866  N   ASN A 109     4263   4328   8422   -153  -1031    515       N  
ATOM    867  CA  ASN A 109     -37.868  20.790  30.665  1.00 44.12           C  
ANISOU  867  CA  ASN A 109     4135   4302   8325    -91   -951    474       C  
ATOM    868  C   ASN A 109     -37.588  22.243  30.267  1.00 43.28           C  
ANISOU  868  C   ASN A 109     3953   4279   8212    -53   -825    429       C  
ATOM    869  O   ASN A 109     -36.438  22.516  29.865  1.00 43.35           O  
ANISOU  869  O   ASN A 109     3962   4302   8207     33   -780    373       O  
ATOM    870  CB  ASN A 109     -36.682  19.943  30.201  1.00 44.43           C  
ANISOU  870  CB  ASN A 109     4257   4273   8349     15  -1001    418       C  
ATOM    871  CG  ASN A 109     -36.856  18.479  30.520  1.00 45.14           C  
ANISOU  871  CG  ASN A 109     4444   4260   8447     -8  -1142    455       C  
ATOM    872  OD1 ASN A 109     -36.701  18.083  31.669  1.00 45.34           O  
ANISOU  872  OD1 ASN A 109     4453   4293   8480    -57  -1171    501       O  
ATOM    873  ND2 ASN A 109     -37.171  17.679  29.516  1.00 45.72           N  
ANISOU  873  ND2 ASN A 109     4627   4229   8512     22  -1239    436       N  
ATOM    874  N   ASN A 110     -38.591  23.125  30.373  1.00 42.45           N  
ANISOU  874  N   ASN A 110     3783   4227   8117   -115   -776    457       N  
ATOM    875  CA  ASN A 110     -38.583  24.487  29.765  1.00 41.34           C  
ANISOU  875  CA  ASN A 110     3592   4140   7974    -85   -681    420       C  
ATOM    876  C   ASN A 110     -38.236  25.553  30.810  1.00 40.16           C  
ANISOU  876  C   ASN A 110     3358   4077   7823   -101   -593    417       C  
ATOM    877  O   ASN A 110     -38.171  26.730  30.425  1.00 39.32           O  
ANISOU  877  O   ASN A 110     3214   4008   7717    -81   -523    389       O  
ATOM    878  CB  ASN A 110     -39.921  24.826  29.096  1.00 41.70           C  
ANISOU  878  CB  ASN A 110     3629   4178   8035   -128   -696    445       C  
ATOM    879  CG  ASN A 110     -41.116  24.758  30.030  1.00 41.79           C  
ANISOU  879  CG  ASN A 110     3581   4228   8067   -220   -709    517       C  
ATOM    880  OD1 ASN A 110     -41.005  24.352  31.185  1.00 41.76           O  
ANISOU  880  OD1 ASN A 110     3556   4251   8058   -259   -714    552       O  
ATOM    881  ND2 ASN A 110     -42.276  25.135  29.529  1.00 42.32           N  
ANISOU  881  ND2 ASN A 110     3619   4303   8154   -255   -716    545       N  
ATOM    882  N   CYS A 111     -38.029  25.159  32.069  1.00 39.89           N  
ANISOU  882  N   CYS A 111     3307   4065   7784   -135   -605    447       N  
ATOM    883  CA  CYS A 111     -37.684  26.059  33.203  1.00 39.55           C  
ANISOU  883  CA  CYS A 111     3201   4095   7728   -151   -537    443       C  
ATOM    884  C   CYS A 111     -36.469  26.939  32.854  1.00 39.40           C  
ANISOU  884  C   CYS A 111     3164   4095   7709    -91   -481    387       C  
ATOM    885  O   CYS A 111     -36.381  28.066  33.402  1.00 39.35           O  
ANISOU  885  O   CYS A 111     3113   4141   7698   -102   -423    374       O  
ATOM    886  CB  CYS A 111     -37.413  25.258  34.471  1.00 39.90           C  
ANISOU  886  CB  CYS A 111     3254   4145   7758   -187   -577    481       C  
ATOM    887  SG  CYS A 111     -36.007  24.121  34.327  1.00 40.20           S  
ANISOU  887  SG  CYS A 111     3353   4119   7801   -127   -648    459       S  
ATOM    888  N   TYR A 112     -35.565  26.477  31.978  1.00 39.02           N  
ANISOU  888  N   TYR A 112     3150   4011   7665    -28   -500    357       N  
ATOM    889  CA  TYR A 112     -34.401  27.281  31.522  1.00 38.47           C  
ANISOU  889  CA  TYR A 112     3048   3971   7595     23   -444    318       C  
ATOM    890  C   TYR A 112     -34.918  28.404  30.618  1.00 38.01           C  
ANISOU  890  C   TYR A 112     2975   3927   7538     22   -391    304       C  
ATOM    891  O   TYR A 112     -34.587  29.563  30.892  1.00 38.08           O  
ANISOU  891  O   TYR A 112     2940   3976   7552      9   -340    295       O  
ATOM    892  CB  TYR A 112     -33.286  26.399  30.940  1.00 38.74           C  
ANISOU  892  CB  TYR A 112     3112   3980   7627    100   -471    296       C  
ATOM    893  CG  TYR A 112     -33.383  25.976  29.493  1.00 38.66           C  
ANISOU  893  CG  TYR A 112     3157   3930   7600    161   -481    271       C  
ATOM    894  CD1 TYR A 112     -32.528  26.500  28.537  1.00 38.37           C  
ANISOU  894  CD1 TYR A 112     3101   3926   7550    225   -423    243       C  
ATOM    895  CD2 TYR A 112     -34.278  24.996  29.088  1.00 38.81           C  
ANISOU  895  CD2 TYR A 112     3253   3878   7613    155   -555    280       C  
ATOM    896  CE1 TYR A 112     -32.588  26.091  27.213  1.00 38.70           C  
ANISOU  896  CE1 TYR A 112     3204   3937   7562    289   -429    217       C  
ATOM    897  CE2 TYR A 112     -34.351  24.574  27.769  1.00 38.93           C  
ANISOU  897  CE2 TYR A 112     3337   3848   7604    216   -576    251       C  
ATOM    898  CZ  TYR A 112     -33.501  25.122  26.826  1.00 38.99           C  
ANISOU  898  CZ  TYR A 112     3331   3895   7588    289   -509    216       C  
ATOM    899  OH  TYR A 112     -33.571  24.704  25.528  1.00 39.37           O  
ANISOU  899  OH  TYR A 112     3458   3904   7597    357   -526    184       O  
ATOM    900  N   LEU A 113     -35.751  28.092  29.626  1.00 38.17           N  
ANISOU  900  N   LEU A 113     3038   3909   7555     28   -414    306       N  
ATOM    901  CA  LEU A 113     -36.357  29.117  28.727  1.00 38.37           C  
ANISOU  901  CA  LEU A 113     3057   3939   7581     25   -376    297       C  
ATOM    902  C   LEU A 113     -37.211  30.096  29.548  1.00 37.88           C  
ANISOU  902  C   LEU A 113     2946   3912   7533    -26   -347    312       C  
ATOM    903  O   LEU A 113     -37.137  31.305  29.302  1.00 37.55           O  
ANISOU  903  O   LEU A 113     2880   3889   7495    -24   -301    297       O  
ATOM    904  CB  LEU A 113     -37.210  28.430  27.656  1.00 38.89           C  
ANISOU  904  CB  LEU A 113     3185   3950   7641     34   -429    302       C  
ATOM    905  CG  LEU A 113     -36.469  27.506  26.693  1.00 39.60           C  
ANISOU  905  CG  LEU A 113     3344   3998   7702    104   -460    275       C  
ATOM    906  CD1 LEU A 113     -37.332  27.198  25.481  1.00 40.04           C  
ANISOU  906  CD1 LEU A 113     3470   3998   7742    113   -507    273       C  
ATOM    907  CD2 LEU A 113     -35.148  28.115  26.250  1.00 39.96           C  
ANISOU  907  CD2 LEU A 113     3363   4090   7729    162   -389    247       C  
ATOM    908  N   ALA A 114     -38.015  29.584  30.477  1.00 38.02           N  
ANISOU  908  N   ALA A 114     2951   3937   7555    -69   -374    343       N  
ATOM    909  CA  ALA A 114     -38.856  30.393  31.388  1.00 37.91           C  
ANISOU  909  CA  ALA A 114     2890   3970   7543   -104   -340    357       C  
ATOM    910  C   ALA A 114     -37.963  31.399  32.125  1.00 37.32           C  
ANISOU  910  C   ALA A 114     2792   3930   7459    -93   -293    327       C  
ATOM    911  O   ALA A 114     -38.231  32.604  32.017  1.00 37.03           O  
ANISOU  911  O   ALA A 114     2739   3905   7426    -87   -256    307       O  
ATOM    912  CB  ALA A 114     -39.606  29.493  32.344  1.00 38.36           C  
ANISOU  912  CB  ALA A 114     2935   4044   7595   -150   -372    404       C  
ATOM    913  N   THR A 115     -36.930  30.911  32.823  1.00 37.16           N  
ANISOU  913  N   THR A 115     2775   3914   7427    -93   -306    325       N  
ATOM    914  CA  THR A 115     -35.982  31.730  33.632  1.00 36.68           C  
ANISOU  914  CA  THR A 115     2696   3881   7359    -93   -282    303       C  
ATOM    915  C   THR A 115     -35.296  32.761  32.732  1.00 35.91           C  
ANISOU  915  C   THR A 115     2591   3775   7277    -72   -254    278       C  
ATOM    916  O   THR A 115     -35.129  33.911  33.175  1.00 35.65           O  
ANISOU  916  O   THR A 115     2548   3754   7243    -84   -234    261       O  
ATOM    917  CB  THR A 115     -34.944  30.865  34.353  1.00 36.76           C  
ANISOU  917  CB  THR A 115     2711   3893   7362    -93   -316    312       C  
ATOM    918  OG1 THR A 115     -35.628  29.918  35.170  1.00 36.96           O  
ANISOU  918  OG1 THR A 115     2750   3922   7369   -123   -348    345       O  
ATOM    919  CG2 THR A 115     -34.021  31.688  35.221  1.00 37.00           C  
ANISOU  919  CG2 THR A 115     2724   3949   7386   -103   -307    295       C  
ATOM    920  N   ALA A 116     -34.926  32.357  31.518  1.00 35.41           N  
ANISOU  920  N   ALA A 116     2539   3691   7223    -43   -256    278       N  
ATOM    921  CA  ALA A 116     -34.398  33.254  30.467  1.00 35.52           C  
ANISOU  921  CA  ALA A 116     2547   3704   7244    -28   -226    268       C  
ATOM    922  C   ALA A 116     -35.395  34.388  30.201  1.00 35.39           C  
ANISOU  922  C   ALA A 116     2537   3676   7233    -43   -209    262       C  
ATOM    923  O   ALA A 116     -34.993  35.558  30.276  1.00 35.75           O  
ANISOU  923  O   ALA A 116     2572   3723   7286    -58   -192    254       O  
ATOM    924  CB  ALA A 116     -34.123  32.466  29.213  1.00 35.76           C  
ANISOU  924  CB  ALA A 116     2602   3719   7266     14   -229    269       C  
ATOM    925  N   LEU A 117     -36.647  34.033  29.905  1.00 35.26           N  
ANISOU  925  N   LEU A 117     2536   3643   7217    -42   -222    269       N  
ATOM    926  CA  LEU A 117     -37.718  34.938  29.410  1.00 35.03           C  
ANISOU  926  CA  LEU A 117     2510   3599   7197    -43   -214    266       C  
ATOM    927  C   LEU A 117     -38.085  35.966  30.489  1.00 34.89           C  
ANISOU  927  C   LEU A 117     2475   3601   7182    -52   -197    249       C  
ATOM    928  O   LEU A 117     -38.367  37.121  30.135  1.00 34.84           O  
ANISOU  928  O   LEU A 117     2475   3575   7184    -44   -189    236       O  
ATOM    929  CB  LEU A 117     -38.915  34.063  29.022  1.00 35.25           C  
ANISOU  929  CB  LEU A 117     2547   3614   7230    -44   -244    287       C  
ATOM    930  CG  LEU A 117     -40.163  34.796  28.535  1.00 35.55           C  
ANISOU  930  CG  LEU A 117     2578   3643   7286    -42   -247    292       C  
ATOM    931  CD1 LEU A 117     -39.853  35.635  27.306  1.00 35.68           C  
ANISOU  931  CD1 LEU A 117     2625   3628   7304    -26   -241    281       C  
ATOM    932  CD2 LEU A 117     -41.278  33.803  28.240  1.00 35.72           C  
ANISOU  932  CD2 LEU A 117     2598   3656   7318    -57   -289    324       C  
ATOM    933  N   LEU A 118     -38.082  35.553  31.755  1.00 34.89           N  
ANISOU  933  N   LEU A 118     2459   3631   7165    -63   -197    250       N  
ATOM    934  CA  LEU A 118     -38.440  36.401  32.922  1.00 35.15           C  
ANISOU  934  CA  LEU A 118     2485   3687   7181    -60   -180    228       C  
ATOM    935  C   LEU A 118     -37.321  37.420  33.176  1.00 35.35           C  
ANISOU  935  C   LEU A 118     2530   3694   7206    -66   -184    201       C  
ATOM    936  O   LEU A 118     -37.647  38.610  33.379  1.00 35.26           O  
ANISOU  936  O   LEU A 118     2537   3665   7193    -52   -180    173       O  
ATOM    937  CB  LEU A 118     -38.685  35.484  34.125  1.00 35.45           C  
ANISOU  937  CB  LEU A 118     2509   3768   7190    -75   -180    245       C  
ATOM    938  CG  LEU A 118     -39.929  34.599  34.003  1.00 35.84           C  
ANISOU  938  CG  LEU A 118     2533   3841   7243    -84   -183    284       C  
ATOM    939  CD1 LEU A 118     -39.795  33.327  34.828  1.00 36.02           C  
ANISOU  939  CD1 LEU A 118     2552   3888   7244   -117   -204    321       C  
ATOM    940  CD2 LEU A 118     -41.188  35.367  34.396  1.00 36.13           C  
ANISOU  940  CD2 LEU A 118     2539   3916   7272    -61   -150    279       C  
ATOM    941  N   THR A 119     -36.058  36.966  33.140  1.00 35.45           N  
ANISOU  941  N   THR A 119     2538   3706   7223    -85   -197    212       N  
ATOM    942  CA  THR A 119     -34.822  37.795  33.216  1.00 35.50           C  
ANISOU  942  CA  THR A 119     2548   3699   7240   -106   -211    205       C  
ATOM    943  C   THR A 119     -34.825  38.842  32.096  1.00 35.57           C  
ANISOU  943  C   THR A 119     2569   3674   7272   -109   -206    207       C  
ATOM    944  O   THR A 119     -34.626  40.033  32.396  1.00 35.88           O  
ANISOU  944  O   THR A 119     2631   3685   7316   -124   -225    191       O  
ATOM    945  CB  THR A 119     -33.558  36.934  33.097  1.00 35.56           C  
ANISOU  945  CB  THR A 119     2527   3725   7257   -116   -221    229       C  
ATOM    946  OG1 THR A 119     -33.501  35.993  34.170  1.00 35.69           O  
ANISOU  946  OG1 THR A 119     2542   3764   7254   -117   -237    231       O  
ATOM    947  CG2 THR A 119     -32.294  37.763  33.103  1.00 36.02           C  
ANISOU  947  CG2 THR A 119     2569   3781   7334   -147   -236    237       C  
ATOM    948  N   LEU A 120     -35.044  38.408  30.854  1.00 35.48           N  
ANISOU  948  N   LEU A 120     2552   3659   7269    -95   -191    227       N  
ATOM    949  CA  LEU A 120     -34.953  39.257  29.634  1.00 35.85           C  
ANISOU  949  CA  LEU A 120     2613   3679   7328   -102   -186    240       C  
ATOM    950  C   LEU A 120     -35.928  40.438  29.728  1.00 36.54           C  
ANISOU  950  C   LEU A 120     2734   3726   7424    -94   -200    218       C  
ATOM    951  O   LEU A 120     -35.650  41.467  29.100  1.00 37.02           O  
ANISOU  951  O   LEU A 120     2816   3752   7497   -114   -213    229       O  
ATOM    952  CB  LEU A 120     -35.228  38.392  28.399  1.00 35.52           C  
ANISOU  952  CB  LEU A 120     2575   3642   7278    -77   -171    258       C  
ATOM    953  CG  LEU A 120     -34.071  37.479  27.988  1.00 35.30           C  
ANISOU  953  CG  LEU A 120     2523   3647   7239    -68   -156    276       C  
ATOM    954  CD1 LEU A 120     -34.554  36.282  27.184  1.00 34.96           C  
ANISOU  954  CD1 LEU A 120     2503   3602   7178    -29   -156    276       C  
ATOM    955  CD2 LEU A 120     -33.024  38.260  27.211  1.00 35.57           C  
ANISOU  955  CD2 LEU A 120     2541   3696   7276    -90   -136    305       C  
ATOM    956  N   GLN A 121     -37.010  40.297  30.499  1.00 37.04           N  
ANISOU  956  N   GLN A 121     2799   3797   7478    -66   -198    193       N  
ATOM    957  CA  GLN A 121     -38.027  41.356  30.729  1.00 37.66           C  
ANISOU  957  CA  GLN A 121     2902   3846   7560    -36   -207    164       C  
ATOM    958  C   GLN A 121     -37.544  42.365  31.785  1.00 38.49           C  
ANISOU  958  C   GLN A 121     3039   3927   7654    -40   -230    130       C  
ATOM    959  O   GLN A 121     -38.259  43.359  32.007  1.00 39.29           O  
ANISOU  959  O   GLN A 121     3176   3996   7757     -4   -245     97       O  
ATOM    960  CB  GLN A 121     -39.348  40.720  31.179  1.00 37.74           C  
ANISOU  960  CB  GLN A 121     2884   3894   7561      0   -188    158       C  
ATOM    961  CG  GLN A 121     -39.988  39.810  30.137  1.00 37.52           C  
ANISOU  961  CG  GLN A 121     2834   3873   7548      0   -187    192       C  
ATOM    962  CD  GLN A 121     -41.207  39.078  30.649  1.00 37.56           C  
ANISOU  962  CD  GLN A 121     2799   3923   7550     17   -175    203       C  
ATOM    963  OE1 GLN A 121     -42.086  39.651  31.286  1.00 38.01           O  
ANISOU  963  OE1 GLN A 121     2838   4001   7603     53   -161    185       O  
ATOM    964  NE2 GLN A 121     -41.284  37.795  30.348  1.00 37.54           N  
ANISOU  964  NE2 GLN A 121     2780   3936   7547     -5   -185    237       N  
ATOM    965  N   GLN A 122     -36.403  42.134  32.437  1.00 38.73           N  
ANISOU  965  N   GLN A 122     3067   3972   7677    -77   -242    135       N  
ATOM    966  CA  GLN A 122     -35.990  42.908  33.639  1.00 39.59           C  
ANISOU  966  CA  GLN A 122     3215   4060   7766    -83   -275     99       C  
ATOM    967  C   GLN A 122     -34.605  43.541  33.455  1.00 40.16           C  
ANISOU  967  C   GLN A 122     3299   4097   7862   -146   -320    123       C  
ATOM    968  O   GLN A 122     -34.092  44.113  34.439  1.00 40.49           O  
ANISOU  968  O   GLN A 122     3378   4114   7890   -164   -365     99       O  
ATOM    969  CB  GLN A 122     -35.967  41.986  34.857  1.00 39.80           C  
ANISOU  969  CB  GLN A 122     3226   4141   7755    -75   -260     89       C  
ATOM    970  CG  GLN A 122     -37.331  41.457  35.252  1.00 39.87           C  
ANISOU  970  CG  GLN A 122     3218   4194   7735    -23   -218     75       C  
ATOM    971  CD  GLN A 122     -37.201  40.448  36.363  1.00 40.08           C  
ANISOU  971  CD  GLN A 122     3229   4278   7722    -31   -205     82       C  
ATOM    972  OE1 GLN A 122     -37.529  40.717  37.513  1.00 40.71           O  
ANISOU  972  OE1 GLN A 122     3336   4379   7752     -6   -200     51       O  
ATOM    973  NE2 GLN A 122     -36.691  39.277  36.025  1.00 40.09           N  
ANISOU  973  NE2 GLN A 122     3192   4301   7738    -63   -203    124       N  
ATOM    974  N   ILE A 123     -34.030  43.460  32.253  1.00 40.57           N  
ANISOU  974  N   ILE A 123     3320   4149   7943   -181   -312    171       N  
ATOM    975  CA  ILE A 123     -32.677  44.004  31.928  1.00 41.48           C  
ANISOU  975  CA  ILE A 123     3422   4251   8085   -251   -345    214       C  
ATOM    976  C   ILE A 123     -32.792  44.833  30.640  1.00 42.69           C  
ANISOU  976  C   ILE A 123     3593   4365   8260   -272   -351    247       C  
ATOM    977  O   ILE A 123     -33.486  44.376  29.710  1.00 42.29           O  
ANISOU  977  O   ILE A 123     3533   4330   8203   -237   -310    255       O  
ATOM    978  CB  ILE A 123     -31.625  42.872  31.837  1.00 40.85           C  
ANISOU  978  CB  ILE A 123     3268   4241   8011   -271   -318    253       C  
ATOM    979  CG1 ILE A 123     -31.898  41.913  30.674  1.00 40.42           C  
ANISOU  979  CG1 ILE A 123     3178   4227   7951   -237   -260    276       C  
ATOM    980  CG2 ILE A 123     -31.510  42.130  33.164  1.00 40.57           C  
ANISOU  980  CG2 ILE A 123     3227   4232   7953   -256   -328    225       C  
ATOM    981  CD1 ILE A 123     -31.138  40.608  30.744  1.00 40.23           C  
ANISOU  981  CD1 ILE A 123     3097   4265   7923   -224   -235    294       C  
ATOM    982  N   GLU A 124     -32.171  46.023  30.619  1.00 44.73           N  
ANISOU  982  N   GLU A 124     3885   4568   8540   -331   -410    269       N  
ATOM    983  CA  GLU A 124     -32.139  46.956  29.457  1.00 45.80           C  
ANISOU  983  CA  GLU A 124     4047   4659   8696   -370   -430    314       C  
ATOM    984  C   GLU A 124     -31.224  46.315  28.404  1.00 45.89           C  
ANISOU  984  C   GLU A 124     3980   4745   8710   -408   -378    387       C  
ATOM    985  O   GLU A 124     -30.019  46.223  28.678  1.00 46.64           O  
ANISOU  985  O   GLU A 124     4021   4878   8820   -464   -387    429       O  
ATOM    986  CB  GLU A 124     -31.685  48.356  29.906  1.00 47.23           C  
ANISOU  986  CB  GLU A 124     4292   4753   8900   -431   -525    319       C  
ATOM    987  CG  GLU A 124     -32.451  49.518  29.263  1.00 48.23           C  
ANISOU  987  CG  GLU A 124     4501   4786   9036   -424   -571    315       C  
ATOM    988  CD  GLU A 124     -33.753  49.988  29.928  1.00 48.70           C  
ANISOU  988  CD  GLU A 124     4640   4782   9082   -332   -597    227       C  
ATOM    989  OE1 GLU A 124     -33.705  50.570  31.045  1.00 49.02           O  
ANISOU  989  OE1 GLU A 124     4742   4769   9114   -320   -658    175       O  
ATOM    990  OE2 GLU A 124     -34.831  49.801  29.313  1.00 48.58           O  
ANISOU  990  OE2 GLU A 124     4627   4771   9060   -267   -560    210       O  
ATOM    991  N   LEU A 125     -31.790  45.832  27.289  1.00 45.47           N  
ANISOU  991  N   LEU A 125     3920   4717   8639   -371   -326    400       N  
ATOM    992  CA  LEU A 125     -31.080  45.068  26.221  1.00 45.74           C  
ANISOU  992  CA  LEU A 125     3892   4830   8655   -378   -263    455       C  
ATOM    993  C   LEU A 125     -31.823  45.218  24.889  1.00 46.22           C  
ANISOU  993  C   LEU A 125     3991   4874   8694   -357   -242    472       C  
ATOM    994  O   LEU A 125     -33.050  45.107  24.909  1.00 46.94           O  
ANISOU  994  O   LEU A 125     4128   4926   8780   -303   -251    425       O  
ATOM    995  CB  LEU A 125     -31.027  43.590  26.615  1.00 44.99           C  
ANISOU  995  CB  LEU A 125     3749   4800   8543   -319   -215    424       C  
ATOM    996  CG  LEU A 125     -30.212  42.697  25.681  1.00 45.25           C  
ANISOU  996  CG  LEU A 125     3723   4916   8552   -304   -153    467       C  
ATOM    997  CD1 LEU A 125     -28.861  42.374  26.299  1.00 45.95           C  
ANISOU  997  CD1 LEU A 125     3731   5066   8660   -331   -148    495       C  
ATOM    998  CD2 LEU A 125     -30.951  41.414  25.341  1.00 44.65           C  
ANISOU  998  CD2 LEU A 125     3661   4858   8445   -223   -117    427       C  
ATOM    999  N   LYS A 126     -31.111  45.413  23.774  1.00 47.20           N  
ANISOU  999  N   LYS A 126     4093   5037   8801   -397   -213    542       N  
ATOM   1000  CA  LYS A 126     -31.709  45.546  22.415  1.00 47.85           C  
ANISOU 1000  CA  LYS A 126     4221   5110   8850   -381   -195    567       C  
ATOM   1001  C   LYS A 126     -30.976  44.604  21.447  1.00 48.61           C  
ANISOU 1001  C   LYS A 126     4268   5305   8896   -359   -116    605       C  
ATOM   1002  O   LYS A 126     -29.740  44.740  21.306  1.00 49.55           O  
ANISOU 1002  O   LYS A 126     4321   5491   9014   -407    -86    667       O  
ATOM   1003  CB  LYS A 126     -31.671  47.005  21.941  1.00 48.86           C  
ANISOU 1003  CB  LYS A 126     4398   5172   8993   -455   -250    621       C  
ATOM   1004  CG  LYS A 126     -32.049  48.057  22.986  1.00 49.42           C  
ANISOU 1004  CG  LYS A 126     4520   5144   9113   -479   -337    586       C  
ATOM   1005  CD  LYS A 126     -33.439  47.894  23.611  1.00 49.12           C  
ANISOU 1005  CD  LYS A 126     4529   5050   9083   -395   -359    496       C  
ATOM   1006  CE  LYS A 126     -34.547  48.639  22.891  1.00 49.14           C  
ANISOU 1006  CE  LYS A 126     4606   4974   9087   -371   -401    491       C  
ATOM   1007  NZ  LYS A 126     -35.721  47.764  22.676  1.00 48.41           N  
ANISOU 1007  NZ  LYS A 126     4513   4899   8980   -286   -371    443       N  
ATOM   1008  N   PHE A 127     -31.714  43.678  20.822  1.00 48.63           N  
ANISOU 1008  N   PHE A 127     4301   5317   8858   -285    -87    570       N  
ATOM   1009  CA  PHE A 127     -31.190  42.620  19.918  1.00 49.41           C  
ANISOU 1009  CA  PHE A 127     4376   5498   8896   -235    -17    584       C  
ATOM   1010  C   PHE A 127     -30.881  43.209  18.540  1.00 49.89           C  
ANISOU 1010  C   PHE A 127     4462   5589   8906   -264     11    653       C  
ATOM   1011  O   PHE A 127     -31.481  44.232  18.174  1.00 49.88           O  
ANISOU 1011  O   PHE A 127     4517   5519   8914   -309    -34    676       O  
ATOM   1012  CB  PHE A 127     -32.188  41.467  19.787  1.00 49.66           C  
ANISOU 1012  CB  PHE A 127     4454   5508   8904   -152    -21    519       C  
ATOM   1013  CG  PHE A 127     -32.265  40.557  20.987  1.00 49.90           C  
ANISOU 1013  CG  PHE A 127     4451   5540   8966   -118    -32    466       C  
ATOM   1014  CD1 PHE A 127     -31.328  39.553  21.177  1.00 50.57           C  
ANISOU 1014  CD1 PHE A 127     4485   5693   9035    -79      8    461       C  
ATOM   1015  CD2 PHE A 127     -33.283  40.693  21.921  1.00 49.67           C  
ANISOU 1015  CD2 PHE A 127     4443   5449   8980   -119    -82    423       C  
ATOM   1016  CE1 PHE A 127     -31.404  38.710  22.276  1.00 50.29           C  
ANISOU 1016  CE1 PHE A 127     4427   5652   9027    -53    -10    419       C  
ATOM   1017  CE2 PHE A 127     -33.355  39.854  23.022  1.00 49.16           C  
ANISOU 1017  CE2 PHE A 127     4351   5392   8935    -95    -90    385       C  
ATOM   1018  CZ  PHE A 127     -32.416  38.864  23.197  1.00 49.61           C  
ANISOU 1018  CZ  PHE A 127     4365   5505   8977    -67    -59    384       C  
ATOM   1019  N   ASN A 128     -29.972  42.562  17.806  1.00 51.03           N  
ANISOU 1019  N   ASN A 128     4565   5832   8992   -233     87    685       N  
ATOM   1020  CA  ASN A 128     -29.535  42.969  16.442  1.00 52.73           C  
ANISOU 1020  CA  ASN A 128     4794   6104   9135   -253    136    758       C  
ATOM   1021  C   ASN A 128     -30.530  42.441  15.410  1.00 53.61           C  
ANISOU 1021  C   ASN A 128     5007   6182   9177   -185    133    721       C  
ATOM   1022  O   ASN A 128     -31.061  43.233  14.635  1.00 55.13           O  
ANISOU 1022  O   ASN A 128     5266   6331   9346   -223    105    757       O  
ATOM   1023  CB  ASN A 128     -28.097  42.544  16.127  1.00 53.35           C  
ANISOU 1023  CB  ASN A 128     4774   6321   9174   -239    228    810       C  
ATOM   1024  CG  ASN A 128     -27.070  43.553  16.594  1.00 54.18           C  
ANISOU 1024  CG  ASN A 128     4787   6465   9334   -349    224    897       C  
ATOM   1025  OD1 ASN A 128     -27.122  44.020  17.729  1.00 53.46           O  
ANISOU 1025  OD1 ASN A 128     4677   6309   9323   -403    157    882       O  
ATOM   1026  ND2 ASN A 128     -26.125  43.888  15.730  1.00 55.93           N  
ANISOU 1026  ND2 ASN A 128     4952   6793   9506   -386    292    993       N  
ATOM   1027  N   PRO A 129     -30.831  41.118  15.350  1.00 53.36           N  
ANISOU 1027  N   PRO A 129     5000   6161   9113    -87    148    652       N  
ATOM   1028  CA  PRO A 129     -31.798  40.600  14.382  1.00 53.22           C  
ANISOU 1028  CA  PRO A 129     5088   6101   9031    -29    126    618       C  
ATOM   1029  C   PRO A 129     -33.180  41.226  14.546  1.00 52.41           C  
ANISOU 1029  C   PRO A 129     5051   5884   8979    -64     35    599       C  
ATOM   1030  O   PRO A 129     -33.679  41.347  15.662  1.00 51.62           O  
ANISOU 1030  O   PRO A 129     4924   5730   8959    -81    -10    565       O  
ATOM   1031  CB  PRO A 129     -31.860  39.091  14.666  1.00 53.02           C  
ANISOU 1031  CB  PRO A 129     5071   6085   8989     66    132    544       C  
ATOM   1032  CG  PRO A 129     -30.561  38.796  15.372  1.00 53.41           C  
ANISOU 1032  CG  PRO A 129     5011   6221   9059     75    192    556       C  
ATOM   1033  CD  PRO A 129     -30.260  40.045  16.177  1.00 53.25           C  
ANISOU 1033  CD  PRO A 129     4922   6189   9118    -30    174    607       C  
ATOM   1034  N   PRO A 130     -33.815  41.691  13.447  1.00 52.77           N  
ANISOU 1034  N   PRO A 130     5181   5893   8975    -73      8    624       N  
ATOM   1035  CA  PRO A 130     -35.245  41.992  13.456  1.00 52.63           C  
ANISOU 1035  CA  PRO A 130     5227   5770   8997    -79    -81    597       C  
ATOM   1036  C   PRO A 130     -36.083  40.878  14.102  1.00 51.80           C  
ANISOU 1036  C   PRO A 130     5126   5628   8927    -23   -121    523       C  
ATOM   1037  O   PRO A 130     -36.903  41.200  14.935  1.00 51.05           O  
ANISOU 1037  O   PRO A 130     5011   5476   8909    -40   -173    501       O  
ATOM   1038  CB  PRO A 130     -35.556  42.132  11.961  1.00 53.38           C  
ANISOU 1038  CB  PRO A 130     5419   5860   9002    -69    -90    630       C  
ATOM   1039  CG  PRO A 130     -34.284  42.718  11.395  1.00 54.07           C  
ANISOU 1039  CG  PRO A 130     5476   6035   9031   -109    -11    706       C  
ATOM   1040  CD  PRO A 130     -33.185  42.008  12.156  1.00 53.88           C  
ANISOU 1040  CD  PRO A 130     5354   6096   9018    -82     62    688       C  
ATOM   1041  N   ALA A 131     -35.833  39.616  13.728  1.00 52.05           N  
ANISOU 1041  N   ALA A 131     5181   5694   8899     43    -96    490       N  
ATOM   1042  CA  ALA A 131     -36.542  38.412  14.227  1.00 51.96           C  
ANISOU 1042  CA  ALA A 131     5184   5645   8910     90   -141    430       C  
ATOM   1043  C   ALA A 131     -36.596  38.424  15.759  1.00 51.78           C  
ANISOU 1043  C   ALA A 131     5075   5616   8981     65   -149    410       C  
ATOM   1044  O   ALA A 131     -37.709  38.360  16.306  1.00 52.34           O  
ANISOU 1044  O   ALA A 131     5146   5632   9108     55   -209    390       O  
ATOM   1045  CB  ALA A 131     -35.880  37.156  13.714  1.00 52.17           C  
ANISOU 1045  CB  ALA A 131     5246   5716   8858    166   -106    401       C  
ATOM   1046  N   LEU A 132     -35.441  38.513  16.422  1.00 52.76           N  
ANISOU 1046  N   LEU A 132     5126   5800   9117     55    -89    420       N  
ATOM   1047  CA  LEU A 132     -35.325  38.451  17.906  1.00 53.18           C  
ANISOU 1047  CA  LEU A 132     5105   5854   9244     35    -94    399       C  
ATOM   1048  C   LEU A 132     -35.977  39.682  18.555  1.00 53.09           C  
ANISOU 1048  C   LEU A 132     5076   5795   9298    -19   -131    410       C  
ATOM   1049  O   LEU A 132     -36.672  39.489  19.562  1.00 52.72           O  
ANISOU 1049  O   LEU A 132     5007   5722   9302    -19   -162    379       O  
ATOM   1050  CB  LEU A 132     -33.851  38.328  18.317  1.00 53.79           C  
ANISOU 1050  CB  LEU A 132     5112   6010   9316     37    -30    415       C  
ATOM   1051  CG  LEU A 132     -33.335  36.900  18.496  1.00 54.44           C  
ANISOU 1051  CG  LEU A 132     5185   6126   9372    106    -11    380       C  
ATOM   1052  CD1 LEU A 132     -31.828  36.888  18.716  1.00 55.30           C  
ANISOU 1052  CD1 LEU A 132     5214   6322   9473    113     54    405       C  
ATOM   1053  CD2 LEU A 132     -34.041  36.193  19.646  1.00 53.71           C  
ANISOU 1053  CD2 LEU A 132     5085   5989   9332    108    -63    340       C  
ATOM   1054  N   GLN A 133     -35.751  40.887  18.018  1.00 53.87           N  
ANISOU 1054  N   GLN A 133     5189   5886   9392    -63   -128    452       N  
ATOM   1055  CA  GLN A 133     -36.226  42.171  18.608  1.00 54.49           C  
ANISOU 1055  CA  GLN A 133     5264   5910   9530   -108   -170    460       C  
ATOM   1056  C   GLN A 133     -37.746  42.305  18.403  1.00 53.75           C  
ANISOU 1056  C   GLN A 133     5214   5749   9458    -85   -231    438       C  
ATOM   1057  O   GLN A 133     -38.440  42.651  19.386  1.00 53.02           O  
ANISOU 1057  O   GLN A 133     5098   5625   9421    -81   -262    409       O  
ATOM   1058  CB  GLN A 133     -35.444  43.350  18.020  1.00 56.15           C  
ANISOU 1058  CB  GLN A 133     5483   6125   9726   -167   -159    521       C  
ATOM   1059  CG  GLN A 133     -35.854  44.710  18.579  1.00 57.16           C  
ANISOU 1059  CG  GLN A 133     5625   6180   9912   -211   -217    527       C  
ATOM   1060  CD  GLN A 133     -35.440  44.932  20.015  1.00 57.44           C  
ANISOU 1060  CD  GLN A 133     5610   6214   9998   -228   -223    500       C  
ATOM   1061  OE1 GLN A 133     -36.172  44.638  20.960  1.00 56.72           O  
ANISOU 1061  OE1 GLN A 133     5509   6102   9939   -191   -242    445       O  
ATOM   1062  NE2 GLN A 133     -34.259  45.501  20.188  1.00 59.38           N  
ANISOU 1062  NE2 GLN A 133     5826   6485  10250   -290   -211    544       N  
ATOM   1063  N   ASP A 134     -38.246  42.045  17.185  1.00 53.31           N  
ANISOU 1063  N   ASP A 134     5219   5677   9358    -67   -250    452       N  
ATOM   1064  CA  ASP A 134     -39.702  41.921  16.892  1.00 52.08           C  
ANISOU 1064  CA  ASP A 134     5097   5466   9223    -43   -317    436       C  
ATOM   1065  C   ASP A 134     -40.311  41.008  17.961  1.00 50.71           C  
ANISOU 1065  C   ASP A 134     4873   5302   9092    -17   -326    394       C  
ATOM   1066  O   ASP A 134     -41.109  41.505  18.763  1.00 50.77           O  
ANISOU 1066  O   ASP A 134     4846   5286   9158    -15   -353    379       O  
ATOM   1067  CB  ASP A 134     -39.984  41.387  15.479  1.00 52.55           C  
ANISOU 1067  CB  ASP A 134     5233   5516   9215    -24   -338    451       C  
ATOM   1068  CG  ASP A 134     -39.989  42.424  14.358  1.00 53.12           C  
ANISOU 1068  CG  ASP A 134     5370   5560   9252    -49   -358    498       C  
ATOM   1069  OD1 ASP A 134     -39.203  43.382  14.435  1.00 53.91           O  
ANISOU 1069  OD1 ASP A 134     5457   5670   9354    -91   -329    532       O  
ATOM   1070  OD2 ASP A 134     -40.773  42.255  13.395  1.00 52.96           O  
ANISOU 1070  OD2 ASP A 134     5417   5503   9202    -35   -411    506       O  
ATOM   1071  N   ALA A 135     -39.877  39.745  18.005  1.00 50.30           N  
ANISOU 1071  N   ALA A 135     4817   5285   9008      2   -303    379       N  
ATOM   1072  CA  ALA A 135     -40.408  38.673  18.884  1.00 50.30           C  
ANISOU 1072  CA  ALA A 135     4782   5292   9038     17   -320    352       C  
ATOM   1073  C   ALA A 135     -40.228  39.023  20.368  1.00 50.08           C  
ANISOU 1073  C   ALA A 135     4681   5286   9058      4   -294    336       C  
ATOM   1074  O   ALA A 135     -41.080  38.593  21.168  1.00 49.99           O  
ANISOU 1074  O   ALA A 135     4634   5276   9083      8   -316    325       O  
ATOM   1075  CB  ALA A 135     -39.739  37.361  18.555  1.00 50.40           C  
ANISOU 1075  CB  ALA A 135     4821   5327   9000     44   -305    340       C  
ATOM   1076  N   TYR A 136     -39.170  39.761  20.722  1.00 50.08           N  
ANISOU 1076  N   TYR A 136     4662   5307   9057    -15   -253    341       N  
ATOM   1077  CA  TYR A 136     -38.844  40.188  22.110  1.00 50.07           C  
ANISOU 1077  CA  TYR A 136     4609   5322   9092    -29   -235    324       C  
ATOM   1078  C   TYR A 136     -39.914  41.146  22.629  1.00 50.99           C  
ANISOU 1078  C   TYR A 136     4719   5402   9250    -24   -267    310       C  
ATOM   1079  O   TYR A 136     -40.161  41.134  23.843  1.00 51.95           O  
ANISOU 1079  O   TYR A 136     4803   5540   9394    -16   -261    286       O  
ATOM   1080  CB  TYR A 136     -37.470  40.857  22.151  1.00 50.42           C  
ANISOU 1080  CB  TYR A 136     4643   5388   9126    -61   -202    342       C  
ATOM   1081  CG  TYR A 136     -36.954  41.337  23.487  1.00 50.06           C  
ANISOU 1081  CG  TYR A 136     4558   5350   9109    -83   -197    327       C  
ATOM   1082  CD1 TYR A 136     -37.273  40.718  24.689  1.00 49.51           C  
ANISOU 1082  CD1 TYR A 136     4457   5298   9054    -67   -198    295       C  
ATOM   1083  CD2 TYR A 136     -36.046  42.382  23.526  1.00 50.46           C  
ANISOU 1083  CD2 TYR A 136     4609   5395   9168   -127   -197    350       C  
ATOM   1084  CE1 TYR A 136     -36.737  41.158  25.892  1.00 49.54           C  
ANISOU 1084  CE1 TYR A 136     4439   5310   9073    -85   -198    280       C  
ATOM   1085  CE2 TYR A 136     -35.499  42.830  24.715  1.00 50.46           C  
ANISOU 1085  CE2 TYR A 136     4584   5394   9191   -151   -207    337       C  
ATOM   1086  CZ  TYR A 136     -35.847  42.221  25.904  1.00 50.25           C  
ANISOU 1086  CZ  TYR A 136     4536   5383   9172   -126   -206    297       C  
ATOM   1087  OH  TYR A 136     -35.285  42.700  27.053  1.00 50.23           O  
ANISOU 1087  OH  TYR A 136     4523   5378   9183   -149   -222    282       O  
ATOM   1088  N   TYR A 137     -40.506  41.959  21.748  1.00 51.36           N  
ANISOU 1088  N   TYR A 137     4806   5406   9303    -21   -300    326       N  
ATOM   1089  CA  TYR A 137     -41.627  42.871  22.094  1.00 51.72           C  
ANISOU 1089  CA  TYR A 137     4846   5412   9390      2   -337    311       C  
ATOM   1090  C   TYR A 137     -42.900  42.048  22.297  1.00 51.99           C  
ANISOU 1090  C   TYR A 137     4843   5464   9445     32   -355    304       C  
ATOM   1091  O   TYR A 137     -43.435  42.025  23.426  1.00 51.87           O  
ANISOU 1091  O   TYR A 137     4777   5476   9454     54   -343    282       O  
ATOM   1092  CB  TYR A 137     -41.831  43.946  21.025  1.00 51.76           C  
ANISOU 1092  CB  TYR A 137     4910   5360   9397     -4   -377    335       C  
ATOM   1093  CG  TYR A 137     -40.860  45.094  21.114  1.00 52.01           C  
ANISOU 1093  CG  TYR A 137     4972   5362   9428    -40   -377    347       C  
ATOM   1094  CD1 TYR A 137     -40.215  45.573  19.984  1.00 52.53           C  
ANISOU 1094  CD1 TYR A 137     5086   5409   9464    -81   -384    395       C  
ATOM   1095  CD2 TYR A 137     -40.565  45.688  22.332  1.00 51.95           C  
ANISOU 1095  CD2 TYR A 137     4947   5347   9444    -39   -375    316       C  
ATOM   1096  CE1 TYR A 137     -39.310  46.619  20.059  1.00 52.59           C  
ANISOU 1096  CE1 TYR A 137     5116   5389   9474   -131   -393    421       C  
ATOM   1097  CE2 TYR A 137     -39.668  46.739  22.423  1.00 52.14           C  
ANISOU 1097  CE2 TYR A 137     5004   5333   9471    -84   -393    332       C  
ATOM   1098  CZ  TYR A 137     -39.042  47.205  21.282  1.00 52.36           C  
ANISOU 1098  CZ  TYR A 137     5072   5342   9478   -135   -404    389       C  
ATOM   1099  OH  TYR A 137     -38.163  48.237  21.363  1.00 53.28           O  
ANISOU 1099  OH  TYR A 137     5217   5422   9603   -194   -430    420       O  
ATOM   1100  N   ARG A 138     -43.349  41.381  21.232  1.00 52.78           N  
ANISOU 1100  N   ARG A 138     4969   5553   9532     30   -385    328       N  
ATOM   1101  CA  ARG A 138     -44.579  40.547  21.228  1.00 53.70           C  
ANISOU 1101  CA  ARG A 138     5051   5679   9672     42   -422    337       C  
ATOM   1102  C   ARG A 138     -44.519  39.533  22.381  1.00 54.14           C  
ANISOU 1102  C   ARG A 138     5050   5788   9732     35   -392    328       C  
ATOM   1103  O   ARG A 138     -45.597  39.147  22.860  1.00 54.97           O  
ANISOU 1103  O   ARG A 138     5099   5917   9869     41   -410    340       O  
ATOM   1104  CB  ARG A 138     -44.782  39.902  19.852  1.00 54.19           C  
ANISOU 1104  CB  ARG A 138     5173   5711   9705     32   -470    362       C  
ATOM   1105  CG  ARG A 138     -45.775  40.646  18.966  1.00 55.27           C  
ANISOU 1105  CG  ARG A 138     5333   5802   9865     44   -532    382       C  
ATOM   1106  CD  ARG A 138     -45.588  40.381  17.480  1.00 55.79           C  
ANISOU 1106  CD  ARG A 138     5490   5830   9878     32   -572    403       C  
ATOM   1107  NE  ARG A 138     -44.834  41.443  16.816  1.00 56.26           N  
ANISOU 1107  NE  ARG A 138     5607   5865   9904     26   -554    412       N  
ATOM   1108  CZ  ARG A 138     -44.024  41.287  15.765  1.00 56.79           C  
ANISOU 1108  CZ  ARG A 138     5750   5927   9898     14   -542    427       C  
ATOM   1109  NH1 ARG A 138     -43.821  40.096  15.225  1.00 57.19           N  
ANISOU 1109  NH1 ARG A 138     5841   5990   9898     21   -547    422       N  
ATOM   1110  NH2 ARG A 138     -43.402  42.336  15.255  1.00 57.09           N  
ANISOU 1110  NH2 ARG A 138     5828   5951   9912     -2   -526    449       N  
ATOM   1111  N   ALA A 139     -43.319  39.138  22.828  1.00 54.51           N  
ANISOU 1111  N   ALA A 139     5106   5856   9748     21   -350    315       N  
ATOM   1112  CA  ALA A 139     -43.098  38.284  24.020  1.00 54.34           C  
ANISOU 1112  CA  ALA A 139     5039   5880   9726     12   -324    307       C  
ATOM   1113  C   ALA A 139     -43.747  38.927  25.251  1.00 55.19           C  
ANISOU 1113  C   ALA A 139     5088   6018   9860     30   -303    292       C  
ATOM   1114  O   ALA A 139     -44.764  38.401  25.732  1.00 54.92           O  
ANISOU 1114  O   ALA A 139     5002   6017   9845     31   -312    309       O  
ATOM   1115  CB  ALA A 139     -41.625  38.054  24.244  1.00 53.72           C  
ANISOU 1115  CB  ALA A 139     4979   5815   9616      2   -287    295       C  
ATOM   1116  N   ARG A 140     -43.198  40.046  25.722  1.00 56.45           N  
ANISOU 1116  N   ARG A 140     5259   6169  10018     42   -279    265       N  
ATOM   1117  CA  ARG A 140     -43.591  40.666  27.017  1.00 58.21           C  
ANISOU 1117  CA  ARG A 140     5446   6421  10248     71   -255    237       C  
ATOM   1118  C   ARG A 140     -45.080  41.021  26.947  1.00 58.21           C  
ANISOU 1118  C   ARG A 140     5405   6431  10280    113   -270    242       C  
ATOM   1119  O   ARG A 140     -45.704  41.161  28.017  1.00 59.13           O  
ANISOU 1119  O   ARG A 140     5471   6596  10396    147   -242    227       O  
ATOM   1120  CB  ARG A 140     -42.716  41.882  27.346  1.00 60.22           C  
ANISOU 1120  CB  ARG A 140     5743   6641  10496     76   -249    204       C  
ATOM   1121  CG  ARG A 140     -41.292  41.781  26.810  1.00 61.97           C  
ANISOU 1121  CG  ARG A 140     6001   6843  10699     30   -247    218       C  
ATOM   1122  CD  ARG A 140     -40.221  42.492  27.615  1.00 63.08           C  
ANISOU 1122  CD  ARG A 140     6160   6974  10831     11   -242    197       C  
ATOM   1123  NE  ARG A 140     -39.266  43.133  26.719  1.00 64.66           N  
ANISOU 1123  NE  ARG A 140     6397   7138  11032    -26   -256    221       N  
ATOM   1124  CZ  ARG A 140     -38.822  44.385  26.831  1.00 66.57           C  
ANISOU 1124  CZ  ARG A 140     6678   7331  11285    -43   -284    215       C  
ATOM   1125  NH1 ARG A 140     -39.211  45.160  27.833  1.00 67.35           N  
ANISOU 1125  NH1 ARG A 140     6795   7405  11390    -13   -304    173       N  
ATOM   1126  NH2 ARG A 140     -37.968  44.854  25.938  1.00 66.96           N  
ANISOU 1126  NH2 ARG A 140     6750   7358  11333    -91   -295    255       N  
ATOM   1127  N   ALA A 141     -45.621  41.138  25.730  1.00 57.24           N  
ANISOU 1127  N   ALA A 141     5299   6269  10179    113   -313    265       N  
ATOM   1128  CA  ALA A 141     -47.064  41.319  25.451  1.00 57.35           C  
ANISOU 1128  CA  ALA A 141     5264   6292  10232    148   -343    284       C  
ATOM   1129  C   ALA A 141     -47.716  39.962  25.147  1.00 56.52           C  
ANISOU 1129  C   ALA A 141     5116   6219  10138    110   -369    332       C  
ATOM   1130  O   ALA A 141     -48.157  39.757  24.002  1.00 56.97           O  
ANISOU 1130  O   ALA A 141     5197   6237  10211     96   -425    360       O  
ATOM   1131  CB  ALA A 141     -47.238  42.290  24.306  1.00 57.69           C  
ANISOU 1131  CB  ALA A 141     5360   6265  10293    165   -390    284       C  
ATOM   1132  N   GLY A 142     -47.745  39.054  26.125  1.00 55.57           N  
ANISOU 1132  N   GLY A 142     4947   6159  10007     88   -338    345       N  
ATOM   1133  CA  GLY A 142     -48.543  37.810  26.079  1.00 55.25           C  
ANISOU 1133  CA  GLY A 142     4855   6152   9984     45   -371    401       C  
ATOM   1134  C   GLY A 142     -48.024  36.761  25.101  1.00 53.84           C  
ANISOU 1134  C   GLY A 142     4746   5919   9791     -3   -426    420       C  
ATOM   1135  O   GLY A 142     -48.066  35.578  25.479  1.00 53.13           O  
ANISOU 1135  O   GLY A 142     4641   5849   9696    -47   -442    452       O  
ATOM   1136  N   GLU A 143     -47.593  37.160  23.893  1.00 53.37           N  
ANISOU 1136  N   GLU A 143     4764   5794   9719      4   -456    405       N  
ATOM   1137  CA  GLU A 143     -47.260  36.268  22.740  1.00 53.84           C  
ANISOU 1137  CA  GLU A 143     4902   5798   9753    -23   -514    418       C  
ATOM   1138  C   GLU A 143     -45.760  35.935  22.732  1.00 52.75           C  
ANISOU 1138  C   GLU A 143     4829   5648   9563    -22   -476    387       C  
ATOM   1139  O   GLU A 143     -45.002  36.602  21.979  1.00 51.69           O  
ANISOU 1139  O   GLU A 143     4751   5486   9400     -4   -459    366       O  
ATOM   1140  CB  GLU A 143     -47.664  36.945  21.424  1.00 55.21           C  
ANISOU 1140  CB  GLU A 143     5125   5918   9931     -7   -564    423       C  
ATOM   1141  CG  GLU A 143     -47.125  36.273  20.161  1.00 55.77           C  
ANISOU 1141  CG  GLU A 143     5302   5934   9955    -19   -610    422       C  
ATOM   1142  CD  GLU A 143     -47.016  37.188  18.948  1.00 56.23           C  
ANISOU 1142  CD  GLU A 143     5428   5945   9989      0   -630    418       C  
ATOM   1143  OE1 GLU A 143     -47.972  37.948  18.698  1.00 58.07           O  
ANISOU 1143  OE1 GLU A 143     5633   6166  10264      9   -666    435       O  
ATOM   1144  OE2 GLU A 143     -45.979  37.144  18.256  1.00 55.53           O  
ANISOU 1144  OE2 GLU A 143     5419   5838   9839      7   -608    401       O  
ATOM   1145  N   ALA A 144     -45.353  34.914  23.500  1.00 52.06           N  
ANISOU 1145  N   ALA A 144     4729   5584   9464    -42   -466    390       N  
ATOM   1146  CA  ALA A 144     -43.943  34.484  23.678  1.00 50.81           C  
ANISOU 1146  CA  ALA A 144     4613   5426   9265    -34   -430    363       C  
ATOM   1147  C   ALA A 144     -43.701  33.120  23.018  1.00 50.15           C  
ANISOU 1147  C   ALA A 144     4596   5302   9154    -40   -486    370       C  
ATOM   1148  O   ALA A 144     -42.664  32.505  23.302  1.00 49.50           O  
ANISOU 1148  O   ALA A 144     4538   5225   9044    -28   -466    351       O  
ATOM   1149  CB  ALA A 144     -43.610  34.451  25.149  1.00 50.51           C  
ANISOU 1149  CB  ALA A 144     4519   5440   9233    -43   -383    357       C  
ATOM   1150  N   ALA A 145     -44.625  32.655  22.176  1.00 50.47           N  
ANISOU 1150  N   ALA A 145     4669   5301   9204    -55   -563    394       N  
ATOM   1151  CA  ALA A 145     -44.486  31.394  21.414  1.00 50.77           C  
ANISOU 1151  CA  ALA A 145     4796   5283   9211    -55   -636    394       C  
ATOM   1152  C   ALA A 145     -43.307  31.549  20.456  1.00 50.37           C  
ANISOU 1152  C   ALA A 145     4827   5214   9095      0   -603    351       C  
ATOM   1153  O   ALA A 145     -42.260  30.947  20.734  1.00 50.72           O  
ANISOU 1153  O   ALA A 145     4894   5267   9110     26   -575    327       O  
ATOM   1154  CB  ALA A 145     -45.765  31.050  20.688  1.00 51.52           C  
ANISOU 1154  CB  ALA A 145     4911   5333   9330    -87   -735    430       C  
ATOM   1155  N   ASN A 146     -43.464  32.370  19.411  1.00 50.34           N  
ANISOU 1155  N   ASN A 146     4860   5195   9072     15   -602    348       N  
ATOM   1156  CA  ASN A 146     -42.407  32.665  18.403  1.00 50.29           C  
ANISOU 1156  CA  ASN A 146     4925   5188   8995     63   -560    320       C  
ATOM   1157  C   ASN A 146     -41.065  32.875  19.115  1.00 49.13           C  
ANISOU 1157  C   ASN A 146     4734   5096   8835     84   -469    301       C  
ATOM   1158  O   ASN A 146     -40.091  32.159  18.795  1.00 49.21           O  
ANISOU 1158  O   ASN A 146     4789   5112   8794    128   -450    277       O  
ATOM   1159  CB  ASN A 146     -42.742  33.897  17.555  1.00 50.49           C  
ANISOU 1159  CB  ASN A 146     4963   5207   9013     60   -552    333       C  
ATOM   1160  CG  ASN A 146     -43.667  33.582  16.401  1.00 51.28           C  
ANISOU 1160  CG  ASN A 146     5143   5246   9092     58   -645    345       C  
ATOM   1161  OD1 ASN A 146     -44.673  32.898  16.577  1.00 52.19           O  
ANISOU 1161  OD1 ASN A 146     5252   5329   9247     29   -727    364       O  
ATOM   1162  ND2 ASN A 146     -43.334  34.075  15.221  1.00 51.35           N  
ANISOU 1162  ND2 ASN A 146     5228   5244   9038     83   -638    342       N  
ATOM   1163  N   PHE A 147     -41.034  33.819  20.056  1.00 47.54           N  
ANISOU 1163  N   PHE A 147     4450   4933   8679     57   -420    310       N  
ATOM   1164  CA  PHE A 147     -39.806  34.286  20.744  1.00 46.25           C  
ANISOU 1164  CA  PHE A 147     4240   4820   8512     63   -344    298       C  
ATOM   1165  C   PHE A 147     -39.037  33.079  21.278  1.00 45.75           C  
ANISOU 1165  C   PHE A 147     4178   4770   8434     86   -341    282       C  
ATOM   1166  O   PHE A 147     -37.835  32.991  20.986  1.00 46.87           O  
ANISOU 1166  O   PHE A 147     4327   4942   8539    122   -295    270       O  
ATOM   1167  CB  PHE A 147     -40.152  35.276  21.856  1.00 45.67           C  
ANISOU 1167  CB  PHE A 147     4091   4768   8491     31   -320    305       C  
ATOM   1168  CG  PHE A 147     -38.945  35.895  22.512  1.00 45.16           C  
ANISOU 1168  CG  PHE A 147     3989   4743   8426     26   -260    297       C  
ATOM   1169  CD1 PHE A 147     -37.970  36.516  21.749  1.00 44.95           C  
ANISOU 1169  CD1 PHE A 147     3978   4731   8368     32   -222    305       C  
ATOM   1170  CD2 PHE A 147     -38.787  35.848  23.887  1.00 44.81           C  
ANISOU 1170  CD2 PHE A 147     3891   4725   8409     11   -246    289       C  
ATOM   1171  CE1 PHE A 147     -36.859  37.078  22.350  1.00 45.20           C  
ANISOU 1171  CE1 PHE A 147     3966   4800   8407     16   -179    308       C  
ATOM   1172  CE2 PHE A 147     -37.677  36.415  24.489  1.00 44.79           C  
ANISOU 1172  CE2 PHE A 147     3857   4751   8407      1   -206    284       C  
ATOM   1173  CZ  PHE A 147     -36.716  37.027  23.718  1.00 45.28           C  
ANISOU 1173  CZ  PHE A 147     3929   4826   8450      1   -177    296       C  
ATOM   1174  N   CYS A 148     -39.717  32.192  22.011  1.00 44.96           N  
ANISOU 1174  N   CYS A 148     4068   4651   8362     66   -391    289       N  
ATOM   1175  CA  CYS A 148     -39.156  30.935  22.579  1.00 44.71           C  
ANISOU 1175  CA  CYS A 148     4050   4615   8322     83   -411    279       C  
ATOM   1176  C   CYS A 148     -38.591  30.066  21.447  1.00 44.80           C  
ANISOU 1176  C   CYS A 148     4152   4593   8276    145   -436    253       C  
ATOM   1177  O   CYS A 148     -37.380  29.775  21.477  1.00 44.86           O  
ANISOU 1177  O   CYS A 148     4159   4629   8255    195   -394    232       O  
ATOM   1178  CB  CYS A 148     -40.206  30.169  23.375  1.00 45.00           C  
ANISOU 1178  CB  CYS A 148     4071   4628   8397     36   -476    306       C  
ATOM   1179  SG  CYS A 148     -40.656  30.972  24.938  1.00 45.35           S  
ANISOU 1179  SG  CYS A 148     4009   4732   8488    -14   -431    328       S  
ATOM   1180  N   ALA A 149     -39.424  29.691  20.472  1.00 44.81           N  
ANISOU 1180  N   ALA A 149     4230   4538   8258    148   -503    255       N  
ATOM   1181  CA  ALA A 149     -39.011  28.938  19.262  1.00 45.04           C  
ANISOU 1181  CA  ALA A 149     4368   4527   8215    217   -534    223       C  
ATOM   1182  C   ALA A 149     -37.723  29.553  18.707  1.00 44.78           C  
ANISOU 1182  C   ALA A 149     4325   4558   8129    277   -435    203       C  
ATOM   1183  O   ALA A 149     -36.748  28.806  18.493  1.00 45.97           O  
ANISOU 1183  O   ALA A 149     4511   4721   8234    352   -417    172       O  
ATOM   1184  CB  ALA A 149     -40.105  28.937  18.224  1.00 45.23           C  
ANISOU 1184  CB  ALA A 149     4467   4492   8224    201   -610    232       C  
ATOM   1185  N   LEU A 150     -37.714  30.870  18.501  1.00 43.86           N  
ANISOU 1185  N   LEU A 150     4160   4483   8020    246   -376    225       N  
ATOM   1186  CA  LEU A 150     -36.521  31.598  17.999  1.00 43.79           C  
ANISOU 1186  CA  LEU A 150     4126   4543   7966    280   -282    226       C  
ATOM   1187  C   LEU A 150     -35.345  31.339  18.944  1.00 43.81           C  
ANISOU 1187  C   LEU A 150     4055   4603   7989    300   -230    220       C  
ATOM   1188  O   LEU A 150     -34.256  31.020  18.445  1.00 44.19           O  
ANISOU 1188  O   LEU A 150     4108   4698   7984    369   -179    206       O  
ATOM   1189  CB  LEU A 150     -36.826  33.093  17.877  1.00 43.02           C  
ANISOU 1189  CB  LEU A 150     3986   4465   7894    221   -250    261       C  
ATOM   1190  CG  LEU A 150     -37.514  33.518  16.584  1.00 43.31           C  
ANISOU 1190  CG  LEU A 150     4101   4468   7886    221   -279    271       C  
ATOM   1191  CD1 LEU A 150     -37.520  35.032  16.460  1.00 43.26           C  
ANISOU 1191  CD1 LEU A 150     4053   4482   7899    171   -242    308       C  
ATOM   1192  CD2 LEU A 150     -36.849  32.895  15.370  1.00 43.90           C  
ANISOU 1192  CD2 LEU A 150     4261   4557   7859    297   -259    251       C  
ATOM   1193  N   ILE A 151     -35.556  31.457  20.256  1.00 43.50           N  
ANISOU 1193  N   ILE A 151     3946   4563   8017    248   -242    230       N  
ATOM   1194  CA  ILE A 151     -34.473  31.257  21.264  1.00 43.81           C  
ANISOU 1194  CA  ILE A 151     3914   4651   8080    258   -204    228       C  
ATOM   1195  C   ILE A 151     -33.934  29.834  21.093  1.00 44.25           C  
ANISOU 1195  C   ILE A 151     4020   4692   8102    338   -232    196       C  
ATOM   1196  O   ILE A 151     -32.721  29.700  20.864  1.00 45.03           O  
ANISOU 1196  O   ILE A 151     4090   4847   8171    399   -177    188       O  
ATOM   1197  CB  ILE A 151     -34.957  31.558  22.699  1.00 43.30           C  
ANISOU 1197  CB  ILE A 151     3789   4580   8081    189   -224    242       C  
ATOM   1198  CG1 ILE A 151     -35.174  33.059  22.910  1.00 43.07           C  
ANISOU 1198  CG1 ILE A 151     3712   4572   8080    132   -190    264       C  
ATOM   1199  CG2 ILE A 151     -33.996  30.986  23.733  1.00 43.36           C  
ANISOU 1199  CG2 ILE A 151     3749   4618   8106    204   -216    237       C  
ATOM   1200  CD1 ILE A 151     -36.070  33.399  24.082  1.00 42.85           C  
ANISOU 1200  CD1 ILE A 151     3650   4529   8100     79   -216    269       C  
ATOM   1201  N   LEU A 152     -34.817  28.834  21.161  1.00 44.41           N  
ANISOU 1201  N   LEU A 152     4110   4636   8126    338   -318    184       N  
ATOM   1202  CA  LEU A 152     -34.506  27.397  20.933  1.00 45.17           C  
ANISOU 1202  CA  LEU A 152     4285   4687   8189    415   -374    149       C  
ATOM   1203  C   LEU A 152     -33.772  27.224  19.598  1.00 46.31           C  
ANISOU 1203  C   LEU A 152     4490   4853   8250    517   -333    116       C  
ATOM   1204  O   LEU A 152     -32.837  26.398  19.540  1.00 46.29           O  
ANISOU 1204  O   LEU A 152     4507   4865   8217    611   -325     83       O  
ATOM   1205  CB  LEU A 152     -35.812  26.597  20.952  1.00 45.22           C  
ANISOU 1205  CB  LEU A 152     4371   4599   8212    374   -486    154       C  
ATOM   1206  CG  LEU A 152     -36.346  26.279  22.347  1.00 44.82           C  
ANISOU 1206  CG  LEU A 152     4270   4532   8228    297   -532    187       C  
ATOM   1207  CD1 LEU A 152     -37.840  25.998  22.314  1.00 44.84           C  
ANISOU 1207  CD1 LEU A 152     4308   4470   8257    224   -620    218       C  
ATOM   1208  CD2 LEU A 152     -35.590  25.112  22.962  1.00 45.00           C  
ANISOU 1208  CD2 LEU A 152     4316   4532   8250    345   -571    171       C  
ATOM   1209  N   ALA A 153     -34.180  27.966  18.565  1.00 47.02           N  
ANISOU 1209  N   ALA A 153     4613   4951   8301    507   -309    123       N  
ATOM   1210  CA  ALA A 153     -33.540  27.938  17.229  1.00 48.57           C  
ANISOU 1210  CA  ALA A 153     4869   5182   8401    600   -259     98       C  
ATOM   1211  C   ALA A 153     -32.084  28.403  17.356  1.00 49.51           C  
ANISOU 1211  C   ALA A 153     4886   5416   8507    644   -145    110       C  
ATOM   1212  O   ALA A 153     -31.186  27.619  17.005  1.00 50.82           O  
ANISOU 1212  O   ALA A 153     5074   5613   8620    756   -119     75       O  
ATOM   1213  CB  ALA A 153     -34.311  28.788  16.249  1.00 48.56           C  
ANISOU 1213  CB  ALA A 153     4913   5168   8367    559   -259    118       C  
ATOM   1214  N   TYR A 154     -31.875  29.610  17.889  1.00 49.60           N  
ANISOU 1214  N   TYR A 154     4789   5485   8570    559    -89    159       N  
ATOM   1215  CA  TYR A 154     -30.577  30.335  17.919  1.00 50.31           C  
ANISOU 1215  CA  TYR A 154     4769   5688   8656    568     14    192       C  
ATOM   1216  C   TYR A 154     -29.573  29.622  18.833  1.00 51.30           C  
ANISOU 1216  C   TYR A 154     4825   5851   8816    617     23    179       C  
ATOM   1217  O   TYR A 154     -28.360  29.715  18.556  1.00 52.42           O  
ANISOU 1217  O   TYR A 154     4894   6091   8930    674    103    193       O  
ATOM   1218  CB  TYR A 154     -30.781  31.789  18.356  1.00 49.57           C  
ANISOU 1218  CB  TYR A 154     4600   5615   8619    450     37    246       C  
ATOM   1219  CG  TYR A 154     -31.138  32.739  17.241  1.00 49.57           C  
ANISOU 1219  CG  TYR A 154     4636   5624   8571    420     66    276       C  
ATOM   1220  CD1 TYR A 154     -30.264  32.962  16.189  1.00 50.33           C  
ANISOU 1220  CD1 TYR A 154     4726   5806   8590    470    147    298       C  
ATOM   1221  CD2 TYR A 154     -32.342  33.425  17.237  1.00 48.99           C  
ANISOU 1221  CD2 TYR A 154     4601   5481   8530    345     13    287       C  
ATOM   1222  CE1 TYR A 154     -30.577  33.832  15.158  1.00 50.48           C  
ANISOU 1222  CE1 TYR A 154     4787   5835   8559    436    170    333       C  
ATOM   1223  CE2 TYR A 154     -32.668  34.304  16.216  1.00 49.13           C  
ANISOU 1223  CE2 TYR A 154     4659   5501   8506    317     28    318       C  
ATOM   1224  CZ  TYR A 154     -31.781  34.512  15.176  1.00 49.83           C  
ANISOU 1224  CZ  TYR A 154     4750   5668   8513    358    104    343       C  
ATOM   1225  OH  TYR A 154     -32.095  35.374  14.170  1.00 50.13           O  
ANISOU 1225  OH  TYR A 154     4835   5708   8504    325    116    381       O  
ATOM   1226  N   CYS A 155     -30.045  28.956  19.893  1.00 51.30           N  
ANISOU 1226  N   CYS A 155     4835   5781   8872    592    -53    161       N  
ATOM   1227  CA  CYS A 155     -29.197  28.156  20.819  1.00 52.13           C  
ANISOU 1227  CA  CYS A 155     4890   5904   9011    638    -66    148       C  
ATOM   1228  C   CYS A 155     -29.058  26.728  20.280  1.00 53.26           C  
ANISOU 1228  C   CYS A 155     5134   6002   9101    765   -110     92       C  
ATOM   1229  O   CYS A 155     -28.384  25.914  20.932  1.00 53.16           O  
ANISOU 1229  O   CYS A 155     5098   5990   9109    822   -134     75       O  
ATOM   1230  CB  CYS A 155     -29.781  28.130  22.225  1.00 51.65           C  
ANISOU 1230  CB  CYS A 155     4804   5791   9027    548   -131    162       C  
ATOM   1231  SG  CYS A 155     -30.287  29.764  22.821  1.00 51.73           S  
ANISOU 1231  SG  CYS A 155     4741   5822   9090    411   -104    211       S  
ATOM   1232  N   ASN A 156     -29.701  26.447  19.141  1.00 53.98           N  
ANISOU 1232  N   ASN A 156     5340   6046   9123    807   -132     63       N  
ATOM   1233  CA  ASN A 156     -29.626  25.165  18.395  1.00 54.98           C  
ANISOU 1233  CA  ASN A 156     5592   6117   9178    938   -181      0       C  
ATOM   1234  C   ASN A 156     -29.983  24.017  19.341  1.00 54.59           C  
ANISOU 1234  C   ASN A 156     5593   5967   9179    936   -297    -19       C  
ATOM   1235  O   ASN A 156     -29.153  23.141  19.540  1.00 56.03           O  
ANISOU 1235  O   ASN A 156     5783   6152   9352   1040   -309    -53       O  
ATOM   1236  CB  ASN A 156     -28.263  24.980  17.725  1.00 56.19           C  
ANISOU 1236  CB  ASN A 156     5709   6376   9263   1079    -85    -22       C  
ATOM   1237  CG  ASN A 156     -28.319  24.018  16.557  1.00 57.78           C  
ANISOU 1237  CG  ASN A 156     6062   6531   9358   1221   -114    -91       C  
ATOM   1238  OD1 ASN A 156     -29.161  23.118  16.523  1.00 57.35           O  
ANISOU 1238  OD1 ASN A 156     6144   6347   9299   1229   -235   -130       O  
ATOM   1239  ND2 ASN A 156     -27.435  24.207  15.590  1.00 59.48           N  
ANISOU 1239  ND2 ASN A 156     6259   6854   9484   1330     -7   -103       N  
ATOM   1240  N   LYS A 157     -31.195  24.042  19.892  1.00 54.18           N  
ANISOU 1240  N   LYS A 157     5572   5833   9179    820   -380      4       N  
ATOM   1241  CA  LYS A 157     -31.734  23.003  20.808  1.00 54.01           C  
ANISOU 1241  CA  LYS A 157     5601   5712   9206    788   -499      4       C  
ATOM   1242  C   LYS A 157     -33.152  22.629  20.369  1.00 53.58           C  
ANISOU 1242  C   LYS A 157     5661   5550   9145    728   -604      8       C  
ATOM   1243  O   LYS A 157     -33.763  23.427  19.632  1.00 53.59           O  
ANISOU 1243  O   LYS A 157     5669   5565   9125    688   -576     20       O  
ATOM   1244  CB  LYS A 157     -31.742  23.538  22.239  1.00 53.26           C  
ANISOU 1244  CB  LYS A 157     5387   5655   9193    681   -483     55       C  
ATOM   1245  CG  LYS A 157     -30.489  24.304  22.634  1.00 53.13           C  
ANISOU 1245  CG  LYS A 157     5241   5754   9193    702   -377     69       C  
ATOM   1246  CD  LYS A 157     -30.344  24.452  24.122  1.00 52.90           C  
ANISOU 1246  CD  LYS A 157     5127   5740   9233    624   -392    104       C  
ATOM   1247  CE  LYS A 157     -30.361  23.117  24.834  1.00 53.28           C  
ANISOU 1247  CE  LYS A 157     5235   5709   9298    650   -494     94       C  
ATOM   1248  NZ  LYS A 157     -29.553  23.150  26.072  1.00 53.46           N  
ANISOU 1248  NZ  LYS A 157     5168   5775   9367    632   -487    117       N  
ATOM   1249  N   THR A 158     -33.646  21.468  20.815  1.00 53.71           N  
ANISOU 1249  N   THR A 158     5761   5461   9183    717   -730      5       N  
ATOM   1250  CA  THR A 158     -34.982  20.905  20.461  1.00 53.84           C  
ANISOU 1250  CA  THR A 158     5889   5364   9203    653   -857     17       C  
ATOM   1251  C   THR A 158     -35.842  20.798  21.728  1.00 52.83           C  
ANISOU 1251  C   THR A 158     5703   5210   9158    514   -918     86       C  
ATOM   1252  O   THR A 158     -35.280  20.621  22.832  1.00 52.27           O  
ANISOU 1252  O   THR A 158     5565   5169   9124    503   -902    103       O  
ATOM   1253  CB  THR A 158     -34.858  19.560  19.726  1.00 55.06           C  
ANISOU 1253  CB  THR A 158     6214   5404   9299    759   -971    -40       C  
ATOM   1254  OG1 THR A 158     -34.766  18.504  20.686  1.00 55.40           O  
ANISOU 1254  OG1 THR A 158     6285   5375   9386    748  -1069    -28       O  
ATOM   1255  CG2 THR A 158     -33.673  19.506  18.783  1.00 55.84           C  
ANISOU 1255  CG2 THR A 158     6351   5554   9311    928   -891   -113       C  
ATOM   1256  N   VAL A 159     -37.161  20.896  21.567  1.00 52.45           N  
ANISOU 1256  N   VAL A 159     5678   5115   9134    414   -986    127       N  
ATOM   1257  CA  VAL A 159     -38.125  20.952  22.702  1.00 52.30           C  
ANISOU 1257  CA  VAL A 159     5585   5097   9188    277  -1024    204       C  
ATOM   1258  C   VAL A 159     -38.068  19.614  23.445  1.00 52.84           C  
ANISOU 1258  C   VAL A 159     5716   5084   9277    263  -1140    222       C  
ATOM   1259  O   VAL A 159     -38.400  18.577  22.833  1.00 54.23           O  
ANISOU 1259  O   VAL A 159     6026   5144   9432    284  -1268    207       O  
ATOM   1260  CB  VAL A 159     -39.552  21.280  22.227  1.00 52.73           C  
ANISOU 1260  CB  VAL A 159     5646   5124   9264    185  -1078    247       C  
ATOM   1261  CG1 VAL A 159     -40.518  21.361  23.402  1.00 52.62           C  
ANISOU 1261  CG1 VAL A 159     5538   5136   9319     54  -1100    330       C  
ATOM   1262  CG2 VAL A 159     -39.590  22.558  21.398  1.00 52.23           C  
ANISOU 1262  CG2 VAL A 159     5542   5127   9176    206   -980    227       C  
ATOM   1263  N   GLY A 160     -37.658  19.652  24.715  1.00 52.15           N  
ANISOU 1263  N   GLY A 160     5542   5046   9224    228  -1103    253       N  
ATOM   1264  CA  GLY A 160     -37.454  18.465  25.565  1.00 52.52           C  
ANISOU 1264  CA  GLY A 160     5637   5025   9290    213  -1203    277       C  
ATOM   1265  C   GLY A 160     -36.046  18.433  26.127  1.00 52.17           C  
ANISOU 1265  C   GLY A 160     5555   5028   9238    303  -1140    240       C  
ATOM   1266  O   GLY A 160     -35.911  18.158  27.340  1.00 52.38           O  
ANISOU 1266  O   GLY A 160     5538   5068   9296    249  -1158    284       O  
ATOM   1267  N   GLU A 161     -35.046  18.700  25.275  1.00 51.66           N  
ANISOU 1267  N   GLU A 161     5501   4995   9129    433  -1070    167       N  
ATOM   1268  CA  GLU A 161     -33.601  18.790  25.632  1.00 51.24           C  
ANISOU 1268  CA  GLU A 161     5392   5007   9070    532   -997    131       C  
ATOM   1269  C   GLU A 161     -33.468  19.578  26.941  1.00 50.09           C  
ANISOU 1269  C   GLU A 161     5110   4951   8970    442   -927    182       C  
ATOM   1270  O   GLU A 161     -34.112  20.642  27.048  1.00 49.44           O  
ANISOU 1270  O   GLU A 161     4954   4930   8900    358   -860    212       O  
ATOM   1271  CB  GLU A 161     -32.826  19.457  24.488  1.00 51.58           C  
ANISOU 1271  CB  GLU A 161     5417   5118   9062    644   -890     71       C  
ATOM   1272  CG  GLU A 161     -31.309  19.447  24.649  1.00 52.14           C  
ANISOU 1272  CG  GLU A 161     5426   5259   9123    761   -820     36       C  
ATOM   1273  CD  GLU A 161     -30.498  19.937  23.453  1.00 52.68           C  
ANISOU 1273  CD  GLU A 161     5480   5402   9132    881   -717    -13       C  
ATOM   1274  OE1 GLU A 161     -29.286  20.160  23.618  1.00 53.07           O  
ANISOU 1274  OE1 GLU A 161     5441   5539   9182    957   -640    -25       O  
ATOM   1275  OE2 GLU A 161     -31.066  20.087  22.355  1.00 53.22           O  
ANISOU 1275  OE2 GLU A 161     5622   5446   9151    896   -715    -36       O  
ATOM   1276  N   LEU A 162     -32.692  19.064  27.906  1.00 50.02           N  
ANISOU 1276  N   LEU A 162     5080   4944   8981    461   -953    191       N  
ATOM   1277  CA  LEU A 162     -32.266  19.813  29.123  1.00 48.91           C  
ANISOU 1277  CA  LEU A 162     4820   4893   8871    402   -886    227       C  
ATOM   1278  C   LEU A 162     -31.631  21.132  28.686  1.00 47.89           C  
ANISOU 1278  C   LEU A 162     4591   4871   8734    432   -753    202       C  
ATOM   1279  O   LEU A 162     -31.290  21.256  27.497  1.00 48.02           O  
ANISOU 1279  O   LEU A 162     4630   4895   8717    518   -714    158       O  
ATOM   1280  CB  LEU A 162     -31.255  18.993  29.925  1.00 49.70           C  
ANISOU 1280  CB  LEU A 162     4925   4974   8985    456   -939    225       C  
ATOM   1281  CG  LEU A 162     -31.854  17.946  30.855  1.00 50.45           C  
ANISOU 1281  CG  LEU A 162     5087   4982   9096    381  -1064    277       C  
ATOM   1282  CD1 LEU A 162     -30.778  16.979  31.322  1.00 51.83           C  
ANISOU 1282  CD1 LEU A 162     5297   5114   9280    469  -1135    261       C  
ATOM   1283  CD2 LEU A 162     -32.541  18.605  32.040  1.00 49.63           C  
ANISOU 1283  CD2 LEU A 162     4909   4938   9008    241  -1032    345       C  
ATOM   1284  N   GLY A 163     -31.454  22.068  29.619  1.00 47.04           N  
ANISOU 1284  N   GLY A 163     4383   4840   8649    364   -691    232       N  
ATOM   1285  CA  GLY A 163     -30.991  23.429  29.291  1.00 46.25           C  
ANISOU 1285  CA  GLY A 163     4193   4832   8548    364   -580    222       C  
ATOM   1286  C   GLY A 163     -30.276  24.110  30.437  1.00 45.39           C  
ANISOU 1286  C   GLY A 163     3989   4789   8465    324   -544    243       C  
ATOM   1287  O   GLY A 163     -30.534  23.756  31.599  1.00 45.15           O  
ANISOU 1287  O   GLY A 163     3964   4742   8447    266   -594    273       O  
ATOM   1288  N   ASP A 164     -29.404  25.058  30.091  1.00 45.04           N  
ANISOU 1288  N   ASP A 164     3868   4819   8424    349   -465    233       N  
ATOM   1289  CA  ASP A 164     -28.664  25.933  31.036  1.00 44.67           C  
ANISOU 1289  CA  ASP A 164     3731   4838   8404    304   -432    254       C  
ATOM   1290  C   ASP A 164     -29.024  27.393  30.738  1.00 44.14           C  
ANISOU 1290  C   ASP A 164     3621   4811   8336    244   -362    261       C  
ATOM   1291  O   ASP A 164     -28.821  27.829  29.591  1.00 44.06           O  
ANISOU 1291  O   ASP A 164     3600   4825   8312    281   -309    250       O  
ATOM   1292  CB  ASP A 164     -27.158  25.700  30.932  1.00 44.66           C  
ANISOU 1292  CB  ASP A 164     3666   4885   8417    385   -419    248       C  
ATOM   1293  CG  ASP A 164     -26.361  26.697  31.742  1.00 44.34           C  
ANISOU 1293  CG  ASP A 164     3528   4910   8407    330   -393    274       C  
ATOM   1294  OD1 ASP A 164     -26.314  26.561  32.970  1.00 44.04           O  
ANISOU 1294  OD1 ASP A 164     3488   4860   8384    282   -444    291       O  
ATOM   1295  OD2 ASP A 164     -25.834  27.625  31.134  1.00 44.89           O  
ANISOU 1295  OD2 ASP A 164     3532   5039   8482    329   -328    281       O  
ATOM   1296  N   VAL A 165     -29.529  28.116  31.738  1.00 44.14           N  
ANISOU 1296  N   VAL A 165     3606   4818   8346    160   -365    278       N  
ATOM   1297  CA  VAL A 165     -29.962  29.538  31.604  1.00 44.26           C  
ANISOU 1297  CA  VAL A 165     3595   4857   8363    104   -314    281       C  
ATOM   1298  C   VAL A 165     -28.784  30.344  31.051  1.00 45.18           C  
ANISOU 1298  C   VAL A 165     3644   5027   8494    121   -267    286       C  
ATOM   1299  O   VAL A 165     -28.981  31.017  30.020  1.00 45.50           O  
ANISOU 1299  O   VAL A 165     3685   5078   8525    124   -221    285       O  
ATOM   1300  CB  VAL A 165     -30.471  30.109  32.941  1.00 43.90           C  
ANISOU 1300  CB  VAL A 165     3547   4814   8317     32   -330    290       C  
ATOM   1301  CG1 VAL A 165     -30.585  31.629  32.916  1.00 43.73           C  
ANISOU 1301  CG1 VAL A 165     3501   4812   8301     -9   -290    286       C  
ATOM   1302  CG2 VAL A 165     -31.798  29.484  33.328  1.00 43.64           C  
ANISOU 1302  CG2 VAL A 165     3566   4747   8267      6   -359    298       C  
ATOM   1303  N   ARG A 166     -27.612  30.232  31.694  1.00 46.02           N  
ANISOU 1303  N   ARG A 166     3693   5169   8621    129   -282    299       N  
ATOM   1304  CA  ARG A 166     -26.375  31.003  31.382  1.00 46.64           C  
ANISOU 1304  CA  ARG A 166     3684   5311   8723    128   -247    321       C  
ATOM   1305  C   ARG A 166     -25.909  30.738  29.947  1.00 47.13           C  
ANISOU 1305  C   ARG A 166     3726   5411   8769    204   -191    320       C  
ATOM   1306  O   ARG A 166     -25.603  31.725  29.250  1.00 47.15           O  
ANISOU 1306  O   ARG A 166     3687   5455   8773    179   -140    343       O  
ATOM   1307  CB  ARG A 166     -25.262  30.633  32.361  1.00 47.67           C  
ANISOU 1307  CB  ARG A 166     3757   5470   8884    132   -290    339       C  
ATOM   1308  CG  ARG A 166     -23.982  31.435  32.186  1.00 48.59           C  
ANISOU 1308  CG  ARG A 166     3768   5658   9034    114   -266    376       C  
ATOM   1309  CD  ARG A 166     -22.989  31.133  33.288  1.00 49.60           C  
ANISOU 1309  CD  ARG A 166     3840   5807   9198    106   -325    396       C  
ATOM   1310  NE  ARG A 166     -21.996  30.162  32.870  1.00 51.07           N  
ANISOU 1310  NE  ARG A 166     3963   6040   9399    203   -318    403       N  
ATOM   1311  CZ  ARG A 166     -20.884  30.461  32.203  1.00 52.82           C  
ANISOU 1311  CZ  ARG A 166     4074   6349   9646    233   -273    438       C  
ATOM   1312  NH1 ARG A 166     -20.610  31.715  31.868  1.00 52.83           N  
ANISOU 1312  NH1 ARG A 166     4018   6391   9662    156   -237    477       N  
ATOM   1313  NH2 ARG A 166     -20.047  29.494  31.869  1.00 54.11           N  
ANISOU 1313  NH2 ARG A 166     4182   6558   9818    342   -265    437       N  
ATOM   1314  N   GLU A 167     -25.833  29.461  29.547  1.00 47.69           N  
ANISOU 1314  N   GLU A 167     3832   5466   8821    295   -205    297       N  
ATOM   1315  CA  GLU A 167     -25.470  29.006  28.173  1.00 48.52           C  
ANISOU 1315  CA  GLU A 167     3942   5601   8891    393   -155    282       C  
ATOM   1316  C   GLU A 167     -26.345  29.745  27.153  1.00 48.21           C  
ANISOU 1316  C   GLU A 167     3949   5548   8818    364   -112    279       C  
ATOM   1317  O   GLU A 167     -25.789  30.288  26.172  1.00 47.95           O  
ANISOU 1317  O   GLU A 167     3875   5578   8764    387    -45    297       O  
ATOM   1318  CB  GLU A 167     -25.647  27.490  28.032  1.00 49.12           C  
ANISOU 1318  CB  GLU A 167     4095   5623   8945    489   -205    243       C  
ATOM   1319  CG  GLU A 167     -25.102  26.928  26.728  1.00 50.40           C  
ANISOU 1319  CG  GLU A 167     4268   5818   9061    614   -159    218       C  
ATOM   1320  CD  GLU A 167     -25.466  25.483  26.417  1.00 51.24           C  
ANISOU 1320  CD  GLU A 167     4485   5845   9136    711   -222    169       C  
ATOM   1321  OE1 GLU A 167     -25.626  24.683  27.367  1.00 51.48           O  
ANISOU 1321  OE1 GLU A 167     4550   5814   9193    703   -305    165       O  
ATOM   1322  OE2 GLU A 167     -25.590  25.159  25.216  1.00 51.94           O  
ANISOU 1322  OE2 GLU A 167     4634   5930   9168    794   -194    137       O  
ATOM   1323  N   THR A 168     -27.662  29.758  27.399  1.00 47.70           N  
ANISOU 1323  N   THR A 168     3964   5410   8750    314   -151    265       N  
ATOM   1324  CA  THR A 168     -28.702  30.420  26.570  1.00 47.23           C  
ANISOU 1324  CA  THR A 168     3955   5322   8666    281   -131    262       C  
ATOM   1325  C   THR A 168     -28.464  31.931  26.531  1.00 47.25           C  
ANISOU 1325  C   THR A 168     3901   5365   8687    209    -87    295       C  
ATOM   1326  O   THR A 168     -28.605  32.505  25.444  1.00 47.59           O  
ANISOU 1326  O   THR A 168     3957   5422   8702    212    -46    304       O  
ATOM   1327  CB  THR A 168     -30.106  30.125  27.107  1.00 46.73           C  
ANISOU 1327  CB  THR A 168     3961   5184   8608    236   -188    251       C  
ATOM   1328  OG1 THR A 168     -30.216  28.710  27.244  1.00 47.32           O  
ANISOU 1328  OG1 THR A 168     4089   5216   8673    288   -243    232       O  
ATOM   1329  CG2 THR A 168     -31.206  30.659  26.216  1.00 46.39           C  
ANISOU 1329  CG2 THR A 168     3968   5110   8546    214   -179    248       C  
ATOM   1330  N   MET A 169     -28.128  32.543  27.671  1.00 47.47           N  
ANISOU 1330  N   MET A 169     3878   5402   8753    145   -106    312       N  
ATOM   1331  CA  MET A 169     -27.912  34.012  27.793  1.00 48.29           C  
ANISOU 1331  CA  MET A 169     3941   5525   8879     67    -89    342       C  
ATOM   1332  C   MET A 169     -26.682  34.427  26.974  1.00 50.83           C  
ANISOU 1332  C   MET A 169     4187   5924   9200     78    -35    383       C  
ATOM   1333  O   MET A 169     -26.774  35.440  26.251  1.00 52.11           O  
ANISOU 1333  O   MET A 169     4349   6095   9355     37     -6    411       O  
ATOM   1334  CB  MET A 169     -27.728  34.431  29.255  1.00 47.35           C  
ANISOU 1334  CB  MET A 169     3799   5394   8795      6   -134    345       C  
ATOM   1335  CG  MET A 169     -28.965  34.192  30.108  1.00 46.39           C  
ANISOU 1335  CG  MET A 169     3743   5216   8666    -10   -173    314       C  
ATOM   1336  SD  MET A 169     -30.438  35.053  29.511  1.00 44.96           S  
ANISOU 1336  SD  MET A 169     3623   4988   8471    -34   -160    301       S  
ATOM   1337  CE  MET A 169     -30.446  36.466  30.613  1.00 44.91           C  
ANISOU 1337  CE  MET A 169     3612   4965   8484   -104   -185    299       C  
ATOM   1338  N   SER A 170     -25.580  33.679  27.075  1.00 52.90           N  
ANISOU 1338  N   SER A 170     4384   6244   9469    133    -24    393       N  
ATOM   1339  CA  SER A 170     -24.378  33.837  26.215  1.00 54.89           C  
ANISOU 1339  CA  SER A 170     4548   6594   9713    165     39    436       C  
ATOM   1340  C   SER A 170     -24.808  34.046  24.761  1.00 56.25           C  
ANISOU 1340  C   SER A 170     4766   6778   9828    196     98    438       C  
ATOM   1341  O   SER A 170     -24.610  35.153  24.237  1.00 57.17           O  
ANISOU 1341  O   SER A 170     4852   6926   9943    132    130    487       O  
ATOM   1342  CB  SER A 170     -23.452  32.657  26.331  1.00 55.88           C  
ANISOU 1342  CB  SER A 170     4622   6770   9839    264     45    425       C  
ATOM   1343  OG  SER A 170     -22.359  32.951  27.187  1.00 57.00           O  
ANISOU 1343  OG  SER A 170     4656   6965  10036    224     25    467       O  
ATOM   1344  N   TYR A 171     -25.399  33.021  24.146  1.00 57.69           N  
ANISOU 1344  N   TYR A 171     5029   6927   9961    285    100    388       N  
ATOM   1345  CA  TYR A 171     -25.692  32.976  22.688  1.00 59.58           C  
ANISOU 1345  CA  TYR A 171     5324   7183  10130    339    152    383       C  
ATOM   1346  C   TYR A 171     -26.621  34.138  22.311  1.00 58.19           C  
ANISOU 1346  C   TYR A 171     5196   6961   9952    249    146    403       C  
ATOM   1347  O   TYR A 171     -26.330  34.818  21.310  1.00 57.91           O  
ANISOU 1347  O   TYR A 171     5147   6976   9879    237    201    443       O  
ATOM   1348  CB  TYR A 171     -26.227  31.599  22.286  1.00 61.77           C  
ANISOU 1348  CB  TYR A 171     5698   7409  10361    445    126    319       C  
ATOM   1349  CG  TYR A 171     -25.147  30.582  21.999  1.00 64.60           C  
ANISOU 1349  CG  TYR A 171     6019   7833  10691    570    160    302       C  
ATOM   1350  CD1 TYR A 171     -24.026  30.470  22.811  1.00 65.87           C  
ANISOU 1350  CD1 TYR A 171     6067   8058  10901    578    166    326       C  
ATOM   1351  CD2 TYR A 171     -25.241  29.728  20.911  1.00 66.54           C  
ANISOU 1351  CD2 TYR A 171     6346   8077  10858    688    180    259       C  
ATOM   1352  CE1 TYR A 171     -23.029  29.540  22.554  1.00 68.29           C  
ANISOU 1352  CE1 TYR A 171     6331   8430  11186    707    196    309       C  
ATOM   1353  CE2 TYR A 171     -24.253  28.792  20.639  1.00 69.05           C  
ANISOU 1353  CE2 TYR A 171     6634   8455  11144    823    211    234       C  
ATOM   1354  CZ  TYR A 171     -23.141  28.694  21.461  1.00 69.81           C  
ANISOU 1354  CZ  TYR A 171     6607   8621  11297    836    222    260       C  
ATOM   1355  OH  TYR A 171     -22.169  27.771  21.182  1.00 70.22           O  
ANISOU 1355  OH  TYR A 171     6623   8737  11321    983    254    235       O  
ATOM   1356  N   LEU A 172     -27.677  34.376  23.098  1.00 56.50           N  
ANISOU 1356  N   LEU A 172     5033   6660   9774    191     82    380       N  
ATOM   1357  CA  LEU A 172     -28.652  35.480  22.864  1.00 55.47           C  
ANISOU 1357  CA  LEU A 172     4949   6476   9649    117     65    392       C  
ATOM   1358  C   LEU A 172     -27.927  36.826  22.959  1.00 55.17           C  
ANISOU 1358  C   LEU A 172     4844   6476   9640     33     84    451       C  
ATOM   1359  O   LEU A 172     -28.284  37.738  22.184  1.00 55.61           O  
ANISOU 1359  O   LEU A 172     4930   6519   9679     -6     95    480       O  
ATOM   1360  CB  LEU A 172     -29.796  35.407  23.883  1.00 54.76           C  
ANISOU 1360  CB  LEU A 172     4904   6305   9595     84      0    357       C  
ATOM   1361  CG  LEU A 172     -30.724  34.197  23.769  1.00 54.39           C  
ANISOU 1361  CG  LEU A 172     4930   6209   9527    140    -35    313       C  
ATOM   1362  CD1 LEU A 172     -31.665  34.137  24.960  1.00 53.92           C  
ANISOU 1362  CD1 LEU A 172     4884   6097   9506     99    -88    296       C  
ATOM   1363  CD2 LEU A 172     -31.508  34.210  22.465  1.00 54.29           C  
ANISOU 1363  CD2 LEU A 172     4992   6167   9469    163    -31    308       C  
ATOM   1364  N   PHE A 173     -26.950  36.941  23.864  1.00 54.13           N  
ANISOU 1364  N   PHE A 173     4629   6385   9552      4     78    474       N  
ATOM   1365  CA  PHE A 173     -26.130  38.164  24.060  1.00 54.05           C  
ANISOU 1365  CA  PHE A 173     4548   6408   9578    -87     78    538       C  
ATOM   1366  C   PHE A 173     -25.264  38.412  22.817  1.00 55.74           C  
ANISOU 1366  C   PHE A 173     4707   6716   9754    -79    152    602       C  
ATOM   1367  O   PHE A 173     -25.012  39.591  22.520  1.00 56.12           O  
ANISOU 1367  O   PHE A 173     4734   6771   9815   -167    151    665       O  
ATOM   1368  CB  PHE A 173     -25.318  38.062  25.354  1.00 53.48           C  
ANISOU 1368  CB  PHE A 173     4405   6353   9559   -116     39    545       C  
ATOM   1369  CG  PHE A 173     -26.065  38.399  26.621  1.00 52.64           C  
ANISOU 1369  CG  PHE A 173     4352   6162   9486   -161    -33    505       C  
ATOM   1370  CD1 PHE A 173     -25.390  38.491  27.829  1.00 52.59           C  
ANISOU 1370  CD1 PHE A 173     4300   6160   9522   -200    -81    512       C  
ATOM   1371  CD2 PHE A 173     -27.432  38.645  26.616  1.00 51.99           C  
ANISOU 1371  CD2 PHE A 173     4362   6000   9389   -160    -55    462       C  
ATOM   1372  CE1 PHE A 173     -26.063  38.805  29.001  1.00 51.88           C  
ANISOU 1372  CE1 PHE A 173     4267   5999   9446   -233   -143    472       C  
ATOM   1373  CE2 PHE A 173     -28.104  38.957  27.788  1.00 51.28           C  
ANISOU 1373  CE2 PHE A 173     4314   5848   9319   -189   -111    425       C  
ATOM   1374  CZ  PHE A 173     -27.419  39.036  28.979  1.00 51.33           C  
ANISOU 1374  CZ  PHE A 173     4286   5861   9355   -223   -152    428       C  
ATOM   1375  N   GLN A 174     -24.850  37.357  22.099  1.00 57.20           N  
ANISOU 1375  N   GLN A 174     4875   6969   9889     22    212    589       N  
ATOM   1376  CA  GLN A 174     -24.086  37.462  20.821  1.00 58.73           C  
ANISOU 1376  CA  GLN A 174     5022   7269  10024     53    300    644       C  
ATOM   1377  C   GLN A 174     -24.862  38.324  19.825  1.00 59.04           C  
ANISOU 1377  C   GLN A 174     5140   7269  10020      6    308    668       C  
ATOM   1378  O   GLN A 174     -24.244  39.192  19.177  1.00 60.17           O  
ANISOU 1378  O   GLN A 174     5233   7480  10149    -54    350    750       O  
ATOM   1379  CB  GLN A 174     -23.874  36.100  20.157  1.00 59.77           C  
ANISOU 1379  CB  GLN A 174     5169   7450  10088    198    353    597       C  
ATOM   1380  CG  GLN A 174     -23.147  35.094  21.030  1.00 60.28           C  
ANISOU 1380  CG  GLN A 174     5167   7545  10189    267    340    567       C  
ATOM   1381  CD  GLN A 174     -21.882  35.682  21.596  1.00 61.40           C  
ANISOU 1381  CD  GLN A 174     5160   7777  10390    204    355    643       C  
ATOM   1382  OE1 GLN A 174     -21.744  35.835  22.807  1.00 61.37           O  
ANISOU 1382  OE1 GLN A 174     5123   7735  10459    145    288    642       O  
ATOM   1383  NE2 GLN A 174     -20.962  36.046  20.715  1.00 63.17           N  
ANISOU 1383  NE2 GLN A 174     5292   8127  10582    210    440    715       N  
ATOM   1384  N   HIS A 175     -26.168  38.064  19.715  1.00 58.54           N  
ANISOU 1384  N   HIS A 175     5195   7105   9939     31    263    604       N  
ATOM   1385  CA  HIS A 175     -27.125  38.776  18.829  1.00 58.22           C  
ANISOU 1385  CA  HIS A 175     5248   7008   9863     -2    251    614       C  
ATOM   1386  C   HIS A 175     -27.677  40.020  19.535  1.00 56.90           C  
ANISOU 1386  C   HIS A 175     5097   6758   9763   -110    181    632       C  
ATOM   1387  O   HIS A 175     -28.642  40.589  19.014  1.00 56.60           O  
ANISOU 1387  O   HIS A 175     5141   6651   9711   -133    151    628       O  
ATOM   1388  CB  HIS A 175     -28.236  37.815  18.385  1.00 58.03           C  
ANISOU 1388  CB  HIS A 175     5333   6920   9793     81    227    540       C  
ATOM   1389  CG  HIS A 175     -27.729  36.642  17.613  1.00 59.25           C  
ANISOU 1389  CG  HIS A 175     5498   7140   9872    197    284    514       C  
ATOM   1390  ND1 HIS A 175     -27.494  36.700  16.252  1.00 60.28           N  
ANISOU 1390  ND1 HIS A 175     5663   7330   9911    237    346    541       N  
ATOM   1391  CD2 HIS A 175     -27.401  35.390  18.004  1.00 59.83           C  
ANISOU 1391  CD2 HIS A 175     5563   7227   9941    289    284    462       C  
ATOM   1392  CE1 HIS A 175     -27.042  35.533  15.836  1.00 61.09           C  
ANISOU 1392  CE1 HIS A 175     5778   7482   9952    358    386    499       C  
ATOM   1393  NE2 HIS A 175     -26.977  34.709  16.893  1.00 60.71           N  
ANISOU 1393  NE2 HIS A 175     5704   7401   9960    392    344    451       N  
ATOM   1394  N   ALA A 176     -27.093  40.422  20.670  1.00 56.49           N  
ANISOU 1394  N   ALA A 176     4976   6707   9779   -169    150    647       N  
ATOM   1395  CA  ALA A 176     -27.434  41.668  21.393  1.00 56.90           C  
ANISOU 1395  CA  ALA A 176     5048   6680   9890   -267     79    663       C  
ATOM   1396  C   ALA A 176     -26.526  42.790  20.895  1.00 58.81           C  
ANISOU 1396  C   ALA A 176     5239   6967  10140   -362     90    762       C  
ATOM   1397  O   ALA A 176     -25.662  42.512  20.045  1.00 60.28           O  
ANISOU 1397  O   ALA A 176     5361   7259  10282   -346    165    818       O  
ATOM   1398  CB  ALA A 176     -27.306  41.481  22.881  1.00 56.39           C  
ANISOU 1398  CB  ALA A 176     4954   6586   9882   -279     29    624       C  
ATOM   1399  N   ASN A 177     -26.737  44.009  21.401  1.00 60.01           N  
ANISOU 1399  N   ASN A 177     5420   7039  10340   -454     16    784       N  
ATOM   1400  CA  ASN A 177     -25.972  45.228  21.025  1.00 61.59           C  
ANISOU 1400  CA  ASN A 177     5587   7255  10559   -569     -2    887       C  
ATOM   1401  C   ASN A 177     -25.182  45.698  22.251  1.00 62.51           C  
ANISOU 1401  C   ASN A 177     5645   7358  10747   -646    -66    907       C  
ATOM   1402  O   ASN A 177     -25.397  46.836  22.709  1.00 63.25           O  
ANISOU 1402  O   ASN A 177     5792   7357  10882   -729   -155    921       O  
ATOM   1403  CB  ASN A 177     -26.895  46.315  20.468  1.00 61.51           C  
ANISOU 1403  CB  ASN A 177     5684   7143  10543   -615    -56    899       C  
ATOM   1404  CG  ASN A 177     -26.151  47.398  19.717  1.00 62.30           C  
ANISOU 1404  CG  ASN A 177     5760   7269  10641   -728    -62   1020       C  
ATOM   1405  OD1 ASN A 177     -24.927  47.498  19.799  1.00 62.05           O  
ANISOU 1405  OD1 ASN A 177     5622   7326  10626   -791    -39   1099       O  
ATOM   1406  ND2 ASN A 177     -26.889  48.212  18.980  1.00 62.45           N  
ANISOU 1406  ND2 ASN A 177     5873   7213  10641   -758    -99   1041       N  
ATOM   1407  N   LEU A 178     -24.288  44.842  22.743  1.00 63.04           N  
ANISOU 1407  N   LEU A 178     5610   7513  10825   -614    -30    908       N  
ATOM   1408  CA  LEU A 178     -23.510  45.060  23.989  1.00 63.56           C  
ANISOU 1408  CA  LEU A 178     5616   7574  10957   -674    -95    920       C  
ATOM   1409  C   LEU A 178     -22.113  45.587  23.648  1.00 64.81           C  
ANISOU 1409  C   LEU A 178     5652   7829  11143   -772    -84   1045       C  
ATOM   1410  O   LEU A 178     -21.343  45.827  24.592  1.00 65.79           O  
ANISOU 1410  O   LEU A 178     5715   7955  11326   -837   -147   1073       O  
ATOM   1411  CB  LEU A 178     -23.421  43.729  24.742  1.00 63.14           C  
ANISOU 1411  CB  LEU A 178     5527   7558  10903   -576    -70    848       C  
ATOM   1412  CG  LEU A 178     -24.756  43.023  24.978  1.00 61.95           C  
ANISOU 1412  CG  LEU A 178     5480   7336  10722   -481    -70    741       C  
ATOM   1413  CD1 LEU A 178     -24.540  41.618  25.522  1.00 61.65           C  
ANISOU 1413  CD1 LEU A 178     5401   7345  10676   -390    -42    690       C  
ATOM   1414  CD2 LEU A 178     -25.645  43.836  25.911  1.00 61.15           C  
ANISOU 1414  CD2 LEU A 178     5473   7111  10646   -520   -159    690       C  
ATOM   1415  N   ASP A 179     -21.804  45.766  22.359  1.00 65.27           N  
ANISOU 1415  N   ASP A 179     5672   7967  11157   -786     -9   1125       N  
ATOM   1416  CA  ASP A 179     -20.425  46.041  21.863  1.00 66.49           C  
ANISOU 1416  CA  ASP A 179     5680   8258  11324   -863     34   1257       C  
ATOM   1417  C   ASP A 179     -19.839  47.290  22.543  1.00 66.30           C  
ANISOU 1417  C   ASP A 179     5633   8177  11379  -1027    -81   1340       C  
ATOM   1418  O   ASP A 179     -18.595  47.368  22.609  1.00 68.51           O  
ANISOU 1418  O   ASP A 179     5768   8565  11697  -1095    -71   1441       O  
ATOM   1419  CB  ASP A 179     -20.370  46.129  20.332  1.00 67.65           C  
ANISOU 1419  CB  ASP A 179     5815   8493  11393   -853    135   1328       C  
ATOM   1420  CG  ASP A 179     -21.454  46.982  19.697  1.00 67.47           C  
ANISOU 1420  CG  ASP A 179     5939   8356  11340   -891     94   1321       C  
ATOM   1421  OD1 ASP A 179     -21.557  46.966  18.454  1.00 67.60           O  
ANISOU 1421  OD1 ASP A 179     5969   8434  11281   -870    172   1365       O  
ATOM   1422  OD2 ASP A 179     -22.189  47.646  20.449  1.00 67.92           O  
ANISOU 1422  OD2 ASP A 179     6098   8265  11444   -933    -14   1271       O  
ATOM   1423  N   SER A 180     -20.677  48.214  23.036  1.00 64.16           N  
ANISOU 1423  N   SER A 180     5499   7744  11134  -1083   -192   1299       N  
ATOM   1424  CA  SER A 180     -20.249  49.447  23.755  1.00 63.74           C  
ANISOU 1424  CA  SER A 180     5463   7601  11153  -1233   -330   1359       C  
ATOM   1425  C   SER A 180     -20.401  49.288  25.279  1.00 62.14           C  
ANISOU 1425  C   SER A 180     5304   7310  10995  -1214   -425   1265       C  
ATOM   1426  O   SER A 180     -20.343  50.319  25.974  1.00 62.01           O  
ANISOU 1426  O   SER A 180     5353   7180  11027  -1315   -557   1279       O  
ATOM   1427  CB  SER A 180     -20.987  50.659  23.243  1.00 63.70           C  
ANISOU 1427  CB  SER A 180     5589   7472  11141  -1306   -400   1382       C  
ATOM   1428  OG  SER A 180     -22.302  50.719  23.767  1.00 62.56           O  
ANISOU 1428  OG  SER A 180     5597   7187  10985  -1225   -450   1250       O  
ATOM   1429  N   CYS A 181     -20.581  48.058  25.778  1.00 60.47           N  
ANISOU 1429  N   CYS A 181     5068   7143  10765  -1090   -367   1174       N  
ATOM   1430  CA  CYS A 181     -20.360  47.673  27.201  1.00 60.18           C  
ANISOU 1430  CA  CYS A 181     5028   7073  10765  -1074   -437   1111       C  
ATOM   1431  C   CYS A 181     -18.882  47.294  27.372  1.00 61.14           C  
ANISOU 1431  C   CYS A 181     4974   7324  10931  -1121   -424   1204       C  
ATOM   1432  O   CYS A 181     -18.325  46.629  26.464  1.00 62.07           O  
ANISOU 1432  O   CYS A 181     4975   7583  11026  -1075   -309   1258       O  
ATOM   1433  CB  CYS A 181     -21.244  46.510  27.647  1.00 59.31           C  
ANISOU 1433  CB  CYS A 181     4970   6950  10612   -928   -386    984       C  
ATOM   1434  SG  CYS A 181     -23.004  46.923  27.812  1.00 59.46           S  
ANISOU 1434  SG  CYS A 181     5178   6821  10593   -871   -418    869       S  
ATOM   1435  N   LYS A 182     -18.272  47.689  28.491  1.00 60.42           N  
ANISOU 1435  N   LYS A 182     4868   7189  10898  -1202   -541   1219       N  
ATOM   1436  CA  LYS A 182     -16.798  47.687  28.675  1.00 61.07           C  
ANISOU 1436  CA  LYS A 182     4780   7379  11043  -1289   -566   1334       C  
ATOM   1437  C   LYS A 182     -16.473  47.373  30.140  1.00 60.88           C  
ANISOU 1437  C   LYS A 182     4762   7310  11057  -1289   -667   1282       C  
ATOM   1438  O   LYS A 182     -16.958  48.113  31.012  1.00 60.97           O  
ANISOU 1438  O   LYS A 182     4910   7178  11077  -1339   -790   1229       O  
ATOM   1439  CB  LYS A 182     -16.272  49.054  28.224  1.00 62.38           C  
ANISOU 1439  CB  LYS A 182     4928   7519  11251  -1461   -642   1464       C  
ATOM   1440  CG  LYS A 182     -14.786  49.316  28.422  1.00 63.89           C  
ANISOU 1440  CG  LYS A 182     4945   7808  11519  -1588   -694   1605       C  
ATOM   1441  CD  LYS A 182     -14.427  50.777  28.240  1.00 65.38           C  
ANISOU 1441  CD  LYS A 182     5158   7925  11757  -1779   -815   1724       C  
ATOM   1442  CE  LYS A 182     -13.200  51.203  29.020  1.00 66.79           C  
ANISOU 1442  CE  LYS A 182     5227   8121  12026  -1923   -946   1828       C  
ATOM   1443  NZ  LYS A 182     -13.055  52.679  29.051  1.00 67.82           N  
ANISOU 1443  NZ  LYS A 182     5436   8128  12204  -2112  -1104   1919       N  
ATOM   1444  N   ARG A 183     -15.679  46.323  30.389  1.00 60.95           N  
ANISOU 1444  N   ARG A 183     4634   7438  11084  -1228   -620   1295       N  
ATOM   1445  CA  ARG A 183     -15.196  45.914  31.739  1.00 61.00           C  
ANISOU 1445  CA  ARG A 183     4625   7423  11129  -1229   -715   1262       C  
ATOM   1446  C   ARG A 183     -13.665  46.040  31.788  1.00 62.85           C  
ANISOU 1446  C   ARG A 183     4664   7771  11442  -1326   -755   1399       C  
ATOM   1447  O   ARG A 183     -13.039  45.933  30.719  1.00 63.25           O  
ANISOU 1447  O   ARG A 183     4569   7959  11501  -1330   -654   1496       O  
ATOM   1448  CB  ARG A 183     -15.668  44.487  32.042  1.00 59.47           C  
ANISOU 1448  CB  ARG A 183     4446   7259  10889  -1064   -637   1156       C  
ATOM   1449  CG  ARG A 183     -15.188  43.915  33.369  1.00 59.41           C  
ANISOU 1449  CG  ARG A 183     4421   7239  10910  -1051   -725   1124       C  
ATOM   1450  CD  ARG A 183     -15.908  42.628  33.732  1.00 58.34           C  
ANISOU 1450  CD  ARG A 183     4347   7098  10721   -902   -667   1013       C  
ATOM   1451  NE  ARG A 183     -17.031  42.843  34.639  1.00 57.63           N  
ANISOU 1451  NE  ARG A 183     4438   6873  10585   -890   -728    909       N  
ATOM   1452  CZ  ARG A 183     -18.022  41.979  34.865  1.00 56.74           C  
ANISOU 1452  CZ  ARG A 183     4414   6730  10413   -780   -678    812       C  
ATOM   1453  NH1 ARG A 183     -18.062  40.813  34.238  1.00 56.40           N  
ANISOU 1453  NH1 ARG A 183     4313   6765  10351   -670   -577    799       N  
ATOM   1454  NH2 ARG A 183     -18.985  42.291  35.719  1.00 56.21           N  
ANISOU 1454  NH2 ARG A 183     4496   6556  10304   -778   -732    731       N  
ATOM   1455  N   VAL A 184     -13.098  46.267  32.980  1.00 64.11           N  
ANISOU 1455  N   VAL A 184     4822   7881  11656  -1400   -896   1408       N  
ATOM   1456  CA  VAL A 184     -11.624  46.300  33.235  1.00 67.03           C  
ANISOU 1456  CA  VAL A 184     4999   8356  12113  -1493   -957   1535       C  
ATOM   1457  C   VAL A 184     -11.314  45.544  34.539  1.00 67.68           C  
ANISOU 1457  C   VAL A 184     5082   8418  12213  -1445  -1040   1475       C  
ATOM   1458  O   VAL A 184     -11.933  45.865  35.574  1.00 66.78           O  
ANISOU 1458  O   VAL A 184     5139   8157  12075  -1462  -1152   1386       O  
ATOM   1459  CB  VAL A 184     -11.090  47.747  33.263  1.00 68.55           C  
ANISOU 1459  CB  VAL A 184     5188   8489  12368  -1696  -1093   1652       C  
ATOM   1460  CG1 VAL A 184      -9.592  47.799  33.517  1.00 70.55           C  
ANISOU 1460  CG1 VAL A 184     5231   8856  12718  -1804  -1164   1795       C  
ATOM   1461  CG2 VAL A 184     -11.422  48.493  31.982  1.00 68.79           C  
ANISOU 1461  CG2 VAL A 184     5228   8533  12374  -1748  -1018   1717       C  
ATOM   1462  N   LEU A 185     -10.364  44.599  34.485  1.00 69.79           N  
ANISOU 1462  N   LEU A 185     5164   8832  12521  -1384   -989   1526       N  
ATOM   1463  CA  LEU A 185      -9.996  43.662  35.587  1.00 70.72           C  
ANISOU 1463  CA  LEU A 185     5260   8953  12655  -1315  -1051   1476       C  
ATOM   1464  C   LEU A 185      -8.485  43.705  35.856  1.00 73.07           C  
ANISOU 1464  C   LEU A 185     5343   9362  13055  -1400  -1127   1610       C  
ATOM   1465  O   LEU A 185      -7.721  43.455  34.905  1.00 73.49           O  
ANISOU 1465  O   LEU A 185     5199   9581  13143  -1379  -1021   1709       O  
ATOM   1466  CB  LEU A 185     -10.394  42.243  35.172  1.00 69.76           C  
ANISOU 1466  CB  LEU A 185     5121   8904  12479  -1119   -904   1395       C  
ATOM   1467  CG  LEU A 185     -11.870  41.904  35.329  1.00 68.42           C  
ANISOU 1467  CG  LEU A 185     5163   8617  12217  -1025   -863   1251       C  
ATOM   1468  CD1 LEU A 185     -12.212  40.620  34.588  1.00 67.97           C  
ANISOU 1468  CD1 LEU A 185     5076   8638  12111   -851   -714   1196       C  
ATOM   1469  CD2 LEU A 185     -12.233  41.801  36.800  1.00 68.34           C  
ANISOU 1469  CD2 LEU A 185     5289   8486  12191  -1035   -992   1171       C  
ATOM   1470  N   ASN A 186      -8.085  43.942  37.112  1.00 74.56           N  
ANISOU 1470  N   ASN A 186     5569   9472  13286  -1481  -1300   1611       N  
ATOM   1471  CA  ASN A 186      -6.676  43.860  37.592  1.00 77.43           C  
ANISOU 1471  CA  ASN A 186     5737   9928  13752  -1555  -1401   1728       C  
ATOM   1472  C   ASN A 186      -6.526  42.653  38.526  1.00 77.85           C  
ANISOU 1472  C   ASN A 186     5790   9988  13800  -1433  -1431   1654       C  
ATOM   1473  O   ASN A 186      -7.294  42.568  39.497  1.00 77.28           O  
ANISOU 1473  O   ASN A 186     5917   9774  13669  -1412  -1509   1541       O  
ATOM   1474  CB  ASN A 186      -6.230  45.139  38.308  1.00 78.52           C  
ANISOU 1474  CB  ASN A 186     5919   9964  13951  -1763  -1606   1802       C  
ATOM   1475  CG  ASN A 186      -5.298  46.002  37.482  1.00 80.45           C  
ANISOU 1475  CG  ASN A 186     5977  10309  14280  -1916  -1614   1980       C  
ATOM   1476  OD1 ASN A 186      -5.696  46.566  36.463  1.00 79.55           O  
ANISOU 1476  OD1 ASN A 186     5878  10208  14138  -1946  -1521   2011       O  
ATOM   1477  ND2 ASN A 186      -4.059  46.132  37.930  1.00 82.85           N  
ANISOU 1477  ND2 ASN A 186     6106  10684  14687  -2022  -1733   2104       N  
ATOM   1478  N   VAL A 187      -5.560  41.771  38.245  1.00 80.02           N  
ANISOU 1478  N   VAL A 187     5847  10423  14131  -1353  -1372   1720       N  
ATOM   1479  CA  VAL A 187      -5.170  40.610  39.104  1.00 80.71           C  
ANISOU 1479  CA  VAL A 187     5899  10532  14235  -1244  -1419   1676       C  
ATOM   1480  C   VAL A 187      -3.810  40.911  39.751  1.00 83.37           C  
ANISOU 1480  C   VAL A 187     6061  10928  14688  -1361  -1574   1804       C  
ATOM   1481  O   VAL A 187      -2.837  41.108  38.997  1.00 83.71           O  
ANISOU 1481  O   VAL A 187     5868  11126  14808  -1402  -1526   1938       O  
ATOM   1482  CB  VAL A 187      -5.118  39.302  38.291  1.00 80.77           C  
ANISOU 1482  CB  VAL A 187     5799  10670  14219  -1040  -1244   1645       C  
ATOM   1483  CG1 VAL A 187      -5.055  38.079  39.195  1.00 80.39           C  
ANISOU 1483  CG1 VAL A 187     5782  10596  14163   -914  -1295   1571       C  
ATOM   1484  CG2 VAL A 187      -6.279  39.199  37.311  1.00 79.49           C  
ANISOU 1484  CG2 VAL A 187     5761  10481  13959   -953  -1083   1560       C  
ATOM   1485  N   VAL A 188      -3.748  40.919  41.089  1.00 84.48           N  
ANISOU 1485  N   VAL A 188     6308  10955  14835  -1412  -1751   1766       N  
ATOM   1486  CA  VAL A 188      -2.542  41.281  41.898  1.00 86.86           C  
ANISOU 1486  CA  VAL A 188     6482  11278  15244  -1543  -1940   1878       C  
ATOM   1487  C   VAL A 188      -2.039  40.039  42.653  1.00 88.53           C  
ANISOU 1487  C   VAL A 188     6629  11531  15478  -1420  -1985   1851       C  
ATOM   1488  O   VAL A 188      -2.640  39.703  43.696  1.00 87.50           O  
ANISOU 1488  O   VAL A 188     6696  11267  15281  -1389  -2073   1745       O  
ATOM   1489  CB  VAL A 188      -2.852  42.436  42.874  1.00 86.39           C  
ANISOU 1489  CB  VAL A 188     6621  11034  15167  -1717  -2140   1860       C  
ATOM   1490  CG1 VAL A 188      -1.683  42.736  43.806  1.00 88.11           C  
ANISOU 1490  CG1 VAL A 188     6737  11254  15487  -1850  -2356   1963       C  
ATOM   1491  CG2 VAL A 188      -3.289  43.699  42.145  1.00 85.85           C  
ANISOU 1491  CG2 VAL A 188     6619  10914  15086  -1842  -2117   1893       C  
ATOM   1492  N   CYS A 189      -0.988  39.382  42.140  1.00 91.43           N  
ANISOU 1492  N   CYS A 189     6729  12078  15931  -1348  -1924   1946       N  
ATOM   1493  CA  CYS A 189      -0.102  38.455  42.902  1.00 93.20           C  
ANISOU 1493  CA  CYS A 189     6830  12357  16222  -1276  -2018   1972       C  
ATOM   1494  C   CYS A 189       1.098  39.268  43.399  1.00 95.18           C  
ANISOU 1494  C   CYS A 189     6918  12647  16597  -1463  -2203   2125       C  
ATOM   1495  O   CYS A 189       1.667  40.028  42.590  1.00 96.68           O  
ANISOU 1495  O   CYS A 189     6934  12945  16855  -1568  -2162   2252       O  
ATOM   1496  CB  CYS A 189       0.367  37.266  42.063  1.00 94.72           C  
ANISOU 1496  CB  CYS A 189     6824  12725  16439  -1073  -1852   1984       C  
ATOM   1497  SG  CYS A 189       1.380  36.070  42.981  1.00 97.33           S  
ANISOU 1497  SG  CYS A 189     7018  13111  16850   -962  -1971   2005       S  
ATOM   1498  N   LYS A 190       1.454  39.130  44.680  1.00 95.20           N  
ANISOU 1498  N   LYS A 190     6979  12564  16627  -1512  -2404   2118       N  
ATOM   1499  CA  LYS A 190       2.606  39.839  45.302  1.00 96.60           C  
ANISOU 1499  CA  LYS A 190     7015  12760  16925  -1695  -2614   2261       C  
ATOM   1500  C   LYS A 190       3.909  39.377  44.635  1.00 98.48           C  
ANISOU 1500  C   LYS A 190     6890  13232  17296  -1647  -2554   2409       C  
ATOM   1501  O   LYS A 190       4.943  40.045  44.848  1.00100.32           O  
ANISOU 1501  O   LYS A 190     6945  13523  17647  -1810  -2697   2561       O  
ATOM   1502  CB  LYS A 190       2.624  39.619  46.818  1.00 96.54           C  
ANISOU 1502  CB  LYS A 190     7170  12609  16899  -1727  -2834   2204       C  
ATOM   1503  CG  LYS A 190       1.750  40.584  47.607  1.00 95.66           C  
ANISOU 1503  CG  LYS A 190     7368  12283  16693  -1859  -2965   2119       C  
ATOM   1504  CD  LYS A 190       1.290  40.034  48.938  1.00 95.08           C  
ANISOU 1504  CD  LYS A 190     7521  12069  16533  -1808  -3091   2004       C  
ATOM   1505  CE  LYS A 190       0.701  41.095  49.842  1.00 94.88           C  
ANISOU 1505  CE  LYS A 190     7771  11847  16428  -1954  -3259   1943       C  
ATOM   1506  NZ  LYS A 190       0.676  40.649  51.255  1.00 95.06           N  
ANISOU 1506  NZ  LYS A 190     7959  11764  16395  -1941  -3431   1879       N  
ATOM   1507  N   THR A 191       3.861  38.289  43.856  1.00 97.56           N  
ANISOU 1507  N   THR A 191     6666  13243  17158  -1430  -2355   2368       N  
ATOM   1508  CA  THR A 191       4.997  37.768  43.048  1.00 98.97           C  
ANISOU 1508  CA  THR A 191     6497  13665  17441  -1338  -2249   2492       C  
ATOM   1509  C   THR A 191       5.094  38.546  41.727  1.00 98.78           C  
ANISOU 1509  C   THR A 191     6332  13772  17427  -1406  -2089   2590       C  
ATOM   1510  O   THR A 191       6.032  39.363  41.594  1.00100.15           O  
ANISOU 1510  O   THR A 191     6297  14043  17709  -1576  -2166   2762       O  
ATOM   1511  CB  THR A 191       4.855  36.260  42.797  1.00 98.40           C  
ANISOU 1511  CB  THR A 191     6402  13656  17327  -1061  -2113   2392       C  
ATOM   1512  OG1 THR A 191       4.731  35.600  44.057  1.00 97.72           O  
ANISOU 1512  OG1 THR A 191     6463  13437  17227  -1019  -2275   2311       O  
ATOM   1513  CG2 THR A 191       6.017  35.668  42.027  1.00100.24           C  
ANISOU 1513  CG2 THR A 191     6288  14139  17658   -937  -2006   2504       C  
ATOM   1514  N   CYS A 192       4.157  38.311  40.800  1.00 95.86           N  
ANISOU 1514  N   CYS A 192     6074  13401  16947  -1287  -1883   2492       N  
ATOM   1515  CA  CYS A 192       4.264  38.698  39.364  1.00 95.74           C  
ANISOU 1515  CA  CYS A 192     5905  13546  16923  -1282  -1683   2573       C  
ATOM   1516  C   CYS A 192       3.419  39.944  39.057  1.00 92.62           C  
ANISOU 1516  C   CYS A 192     5698  13025  16467  -1458  -1688   2566       C  
ATOM   1517  O   CYS A 192       2.892  40.032  37.930  1.00 91.39           O  
ANISOU 1517  O   CYS A 192     5558  12926  16240  -1400  -1499   2547       O  
ATOM   1518  CB  CYS A 192       3.864  37.530  38.470  1.00 95.57           C  
ANISOU 1518  CB  CYS A 192     5873  13617  16819  -1016  -1455   2471       C  
ATOM   1519  SG  CYS A 192       2.298  36.756  38.953  1.00 94.88           S  
ANISOU 1519  SG  CYS A 192     6162  13302  16586   -874  -1438   2233       S  
ATOM   1520  N   GLY A 193       3.320  40.878  40.010  1.00 90.79           N  
ANISOU 1520  N   GLY A 193     5605  12627  16261  -1660  -1902   2583       N  
ATOM   1521  CA  GLY A 193       2.684  42.198  39.832  1.00 89.00           C  
ANISOU 1521  CA  GLY A 193     5545  12271  15998  -1848  -1950   2596       C  
ATOM   1522  C   GLY A 193       1.220  42.090  39.434  1.00 85.50           C  
ANISOU 1522  C   GLY A 193     5370  11704  15411  -1746  -1820   2429       C  
ATOM   1523  O   GLY A 193       0.506  41.263  40.040  1.00 83.95           O  
ANISOU 1523  O   GLY A 193     5348  11406  15140  -1606  -1817   2275       O  
ATOM   1524  N   GLN A 194       0.805  42.876  38.431  1.00 83.57           N  
ANISOU 1524  N   GLN A 194     5147  11474  15131  -1815  -1716   2467       N  
ATOM   1525  CA  GLN A 194      -0.615  43.172  38.092  1.00 80.14           C  
ANISOU 1525  CA  GLN A 194     4983  10892  14573  -1780  -1637   2331       C  
ATOM   1526  C   GLN A 194      -0.953  42.660  36.684  1.00 78.65           C  
ANISOU 1526  C   GLN A 194     4721  10840  14320  -1632  -1384   2316       C  
ATOM   1527  O   GLN A 194      -0.093  42.801  35.795  1.00 79.40           O  
ANISOU 1527  O   GLN A 194     4572  11125  14469  -1659  -1293   2460       O  
ATOM   1528  CB  GLN A 194      -0.848  44.681  38.183  1.00 80.46           C  
ANISOU 1528  CB  GLN A 194     5142  10801  14625  -2007  -1768   2388       C  
ATOM   1529  CG  GLN A 194      -0.561  45.253  39.565  1.00 81.06           C  
ANISOU 1529  CG  GLN A 194     5321  10724  14751  -2155  -2030   2393       C  
ATOM   1530  CD  GLN A 194      -0.946  46.707  39.689  1.00 81.28           C  
ANISOU 1530  CD  GLN A 194     5518  10588  14775  -2355  -2168   2420       C  
ATOM   1531  OE1 GLN A 194      -1.367  47.165  40.750  1.00 80.77           O  
ANISOU 1531  OE1 GLN A 194     5672  10334  14683  -2419  -2343   2338       O  
ATOM   1532  NE2 GLN A 194      -0.802  47.447  38.601  1.00 81.88           N  
ANISOU 1532  NE2 GLN A 194     5500  10735  14873  -2452  -2092   2534       N  
ATOM   1533  N   GLN A 195      -2.161  42.096  36.500  1.00 75.66           N  
ANISOU 1533  N   GLN A 195     4548  10371  13827  -1484  -1280   2153       N  
ATOM   1534  CA  GLN A 195      -2.736  41.708  35.177  1.00 73.91           C  
ANISOU 1534  CA  GLN A 195     4324  10234  13522  -1350  -1057   2115       C  
ATOM   1535  C   GLN A 195      -4.058  42.450  34.935  1.00 71.73           C  
ANISOU 1535  C   GLN A 195     4302   9792  13157  -1401  -1045   2027       C  
ATOM   1536  O   GLN A 195      -5.075  42.073  35.555  1.00 70.22           O  
ANISOU 1536  O   GLN A 195     4329   9453  12897  -1326  -1073   1878       O  
ATOM   1537  CB  GLN A 195      -2.989  40.202  35.065  1.00 72.70           C  
ANISOU 1537  CB  GLN A 195     4175  10130  13315  -1105   -939   1999       C  
ATOM   1538  CG  GLN A 195      -3.596  39.807  33.723  1.00 71.94           C  
ANISOU 1538  CG  GLN A 195     4098  10107  13127   -969   -727   1954       C  
ATOM   1539  CD  GLN A 195      -3.908  38.336  33.610  1.00 71.19           C  
ANISOU 1539  CD  GLN A 195     4035  10036  12975   -731   -629   1833       C  
ATOM   1540  OE1 GLN A 195      -5.041  37.907  33.826  1.00 69.57           O  
ANISOU 1540  OE1 GLN A 195     4047   9693  12690   -655   -621   1694       O  
ATOM   1541  NE2 GLN A 195      -2.903  37.552  33.256  1.00 72.10           N  
ANISOU 1541  NE2 GLN A 195     3933  10330  13132   -610   -558   1888       N  
ATOM   1542  N   GLN A 196      -4.043  43.426  34.023  1.00 71.75           N  
ANISOU 1542  N   GLN A 196     4269   9831  13160  -1517   -998   2123       N  
ATOM   1543  CA  GLN A 196      -5.234  44.195  33.567  1.00 69.99           C  
ANISOU 1543  CA  GLN A 196     4261   9473  12858  -1561   -973   2059       C  
ATOM   1544  C   GLN A 196      -5.745  43.594  32.254  1.00 69.36           C  
ANISOU 1544  C   GLN A 196     4167   9492  12691  -1408   -755   2021       C  
ATOM   1545  O   GLN A 196      -4.936  43.449  31.322  1.00 70.49           O  
ANISOU 1545  O   GLN A 196     4101   9827  12854  -1390   -638   2134       O  
ATOM   1546  CB  GLN A 196      -4.897  45.680  33.403  1.00 70.82           C  
ANISOU 1546  CB  GLN A 196     4352   9538  13017  -1793  -1080   2193       C  
ATOM   1547  CG  GLN A 196      -5.601  46.357  32.232  1.00 70.16           C  
ANISOU 1547  CG  GLN A 196     4345   9441  12869  -1823   -976   2210       C  
ATOM   1548  CD  GLN A 196      -6.054  47.767  32.523  1.00 70.13           C  
ANISOU 1548  CD  GLN A 196     4512   9256  12878  -2010  -1130   2231       C  
ATOM   1549  OE1 GLN A 196      -6.706  48.405  31.699  1.00 69.52           O  
ANISOU 1549  OE1 GLN A 196     4526   9135  12750  -2043  -1076   2237       O  
ATOM   1550  NE2 GLN A 196      -5.736  48.259  33.710  1.00 70.50           N  
ANISOU 1550  NE2 GLN A 196     4613   9185  12985  -2125  -1333   2236       N  
ATOM   1551  N   THR A 197      -7.041  43.277  32.186  1.00 67.67           N  
ANISOU 1551  N   THR A 197     4169   9158  12385  -1305   -704   1871       N  
ATOM   1552  CA  THR A 197      -7.730  42.824  30.947  1.00 67.23           C  
ANISOU 1552  CA  THR A 197     4149   9157  12236  -1175   -520   1821       C  
ATOM   1553  C   THR A 197      -8.907  43.766  30.647  1.00 66.17           C  
ANISOU 1553  C   THR A 197     4224   8872  12045  -1249   -538   1773       C  
ATOM   1554  O   THR A 197      -9.656  44.095  31.586  1.00 64.60           O  
ANISOU 1554  O   THR A 197     4207   8499  11838  -1286   -656   1683       O  
ATOM   1555  CB  THR A 197      -8.150  41.352  31.055  1.00 66.14           C  
ANISOU 1555  CB  THR A 197     4054   9031  12042   -958   -438   1689       C  
ATOM   1556  OG1 THR A 197      -9.418  41.293  31.710  1.00 64.85           O  
ANISOU 1556  OG1 THR A 197     4131   8683  11826   -933   -496   1549       O  
ATOM   1557  CG2 THR A 197      -7.140  40.500  31.796  1.00 66.62           C  
ANISOU 1557  CG2 THR A 197     3965   9174  12170   -895   -483   1709       C  
ATOM   1558  N   THR A 198      -9.033  44.194  29.384  1.00 67.06           N  
ANISOU 1558  N   THR A 198     4308   9055  12116  -1267   -427   1836       N  
ATOM   1559  CA  THR A 198     -10.114  45.071  28.856  1.00 66.35           C  
ANISOU 1559  CA  THR A 198     4398   8842  11970  -1326   -427   1805       C  
ATOM   1560  C   THR A 198     -10.937  44.268  27.847  1.00 65.23           C  
ANISOU 1560  C   THR A 198     4320   8738  11726  -1156   -262   1718       C  
ATOM   1561  O   THR A 198     -10.470  44.092  26.701  1.00 65.35           O  
ANISOU 1561  O   THR A 198     4211   8908  11708  -1119   -129   1796       O  
ATOM   1562  CB  THR A 198      -9.548  46.372  28.267  1.00 68.22           C  
ANISOU 1562  CB  THR A 198     4560   9111  12248  -1517   -465   1968       C  
ATOM   1563  OG1 THR A 198      -9.452  47.303  29.344  1.00 68.95           O  
ANISOU 1563  OG1 THR A 198     4730   9058  12410  -1674   -661   1985       O  
ATOM   1564  CG2 THR A 198     -10.390  46.973  27.160  1.00 67.72           C  
ANISOU 1564  CG2 THR A 198     4608   9009  12110  -1533   -391   1970       C  
ATOM   1565  N   LEU A 199     -12.111  43.803  28.287  1.00 64.00           N  
ANISOU 1565  N   LEU A 199     4350   8447  11519  -1061   -276   1566       N  
ATOM   1566  CA  LEU A 199     -13.113  43.057  27.482  1.00 62.67           C  
ANISOU 1566  CA  LEU A 199     4283   8272  11256   -909   -154   1465       C  
ATOM   1567  C   LEU A 199     -14.176  44.048  27.005  1.00 61.67           C  
ANISOU 1567  C   LEU A 199     4318   8024  11089   -980   -173   1448       C  
ATOM   1568  O   LEU A 199     -14.419  45.035  27.728  1.00 61.12           O  
ANISOU 1568  O   LEU A 199     4334   7827  11059  -1103   -303   1452       O  
ATOM   1569  CB  LEU A 199     -13.726  41.954  28.351  1.00 61.55           C  
ANISOU 1569  CB  LEU A 199     4236   8055  11095   -780   -176   1326       C  
ATOM   1570  CG  LEU A 199     -12.723  41.077  29.104  1.00 62.62           C  
ANISOU 1570  CG  LEU A 199     4238   8271  11283   -725   -202   1337       C  
ATOM   1571  CD1 LEU A 199     -13.415  40.226  30.162  1.00 61.20           C  
ANISOU 1571  CD1 LEU A 199     4180   7983  11088   -639   -261   1210       C  
ATOM   1572  CD2 LEU A 199     -11.931  40.203  28.138  1.00 63.76           C  
ANISOU 1572  CD2 LEU A 199     4221   8596  11407   -602    -64   1380       C  
ATOM   1573  N   LYS A 200     -14.748  43.801  25.822  1.00 61.53           N  
ANISOU 1573  N   LYS A 200     4341   8044  10993   -901    -55   1429       N  
ATOM   1574  CA  LYS A 200     -15.889  44.558  25.237  1.00 61.01           C  
ANISOU 1574  CA  LYS A 200     4435   7866  10878   -936    -61   1399       C  
ATOM   1575  C   LYS A 200     -16.922  43.549  24.724  1.00 60.05           C  
ANISOU 1575  C   LYS A 200     4415   7725  10674   -773     26   1281       C  
ATOM   1576  O   LYS A 200     -16.551  42.372  24.546  1.00 60.20           O  
ANISOU 1576  O   LYS A 200     4363   7841  10667   -645    107   1250       O  
ATOM   1577  CB  LYS A 200     -15.401  45.471  24.108  1.00 62.48           C  
ANISOU 1577  CB  LYS A 200     4554   8133  11054  -1041    -16   1537       C  
ATOM   1578  CG  LYS A 200     -15.277  44.802  22.744  1.00 62.96           C  
ANISOU 1578  CG  LYS A 200     4554   8338  11029   -933    147   1561       C  
ATOM   1579  CD  LYS A 200     -14.206  45.390  21.849  1.00 64.65           C  
ANISOU 1579  CD  LYS A 200     4609   8710  11243  -1027    211   1729       C  
ATOM   1580  CE  LYS A 200     -13.719  44.396  20.814  1.00 65.27           C  
ANISOU 1580  CE  LYS A 200     4580   8976  11242   -882    382   1743       C  
ATOM   1581  NZ  LYS A 200     -12.657  44.969  19.956  1.00 67.32           N  
ANISOU 1581  NZ  LYS A 200     4670   9412  11494   -973    458   1918       N  
ATOM   1582  N   GLY A 201     -18.160  43.991  24.488  1.00 59.35           N  
ANISOU 1582  N   GLY A 201     4488   7514  10548   -775      4   1219       N  
ATOM   1583  CA  GLY A 201     -19.241  43.138  23.957  1.00 58.05           C  
ANISOU 1583  CA  GLY A 201     4428   7317  10308   -640     70   1116       C  
ATOM   1584  C   GLY A 201     -19.750  42.166  25.008  1.00 57.27           C  
ANISOU 1584  C   GLY A 201     4384   7156  10220   -549     33   1002       C  
ATOM   1585  O   GLY A 201     -19.847  42.566  26.186  1.00 57.60           O  
ANISOU 1585  O   GLY A 201     4459   7112  10311   -610    -66    977       O  
ATOM   1586  N   VAL A 202     -20.057  40.930  24.602  1.00 56.56           N  
ANISOU 1586  N   VAL A 202     4309   7102  10077   -411    105    936       N  
ATOM   1587  CA  VAL A 202     -20.737  39.901  25.448  1.00 55.05           C  
ANISOU 1587  CA  VAL A 202     4189   6842   9882   -322     72    829       C  
ATOM   1588  C   VAL A 202     -19.901  39.622  26.706  1.00 54.71           C  
ANISOU 1588  C   VAL A 202     4069   6816   9902   -343      9    836       C  
ATOM   1589  O   VAL A 202     -20.498  39.487  27.791  1.00 53.54           O  
ANISOU 1589  O   VAL A 202     3996   6575   9769   -349    -63    773       O  
ATOM   1590  CB  VAL A 202     -21.000  38.609  24.650  1.00 55.00           C  
ANISOU 1590  CB  VAL A 202     4205   6881   9811   -176    153    776       C  
ATOM   1591  CG1 VAL A 202     -21.597  37.517  25.528  1.00 53.79           C  
ANISOU 1591  CG1 VAL A 202     4117   6660   9660    -99    109    684       C  
ATOM   1592  CG2 VAL A 202     -21.871  38.882  23.429  1.00 54.97           C  
ANISOU 1592  CG2 VAL A 202     4291   6853   9741   -159    201    767       C  
ATOM   1593  N   GLU A 203     -18.573  39.563  26.566  1.00 55.39           N  
ANISOU 1593  N   GLU A 203     4004   7019  10019   -355     37    916       N  
ATOM   1594  CA  GLU A 203     -17.636  39.087  27.622  1.00 55.35           C  
ANISOU 1594  CA  GLU A 203     3903   7051  10073   -353    -16    928       C  
ATOM   1595  C   GLU A 203     -17.527  40.135  28.738  1.00 54.50           C  
ANISOU 1595  C   GLU A 203     3817   6864  10027   -493   -137    954       C  
ATOM   1596  O   GLU A 203     -16.931  39.812  29.783  1.00 54.16           O  
ANISOU 1596  O   GLU A 203     3725   6822  10028   -502   -205    953       O  
ATOM   1597  CB  GLU A 203     -16.256  38.781  27.033  1.00 57.22           C  
ANISOU 1597  CB  GLU A 203     3959   7452  10329   -321     53   1015       C  
ATOM   1598  CG  GLU A 203     -16.284  38.038  25.701  1.00 58.11           C  
ANISOU 1598  CG  GLU A 203     4056   7656  10366   -190    183   1003       C  
ATOM   1599  CD  GLU A 203     -15.895  38.862  24.476  1.00 59.79           C  
ANISOU 1599  CD  GLU A 203     4201   7965  10548   -245    266   1100       C  
ATOM   1600  OE1 GLU A 203     -16.781  39.096  23.623  1.00 59.17           O  
ANISOU 1600  OE1 GLU A 203     4233   7844  10404   -234    307   1074       O  
ATOM   1601  OE2 GLU A 203     -14.695  39.250  24.358  1.00 61.60           O  
ANISOU 1601  OE2 GLU A 203     4264   8321  10820   -301    288   1210       O  
ATOM   1602  N   ALA A 204     -18.085  41.335  28.527  1.00 53.90           N  
ANISOU 1602  N   ALA A 204     3818   6712   9948   -592   -170    972       N  
ATOM   1603  CA  ALA A 204     -17.972  42.508  29.427  1.00 53.67           C  
ANISOU 1603  CA  ALA A 204     3825   6596   9969   -729   -292   1000       C  
ATOM   1604  C   ALA A 204     -18.985  42.414  30.569  1.00 52.25           C  
ANISOU 1604  C   ALA A 204     3790   6287   9773   -706   -367    893       C  
ATOM   1605  O   ALA A 204     -18.657  42.899  31.669  1.00 51.86           O  
ANISOU 1605  O   ALA A 204     3758   6184   9761   -780   -474    895       O  
ATOM   1606  CB  ALA A 204     -18.167  43.781  28.641  1.00 53.98           C  
ANISOU 1606  CB  ALA A 204     3897   6604  10006   -830   -299   1063       C  
ATOM   1607  N   VAL A 205     -20.160  41.822  30.305  1.00 51.45           N  
ANISOU 1607  N   VAL A 205     3788   6144   9616   -611   -314    807       N  
ATOM   1608  CA  VAL A 205     -21.333  41.783  31.237  1.00 50.77           C  
ANISOU 1608  CA  VAL A 205     3841   5947   9502   -585   -365    710       C  
ATOM   1609  C   VAL A 205     -21.338  40.470  32.040  1.00 50.88           C  
ANISOU 1609  C   VAL A 205     3848   5979   9504   -501   -364    657       C  
ATOM   1610  O   VAL A 205     -21.896  40.481  33.158  1.00 51.16           O  
ANISOU 1610  O   VAL A 205     3966   5943   9527   -506   -426    600       O  
ATOM   1611  CB  VAL A 205     -22.675  42.001  30.500  1.00 49.59           C  
ANISOU 1611  CB  VAL A 205     3796   5739   9305   -546   -319    661       C  
ATOM   1612  CG1 VAL A 205     -22.745  43.373  29.848  1.00 49.97           C  
ANISOU 1612  CG1 VAL A 205     3872   5747   9365   -634   -341    711       C  
ATOM   1613  CG2 VAL A 205     -22.987  40.918  29.478  1.00 48.83           C  
ANISOU 1613  CG2 VAL A 205     3680   5703   9169   -444   -219    645       C  
ATOM   1614  N   MET A 206     -20.749  39.389  31.512  1.00 51.34           N  
ANISOU 1614  N   MET A 206     3817   6126   9561   -424   -300    674       N  
ATOM   1615  CA  MET A 206     -20.800  38.031  32.124  1.00 50.93           C  
ANISOU 1615  CA  MET A 206     3769   6084   9496   -334   -302    624       C  
ATOM   1616  C   MET A 206     -19.505  37.755  32.891  1.00 51.20           C  
ANISOU 1616  C   MET A 206     3698   6172   9581   -353   -357    669       C  
ATOM   1617  O   MET A 206     -18.424  37.982  32.318  1.00 51.81           O  
ANISOU 1617  O   MET A 206     3650   6338   9696   -374   -332    743       O  
ATOM   1618  CB  MET A 206     -20.975  36.948  31.056  1.00 51.37           C  
ANISOU 1618  CB  MET A 206     3810   6191   9516   -220   -212    606       C  
ATOM   1619  CG  MET A 206     -22.284  37.049  30.302  1.00 51.26           C  
ANISOU 1619  CG  MET A 206     3901   6122   9452   -194   -169    562       C  
ATOM   1620  SD  MET A 206     -22.457  35.756  29.050  1.00 52.27           S  
ANISOU 1620  SD  MET A 206     4031   6297   9531    -61    -83    537       S  
ATOM   1621  CE  MET A 206     -22.966  34.381  30.083  1.00 51.69           C  
ANISOU 1621  CE  MET A 206     4021   6168   9450      5   -136    472       C  
ATOM   1622  N   TYR A 207     -19.625  37.280  34.135  1.00 50.39           N  
ANISOU 1622  N   TYR A 207     3642   6024   9478   -348   -429    630       N  
ATOM   1623  CA  TYR A 207     -18.526  36.652  34.914  1.00 50.58           C  
ANISOU 1623  CA  TYR A 207     3580   6094   9544   -338   -486    658       C  
ATOM   1624  C   TYR A 207     -19.002  35.299  35.447  1.00 49.29           C  
ANISOU 1624  C   TYR A 207     3475   5905   9348   -244   -492    599       C  
ATOM   1625  O   TYR A 207     -20.218  35.135  35.721  1.00 48.34           O  
ANISOU 1625  O   TYR A 207     3476   5713   9176   -231   -488    540       O  
ATOM   1626  CB  TYR A 207     -18.053  37.556  36.056  1.00 51.64           C  
ANISOU 1626  CB  TYR A 207     3722   6187   9711   -449   -599    683       C  
ATOM   1627  CG  TYR A 207     -16.909  37.006  36.877  1.00 52.81           C  
ANISOU 1627  CG  TYR A 207     3779   6378   9906   -450   -673    720       C  
ATOM   1628  CD1 TYR A 207     -15.599  37.066  36.423  1.00 54.01           C  
ANISOU 1628  CD1 TYR A 207     3766   6630  10124   -465   -669    804       C  
ATOM   1629  CD2 TYR A 207     -17.132  36.429  38.118  1.00 52.82           C  
ANISOU 1629  CD2 TYR A 207     3856   6327   9886   -436   -749    676       C  
ATOM   1630  CE1 TYR A 207     -14.547  36.565  37.174  1.00 55.06           C  
ANISOU 1630  CE1 TYR A 207     3806   6805  10308   -462   -743    841       C  
ATOM   1631  CE2 TYR A 207     -16.092  35.931  38.886  1.00 53.63           C  
ANISOU 1631  CE2 TYR A 207     3881   6462  10031   -438   -829    712       C  
ATOM   1632  CZ  TYR A 207     -14.793  35.996  38.413  1.00 54.99           C  
ANISOU 1632  CZ  TYR A 207     3885   6731  10278   -448   -829    793       C  
ATOM   1633  OH  TYR A 207     -13.773  35.495  39.175  1.00 55.98           O  
ANISOU 1633  OH  TYR A 207     3926   6891  10453   -445   -914    830       O  
ATOM   1634  N   MET A 208     -18.056  34.364  35.574  1.00 48.89           N  
ANISOU 1634  N   MET A 208     3333   5912   9328   -181   -505    622       N  
ATOM   1635  CA  MET A 208     -18.262  32.977  36.063  1.00 47.88           C  
ANISOU 1635  CA  MET A 208     3248   5762   9180    -89   -527    580       C  
ATOM   1636  C   MET A 208     -17.237  32.699  37.169  1.00 48.31           C  
ANISOU 1636  C   MET A 208     3241   5832   9280   -108   -625    612       C  
ATOM   1637  O   MET A 208     -16.044  32.624  36.836  1.00 49.90           O  
ANISOU 1637  O   MET A 208     3302   6119   9536    -86   -621    666       O  
ATOM   1638  CB  MET A 208     -18.085  31.993  34.900  1.00 47.72           C  
ANISOU 1638  CB  MET A 208     3184   5795   9151     36   -446    571       C  
ATOM   1639  CG  MET A 208     -18.207  30.535  35.290  1.00 47.66           C  
ANISOU 1639  CG  MET A 208     3223   5755   9128    135   -481    532       C  
ATOM   1640  SD  MET A 208     -19.689  30.194  36.258  1.00 46.21           S  
ANISOU 1640  SD  MET A 208     3213   5454   8889     96   -534    478       S  
ATOM   1641  CE  MET A 208     -19.664  28.404  36.302  1.00 46.51           C  
ANISOU 1641  CE  MET A 208     3291   5463   8917    221   -568    450       C  
ATOM   1642  N   GLY A 209     -17.669  32.602  38.433  1.00 47.47           N  
ANISOU 1642  N   GLY A 209     3230   5656   9149   -150   -709    586       N  
ATOM   1643  CA  GLY A 209     -16.766  32.367  39.579  1.00 47.89           C  
ANISOU 1643  CA  GLY A 209     3245   5714   9238   -177   -817    615       C  
ATOM   1644  C   GLY A 209     -17.393  32.665  40.931  1.00 47.49           C  
ANISOU 1644  C   GLY A 209     3322   5583   9138   -249   -901    586       C  
ATOM   1645  O   GLY A 209     -17.181  31.852  41.854  1.00 47.75           O  
ANISOU 1645  O   GLY A 209     3382   5597   9163   -227   -975    584       O  
ATOM   1646  N   THR A 210     -18.096  33.796  41.064  1.00 47.27           N  
ANISOU 1646  N   THR A 210     3370   5512   9076   -326   -895    564       N  
ATOM   1647  CA  THR A 210     -18.759  34.262  42.317  1.00 47.42           C  
ANISOU 1647  CA  THR A 210     3521   5461   9034   -387   -963    528       C  
ATOM   1648  C   THR A 210     -20.005  35.082  41.953  1.00 46.98           C  
ANISOU 1648  C   THR A 210     3560   5364   8927   -405   -897    482       C  
ATOM   1649  O   THR A 210     -20.025  35.652  40.844  1.00 46.43           O  
ANISOU 1649  O   THR A 210     3440   5313   8885   -408   -833    495       O  
ATOM   1650  CB  THR A 210     -17.774  35.045  43.199  1.00 48.30           C  
ANISOU 1650  CB  THR A 210     3608   5565   9178   -475  -1080    564       C  
ATOM   1651  OG1 THR A 210     -18.441  35.544  44.359  1.00 48.12           O  
ANISOU 1651  OG1 THR A 210     3728   5475   9081   -522  -1141    520       O  
ATOM   1652  CG2 THR A 210     -17.137  36.211  42.478  1.00 48.95           C  
ANISOU 1652  CG2 THR A 210     3607   5669   9321   -543  -1079    608       C  
ATOM   1653  N   LEU A 211     -20.994  35.134  42.853  1.00 47.21           N  
ANISOU 1653  N   LEU A 211     3714   5344   8878   -413   -913    435       N  
ATOM   1654  CA  LEU A 211     -22.319  35.778  42.615  1.00 47.57           C  
ANISOU 1654  CA  LEU A 211     3850   5355   8869   -412   -849    386       C  
ATOM   1655  C   LEU A 211     -22.356  37.190  43.226  1.00 49.02           C  
ANISOU 1655  C   LEU A 211     4103   5490   9030   -480   -907    364       C  
ATOM   1656  O   LEU A 211     -23.218  37.996  42.789  1.00 48.86           O  
ANISOU 1656  O   LEU A 211     4135   5441   8987   -479   -860    331       O  
ATOM   1657  CB  LEU A 211     -23.432  34.906  43.216  1.00 47.06           C  
ANISOU 1657  CB  LEU A 211     3870   5281   8729   -369   -821    353       C  
ATOM   1658  CG  LEU A 211     -23.489  33.454  42.738  1.00 46.48           C  
ANISOU 1658  CG  LEU A 211     3757   5233   8671   -307   -787    372       C  
ATOM   1659  CD1 LEU A 211     -24.354  32.611  43.656  1.00 46.03           C  
ANISOU 1659  CD1 LEU A 211     3783   5162   8541   -294   -796    361       C  
ATOM   1660  CD2 LEU A 211     -23.989  33.365  41.306  1.00 45.96           C  
ANISOU 1660  CD2 LEU A 211     3653   5177   8629   -264   -696    367       C  
ATOM   1661  N   SER A 212     -21.493  37.485  44.206  1.00 50.31           N  
ANISOU 1661  N   SER A 212     4278   5638   9198   -533  -1015    380       N  
ATOM   1662  CA  SER A 212     -21.510  38.767  44.956  1.00 51.42           C  
ANISOU 1662  CA  SER A 212     4513   5717   9306   -595  -1096    351       C  
ATOM   1663  C   SER A 212     -20.765  39.836  44.152  1.00 53.14           C  
ANISOU 1663  C   SER A 212     4665   5922   9604   -661  -1125    392       C  
ATOM   1664  O   SER A 212     -19.510  39.790  44.111  1.00 54.56           O  
ANISOU 1664  O   SER A 212     4743   6130   9855   -711  -1191    456       O  
ATOM   1665  CB  SER A 212     -20.943  38.616  46.335  1.00 52.01           C  
ANISOU 1665  CB  SER A 212     4641   5773   9345   -628  -1211    350       C  
ATOM   1666  OG  SER A 212     -21.007  39.848  47.037  1.00 52.38           O  
ANISOU 1666  OG  SER A 212     4799   5750   9350   -679  -1295    313       O  
ATOM   1667  N   TYR A 213     -21.521  40.758  43.540  1.00 53.44           N  
ANISOU 1667  N   TYR A 213     4754   5921   9629   -663  -1081    362       N  
ATOM   1668  CA  TYR A 213     -21.016  41.885  42.711  1.00 53.97           C  
ANISOU 1668  CA  TYR A 213     4779   5963   9761   -732  -1106    403       C  
ATOM   1669  C   TYR A 213     -20.171  42.820  43.583  1.00 55.72           C  
ANISOU 1669  C   TYR A 213     5045   6124   9999   -827  -1258    419       C  
ATOM   1670  O   TYR A 213     -19.264  43.467  43.039  1.00 56.82           O  
ANISOU 1670  O   TYR A 213     5106   6266  10216   -910  -1308    489       O  
ATOM   1671  CB  TYR A 213     -22.192  42.610  42.048  1.00 53.06           C  
ANISOU 1671  CB  TYR A 213     4739   5804   9614   -702  -1038    356       C  
ATOM   1672  CG  TYR A 213     -21.841  43.670  41.032  1.00 52.93           C  
ANISOU 1672  CG  TYR A 213     4687   5764   9660   -767  -1049    402       C  
ATOM   1673  CD1 TYR A 213     -20.709  43.580  40.237  1.00 53.30           C  
ANISOU 1673  CD1 TYR A 213     4591   5872   9788   -822  -1048    495       C  
ATOM   1674  CD2 TYR A 213     -22.682  44.753  40.835  1.00 52.59           C  
ANISOU 1674  CD2 TYR A 213     4750   5641   9589   -768  -1056    358       C  
ATOM   1675  CE1 TYR A 213     -20.408  44.554  39.297  1.00 53.63           C  
ANISOU 1675  CE1 TYR A 213     4599   5897   9879   -891  -1055    550       C  
ATOM   1676  CE2 TYR A 213     -22.399  45.733  39.897  1.00 52.85           C  
ANISOU 1676  CE2 TYR A 213     4762   5643   9676   -833  -1074    407       C  
ATOM   1677  CZ  TYR A 213     -21.257  45.634  39.125  1.00 53.33           C  
ANISOU 1677  CZ  TYR A 213     4681   5768   9814   -902  -1073    508       C  
ATOM   1678  OH  TYR A 213     -20.979  46.599  38.201  1.00 53.53           O  
ANISOU 1678  OH  TYR A 213     4682   5769   9886   -976  -1089    569       O  
ATOM   1679  N   GLU A 214     -20.472  42.892  44.885  1.00 56.78           N  
ANISOU 1679  N   GLU A 214     5306   6210  10058   -819  -1331    360       N  
ATOM   1680  CA  GLU A 214     -19.660  43.612  45.903  1.00 59.05           C  
ANISOU 1680  CA  GLU A 214     5657   6434  10346   -903  -1494    368       C  
ATOM   1681  C   GLU A 214     -18.275  42.964  45.989  1.00 60.85           C  
ANISOU 1681  C   GLU A 214     5741   6724  10655   -956  -1557    456       C  
ATOM   1682  O   GLU A 214     -17.269  43.689  45.826  1.00 62.32           O  
ANISOU 1682  O   GLU A 214     5866   6892  10918  -1057  -1656    523       O  
ATOM   1683  CB  GLU A 214     -20.340  43.581  47.272  1.00 59.32           C  
ANISOU 1683  CB  GLU A 214     5857   6421  10261   -859  -1538    282       C  
ATOM   1684  CG  GLU A 214     -21.403  44.648  47.442  1.00 59.91           C  
ANISOU 1684  CG  GLU A 214     6090   6413  10260   -827  -1535    196       C  
ATOM   1685  CD  GLU A 214     -20.897  45.969  47.999  1.00 61.67           C  
ANISOU 1685  CD  GLU A 214     6425   6524  10480   -906  -1697    180       C  
ATOM   1686  OE1 GLU A 214     -20.723  46.923  47.206  1.00 61.96           O  
ANISOU 1686  OE1 GLU A 214     6450   6509  10583   -961  -1728    207       O  
ATOM   1687  OE2 GLU A 214     -20.691  46.045  49.232  1.00 62.80           O  
ANISOU 1687  OE2 GLU A 214     6678   6627  10553   -914  -1802    142       O  
ATOM   1688  N   GLN A 215     -18.229  41.651  46.243  1.00 61.28           N  
ANISOU 1688  N   GLN A 215     5740   6846  10695   -891  -1507    460       N  
ATOM   1689  CA  GLN A 215     -16.966  40.871  46.326  1.00 62.17           C  
ANISOU 1689  CA  GLN A 215     5710   7026  10885   -915  -1558    539       C  
ATOM   1690  C   GLN A 215     -16.131  41.186  45.087  1.00 62.67           C  
ANISOU 1690  C   GLN A 215     5604   7146  11059   -960  -1527    626       C  
ATOM   1691  O   GLN A 215     -14.970  41.590  45.254  1.00 64.54           O  
ANISOU 1691  O   GLN A 215     5758   7394  11371  -1049  -1635    699       O  
ATOM   1692  CB  GLN A 215     -17.219  39.364  46.419  1.00 61.80           C  
ANISOU 1692  CB  GLN A 215     5626   7042  10813   -818  -1481    529       C  
ATOM   1693  CG  GLN A 215     -17.279  38.839  47.846  1.00 62.16           C  
ANISOU 1693  CG  GLN A 215     5774   7060  10783   -809  -1566    497       C  
ATOM   1694  CD  GLN A 215     -17.526  37.351  47.890  1.00 62.06           C  
ANISOU 1694  CD  GLN A 215     5728   7099  10750   -722  -1500    498       C  
ATOM   1695  OE1 GLN A 215     -17.240  36.623  46.940  1.00 62.16           O  
ANISOU 1695  OE1 GLN A 215     5617   7173  10829   -674  -1425    534       O  
ATOM   1696  NE2 GLN A 215     -18.075  36.887  49.001  1.00 62.17           N  
ANISOU 1696  NE2 GLN A 215     5864   7088  10668   -701  -1532    458       N  
ATOM   1697  N   PHE A 216     -16.729  41.050  43.902  1.00 61.66           N  
ANISOU 1697  N   PHE A 216     5434   7056  10937   -906  -1388    621       N  
ATOM   1698  CA  PHE A 216     -16.061  41.266  42.593  1.00 62.06           C  
ANISOU 1698  CA  PHE A 216     5328   7178  11074   -933  -1329    702       C  
ATOM   1699  C   PHE A 216     -15.313  42.609  42.587  1.00 62.97           C  
ANISOU 1699  C   PHE A 216     5425   7251  11247  -1069  -1442    766       C  
ATOM   1700  O   PHE A 216     -14.353  42.739  41.813  1.00 63.42           O  
ANISOU 1700  O   PHE A 216     5321   7385  11389  -1120  -1431    864       O  
ATOM   1701  CB  PHE A 216     -17.083  41.183  41.461  1.00 61.31           C  
ANISOU 1701  CB  PHE A 216     5251   7095  10948   -864  -1182    668       C  
ATOM   1702  CG  PHE A 216     -16.476  40.910  40.111  1.00 62.01           C  
ANISOU 1702  CG  PHE A 216     5176   7283  11099   -848  -1088    742       C  
ATOM   1703  CD1 PHE A 216     -16.606  41.817  39.069  1.00 62.52           C  
ANISOU 1703  CD1 PHE A 216     5223   7348  11184   -895  -1043    777       C  
ATOM   1704  CD2 PHE A 216     -15.763  39.744  39.891  1.00 62.58           C  
ANISOU 1704  CD2 PHE A 216     5118   7451  11205   -780  -1047    776       C  
ATOM   1705  CE1 PHE A 216     -16.038  41.559  37.830  1.00 63.06           C  
ANISOU 1705  CE1 PHE A 216     5143   7519  11296   -877   -949    848       C  
ATOM   1706  CE2 PHE A 216     -15.196  39.488  38.654  1.00 63.32           C  
ANISOU 1706  CE2 PHE A 216     5066   7647  11345   -750   -952    839       C  
ATOM   1707  CZ  PHE A 216     -15.336  40.394  37.626  1.00 63.66           C  
ANISOU 1707  CZ  PHE A 216     5090   7698  11397   -800   -899    876       C  
ATOM   1708  N   LYS A 217     -15.738  43.570  43.414  1.00 63.46           N  
ANISOU 1708  N   LYS A 217     5649   7199  11263  -1125  -1547    715       N  
ATOM   1709  CA  LYS A 217     -15.106  44.910  43.555  1.00 65.76           C  
ANISOU 1709  CA  LYS A 217     5963   7419  11603  -1263  -1687    767       C  
ATOM   1710  C   LYS A 217     -14.092  44.900  44.706  1.00 67.88           C  
ANISOU 1710  C   LYS A 217     6222   7669  11900  -1337  -1854    802       C  
ATOM   1711  O   LYS A 217     -13.033  45.560  44.567  1.00 68.94           O  
ANISOU 1711  O   LYS A 217     6264   7808  12122  -1461  -1960    900       O  
ATOM   1712  CB  LYS A 217     -16.175  45.977  43.809  1.00 65.47           C  
ANISOU 1712  CB  LYS A 217     6129   7253  11494  -1267  -1721    680       C  
ATOM   1713  CG  LYS A 217     -17.157  46.202  42.668  1.00 64.22           C  
ANISOU 1713  CG  LYS A 217     5986   7097  11316  -1211  -1583    654       C  
ATOM   1714  CD  LYS A 217     -18.411  46.928  43.098  1.00 63.91           C  
ANISOU 1714  CD  LYS A 217     6151   6943  11188  -1165  -1596    544       C  
ATOM   1715  CE  LYS A 217     -19.251  47.413  41.936  1.00 63.26           C  
ANISOU 1715  CE  LYS A 217     6082   6846  11104  -1135  -1496    534       C  
ATOM   1716  NZ  LYS A 217     -20.493  48.070  42.403  1.00 62.98           N  
ANISOU 1716  NZ  LYS A 217     6236   6707  10984  -1072  -1506    423       N  
ATOM   1717  N   LYS A 218     -14.418  44.192  45.793  1.00 68.75           N  
ANISOU 1717  N   LYS A 218     6424   7759  11936  -1272  -1881    730       N  
ATOM   1718  CA  LYS A 218     -13.623  44.124  47.053  1.00 71.11           C  
ANISOU 1718  CA  LYS A 218     6754   8026  12237  -1329  -2048    745       C  
ATOM   1719  C   LYS A 218     -12.489  43.087  46.953  1.00 72.47           C  
ANISOU 1719  C   LYS A 218     6724   8315  12495  -1323  -2050    834       C  
ATOM   1720  O   LYS A 218     -11.597  43.135  47.820  1.00 73.81           O  
ANISOU 1720  O   LYS A 218     6878   8468  12697  -1393  -2204    875       O  
ATOM   1721  CB  LYS A 218     -14.544  43.804  48.237  1.00 70.64           C  
ANISOU 1721  CB  LYS A 218     6891   7903  12045  -1254  -2065    631       C  
ATOM   1722  CG  LYS A 218     -15.412  44.961  48.722  1.00 70.75           C  
ANISOU 1722  CG  LYS A 218     7119   7790  11970  -1267  -2121    541       C  
ATOM   1723  CD  LYS A 218     -14.636  46.169  49.225  1.00 72.52           C  
ANISOU 1723  CD  LYS A 218     7410   7914  12229  -1400  -2322    573       C  
ATOM   1724  CE  LYS A 218     -13.614  45.842  50.299  1.00 73.71           C  
ANISOU 1724  CE  LYS A 218     7548   8061  12394  -1461  -2483    612       C  
ATOM   1725  NZ  LYS A 218     -12.962  47.061  50.838  1.00 74.91           N  
ANISOU 1725  NZ  LYS A 218     7792   8098  12572  -1594  -2696    635       N  
ATOM   1726  N   GLY A 219     -12.529  42.172  45.974  1.00 72.89           N  
ANISOU 1726  N   GLY A 219     6636   8476  12580  -1235  -1893    858       N  
ATOM   1727  CA  GLY A 219     -11.418  41.253  45.642  1.00 73.91           C  
ANISOU 1727  CA  GLY A 219     6554   8727  12800  -1212  -1877    946       C  
ATOM   1728  C   GLY A 219     -11.801  39.785  45.765  1.00 73.47           C  
ANISOU 1728  C   GLY A 219     6491   8720  12701  -1071  -1785    898       C  
ATOM   1729  O   GLY A 219     -12.288  39.395  46.840  1.00 72.76           O  
ANISOU 1729  O   GLY A 219     6542   8570  12533  -1042  -1839    832       O  
ATOM   1730  N   VAL A 220     -11.583  39.007  44.697  1.00 74.48           N  
ANISOU 1730  N   VAL A 220     6470   8953  12874   -987  -1654    932       N  
ATOM   1731  CA  VAL A 220     -11.705  37.514  44.650  1.00 74.98           C  
ANISOU 1731  CA  VAL A 220     6497   9071  12921   -851  -1579    904       C  
ATOM   1732  C   VAL A 220     -10.289  36.931  44.510  1.00 77.93           C  
ANISOU 1732  C   VAL A 220     6662   9548  13398   -836  -1619    996       C  
ATOM   1733  O   VAL A 220      -9.427  37.630  43.952  1.00 78.73           O  
ANISOU 1733  O   VAL A 220     6618   9711  13582   -912  -1634   1084       O  
ATOM   1734  CB  VAL A 220     -12.627  37.059  43.498  1.00 72.81           C  
ANISOU 1734  CB  VAL A 220     6231   8824  12607   -750  -1403    859       C  
ATOM   1735  CG1 VAL A 220     -12.775  35.544  43.436  1.00 71.85           C  
ANISOU 1735  CG1 VAL A 220     6091   8740  12468   -615  -1344    829       C  
ATOM   1736  CG2 VAL A 220     -13.994  37.720  43.574  1.00 71.44           C  
ANISOU 1736  CG2 VAL A 220     6240   8558  12343   -766  -1365    779       C  
ATOM   1737  N   GLN A 221     -10.064  35.705  45.002  1.00 79.89           N  
ANISOU 1737  N   GLN A 221     6893   9817  13644   -743  -1639    982       N  
ATOM   1738  CA  GLN A 221      -8.731  35.039  45.088  1.00 82.17           C  
ANISOU 1738  CA  GLN A 221     6995  10196  14028   -711  -1699   1060       C  
ATOM   1739  C   GLN A 221      -8.695  33.823  44.152  1.00 83.26           C  
ANISOU 1739  C   GLN A 221     7036  10418  14179   -549  -1565   1050       C  
ATOM   1740  O   GLN A 221      -9.550  32.945  44.312  1.00 82.48           O  
ANISOU 1740  O   GLN A 221     7060  10268  14008   -457  -1523    974       O  
ATOM   1741  CB  GLN A 221      -8.450  34.629  46.536  1.00 82.16           C  
ANISOU 1741  CB  GLN A 221     7072  10132  14011   -733  -1860   1052       C  
ATOM   1742  CG  GLN A 221      -8.181  35.807  47.464  1.00 82.98           C  
ANISOU 1742  CG  GLN A 221     7249  10163  14115   -889  -2017   1075       C  
ATOM   1743  CD  GLN A 221      -9.396  36.679  47.682  1.00 82.02           C  
ANISOU 1743  CD  GLN A 221     7336   9936  13889   -943  -1996    994       C  
ATOM   1744  OE1 GLN A 221     -10.366  36.275  48.319  1.00 82.33           O  
ANISOU 1744  OE1 GLN A 221     7548   9908  13824   -897  -1983    912       O  
ATOM   1745  NE2 GLN A 221      -9.355  37.893  47.157  1.00 81.45           N  
ANISOU 1745  NE2 GLN A 221     7248   9853  13845  -1039  -1993   1023       N  
ATOM   1746  N   ILE A 222      -7.712  33.759  43.248  1.00 87.16           N  
ANISOU 1746  N   ILE A 222     7316  11038  14759   -514  -1509   1127       N  
ATOM   1747  CA  ILE A 222      -7.664  32.812  42.088  1.00 89.58           C  
ANISOU 1747  CA  ILE A 222     7526  11437  15072   -354  -1360   1115       C  
ATOM   1748  C   ILE A 222      -6.317  32.082  42.081  1.00 93.72           C  
ANISOU 1748  C   ILE A 222     7843  12075  15690   -274  -1397   1185       C  
ATOM   1749  O   ILE A 222      -5.344  32.566  42.663  1.00 94.26           O  
ANISOU 1749  O   ILE A 222     7798  12178  15837   -366  -1513   1267       O  
ATOM   1750  CB  ILE A 222      -7.920  33.591  40.775  1.00 89.74           C  
ANISOU 1750  CB  ILE A 222     7495  11517  15085   -378  -1221   1136       C  
ATOM   1751  CG1 ILE A 222      -8.190  32.667  39.580  1.00 88.94           C  
ANISOU 1751  CG1 ILE A 222     7357  11483  14952   -211  -1062   1097       C  
ATOM   1752  CG2 ILE A 222      -6.786  34.573  40.486  1.00 91.05           C  
ANISOU 1752  CG2 ILE A 222     7469  11781  15343   -492  -1253   1257       C  
ATOM   1753  CD1 ILE A 222      -8.596  33.388  38.309  1.00 88.23           C  
ANISOU 1753  CD1 ILE A 222     7250  11439  14834   -232   -926   1108       C  
ATOM   1754  N   PRO A 223      -6.215  30.879  41.459  1.00 95.73           N  
ANISOU 1754  N   PRO A 223     8045  12386  15942    -94  -1310   1154       N  
ATOM   1755  CA  PRO A 223      -4.916  30.327  41.070  1.00 98.23           C  
ANISOU 1755  CA  PRO A 223     8129  12843  16348      5  -1299   1224       C  
ATOM   1756  C   PRO A 223      -4.240  31.205  40.004  1.00100.67           C  
ANISOU 1756  C   PRO A 223     8240  13298  16709    -42  -1199   1316       C  
ATOM   1757  O   PRO A 223      -4.822  31.383  38.941  1.00 98.94           O  
ANISOU 1757  O   PRO A 223     8050  13105  16435     -7  -1055   1288       O  
ATOM   1758  CB  PRO A 223      -5.233  28.933  40.499  1.00 97.61           C  
ANISOU 1758  CB  PRO A 223     8089  12769  16228    216  -1211   1147       C  
ATOM   1759  CG  PRO A 223      -6.631  28.616  41.000  1.00 95.54           C  
ANISOU 1759  CG  PRO A 223     8090  12344  15865    202  -1231   1046       C  
ATOM   1760  CD  PRO A 223      -7.320  29.955  41.155  1.00 94.55           C  
ANISOU 1760  CD  PRO A 223     8059  12163  15703     25  -1232   1050       C  
ATOM   1761  N   CYS A 224      -3.053  31.740  40.316  1.00103.69           N  
ANISOU 1761  N   CYS A 224     8431  13772  17194   -130  -1283   1430       N  
ATOM   1762  CA  CYS A 224      -2.200  32.540  39.393  1.00105.25           C  
ANISOU 1762  CA  CYS A 224     8401  14132  17457   -189  -1204   1549       C  
ATOM   1763  C   CYS A 224      -1.044  31.674  38.887  1.00106.30           C  
ANISOU 1763  C   CYS A 224     8286  14440  17660    -26  -1145   1605       C  
ATOM   1764  O   CYS A 224      -0.845  30.568  39.436  1.00106.39           O  
ANISOU 1764  O   CYS A 224     8313  14425  17683    108  -1204   1556       O  
ATOM   1765  CB  CYS A 224      -1.660  33.793  40.074  1.00106.98           C  
ANISOU 1765  CB  CYS A 224     8564  14333  17747   -415  -1347   1651       C  
ATOM   1766  SG  CYS A 224      -0.159  34.474  39.314  1.00111.75           S  
ANISOU 1766  SG  CYS A 224     8820  15162  18475   -487  -1312   1838       S  
ATOM   1767  N   THR A 225      -0.321  32.177  37.879  1.00106.36           N  
ANISOU 1767  N   THR A 225     8076  14624  17710    -37  -1034   1707       N  
ATOM   1768  CA  THR A 225       0.936  31.594  37.340  1.00106.43           C  
ANISOU 1768  CA  THR A 225     7800  14840  17795     99   -968   1790       C  
ATOM   1769  C   THR A 225       2.127  32.113  38.160  1.00106.83           C  
ANISOU 1769  C   THR A 225     7652  14957  17980    -37  -1126   1927       C  
ATOM   1770  O   THR A 225       3.244  32.135  37.613  1.00109.17           O  
ANISOU 1770  O   THR A 225     7666  15457  18357      0  -1067   2044       O  
ATOM   1771  CB  THR A 225       1.077  31.888  35.840  1.00106.37           C  
ANISOU 1771  CB  THR A 225     7660  15000  17752    152   -760   1838       C  
ATOM   1772  OG1 THR A 225       1.155  33.304  35.679  1.00106.58           O  
ANISOU 1772  OG1 THR A 225     7640  15047  17807    -78   -778   1946       O  
ATOM   1773  CG2 THR A 225      -0.072  31.346  35.017  1.00104.39           C  
ANISOU 1773  CG2 THR A 225     7609  14682  17370    289   -618   1703       C  
ATOM   1774  N   CYS A 226       1.890  32.533  39.412  1.00104.53           N  
ANISOU 1774  N   CYS A 226     7501  14505  17708   -191  -1319   1916       N  
ATOM   1775  CA  CYS A 226       2.929  32.695  40.467  1.00105.02           C  
ANISOU 1775  CA  CYS A 226     7428  14585  17888   -289  -1514   2014       C  
ATOM   1776  C   CYS A 226       2.883  31.498  41.429  1.00105.11           C  
ANISOU 1776  C   CYS A 226     7538  14502  17895   -153  -1623   1926       C  
ATOM   1777  O   CYS A 226       3.636  31.515  42.421  1.00106.44           O  
ANISOU 1777  O   CYS A 226     7633  14659  18150   -222  -1802   1989       O  
ATOM   1778  CB  CYS A 226       2.788  34.016  41.220  1.00103.34           C  
ANISOU 1778  CB  CYS A 226     7308  14258  17696   -556  -1673   2068       C  
ATOM   1779  SG  CYS A 226       1.177  34.294  42.001  1.00 98.65           S  
ANISOU 1779  SG  CYS A 226     7117  13396  16967   -629  -1739   1911       S  
ATOM   1780  N   GLY A 227       2.049  30.493  41.133  1.00104.47           N  
ANISOU 1780  N   GLY A 227     7619  14354  17719     28  -1527   1792       N  
ATOM   1781  CA  GLY A 227       1.996  29.207  41.858  1.00105.20           C  
ANISOU 1781  CA  GLY A 227     7802  14368  17802    183  -1609   1711       C  
ATOM   1782  C   GLY A 227       0.860  29.152  42.870  1.00104.57           C  
ANISOU 1782  C   GLY A 227     8033  14067  17632    107  -1716   1608       C  
ATOM   1783  O   GLY A 227       0.126  28.139  42.870  1.00104.11           O  
ANISOU 1783  O   GLY A 227     8136  13922  17497    250  -1680   1499       O  
ATOM   1784  N   LYS A 228       0.707  30.199  43.693  1.00104.53           N  
ANISOU 1784  N   LYS A 228     8114  13973  17630   -106  -1845   1643       N  
ATOM   1785  CA  LYS A 228      -0.209  30.226  44.870  1.00102.34           C  
ANISOU 1785  CA  LYS A 228     8113  13500  17270   -190  -1973   1562       C  
ATOM   1786  C   LYS A 228      -1.387  31.171  44.578  1.00100.25           C  
ANISOU 1786  C   LYS A 228     8035  13145  16908   -305  -1898   1506       C  
ATOM   1787  O   LYS A 228      -1.874  31.171  43.423  1.00 97.50           O  
ANISOU 1787  O   LYS A 228     7677  12848  16519   -235  -1721   1475       O  
ATOM   1788  CB  LYS A 228       0.580  30.573  46.143  1.00102.90           C  
ANISOU 1788  CB  LYS A 228     8149  13534  17411   -319  -2197   1634       C  
ATOM   1789  CG  LYS A 228       1.297  31.920  46.144  1.00104.24           C  
ANISOU 1789  CG  LYS A 228     8181  13762  17662   -516  -2269   1752       C  
ATOM   1790  CD  LYS A 228       2.736  31.855  45.668  1.00106.44           C  
ANISOU 1790  CD  LYS A 228     8125  14231  18084   -486  -2271   1887       C  
ATOM   1791  CE  LYS A 228       3.304  33.203  45.272  1.00107.43           C  
ANISOU 1791  CE  LYS A 228     8098  14436  18282   -677  -2286   2012       C  
ATOM   1792  NZ  LYS A 228       4.114  33.799  46.360  1.00108.96           N  
ANISOU 1792  NZ  LYS A 228     8241  14594  18563   -848  -2523   2106       N  
ATOM   1793  N   GLN A 229      -1.830  31.939  45.582  1.00100.05           N  
ANISOU 1793  N   GLN A 229     8179  12992  16843   -465  -2029   1491       N  
ATOM   1794  CA  GLN A 229      -3.133  32.656  45.585  1.00 98.52           C  
ANISOU 1794  CA  GLN A 229     8215  12679  16539   -548  -1982   1410       C  
ATOM   1795  C   GLN A 229      -2.922  34.123  45.190  1.00 98.68           C  
ANISOU 1795  C   GLN A 229     8176  12723  16595   -717  -1986   1482       C  
ATOM   1796  O   GLN A 229      -2.276  34.866  45.961  1.00 99.69           O  
ANISOU 1796  O   GLN A 229     8275  12825  16778   -862  -2150   1550       O  
ATOM   1797  CB  GLN A 229      -3.791  32.520  46.962  1.00 97.82           C  
ANISOU 1797  CB  GLN A 229     8362  12435  16368   -596  -2119   1340       C  
ATOM   1798  CG  GLN A 229      -5.306  32.393  46.905  1.00 95.79           C  
ANISOU 1798  CG  GLN A 229     8341  12075  15979   -562  -2023   1225       C  
ATOM   1799  CD  GLN A 229      -5.760  31.325  45.939  1.00 94.77           C  
ANISOU 1799  CD  GLN A 229     8193  11991  15825   -389  -1862   1174       C  
ATOM   1800  OE1 GLN A 229      -6.683  31.527  45.154  1.00 93.48           O  
ANISOU 1800  OE1 GLN A 229     8105  11812  15599   -368  -1728   1122       O  
ATOM   1801  NE2 GLN A 229      -5.097  30.180  45.975  1.00 94.76           N  
ANISOU 1801  NE2 GLN A 229     8092  12038  15871   -261  -1884   1190       N  
ATOM   1802  N   ALA A 230      -3.441  34.503  44.017  1.00 97.07           N  
ANISOU 1802  N   ALA A 230     7960  12561  16361   -699  -1821   1469       N  
ATOM   1803  CA  ALA A 230      -3.535  35.896  43.520  1.00 96.28           C  
ANISOU 1803  CA  ALA A 230     7852  12459  16271   -854  -1806   1521       C  
ATOM   1804  C   ALA A 230      -4.985  36.373  43.643  1.00 92.82           C  
ANISOU 1804  C   ALA A 230     7677  11876  15714   -885  -1771   1411       C  
ATOM   1805  O   ALA A 230      -5.871  35.523  43.863  1.00 92.54           O  
ANISOU 1805  O   ALA A 230     7787  11777  15594   -772  -1721   1307       O  
ATOM   1806  CB  ALA A 230      -3.059  35.974  42.092  1.00 97.65           C  
ANISOU 1806  CB  ALA A 230     7819  12792  16492   -808  -1645   1594       C  
ATOM   1807  N   THR A 231      -5.210  37.679  43.481  1.00 90.08           N  
ANISOU 1807  N   THR A 231     7382  11480  15364  -1031  -1799   1438       N  
ATOM   1808  CA  THR A 231      -6.518  38.350  43.708  1.00 85.99           C  
ANISOU 1808  CA  THR A 231     7110  10818  14741  -1076  -1792   1341       C  
ATOM   1809  C   THR A 231      -6.983  39.041  42.419  1.00 83.00           C  
ANISOU 1809  C   THR A 231     6711  10472  14350  -1095  -1652   1355       C  
ATOM   1810  O   THR A 231      -6.191  39.822  41.856  1.00 83.97           O  
ANISOU 1810  O   THR A 231     6686  10667  14552  -1198  -1666   1466       O  
ATOM   1811  CB  THR A 231      -6.412  39.316  44.894  1.00 86.55           C  
ANISOU 1811  CB  THR A 231     7306  10769  14809  -1230  -1990   1345       C  
ATOM   1812  OG1 THR A 231      -6.215  38.504  46.053  1.00 86.22           O  
ANISOU 1812  OG1 THR A 231     7317  10691  14750  -1185  -2096   1312       O  
ATOM   1813  CG2 THR A 231      -7.626  40.204  45.070  1.00 85.55           C  
ANISOU 1813  CG2 THR A 231     7413  10506  14585  -1280  -1989   1257       C  
ATOM   1814  N   LYS A 232      -8.212  38.740  41.981  1.00 78.12           N  
ANISOU 1814  N   LYS A 232     6235   9806  13639  -1004  -1529   1253       N  
ATOM   1815  CA  LYS A 232      -8.948  39.447  40.897  1.00 75.37           C  
ANISOU 1815  CA  LYS A 232     5929   9450  13254  -1021  -1411   1242       C  
ATOM   1816  C   LYS A 232      -9.862  40.495  41.547  1.00 72.57           C  
ANISOU 1816  C   LYS A 232     5792   8940  12839  -1117  -1496   1179       C  
ATOM   1817  O   LYS A 232     -10.360  40.226  42.658  1.00 71.80           O  
ANISOU 1817  O   LYS A 232     5845   8751  12685  -1098  -1574   1100       O  
ATOM   1818  CB  LYS A 232      -9.759  38.442  40.069  1.00 74.60           C  
ANISOU 1818  CB  LYS A 232     5861   9388  13093   -858  -1241   1168       C  
ATOM   1819  CG  LYS A 232      -9.941  38.798  38.598  1.00 74.77           C  
ANISOU 1819  CG  LYS A 232     5815   9483  13110   -843  -1095   1201       C  
ATOM   1820  CD  LYS A 232     -10.932  37.916  37.850  1.00 73.64           C  
ANISOU 1820  CD  LYS A 232     5746   9341  12890   -694   -949   1112       C  
ATOM   1821  CE  LYS A 232     -10.708  36.431  38.060  1.00 73.75           C  
ANISOU 1821  CE  LYS A 232     5721   9399  12900   -545   -924   1074       C  
ATOM   1822  NZ  LYS A 232     -11.226  35.606  36.941  1.00 73.14           N  
ANISOU 1822  NZ  LYS A 232     5646   9368  12773   -403   -774   1028       N  
ATOM   1823  N   TYR A 233     -10.062  41.646  40.895  1.00 70.30           N  
ANISOU 1823  N   TYR A 233     5524   8626  12559  -1212  -1484   1214       N  
ATOM   1824  CA  TYR A 233     -11.044  42.684  41.312  1.00 67.81           C  
ANISOU 1824  CA  TYR A 233     5423   8161  12181  -1279  -1546   1144       C  
ATOM   1825  C   TYR A 233     -11.490  43.509  40.102  1.00 66.14           C  
ANISOU 1825  C   TYR A 233     5212   7950  11965  -1315  -1456   1170       C  
ATOM   1826  O   TYR A 233     -10.819  43.474  39.045  1.00 65.63           O  
ANISOU 1826  O   TYR A 233     4972   8005  11957  -1327  -1374   1266       O  
ATOM   1827  CB  TYR A 233     -10.482  43.581  42.421  1.00 68.75           C  
ANISOU 1827  CB  TYR A 233     5603   8188  12330  -1419  -1751   1173       C  
ATOM   1828  CG  TYR A 233      -9.316  44.455  42.031  1.00 70.13           C  
ANISOU 1828  CG  TYR A 233     5626   8407  12610  -1571  -1837   1315       C  
ATOM   1829  CD1 TYR A 233      -8.011  44.037  42.238  1.00 71.42           C  
ANISOU 1829  CD1 TYR A 233     5593   8674  12866  -1608  -1899   1419       C  
ATOM   1830  CD2 TYR A 233      -9.511  45.710  41.479  1.00 70.23           C  
ANISOU 1830  CD2 TYR A 233     5689   8359  12636  -1683  -1865   1354       C  
ATOM   1831  CE1 TYR A 233      -6.932  44.831  41.889  1.00 72.76           C  
ANISOU 1831  CE1 TYR A 233     5607   8897  13139  -1758  -1980   1564       C  
ATOM   1832  CE2 TYR A 233      -8.443  46.519  41.126  1.00 71.77           C  
ANISOU 1832  CE2 TYR A 233     5743   8594  12930  -1839  -1952   1499       C  
ATOM   1833  CZ  TYR A 233      -7.148  46.080  41.337  1.00 72.89           C  
ANISOU 1833  CZ  TYR A 233     5678   8850  13164  -1881  -2008   1608       C  
ATOM   1834  OH  TYR A 233      -6.085  46.862  40.994  1.00 74.28           O  
ANISOU 1834  OH  TYR A 233     5698   9080  13444  -2044  -2094   1765       O  
ATOM   1835  N   LEU A 234     -12.610  44.221  40.274  1.00 64.30           N  
ANISOU 1835  N   LEU A 234     5175   7592  11664  -1324  -1470   1086       N  
ATOM   1836  CA  LEU A 234     -13.229  45.101  39.249  1.00 63.01           C  
ANISOU 1836  CA  LEU A 234     5057   7396  11487  -1357  -1405   1094       C  
ATOM   1837  C   LEU A 234     -12.594  46.490  39.339  1.00 63.59           C  
ANISOU 1837  C   LEU A 234     5134   7405  11619  -1531  -1550   1181       C  
ATOM   1838  O   LEU A 234     -12.632  47.081  40.438  1.00 63.76           O  
ANISOU 1838  O   LEU A 234     5288   7308  11629  -1593  -1705   1142       O  
ATOM   1839  CB  LEU A 234     -14.741  45.188  39.481  1.00 61.31           C  
ANISOU 1839  CB  LEU A 234     5047   7073  11173  -1275  -1365    961       C  
ATOM   1840  CG  LEU A 234     -15.497  46.075  38.493  1.00 60.94           C  
ANISOU 1840  CG  LEU A 234     5066   6978  11108  -1296  -1309    958       C  
ATOM   1841  CD1 LEU A 234     -15.444  45.490  37.091  1.00 60.42           C  
ANISOU 1841  CD1 LEU A 234     4867   7036  11054  -1236  -1146   1007       C  
ATOM   1842  CD2 LEU A 234     -16.937  46.281  38.935  1.00 59.84           C  
ANISOU 1842  CD2 LEU A 234     5129   6727  10880  -1221  -1298    829       C  
ATOM   1843  N   VAL A 235     -12.065  46.979  38.214  1.00 63.35           N  
ANISOU 1843  N   VAL A 235     4975   7448  11645  -1604  -1502   1294       N  
ATOM   1844  CA  VAL A 235     -11.449  48.329  38.059  1.00 64.25           C  
ANISOU 1844  CA  VAL A 235     5078   7510  11824  -1787  -1632   1403       C  
ATOM   1845  C   VAL A 235     -12.518  49.311  37.576  1.00 62.95           C  
ANISOU 1845  C   VAL A 235     5087   7221  11610  -1804  -1627   1352       C  
ATOM   1846  O   VAL A 235     -12.736  50.332  38.257  1.00 63.40           O  
ANISOU 1846  O   VAL A 235     5301   7124  11661  -1890  -1784   1324       O  
ATOM   1847  CB  VAL A 235     -10.279  48.276  37.063  1.00 65.55           C  
ANISOU 1847  CB  VAL A 235     4990   7841  12072  -1858  -1571   1568       C  
ATOM   1848  CG1 VAL A 235      -9.718  49.662  36.781  1.00 67.29           C  
ANISOU 1848  CG1 VAL A 235     5196   8011  12359  -2058  -1697   1696       C  
ATOM   1849  CG2 VAL A 235      -9.195  47.320  37.534  1.00 66.21           C  
ANISOU 1849  CG2 VAL A 235     4890   8052  12213  -1830  -1581   1620       C  
ATOM   1850  N   GLN A 236     -13.121  49.012  36.421  1.00 61.10           N  
ANISOU 1850  N   GLN A 236     4824   7051  11340  -1722  -1460   1344       N  
ATOM   1851  CA  GLN A 236     -14.160  49.846  35.763  1.00 59.89           C  
ANISOU 1851  CA  GLN A 236     4815   6799  11142  -1724  -1435   1305       C  
ATOM   1852  C   GLN A 236     -15.211  48.939  35.113  1.00 57.40           C  
ANISOU 1852  C   GLN A 236     4526   6530  10750  -1555  -1255   1212       C  
ATOM   1853  O   GLN A 236     -14.815  48.034  34.348  1.00 57.27           O  
ANISOU 1853  O   GLN A 236     4356   6662  10740  -1492  -1121   1256       O  
ATOM   1854  CB  GLN A 236     -13.529  50.751  34.703  1.00 61.32           C  
ANISOU 1854  CB  GLN A 236     4902   7017  11379  -1864  -1444   1454       C  
ATOM   1855  CG  GLN A 236     -14.431  51.905  34.284  1.00 61.49           C  
ANISOU 1855  CG  GLN A 236     5097   6894  11372  -1907  -1490   1428       C  
ATOM   1856  CD  GLN A 236     -13.955  52.625  33.045  1.00 62.80           C  
ANISOU 1856  CD  GLN A 236     5169   7113  11577  -2027  -1465   1577       C  
ATOM   1857  OE1 GLN A 236     -12.979  52.238  32.405  1.00 63.64           O  
ANISOU 1857  OE1 GLN A 236     5070   7384  11725  -2070  -1390   1703       O  
ATOM   1858  NE2 GLN A 236     -14.658  53.689  32.689  1.00 63.03           N  
ANISOU 1858  NE2 GLN A 236     5352   7007  11589  -2077  -1526   1567       N  
ATOM   1859  N   GLN A 237     -16.493  49.186  35.410  1.00 55.07           N  
ANISOU 1859  N   GLN A 237     4419   6116  10389  -1484  -1258   1089       N  
ATOM   1860  CA  GLN A 237     -17.655  48.661  34.644  1.00 52.55           C  
ANISOU 1860  CA  GLN A 237     4148   5812  10004  -1354  -1111   1014       C  
ATOM   1861  C   GLN A 237     -18.444  49.832  34.042  1.00 51.73           C  
ANISOU 1861  C   GLN A 237     4170   5599   9884  -1394  -1139   1007       C  
ATOM   1862  O   GLN A 237     -18.777  50.769  34.798  1.00 51.49           O  
ANISOU 1862  O   GLN A 237     4285   5427   9849  -1440  -1270    961       O  
ATOM   1863  CB  GLN A 237     -18.566  47.818  35.536  1.00 51.10           C  
ANISOU 1863  CB  GLN A 237     4062   5595   9755  -1223  -1082    878       C  
ATOM   1864  CG  GLN A 237     -19.537  46.950  34.748  1.00 49.53           C  
ANISOU 1864  CG  GLN A 237     3866   5448   9503  -1092   -928    821       C  
ATOM   1865  CD  GLN A 237     -18.864  45.713  34.212  1.00 49.10           C  
ANISOU 1865  CD  GLN A 237     3653   5540   9463  -1034   -823    866       C  
ATOM   1866  OE1 GLN A 237     -18.199  44.992  34.949  1.00 49.15           O  
ANISOU 1866  OE1 GLN A 237     3593   5592   9486  -1018   -849    869       O  
ATOM   1867  NE2 GLN A 237     -19.033  45.457  32.925  1.00 48.64           N  
ANISOU 1867  NE2 GLN A 237     3537   5550   9391   -994   -708    898       N  
ATOM   1868  N   GLU A 238     -18.709  49.770  32.731  1.00 50.88           N  
ANISOU 1868  N   GLU A 238     4013   5552   9765  -1372  -1025   1050       N  
ATOM   1869  CA  GLU A 238     -19.662  50.646  31.995  1.00 50.46           C  
ANISOU 1869  CA  GLU A 238     4079   5407   9686  -1376  -1023   1032       C  
ATOM   1870  C   GLU A 238     -20.621  49.741  31.206  1.00 48.48           C  
ANISOU 1870  C   GLU A 238     3829   5215   9376  -1236   -868    970       C  
ATOM   1871  O   GLU A 238     -20.186  49.173  30.183  1.00 48.31           O  
ANISOU 1871  O   GLU A 238     3685   5317   9351  -1222   -759   1038       O  
ATOM   1872  CB  GLU A 238     -18.916  51.653  31.106  1.00 52.03           C  
ANISOU 1872  CB  GLU A 238     4223   5613   9933  -1524  -1067   1175       C  
ATOM   1873  CG  GLU A 238     -18.052  52.637  31.890  1.00 53.74           C  
ANISOU 1873  CG  GLU A 238     4458   5747  10213  -1678  -1246   1240       C  
ATOM   1874  CD  GLU A 238     -17.727  53.958  31.204  1.00 55.34           C  
ANISOU 1874  CD  GLU A 238     4686   5883  10456  -1833  -1338   1357       C  
ATOM   1875  OE1 GLU A 238     -16.535  54.181  30.867  1.00 56.81           O  
ANISOU 1875  OE1 GLU A 238     4727   6153  10702  -1967  -1365   1506       O  
ATOM   1876  OE2 GLU A 238     -18.654  54.782  31.033  1.00 55.11           O  
ANISOU 1876  OE2 GLU A 238     4821   5716  10403  -1823  -1390   1305       O  
ATOM   1877  N   SER A 239     -21.861  49.595  31.699  1.00 46.86           N  
ANISOU 1877  N   SER A 239     3753   4928   9121  -1134   -863    846       N  
ATOM   1878  CA  SER A 239     -22.938  48.720  31.155  1.00 45.14           C  
ANISOU 1878  CA  SER A 239     3555   4746   8849  -1002   -740    774       C  
ATOM   1879  C   SER A 239     -24.210  48.898  31.981  1.00 43.91           C  
ANISOU 1879  C   SER A 239     3544   4485   8653   -923   -775    652       C  
ATOM   1880  O   SER A 239     -24.138  49.329  33.132  1.00 43.93           O  
ANISOU 1880  O   SER A 239     3617   4415   8657   -944   -872    609       O  
ATOM   1881  CB  SER A 239     -22.515  47.271  31.143  1.00 44.79           C  
ANISOU 1881  CB  SER A 239     3395   4828   8794   -929   -644    772       C  
ATOM   1882  OG  SER A 239     -22.283  46.798  32.464  1.00 44.88           O  
ANISOU 1882  OG  SER A 239     3414   4830   8808   -910   -697    722       O  
ATOM   1883  N   PRO A 240     -25.402  48.550  31.430  1.00 42.47           N  
ANISOU 1883  N   PRO A 240     3408   4298   8430   -827   -696    594       N  
ATOM   1884  CA  PRO A 240     -26.667  48.662  32.162  1.00 41.46           C  
ANISOU 1884  CA  PRO A 240     3396   4093   8263   -742   -713    486       C  
ATOM   1885  C   PRO A 240     -26.925  47.539  33.189  1.00 40.39           C  
ANISOU 1885  C   PRO A 240     3247   4004   8093   -664   -677    418       C  
ATOM   1886  O   PRO A 240     -27.525  47.807  34.219  1.00 40.33           O  
ANISOU 1886  O   PRO A 240     3329   3938   8056   -626   -722    343       O  
ATOM   1887  CB  PRO A 240     -27.708  48.666  31.030  1.00 40.85           C  
ANISOU 1887  CB  PRO A 240     3343   4010   8166   -684   -643    476       C  
ATOM   1888  CG  PRO A 240     -27.086  47.839  29.931  1.00 40.68           C  
ANISOU 1888  CG  PRO A 240     3207   4099   8148   -693   -552    549       C  
ATOM   1889  CD  PRO A 240     -25.595  48.064  30.053  1.00 41.90           C  
ANISOU 1889  CD  PRO A 240     3278   4297   8345   -796   -592    635       C  
ATOM   1890  N   PHE A 241     -26.473  46.315  32.914  1.00 39.46           N  
ANISOU 1890  N   PHE A 241     3027   3989   7976   -638   -601    445       N  
ATOM   1891  CA  PHE A 241     -26.562  45.175  33.865  1.00 38.86           C  
ANISOU 1891  CA  PHE A 241     2933   3957   7873   -579   -578    398       C  
ATOM   1892  C   PHE A 241     -25.247  44.380  33.887  1.00 39.22           C  
ANISOU 1892  C   PHE A 241     2862   4089   7948   -609   -569    459       C  
ATOM   1893  O   PHE A 241     -24.400  44.564  32.987  1.00 39.46           O  
ANISOU 1893  O   PHE A 241     2810   4166   8015   -658   -551    537       O  
ATOM   1894  CB  PHE A 241     -27.725  44.259  33.482  1.00 37.54           C  
ANISOU 1894  CB  PHE A 241     2777   3818   7668   -483   -491    352       C  
ATOM   1895  CG  PHE A 241     -27.513  43.541  32.178  1.00 36.97           C  
ANISOU 1895  CG  PHE A 241     2628   3813   7604   -462   -412    399       C  
ATOM   1896  CD1 PHE A 241     -26.855  42.321  32.143  1.00 36.78           C  
ANISOU 1896  CD1 PHE A 241     2524   3867   7581   -434   -371    418       C  
ATOM   1897  CD2 PHE A 241     -27.928  44.108  30.985  1.00 36.74           C  
ANISOU 1897  CD2 PHE A 241     2616   3767   7577   -468   -384    422       C  
ATOM   1898  CE1 PHE A 241     -26.638  41.669  30.941  1.00 36.62           C  
ANISOU 1898  CE1 PHE A 241     2447   3908   7558   -401   -300    452       C  
ATOM   1899  CE2 PHE A 241     -27.718  43.450  29.784  1.00 36.69           C  
ANISOU 1899  CE2 PHE A 241     2552   3825   7564   -444   -312    461       C  
ATOM   1900  CZ  PHE A 241     -27.072  42.234  29.764  1.00 36.63           C  
ANISOU 1900  CZ  PHE A 241     2469   3896   7551   -406   -268    473       C  
ATOM   1901  N   VAL A 242     -25.100  43.510  34.890  1.00 39.21           N  
ANISOU 1901  N   VAL A 242     2852   4114   7931   -576   -580    427       N  
ATOM   1902  CA  VAL A 242     -24.085  42.413  34.917  1.00 39.69           C  
ANISOU 1902  CA  VAL A 242     2803   4263   8015   -565   -557    469       C  
ATOM   1903  C   VAL A 242     -24.751  41.117  35.403  1.00 39.16           C  
ANISOU 1903  C   VAL A 242     2755   4217   7905   -478   -516    416       C  
ATOM   1904  O   VAL A 242     -25.539  41.161  36.382  1.00 38.67           O  
ANISOU 1904  O   VAL A 242     2779   4110   7803   -459   -543    357       O  
ATOM   1905  CB  VAL A 242     -22.848  42.765  35.769  1.00 40.71           C  
ANISOU 1905  CB  VAL A 242     2890   4395   8183   -644   -652    511       C  
ATOM   1906  CG1 VAL A 242     -22.007  43.846  35.105  1.00 41.80           C  
ANISOU 1906  CG1 VAL A 242     2975   4531   8373   -742   -689    591       C  
ATOM   1907  CG2 VAL A 242     -23.202  43.164  37.195  1.00 40.79           C  
ANISOU 1907  CG2 VAL A 242     3008   4330   8160   -657   -741    451       C  
ATOM   1908  N   MET A 243     -24.427  40.014  34.721  1.00 39.14           N  
ANISOU 1908  N   MET A 243     2677   4283   7910   -426   -453    438       N  
ATOM   1909  CA  MET A 243     -24.779  38.619  35.087  1.00 38.82           C  
ANISOU 1909  CA  MET A 243     2640   4265   7842   -351   -428    407       C  
ATOM   1910  C   MET A 243     -23.592  37.987  35.818  1.00 39.67           C  
ANISOU 1910  C   MET A 243     2679   4414   7977   -358   -475    435       C  
ATOM   1911  O   MET A 243     -22.550  37.773  35.173  1.00 40.43           O  
ANISOU 1911  O   MET A 243     2674   4574   8113   -355   -456    487       O  
ATOM   1912  CB  MET A 243     -25.073  37.816  33.818  1.00 38.35           C  
ANISOU 1912  CB  MET A 243     2553   4243   7775   -283   -347    411       C  
ATOM   1913  CG  MET A 243     -25.634  36.444  34.073  1.00 37.75           C  
ANISOU 1913  CG  MET A 243     2504   4168   7670   -212   -333    378       C  
ATOM   1914  SD  MET A 243     -26.065  35.617  32.523  1.00 37.25           S  
ANISOU 1914  SD  MET A 243     2436   4127   7589   -134   -257    376       S  
ATOM   1915  CE  MET A 243     -26.692  34.072  33.178  1.00 37.00           C  
ANISOU 1915  CE  MET A 243     2452   4073   7531    -76   -280    343       C  
ATOM   1916  N   MET A 244     -23.738  37.723  37.117  1.00 40.03           N  
ANISOU 1916  N   MET A 244     2776   4432   8000   -365   -534    407       N  
ATOM   1917  CA  MET A 244     -22.717  37.034  37.950  1.00 40.78           C  
ANISOU 1917  CA  MET A 244     2821   4558   8116   -368   -593    430       C  
ATOM   1918  C   MET A 244     -23.124  35.560  38.104  1.00 40.75           C  
ANISOU 1918  C   MET A 244     2830   4565   8084   -290   -570    409       C  
ATOM   1919  O   MET A 244     -24.116  35.281  38.800  1.00 39.87           O  
ANISOU 1919  O   MET A 244     2807   4419   7922   -280   -575    371       O  
ATOM   1920  CB  MET A 244     -22.586  37.698  39.325  1.00 41.14           C  
ANISOU 1920  CB  MET A 244     2929   4557   8144   -430   -688    415       C  
ATOM   1921  CG  MET A 244     -22.292  39.202  39.278  1.00 41.74           C  
ANISOU 1921  CG  MET A 244     3021   4596   8243   -512   -735    430       C  
ATOM   1922  SD  MET A 244     -20.661  39.714  38.633  1.00 42.87           S  
ANISOU 1922  SD  MET A 244     3019   4791   8475   -585   -771    524       S  
ATOM   1923  CE  MET A 244     -19.606  38.397  39.235  1.00 43.39           C  
ANISOU 1923  CE  MET A 244     2990   4923   8570   -547   -804    555       C  
ATOM   1924  N   SER A 245     -22.379  34.652  37.464  1.00 41.74           N  
ANISOU 1924  N   SER A 245     2873   4741   8242   -234   -545    437       N  
ATOM   1925  CA  SER A 245     -22.624  33.186  37.467  1.00 41.88           C  
ANISOU 1925  CA  SER A 245     2907   4762   8243   -154   -536    421       C  
ATOM   1926  C   SER A 245     -21.645  32.489  38.413  1.00 42.78           C  
ANISOU 1926  C   SER A 245     2981   4890   8379   -146   -613    443       C  
ATOM   1927  O   SER A 245     -20.590  33.073  38.699  1.00 43.42           O  
ANISOU 1927  O   SER A 245     2989   5002   8504   -189   -655    479       O  
ATOM   1928  CB  SER A 245     -22.521  32.620  36.083  1.00 41.97           C  
ANISOU 1928  CB  SER A 245     2873   4807   8264    -78   -465    425       C  
ATOM   1929  OG  SER A 245     -23.602  33.068  35.283  1.00 41.56           O  
ANISOU 1929  OG  SER A 245     2877   4730   8182    -81   -406    401       O  
ATOM   1930  N   ALA A 246     -21.999  31.279  38.851  1.00 42.99           N  
ANISOU 1930  N   ALA A 246     3057   4894   8382    -96   -637    427       N  
ATOM   1931  CA  ALA A 246     -21.219  30.430  39.780  1.00 44.11           C  
ANISOU 1931  CA  ALA A 246     3181   5037   8539    -79   -719    446       C  
ATOM   1932  C   ALA A 246     -21.939  29.095  39.958  1.00 44.60           C  
ANISOU 1932  C   ALA A 246     3320   5058   8566    -25   -732    429       C  
ATOM   1933  O   ALA A 246     -23.166  29.038  39.885  1.00 43.74           O  
ANISOU 1933  O   ALA A 246     3291   4915   8410    -38   -699    406       O  
ATOM   1934  CB  ALA A 246     -21.041  31.140  41.099  1.00 44.20           C  
ANISOU 1934  CB  ALA A 246     3226   5031   8535   -163   -795    454       C  
ATOM   1935  N   PRO A 247     -21.203  27.977  40.167  1.00 46.00           N  
ANISOU 1935  N   PRO A 247     3471   5236   8768     37   -787    444       N  
ATOM   1936  CA  PRO A 247     -21.819  26.694  40.514  1.00 46.39           C  
ANISOU 1936  CA  PRO A 247     3606   5231   8786     73   -828    437       C  
ATOM   1937  C   PRO A 247     -22.894  26.797  41.595  1.00 46.70           C  
ANISOU 1937  C   PRO A 247     3748   5233   8761     -6   -854    438       C  
ATOM   1938  O   PRO A 247     -22.672  27.424  42.630  1.00 47.35           O  
ANISOU 1938  O   PRO A 247     3840   5323   8825    -70   -895    448       O  
ATOM   1939  CB  PRO A 247     -20.626  25.887  41.027  1.00 47.07           C  
ANISOU 1939  CB  PRO A 247     3645   5325   8914    123   -912    462       C  
ATOM   1940  CG  PRO A 247     -19.479  26.392  40.185  1.00 47.69           C  
ANISOU 1940  CG  PRO A 247     3589   5475   9053    168   -871    472       C  
ATOM   1941  CD  PRO A 247     -19.745  27.874  40.017  1.00 47.01           C  
ANISOU 1941  CD  PRO A 247     3482   5417   8960     79   -815    473       C  
ATOM   1942  N   PRO A 248     -24.083  26.181  41.392  1.00 46.74           N  
ANISOU 1942  N   PRO A 248     3832   5200   8727     -3   -833    430       N  
ATOM   1943  CA  PRO A 248     -25.172  26.259  42.363  1.00 46.56           C  
ANISOU 1943  CA  PRO A 248     3891   5161   8638    -75   -842    439       C  
ATOM   1944  C   PRO A 248     -24.633  26.108  43.789  1.00 47.45           C  
ANISOU 1944  C   PRO A 248     4029   5273   8726   -115   -926    465       C  
ATOM   1945  O   PRO A 248     -24.047  25.090  44.086  1.00 47.49           O  
ANISOU 1945  O   PRO A 248     4040   5253   8748    -83  -1000    489       O  
ATOM   1946  CB  PRO A 248     -26.088  25.099  41.965  1.00 46.27           C  
ANISOU 1946  CB  PRO A 248     3914   5079   8585    -53   -848    450       C  
ATOM   1947  CG  PRO A 248     -25.895  25.001  40.467  1.00 46.17           C  
ANISOU 1947  CG  PRO A 248     3862   5062   8616     20   -800    422       C  
ATOM   1948  CD  PRO A 248     -24.438  25.347  40.232  1.00 46.79           C  
ANISOU 1948  CD  PRO A 248     3852   5180   8746     68   -806    416       C  
ATOM   1949  N   ALA A 249     -24.822  27.151  44.597  1.00 48.27           N  
ANISOU 1949  N   ALA A 249     4153   5400   8787   -178   -918    457       N  
ATOM   1950  CA  ALA A 249     -24.252  27.315  45.952  1.00 49.56           C  
ANISOU 1950  CA  ALA A 249     4346   5567   8916   -222   -998    473       C  
ATOM   1951  C   ALA A 249     -25.343  27.838  46.892  1.00 49.97           C  
ANISOU 1951  C   ALA A 249     4483   5630   8870   -280   -972    466       C  
ATOM   1952  O   ALA A 249     -26.015  28.808  46.531  1.00 49.07           O  
ANISOU 1952  O   ALA A 249     4372   5533   8739   -290   -898    432       O  
ATOM   1953  CB  ALA A 249     -23.071  28.252  45.884  1.00 49.73           C  
ANISOU 1953  CB  ALA A 249     4296   5609   8991   -230  -1024    465       C  
ATOM   1954  N   GLN A 250     -25.509  27.198  48.051  1.00 51.95           N  
ANISOU 1954  N   GLN A 250     4804   5877   9057   -311  -1030    498       N  
ATOM   1955  CA  GLN A 250     -26.489  27.595  49.095  1.00 53.33           C  
ANISOU 1955  CA  GLN A 250     5062   6080   9121   -359  -1004    497       C  
ATOM   1956  C   GLN A 250     -26.199  29.050  49.496  1.00 54.16           C  
ANISOU 1956  C   GLN A 250     5179   6199   9199   -376   -998    449       C  
ATOM   1957  O   GLN A 250     -25.227  29.280  50.225  1.00 55.41           O  
ANISOU 1957  O   GLN A 250     5350   6345   9355   -396  -1085    452       O  
ATOM   1958  CB  GLN A 250     -26.423  26.613  50.269  1.00 54.27           C  
ANISOU 1958  CB  GLN A 250     5248   6193   9177   -390  -1083    550       C  
ATOM   1959  CG  GLN A 250     -27.781  26.317  50.897  1.00 55.11           C  
ANISOU 1959  CG  GLN A 250     5421   6336   9181   -427  -1031    579       C  
ATOM   1960  CD  GLN A 250     -28.677  25.441  50.050  1.00 55.23           C  
ANISOU 1960  CD  GLN A 250     5415   6342   9228   -421   -988    612       C  
ATOM   1961  OE1 GLN A 250     -28.325  25.018  48.947  1.00 55.33           O  
ANISOU 1961  OE1 GLN A 250     5376   6313   9331   -380   -995    604       O  
ATOM   1962  NE2 GLN A 250     -29.860  25.153  50.570  1.00 55.28           N  
ANISOU 1962  NE2 GLN A 250     5462   6390   9152   -463   -944    653       N  
ATOM   1963  N   TYR A 251     -27.018  29.997  49.031  1.00 54.67           N  
ANISOU 1963  N   TYR A 251     5244   6280   9247   -369   -911    407       N  
ATOM   1964  CA  TYR A 251     -26.760  31.458  49.133  1.00 55.54           C  
ANISOU 1964  CA  TYR A 251     5367   6384   9349   -378   -909    355       C  
ATOM   1965  C   TYR A 251     -28.062  32.211  49.450  1.00 55.94           C  
ANISOU 1965  C   TYR A 251     5480   6462   9311   -370   -828    316       C  
ATOM   1966  O   TYR A 251     -29.088  31.938  48.802  1.00 55.14           O  
ANISOU 1966  O   TYR A 251     5355   6383   9212   -349   -745    322       O  
ATOM   1967  CB  TYR A 251     -26.103  31.922  47.831  1.00 55.36           C  
ANISOU 1967  CB  TYR A 251     5253   6341   9436   -361   -894    345       C  
ATOM   1968  CG  TYR A 251     -25.670  33.365  47.775  1.00 56.25           C  
ANISOU 1968  CG  TYR A 251     5371   6435   9565   -382   -911    306       C  
ATOM   1969  CD1 TYR A 251     -25.287  34.068  48.910  1.00 57.31           C  
ANISOU 1969  CD1 TYR A 251     5578   6553   9641   -417   -986    286       C  
ATOM   1970  CD2 TYR A 251     -25.598  34.018  46.555  1.00 56.36           C  
ANISOU 1970  CD2 TYR A 251     5322   6441   9650   -372   -864    295       C  
ATOM   1971  CE1 TYR A 251     -24.881  35.391  48.836  1.00 58.00           C  
ANISOU 1971  CE1 TYR A 251     5682   6607   9747   -442  -1020    253       C  
ATOM   1972  CE2 TYR A 251     -25.185  35.337  46.461  1.00 56.96           C  
ANISOU 1972  CE2 TYR A 251     5405   6489   9745   -402   -891    270       C  
ATOM   1973  CZ  TYR A 251     -24.826  36.026  47.606  1.00 57.88           C  
ANISOU 1973  CZ  TYR A 251     5600   6581   9811   -438   -974    249       C  
ATOM   1974  OH  TYR A 251     -24.424  37.326  47.506  1.00 58.94           O  
ANISOU 1974  OH  TYR A 251     5753   6674   9967   -474  -1019    226       O  
ATOM   1975  N   GLU A 252     -28.000  33.135  50.421  1.00 57.42           N  
ANISOU 1975  N   GLU A 252     5747   6648   9421   -381   -859    277       N  
ATOM   1976  CA  GLU A 252     -29.116  34.015  50.875  1.00 57.71           C  
ANISOU 1976  CA  GLU A 252     5854   6713   9360   -355   -790    226       C  
ATOM   1977  C   GLU A 252     -29.165  35.276  50.000  1.00 56.12           C  
ANISOU 1977  C   GLU A 252     5634   6474   9213   -333   -763    172       C  
ATOM   1978  O   GLU A 252     -28.234  36.092  50.102  1.00 56.26           O  
ANISOU 1978  O   GLU A 252     5672   6443   9260   -356   -841    148       O  
ATOM   1979  CB  GLU A 252     -28.915  34.389  52.348  1.00 60.11           C  
ANISOU 1979  CB  GLU A 252     6270   7023   9546   -366   -850    203       C  
ATOM   1980  CG  GLU A 252     -29.953  35.353  52.906  1.00 62.15           C  
ANISOU 1980  CG  GLU A 252     6611   7310   9690   -320   -785    139       C  
ATOM   1981  CD  GLU A 252     -30.795  34.820  54.057  1.00 64.35           C  
ANISOU 1981  CD  GLU A 252     6957   7668   9824   -309   -740    158       C  
ATOM   1982  OE1 GLU A 252     -30.866  35.510  55.107  1.00 65.67           O  
ANISOU 1982  OE1 GLU A 252     7236   7844   9872   -286   -761    108       O  
ATOM   1983  OE2 GLU A 252     -31.387  33.722  53.906  1.00 65.23           O  
ANISOU 1983  OE2 GLU A 252     7015   7832   9937   -323   -687    224       O  
ATOM   1984  N   LEU A 253     -30.209  35.423  49.176  1.00 54.31           N  
ANISOU 1984  N   LEU A 253     5368   6265   9000   -298   -667    161       N  
ATOM   1985  CA  LEU A 253     -30.508  36.668  48.412  1.00 53.19           C  
ANISOU 1985  CA  LEU A 253     5225   6090   8893   -271   -636    109       C  
ATOM   1986  C   LEU A 253     -31.254  37.651  49.322  1.00 53.25           C  
ANISOU 1986  C   LEU A 253     5333   6106   8790   -229   -617     44       C  
ATOM   1987  O   LEU A 253     -32.334  37.289  49.849  1.00 53.69           O  
ANISOU 1987  O   LEU A 253     5408   6230   8761   -194   -543     45       O  
ATOM   1988  CB  LEU A 253     -31.344  36.343  47.170  1.00 52.05           C  
ANISOU 1988  CB  LEU A 253     5004   5964   8809   -246   -549    127       C  
ATOM   1989  CG  LEU A 253     -30.600  35.647  46.036  1.00 51.44           C  
ANISOU 1989  CG  LEU A 253     4839   5866   8840   -268   -564    172       C  
ATOM   1990  CD1 LEU A 253     -31.532  35.397  44.865  1.00 50.87           C  
ANISOU 1990  CD1 LEU A 253     4713   5806   8809   -241   -486    182       C  
ATOM   1991  CD2 LEU A 253     -29.395  36.455  45.587  1.00 51.73           C  
ANISOU 1991  CD2 LEU A 253     4855   5852   8946   -294   -626    162       C  
ATOM   1992  N   LYS A 254     -30.694  38.850  49.489  1.00 52.54           N  
ANISOU 1992  N   LYS A 254     5307   5952   8701   -232   -683     -8       N  
ATOM   1993  CA  LYS A 254     -31.261  39.933  50.328  1.00 52.34           C  
ANISOU 1993  CA  LYS A 254     5400   5915   8571   -179   -685    -86       C  
ATOM   1994  C   LYS A 254     -32.050  40.889  49.431  1.00 50.55           C  
ANISOU 1994  C   LYS A 254     5164   5661   8379   -126   -629   -130       C  
ATOM   1995  O   LYS A 254     -31.575  41.206  48.315  1.00 48.91           O  
ANISOU 1995  O   LYS A 254     4898   5402   8283   -159   -650   -112       O  
ATOM   1996  CB  LYS A 254     -30.149  40.647  51.102  1.00 54.03           C  
ANISOU 1996  CB  LYS A 254     5708   6057   8762   -218   -817   -117       C  
ATOM   1997  CG  LYS A 254     -30.258  40.563  52.621  1.00 55.68           C  
ANISOU 1997  CG  LYS A 254     6035   6294   8824   -198   -847   -147       C  
ATOM   1998  CD  LYS A 254     -30.575  41.897  53.285  1.00 57.24           C  
ANISOU 1998  CD  LYS A 254     6378   6441   8926   -139   -883   -245       C  
ATOM   1999  CE  LYS A 254     -29.444  42.903  53.157  1.00 57.74           C  
ANISOU 1999  CE  LYS A 254     6498   6386   9055   -195  -1028   -269       C  
ATOM   2000  NZ  LYS A 254     -29.533  43.980  54.172  1.00 59.00           N  
ANISOU 2000  NZ  LYS A 254     6835   6486   9095   -148  -1102   -362       N  
ATOM   2001  N   HIS A 255     -33.217  41.311  49.926  1.00 49.77           N  
ANISOU 2001  N   HIS A 255     5120   5604   8184    -44   -558   -183       N  
ATOM   2002  CA  HIS A 255     -34.210  42.163  49.221  1.00 48.62           C  
ANISOU 2002  CA  HIS A 255     4970   5447   8055     28   -495   -229       C  
ATOM   2003  C   HIS A 255     -33.531  43.447  48.730  1.00 47.88           C  
ANISOU 2003  C   HIS A 255     4935   5234   8022     14   -588   -274       C  
ATOM   2004  O   HIS A 255     -32.831  44.100  49.536  1.00 48.32           O  
ANISOU 2004  O   HIS A 255     5099   5228   8030      0   -687   -317       O  
ATOM   2005  CB  HIS A 255     -35.418  42.419  50.137  1.00 49.57           C  
ANISOU 2005  CB  HIS A 255     5149   5641   8041    129   -416   -282       C  
ATOM   2006  CG  HIS A 255     -36.273  43.568  49.722  1.00 50.00           C  
ANISOU 2006  CG  HIS A 255     5237   5667   8094    223   -382   -353       C  
ATOM   2007  ND1 HIS A 255     -36.634  43.789  48.408  1.00 49.12           N  
ANISOU 2007  ND1 HIS A 255     5045   5526   8092    224   -354   -335       N  
ATOM   2008  CD2 HIS A 255     -36.850  44.551  50.445  1.00 51.18           C  
ANISOU 2008  CD2 HIS A 255     5495   5809   8140    328   -375   -444       C  
ATOM   2009  CE1 HIS A 255     -37.382  44.869  48.339  1.00 49.81           C  
ANISOU 2009  CE1 HIS A 255     5187   5585   8152    321   -338   -408       C  
ATOM   2010  NE2 HIS A 255     -37.528  45.354  49.573  1.00 51.13           N  
ANISOU 2010  NE2 HIS A 255     5471   5765   8191    391   -349   -479       N  
ATOM   2011  N   GLY A 256     -33.707  43.750  47.440  1.00 46.19           N  
ANISOU 2011  N   GLY A 256     4653   4987   7910      8   -566   -257       N  
ATOM   2012  CA  GLY A 256     -33.356  45.035  46.805  1.00 45.64           C  
ANISOU 2012  CA  GLY A 256     4633   4808   7899      1   -638   -292       C  
ATOM   2013  C   GLY A 256     -31.869  45.318  46.828  1.00 44.96           C  
ANISOU 2013  C   GLY A 256     4567   4646   7869    -99   -762   -264       C  
ATOM   2014  O   GLY A 256     -31.530  46.504  46.879  1.00 45.65           O  
ANISOU 2014  O   GLY A 256     4746   4635   7963   -107   -853   -306       O  
ATOM   2015  N   THR A 257     -31.030  44.270  46.796  1.00 43.79           N  
ANISOU 2015  N   THR A 257     4335   4540   7761   -171   -772   -193       N  
ATOM   2016  CA  THR A 257     -29.548  44.319  46.615  1.00 43.03           C  
ANISOU 2016  CA  THR A 257     4207   4399   7743   -273   -876   -141       C  
ATOM   2017  C   THR A 257     -29.161  43.555  45.341  1.00 41.42           C  
ANISOU 2017  C   THR A 257     3857   4233   7645   -314   -825    -62       C  
ATOM   2018  O   THR A 257     -28.063  42.973  45.318  1.00 41.27           O  
ANISOU 2018  O   THR A 257     3773   4231   7677   -378   -870     -5       O  
ATOM   2019  CB  THR A 257     -28.784  43.702  47.797  1.00 43.43           C  
ANISOU 2019  CB  THR A 257     4287   4471   7743   -309   -942   -129       C  
ATOM   2020  OG1 THR A 257     -28.995  42.289  47.791  1.00 42.69           O  
ANISOU 2020  OG1 THR A 257     4106   4468   7644   -300   -864    -81       O  
ATOM   2021  CG2 THR A 257     -29.179  44.269  49.143  1.00 44.54           C  
ANISOU 2021  CG2 THR A 257     4579   4588   7754   -260   -985   -207       C  
ATOM   2022  N   PHE A 258     -30.044  43.540  44.340  1.00 40.12           N  
ANISOU 2022  N   PHE A 258     3648   4086   7508   -272   -736    -61       N  
ATOM   2023  CA  PHE A 258     -29.891  42.821  43.048  1.00 38.98           C  
ANISOU 2023  CA  PHE A 258     3382   3979   7447   -292   -677      1       C  
ATOM   2024  C   PHE A 258     -31.209  42.923  42.282  1.00 38.22           C  
ANISOU 2024  C   PHE A 258     3277   3896   7346   -227   -588    -18       C  
ATOM   2025  O   PHE A 258     -32.225  43.209  42.922  1.00 38.58           O  
ANISOU 2025  O   PHE A 258     3385   3950   7322   -163   -558    -72       O  
ATOM   2026  CB  PHE A 258     -29.541  41.343  43.247  1.00 38.48           C  
ANISOU 2026  CB  PHE A 258     3246   3988   7386   -301   -649     48       C  
ATOM   2027  CG  PHE A 258     -30.674  40.502  43.783  1.00 38.06           C  
ANISOU 2027  CG  PHE A 258     3205   3992   7261   -245   -577     33       C  
ATOM   2028  CD1 PHE A 258     -31.493  39.792  42.921  1.00 37.19           C  
ANISOU 2028  CD1 PHE A 258     3033   3921   7174   -214   -494     55       C  
ATOM   2029  CD2 PHE A 258     -30.925  40.432  45.145  1.00 38.50           C  
ANISOU 2029  CD2 PHE A 258     3336   4067   7224   -227   -595      1       C  
ATOM   2030  CE1 PHE A 258     -32.539  39.029  43.407  1.00 37.08           C  
ANISOU 2030  CE1 PHE A 258     3023   3965   7102   -177   -435     56       C  
ATOM   2031  CE2 PHE A 258     -31.975  39.670  45.629  1.00 38.44           C  
ANISOU 2031  CE2 PHE A 258     3330   4126   7149   -184   -523      1       C  
ATOM   2032  CZ  PHE A 258     -32.780  38.971  44.760  1.00 37.70           C  
ANISOU 2032  CZ  PHE A 258     3164   4071   7089   -164   -446     33       C  
ATOM   2033  N   THR A 259     -31.179  42.696  40.969  1.00 37.39           N  
ANISOU 2033  N   THR A 259     3095   3799   7311   -241   -548     23       N  
ATOM   2034  CA  THR A 259     -32.363  42.752  40.082  1.00 36.98           C  
ANISOU 2034  CA  THR A 259     3027   3755   7267   -188   -475     14       C  
ATOM   2035  C   THR A 259     -33.111  41.423  40.223  1.00 36.67           C  
ANISOU 2035  C   THR A 259     2939   3791   7200   -154   -404     30       C  
ATOM   2036  O   THR A 259     -34.100  41.377  40.969  1.00 36.74           O  
ANISOU 2036  O   THR A 259     2980   3831   7146   -105   -370     -2       O  
ATOM   2037  CB  THR A 259     -31.967  43.062  38.632  1.00 36.72           C  
ANISOU 2037  CB  THR A 259     2944   3696   7309   -222   -471     56       C  
ATOM   2038  OG1 THR A 259     -31.136  44.225  38.575  1.00 37.40           O  
ANISOU 2038  OG1 THR A 259     3069   3714   7424   -275   -549     59       O  
ATOM   2039  CG2 THR A 259     -33.175  43.261  37.744  1.00 36.35           C  
ANISOU 2039  CG2 THR A 259     2895   3646   7270   -171   -415     44       C  
ATOM   2040  N   CYS A 260     -32.629  40.372  39.560  1.00 36.39           N  
ANISOU 2040  N   CYS A 260     2832   3788   7206   -180   -386     82       N  
ATOM   2041  CA  CYS A 260     -33.225  39.012  39.582  1.00 36.17           C  
ANISOU 2041  CA  CYS A 260     2763   3815   7162   -161   -339    108       C  
ATOM   2042  C   CYS A 260     -32.107  37.967  39.502  1.00 36.34           C  
ANISOU 2042  C   CYS A 260     2739   3853   7213   -193   -366    152       C  
ATOM   2043  O   CYS A 260     -31.002  38.315  39.042  1.00 36.57           O  
ANISOU 2043  O   CYS A 260     2743   3863   7288   -223   -398    168       O  
ATOM   2044  CB  CYS A 260     -34.208  38.841  38.433  1.00 35.58           C  
ANISOU 2044  CB  CYS A 260     2657   3745   7114   -132   -287    119       C  
ATOM   2045  SG  CYS A 260     -33.421  38.991  36.809  1.00 35.29           S  
ANISOU 2045  SG  CYS A 260     2580   3678   7150   -154   -290    150       S  
ATOM   2046  N   ALA A 261     -32.397  36.742  39.941  1.00 36.56           N  
ANISOU 2046  N   ALA A 261     2755   3918   7216   -186   -355    174       N  
ATOM   2047  CA  ALA A 261     -31.437  35.627  40.093  1.00 36.93           C  
ANISOU 2047  CA  ALA A 261     2771   3978   7282   -203   -389    210       C  
ATOM   2048  C   ALA A 261     -31.926  34.415  39.294  1.00 37.18           C  
ANISOU 2048  C   ALA A 261     2773   4020   7333   -182   -362    240       C  
ATOM   2049  O   ALA A 261     -32.921  34.550  38.541  1.00 37.69           O  
ANISOU 2049  O   ALA A 261     2836   4082   7403   -164   -320    235       O  
ATOM   2050  CB  ALA A 261     -31.283  35.290  41.554  1.00 37.28           C  
ANISOU 2050  CB  ALA A 261     2854   4040   7269   -219   -427    210       C  
ATOM   2051  N   SER A 262     -31.226  33.285  39.428  1.00 37.31           N  
ANISOU 2051  N   SER A 262     2773   4041   7362   -182   -396    269       N  
ATOM   2052  CA  SER A 262     -31.656  31.952  38.937  1.00 37.11           C  
ANISOU 2052  CA  SER A 262     2744   4012   7345   -164   -396    296       C  
ATOM   2053  C   SER A 262     -31.273  30.913  39.993  1.00 37.71           C  
ANISOU 2053  C   SER A 262     2837   4092   7396   -178   -449    323       C  
ATOM   2054  O   SER A 262     -30.083  30.819  40.312  1.00 38.30           O  
ANISOU 2054  O   SER A 262     2896   4165   7490   -177   -492    327       O  
ATOM   2055  CB  SER A 262     -31.054  31.647  37.590  1.00 36.87           C  
ANISOU 2055  CB  SER A 262     2680   3966   7364   -130   -388    299       C  
ATOM   2056  OG  SER A 262     -31.046  32.808  36.763  1.00 36.77           O  
ANISOU 2056  OG  SER A 262     2649   3950   7370   -128   -350    280       O  
ATOM   2057  N   GLU A 263     -32.264  30.233  40.572  1.00 38.06           N  
ANISOU 2057  N   GLU A 263     2911   4148   7400   -197   -449    348       N  
ATOM   2058  CA  GLU A 263     -32.073  29.088  41.497  1.00 38.38           C  
ANISOU 2058  CA  GLU A 263     2979   4188   7414   -218   -506    388       C  
ATOM   2059  C   GLU A 263     -32.019  27.811  40.656  1.00 37.99           C  
ANISOU 2059  C   GLU A 263     2931   4097   7404   -196   -541    413       C  
ATOM   2060  O   GLU A 263     -32.655  27.791  39.586  1.00 37.47           O  
ANISOU 2060  O   GLU A 263     2857   4016   7362   -179   -511    407       O  
ATOM   2061  CB  GLU A 263     -33.206  29.027  42.522  1.00 39.12           C  
ANISOU 2061  CB  GLU A 263     3102   4323   7438   -256   -485    414       C  
ATOM   2062  CG  GLU A 263     -33.005  27.978  43.605  1.00 40.12           C  
ANISOU 2062  CG  GLU A 263     3264   4453   7525   -290   -544    463       C  
ATOM   2063  CD  GLU A 263     -34.285  27.438  44.222  1.00 41.07           C  
ANISOU 2063  CD  GLU A 263     3401   4614   7588   -334   -524    517       C  
ATOM   2064  OE1 GLU A 263     -35.203  27.066  43.456  1.00 41.16           O  
ANISOU 2064  OE1 GLU A 263     3392   4621   7625   -341   -503    540       O  
ATOM   2065  OE2 GLU A 263     -34.367  27.391  45.471  1.00 42.36           O  
ANISOU 2065  OE2 GLU A 263     3595   4818   7678   -365   -532    540       O  
ATOM   2066  N   TYR A 264     -31.276  26.803  41.119  1.00 37.98           N  
ANISOU 2066  N   TYR A 264     2948   4072   7408   -191   -611    438       N  
ATOM   2067  CA  TYR A 264     -31.122  25.488  40.450  1.00 37.69           C  
ANISOU 2067  CA  TYR A 264     2934   3982   7404   -159   -665    458       C  
ATOM   2068  C   TYR A 264     -30.951  24.387  41.500  1.00 38.53           C  
ANISOU 2068  C   TYR A 264     3086   4067   7487   -188   -747    505       C  
ATOM   2069  O   TYR A 264     -29.833  24.223  42.034  1.00 38.58           O  
ANISOU 2069  O   TYR A 264     3086   4068   7503   -168   -795    503       O  
ATOM   2070  CB  TYR A 264     -29.941  25.545  39.491  1.00 37.23           C  
ANISOU 2070  CB  TYR A 264     2839   3909   7398    -86   -665    422       C  
ATOM   2071  CG  TYR A 264     -29.749  24.322  38.637  1.00 37.23           C  
ANISOU 2071  CG  TYR A 264     2868   3852   7424    -27   -713    423       C  
ATOM   2072  CD1 TYR A 264     -29.058  23.221  39.116  1.00 37.77           C  
ANISOU 2072  CD1 TYR A 264     2965   3882   7502      0   -797    442       C  
ATOM   2073  CD2 TYR A 264     -30.210  24.284  37.335  1.00 36.79           C  
ANISOU 2073  CD2 TYR A 264     2821   3775   7382      9   -681    400       C  
ATOM   2074  CE1 TYR A 264     -28.841  22.104  38.328  1.00 38.11           C  
ANISOU 2074  CE1 TYR A 264     3049   3863   7567     69   -850    433       C  
ATOM   2075  CE2 TYR A 264     -29.999  23.176  36.533  1.00 37.24           C  
ANISOU 2075  CE2 TYR A 264     2921   3773   7455     75   -731    391       C  
ATOM   2076  CZ  TYR A 264     -29.311  22.084  37.030  1.00 37.87           C  
ANISOU 2076  CZ  TYR A 264     3033   3811   7543    109   -816    405       C  
ATOM   2077  OH  TYR A 264     -29.100  20.985  36.255  1.00 38.67           O  
ANISOU 2077  OH  TYR A 264     3191   3844   7656    187   -874    388       O  
ATOM   2078  N   THR A 265     -32.051  23.679  41.784  1.00 38.99           N  
ANISOU 2078  N   THR A 265     3183   4113   7516   -239   -766    555       N  
ATOM   2079  CA  THR A 265     -32.114  22.446  42.608  1.00 39.77           C  
ANISOU 2079  CA  THR A 265     3337   4178   7592   -279   -855    617       C  
ATOM   2080  C   THR A 265     -31.883  21.251  41.686  1.00 40.52           C  
ANISOU 2080  C   THR A 265     3472   4184   7736   -233   -931    620       C  
ATOM   2081  O   THR A 265     -32.369  21.301  40.545  1.00 40.32           O  
ANISOU 2081  O   THR A 265     3443   4138   7738   -207   -904    597       O  
ATOM   2082  CB  THR A 265     -33.458  22.327  43.333  1.00 39.76           C  
ANISOU 2082  CB  THR A 265     3352   4219   7535   -366   -834    681       C  
ATOM   2083  OG1 THR A 265     -33.733  23.594  43.924  1.00 39.25           O  
ANISOU 2083  OG1 THR A 265     3251   4237   7424   -380   -747    656       O  
ATOM   2084  CG2 THR A 265     -33.463  21.259  44.405  1.00 40.66           C  
ANISOU 2084  CG2 THR A 265     3522   4315   7612   -424   -919    757       C  
ATOM   2085  N   GLY A 266     -31.171  20.228  42.166  1.00 41.77           N  
ANISOU 2085  N   GLY A 266     3677   4290   7903   -218  -1030    646       N  
ATOM   2086  CA  GLY A 266     -30.820  19.031  41.378  1.00 42.88           C  
ANISOU 2086  CA  GLY A 266     3872   4333   8085   -156  -1119    640       C  
ATOM   2087  C   GLY A 266     -29.342  19.008  41.050  1.00 43.82           C  
ANISOU 2087  C   GLY A 266     3964   4441   8245    -47  -1137    585       C  
ATOM   2088  O   GLY A 266     -28.684  20.043  41.228  1.00 43.61           O  
ANISOU 2088  O   GLY A 266     3864   4483   8221    -31  -1071    554       O  
ATOM   2089  N   ASN A 267     -28.838  17.869  40.577  1.00 45.38           N  
ANISOU 2089  N   ASN A 267     4217   4552   8472     27  -1228    577       N  
ATOM   2090  CA  ASN A 267     -27.392  17.657  40.327  1.00 46.84           C  
ANISOU 2090  CA  ASN A 267     4369   4729   8696    146  -1255    532       C  
ATOM   2091  C   ASN A 267     -27.166  17.326  38.851  1.00 47.38           C  
ANISOU 2091  C   ASN A 267     4450   4759   8790    262  -1241    472       C  
ATOM   2092  O   ASN A 267     -26.363  18.040  38.198  1.00 47.57           O  
ANISOU 2092  O   ASN A 267     4392   4847   8834    339  -1162    422       O  
ATOM   2093  CB  ASN A 267     -26.845  16.589  41.269  1.00 48.34           C  
ANISOU 2093  CB  ASN A 267     4618   4858   8891    151  -1383    573       C  
ATOM   2094  CG  ASN A 267     -26.776  17.093  42.692  1.00 48.84           C  
ANISOU 2094  CG  ASN A 267     4657   4978   8921     56  -1385    622       C  
ATOM   2095  OD1 ASN A 267     -27.442  16.560  43.577  1.00 49.66           O  
ANISOU 2095  OD1 ASN A 267     4827   5054   8986    -34  -1446    688       O  
ATOM   2096  ND2 ASN A 267     -26.000  18.144  42.908  1.00 49.05           N  
ANISOU 2096  ND2 ASN A 267     4593   5087   8957     72  -1320    593       N  
ATOM   2097  N   TYR A 268     -27.843  16.289  38.351  1.00 47.77           N  
ANISOU 2097  N   TYR A 268     4603   4710   8836    271  -1319    479       N  
ATOM   2098  CA  TYR A 268     -27.662  15.752  36.977  1.00 48.01           C  
ANISOU 2098  CA  TYR A 268     4680   4681   8877    392  -1331    417       C  
ATOM   2099  C   TYR A 268     -28.920  16.094  36.170  1.00 47.51           C  
ANISOU 2099  C   TYR A 268     4645   4610   8793    332  -1286    417       C  
ATOM   2100  O   TYR A 268     -29.125  17.289  35.886  1.00 47.42           O  
ANISOU 2100  O   TYR A 268     4552   4689   8775    303  -1168    402       O  
ATOM   2101  CB  TYR A 268     -27.289  14.267  37.052  1.00 48.85           C  
ANISOU 2101  CB  TYR A 268     4897   4665   8997    466  -1480    418       C  
ATOM   2102  CG  TYR A 268     -26.362  13.922  38.189  1.00 49.16           C  
ANISOU 2102  CG  TYR A 268     4916   4708   9056    478  -1546    448       C  
ATOM   2103  CD1 TYR A 268     -25.000  14.181  38.123  1.00 49.40           C  
ANISOU 2103  CD1 TYR A 268     4858   4797   9114    596  -1512    405       C  
ATOM   2104  CD2 TYR A 268     -26.853  13.340  39.346  1.00 49.45           C  
ANISOU 2104  CD2 TYR A 268     5015   4693   9080    367  -1644    526       C  
ATOM   2105  CE1 TYR A 268     -24.152  13.863  39.174  1.00 49.85           C  
ANISOU 2105  CE1 TYR A 268     4893   4853   9192    605  -1584    435       C  
ATOM   2106  CE2 TYR A 268     -26.019  13.013  40.404  1.00 50.10           C  
ANISOU 2106  CE2 TYR A 268     5087   4772   9174    374  -1714    557       C  
ATOM   2107  CZ  TYR A 268     -24.663  13.279  40.321  1.00 50.10           C  
ANISOU 2107  CZ  TYR A 268     5002   4825   9208    495  -1688    509       C  
ATOM   2108  OH  TYR A 268     -23.854  12.950  41.369  1.00 50.48           O  
ANISOU 2108  OH  TYR A 268     5039   4867   9272    501  -1769    542       O  
ATOM   2109  N   GLN A 269     -29.767  15.105  35.881  1.00 47.67           N  
ANISOU 2109  N   GLN A 269     4780   4523   8808    304  -1387    440       N  
ATOM   2110  CA  GLN A 269     -30.898  15.211  34.918  1.00 46.91           C  
ANISOU 2110  CA  GLN A 269     4725   4398   8699    266  -1373    435       C  
ATOM   2111  C   GLN A 269     -32.188  15.495  35.700  1.00 46.09           C  
ANISOU 2111  C   GLN A 269     4603   4321   8586     98  -1369    521       C  
ATOM   2112  O   GLN A 269     -33.252  15.538  35.068  1.00 45.89           O  
ANISOU 2112  O   GLN A 269     4603   4274   8557     45  -1372    536       O  
ATOM   2113  CB  GLN A 269     -30.991  13.940  34.065  1.00 47.84           C  
ANISOU 2113  CB  GLN A 269     4983   4375   8816    342  -1500    406       C  
ATOM   2114  CG  GLN A 269     -29.977  12.857  34.429  1.00 48.78           C  
ANISOU 2114  CG  GLN A 269     5169   4414   8949    442  -1609    390       C  
ATOM   2115  CD  GLN A 269     -30.618  11.535  34.758  1.00 49.78           C  
ANISOU 2115  CD  GLN A 269     5437   4395   9082    382  -1785    445       C  
ATOM   2116  OE1 GLN A 269     -30.641  11.100  35.906  1.00 50.22           O  
ANISOU 2116  OE1 GLN A 269     5503   4429   9146    301  -1856    517       O  
ATOM   2117  NE2 GLN A 269     -31.142  10.880  33.738  1.00 50.53           N  
ANISOU 2117  NE2 GLN A 269     5648   4381   9167    418  -1865    415       N  
ATOM   2118  N   CYS A 270     -32.078  15.640  37.029  1.00 45.69           N  
ANISOU 2118  N   CYS A 270     4511   4319   8528     22  -1367    576       N  
ATOM   2119  CA  CYS A 270     -33.110  16.174  37.963  1.00 44.59           C  
ANISOU 2119  CA  CYS A 270     4323   4251   8365   -121  -1324    653       C  
ATOM   2120  C   CYS A 270     -32.852  17.662  38.221  1.00 43.34           C  
ANISOU 2120  C   CYS A 270     4052   4219   8195   -119  -1181    620       C  
ATOM   2121  O   CYS A 270     -33.434  18.206  39.180  1.00 43.17           O  
ANISOU 2121  O   CYS A 270     3987   4271   8145   -211  -1135    669       O  
ATOM   2122  CB  CYS A 270     -33.091  15.439  39.298  1.00 45.07           C  
ANISOU 2122  CB  CYS A 270     4420   4291   8410   -198  -1410    733       C  
ATOM   2123  SG  CYS A 270     -33.180  13.641  39.114  1.00 46.19           S  
ANISOU 2123  SG  CYS A 270     4712   4265   8573   -196  -1606    774       S  
ATOM   2124  N   GLY A 271     -31.982  18.285  37.419  1.00 42.44           N  
ANISOU 2124  N   GLY A 271     3897   4131   8097    -16  -1116    542       N  
ATOM   2125  CA  GLY A 271     -31.831  19.749  37.370  1.00 41.33           C  
ANISOU 2125  CA  GLY A 271     3660   4092   7951    -17   -989    509       C  
ATOM   2126  C   GLY A 271     -33.173  20.420  37.132  1.00 40.41           C  
ANISOU 2126  C   GLY A 271     3521   4011   7819    -93   -930    530       C  
ATOM   2127  O   GLY A 271     -33.959  19.875  36.340  1.00 40.24           O  
ANISOU 2127  O   GLY A 271     3548   3933   7806   -102   -970    540       O  
ATOM   2128  N   HIS A 272     -33.430  21.546  37.804  1.00 39.66           N  
ANISOU 2128  N   HIS A 272     3360   4003   7705   -141   -846    536       N  
ATOM   2129  CA  HIS A 272     -34.662  22.366  37.656  1.00 39.12           C  
ANISOU 2129  CA  HIS A 272     3256   3984   7624   -198   -777    550       C  
ATOM   2130  C   HIS A 272     -34.420  23.807  38.137  1.00 38.39           C  
ANISOU 2130  C   HIS A 272     3096   3975   7514   -198   -682    519       C  
ATOM   2131  O   HIS A 272     -34.074  23.996  39.327  1.00 38.55           O  
ANISOU 2131  O   HIS A 272     3108   4033   7505   -227   -681    534       O  
ATOM   2132  CB  HIS A 272     -35.838  21.702  38.383  1.00 39.57           C  
ANISOU 2132  CB  HIS A 272     3333   4042   7660   -294   -819    632       C  
ATOM   2133  CG  HIS A 272     -37.018  22.598  38.517  1.00 39.37           C  
ANISOU 2133  CG  HIS A 272     3249   4091   7616   -345   -740    652       C  
ATOM   2134  ND1 HIS A 272     -37.706  23.067  37.418  1.00 39.13           N  
ANISOU 2134  ND1 HIS A 272     3199   4057   7611   -330   -706    630       N  
ATOM   2135  CD2 HIS A 272     -37.611  23.137  39.605  1.00 39.57           C  
ANISOU 2135  CD2 HIS A 272     3233   4202   7599   -399   -686    687       C  
ATOM   2136  CE1 HIS A 272     -38.689  23.847  37.826  1.00 39.21           C  
ANISOU 2136  CE1 HIS A 272     3150   4143   7602   -372   -638    653       C  
ATOM   2137  NE2 HIS A 272     -38.647  23.910  39.165  1.00 39.44           N  
ANISOU 2137  NE2 HIS A 272     3165   4232   7586   -410   -619    685       N  
ATOM   2138  N   TYR A 273     -34.639  24.781  37.247  1.00 37.42           N  
ANISOU 2138  N   TYR A 273     2940   3872   7405   -171   -614    478       N  
ATOM   2139  CA  TYR A 273     -34.500  26.234  37.513  1.00 36.75           C  
ANISOU 2139  CA  TYR A 273     2805   3849   7310   -170   -534    444       C  
ATOM   2140  C   TYR A 273     -35.797  26.825  38.069  1.00 36.51           C  
ANISOU 2140  C   TYR A 273     2754   3869   7249   -222   -489    468       C  
ATOM   2141  O   TYR A 273     -36.872  26.558  37.507  1.00 36.84           O  
ANISOU 2141  O   TYR A 273     2793   3901   7300   -242   -489    493       O  
ATOM   2142  CB  TYR A 273     -34.207  27.004  36.227  1.00 36.52           C  
ANISOU 2142  CB  TYR A 273     2755   3811   7308   -120   -489    397       C  
ATOM   2143  CG  TYR A 273     -32.783  26.951  35.741  1.00 36.58           C  
ANISOU 2143  CG  TYR A 273     2751   3808   7337    -60   -496    367       C  
ATOM   2144  CD1 TYR A 273     -32.436  26.161  34.660  1.00 36.67           C  
ANISOU 2144  CD1 TYR A 273     2790   3777   7366     -1   -523    354       C  
ATOM   2145  CD2 TYR A 273     -31.794  27.725  36.327  1.00 36.40           C  
ANISOU 2145  CD2 TYR A 273     2690   3823   7318    -58   -477    352       C  
ATOM   2146  CE1 TYR A 273     -31.136  26.120  34.187  1.00 36.92           C  
ANISOU 2146  CE1 TYR A 273     2797   3816   7413     65   -516    329       C  
ATOM   2147  CE2 TYR A 273     -30.489  27.697  35.863  1.00 36.60           C  
ANISOU 2147  CE2 TYR A 273     2683   3852   7368     -7   -480    336       C  
ATOM   2148  CZ  TYR A 273     -30.158  26.886  34.793  1.00 36.77           C  
ANISOU 2148  CZ  TYR A 273     2721   3846   7405     59   -492    325       C  
ATOM   2149  OH  TYR A 273     -28.888  26.840  34.306  1.00 37.09           O  
ANISOU 2149  OH  TYR A 273     2718   3907   7465    122   -483    311       O  
ATOM   2150  N   LYS A 274     -35.685  27.636  39.120  1.00 36.22           N  
ANISOU 2150  N   LYS A 274     2700   3884   7175   -236   -452    458       N  
ATOM   2151  CA  LYS A 274     -36.701  28.649  39.508  1.00 35.86           C  
ANISOU 2151  CA  LYS A 274     2628   3897   7099   -250   -385    452       C  
ATOM   2152  C   LYS A 274     -36.107  30.021  39.186  1.00 35.39           C  
ANISOU 2152  C   LYS A 274     2557   3839   7051   -211   -344    389       C  
ATOM   2153  O   LYS A 274     -35.003  30.051  38.628  1.00 35.35           O  
ANISOU 2153  O   LYS A 274     2552   3798   7079   -186   -366    365       O  
ATOM   2154  CB  LYS A 274     -37.082  28.498  40.981  1.00 36.21           C  
ANISOU 2154  CB  LYS A 274     2679   3999   7077   -289   -378    487       C  
ATOM   2155  CG  LYS A 274     -37.762  27.182  41.321  1.00 36.64           C  
ANISOU 2155  CG  LYS A 274     2743   4058   7119   -345   -420    567       C  
ATOM   2156  CD  LYS A 274     -38.397  27.167  42.692  1.00 37.21           C  
ANISOU 2156  CD  LYS A 274     2811   4210   7115   -387   -391    612       C  
ATOM   2157  CE  LYS A 274     -38.649  25.767  43.201  1.00 37.73           C  
ANISOU 2157  CE  LYS A 274     2901   4269   7166   -455   -456    701       C  
ATOM   2158  NZ  LYS A 274     -39.300  25.802  44.527  1.00 38.56           N  
ANISOU 2158  NZ  LYS A 274     2996   4468   7183   -498   -415    753       N  
ATOM   2159  N   HIS A 275     -36.821  31.105  39.488  1.00 35.40           N  
ANISOU 2159  N   HIS A 275     2545   3878   7027   -203   -291    366       N  
ATOM   2160  CA  HIS A 275     -36.401  32.499  39.187  1.00 35.15           C  
ANISOU 2160  CA  HIS A 275     2514   3835   7006   -172   -264    309       C  
ATOM   2161  C   HIS A 275     -36.876  33.435  40.301  1.00 35.33           C  
ANISOU 2161  C   HIS A 275     2552   3901   6969   -163   -231    283       C  
ATOM   2162  O   HIS A 275     -38.092  33.526  40.508  1.00 35.47           O  
ANISOU 2162  O   HIS A 275     2551   3964   6961   -155   -188    295       O  
ATOM   2163  CB  HIS A 275     -36.926  32.938  37.817  1.00 34.84           C  
ANISOU 2163  CB  HIS A 275     2455   3770   7012   -150   -241    297       C  
ATOM   2164  CG  HIS A 275     -36.624  34.365  37.496  1.00 34.83           C  
ANISOU 2164  CG  HIS A 275     2460   3751   7022   -127   -221    250       C  
ATOM   2165  ND1 HIS A 275     -35.469  34.747  36.837  1.00 34.55           N  
ANISOU 2165  ND1 HIS A 275     2427   3680   7021   -125   -239    236       N  
ATOM   2166  CD2 HIS A 275     -37.314  35.499  37.741  1.00 34.86           C  
ANISOU 2166  CD2 HIS A 275     2471   3765   7008   -104   -191    218       C  
ATOM   2167  CE1 HIS A 275     -35.474  36.053  36.679  1.00 34.46           C  
ANISOU 2167  CE1 HIS A 275     2427   3652   7015   -116   -228    203       C  
ATOM   2168  NE2 HIS A 275     -36.589  36.537  37.229  1.00 34.70           N  
ANISOU 2168  NE2 HIS A 275     2467   3703   7013    -97   -201    186       N  
ATOM   2169  N   ILE A 276     -35.938  34.091  40.983  1.00 35.46           N  
ANISOU 2169  N   ILE A 276     2600   3907   6964   -162   -253    248       N  
ATOM   2170  CA  ILE A 276     -36.211  35.011  42.122  1.00 36.10           C  
ANISOU 2170  CA  ILE A 276     2721   4017   6976   -145   -235    211       C  
ATOM   2171  C   ILE A 276     -35.953  36.437  41.645  1.00 36.10           C  
ANISOU 2171  C   ILE A 276     2741   3972   7000   -117   -236    154       C  
ATOM   2172  O   ILE A 276     -34.908  36.674  41.044  1.00 35.62           O  
ANISOU 2172  O   ILE A 276     2678   3865   6992   -136   -275    151       O  
ATOM   2173  CB  ILE A 276     -35.362  34.659  43.356  1.00 36.61           C  
ANISOU 2173  CB  ILE A 276     2827   4093   6991   -171   -280    216       C  
ATOM   2174  CG1 ILE A 276     -35.864  33.391  44.052  1.00 36.87           C  
ANISOU 2174  CG1 ILE A 276     2854   4176   6979   -199   -276    275       C  
ATOM   2175  CG2 ILE A 276     -35.302  35.840  44.312  1.00 37.31           C  
ANISOU 2175  CG2 ILE A 276     2977   4185   7013   -147   -282    159       C  
ATOM   2176  CD1 ILE A 276     -35.397  32.111  43.408  1.00 36.51           C  
ANISOU 2176  CD1 ILE A 276     2781   4099   6992   -229   -319    326       C  
ATOM   2177  N   THR A 277     -36.887  37.341  41.932  1.00 36.80           N  
ANISOU 2177  N   THR A 277     2850   4080   7051    -72   -197    116       N  
ATOM   2178  CA  THR A 277     -36.870  38.749  41.477  1.00 37.21           C  
ANISOU 2178  CA  THR A 277     2933   4079   7123    -39   -204     62       C  
ATOM   2179  C   THR A 277     -37.134  39.653  42.686  1.00 38.38           C  
ANISOU 2179  C   THR A 277     3152   4239   7189      4   -203      4       C  
ATOM   2180  O   THR A 277     -37.982  39.303  43.509  1.00 39.31           O  
ANISOU 2180  O   THR A 277     3268   4430   7237     35   -154      7       O  
ATOM   2181  CB  THR A 277     -37.849  38.918  40.312  1.00 36.89           C  
ANISOU 2181  CB  THR A 277     2848   4035   7130    -11   -164     70       C  
ATOM   2182  OG1 THR A 277     -37.425  40.064  39.579  1.00 36.88           O  
ANISOU 2182  OG1 THR A 277     2877   3964   7172     -3   -194     37       O  
ATOM   2183  CG2 THR A 277     -39.290  39.060  40.752  1.00 37.39           C  
ANISOU 2183  CG2 THR A 277     2893   4162   7148     44   -104     61       C  
ATOM   2184  N   SER A 278     -36.400  40.756  42.802  1.00 39.08           N  
ANISOU 2184  N   SER A 278     3307   4258   7282      6   -259    -43       N  
ATOM   2185  CA  SER A 278     -36.494  41.710  43.931  1.00 40.38           C  
ANISOU 2185  CA  SER A 278     3566   4411   7364     52   -280   -111       C  
ATOM   2186  C   SER A 278     -37.366  42.882  43.492  1.00 40.98           C  
ANISOU 2186  C   SER A 278     3670   4453   7445    127   -260   -165       C  
ATOM   2187  O   SER A 278     -36.874  43.704  42.698  1.00 40.86           O  
ANISOU 2187  O   SER A 278     3677   4353   7494    108   -312   -177       O  
ATOM   2188  CB  SER A 278     -35.133  42.167  44.383  1.00 40.82           C  
ANISOU 2188  CB  SER A 278     3686   4399   7424      1   -376   -126       C  
ATOM   2189  OG  SER A 278     -35.219  42.854  45.624  1.00 42.10           O  
ANISOU 2189  OG  SER A 278     3952   4553   7489     44   -404   -191       O  
ATOM   2190  N   LYS A 279     -38.616  42.907  43.965  1.00 41.80           N  
ANISOU 2190  N   LYS A 279     3766   4629   7487    208   -187   -188       N  
ATOM   2191  CA  LYS A 279     -39.619  43.978  43.718  1.00 42.39           C  
ANISOU 2191  CA  LYS A 279     3864   4687   7554    306   -160   -246       C  
ATOM   2192  C   LYS A 279     -40.004  44.548  45.089  1.00 43.60           C  
ANISOU 2192  C   LYS A 279     4104   4874   7585    394   -144   -319       C  
ATOM   2193  O   LYS A 279     -39.072  44.729  45.892  1.00 44.14           O  
ANISOU 2193  O   LYS A 279     4261   4903   7607    364   -209   -345       O  
ATOM   2194  CB  LYS A 279     -40.713  43.401  42.817  1.00 41.95           C  
ANISOU 2194  CB  LYS A 279     3696   4693   7549    322    -88   -196       C  
ATOM   2195  CG  LYS A 279     -40.262  43.257  41.368  1.00 41.16           C  
ANISOU 2195  CG  LYS A 279     3552   4527   7558    256   -123   -151       C  
ATOM   2196  CD  LYS A 279     -40.795  42.043  40.638  1.00 40.96           C  
ANISOU 2196  CD  LYS A 279     3421   4562   7577    217    -78    -75       C  
ATOM   2197  CE  LYS A 279     -42.052  42.312  39.831  1.00 41.53           C  
ANISOU 2197  CE  LYS A 279     3438   4653   7688    272    -39    -69       C  
ATOM   2198  NZ  LYS A 279     -42.212  41.346  38.717  1.00 40.83           N  
ANISOU 2198  NZ  LYS A 279     3274   4571   7667    214    -37      1       N  
ATOM   2199  N   GLU A 280     -41.274  44.848  45.375  1.00 44.23           N  
ANISOU 2199  N   GLU A 280     4167   5026   7612    503    -67   -351       N  
ATOM   2200  CA  GLU A 280     -41.627  45.491  46.671  1.00 45.86           C  
ANISOU 2200  CA  GLU A 280     4469   5266   7688    609    -47   -433       C  
ATOM   2201  C   GLU A 280     -41.065  44.621  47.806  1.00 45.98           C  
ANISOU 2201  C   GLU A 280     4508   5345   7615    554    -43   -404       C  
ATOM   2202  O   GLU A 280     -40.513  45.198  48.766  1.00 46.80           O  
ANISOU 2202  O   GLU A 280     4740   5409   7632    581    -98   -471       O  
ATOM   2203  CB  GLU A 280     -43.131  45.762  46.788  1.00 47.03           C  
ANISOU 2203  CB  GLU A 280     4562   5513   7792    741     55   -458       C  
ATOM   2204  CG  GLU A 280     -43.982  44.564  47.178  1.00 47.36           C  
ANISOU 2204  CG  GLU A 280     4480   5722   7791    731    167   -378       C  
ATOM   2205  CD  GLU A 280     -44.536  43.754  46.019  1.00 46.59           C  
ANISOU 2205  CD  GLU A 280     4236   5660   7806    668    201   -284       C  
ATOM   2206  OE1 GLU A 280     -43.845  43.637  44.982  1.00 45.20           O  
ANISOU 2206  OE1 GLU A 280     4052   5385   7736    583    132   -256       O  
ATOM   2207  OE2 GLU A 280     -45.685  43.271  46.149  1.00 47.54           O  
ANISOU 2207  OE2 GLU A 280     4248   5909   7903    707    294   -238       O  
ATOM   2208  N   THR A 281     -41.202  43.293  47.669  1.00 45.20           N  
ANISOU 2208  N   THR A 281     4300   5333   7539    477      6   -309       N  
ATOM   2209  CA  THR A 281     -40.555  42.224  48.484  1.00 44.79           C  
ANISOU 2209  CA  THR A 281     4252   5329   7435    395     -4   -254       C  
ATOM   2210  C   THR A 281     -39.891  41.254  47.496  1.00 43.03           C  
ANISOU 2210  C   THR A 281     3948   5069   7332    278    -42   -170       C  
ATOM   2211  O   THR A 281     -39.568  41.706  46.386  1.00 42.18           O  
ANISOU 2211  O   THR A 281     3824   4875   7326    260    -83   -177       O  
ATOM   2212  CB  THR A 281     -41.572  41.568  49.432  1.00 45.78           C  
ANISOU 2212  CB  THR A 281     4335   5610   7448    438    101   -221       C  
ATOM   2213  OG1 THR A 281     -40.874  40.754  50.375  1.00 45.90           O  
ANISOU 2213  OG1 THR A 281     4391   5655   7394    368     73   -182       O  
ATOM   2214  CG2 THR A 281     -42.613  40.736  48.714  1.00 45.34           C  
ANISOU 2214  CG2 THR A 281     4130   5643   7452    419    182   -135       C  
ATOM   2215  N   LEU A 282     -39.708  39.982  47.859  1.00 42.61           N  
ANISOU 2215  N   LEU A 282     3849   5076   7263    206    -31    -93       N  
ATOM   2216  CA  LEU A 282     -39.123  38.945  46.962  1.00 41.48           C  
ANISOU 2216  CA  LEU A 282     3634   4900   7223    111    -67    -17       C  
ATOM   2217  C   LEU A 282     -40.216  38.014  46.419  1.00 41.18           C  
ANISOU 2217  C   LEU A 282     3487   4940   7217     98      2     57       C  
ATOM   2218  O   LEU A 282     -41.126  37.648  47.190  1.00 42.04           O  
ANISOU 2218  O   LEU A 282     3570   5156   7246    121     70     85       O  
ATOM   2219  CB  LEU A 282     -38.075  38.147  47.741  1.00 41.58           C  
ANISOU 2219  CB  LEU A 282     3684   4907   7204     40   -127     15       C  
ATOM   2220  CG  LEU A 282     -36.782  38.892  48.058  1.00 41.72           C  
ANISOU 2220  CG  LEU A 282     3792   4835   7224     24   -222    -37       C  
ATOM   2221  CD1 LEU A 282     -35.920  38.067  49.000  1.00 42.01           C  
ANISOU 2221  CD1 LEU A 282     3863   4883   7215    -34   -278      0       C  
ATOM   2222  CD2 LEU A 282     -36.022  39.239  46.784  1.00 40.78           C  
ANISOU 2222  CD2 LEU A 282     3640   4623   7230    -10   -274    -36       C  
ATOM   2223  N   TYR A 283     -40.108  37.629  45.142  1.00 40.20           N  
ANISOU 2223  N   TYR A 283     3303   4766   7202     58    -18     92       N  
ATOM   2224  CA  TYR A 283     -41.013  36.665  44.458  1.00 40.00           C  
ANISOU 2224  CA  TYR A 283     3183   4790   7224     29     19    168       C  
ATOM   2225  C   TYR A 283     -40.194  35.523  43.839  1.00 39.09           C  
ANISOU 2225  C   TYR A 283     3052   4624   7177    -51    -41    224       C  
ATOM   2226  O   TYR A 283     -39.234  35.803  43.096  1.00 38.28           O  
ANISOU 2226  O   TYR A 283     2970   4436   7136    -62    -92    198       O  
ATOM   2227  CB  TYR A 283     -41.839  37.356  43.369  1.00 39.77           C  
ANISOU 2227  CB  TYR A 283     3108   4744   7258     77     47    148       C  
ATOM   2228  CG  TYR A 283     -42.846  38.369  43.851  1.00 40.63           C  
ANISOU 2228  CG  TYR A 283     3215   4910   7310    173    111     98       C  
ATOM   2229  CD1 TYR A 283     -42.447  39.587  44.369  1.00 41.00           C  
ANISOU 2229  CD1 TYR A 283     3351   4916   7311    240     96      9       C  
ATOM   2230  CD2 TYR A 283     -44.203  38.132  43.745  1.00 41.29           C  
ANISOU 2230  CD2 TYR A 283     3208   5088   7392    203    179    141       C  
ATOM   2231  CE1 TYR A 283     -43.365  40.532  44.791  1.00 42.02           C  
ANISOU 2231  CE1 TYR A 283     3490   5091   7384    347    151    -46       C  
ATOM   2232  CE2 TYR A 283     -45.137  39.066  44.161  1.00 42.34           C  
ANISOU 2232  CE2 TYR A 283     3329   5282   7474    309    243     93       C  
ATOM   2233  CZ  TYR A 283     -44.718  40.275  44.682  1.00 42.65           C  
ANISOU 2233  CZ  TYR A 283     3468   5274   7460    389    231     -6       C  
ATOM   2234  OH  TYR A 283     -45.638  41.191  45.092  1.00 43.51           O  
ANISOU 2234  OH  TYR A 283     3575   5439   7515    510    291    -62       O  
ATOM   2235  N   CYS A 284     -40.584  34.278  44.129  1.00 39.14           N  
ANISOU 2235  N   CYS A 284     3022   4681   7169   -103    -37    302       N  
ATOM   2236  CA  CYS A 284     -40.062  33.041  43.492  1.00 38.77           C  
ANISOU 2236  CA  CYS A 284     2959   4585   7184   -168    -96    360       C  
ATOM   2237  C   CYS A 284     -41.051  32.575  42.417  1.00 38.45           C  
ANISOU 2237  C   CYS A 284     2853   4548   7207   -181    -83    406       C  
ATOM   2238  O   CYS A 284     -42.146  32.106  42.773  1.00 39.30           O  
ANISOU 2238  O   CYS A 284     2911   4732   7287   -201    -47    465       O  
ATOM   2239  CB  CYS A 284     -39.836  31.940  44.527  1.00 39.45           C  
ANISOU 2239  CB  CYS A 284     3065   4708   7215   -223   -122    422       C  
ATOM   2240  SG  CYS A 284     -38.916  30.511  43.887  1.00 38.94           S  
ANISOU 2240  SG  CYS A 284     3011   4561   7221   -283   -216    473       S  
ATOM   2241  N   ILE A 285     -40.687  32.708  41.145  1.00 37.58           N  
ANISOU 2241  N   ILE A 285     2740   4362   7174   -173   -113    384       N  
ATOM   2242  CA  ILE A 285     -41.557  32.309  40.006  1.00 37.48           C  
ANISOU 2242  CA  ILE A 285     2680   4337   7222   -184   -117    421       C  
ATOM   2243  C   ILE A 285     -41.111  30.916  39.556  1.00 37.75           C  
ANISOU 2243  C   ILE A 285     2730   4321   7291   -238   -186    472       C  
ATOM   2244  O   ILE A 285     -40.032  30.824  38.919  1.00 37.15           O  
ANISOU 2244  O   ILE A 285     2690   4174   7249   -227   -226    441       O  
ATOM   2245  CB  ILE A 285     -41.502  33.366  38.886  1.00 36.78           C  
ANISOU 2245  CB  ILE A 285     2593   4196   7183   -136   -109    364       C  
ATOM   2246  CG1 ILE A 285     -42.021  34.719  39.380  1.00 36.96           C  
ANISOU 2246  CG1 ILE A 285     2611   4258   7171    -75    -54    312       C  
ATOM   2247  CG2 ILE A 285     -42.245  32.894  37.645  1.00 36.62           C  
ANISOU 2247  CG2 ILE A 285     2538   4150   7222   -150   -129    400       C  
ATOM   2248  CD1 ILE A 285     -41.817  35.851  38.401  1.00 36.55           C  
ANISOU 2248  CD1 ILE A 285     2578   4143   7163    -32    -59    257       C  
ATOM   2249  N   ASP A 286     -41.903  29.889  39.910  1.00 38.75           N  
ANISOU 2249  N   ASP A 286     2830   4486   7407   -293   -201    551       N  
ATOM   2250  CA  ASP A 286     -41.692  28.456  39.558  1.00 39.00           C  
ANISOU 2250  CA  ASP A 286     2887   4463   7468   -349   -281    610       C  
ATOM   2251  C   ASP A 286     -42.603  28.106  38.380  1.00 38.87           C  
ANISOU 2251  C   ASP A 286     2841   4416   7509   -366   -309    642       C  
ATOM   2252  O   ASP A 286     -43.484  27.239  38.542  1.00 39.19           O  
ANISOU 2252  O   ASP A 286     2854   4480   7554   -430   -339    725       O  
ATOM   2253  CB  ASP A 286     -41.946  27.529  40.753  1.00 40.08           C  
ANISOU 2253  CB  ASP A 286     3024   4649   7554   -413   -299    687       C  
ATOM   2254  CG  ASP A 286     -41.418  26.111  40.569  1.00 40.46           C  
ANISOU 2254  CG  ASP A 286     3125   4620   7628   -462   -399    735       C  
ATOM   2255  OD1 ASP A 286     -40.809  25.835  39.510  1.00 40.02           O  
ANISOU 2255  OD1 ASP A 286     3106   4475   7624   -433   -450    699       O  
ATOM   2256  OD2 ASP A 286     -41.606  25.288  41.496  1.00 41.46           O  
ANISOU 2256  OD2 ASP A 286     3261   4775   7716   -524   -428    808       O  
ATOM   2257  N   GLY A 287     -42.377  28.767  37.244  1.00 38.60           N  
ANISOU 2257  N   GLY A 287     2817   4331   7515   -317   -305    584       N  
ATOM   2258  CA  GLY A 287     -43.192  28.639  36.025  1.00 39.10           C  
ANISOU 2258  CA  GLY A 287     2864   4362   7630   -322   -333    602       C  
ATOM   2259  C   GLY A 287     -44.488  29.404  36.185  1.00 40.14           C  
ANISOU 2259  C   GLY A 287     2916   4573   7763   -317   -275    622       C  
ATOM   2260  O   GLY A 287     -44.418  30.641  36.314  1.00 40.89           O  
ANISOU 2260  O   GLY A 287     2995   4695   7843   -258   -212    563       O  
ATOM   2261  N   ALA A 288     -45.621  28.701  36.240  1.00 41.03           N  
ANISOU 2261  N   ALA A 288     2975   4723   7891   -377   -300    707       N  
ATOM   2262  CA  ALA A 288     -46.961  29.291  36.474  1.00 41.84           C  
ANISOU 2262  CA  ALA A 288     2977   4922   7997   -373   -243    743       C  
ATOM   2263  C   ALA A 288     -47.209  29.483  37.974  1.00 42.66           C  
ANISOU 2263  C   ALA A 288     3034   5141   8031   -375   -166    768       C  
ATOM   2264  O   ALA A 288     -48.322  29.876  38.304  1.00 43.55           O  
ANISOU 2264  O   ALA A 288     3054   5353   8137   -365   -110    806       O  
ATOM   2265  CB  ALA A 288     -48.035  28.424  35.857  1.00 42.14           C  
ANISOU 2265  CB  ALA A 288     2969   4955   8086   -446   -310    835       C  
ATOM   2266  N   LEU A 289     -46.217  29.251  38.841  1.00 42.86           N  
ANISOU 2266  N   LEU A 289     3120   5159   8004   -378   -163    747       N  
ATOM   2267  CA  LEU A 289     -46.432  29.115  40.308  1.00 44.13           C  
ANISOU 2267  CA  LEU A 289     3255   5426   8086   -399   -109    789       C  
ATOM   2268  C   LEU A 289     -45.601  30.147  41.076  1.00 44.37           C  
ANISOU 2268  C   LEU A 289     3333   5470   8053   -323    -51    697       C  
ATOM   2269  O   LEU A 289     -44.372  29.975  41.152  1.00 44.88           O  
ANISOU 2269  O   LEU A 289     3477   5461   8112   -323    -94    656       O  
ATOM   2270  CB  LEU A 289     -46.065  27.687  40.723  1.00 44.49           C  
ANISOU 2270  CB  LEU A 289     3339   5441   8122   -492   -184    868       C  
ATOM   2271  CG  LEU A 289     -47.115  26.621  40.407  1.00 45.10           C  
ANISOU 2271  CG  LEU A 289     3361   5533   8239   -587   -240    986       C  
ATOM   2272  CD1 LEU A 289     -46.542  25.221  40.583  1.00 45.21           C  
ANISOU 2272  CD1 LEU A 289     3448   5470   8257   -671   -345   1047       C  
ATOM   2273  CD2 LEU A 289     -48.348  26.805  41.274  1.00 46.24           C  
ANISOU 2273  CD2 LEU A 289     3394   5835   8341   -612   -157   1067       C  
ATOM   2274  N   LEU A 290     -46.272  31.137  41.670  1.00 45.03           N  
ANISOU 2274  N   LEU A 290     3370   5648   8089   -261     36    670       N  
ATOM   2275  CA  LEU A 290     -45.667  32.309  42.355  1.00 45.09           C  
ANISOU 2275  CA  LEU A 290     3431   5664   8034   -177     85    573       C  
ATOM   2276  C   LEU A 290     -45.560  32.030  43.855  1.00 45.97           C  
ANISOU 2276  C   LEU A 290     3562   5863   8040   -192    123    599       C  
ATOM   2277  O   LEU A 290     -46.305  31.184  44.347  1.00 46.27           O  
ANISOU 2277  O   LEU A 290     3542   5987   8051   -252    141    696       O  
ATOM   2278  CB  LEU A 290     -46.555  33.530  42.095  1.00 45.81           C  
ANISOU 2278  CB  LEU A 290     3471   5801   8130    -86    152    525       C  
ATOM   2279  CG  LEU A 290     -46.007  34.878  42.563  1.00 45.89           C  
ANISOU 2279  CG  LEU A 290     3550   5792   8091      7    183    414       C  
ATOM   2280  CD1 LEU A 290     -44.698  35.201  41.862  1.00 44.99           C  
ANISOU 2280  CD1 LEU A 290     3523   5545   8026      1    113    352       C  
ATOM   2281  CD2 LEU A 290     -47.024  35.982  42.329  1.00 46.50           C  
ANISOU 2281  CD2 LEU A 290     3577   5916   8174    105    242    373       C  
ATOM   2282  N   THR A 291     -44.666  32.747  44.541  1.00 46.52           N  
ANISOU 2282  N   THR A 291     3713   5910   8051   -144    129    519       N  
ATOM   2283  CA  THR A 291     -44.398  32.642  46.001  1.00 47.55           C  
ANISOU 2283  CA  THR A 291     3888   6111   8066   -146    157    525       C  
ATOM   2284  C   THR A 291     -43.783  33.960  46.479  1.00 47.71           C  
ANISOU 2284  C   THR A 291     3990   6105   8033    -57    172    410       C  
ATOM   2285  O   THR A 291     -43.186  34.650  45.649  1.00 47.06           O  
ANISOU 2285  O   THR A 291     3938   5922   8018    -27    133    342       O  
ATOM   2286  CB  THR A 291     -43.538  31.403  46.277  1.00 47.32           C  
ANISOU 2286  CB  THR A 291     3904   6034   8040   -239     77    585       C  
ATOM   2287  OG1 THR A 291     -44.432  30.292  46.216  1.00 47.80           O  
ANISOU 2287  OG1 THR A 291     3893   6152   8115   -316     78    701       O  
ATOM   2288  CG2 THR A 291     -42.822  31.425  47.611  1.00 48.01           C  
ANISOU 2288  CG2 THR A 291     4070   6147   8022   -240     73    568       C  
ATOM   2289  N   LYS A 292     -43.953  34.302  47.757  1.00 49.21           N  
ANISOU 2289  N   LYS A 292     4215   6381   8102    -17    225    392       N  
ATOM   2290  CA  LYS A 292     -43.470  35.576  48.349  1.00 50.27           C  
ANISOU 2290  CA  LYS A 292     4442   6490   8168     73    232    279       C  
ATOM   2291  C   LYS A 292     -42.788  35.298  49.688  1.00 51.91           C  
ANISOU 2291  C   LYS A 292     4737   6723   8260     51    213    279       C  
ATOM   2292  O   LYS A 292     -43.307  34.451  50.448  1.00 52.35           O  
ANISOU 2292  O   LYS A 292     4761   6886   8244      9    255    362       O  
ATOM   2293  CB  LYS A 292     -44.624  36.557  48.561  1.00 51.26           C  
ANISOU 2293  CB  LYS A 292     4531   6702   8240    186    328    233       C  
ATOM   2294  CG  LYS A 292     -45.158  37.205  47.294  1.00 50.87           C  
ANISOU 2294  CG  LYS A 292     4424   6604   8297    232    332    204       C  
ATOM   2295  CD  LYS A 292     -46.194  38.262  47.574  1.00 52.13           C  
ANISOU 2295  CD  LYS A 292     4561   6842   8404    363    416    146       C  
ATOM   2296  CE  LYS A 292     -47.553  37.685  47.915  1.00 53.28           C  
ANISOU 2296  CE  LYS A 292     4578   7155   8511    372    516    234       C  
ATOM   2297  NZ  LYS A 292     -48.428  38.711  48.527  1.00 54.68           N  
ANISOU 2297  NZ  LYS A 292     4744   7430   8599    521    610    168       N  
ATOM   2298  N   SER A 293     -41.687  36.015  49.952  1.00 53.05           N  
ANISOU 2298  N   SER A 293     4988   6777   8391     73    147    195       N  
ATOM   2299  CA  SER A 293     -40.874  35.955  51.197  1.00 54.62           C  
ANISOU 2299  CA  SER A 293     5292   6977   8483     58    106    177       C  
ATOM   2300  C   SER A 293     -40.218  37.318  51.463  1.00 55.61           C  
ANISOU 2300  C   SER A 293     5528   7023   8577    130     62     58       C  
ATOM   2301  O   SER A 293     -40.192  38.146  50.538  1.00 55.06           O  
ANISOU 2301  O   SER A 293     5449   6879   8592    168     48      3       O  
ATOM   2302  CB  SER A 293     -39.843  34.855  51.096  1.00 54.42           C  
ANISOU 2302  CB  SER A 293     5274   6890   8513    -46     15    241       C  
ATOM   2303  OG  SER A 293     -39.095  34.957  49.887  1.00 53.38           O  
ANISOU 2303  OG  SER A 293     5120   6642   8517    -70    -50    222       O  
ATOM   2304  N   SER A 294     -39.712  37.537  52.682  1.00 57.66           N  
ANISOU 2304  N   SER A 294     5896   7293   8716    143     33     22       N  
ATOM   2305  CA  SER A 294     -38.881  38.714  53.064  1.00 58.97           C  
ANISOU 2305  CA  SER A 294     6192   7365   8849    189    -43    -83       C  
ATOM   2306  C   SER A 294     -37.421  38.507  52.621  1.00 59.49           C  
ANISOU 2306  C   SER A 294     6278   7307   9018     98   -171    -71       C  
ATOM   2307  O   SER A 294     -36.803  39.488  52.155  1.00 59.47           O  
ANISOU 2307  O   SER A 294     6320   7199   9073    113   -237   -137       O  
ATOM   2308  CB  SER A 294     -38.966  38.999  54.542  1.00 59.99           C  
ANISOU 2308  CB  SER A 294     6435   7556   8801    241    -29   -125       C  
ATOM   2309  OG  SER A 294     -39.837  40.086  54.790  1.00 60.60           O  
ANISOU 2309  OG  SER A 294     6555   7672   8798    372     40   -212       O  
ATOM   2310  N   GLU A 295     -36.887  37.290  52.795  1.00 60.49           N  
ANISOU 2310  N   GLU A 295     6371   7446   9163     10   -207     11       N  
ATOM   2311  CA  GLU A 295     -35.528  36.877  52.343  1.00 60.64           C  
ANISOU 2311  CA  GLU A 295     6383   7369   9287    -70   -318     38       C  
ATOM   2312  C   GLU A 295     -35.664  35.553  51.585  1.00 58.82           C  
ANISOU 2312  C   GLU A 295     6044   7159   9144   -130   -301    133       C  
ATOM   2313  O   GLU A 295     -36.720  34.912  51.728  1.00 58.30           O  
ANISOU 2313  O   GLU A 295     5931   7182   9036   -128   -221    185       O  
ATOM   2314  CB  GLU A 295     -34.551  36.775  53.522  1.00 63.12           C  
ANISOU 2314  CB  GLU A 295     6798   7662   9521   -103   -411     31       C  
ATOM   2315  CG  GLU A 295     -35.204  36.462  54.866  1.00 65.92           C  
ANISOU 2315  CG  GLU A 295     7219   8119   9708    -80   -361     44       C  
ATOM   2316  CD  GLU A 295     -34.242  36.244  56.032  1.00 68.11           C  
ANISOU 2316  CD  GLU A 295     7601   8375   9901   -120   -462     47       C  
ATOM   2317  OE1 GLU A 295     -34.416  35.243  56.771  1.00 69.32           O  
ANISOU 2317  OE1 GLU A 295     7760   8599   9979   -159   -449    118       O  
ATOM   2318  OE2 GLU A 295     -33.321  37.076  56.211  1.00 69.11           O  
ANISOU 2318  OE2 GLU A 295     7806   8412  10038   -120   -561    -16       O  
ATOM   2319  N   TYR A 296     -34.660  35.185  50.783  1.00 57.26           N  
ANISOU 2319  N   TYR A 296     5807   6883   9064   -179   -373    154       N  
ATOM   2320  CA  TYR A 296     -34.600  33.877  50.077  1.00 56.60           C  
ANISOU 2320  CA  TYR A 296     5643   6799   9061   -229   -380    235       C  
ATOM   2321  C   TYR A 296     -33.198  33.281  50.219  1.00 56.56           C  
ANISOU 2321  C   TYR A 296     5650   6735   9102   -278   -486    260       C  
ATOM   2322  O   TYR A 296     -32.207  33.993  49.977  1.00 56.66           O  
ANISOU 2322  O   TYR A 296     5675   6685   9165   -278   -546    219       O  
ATOM   2323  CB  TYR A 296     -34.988  33.990  48.600  1.00 55.72           C  
ANISOU 2323  CB  TYR A 296     5451   6659   9059   -214   -341    234       C  
ATOM   2324  CG  TYR A 296     -35.294  32.661  47.954  1.00 55.64           C  
ANISOU 2324  CG  TYR A 296     5375   6657   9106   -251   -336    311       C  
ATOM   2325  CD1 TYR A 296     -36.566  32.110  48.026  1.00 56.40           C  
ANISOU 2325  CD1 TYR A 296     5435   6824   9167   -257   -270    361       C  
ATOM   2326  CD2 TYR A 296     -34.310  31.932  47.301  1.00 55.25           C  
ANISOU 2326  CD2 TYR A 296     5302   6547   9143   -279   -403    337       C  
ATOM   2327  CE1 TYR A 296     -36.858  30.881  47.455  1.00 56.33           C  
ANISOU 2327  CE1 TYR A 296     5380   6810   9211   -300   -285    434       C  
ATOM   2328  CE2 TYR A 296     -34.584  30.703  46.720  1.00 55.22           C  
ANISOU 2328  CE2 TYR A 296     5258   6537   9186   -305   -412    399       C  
ATOM   2329  CZ  TYR A 296     -35.863  30.176  46.799  1.00 55.96           C  
ANISOU 2329  CZ  TYR A 296     5329   6687   9246   -321   -360    449       C  
ATOM   2330  OH  TYR A 296     -36.153  28.965  46.240  1.00 55.96           O  
ANISOU 2330  OH  TYR A 296     5302   6667   9292   -355   -387    513       O  
ATOM   2331  N   LYS A 297     -33.148  32.006  50.615  1.00 56.33           N  
ANISOU 2331  N   LYS A 297     5615   6728   9058   -319   -512    333       N  
ATOM   2332  CA  LYS A 297     -31.931  31.158  50.693  1.00 55.67           C  
ANISOU 2332  CA  LYS A 297     5530   6593   9026   -358   -613    371       C  
ATOM   2333  C   LYS A 297     -32.116  29.966  49.749  1.00 53.74           C  
ANISOU 2333  C   LYS A 297     5219   6332   8865   -372   -612    429       C  
ATOM   2334  O   LYS A 297     -33.260  29.507  49.587  1.00 54.46           O  
ANISOU 2334  O   LYS A 297     5290   6466   8934   -380   -550    467       O  
ATOM   2335  CB  LYS A 297     -31.704  30.704  52.139  1.00 57.46           C  
ANISOU 2335  CB  LYS A 297     5835   6850   9146   -389   -665    402       C  
ATOM   2336  CG  LYS A 297     -30.464  29.848  52.366  1.00 58.43           C  
ANISOU 2336  CG  LYS A 297     5962   6921   9315   -423   -780    442       C  
ATOM   2337  CD  LYS A 297     -29.748  30.141  53.673  1.00 60.07           C  
ANISOU 2337  CD  LYS A 297     6258   7128   9438   -443   -860    431       C  
ATOM   2338  CE  LYS A 297     -28.381  29.490  53.766  1.00 60.66           C  
ANISOU 2338  CE  LYS A 297     6321   7145   9582   -467   -984    462       C  
ATOM   2339  NZ  LYS A 297     -27.414  30.064  52.800  1.00 60.63           N  
ANISOU 2339  NZ  LYS A 297     6244   7088   9702   -448  -1016    426       N  
ATOM   2340  N   GLY A 298     -31.037  29.482  49.143  1.00 51.95           N  
ANISOU 2340  N   GLY A 298     4960   6046   8731   -372   -681    438       N  
ATOM   2341  CA  GLY A 298     -31.087  28.289  48.283  1.00 50.46           C  
ANISOU 2341  CA  GLY A 298     4729   5827   8614   -373   -697    485       C  
ATOM   2342  C   GLY A 298     -30.004  28.302  47.213  1.00 49.09           C  
ANISOU 2342  C   GLY A 298     4502   5601   8549   -339   -732    462       C  
ATOM   2343  O   GLY A 298     -29.178  29.214  47.148  1.00 47.76           O  
ANISOU 2343  O   GLY A 298     4316   5422   8406   -328   -746    421       O  
ATOM   2344  N   PRO A 299     -30.017  27.287  46.325  1.00 48.04           N  
ANISOU 2344  N   PRO A 299     4341   5435   8477   -321   -746    489       N  
ATOM   2345  CA  PRO A 299     -28.949  27.097  45.348  1.00 47.39           C  
ANISOU 2345  CA  PRO A 299     4207   5313   8485   -276   -776    472       C  
ATOM   2346  C   PRO A 299     -29.070  28.095  44.188  1.00 45.78           C  
ANISOU 2346  C   PRO A 299     3953   5114   8325   -247   -703    427       C  
ATOM   2347  O   PRO A 299     -29.772  27.806  43.236  1.00 44.58           O  
ANISOU 2347  O   PRO A 299     3790   4952   8196   -229   -662    427       O  
ATOM   2348  CB  PRO A 299     -29.158  25.640  44.912  1.00 47.75           C  
ANISOU 2348  CB  PRO A 299     4266   5318   8556   -261   -816    513       C  
ATOM   2349  CG  PRO A 299     -30.655  25.443  45.016  1.00 47.91           C  
ANISOU 2349  CG  PRO A 299     4317   5359   8527   -303   -769    542       C  
ATOM   2350  CD  PRO A 299     -31.083  26.284  46.201  1.00 48.19           C  
ANISOU 2350  CD  PRO A 299     4378   5453   8478   -343   -735    539       C  
ATOM   2351  N   ILE A 300     -28.377  29.235  44.312  1.00 45.09           N  
ANISOU 2351  N   ILE A 300     3844   5037   8248   -251   -701    394       N  
ATOM   2352  CA  ILE A 300     -28.311  30.319  43.284  1.00 43.82           C  
ANISOU 2352  CA  ILE A 300     3640   4878   8130   -234   -646    359       C  
ATOM   2353  C   ILE A 300     -27.132  30.021  42.359  1.00 42.79           C  
ANISOU 2353  C   ILE A 300     3440   4739   8079   -198   -666    366       C  
ATOM   2354  O   ILE A 300     -26.053  29.720  42.889  1.00 43.44           O  
ANISOU 2354  O   ILE A 300     3501   4823   8181   -198   -731    383       O  
ATOM   2355  CB  ILE A 300     -28.163  31.714  43.924  1.00 44.23           C  
ANISOU 2355  CB  ILE A 300     3714   4938   8153   -264   -648    326       C  
ATOM   2356  CG1 ILE A 300     -29.078  31.904  45.139  1.00 44.76           C  
ANISOU 2356  CG1 ILE A 300     3856   5024   8124   -286   -640    317       C  
ATOM   2357  CG2 ILE A 300     -28.370  32.800  42.877  1.00 43.83           C  
ANISOU 2357  CG2 ILE A 300     3634   4880   8138   -255   -593    297       C  
ATOM   2358  CD1 ILE A 300     -30.507  31.472  44.922  1.00 44.44           C  
ANISOU 2358  CD1 ILE A 300     3828   5006   8049   -276   -573    328       C  
ATOM   2359  N   THR A 301     -27.346  30.109  41.043  1.00 41.33           N  
ANISOU 2359  N   THR A 301     3220   4551   7930   -164   -610    355       N  
ATOM   2360  CA  THR A 301     -26.324  29.864  39.990  1.00 40.67           C  
ANISOU 2360  CA  THR A 301     3067   4476   7910   -115   -606    361       C  
ATOM   2361  C   THR A 301     -26.124  31.123  39.130  1.00 39.72           C  
ANISOU 2361  C   THR A 301     2902   4373   7816   -126   -553    347       C  
ATOM   2362  O   THR A 301     -25.096  31.177  38.442  1.00 40.39           O  
ANISOU 2362  O   THR A 301     2914   4484   7947   -100   -547    361       O  
ATOM   2363  CB  THR A 301     -26.693  28.623  39.163  1.00 40.54           C  
ANISOU 2363  CB  THR A 301     3064   4436   7900    -57   -598    364       C  
ATOM   2364  OG1 THR A 301     -25.501  28.050  38.628  1.00 40.94           O  
ANISOU 2364  OG1 THR A 301     3058   4499   7996      5   -618    371       O  
ATOM   2365  CG2 THR A 301     -27.648  28.912  38.027  1.00 40.09           C  
ANISOU 2365  CG2 THR A 301     3021   4371   7839    -44   -531    346       C  
ATOM   2366  N   ASP A 302     -27.059  32.083  39.153  1.00 38.29           N  
ANISOU 2366  N   ASP A 302     2760   4182   7606   -159   -517    326       N  
ATOM   2367  CA  ASP A 302     -26.974  33.368  38.402  1.00 37.45           C  
ANISOU 2367  CA  ASP A 302     2628   4079   7522   -178   -479    316       C  
ATOM   2368  C   ASP A 302     -27.596  34.486  39.242  1.00 37.01           C  
ANISOU 2368  C   ASP A 302     2630   4003   7428   -223   -489    290       C  
ATOM   2369  O   ASP A 302     -28.534  34.194  39.980  1.00 37.23           O  
ANISOU 2369  O   ASP A 302     2713   4027   7405   -221   -485    275       O  
ATOM   2370  CB  ASP A 302     -27.671  33.261  37.047  1.00 36.76           C  
ANISOU 2370  CB  ASP A 302     2537   3986   7440   -142   -415    309       C  
ATOM   2371  CG  ASP A 302     -27.016  32.261  36.116  1.00 36.80           C  
ANISOU 2371  CG  ASP A 302     2499   4010   7473    -84   -403    325       C  
ATOM   2372  OD1 ASP A 302     -25.898  32.532  35.686  1.00 37.39           O  
ANISOU 2372  OD1 ASP A 302     2505   4118   7582    -76   -399    344       O  
ATOM   2373  OD2 ASP A 302     -27.621  31.217  35.844  1.00 36.45           O  
ANISOU 2373  OD2 ASP A 302     2489   3947   7413    -45   -402    319       O  
ATOM   2374  N   VAL A 303     -27.064  35.706  39.149  1.00 36.79           N  
ANISOU 2374  N   VAL A 303     2590   3965   7422   -260   -505    287       N  
ATOM   2375  CA  VAL A 303     -27.589  36.927  39.832  1.00 36.77           C  
ANISOU 2375  CA  VAL A 303     2655   3929   7384   -292   -524    253       C  
ATOM   2376  C   VAL A 303     -27.305  38.134  38.930  1.00 36.90           C  
ANISOU 2376  C   VAL A 303     2654   3923   7442   -319   -517    258       C  
ATOM   2377  O   VAL A 303     -26.118  38.452  38.715  1.00 37.23           O  
ANISOU 2377  O   VAL A 303     2639   3974   7530   -359   -554    295       O  
ATOM   2378  CB  VAL A 303     -26.979  37.130  41.234  1.00 37.27           C  
ANISOU 2378  CB  VAL A 303     2756   3983   7420   -327   -603    247       C  
ATOM   2379  CG1 VAL A 303     -27.527  38.376  41.908  1.00 37.52           C  
ANISOU 2379  CG1 VAL A 303     2875   3974   7405   -344   -626    200       C  
ATOM   2380  CG2 VAL A 303     -27.183  35.925  42.136  1.00 37.23           C  
ANISOU 2380  CG2 VAL A 303     2772   4000   7370   -308   -615    253       C  
ATOM   2381  N   PHE A 304     -28.360  38.780  38.427  1.00 36.65           N  
ANISOU 2381  N   PHE A 304     2665   3867   7394   -302   -476    230       N  
ATOM   2382  CA  PHE A 304     -28.283  39.981  37.558  1.00 36.86           C  
ANISOU 2382  CA  PHE A 304     2692   3860   7453   -328   -475    236       C  
ATOM   2383  C   PHE A 304     -28.295  41.214  38.471  1.00 37.72           C  
ANISOU 2383  C   PHE A 304     2879   3913   7541   -362   -542    203       C  
ATOM   2384  O   PHE A 304     -28.901  41.144  39.561  1.00 37.79           O  
ANISOU 2384  O   PHE A 304     2952   3914   7492   -336   -555    158       O  
ATOM   2385  CB  PHE A 304     -29.395  39.941  36.506  1.00 36.16           C  
ANISOU 2385  CB  PHE A 304     2611   3767   7360   -286   -407    226       C  
ATOM   2386  CG  PHE A 304     -29.297  38.782  35.541  1.00 35.63           C  
ANISOU 2386  CG  PHE A 304     2485   3743   7309   -253   -357    255       C  
ATOM   2387  CD1 PHE A 304     -28.829  38.966  34.248  1.00 35.54           C  
ANISOU 2387  CD1 PHE A 304     2428   3743   7329   -258   -328    289       C  
ATOM   2388  CD2 PHE A 304     -29.659  37.498  35.926  1.00 35.28           C  
ANISOU 2388  CD2 PHE A 304     2437   3724   7242   -217   -343    250       C  
ATOM   2389  CE1 PHE A 304     -28.741  37.901  33.362  1.00 35.26           C  
ANISOU 2389  CE1 PHE A 304     2355   3745   7297   -215   -284    306       C  
ATOM   2390  CE2 PHE A 304     -29.559  36.432  35.042  1.00 35.00           C  
ANISOU 2390  CE2 PHE A 304     2366   3712   7218   -181   -312    270       C  
ATOM   2391  CZ  PHE A 304     -29.106  36.635  33.759  1.00 35.00           C  
ANISOU 2391  CZ  PHE A 304     2329   3724   7244   -173   -281    293       C  
ATOM   2392  N   TYR A 305     -27.577  42.271  38.077  1.00 38.64           N  
ANISOU 2392  N   TYR A 305     2990   3991   7697   -420   -591    227       N  
ATOM   2393  CA  TYR A 305     -27.422  43.542  38.836  1.00 39.59           C  
ANISOU 2393  CA  TYR A 305     3196   4038   7806   -461   -679    199       C  
ATOM   2394  C   TYR A 305     -27.501  44.728  37.876  1.00 40.52           C  
ANISOU 2394  C   TYR A 305     3334   4100   7961   -494   -694    216       C  
ATOM   2395  O   TYR A 305     -27.044  44.582  36.726  1.00 39.98           O  
ANISOU 2395  O   TYR A 305     3185   4066   7939   -521   -656    276       O  
ATOM   2396  CB  TYR A 305     -26.070  43.622  39.550  1.00 39.81           C  
ANISOU 2396  CB  TYR A 305     3199   4065   7860   -533   -770    235       C  
ATOM   2397  CG  TYR A 305     -25.843  42.597  40.628  1.00 39.34           C  
ANISOU 2397  CG  TYR A 305     3135   4046   7765   -512   -783    223       C  
ATOM   2398  CD1 TYR A 305     -26.084  42.898  41.958  1.00 39.66           C  
ANISOU 2398  CD1 TYR A 305     3277   4049   7741   -506   -845    170       C  
ATOM   2399  CD2 TYR A 305     -25.364  41.333  40.322  1.00 38.76           C  
ANISOU 2399  CD2 TYR A 305     2963   4045   7716   -494   -740    265       C  
ATOM   2400  CE1 TYR A 305     -25.870  41.963  42.958  1.00 39.74           C  
ANISOU 2400  CE1 TYR A 305     3290   4097   7711   -492   -861    167       C  
ATOM   2401  CE2 TYR A 305     -25.140  40.389  41.310  1.00 38.77           C  
ANISOU 2401  CE2 TYR A 305     2967   4076   7687   -478   -763    260       C  
ATOM   2402  CZ  TYR A 305     -25.397  40.703  42.633  1.00 39.24           C  
ANISOU 2402  CZ  TYR A 305     3126   4100   7681   -482   -823    215       C  
ATOM   2403  OH  TYR A 305     -25.186  39.775  43.610  1.00 39.26           O  
ANISOU 2403  OH  TYR A 305     3137   4131   7646   -471   -850    216       O  
ATOM   2404  N   LYS A 306     -28.025  45.861  38.357  1.00 42.24           N  
ANISOU 2404  N   LYS A 306     3661   4234   8152   -490   -752    164       N  
ATOM   2405  CA  LYS A 306     -28.083  47.150  37.608  1.00 43.55           C  
ANISOU 2405  CA  LYS A 306     3873   4322   8353   -528   -796    177       C  
ATOM   2406  C   LYS A 306     -26.777  47.936  37.822  1.00 45.34           C  
ANISOU 2406  C   LYS A 306     4099   4501   8625   -640   -911    231       C  
ATOM   2407  O   LYS A 306     -26.306  48.028  38.978  1.00 46.01           O  
ANISOU 2407  O   LYS A 306     4231   4561   8688   -662   -991    206       O  
ATOM   2408  CB  LYS A 306     -29.316  47.965  38.018  1.00 43.61           C  
ANISOU 2408  CB  LYS A 306     4003   4254   8310   -455   -810     92       C  
ATOM   2409  CG  LYS A 306     -30.537  47.765  37.125  1.00 43.01           C  
ANISOU 2409  CG  LYS A 306     3913   4199   8229   -379   -718     75       C  
ATOM   2410  CD  LYS A 306     -31.424  48.994  36.983  1.00 43.60           C  
ANISOU 2410  CD  LYS A 306     4091   4179   8293   -335   -756     24       C  
ATOM   2411  CE  LYS A 306     -30.838  50.086  36.107  1.00 44.16           C  
ANISOU 2411  CE  LYS A 306     4186   4169   8421   -416   -831     76       C  
ATOM   2412  NZ  LYS A 306     -30.632  49.640  34.707  1.00 43.54           N  
ANISOU 2412  NZ  LYS A 306     4009   4144   8386   -453   -765    156       N  
ATOM   2413  N   GLU A 307     -26.204  48.459  36.734  1.00 46.47           N  
ANISOU 2413  N   GLU A 307     4190   4638   8827   -714   -922    308       N  
ATOM   2414  CA  GLU A 307     -25.047  49.395  36.742  1.00 48.61           C  
ANISOU 2414  CA  GLU A 307     4458   4858   9152   -839  -1038    378       C  
ATOM   2415  C   GLU A 307     -25.289  50.449  35.658  1.00 49.52           C  
ANISOU 2415  C   GLU A 307     4607   4910   9299   -882  -1057    418       C  
ATOM   2416  O   GLU A 307     -26.214  50.251  34.841  1.00 48.70           O  
ANISOU 2416  O   GLU A 307     4503   4822   9176   -812   -967    398       O  
ATOM   2417  CB  GLU A 307     -23.728  48.645  36.510  1.00 49.01           C  
ANISOU 2417  CB  GLU A 307     4354   5012   9253   -906  -1021    472       C  
ATOM   2418  CG  GLU A 307     -22.479  49.431  36.896  1.00 50.08           C  
ANISOU 2418  CG  GLU A 307     4473   5109   9443  -1038  -1156    544       C  
ATOM   2419  CD  GLU A 307     -22.371  49.776  38.373  1.00 50.73           C  
ANISOU 2419  CD  GLU A 307     4667   5111   9496  -1049  -1280    481       C  
ATOM   2420  OE1 GLU A 307     -22.555  50.956  38.731  1.00 51.63           O  
ANISOU 2420  OE1 GLU A 307     4912   5100   9604  -1090  -1395    453       O  
ATOM   2421  OE2 GLU A 307     -22.096  48.860  39.164  1.00 50.78           O  
ANISOU 2421  OE2 GLU A 307     4636   5175   9481  -1015  -1268    460       O  
ATOM   2422  N   ASN A 308     -24.509  51.533  35.672  1.00 51.17           N  
ANISOU 2422  N   ASN A 308     4847   5041   9551   -998  -1180    475       N  
ATOM   2423  CA  ASN A 308     -24.499  52.568  34.605  1.00 52.40           C  
ANISOU 2423  CA  ASN A 308     5027   5136   9745  -1070  -1216    542       C  
ATOM   2424  C   ASN A 308     -23.041  52.875  34.255  1.00 53.85           C  
ANISOU 2424  C   ASN A 308     5106   5355   9998  -1225  -1278    677       C  
ATOM   2425  O   ASN A 308     -22.643  52.644  33.094  1.00 53.49           O  
ANISOU 2425  O   ASN A 308     4945   5399   9979  -1265  -1199    772       O  
ATOM   2426  CB  ASN A 308     -25.281  53.812  35.040  1.00 53.28           C  
ANISOU 2426  CB  ASN A 308     5322   5084   9836  -1050  -1328    466       C  
ATOM   2427  CG  ASN A 308     -25.843  54.589  33.868  1.00 53.58           C  
ANISOU 2427  CG  ASN A 308     5401   5065   9891  -1060  -1324    499       C  
ATOM   2428  OD1 ASN A 308     -25.094  55.110  33.045  1.00 54.11           O  
ANISOU 2428  OD1 ASN A 308     5421   5130  10009  -1181  -1361    613       O  
ATOM   2429  ND2 ASN A 308     -27.162  54.657  33.780  1.00 53.38           N  
ANISOU 2429  ND2 ASN A 308     5458   5000   9823   -936  -1277    407       N  
ATOM   2430  N   SER A 309     -22.304  53.390  35.246  1.00 55.51           N  
ANISOU 2430  N   SER A 309     5358   5500  10230  -1306  -1419    685       N  
ATOM   2431  CA  SER A 309     -20.836  53.604  35.249  1.00 56.75           C  
ANISOU 2431  CA  SER A 309     5406   5695  10458  -1459  -1501    812       C  
ATOM   2432  C   SER A 309     -20.314  53.366  36.670  1.00 57.47           C  
ANISOU 2432  C   SER A 309     5525   5764  10544  -1470  -1599    768       C  
ATOM   2433  O   SER A 309     -20.891  53.942  37.608  1.00 57.50           O  
ANISOU 2433  O   SER A 309     5701   5641  10504  -1433  -1698    667       O  
ATOM   2434  CB  SER A 309     -20.481  54.978  34.755  1.00 58.15           C  
ANISOU 2434  CB  SER A 309     5641   5766  10685  -1598  -1629    897       C  
ATOM   2435  OG  SER A 309     -19.070  55.120  34.644  1.00 59.65           O  
ANISOU 2435  OG  SER A 309     5698   6016  10949  -1754  -1694   1040       O  
ATOM   2436  N   TYR A 310     -19.294  52.514  36.813  1.00 58.24           N  
ANISOU 2436  N   TYR A 310     5463   5986  10678  -1505  -1569    837       N  
ATOM   2437  CA  TYR A 310     -18.541  52.284  38.072  1.00 59.51           C  
ANISOU 2437  CA  TYR A 310     5623   6138  10848  -1543  -1678    827       C  
ATOM   2438  C   TYR A 310     -17.041  52.401  37.790  1.00 61.97           C  
ANISOU 2438  C   TYR A 310     5767   6523  11254  -1695  -1742    982       C  
ATOM   2439  O   TYR A 310     -16.610  52.114  36.650  1.00 62.31           O  
ANISOU 2439  O   TYR A 310     5651   6685  11336  -1721  -1637   1083       O  
ATOM   2440  CB  TYR A 310     -18.865  50.913  38.665  1.00 58.18           C  
ANISOU 2440  CB  TYR A 310     5418   6060  10628  -1411  -1573    748       C  
ATOM   2441  CG  TYR A 310     -18.004  50.517  39.838  1.00 58.79           C  
ANISOU 2441  CG  TYR A 310     5469   6150  10716  -1448  -1672    754       C  
ATOM   2442  CD1 TYR A 310     -18.228  51.035  41.104  1.00 59.17           C  
ANISOU 2442  CD1 TYR A 310     5686   6078  10716  -1450  -1808    671       C  
ATOM   2443  CD2 TYR A 310     -16.959  49.620  39.681  1.00 59.16           C  
ANISOU 2443  CD2 TYR A 310     5327   6332  10818  -1473  -1633    841       C  
ATOM   2444  CE1 TYR A 310     -17.442  50.667  42.185  1.00 59.85           C  
ANISOU 2444  CE1 TYR A 310     5758   6173  10807  -1486  -1908    678       C  
ATOM   2445  CE2 TYR A 310     -16.161  49.245  40.750  1.00 59.81           C  
ANISOU 2445  CE2 TYR A 310     5383   6426  10916  -1506  -1732    850       C  
ATOM   2446  CZ  TYR A 310     -16.403  49.768  42.008  1.00 60.17           C  
ANISOU 2446  CZ  TYR A 310     5603   6347  10912  -1518  -1873    771       C  
ATOM   2447  OH  TYR A 310     -15.611  49.388  43.056  1.00 60.70           O  
ANISOU 2447  OH  TYR A 310     5650   6423  10989  -1553  -1979    783       O  
ATOM   2448  N   THR A 311     -16.284  52.839  38.800  1.00 64.10           N  
ANISOU 2448  N   THR A 311     6073   6726  11553  -1791  -1914   1002       N  
ATOM   2449  CA  THR A 311     -14.798  52.779  38.857  1.00 65.66           C  
ANISOU 2449  CA  THR A 311     6099   7005  11843  -1929  -1992   1143       C  
ATOM   2450  C   THR A 311     -14.380  52.620  40.323  1.00 66.61           C  
ANISOU 2450  C   THR A 311     6285   7069  11953  -1942  -2135   1093       C  
ATOM   2451  O   THR A 311     -14.862  53.412  41.157  1.00 67.11           O  
ANISOU 2451  O   THR A 311     6556   6971  11969  -1951  -2271   1007       O  
ATOM   2452  CB  THR A 311     -14.149  54.010  38.211  1.00 67.28           C  
ANISOU 2452  CB  THR A 311     6280   7157  12125  -2110  -2105   1279       C  
ATOM   2453  OG1 THR A 311     -15.051  54.600  37.275  1.00 66.82           O  
ANISOU 2453  OG1 THR A 311     6307   7043  12036  -2082  -2040   1259       O  
ATOM   2454  CG2 THR A 311     -12.853  53.669  37.511  1.00 68.43           C  
ANISOU 2454  CG2 THR A 311     6166   7471  12362  -2214  -2064   1453       C  
ATOM   2455  N   THR A 312     -13.539  51.628  40.625  1.00 67.20           N  
ANISOU 2455  N   THR A 312     6198   7272  12063  -1934  -2106   1141       N  
ATOM   2456  CA  THR A 312     -13.149  51.243  42.009  1.00 67.94           C  
ANISOU 2456  CA  THR A 312     6340   7334  12138  -1928  -2224   1093       C  
ATOM   2457  C   THR A 312     -12.120  52.249  42.539  1.00 69.86           C  
ANISOU 2457  C   THR A 312     6596   7491  12455  -2114  -2454   1185       C  
ATOM   2458  O   THR A 312     -11.312  52.744  41.735  1.00 70.38           O  
ANISOU 2458  O   THR A 312     6519   7606  12615  -2247  -2480   1331       O  
ATOM   2459  CB  THR A 312     -12.652  49.791  42.046  1.00 67.81           C  
ANISOU 2459  CB  THR A 312     6144   7483  12138  -1845  -2111   1115       C  
ATOM   2460  OG1 THR A 312     -12.806  49.285  43.374  1.00 67.85           O  
ANISOU 2460  OG1 THR A 312     6255   7440  12082  -1786  -2183   1022       O  
ATOM   2461  CG2 THR A 312     -11.216  49.645  41.587  1.00 69.03           C  
ANISOU 2461  CG2 THR A 312     6055   7762  12408  -1955  -2137   1280       C  
ATOM   2462  N   THR A 313     -12.151  52.525  43.846  1.00 70.80           N  
ANISOU 2462  N   THR A 313     6881   7489  12529  -2125  -2617   1107       N  
ATOM   2463  CA  THR A 313     -11.251  53.485  44.541  1.00 73.25           C  
ANISOU 2463  CA  THR A 313     7246   7687  12895  -2298  -2869   1175       C  
ATOM   2464  C   THR A 313     -10.040  52.721  45.107  1.00 74.63           C  
ANISOU 2464  C   THR A 313     7246   7969  13138  -2352  -2933   1261       C  
ATOM   2465  O   THR A 313      -9.747  52.884  46.312  1.00 75.36           O  
ANISOU 2465  O   THR A 313     7457   7969  13205  -2389  -3110   1221       O  
ATOM   2466  CB  THR A 313     -12.035  54.284  45.592  1.00 73.27           C  
ANISOU 2466  CB  THR A 313     7553   7488  12798  -2268  -3015   1031       C  
ATOM   2467  OG1 THR A 313     -12.322  53.449  46.714  1.00 72.45           O  
ANISOU 2467  OG1 THR A 313     7526   7396  12604  -2152  -3005    920       O  
ATOM   2468  CG2 THR A 313     -13.334  54.842  45.053  1.00 72.13           C  
ANISOU 2468  CG2 THR A 313     7564   7259  12581  -2173  -2924    931       C  
ATOM   2469  N   ILE A 314      -9.368  51.929  44.255  1.00 75.01           N  
ANISOU 2469  N   ILE A 314     7029   8204  13264  -2349  -2797   1373       N  
ATOM   2470  CA  ILE A 314      -8.169  51.090  44.581  1.00 76.27           C  
ANISOU 2470  CA  ILE A 314     6975   8499  13504  -2380  -2827   1470       C  
ATOM   2471  C   ILE A 314      -6.995  51.563  43.704  1.00 78.35           C  
ANISOU 2471  C   ILE A 314     7004   8861  13904  -2545  -2861   1669       C  
ATOM   2472  O   ILE A 314      -7.023  51.303  42.475  1.00 78.12           O  
ANISOU 2472  O   ILE A 314     6819   8961  13899  -2511  -2679   1732       O  
ATOM   2473  CB  ILE A 314      -8.465  49.584  44.385  1.00 74.39           C  
ANISOU 2473  CB  ILE A 314     6629   8408  13226  -2196  -2619   1415       C  
ATOM   2474  CG1 ILE A 314      -9.659  49.112  45.222  1.00 72.97           C  
ANISOU 2474  CG1 ILE A 314     6672   8142  12911  -2045  -2579   1235       C  
ATOM   2475  CG2 ILE A 314      -7.224  48.740  44.653  1.00 74.78           C  
ANISOU 2475  CG2 ILE A 314     6455   8594  13363  -2216  -2651   1515       C  
ATOM   2476  CD1 ILE A 314     -10.321  47.849  44.703  1.00 71.15           C  
ANISOU 2476  CD1 ILE A 314     6376   8026  12630  -1868  -2353   1173       C  
ATOM   2477  N   LYS A 315      -6.005  52.231  44.311  1.00 79.88           N  
ANISOU 2477  N   LYS A 315     7172   9000  14179  -2720  -3087   1769       N  
ATOM   2478  CA  LYS A 315      -4.859  52.867  43.610  1.00 81.49           C  
ANISOU 2478  CA  LYS A 315     7163   9280  14518  -2914  -3160   1976       C  
ATOM   2479  C   LYS A 315      -5.375  53.687  42.421  1.00 80.96           C  
ANISOU 2479  C   LYS A 315     7122   9190  14447  -2961  -3073   2017       C  
ATOM   2480  O   LYS A 315      -4.764  54.671  42.007  1.00 82.50           O  
ANISOU 2480  O   LYS A 315     7262   9358  14724  -3151  -3191   2160       O  
ATOM   2481  CB  LYS A 315      -3.868  51.799  43.147  1.00 82.12           C  
ANISOU 2481  CB  LYS A 315     6919   9599  14681  -2878  -3036   2093       C  
ATOM   2482  CG  LYS A 315      -3.311  50.923  44.260  1.00 82.58           C  
ANISOU 2482  CG  LYS A 315     6935   9689  14752  -2826  -3121   2063       C  
ATOM   2483  CD  LYS A 315      -1.864  50.531  44.056  1.00 84.35           C  
ANISOU 2483  CD  LYS A 315     6839  10095  15114  -2908  -3149   2245       C  
ATOM   2484  CE  LYS A 315      -1.214  50.050  45.333  1.00 85.26           C  
ANISOU 2484  CE  LYS A 315     6951  10187  15257  -2918  -3322   2234       C  
ATOM   2485  NZ  LYS A 315      -0.199  49.006  45.067  1.00 86.17           N  
ANISOU 2485  NZ  LYS A 315     6754  10520  15463  -2860  -3238   2339       N  
TER    2486      LYS A 315                                                      
ATOM   2487  N   THR B   4     -14.302  25.955  -8.476  1.00105.80           N  
ANISOU 2487  N   THR B   4    11562  14535  14099   1477   -235   2710       N  
ATOM   2488  CA  THR B   4     -14.037  24.665  -7.756  1.00104.30           C  
ANISOU 2488  CA  THR B   4    11290  14373  13966   1383   -269   2510       C  
ATOM   2489  C   THR B   4     -12.772  24.782  -6.894  1.00101.95           C  
ANISOU 2489  C   THR B   4    11015  13928  13793   1222   -201   2513       C  
ATOM   2490  O   THR B   4     -11.814  25.438  -7.344  1.00102.67           O  
ANISOU 2490  O   THR B   4    11148  13996  13866   1175   -124   2654       O  
ATOM   2491  CB  THR B   4     -13.885  23.482  -8.726  1.00104.87           C  
ANISOU 2491  CB  THR B   4    11275  14678  13890   1417   -295   2423       C  
ATOM   2492  OG1 THR B   4     -12.837  23.784  -9.647  1.00105.79           O  
ANISOU 2492  OG1 THR B   4    11411  14867  13917   1403   -219   2553       O  
ATOM   2493  CG2 THR B   4     -15.148  23.155  -9.494  1.00105.79           C  
ANISOU 2493  CG2 THR B   4    11350  14962  13881   1557   -378   2380       C  
ATOM   2494  N   ILE B   5     -12.775  24.158  -5.710  1.00 99.14           N  
ANISOU 2494  N   ILE B   5    10627  13485  13555   1138   -229   2366       N  
ATOM   2495  CA  ILE B   5     -11.581  23.993  -4.823  1.00 97.41           C  
ANISOU 2495  CA  ILE B   5    10403  13160  13446    982   -181   2334       C  
ATOM   2496  C   ILE B   5     -11.203  22.507  -4.810  1.00 95.08           C  
ANISOU 2496  C   ILE B   5    10010  12996  13119    950   -204   2179       C  
ATOM   2497  O   ILE B   5     -11.764  21.754  -5.631  1.00 95.72           O  
ANISOU 2497  O   ILE B   5    10042  13242  13084   1041   -246   2117       O  
ATOM   2498  CB  ILE B   5     -11.845  24.556  -3.407  1.00 96.96           C  
ANISOU 2498  CB  ILE B   5    10401  12887  13551    914   -189   2301       C  
ATOM   2499  CG1 ILE B   5     -12.856  23.718  -2.616  1.00 95.70           C  
ANISOU 2499  CG1 ILE B   5    10194  12729  13439    945   -265   2129       C  
ATOM   2500  CG2 ILE B   5     -12.266  26.016  -3.489  1.00 98.46           C  
ANISOU 2500  CG2 ILE B   5    10699  12942  13767    961   -161   2452       C  
ATOM   2501  CD1 ILE B   5     -13.185  24.267  -1.243  1.00 94.54           C  
ANISOU 2501  CD1 ILE B   5    10102  12381  13437    892   -272   2094       C  
ATOM   2502  N   LYS B   6     -10.274  22.108  -3.934  1.00 92.66           N  
ANISOU 2502  N   LYS B   6     9679  12620  12907    828   -177   2121       N  
ATOM   2503  CA  LYS B   6      -9.795  20.706  -3.794  1.00 90.51           C  
ANISOU 2503  CA  LYS B   6     9322  12447  12621    794   -188   1980       C  
ATOM   2504  C   LYS B   6      -9.975  20.265  -2.335  1.00 86.52           C  
ANISOU 2504  C   LYS B   6     8804  11815  12252    720   -221   1853       C  
ATOM   2505  O   LYS B   6      -9.691  21.074  -1.432  1.00 84.64           O  
ANISOU 2505  O   LYS B   6     8615  11420  12124    640   -201   1901       O  
ATOM   2506  CB  LYS B   6      -8.340  20.602  -4.272  1.00 91.93           C  
ANISOU 2506  CB  LYS B   6     9471  12695  12761    728   -112   2052       C  
ATOM   2507  CG  LYS B   6      -7.944  19.267  -4.896  1.00 92.07           C  
ANISOU 2507  CG  LYS B   6     9410  12885  12684    761   -110   1953       C  
ATOM   2508  CD  LYS B   6      -6.625  19.313  -5.652  1.00 92.69           C  
ANISOU 2508  CD  LYS B   6     9461  13063  12693    730    -28   2053       C  
ATOM   2509  CE  LYS B   6      -5.968  17.956  -5.794  1.00 91.97           C  
ANISOU 2509  CE  LYS B   6     9292  13091  12559    732    -14   1938       C  
ATOM   2510  NZ  LYS B   6      -4.589  18.066  -6.324  1.00 92.25           N  
ANISOU 2510  NZ  LYS B   6     9290  13209  12549    690     73   2040       N  
ATOM   2511  N   VAL B   7     -10.462  19.038  -2.128  1.00 84.33           N  
ANISOU 2511  N   VAL B   7     8471  11604  11966    747   -270   1698       N  
ATOM   2512  CA  VAL B   7     -10.712  18.425  -0.787  1.00 82.72           C  
ANISOU 2512  CA  VAL B   7     8249  11301  11880    688   -303   1567       C  
ATOM   2513  C   VAL B   7     -10.602  16.900  -0.914  1.00 80.62           C  
ANISOU 2513  C   VAL B   7     7912  11145  11575    698   -321   1425       C  
ATOM   2514  O   VAL B   7     -10.553  16.399  -2.063  1.00 81.00           O  
ANISOU 2514  O   VAL B   7     7933  11341  11501    762   -317   1419       O  
ATOM   2515  CB  VAL B   7     -12.085  18.830  -0.203  1.00 83.03           C  
ANISOU 2515  CB  VAL B   7     8320  11253  11971    735   -360   1529       C  
ATOM   2516  CG1 VAL B   7     -12.167  20.315   0.120  1.00 83.42           C  
ANISOU 2516  CG1 VAL B   7     8453  11163  12080    722   -336   1657       C  
ATOM   2517  CG2 VAL B   7     -13.240  18.414  -1.105  1.00 83.46           C  
ANISOU 2517  CG2 VAL B   7     8347  11439  11924    851   -414   1483       C  
ATOM   2518  N   PHE B   8     -10.578  16.202   0.229  1.00 77.73           N  
ANISOU 2518  N   PHE B   8     7525  10703  11305    640   -337   1316       N  
ATOM   2519  CA  PHE B   8     -10.582  14.719   0.338  1.00 75.40           C  
ANISOU 2519  CA  PHE B   8     7176  10474  10999    645   -354   1170       C  
ATOM   2520  C   PHE B   8     -11.886  14.249   0.997  1.00 72.71           C  
ANISOU 2520  C   PHE B   8     6831  10087  10708    666   -418   1052       C  
ATOM   2521  O   PHE B   8     -12.219  14.700   2.107  1.00 71.27           O  
ANISOU 2521  O   PHE B   8     6672   9777  10629    624   -431   1048       O  
ATOM   2522  CB  PHE B   8      -9.370  14.228   1.133  1.00 75.43           C  
ANISOU 2522  CB  PHE B   8     7152  10435  11071    561   -312   1152       C  
ATOM   2523  CG  PHE B   8      -8.047  14.737   0.624  1.00 77.21           C  
ANISOU 2523  CG  PHE B   8     7369  10705  11261    527   -246   1273       C  
ATOM   2524  CD1 PHE B   8      -7.562  14.338  -0.612  1.00 77.93           C  
ANISOU 2524  CD1 PHE B   8     7433  10942  11234    581   -213   1297       C  
ATOM   2525  CD2 PHE B   8      -7.289  15.620   1.380  1.00 77.55           C  
ANISOU 2525  CD2 PHE B   8     7428  10648  11387    435   -216   1361       C  
ATOM   2526  CE1 PHE B   8      -6.350  14.816  -1.084  1.00 78.85           C  
ANISOU 2526  CE1 PHE B   8     7533  11107  11316    548   -147   1414       C  
ATOM   2527  CE2 PHE B   8      -6.075  16.093   0.907  1.00 78.38           C  
ANISOU 2527  CE2 PHE B   8     7517  10800  11462    392   -155   1475       C  
ATOM   2528  CZ  PHE B   8      -5.610  15.691  -0.324  1.00 79.29           C  
ANISOU 2528  CZ  PHE B   8     7599  11065  11461    450   -118   1505       C  
ATOM   2529  N   THR B   9     -12.614  13.366   0.315  1.00 70.70           N  
ANISOU 2529  N   THR B   9     6546   9938  10377    726   -456    956       N  
ATOM   2530  CA  THR B   9     -13.736  12.583   0.886  1.00 68.61           C  
ANISOU 2530  CA  THR B   9     6260   9653  10155    732   -511    821       C  
ATOM   2531  C   THR B   9     -13.173  11.244   1.371  1.00 66.93           C  
ANISOU 2531  C   THR B   9     6019   9432   9977    686   -493    706       C  
ATOM   2532  O   THR B   9     -12.119  10.824   0.853  1.00 66.31           O  
ANISOU 2532  O   THR B   9     5932   9414   9850    684   -448    721       O  
ATOM   2533  CB  THR B   9     -14.871  12.429  -0.132  1.00 69.24           C  
ANISOU 2533  CB  THR B   9     6320   9855  10132    813   -565    782       C  
ATOM   2534  OG1 THR B   9     -14.322  11.957  -1.363  1.00 69.63           O  
ANISOU 2534  OG1 THR B   9     6357  10041  10056    851   -547    781       O  
ATOM   2535  CG2 THR B   9     -15.615  13.725  -0.364  1.00 70.04           C  
ANISOU 2535  CG2 THR B   9     6447   9945  10219    868   -589    889       C  
ATOM   2536  N   THR B  10     -13.843  10.619   2.341  1.00 65.36           N  
ANISOU 2536  N   THR B  10     5811   9162   9862    656   -522    604       N  
ATOM   2537  CA  THR B  10     -13.480   9.295   2.907  1.00 64.38           C  
ANISOU 2537  CA  THR B  10     5668   9012   9781    617   -507    491       C  
ATOM   2538  C   THR B  10     -14.616   8.796   3.806  1.00 63.44           C  
ANISOU 2538  C   THR B  10     5539   8827   9739    595   -549    389       C  
ATOM   2539  O   THR B  10     -15.502   9.598   4.139  1.00 62.71           O  
ANISOU 2539  O   THR B  10     5452   8697   9677    605   -582    420       O  
ATOM   2540  CB  THR B  10     -12.157   9.369   3.679  1.00 63.50           C  
ANISOU 2540  CB  THR B  10     5561   8829   9733    562   -453    546       C  
ATOM   2541  OG1 THR B  10     -11.722   8.033   3.933  1.00 62.70           O  
ANISOU 2541  OG1 THR B  10     5443   8730   9647    551   -432    449       O  
ATOM   2542  CG2 THR B  10     -12.276  10.137   4.978  1.00 62.87           C  
ANISOU 2542  CG2 THR B  10     5501   8620   9763    507   -459    587       C  
ATOM   2543  N   VAL B  11     -14.562   7.518   4.186  1.00 63.52           N  
ANISOU 2543  N   VAL B  11     5537   8818   9778    569   -542    278       N  
ATOM   2544  CA  VAL B  11     -15.494   6.873   5.159  1.00 63.03           C  
ANISOU 2544  CA  VAL B  11     5465   8683   9799    534   -569    179       C  
ATOM   2545  C   VAL B  11     -14.723   6.432   6.416  1.00 62.47           C  
ANISOU 2545  C   VAL B  11     5406   8504   9826    480   -529    173       C  
ATOM   2546  O   VAL B  11     -15.402   6.103   7.409  1.00 60.86           O  
ANISOU 2546  O   VAL B  11     5199   8224   9699    446   -543    118       O  
ATOM   2547  CB  VAL B  11     -16.252   5.692   4.514  1.00 63.71           C  
ANISOU 2547  CB  VAL B  11     5531   8839   9836    545   -597     47       C  
ATOM   2548  CG1 VAL B  11     -17.405   6.168   3.642  1.00 64.39           C  
ANISOU 2548  CG1 VAL B  11     5592   9024   9848    587   -656     40       C  
ATOM   2549  CG2 VAL B  11     -15.333   4.771   3.721  1.00 64.33           C  
ANISOU 2549  CG2 VAL B  11     5620   8975   9846    563   -560      4       C  
ATOM   2550  N   ASP B  12     -13.376   6.446   6.393  1.00 63.28           N  
ANISOU 2550  N   ASP B  12     5515   8606   9919    473   -481    233       N  
ATOM   2551  CA  ASP B  12     -12.513   5.766   7.405  1.00 62.89           C  
ANISOU 2551  CA  ASP B  12     5467   8485   9941    435   -443    218       C  
ATOM   2552  C   ASP B  12     -11.327   6.630   7.864  1.00 63.61           C  
ANISOU 2552  C   ASP B  12     5559   8550  10057    406   -411    333       C  
ATOM   2553  O   ASP B  12     -10.770   6.294   8.931  1.00 62.66           O  
ANISOU 2553  O   ASP B  12     5436   8365  10005    369   -391    331       O  
ATOM   2554  CB  ASP B  12     -12.008   4.415   6.885  1.00 62.73           C  
ANISOU 2554  CB  ASP B  12     5444   8507   9882    461   -411    139       C  
ATOM   2555  CG  ASP B  12     -11.450   4.446   5.474  1.00 63.13           C  
ANISOU 2555  CG  ASP B  12     5490   8675   9822    514   -393    163       C  
ATOM   2556  OD1 ASP B  12     -11.203   5.550   4.962  1.00 63.71           O  
ANISOU 2556  OD1 ASP B  12     5559   8795   9853    524   -395    263       O  
ATOM   2557  OD2 ASP B  12     -11.271   3.361   4.901  1.00 63.59           O  
ANISOU 2557  OD2 ASP B  12     5553   8773   9836    545   -372     82       O  
ATOM   2558  N   ASN B  13     -10.925   7.659   7.102  1.00 65.67           N  
ANISOU 2558  N   ASN B  13     5822   8864  10264    419   -405    430       N  
ATOM   2559  CA  ASN B  13      -9.833   8.609   7.468  1.00 66.68           C  
ANISOU 2559  CA  ASN B  13     5950   8968  10414    376   -376    545       C  
ATOM   2560  C   ASN B  13      -8.484   7.876   7.380  1.00 67.49           C  
ANISOU 2560  C   ASN B  13     6020   9122  10501    375   -326    556       C  
ATOM   2561  O   ASN B  13      -7.613   8.098   8.252  1.00 67.04           O  
ANISOU 2561  O   ASN B  13     5948   9025  10497    323   -307    604       O  
ATOM   2562  CB  ASN B  13     -10.079   9.236   8.849  1.00 66.40           C  
ANISOU 2562  CB  ASN B  13     5935   8817  10475    316   -393    560       C  
ATOM   2563  CG  ASN B  13      -9.217  10.446   9.156  1.00 66.73           C  
ANISOU 2563  CG  ASN B  13     5988   8826  10538    260   -376    673       C  
ATOM   2564  OD1 ASN B  13      -8.425  10.891   8.329  1.00 68.13           O  
ANISOU 2564  OD1 ASN B  13     6154   9067  10662    263   -348    752       O  
ATOM   2565  ND2 ASN B  13      -9.359  10.983  10.356  1.00 66.23           N  
ANISOU 2565  ND2 ASN B  13     5949   8663  10552    205   -390    679       N  
ATOM   2566  N   ILE B  14      -8.325   7.029   6.358  1.00 68.71           N  
ANISOU 2566  N   ILE B  14     6161   9365  10579    434   -307    511       N  
ATOM   2567  CA  ILE B  14      -7.091   6.231   6.083  1.00 69.12           C  
ANISOU 2567  CA  ILE B  14     6181   9480  10600    458   -252    515       C  
ATOM   2568  C   ILE B  14      -6.846   6.240   4.569  1.00 72.33           C  
ANISOU 2568  C   ILE B  14     6582  10008  10889    518   -228    536       C  
ATOM   2569  O   ILE B  14      -5.739   6.634   4.146  1.00 72.84           O  
ANISOU 2569  O   ILE B  14     6617  10142  10917    519   -184    627       O  
ATOM   2570  CB  ILE B  14      -7.221   4.809   6.671  1.00 66.96           C  
ANISOU 2570  CB  ILE B  14     5911   9163  10366    476   -244    404       C  
ATOM   2571  CG1 ILE B  14      -7.187   4.846   8.202  1.00 65.59           C  
ANISOU 2571  CG1 ILE B  14     5737   8885  10298    418   -256    408       C  
ATOM   2572  CG2 ILE B  14      -6.160   3.877   6.106  1.00 67.67           C  
ANISOU 2572  CG2 ILE B  14     5978   9327  10405    531   -186    392       C  
ATOM   2573  CD1 ILE B  14      -7.100   3.491   8.866  1.00 65.07           C  
ANISOU 2573  CD1 ILE B  14     5674   8773  10274    437   -237    326       C  
ATOM   2574  N   ASN B  15      -7.849   5.825   3.791  1.00 76.16           N  
ANISOU 2574  N   ASN B  15     7091  10529  11317    563   -258    454       N  
ATOM   2575  CA  ASN B  15      -7.888   5.949   2.309  1.00 79.50           C  
ANISOU 2575  CA  ASN B  15     7515  11073  11615    623   -250    467       C  
ATOM   2576  C   ASN B  15      -8.565   7.286   1.963  1.00 80.95           C  
ANISOU 2576  C   ASN B  15     7714  11264  11777    614   -288    551       C  
ATOM   2577  O   ASN B  15      -9.816   7.308   1.901  1.00 82.36           O  
ANISOU 2577  O   ASN B  15     7910  11427  11954    625   -343    491       O  
ATOM   2578  CB  ASN B  15      -8.599   4.750   1.665  1.00 80.13           C  
ANISOU 2578  CB  ASN B  15     7613  11193  11638    673   -266    325       C  
ATOM   2579  CG  ASN B  15      -7.857   3.434   1.812  1.00 80.17           C  
ANISOU 2579  CG  ASN B  15     7617  11192  11650    698   -216    249       C  
ATOM   2580  OD1 ASN B  15      -7.640   2.946   2.921  1.00 78.79           O  
ANISOU 2580  OD1 ASN B  15     7440  10924  11571    667   -206    225       O  
ATOM   2581  ND2 ASN B  15      -7.486   2.830   0.693  1.00 81.26           N  
ANISOU 2581  ND2 ASN B  15     7761  11431  11684    762   -183    209       N  
ATOM   2582  N   LEU B  16      -7.773   8.353   1.773  1.00 81.60           N  
ANISOU 2582  N   LEU B  16     7789  11367  11847    594   -257    686       N  
ATOM   2583  CA  LEU B  16      -8.259   9.723   1.435  1.00 82.32           C  
ANISOU 2583  CA  LEU B  16     7905  11452  11921    589   -280    789       C  
ATOM   2584  C   LEU B  16      -8.464   9.838  -0.082  1.00 84.42           C  
ANISOU 2584  C   LEU B  16     8175  11852  12048    663   -277    813       C  
ATOM   2585  O   LEU B  16      -7.454   9.854  -0.813  1.00 86.16           O  
ANISOU 2585  O   LEU B  16     8377  12161  12199    681   -221    877       O  
ATOM   2586  CB  LEU B  16      -7.251  10.772   1.919  1.00 82.07           C  
ANISOU 2586  CB  LEU B  16     7868  11373  11940    522   -242    922       C  
ATOM   2587  CG  LEU B  16      -6.864  10.721   3.397  1.00 80.92           C  
ANISOU 2587  CG  LEU B  16     7714  11112  11916    444   -243    907       C  
ATOM   2588  CD1 LEU B  16      -6.036  11.942   3.774  1.00 80.91           C  
ANISOU 2588  CD1 LEU B  16     7717  11067  11958    368   -216   1038       C  
ATOM   2589  CD2 LEU B  16      -8.089  10.615   4.290  1.00 79.86           C  
ANISOU 2589  CD2 LEU B  16     7610  10877  11856    435   -300    824       C  
ATOM   2590  N   HIS B  17      -9.724   9.926  -0.525  1.00 85.94           N  
ANISOU 2590  N   HIS B  17     8385  12067  12199    706   -333    767       N  
ATOM   2591  CA  HIS B  17     -10.138  10.105  -1.945  1.00 87.45           C  
ANISOU 2591  CA  HIS B  17     8582  12393  12250    782   -346    788       C  
ATOM   2592  C   HIS B  17     -10.140  11.604  -2.272  1.00 87.78           C  
ANISOU 2592  C   HIS B  17     8649  12430  12274    787   -340    948       C  
ATOM   2593  O   HIS B  17     -10.853  12.350  -1.579  1.00 87.71           O  
ANISOU 2593  O   HIS B  17     8662  12322  12341    767   -375    976       O  
ATOM   2594  CB  HIS B  17     -11.503   9.439  -2.192  1.00 87.50           C  
ANISOU 2594  CB  HIS B  17     8587  12436  12223    819   -416    657       C  
ATOM   2595  CG  HIS B  17     -11.552   8.011  -1.765  1.00 87.93           C  
ANISOU 2595  CG  HIS B  17     8629  12466  12312    800   -419    502       C  
ATOM   2596  ND1 HIS B  17     -11.027   6.994  -2.537  1.00 89.69           N  
ANISOU 2596  ND1 HIS B  17     8849  12780  12450    835   -388    427       N  
ATOM   2597  CD2 HIS B  17     -12.033   7.429  -0.644  1.00 87.81           C  
ANISOU 2597  CD2 HIS B  17     8611  12343  12407    752   -443    412       C  
ATOM   2598  CE1 HIS B  17     -11.191   5.843  -1.914  1.00 89.88           C  
ANISOU 2598  CE1 HIS B  17     8873  12741  12535    809   -393    297       C  
ATOM   2599  NE2 HIS B  17     -11.806   6.083  -0.748  1.00 88.73           N  
ANISOU 2599  NE2 HIS B  17     8726  12476  12509    756   -426    289       N  
ATOM   2600  N   THR B  18      -9.363  12.031  -3.272  1.00 87.90           N  
ANISOU 2600  N   THR B  18     8664  12542  12192    816   -291   1051       N  
ATOM   2601  CA  THR B  18      -9.200  13.461  -3.655  1.00 88.82           C  
ANISOU 2601  CA  THR B  18     8810  12649  12288    818   -269   1220       C  
ATOM   2602  C   THR B  18     -10.337  13.875  -4.592  1.00 89.28           C  
ANISOU 2602  C   THR B  18     8888  12787  12244    905   -319   1239       C  
ATOM   2603  O   THR B  18     -10.671  13.088  -5.503  1.00 90.33           O  
ANISOU 2603  O   THR B  18     9002  13055  12262    969   -340   1159       O  
ATOM   2604  CB  THR B  18      -7.841  13.730  -4.310  1.00 89.64           C  
ANISOU 2604  CB  THR B  18     8900  12827  12332    806   -188   1332       C  
ATOM   2605  OG1 THR B  18      -6.843  13.021  -3.575  1.00 89.98           O  
ANISOU 2605  OG1 THR B  18     8905  12836  12446    746   -149   1285       O  
ATOM   2606  CG2 THR B  18      -7.502  15.204  -4.355  1.00 89.88           C  
ANISOU 2606  CG2 THR B  18     8965  12799  12384    772   -155   1509       C  
ATOM   2607  N   GLN B  19     -10.886  15.074  -4.376  1.00 88.20           N  
ANISOU 2607  N   GLN B  19     8791  12574  12146    911   -337   1341       N  
ATOM   2608  CA  GLN B  19     -12.113  15.564  -5.056  1.00 88.66           C  
ANISOU 2608  CA  GLN B  19     8866  12692  12128   1000   -393   1366       C  
ATOM   2609  C   GLN B  19     -11.888  16.982  -5.597  1.00 89.81           C  
ANISOU 2609  C   GLN B  19     9060  12823  12237   1028   -356   1557       C  
ATOM   2610  O   GLN B  19     -10.899  17.635  -5.192  1.00 89.63           O  
ANISOU 2610  O   GLN B  19     9064  12708  12282    956   -293   1658       O  
ATOM   2611  CB  GLN B  19     -13.299  15.535  -4.088  1.00 87.17           C  
ANISOU 2611  CB  GLN B  19     8676  12406  12036    995   -459   1282       C  
ATOM   2612  CG  GLN B  19     -13.653  14.145  -3.574  1.00 85.94           C  
ANISOU 2612  CG  GLN B  19     8476  12261  11916    967   -496   1096       C  
ATOM   2613  CD  GLN B  19     -14.344  13.271  -4.593  1.00 86.48           C  
ANISOU 2613  CD  GLN B  19     8509  12492  11856   1034   -544    995       C  
ATOM   2614  OE1 GLN B  19     -14.626  13.682  -5.716  1.00 87.23           O  
ANISOU 2614  OE1 GLN B  19     8607  12711  11825   1110   -557   1059       O  
ATOM   2615  NE2 GLN B  19     -14.635  12.043  -4.196  1.00 86.46           N  
ANISOU 2615  NE2 GLN B  19     8475  12490  11883   1003   -571    834       N  
ATOM   2616  N   VAL B  20     -12.783  17.412  -6.493  1.00 90.03           N  
ANISOU 2616  N   VAL B  20     9100  12945  12162   1128   -394   1605       N  
ATOM   2617  CA  VAL B  20     -12.854  18.779  -7.088  1.00 91.20           C  
ANISOU 2617  CA  VAL B  20     9304  13081  12264   1181   -368   1792       C  
ATOM   2618  C   VAL B  20     -14.318  19.243  -7.009  1.00 91.88           C  
ANISOU 2618  C   VAL B  20     9401  13156  12351   1265   -441   1788       C  
ATOM   2619  O   VAL B  20     -15.125  18.813  -7.862  1.00 93.17           O  
ANISOU 2619  O   VAL B  20     9529  13477  12393   1355   -497   1741       O  
ATOM   2620  CB  VAL B  20     -12.295  18.791  -8.527  1.00 92.38           C  
ANISOU 2620  CB  VAL B  20     9450  13404  12247   1240   -329   1878       C  
ATOM   2621  CG1 VAL B  20     -12.781  17.608  -9.358  1.00 92.06           C  
ANISOU 2621  CG1 VAL B  20     9353  13552  12071   1305   -381   1741       C  
ATOM   2622  CG2 VAL B  20     -12.577  20.104  -9.243  1.00 93.78           C  
ANISOU 2622  CG2 VAL B  20     9684  13588  12359   1315   -312   2066       C  
ATOM   2623  N   VAL B  21     -14.647  20.073  -6.010  1.00 90.95           N  
ANISOU 2623  N   VAL B  21     9329  12863  12364   1238   -440   1832       N  
ATOM   2624  CA  VAL B  21     -16.051  20.432  -5.635  1.00 90.77           C  
ANISOU 2624  CA  VAL B  21     9309  12805  12374   1312   -506   1808       C  
ATOM   2625  C   VAL B  21     -16.458  21.741  -6.324  1.00 92.10           C  
ANISOU 2625  C   VAL B  21     9538  12972  12483   1414   -493   1987       C  
ATOM   2626  O   VAL B  21     -15.732  22.744  -6.171  1.00 91.43           O  
ANISOU 2626  O   VAL B  21     9528  12760  12448   1376   -425   2125       O  
ATOM   2627  CB  VAL B  21     -16.243  20.522  -4.106  1.00 89.41           C  
ANISOU 2627  CB  VAL B  21     9153  12445  12373   1236   -510   1741       C  
ATOM   2628  CG1 VAL B  21     -16.396  19.147  -3.484  1.00 88.40           C  
ANISOU 2628  CG1 VAL B  21     8955  12344  12286   1178   -549   1551       C  
ATOM   2629  CG2 VAL B  21     -15.134  21.297  -3.413  1.00 89.10           C  
ANISOU 2629  CG2 VAL B  21     9182  12234  12438   1136   -435   1832       C  
ATOM   2630  N   ASP B  22     -17.594  21.718  -7.037  1.00 92.55           N  
ANISOU 2630  N   ASP B  22     9562  13165  12438   1536   -558   1983       N  
ATOM   2631  CA  ASP B  22     -18.250  22.904  -7.653  1.00 93.04           C  
ANISOU 2631  CA  ASP B  22     9672  13237  12439   1662   -561   2146       C  
ATOM   2632  C   ASP B  22     -18.714  23.830  -6.521  1.00 92.30           C  
ANISOU 2632  C   ASP B  22     9640  12932  12495   1661   -549   2187       C  
ATOM   2633  O   ASP B  22     -19.331  23.326  -5.560  1.00 90.98           O  
ANISOU 2633  O   ASP B  22     9433  12713  12420   1631   -592   2053       O  
ATOM   2634  CB  ASP B  22     -19.395  22.481  -8.580  1.00 93.42           C  
ANISOU 2634  CB  ASP B  22     9649  13502  12343   1788   -646   2104       C  
ATOM   2635  CG  ASP B  22     -19.723  23.497  -9.660  1.00 95.00           C  
ANISOU 2635  CG  ASP B  22     9890  13784  12419   1926   -639   2289       C  
ATOM   2636  OD1 ASP B  22     -19.950  24.673  -9.314  1.00 94.73           O  
ANISOU 2636  OD1 ASP B  22     9932  13606  12453   1974   -607   2423       O  
ATOM   2637  OD2 ASP B  22     -19.746  23.103 -10.842  1.00 96.30           O  
ANISOU 2637  OD2 ASP B  22    10016  14155  12418   1987   -664   2298       O  
ATOM   2638  N   MET B  23     -18.417  25.127  -6.639  1.00 92.84           N  
ANISOU 2638  N   MET B  23     9807  12881  12584   1691   -488   2365       N  
ATOM   2639  CA  MET B  23     -18.532  26.134  -5.547  1.00 92.36           C  
ANISOU 2639  CA  MET B  23     9836  12582  12674   1666   -452   2418       C  
ATOM   2640  C   MET B  23     -19.991  26.576  -5.372  1.00 92.64           C  
ANISOU 2640  C   MET B  23     9866  12617  12715   1806   -507   2424       C  
ATOM   2641  O   MET B  23     -20.407  26.749  -4.210  1.00 91.78           O  
ANISOU 2641  O   MET B  23     9776  12361  12733   1780   -511   2359       O  
ATOM   2642  CB  MET B  23     -17.651  27.350  -5.847  1.00 93.84           C  
ANISOU 2642  CB  MET B  23    10138  12641  12875   1644   -362   2609       C  
ATOM   2643  CG  MET B  23     -16.204  27.146  -5.458  1.00 93.19           C  
ANISOU 2643  CG  MET B  23    10072  12478  12858   1474   -299   2597       C  
ATOM   2644  SD  MET B  23     -15.964  27.400  -3.684  1.00 92.44           S  
ANISOU 2644  SD  MET B  23    10027  12128  12967   1341   -280   2511       S  
ATOM   2645  CE  MET B  23     -15.949  29.189  -3.604  1.00 93.87           C  
ANISOU 2645  CE  MET B  23    10366  12091  13209   1372   -209   2708       C  
ATOM   2646  N   SER B  24     -20.725  26.766  -6.475  1.00 93.94           N  
ANISOU 2646  N   SER B  24    10003  12948  12742   1953   -545   2502       N  
ATOM   2647  CA  SER B  24     -22.188  27.048  -6.499  1.00 94.92           C  
ANISOU 2647  CA  SER B  24    10091  13132  12840   2106   -609   2506       C  
ATOM   2648  C   SER B  24     -22.946  25.912  -5.808  1.00 93.28           C  
ANISOU 2648  C   SER B  24     9771  12997  12674   2071   -685   2300       C  
ATOM   2649  O   SER B  24     -23.543  26.158  -4.738  1.00 92.53           O  
ANISOU 2649  O   SER B  24     9685  12772  12697   2073   -690   2252       O  
ATOM   2650  CB  SER B  24     -22.691  27.226  -7.905  1.00 97.15           C  
ANISOU 2650  CB  SER B  24    10342  13625  12944   2254   -644   2610       C  
ATOM   2651  OG  SER B  24     -22.130  26.252  -8.777  1.00 96.99           O  
ANISOU 2651  OG  SER B  24    10255  13793  12801   2205   -665   2548       O  
ATOM   2652  N   MET B  25     -22.912  24.721  -6.419  1.00 92.36           N  
ANISOU 2652  N   MET B  25     9555  13077  12459   2039   -738   2185       N  
ATOM   2653  CA  MET B  25     -23.543  23.479  -5.901  1.00 90.33           C  
ANISOU 2653  CA  MET B  25     9187  12904  12228   1987   -808   1982       C  
ATOM   2654  C   MET B  25     -23.025  23.221  -4.482  1.00 87.17           C  
ANISOU 2654  C   MET B  25     8817  12304  11999   1849   -769   1887       C  
ATOM   2655  O   MET B  25     -21.814  23.425  -4.239  1.00 85.44           O  
ANISOU 2655  O   MET B  25     8668  11961  11830   1751   -700   1929       O  
ATOM   2656  CB  MET B  25     -23.219  22.273  -6.792  1.00 90.82           C  
ANISOU 2656  CB  MET B  25     9172  13168  12166   1945   -847   1880       C  
ATOM   2657  CG  MET B  25     -23.869  22.327  -8.166  1.00 92.58           C  
ANISOU 2657  CG  MET B  25     9345  13623  12205   2077   -904   1938       C  
ATOM   2658  SD  MET B  25     -22.984  21.323  -9.386  1.00 92.81           S  
ANISOU 2658  SD  MET B  25     9343  13844  12074   2029   -906   1882       S  
ATOM   2659  CE  MET B  25     -23.361  19.671  -8.799  1.00 91.65           C  
ANISOU 2659  CE  MET B  25     9095  13756  11972   1918   -970   1618       C  
ATOM   2660  N   THR B  26     -23.921  22.805  -3.582  1.00 84.81           N  
ANISOU 2660  N   THR B  26     8461  11982  11780   1843   -812   1769       N  
ATOM   2661  CA  THR B  26     -23.603  22.426  -2.182  1.00 81.03           C  
ANISOU 2661  CA  THR B  26     7996  11337  11453   1720   -786   1662       C  
ATOM   2662  C   THR B  26     -22.748  21.156  -2.205  1.00 78.25           C  
ANISOU 2662  C   THR B  26     7601  11037  11091   1592   -786   1537       C  
ATOM   2663  O   THR B  26     -22.477  20.639  -3.310  1.00 77.46           O  
ANISOU 2663  O   THR B  26     7464  11097  10867   1606   -805   1533       O  
ATOM   2664  CB  THR B  26     -24.882  22.245  -1.354  1.00 80.41           C  
ANISOU 2664  CB  THR B  26     7855  11254  11441   1761   -834   1572       C  
ATOM   2665  OG1 THR B  26     -25.689  21.263  -2.004  1.00 80.63           O  
ANISOU 2665  OG1 THR B  26     7762  11498  11374   1792   -913   1472       O  
ATOM   2666  CG2 THR B  26     -25.669  23.528  -1.195  1.00 81.24           C  
ANISOU 2666  CG2 THR B  26     8011  11286  11570   1894   -822   1695       C  
ATOM   2667  N   TYR B  27     -22.342  20.679  -1.029  1.00 76.15           N  
ANISOU 2667  N   TYR B  27     7342  10642  10948   1477   -764   1440       N  
ATOM   2668  CA  TYR B  27     -21.657  19.374  -0.853  1.00 74.92           C  
ANISOU 2668  CA  TYR B  27     7141  10522  10800   1363   -765   1307       C  
ATOM   2669  C   TYR B  27     -22.615  18.255  -1.279  1.00 75.33           C  
ANISOU 2669  C   TYR B  27     7088  10749  10785   1387   -841   1173       C  
ATOM   2670  O   TYR B  27     -22.308  17.551  -2.262  1.00 75.50           O  
ANISOU 2670  O   TYR B  27     7074  10913  10696   1385   -859   1137       O  
ATOM   2671  CB  TYR B  27     -21.151  19.224   0.585  1.00 73.03           C  
ANISOU 2671  CB  TYR B  27     6934  10104  10707   1252   -728   1246       C  
ATOM   2672  CG  TYR B  27     -19.842  19.926   0.847  1.00 72.55           C  
ANISOU 2672  CG  TYR B  27     6961   9909  10695   1183   -655   1343       C  
ATOM   2673  CD1 TYR B  27     -19.756  20.983   1.740  1.00 72.33           C  
ANISOU 2673  CD1 TYR B  27     7013   9701  10767   1168   -618   1412       C  
ATOM   2674  CD2 TYR B  27     -18.685  19.543   0.183  1.00 72.50           C  
ANISOU 2674  CD2 TYR B  27     6955   9959  10631   1130   -623   1366       C  
ATOM   2675  CE1 TYR B  27     -18.552  21.632   1.977  1.00 72.31           C  
ANISOU 2675  CE1 TYR B  27     7087   9577  10807   1089   -554   1496       C  
ATOM   2676  CE2 TYR B  27     -17.473  20.179   0.410  1.00 72.25           C  
ANISOU 2676  CE2 TYR B  27     6991   9817  10643   1057   -557   1457       C  
ATOM   2677  CZ  TYR B  27     -17.406  21.228   1.311  1.00 71.99           C  
ANISOU 2677  CZ  TYR B  27     7035   9605  10712   1030   -525   1521       C  
ATOM   2678  OH  TYR B  27     -16.222  21.865   1.535  1.00 71.19           O  
ANISOU 2678  OH  TYR B  27     6996   9397  10653    945   -464   1606       O  
ATOM   2679  N   GLY B  28     -23.753  18.142  -0.585  1.00 76.02           N  
ANISOU 2679  N   GLY B  28     7126  10827  10930   1411   -882   1106       N  
ATOM   2680  CA  GLY B  28     -24.799  17.122  -0.806  1.00 76.66           C  
ANISOU 2680  CA  GLY B  28     7100  11060  10967   1420   -956    972       C  
ATOM   2681  C   GLY B  28     -24.959  16.738  -2.268  1.00 78.32           C  
ANISOU 2681  C   GLY B  28     7262  11480  11015   1474  -1003    969       C  
ATOM   2682  O   GLY B  28     -24.815  15.541  -2.577  1.00 77.65           O  
ANISOU 2682  O   GLY B  28     7130  11483  10890   1409  -1028    841       O  
ATOM   2683  N   GLN B  29     -25.212  17.719  -3.141  1.00 80.56           N  
ANISOU 2683  N   GLN B  29     7564  11836  11206   1592  -1012   1107       N  
ATOM   2684  CA  GLN B  29     -25.622  17.516  -4.560  1.00 83.22           C  
ANISOU 2684  CA  GLN B  29     7847  12399  11372   1672  -1070   1118       C  
ATOM   2685  C   GLN B  29     -24.710  16.497  -5.258  1.00 83.58           C  
ANISOU 2685  C   GLN B  29     7892  12525  11337   1597  -1061   1036       C  
ATOM   2686  O   GLN B  29     -25.158  15.885  -6.245  1.00 84.65           O  
ANISOU 2686  O   GLN B  29     7966  12856  11341   1628  -1122    973       O  
ATOM   2687  CB  GLN B  29     -25.617  18.851  -5.308  1.00 84.71           C  
ANISOU 2687  CB  GLN B  29     8092  12608  11485   1801  -1052   1313       C  
ATOM   2688  CG  GLN B  29     -26.768  19.766  -4.914  1.00 85.46           C  
ANISOU 2688  CG  GLN B  29     8170  12680  11619   1913  -1077   1387       C  
ATOM   2689  CD  GLN B  29     -26.617  21.161  -5.469  1.00 86.96           C  
ANISOU 2689  CD  GLN B  29     8442  12835  11763   2034  -1039   1592       C  
ATOM   2690  OE1 GLN B  29     -26.308  22.106  -4.746  1.00 86.41           O  
ANISOU 2690  OE1 GLN B  29     8463  12569  11797   2041   -975   1687       O  
ATOM   2691  NE2 GLN B  29     -26.838  21.302  -6.766  1.00 88.66           N  
ANISOU 2691  NE2 GLN B  29     8631  13240  11816   2132  -1077   1663       N  
ATOM   2692  N   GLN B  30     -23.487  16.307  -4.760  1.00 83.90           N  
ANISOU 2692  N   GLN B  30     7997  12428  11452   1504   -990   1034       N  
ATOM   2693  CA  GLN B  30     -22.427  15.522  -5.447  1.00 84.81           C  
ANISOU 2693  CA  GLN B  30     8127  12606  11491   1450   -961    988       C  
ATOM   2694  C   GLN B  30     -21.874  14.417  -4.532  1.00 84.28           C  
ANISOU 2694  C   GLN B  30     8055  12437  11529   1325   -936    846       C  
ATOM   2695  O   GLN B  30     -21.233  13.499  -5.085  1.00 85.27           O  
ANISOU 2695  O   GLN B  30     8175  12634  11590   1286   -925    768       O  
ATOM   2696  CB  GLN B  30     -21.341  16.474  -5.958  1.00 85.26           C  
ANISOU 2696  CB  GLN B  30     8263  12620  11509   1478   -889   1158       C  
ATOM   2697  CG  GLN B  30     -21.289  17.811  -5.222  1.00 85.64           C  
ANISOU 2697  CG  GLN B  30     8379  12497  11662   1500   -846   1302       C  
ATOM   2698  CD  GLN B  30     -20.750  18.940  -6.066  1.00 87.61           C  
ANISOU 2698  CD  GLN B  30     8695  12758  11833   1570   -800   1491       C  
ATOM   2699  OE1 GLN B  30     -20.853  18.930  -7.291  1.00 89.32           O  
ANISOU 2699  OE1 GLN B  30     8894  13144  11899   1646   -822   1535       O  
ATOM   2700  NE2 GLN B  30     -20.180  19.938  -5.409  1.00 87.35           N  
ANISOU 2700  NE2 GLN B  30     8742  12543  11902   1543   -736   1605       N  
ATOM   2701  N   PHE B  31     -22.116  14.478  -3.211  1.00 83.33           N  
ANISOU 2701  N   PHE B  31     7939  12163  11559   1271   -925    814       N  
ATOM   2702  CA  PHE B  31     -21.614  13.500  -2.204  1.00 81.70           C  
ANISOU 2702  CA  PHE B  31     7732  11847  11462   1158   -897    694       C  
ATOM   2703  C   PHE B  31     -22.703  13.054  -1.214  1.00 80.90           C  
ANISOU 2703  C   PHE B  31     7580  11702  11456   1127   -938    588       C  
ATOM   2704  O   PHE B  31     -22.353  12.314  -0.268  1.00 80.27           O  
ANISOU 2704  O   PHE B  31     7504  11518  11475   1037   -913    501       O  
ATOM   2705  CB  PHE B  31     -20.461  14.096  -1.392  1.00 81.16           C  
ANISOU 2705  CB  PHE B  31     7736  11606  11494   1105   -820    781       C  
ATOM   2706  CG  PHE B  31     -19.281  14.595  -2.188  1.00 81.90           C  
ANISOU 2706  CG  PHE B  31     7880  11722  11517   1117   -766    896       C  
ATOM   2707  CD1 PHE B  31     -18.754  13.853  -3.235  1.00 82.81           C  
ANISOU 2707  CD1 PHE B  31     7978  11969  11515   1124   -762    857       C  
ATOM   2708  CD2 PHE B  31     -18.667  15.792  -1.857  1.00 82.03           C  
ANISOU 2708  CD2 PHE B  31     7961  11620  11585   1116   -714   1040       C  
ATOM   2709  CE1 PHE B  31     -17.658  14.312  -3.951  1.00 83.14           C  
ANISOU 2709  CE1 PHE B  31     8059  12038  11491   1136   -705    968       C  
ATOM   2710  CE2 PHE B  31     -17.571  16.247  -2.570  1.00 82.46           C  
ANISOU 2710  CE2 PHE B  31     8055  11696  11579   1116   -659   1151       C  
ATOM   2711  CZ  PHE B  31     -17.068  15.508  -3.616  1.00 83.06           C  
ANISOU 2711  CZ  PHE B  31     8105  11915  11536   1129   -654   1118       C  
ATOM   2712  N   GLY B  32     -23.962  13.463  -1.403  1.00 81.70           N  
ANISOU 2712  N   GLY B  32     7629  11883  11528   1199   -997    599       N  
ATOM   2713  CA  GLY B  32     -25.071  13.150  -0.478  1.00 81.23           C  
ANISOU 2713  CA  GLY B  32     7510  11795  11557   1176  -1032    513       C  
ATOM   2714  C   GLY B  32     -24.718  13.526   0.960  1.00 79.99           C  
ANISOU 2714  C   GLY B  32     7404  11436  11550   1125   -977    536       C  
ATOM   2715  O   GLY B  32     -24.243  14.632   1.207  1.00 80.35           O  
ANISOU 2715  O   GLY B  32     7519  11382  11629   1159   -935    661       O  
ATOM   2716  N   PRO B  33     -24.924  12.631   1.955  1.00 79.19           N  
ANISOU 2716  N   PRO B  33     7276  11268  11544   1039   -974    418       N  
ATOM   2717  CA  PRO B  33     -24.497  12.902   3.329  1.00 78.01           C  
ANISOU 2717  CA  PRO B  33     7177  10936  11527    985   -921    434       C  
ATOM   2718  C   PRO B  33     -23.008  13.276   3.382  1.00 75.98           C  
ANISOU 2718  C   PRO B  33     7005  10579  11283    950   -859    512       C  
ATOM   2719  O   PRO B  33     -22.200  12.485   2.939  1.00 74.72           O  
ANISOU 2719  O   PRO B  33     6849  10454  11085    905   -844    467       O  
ATOM   2720  CB  PRO B  33     -24.772  11.587   4.075  1.00 77.79           C  
ANISOU 2720  CB  PRO B  33     7104  10886  11564    892   -928    286       C  
ATOM   2721  CG  PRO B  33     -25.872  10.933   3.266  1.00 78.83           C  
ANISOU 2721  CG  PRO B  33     7145  11186  11617    913   -997    200       C  
ATOM   2722  CD  PRO B  33     -25.591  11.327   1.828  1.00 79.81           C  
ANISOU 2722  CD  PRO B  33     7278  11440  11606    985  -1020    265       C  
ATOM   2723  N   THR B  34     -22.708  14.481   3.881  1.00 75.11           N  
ANISOU 2723  N   THR B  34     6960  10355  11224    974   -823    625       N  
ATOM   2724  CA  THR B  34     -21.347  15.079   3.958  1.00 74.66           C  
ANISOU 2724  CA  THR B  34     6982  10201  11184    938   -764    718       C  
ATOM   2725  C   THR B  34     -21.158  15.696   5.350  1.00 73.68           C  
ANISOU 2725  C   THR B  34     6911   9901  11180    894   -727    741       C  
ATOM   2726  O   THR B  34     -22.086  16.387   5.812  1.00 74.59           O  
ANISOU 2726  O   THR B  34     7031   9974  11333    948   -740    764       O  
ATOM   2727  CB  THR B  34     -21.133  16.120   2.849  1.00 75.15           C  
ANISOU 2727  CB  THR B  34     7081  10315  11157   1018   -757    855       C  
ATOM   2728  OG1 THR B  34     -21.888  15.737   1.698  1.00 75.05           O  
ANISOU 2728  OG1 THR B  34     7007  10479  11030   1089   -810    829       O  
ATOM   2729  CG2 THR B  34     -19.674  16.283   2.478  1.00 74.82           C  
ANISOU 2729  CG2 THR B  34     7089  10246  11093    969   -703    925       C  
ATOM   2730  N   TYR B  35     -20.005  15.459   5.986  1.00 72.40           N  
ANISOU 2730  N   TYR B  35     6785   9649  11073    804   -684    735       N  
ATOM   2731  CA  TYR B  35     -19.731  15.842   7.397  1.00 71.45           C  
ANISOU 2731  CA  TYR B  35     6710   9372  11063    744   -654    733       C  
ATOM   2732  C   TYR B  35     -18.321  16.444   7.537  1.00 72.28           C  
ANISOU 2732  C   TYR B  35     6879   9394  11187    682   -605    817       C  
ATOM   2733  O   TYR B  35     -17.364  15.927   6.913  1.00 71.91           O  
ANISOU 2733  O   TYR B  35     6817   9409  11094    649   -588    825       O  
ATOM   2734  CB  TYR B  35     -19.918  14.625   8.306  1.00 69.77           C  
ANISOU 2734  CB  TYR B  35     6453   9147  10908    682   -662    606       C  
ATOM   2735  CG  TYR B  35     -21.270  13.961   8.217  1.00 69.47           C  
ANISOU 2735  CG  TYR B  35     6345   9191  10859    722   -707    518       C  
ATOM   2736  CD1 TYR B  35     -22.308  14.341   9.053  1.00 69.12           C  
ANISOU 2736  CD1 TYR B  35     6292   9097  10872    749   -717    500       C  
ATOM   2737  CD2 TYR B  35     -21.514  12.944   7.306  1.00 69.22           C  
ANISOU 2737  CD2 TYR B  35     6252   9289  10756    729   -738    448       C  
ATOM   2738  CE1 TYR B  35     -23.552  13.735   8.985  1.00 68.81           C  
ANISOU 2738  CE1 TYR B  35     6176   9144  10824    779   -758    422       C  
ATOM   2739  CE2 TYR B  35     -22.752  12.327   7.223  1.00 69.13           C  
ANISOU 2739  CE2 TYR B  35     6171   9358  10735    750   -783    362       C  
ATOM   2740  CZ  TYR B  35     -23.777  12.722   8.067  1.00 69.31           C  
ANISOU 2740  CZ  TYR B  35     6175   9338  10819    773   -793    353       C  
ATOM   2741  OH  TYR B  35     -25.002  12.119   7.993  1.00 69.39           O  
ANISOU 2741  OH  TYR B  35     6104   9438  10822    787   -836    272       O  
ATOM   2742  N   LEU B  36     -18.210  17.517   8.333  1.00 72.79           N  
ANISOU 2742  N   LEU B  36     7014   9324  11318    665   -580    876       N  
ATOM   2743  CA  LEU B  36     -16.937  18.159   8.761  1.00 73.28           C  
ANISOU 2743  CA  LEU B  36     7138   9285  11419    582   -536    944       C  
ATOM   2744  C   LEU B  36     -16.878  18.134  10.293  1.00 72.58           C  
ANISOU 2744  C   LEU B  36     7073   9075  11426    513   -527    884       C  
ATOM   2745  O   LEU B  36     -17.489  19.016  10.927  1.00 72.17           O  
ANISOU 2745  O   LEU B  36     7077   8923  11421    538   -523    903       O  
ATOM   2746  CB  LEU B  36     -16.878  19.592   8.215  1.00 75.01           C  
ANISOU 2746  CB  LEU B  36     7433   9448  11620    623   -513   1075       C  
ATOM   2747  CG  LEU B  36     -15.625  20.396   8.575  1.00 75.63           C  
ANISOU 2747  CG  LEU B  36     7579   9418  11738    529   -467   1153       C  
ATOM   2748  CD1 LEU B  36     -14.358  19.666   8.151  1.00 75.58           C  
ANISOU 2748  CD1 LEU B  36     7525   9492  11698    457   -448   1155       C  
ATOM   2749  CD2 LEU B  36     -15.669  21.784   7.952  1.00 76.75           C  
ANISOU 2749  CD2 LEU B  36     7803   9498  11861    574   -441   1285       C  
ATOM   2750  N   ASP B  37     -16.170  17.147  10.853  1.00 72.69           N  
ANISOU 2750  N   ASP B  37     7050   9102  11464    437   -522    817       N  
ATOM   2751  CA  ASP B  37     -16.108  16.847  12.311  1.00 72.01           C  
ANISOU 2751  CA  ASP B  37     6973   8930  11457    374   -518    748       C  
ATOM   2752  C   ASP B  37     -17.536  16.667  12.850  1.00 71.54           C  
ANISOU 2752  C   ASP B  37     6897   8858  11424    432   -543    679       C  
ATOM   2753  O   ASP B  37     -17.859  17.261  13.898  1.00 71.07           O  
ANISOU 2753  O   ASP B  37     6885   8695  11423    420   -534    669       O  
ATOM   2754  CB  ASP B  37     -15.306  17.914  13.067  1.00 72.35           C  
ANISOU 2754  CB  ASP B  37     7091   8850  11549    302   -491    806       C  
ATOM   2755  CG  ASP B  37     -13.810  17.656  13.081  1.00 71.74           C  
ANISOU 2755  CG  ASP B  37     6999   8789  11467    209   -469    834       C  
ATOM   2756  OD1 ASP B  37     -13.421  16.490  13.282  1.00 71.00           O  
ANISOU 2756  OD1 ASP B  37     6845   8760  11371    185   -474    773       O  
ATOM   2757  OD2 ASP B  37     -13.049  18.623  12.890  1.00 72.27           O  
ANISOU 2757  OD2 ASP B  37     7115   8807  11537    163   -446    919       O  
ATOM   2758  N   GLY B  38     -18.357  15.877  12.147  1.00 71.70           N  
ANISOU 2758  N   GLY B  38     6852   8986  11401    490   -571    630       N  
ATOM   2759  CA  GLY B  38     -19.709  15.465  12.580  1.00 71.53           C  
ANISOU 2759  CA  GLY B  38     6791   8985  11403    536   -596    555       C  
ATOM   2760  C   GLY B  38     -20.783  16.451  12.151  1.00 72.54           C  
ANISOU 2760  C   GLY B  38     6932   9118  11511    634   -610    605       C  
ATOM   2761  O   GLY B  38     -21.914  16.004  11.855  1.00 72.63           O  
ANISOU 2761  O   GLY B  38     6879   9214  11501    691   -642    557       O  
ATOM   2762  N   ALA B  39     -20.454  17.747  12.144  1.00 72.96           N  
ANISOU 2762  N   ALA B  39     7065   9083  11572    652   -587    699       N  
ATOM   2763  CA  ALA B  39     -21.329  18.850  11.685  1.00 73.63           C  
ANISOU 2763  CA  ALA B  39     7181   9157  11637    758   -592    770       C  
ATOM   2764  C   ALA B  39     -21.782  18.576  10.245  1.00 73.82           C  
ANISOU 2764  C   ALA B  39     7144   9332  11570    834   -626    796       C  
ATOM   2765  O   ALA B  39     -21.031  18.906   9.306  1.00 73.85           O  
ANISOU 2765  O   ALA B  39     7173   9365  11519    835   -617    874       O  
ATOM   2766  CB  ALA B  39     -20.606  20.170  11.811  1.00 74.42           C  
ANISOU 2766  CB  ALA B  39     7390   9127  11759    743   -554    869       C  
ATOM   2767  N   ASP B  40     -22.959  17.960  10.100  1.00 73.17           N  
ANISOU 2767  N   ASP B  40     6980   9350  11469    889   -665    730       N  
ATOM   2768  CA  ASP B  40     -23.646  17.702   8.806  1.00 73.50           C  
ANISOU 2768  CA  ASP B  40     6953   9553  11418    970   -709    740       C  
ATOM   2769  C   ASP B  40     -23.559  18.965   7.937  1.00 74.58           C  
ANISOU 2769  C   ASP B  40     7149   9682  11503   1057   -699    876       C  
ATOM   2770  O   ASP B  40     -24.140  19.991   8.329  1.00 74.92           O  
ANISOU 2770  O   ASP B  40     7239   9645  11579   1128   -685    933       O  
ATOM   2771  CB  ASP B  40     -25.092  17.266   9.061  1.00 73.23           C  
ANISOU 2771  CB  ASP B  40     6833   9597  11393   1022   -747    666       C  
ATOM   2772  CG  ASP B  40     -25.834  16.736   7.845  1.00 73.49           C  
ANISOU 2772  CG  ASP B  40     6774   9815  11331   1081   -804    645       C  
ATOM   2773  OD1 ASP B  40     -25.589  17.244   6.733  1.00 74.44           O  
ANISOU 2773  OD1 ASP B  40     6913  10000  11371   1140   -814    728       O  
ATOM   2774  OD2 ASP B  40     -26.659  15.819   8.025  1.00 72.21           O  
ANISOU 2774  OD2 ASP B  40     6523   9735  11175   1063   -837    545       O  
ATOM   2775  N   VAL B  41     -22.848  18.890   6.809  1.00 75.53           N  
ANISOU 2775  N   VAL B  41     7273   9880  11544   1055   -701    928       N  
ATOM   2776  CA  VAL B  41     -22.654  20.027   5.858  1.00 78.11           C  
ANISOU 2776  CA  VAL B  41     7658  10208  11809   1134   -686   1070       C  
ATOM   2777  C   VAL B  41     -23.329  19.689   4.521  1.00 80.21           C  
ANISOU 2777  C   VAL B  41     7850  10668  11958   1224   -737   1079       C  
ATOM   2778  O   VAL B  41     -23.029  20.378   3.519  1.00 80.99           O  
ANISOU 2778  O   VAL B  41     7986  10805  11982   1283   -728   1193       O  
ATOM   2779  CB  VAL B  41     -21.160  20.368   5.669  1.00 78.37           C  
ANISOU 2779  CB  VAL B  41     7763  10168  11844   1053   -637   1142       C  
ATOM   2780  CG1 VAL B  41     -20.578  21.085   6.879  1.00 77.94           C  
ANISOU 2780  CG1 VAL B  41     7798   9921  11895    981   -589   1161       C  
ATOM   2781  CG2 VAL B  41     -20.327  19.145   5.316  1.00 77.76           C  
ANISOU 2781  CG2 VAL B  41     7632  10182  11730    971   -642   1069       C  
ATOM   2782  N   THR B  42     -24.223  18.691   4.505  1.00 81.59           N  
ANISOU 2782  N   THR B  42     7925  10961  12114   1232   -789    966       N  
ATOM   2783  CA  THR B  42     -24.991  18.253   3.304  1.00 83.33           C  
ANISOU 2783  CA  THR B  42     8060  11381  12218   1307   -850    950       C  
ATOM   2784  C   THR B  42     -25.693  19.466   2.677  1.00 85.09           C  
ANISOU 2784  C   THR B  42     8303  11639  12388   1450   -861   1080       C  
ATOM   2785  O   THR B  42     -25.647  19.593   1.433  1.00 84.59           O  
ANISOU 2785  O   THR B  42     8226  11704  12209   1513   -884   1142       O  
ATOM   2786  CB  THR B  42     -25.993  17.143   3.651  1.00 83.00           C  
ANISOU 2786  CB  THR B  42     7911  11432  12192   1283   -902    806       C  
ATOM   2787  OG1 THR B  42     -25.276  16.072   4.265  1.00 81.89           O  
ANISOU 2787  OG1 THR B  42     7769  11239  12106   1156   -882    700       O  
ATOM   2788  CG2 THR B  42     -26.744  16.616   2.446  1.00 83.95           C  
ANISOU 2788  CG2 THR B  42     7939  11765  12191   1340   -970    772       C  
ATOM   2789  N   LYS B  43     -26.284  20.329   3.514  1.00 86.72           N  
ANISOU 2789  N   LYS B  43     8546  11731  12672   1504   -841   1121       N  
ATOM   2790  CA  LYS B  43     -27.132  21.481   3.097  1.00 89.20           C  
ANISOU 2790  CA  LYS B  43     8877  12064  12949   1658   -848   1239       C  
ATOM   2791  C   LYS B  43     -26.280  22.735   2.842  1.00 90.16           C  
ANISOU 2791  C   LYS B  43     9132  12051  13074   1687   -787   1394       C  
ATOM   2792  O   LYS B  43     -26.806  23.653   2.184  1.00 92.85           O  
ANISOU 2792  O   LYS B  43     9496  12423  13359   1822   -790   1513       O  
ATOM   2793  CB  LYS B  43     -28.221  21.759   4.142  1.00 89.78           C  
ANISOU 2793  CB  LYS B  43     8924  12081  13106   1711   -850   1203       C  
ATOM   2794  CG  LYS B  43     -29.495  20.937   3.982  1.00 90.38           C  
ANISOU 2794  CG  LYS B  43     8853  12341  13144   1750   -920   1108       C  
ATOM   2795  CD  LYS B  43     -30.619  21.360   4.906  1.00 90.90           C  
ANISOU 2795  CD  LYS B  43     8888  12367  13281   1826   -916   1095       C  
ATOM   2796  CE  LYS B  43     -31.906  20.606   4.649  1.00 91.42           C  
ANISOU 2796  CE  LYS B  43     8794  12636  13303   1866   -987   1014       C  
ATOM   2797  NZ  LYS B  43     -32.735  20.516   5.873  1.00 91.46           N  
ANISOU 2797  NZ  LYS B  43     8756  12590  13404   1866   -972    948       N  
ATOM   2798  N   ILE B  44     -25.031  22.789   3.325  1.00 89.25           N  
ANISOU 2798  N   ILE B  44     9098  11793  13018   1567   -732   1397       N  
ATOM   2799  CA  ILE B  44     -24.125  23.967   3.138  1.00 89.51           C  
ANISOU 2799  CA  ILE B  44     9260  11686  13064   1567   -669   1540       C  
ATOM   2800  C   ILE B  44     -23.193  23.695   1.947  1.00 90.18           C  
ANISOU 2800  C   ILE B  44     9341  11873  13049   1535   -664   1595       C  
ATOM   2801  O   ILE B  44     -23.104  22.525   1.515  1.00 88.52           O  
ANISOU 2801  O   ILE B  44     9041  11809  12781   1492   -704   1499       O  
ATOM   2802  CB  ILE B  44     -23.369  24.323   4.439  1.00 87.90           C  
ANISOU 2802  CB  ILE B  44     9145  11265  12985   1454   -613   1516       C  
ATOM   2803  CG1 ILE B  44     -22.061  23.548   4.610  1.00 86.83           C  
ANISOU 2803  CG1 ILE B  44     9004  11118  12866   1299   -594   1460       C  
ATOM   2804  CG2 ILE B  44     -24.273  24.170   5.653  1.00 86.97           C  
ANISOU 2804  CG2 ILE B  44     9003  11087  12952   1467   -624   1419       C  
ATOM   2805  CD1 ILE B  44     -20.827  24.365   4.322  1.00 87.24           C  
ANISOU 2805  CD1 ILE B  44     9156  11068  12923   1240   -535   1576       C  
ATOM   2806  N   LYS B  45     -22.535  24.745   1.439  1.00 92.14           N  
ANISOU 2806  N   LYS B  45     9687  12043  13277   1557   -613   1744       N  
ATOM   2807  CA  LYS B  45     -21.835  24.752   0.125  1.00 93.61           C  
ANISOU 2807  CA  LYS B  45     9876  12342  13349   1567   -603   1835       C  
ATOM   2808  C   LYS B  45     -20.334  24.949   0.318  1.00 93.77           C  
ANISOU 2808  C   LYS B  45     9966  12247  13412   1433   -536   1877       C  
ATOM   2809  O   LYS B  45     -19.910  25.559   1.297  1.00 92.73           O  
ANISOU 2809  O   LYS B  45     9914  11926  13391   1362   -492   1890       O  
ATOM   2810  CB  LYS B  45     -22.418  25.847  -0.774  1.00 95.22           C  
ANISOU 2810  CB  LYS B  45    10127  12574  13477   1721   -598   1995       C  
ATOM   2811  CG  LYS B  45     -21.988  27.271  -0.444  1.00 95.42           C  
ANISOU 2811  CG  LYS B  45    10295  12385  13572   1729   -524   2138       C  
ATOM   2812  CD  LYS B  45     -22.920  28.324  -1.007  1.00 96.43           C  
ANISOU 2812  CD  LYS B  45    10469  12516  13653   1908   -524   2275       C  
ATOM   2813  CE  LYS B  45     -22.191  29.551  -1.509  1.00 97.36           C  
ANISOU 2813  CE  LYS B  45    10720  12507  13763   1922   -448   2460       C  
ATOM   2814  NZ  LYS B  45     -23.131  30.644  -1.853  1.00 98.86           N  
ANISOU 2814  NZ  LYS B  45    10971  12660  13928   2103   -440   2594       N  
ATOM   2815  N   PRO B  46     -19.492  24.466  -0.628  1.00 95.43           N  
ANISOU 2815  N   PRO B  46    10148  12576  13533   1395   -526   1902       N  
ATOM   2816  CA  PRO B  46     -18.036  24.538  -0.482  1.00 96.37           C  
ANISOU 2816  CA  PRO B  46    10311  12616  13688   1264   -464   1937       C  
ATOM   2817  C   PRO B  46     -17.557  25.969  -0.186  1.00 98.83           C  
ANISOU 2817  C   PRO B  46    10749  12734  14067   1243   -397   2080       C  
ATOM   2818  O   PRO B  46     -17.616  26.805  -1.072  1.00101.56           O  
ANISOU 2818  O   PRO B  46    11148  13093  14347   1323   -372   2225       O  
ATOM   2819  CB  PRO B  46     -17.502  24.018  -1.829  1.00 96.57           C  
ANISOU 2819  CB  PRO B  46    10289  12827  13576   1283   -463   1975       C  
ATOM   2820  CG  PRO B  46     -18.623  23.150  -2.364  1.00 96.23           C  
ANISOU 2820  CG  PRO B  46    10151  12966  13444   1379   -542   1878       C  
ATOM   2821  CD  PRO B  46     -19.893  23.831  -1.895  1.00 96.31           C  
ANISOU 2821  CD  PRO B  46    10181  12914  13499   1478   -574   1895       C  
ATOM   2822  N   HIS B  47     -17.121  26.207   1.057  1.00 99.47           N  
ANISOU 2822  N   HIS B  47    10879  12640  14275   1135   -370   2035       N  
ATOM   2823  CA  HIS B  47     -16.660  27.520   1.592  1.00100.80           C  
ANISOU 2823  CA  HIS B  47    11175  12593  14529   1086   -308   2138       C  
ATOM   2824  C   HIS B  47     -15.126  27.612   1.495  1.00100.53           C  
ANISOU 2824  C   HIS B  47    11162  12524  14509    938   -251   2191       C  
ATOM   2825  O   HIS B  47     -14.499  26.632   1.024  1.00100.97           O  
ANISOU 2825  O   HIS B  47    11130  12728  14506    893   -261   2146       O  
ATOM   2826  CB  HIS B  47     -17.198  27.718   3.021  1.00101.27           C  
ANISOU 2826  CB  HIS B  47    11272  12495  14708   1062   -318   2045       C  
ATOM   2827  CG  HIS B  47     -17.505  29.138   3.377  1.00103.29           C  
ANISOU 2827  CG  HIS B  47    11663  12555  15026   1104   -275   2144       C  
ATOM   2828  ND1 HIS B  47     -18.623  29.799   2.898  1.00103.99           N  
ANISOU 2828  ND1 HIS B  47    11785  12647  15076   1273   -284   2220       N  
ATOM   2829  CD2 HIS B  47     -16.858  30.019   4.173  1.00103.58           C  
ANISOU 2829  CD2 HIS B  47    11812  12383  15158   1003   -222   2176       C  
ATOM   2830  CE1 HIS B  47     -18.643  31.028   3.374  1.00104.76           C  
ANISOU 2830  CE1 HIS B  47    12018  12537  15246   1280   -232   2298       C  
ATOM   2831  NE2 HIS B  47     -17.570  31.189   4.158  1.00104.52           N  
ANISOU 2831  NE2 HIS B  47    12041  12370  15299   1110   -195   2268       N  
ATOM   2832  N   ASN B  48     -14.552  28.747   1.923  1.00 99.34           N  
ANISOU 2832  N   ASN B  48    11125  12186  14435    866   -193   2282       N  
ATOM   2833  CA  ASN B  48     -13.136  29.155   1.689  1.00 96.95           C  
ANISOU 2833  CA  ASN B  48    10855  11838  14142    730   -129   2373       C  
ATOM   2834  C   ASN B  48     -12.204  28.410   2.649  1.00 93.38           C  
ANISOU 2834  C   ASN B  48    10346  11375  13759    571   -134   2256       C  
ATOM   2835  O   ASN B  48     -11.202  27.848   2.175  1.00 92.60           O  
ANISOU 2835  O   ASN B  48    10179  11387  13616    498   -115   2269       O  
ATOM   2836  CB  ASN B  48     -12.946  30.666   1.854  1.00 97.95           C  
ANISOU 2836  CB  ASN B  48    11130  11753  14332    703    -66   2505       C  
ATOM   2837  CG  ASN B  48     -13.890  31.484   0.996  1.00 98.99           C  
ANISOU 2837  CG  ASN B  48    11330  11876  14403    873    -57   2631       C  
ATOM   2838  OD1 ASN B  48     -14.703  32.249   1.513  1.00 98.49           O  
ANISOU 2838  OD1 ASN B  48    11357  11667  14397    944    -55   2642       O  
ATOM   2839  ND2 ASN B  48     -13.799  31.320  -0.313  1.00 99.74           N  
ANISOU 2839  ND2 ASN B  48    11384  12132  14377    946    -50   2727       N  
ATOM   2840  N   SER B  49     -12.524  28.443   3.946  1.00 91.65           N  
ANISOU 2840  N   SER B  49    10154  11027  13639    526   -154   2154       N  
ATOM   2841  CA  SER B  49     -11.825  27.723   5.046  1.00 90.37           C  
ANISOU 2841  CA  SER B  49     9940  10849  13546    390   -169   2031       C  
ATOM   2842  C   SER B  49     -11.434  26.311   4.594  1.00 89.64           C  
ANISOU 2842  C   SER B  49     9713  10959  13385    387   -196   1958       C  
ATOM   2843  O   SER B  49     -10.251  25.954   4.729  1.00 89.32           O  
ANISOU 2843  O   SER B  49     9628  10952  13355    269   -174   1955       O  
ATOM   2844  CB  SER B  49     -12.699  27.651   6.275  1.00 89.31           C  
ANISOU 2844  CB  SER B  49     9829  10615  13487    411   -206   1914       C  
ATOM   2845  OG  SER B  49     -13.933  28.323   6.062  1.00 89.90           O  
ANISOU 2845  OG  SER B  49     9968  10635  13554    553   -213   1953       O  
ATOM   2846  N   HIS B  50     -12.410  25.567   4.059  1.00 89.88           N  
ANISOU 2846  N   HIS B  50     9683  11118  13347    514   -242   1904       N  
ATOM   2847  CA  HIS B  50     -12.403  24.091   3.859  1.00 88.91           C  
ANISOU 2847  CA  HIS B  50     9442  11164  13173    528   -281   1791       C  
ATOM   2848  C   HIS B  50     -11.159  23.626   3.089  1.00 89.90           C  
ANISOU 2848  C   HIS B  50     9513  11407  13237    468   -246   1836       C  
ATOM   2849  O   HIS B  50     -10.478  22.715   3.587  1.00 88.67           O  
ANISOU 2849  O   HIS B  50     9291  11293  13104    392   -249   1751       O  
ATOM   2850  CB  HIS B  50     -13.688  23.639   3.146  1.00 88.87           C  
ANISOU 2850  CB  HIS B  50     9398  11277  13091    676   -330   1756       C  
ATOM   2851  CG  HIS B  50     -14.944  23.898   3.912  1.00 88.08           C  
ANISOU 2851  CG  HIS B  50     9325  11093  13046    742   -367   1699       C  
ATOM   2852  ND1 HIS B  50     -16.124  24.259   3.292  1.00 88.24           N  
ANISOU 2852  ND1 HIS B  50     9353  11160  13013    881   -394   1736       N  
ATOM   2853  CD2 HIS B  50     -15.214  23.851   5.235  1.00 86.88           C  
ANISOU 2853  CD2 HIS B  50     9190  10825  12993    694   -378   1610       C  
ATOM   2854  CE1 HIS B  50     -17.066  24.420   4.197  1.00 87.44           C  
ANISOU 2854  CE1 HIS B  50     9268  10975  12979    918   -419   1673       C  
ATOM   2855  NE2 HIS B  50     -16.535  24.176   5.398  1.00 86.68           N  
ANISOU 2855  NE2 HIS B  50     9181  10775  12975    803   -408   1594       N  
ATOM   2856  N   GLU B  51     -10.886  24.220   1.922  1.00 92.83           N  
ANISOU 2856  N   GLU B  51     9908  11832  13529    508   -209   1968       N  
ATOM   2857  CA  GLU B  51      -9.934  23.697   0.899  1.00 94.61           C  
ANISOU 2857  CA  GLU B  51    10071  12213  13662    493   -176   2015       C  
ATOM   2858  C   GLU B  51      -8.743  22.997   1.572  1.00 94.03           C  
ANISOU 2858  C   GLU B  51     9936  12152  13638    366   -158   1952       C  
ATOM   2859  O   GLU B  51      -8.026  23.661   2.349  1.00 93.65           O  
ANISOU 2859  O   GLU B  51     9925  11979  13676    249   -128   1990       O  
ATOM   2860  CB  GLU B  51      -9.437  24.818  -0.019  1.00 97.32           C  
ANISOU 2860  CB  GLU B  51    10476  12540  13958    493   -116   2194       C  
ATOM   2861  CG  GLU B  51      -8.606  24.308  -1.187  1.00 98.90           C  
ANISOU 2861  CG  GLU B  51    10612  12918  14046    501    -79   2249       C  
ATOM   2862  CD  GLU B  51      -8.236  25.343  -2.237  1.00101.55           C  
ANISOU 2862  CD  GLU B  51    11004  13263  14314    521    -18   2434       C  
ATOM   2863  OE1 GLU B  51      -8.216  26.546  -1.903  1.00102.62           O  
ANISOU 2863  OE1 GLU B  51    11236  13235  14520    478     13   2533       O  
ATOM   2864  OE2 GLU B  51      -7.966  24.942  -3.391  1.00102.79           O  
ANISOU 2864  OE2 GLU B  51    11116  13589  14349    579      1   2478       O  
ATOM   2865  N   GLY B  52      -8.541  21.711   1.256  1.00 93.57           N  
ANISOU 2865  N   GLY B  52     9786  12240  13523    391   -174   1862       N  
ATOM   2866  CA  GLY B  52      -7.421  20.879   1.738  1.00 92.18           C  
ANISOU 2866  CA  GLY B  52     9538  12108  13375    299   -155   1805       C  
ATOM   2867  C   GLY B  52      -7.864  19.861   2.777  1.00 90.44           C  
ANISOU 2867  C   GLY B  52     9280  11866  13215    294   -205   1647       C  
ATOM   2868  O   GLY B  52      -7.066  18.958   3.085  1.00 90.13           O  
ANISOU 2868  O   GLY B  52     9174  11885  13185    248   -194   1588       O  
ATOM   2869  N   LYS B  53      -9.097  19.984   3.280  1.00 90.12           N  
ANISOU 2869  N   LYS B  53     9278  11750  13212    346   -253   1585       N  
ATOM   2870  CA  LYS B  53      -9.610  19.220   4.452  1.00 89.30           C  
ANISOU 2870  CA  LYS B  53     9153  11593  13182    329   -296   1448       C  
ATOM   2871  C   LYS B  53     -10.089  17.826   4.029  1.00 88.51           C  
ANISOU 2871  C   LYS B  53     8984  11620  13023    400   -328   1334       C  
ATOM   2872  O   LYS B  53     -10.129  17.544   2.811  1.00 88.66           O  
ANISOU 2872  O   LYS B  53     8980  11767  12940    469   -322   1358       O  
ATOM   2873  CB  LYS B  53     -10.735  19.989   5.157  1.00 89.33           C  
ANISOU 2873  CB  LYS B  53     9225  11466  13249    357   -326   1436       C  
ATOM   2874  CG  LYS B  53     -10.309  20.719   6.425  1.00 89.66           C  
ANISOU 2874  CG  LYS B  53     9319  11349  13397    252   -313   1445       C  
ATOM   2875  CD  LYS B  53     -11.141  21.943   6.752  1.00 90.58           C  
ANISOU 2875  CD  LYS B  53     9531  11326  13557    283   -316   1492       C  
ATOM   2876  CE  LYS B  53     -10.740  22.610   8.052  1.00 90.77           C  
ANISOU 2876  CE  LYS B  53     9615  11191  13682    176   -305   1481       C  
ATOM   2877  NZ  LYS B  53      -9.345  23.113   8.012  1.00 91.13           N  
ANISOU 2877  NZ  LYS B  53     9669  11213  13741     54   -261   1562       N  
ATOM   2878  N   THR B  54     -10.413  16.996   5.030  1.00 86.56           N  
ANISOU 2878  N   THR B  54     8711  11336  12839    379   -357   1215       N  
ATOM   2879  CA  THR B  54     -10.960  15.620   4.903  1.00 84.63           C  
ANISOU 2879  CA  THR B  54     8412  11176  12564    428   -388   1088       C  
ATOM   2880  C   THR B  54     -12.373  15.587   5.496  1.00 82.40           C  
ANISOU 2880  C   THR B  54     8145  10837  12324    467   -439   1012       C  
ATOM   2881  O   THR B  54     -12.493  15.734   6.727  1.00 79.98           O  
ANISOU 2881  O   THR B  54     7857  10419  12109    416   -445    979       O  
ATOM   2882  CB  THR B  54     -10.049  14.592   5.587  1.00 83.90           C  
ANISOU 2882  CB  THR B  54     8275  11091  12511    367   -370   1020       C  
ATOM   2883  OG1 THR B  54      -8.866  14.455   4.796  1.00 83.45           O  
ANISOU 2883  OG1 THR B  54     8187  11125  12393    356   -324   1082       O  
ATOM   2884  CG2 THR B  54     -10.713  13.242   5.766  1.00 83.39           C  
ANISOU 2884  CG2 THR B  54     8174  11064  12445    403   -401    884       C  
ATOM   2885  N   PHE B  55     -13.384  15.402   4.642  1.00 82.25           N  
ANISOU 2885  N   PHE B  55     8112  10901  12235    554   -473    987       N  
ATOM   2886  CA  PHE B  55     -14.815  15.241   5.012  1.00 82.12           C  
ANISOU 2886  CA  PHE B  55     8088  10870  12243    602   -523    911       C  
ATOM   2887  C   PHE B  55     -15.158  13.749   5.067  1.00 81.31           C  
ANISOU 2887  C   PHE B  55     7927  10836  12131    601   -548    772       C  
ATOM   2888  O   PHE B  55     -14.530  12.959   4.330  1.00 83.81           O  
ANISOU 2888  O   PHE B  55     8216  11244  12383    603   -534    746       O  
ATOM   2889  CB  PHE B  55     -15.719  15.950   3.999  1.00 83.17           C  
ANISOU 2889  CB  PHE B  55     8231  11069  12299    698   -550    973       C  
ATOM   2890  CG  PHE B  55     -15.581  17.450   3.968  1.00 83.68           C  
ANISOU 2890  CG  PHE B  55     8366  11048  12379    712   -524   1110       C  
ATOM   2891  CD1 PHE B  55     -16.501  18.263   4.615  1.00 83.56           C  
ANISOU 2891  CD1 PHE B  55     8389  10936  12422    746   -540   1128       C  
ATOM   2892  CD2 PHE B  55     -14.532  18.051   3.291  1.00 84.24           C  
ANISOU 2892  CD2 PHE B  55     8466  11131  12407    692   -478   1225       C  
ATOM   2893  CE1 PHE B  55     -16.374  19.643   4.587  1.00 84.00           C  
ANISOU 2893  CE1 PHE B  55     8524  10896  12496    761   -511   1252       C  
ATOM   2894  CE2 PHE B  55     -14.405  19.432   3.266  1.00 85.34           C  
ANISOU 2894  CE2 PHE B  55     8680  11177  12567    697   -450   1353       C  
ATOM   2895  CZ  PHE B  55     -15.326  20.224   3.914  1.00 84.79           C  
ANISOU 2895  CZ  PHE B  55     8659  10998  12557    732   -466   1365       C  
ATOM   2896  N   TYR B  56     -16.117  13.377   5.921  1.00 79.01           N  
ANISOU 2896  N   TYR B  56     7622  10496  11902    597   -579    686       N  
ATOM   2897  CA  TYR B  56     -16.773  12.045   5.919  1.00 77.48           C  
ANISOU 2897  CA  TYR B  56     7376  10361  11699    599   -609    553       C  
ATOM   2898  C   TYR B  56     -17.994  12.124   5.001  1.00 77.06           C  
ANISOU 2898  C   TYR B  56     7292  10412  11572    676   -659    534       C  
ATOM   2899  O   TYR B  56     -18.683  13.163   5.024  1.00 76.23           O  
ANISOU 2899  O   TYR B  56     7204  10286  11472    724   -676    601       O  
ATOM   2900  CB  TYR B  56     -17.164  11.611   7.334  1.00 77.16           C  
ANISOU 2900  CB  TYR B  56     7331  10219  11764    548   -612    479       C  
ATOM   2901  CG  TYR B  56     -16.018  11.154   8.203  1.00 77.13           C  
ANISOU 2901  CG  TYR B  56     7341  10144  11820    476   -572    470       C  
ATOM   2902  CD1 TYR B  56     -15.748   9.805   8.384  1.00 76.51           C  
ANISOU 2902  CD1 TYR B  56     7235  10083  11750    449   -563    377       C  
ATOM   2903  CD2 TYR B  56     -15.212  12.070   8.865  1.00 77.28           C  
ANISOU 2903  CD2 TYR B  56     7401  10075  11886    434   -543    554       C  
ATOM   2904  CE1 TYR B  56     -14.704   9.379   9.190  1.00 76.21           C  
ANISOU 2904  CE1 TYR B  56     7204   9989  11763    395   -527    376       C  
ATOM   2905  CE2 TYR B  56     -14.165  11.661   9.675  1.00 76.50           C  
ANISOU 2905  CE2 TYR B  56     7304   9927  11836    368   -513    547       C  
ATOM   2906  CZ  TYR B  56     -13.908  10.309   9.837  1.00 76.04           C  
ANISOU 2906  CZ  TYR B  56     7212   9898  11782    355   -505    462       C  
ATOM   2907  OH  TYR B  56     -12.879   9.897  10.633  1.00 73.83           O  
ANISOU 2907  OH  TYR B  56     6929   9579  11544    302   -476    464       O  
ATOM   2908  N   VAL B  57     -18.227  11.074   4.207  1.00 76.89           N  
ANISOU 2908  N   VAL B  57     7230  10503  11481    690   -682    447       N  
ATOM   2909  CA  VAL B  57     -19.402  10.942   3.292  1.00 77.46           C  
ANISOU 2909  CA  VAL B  57     7258  10700  11470    753   -740    406       C  
ATOM   2910  C   VAL B  57     -20.000   9.541   3.446  1.00 77.48           C  
ANISOU 2910  C   VAL B  57     7215  10739  11484    715   -767    252       C  
ATOM   2911  O   VAL B  57     -19.323   8.662   4.006  1.00 76.76           O  
ANISOU 2911  O   VAL B  57     7135  10586  11444    654   -734    191       O  
ATOM   2912  CB  VAL B  57     -19.028  11.222   1.824  1.00 78.00           C  
ANISOU 2912  CB  VAL B  57     7332  10898  11407    813   -742    468       C  
ATOM   2913  CG1 VAL B  57     -18.803  12.705   1.574  1.00 78.39           C  
ANISOU 2913  CG1 VAL B  57     7424  10920  11440    863   -724    627       C  
ATOM   2914  CG2 VAL B  57     -17.825  10.404   1.377  1.00 77.53           C  
ANISOU 2914  CG2 VAL B  57     7282  10869  11306    782   -700    438       C  
ATOM   2915  N   LEU B  58     -21.229   9.356   2.959  1.00 79.11           N  
ANISOU 2915  N   LEU B  58     7369  11043  11644    748   -826    195       N  
ATOM   2916  CA  LEU B  58     -21.941   8.050   2.947  1.00 79.03           C  
ANISOU 2916  CA  LEU B  58     7310  11082  11634    705   -859     44       C  
ATOM   2917  C   LEU B  58     -21.288   7.163   1.892  1.00 78.28           C  
ANISOU 2917  C   LEU B  58     7225  11074  11443    701   -853    -17       C  
ATOM   2918  O   LEU B  58     -20.814   7.667   0.875  1.00 78.39           O  
ANISOU 2918  O   LEU B  58     7255  11173  11357    757   -850     53       O  
ATOM   2919  CB  LEU B  58     -23.424   8.290   2.632  1.00 80.50           C  
ANISOU 2919  CB  LEU B  58     7429  11369  11786    745   -928     17       C  
ATOM   2920  CG  LEU B  58     -24.377   7.149   2.993  1.00 81.37           C  
ANISOU 2920  CG  LEU B  58     7481  11501  11934    681   -962   -128       C  
ATOM   2921  CD1 LEU B  58     -24.800   7.235   4.456  1.00 80.75           C  
ANISOU 2921  CD1 LEU B  58     7396  11296  11989    639   -941   -132       C  
ATOM   2922  CD2 LEU B  58     -25.598   7.139   2.082  1.00 82.75           C  
ANISOU 2922  CD2 LEU B  58     7578  11844  12018    721  -1039   -171       C  
ATOM   2923  N   PRO B  59     -21.217   5.828   2.098  1.00 76.78           N  
ANISOU 2923  N   PRO B  59     7031  10861  11278    639   -844   -147       N  
ATOM   2924  CA  PRO B  59     -20.908   4.914   1.001  1.00 77.85           C  
ANISOU 2924  CA  PRO B  59     7173  11094  11311    642   -849   -233       C  
ATOM   2925  C   PRO B  59     -21.891   5.138  -0.163  1.00 79.84           C  
ANISOU 2925  C   PRO B  59     7376  11516  11441    691   -921   -256       C  
ATOM   2926  O   PRO B  59     -23.063   4.883   0.020  1.00 80.39           O  
ANISOU 2926  O   PRO B  59     7392  11621  11530    666   -975   -328       O  
ATOM   2927  CB  PRO B  59     -21.063   3.519   1.630  1.00 77.35           C  
ANISOU 2927  CB  PRO B  59     7112  10956  11319    563   -836   -376       C  
ATOM   2928  CG  PRO B  59     -20.885   3.741   3.122  1.00 75.89           C  
ANISOU 2928  CG  PRO B  59     6941  10617  11275    523   -799   -331       C  
ATOM   2929  CD  PRO B  59     -21.402   5.139   3.385  1.00 75.62           C  
ANISOU 2929  CD  PRO B  59     6885  10590  11257    566   -824   -216       C  
ATOM   2930  N   ASN B  60     -21.407   5.648  -1.303  1.00 81.98           N  
ANISOU 2930  N   ASN B  60     7663  11895  11590    759   -921   -187       N  
ATOM   2931  CA  ASN B  60     -22.229   5.935  -2.515  1.00 84.43           C  
ANISOU 2931  CA  ASN B  60     7930  12386  11762    819   -990   -192       C  
ATOM   2932  C   ASN B  60     -21.671   5.171  -3.729  1.00 88.05           C  
ANISOU 2932  C   ASN B  60     8412  12957  12086    833   -986   -265       C  
ATOM   2933  O   ASN B  60     -21.988   5.572  -4.868  1.00 90.29           O  
ANISOU 2933  O   ASN B  60     8675  13399  12230    899  -1028   -236       O  
ATOM   2934  CB  ASN B  60     -22.352   7.444  -2.774  1.00 83.55           C  
ANISOU 2934  CB  ASN B  60     7817  12311  11616    905  -1000    -23       C  
ATOM   2935  CG  ASN B  60     -21.065   8.125  -3.201  1.00 82.28           C  
ANISOU 2935  CG  ASN B  60     7716  12133  11413    947   -936    107       C  
ATOM   2936  OD1 ASN B  60     -21.038   9.339  -3.391  1.00 80.30           O  
ANISOU 2936  OD1 ASN B  60     7479  11889  11141   1009   -931    251       O  
ATOM   2937  ND2 ASN B  60     -19.996   7.364  -3.366  1.00 81.97           N  
ANISOU 2937  ND2 ASN B  60     7713  12069  11359    915   -883     62       N  
ATOM   2938  N   ASP B  61     -20.891   4.106  -3.494  1.00 89.97           N  
ANISOU 2938  N   ASP B  61     8696  13124  12364    781   -934   -356       N  
ATOM   2939  CA  ASP B  61     -20.291   3.234  -4.544  1.00 92.23           C  
ANISOU 2939  CA  ASP B  61     9015  13495  12532    793   -917   -444       C  
ATOM   2940  C   ASP B  61     -19.614   2.029  -3.867  1.00 91.81           C  
ANISOU 2940  C   ASP B  61     9006  13307  12567    730   -857   -547       C  
ATOM   2941  O   ASP B  61     -19.840   1.837  -2.652  1.00 89.98           O  
ANISOU 2941  O   ASP B  61     8769  12940  12478    671   -845   -561       O  
ATOM   2942  CB  ASP B  61     -19.337   4.033  -5.441  1.00 93.29           C  
ANISOU 2942  CB  ASP B  61     9177  13710  12557    876   -878   -313       C  
ATOM   2943  CG  ASP B  61     -18.123   4.591  -4.719  1.00 92.67           C  
ANISOU 2943  CG  ASP B  61     9135  13506  12568    878   -796   -184       C  
ATOM   2944  OD1 ASP B  61     -18.086   4.497  -3.476  1.00 92.18           O  
ANISOU 2944  OD1 ASP B  61     9075  13297  12651    822   -775   -186       O  
ATOM   2945  OD2 ASP B  61     -17.221   5.111  -5.406  1.00 93.26           O  
ANISOU 2945  OD2 ASP B  61     9232  13638  12561    931   -752    -84       O  
ATOM   2946  N   ASP B  62     -18.812   1.256  -4.614  1.00 92.68           N  
ANISOU 2946  N   ASP B  62     9162  13457  12596    748   -816   -613       N  
ATOM   2947  CA  ASP B  62     -18.215  -0.030  -4.156  1.00 93.02           C  
ANISOU 2947  CA  ASP B  62     9254  13385  12703    703   -758   -726       C  
ATOM   2948  C   ASP B  62     -16.766   0.174  -3.692  1.00 91.01           C  
ANISOU 2948  C   ASP B  62     9036  13044  12500    734   -667   -620       C  
ATOM   2949  O   ASP B  62     -16.168  -0.822  -3.246  1.00 90.88           O  
ANISOU 2949  O   ASP B  62     9059  12929  12541    712   -612   -692       O  
ATOM   2950  CB  ASP B  62     -18.308  -1.116  -5.236  1.00 95.15           C  
ANISOU 2950  CB  ASP B  62     9556  13744  12852    706   -769   -885       C  
ATOM   2951  CG  ASP B  62     -19.477  -2.078  -5.074  1.00 96.22           C  
ANISOU 2951  CG  ASP B  62     9678  13860  13018    620   -827  -1057       C  
ATOM   2952  OD1 ASP B  62     -20.037  -2.155  -3.956  1.00 95.01           O  
ANISOU 2952  OD1 ASP B  62     9501  13594  13002    554   -837  -1063       O  
ATOM   2953  OD2 ASP B  62     -19.815  -2.754  -6.069  1.00 97.44           O  
ANISOU 2953  OD2 ASP B  62     9848  14117  13056    615   -859  -1188       O  
ATOM   2954  N   THR B  63     -16.231   1.399  -3.765  1.00 89.86           N  
ANISOU 2954  N   THR B  63     8875  12930  12338    780   -650   -454       N  
ATOM   2955  CA  THR B  63     -14.883   1.762  -3.239  1.00 88.66           C  
ANISOU 2955  CA  THR B  63     8740  12702  12242    796   -569   -336       C  
ATOM   2956  C   THR B  63     -14.982   2.152  -1.756  1.00 86.90           C  
ANISOU 2956  C   THR B  63     8506  12331  12182    740   -566   -280       C  
ATOM   2957  O   THR B  63     -13.961   2.036  -1.053  1.00 85.95           O  
ANISOU 2957  O   THR B  63     8400  12124  12134    730   -504   -231       O  
ATOM   2958  CB  THR B  63     -14.230   2.878  -4.067  1.00 88.82           C  
ANISOU 2958  CB  THR B  63     8754  12828  12165    860   -549   -187       C  
ATOM   2959  OG1 THR B  63     -12.823   2.836  -3.824  1.00 87.97           O  
ANISOU 2959  OG1 THR B  63     8660  12678  12083    872   -464   -116       O  
ATOM   2960  CG2 THR B  63     -14.757   4.260  -3.746  1.00 88.36           C  
ANISOU 2960  CG2 THR B  63     8669  12760  12141    859   -587    -56       C  
ATOM   2961  N   LEU B  64     -16.159   2.595  -1.304  1.00 86.97           N  
ANISOU 2961  N   LEU B  64     8485  12320  12238    710   -629   -285       N  
ATOM   2962  CA  LEU B  64     -16.406   3.091   0.077  1.00 85.67           C  
ANISOU 2962  CA  LEU B  64     8310  12026  12215    663   -631   -231       C  
ATOM   2963  C   LEU B  64     -17.114   2.010   0.899  1.00 84.74           C  
ANISOU 2963  C   LEU B  64     8190  11819  12188    598   -645   -363       C  
ATOM   2964  O   LEU B  64     -16.707   1.810   2.060  1.00 84.13           O  
ANISOU 2964  O   LEU B  64     8126  11616  12223    560   -608   -346       O  
ATOM   2965  CB  LEU B  64     -17.242   4.372   0.003  1.00 86.31           C  
ANISOU 2965  CB  LEU B  64     8360  12148  12284    685   -684   -139       C  
ATOM   2966  CG  LEU B  64     -16.547   5.562  -0.658  1.00 87.00           C  
ANISOU 2966  CG  LEU B  64     8457  12295  12300    742   -662     12       C  
ATOM   2967  CD1 LEU B  64     -17.555   6.607  -1.113  1.00 88.10           C  
ANISOU 2967  CD1 LEU B  64     8573  12509  12391    785   -721     77       C  
ATOM   2968  CD2 LEU B  64     -15.524   6.184   0.279  1.00 85.84           C  
ANISOU 2968  CD2 LEU B  64     8331  12033  12248    715   -606    122       C  
ATOM   2969  N   ARG B  65     -18.134   1.359   0.325  1.00 84.67           N  
ANISOU 2969  N   ARG B  65     8164  11877  12128    582   -697   -485       N  
ATOM   2970  CA  ARG B  65     -18.865   0.219   0.950  1.00 84.17           C  
ANISOU 2970  CA  ARG B  65     8100  11738  12140    510   -709   -623       C  
ATOM   2971  C   ARG B  65     -17.851  -0.810   1.461  1.00 82.34           C  
ANISOU 2971  C   ARG B  65     7923  11394  11966    493   -635   -666       C  
ATOM   2972  O   ARG B  65     -18.008  -1.280   2.608  1.00 81.42           O  
ANISOU 2972  O   ARG B  65     7815  11153  11967    440   -616   -691       O  
ATOM   2973  CB  ARG B  65     -19.836  -0.441  -0.035  1.00 86.31           C  
ANISOU 2973  CB  ARG B  65     8352  12120  12320    493   -769   -759       C  
ATOM   2974  CG  ARG B  65     -21.302  -0.305   0.348  1.00 87.40           C  
ANISOU 2974  CG  ARG B  65     8428  12277  12500    443   -839   -802       C  
ATOM   2975  CD  ARG B  65     -22.191  -1.161  -0.533  1.00 90.03           C  
ANISOU 2975  CD  ARG B  65     8740  12712  12753    404   -895   -957       C  
ATOM   2976  NE  ARG B  65     -22.164  -0.701  -1.919  1.00 92.50           N  
ANISOU 2976  NE  ARG B  65     9042  13197  12907    473   -935   -941       N  
ATOM   2977  CZ  ARG B  65     -23.025   0.160  -2.468  1.00 93.22           C  
ANISOU 2977  CZ  ARG B  65     9067  13426  12924    509  -1007   -894       C  
ATOM   2978  NH1 ARG B  65     -24.018   0.674  -1.758  1.00 92.42           N  
ANISOU 2978  NH1 ARG B  65     8902  13314  12898    486  -1048   -861       N  
ATOM   2979  NH2 ARG B  65     -22.889   0.505  -3.737  1.00 94.30           N  
ANISOU 2979  NH2 ARG B  65     9202  13717  12908    576  -1035   -875       N  
ATOM   2980  N   VAL B  66     -16.861  -1.146   0.630  1.00 81.02           N  
ANISOU 2980  N   VAL B  66     7792  11276  11715    544   -592   -671       N  
ATOM   2981  CA  VAL B  66     -15.732  -2.055   0.991  1.00 79.35           C  
ANISOU 2981  CA  VAL B  66     7631  10974  11543    554   -513   -694       C  
ATOM   2982  C   VAL B  66     -14.990  -1.471   2.201  1.00 76.44           C  
ANISOU 2982  C   VAL B  66     7255  10508  11282    549   -473   -569       C  
ATOM   2983  O   VAL B  66     -14.939  -2.159   3.240  1.00 75.19           O  
ANISOU 2983  O   VAL B  66     7114  10226  11226    511   -446   -602       O  
ATOM   2984  CB  VAL B  66     -14.789  -2.309  -0.202  1.00 80.62           C  
ANISOU 2984  CB  VAL B  66     7820  11230  11580    626   -472   -701       C  
ATOM   2985  CG1 VAL B  66     -15.447  -3.196  -1.249  1.00 82.34           C  
ANISOU 2985  CG1 VAL B  66     8063  11520  11702    622   -503   -858       C  
ATOM   2986  CG2 VAL B  66     -14.272  -1.025  -0.834  1.00 80.75           C  
ANISOU 2986  CG2 VAL B  66     7806  11356  11516    682   -475   -558       C  
ATOM   2987  N   GLU B  67     -14.484  -0.239   2.084  1.00 75.10           N  
ANISOU 2987  N   GLU B  67     7059  10388  11086    581   -473   -430       N  
ATOM   2988  CA  GLU B  67     -13.600   0.408   3.095  1.00 73.94           C  
ANISOU 2988  CA  GLU B  67     6905  10165  11021    574   -434   -307       C  
ATOM   2989  C   GLU B  67     -14.364   0.563   4.414  1.00 71.09           C  
ANISOU 2989  C   GLU B  67     6534   9696  10780    513   -460   -309       C  
ATOM   2990  O   GLU B  67     -13.746   0.357   5.480  1.00 70.38           O  
ANISOU 2990  O   GLU B  67     6452   9511  10776    493   -422   -277       O  
ATOM   2991  CB  GLU B  67     -13.089   1.764   2.598  1.00 75.03           C  
ANISOU 2991  CB  GLU B  67     7022  10382  11104    607   -435   -167       C  
ATOM   2992  CG  GLU B  67     -11.894   1.657   1.664  1.00 76.47           C  
ANISOU 2992  CG  GLU B  67     7211  10650  11194    664   -381   -127       C  
ATOM   2993  CD  GLU B  67     -11.381   2.976   1.108  1.00 77.63           C  
ANISOU 2993  CD  GLU B  67     7339  10874  11282    689   -376     15       C  
ATOM   2994  OE1 GLU B  67     -11.705   4.036   1.688  1.00 78.86           O  
ANISOU 2994  OE1 GLU B  67     7483  10986  11492    659   -402    101       O  
ATOM   2995  OE2 GLU B  67     -10.656   2.944   0.094  1.00 78.59           O  
ANISOU 2995  OE2 GLU B  67     7461  11096  11304    740   -340     42       O  
ATOM   2996  N   ALA B  68     -15.653   0.908   4.331  1.00 68.59           N  
ANISOU 2996  N   ALA B  68     6194   9404  10462    491   -522   -343       N  
ATOM   2997  CA  ALA B  68     -16.579   1.048   5.478  1.00 66.37           C  
ANISOU 2997  CA  ALA B  68     5897   9038  10283    437   -549   -355       C  
ATOM   2998  C   ALA B  68     -16.722  -0.298   6.197  1.00 64.81           C  
ANISOU 2998  C   ALA B  68     5722   8743  10159    392   -522   -460       C  
ATOM   2999  O   ALA B  68     -16.591  -0.324   7.436  1.00 63.03           O  
ANISOU 2999  O   ALA B  68     5502   8415  10030    360   -500   -429       O  
ATOM   3000  CB  ALA B  68     -17.916   1.555   5.001  1.00 67.10           C  
ANISOU 3000  CB  ALA B  68     5951   9205  10338    436   -617   -380       C  
ATOM   3001  N   PHE B  69     -16.981  -1.375   5.450  1.00 64.14           N  
ANISOU 3001  N   PHE B  69     5655   8687  10027    387   -523   -579       N  
ATOM   3002  CA  PHE B  69     -17.194  -2.731   6.017  1.00 63.42           C  
ANISOU 3002  CA  PHE B  69     5597   8495  10003    340   -495   -687       C  
ATOM   3003  C   PHE B  69     -15.869  -3.273   6.559  1.00 62.55           C  
ANISOU 3003  C   PHE B  69     5530   8303   9932    369   -420   -649       C  
ATOM   3004  O   PHE B  69     -15.867  -3.872   7.652  1.00 61.38           O  
ANISOU 3004  O   PHE B  69     5401   8041   9879    335   -390   -661       O  
ATOM   3005  CB  PHE B  69     -17.790  -3.697   4.994  1.00 64.10           C  
ANISOU 3005  CB  PHE B  69     5699   8631  10022    324   -515   -830       C  
ATOM   3006  CG  PHE B  69     -17.966  -5.080   5.562  1.00 64.17           C  
ANISOU 3006  CG  PHE B  69     5754   8519  10105    271   -479   -938       C  
ATOM   3007  CD1 PHE B  69     -18.718  -5.272   6.712  1.00 63.32           C  
ANISOU 3007  CD1 PHE B  69     5633   8320  10106    203   -483   -947       C  
ATOM   3008  CD2 PHE B  69     -17.336  -6.176   4.993  1.00 64.99           C  
ANISOU 3008  CD2 PHE B  69     5923   8596  10173    294   -431  -1022       C  
ATOM   3009  CE1 PHE B  69     -18.862  -6.534   7.264  1.00 63.46           C  
ANISOU 3009  CE1 PHE B  69     5699   8218  10195    152   -442  -1035       C  
ATOM   3010  CE2 PHE B  69     -17.488  -7.441   5.543  1.00 65.27           C  
ANISOU 3010  CE2 PHE B  69     6012   8503  10282    248   -391  -1114       C  
ATOM   3011  CZ  PHE B  69     -18.249  -7.617   6.677  1.00 64.55           C  
ANISOU 3011  CZ  PHE B  69     5906   8318  10300    174   -396  -1117       C  
ATOM   3012  N   GLU B  70     -14.781  -3.080   5.810  1.00 63.40           N  
ANISOU 3012  N   GLU B  70     5648   8475   9966    434   -389   -601       N  
ATOM   3013  CA  GLU B  70     -13.398  -3.399   6.263  1.00 63.54           C  
ANISOU 3013  CA  GLU B  70     5687   8443  10009    475   -320   -540       C  
ATOM   3014  C   GLU B  70     -13.161  -2.727   7.622  1.00 61.92           C  
ANISOU 3014  C   GLU B  70     5459   8168   9898    447   -317   -438       C  
ATOM   3015  O   GLU B  70     -12.854  -3.452   8.590  1.00 61.63           O  
ANISOU 3015  O   GLU B  70     5446   8033   9938    436   -279   -446       O  
ATOM   3016  CB  GLU B  70     -12.360  -2.955   5.227  1.00 64.48           C  
ANISOU 3016  CB  GLU B  70     5799   8672  10028    545   -295   -479       C  
ATOM   3017  CG  GLU B  70     -11.927  -4.060   4.274  1.00 66.29           C  
ANISOU 3017  CG  GLU B  70     6072   8929  10185    596   -253   -575       C  
ATOM   3018  CD  GLU B  70     -10.598  -4.726   4.612  1.00 67.56           C  
ANISOU 3018  CD  GLU B  70     6254   9046  10367    652   -173   -543       C  
ATOM   3019  OE1 GLU B  70      -9.828  -5.023   3.671  1.00 68.47           O  
ANISOU 3019  OE1 GLU B  70     6383   9235  10396    721   -131   -553       O  
ATOM   3020  OE2 GLU B  70     -10.327  -4.948   5.815  1.00 67.83           O  
ANISOU 3020  OE2 GLU B  70     6289   8982  10500    633   -151   -505       O  
ATOM   3021  N   TYR B  71     -13.357  -1.406   7.700  1.00 60.92           N  
ANISOU 3021  N   TYR B  71     5295   8086   9763    436   -355   -348       N  
ATOM   3022  CA  TYR B  71     -12.974  -0.557   8.861  1.00 59.47           C  
ANISOU 3022  CA  TYR B  71     5093   7850   9649    412   -352   -243       C  
ATOM   3023  C   TYR B  71     -13.952  -0.729  10.034  1.00 58.30           C  
ANISOU 3023  C   TYR B  71     4947   7608   9593    356   -373   -278       C  
ATOM   3024  O   TYR B  71     -13.470  -0.828  11.184  1.00 57.51           O  
ANISOU 3024  O   TYR B  71     4854   7434   9563    339   -346   -236       O  
ATOM   3025  CB  TYR B  71     -12.856   0.916   8.451  1.00 59.34           C  
ANISOU 3025  CB  TYR B  71     5050   7904   9591    420   -381   -141       C  
ATOM   3026  CG  TYR B  71     -12.094   1.762   9.442  1.00 58.55           C  
ANISOU 3026  CG  TYR B  71     4939   7761   9544    399   -367    -32       C  
ATOM   3027  CD1 TYR B  71     -10.828   1.388   9.856  1.00 58.11           C  
ANISOU 3027  CD1 TYR B  71     4880   7692   9504    410   -319     10       C  
ATOM   3028  CD2 TYR B  71     -12.635   2.921   9.978  1.00 58.01           C  
ANISOU 3028  CD2 TYR B  71     4864   7668   9509    367   -402     24       C  
ATOM   3029  CE1 TYR B  71     -10.120   2.136  10.778  1.00 57.69           C  
ANISOU 3029  CE1 TYR B  71     4812   7610   9495    380   -313    102       C  
ATOM   3030  CE2 TYR B  71     -11.938   3.685  10.900  1.00 57.21           C  
ANISOU 3030  CE2 TYR B  71     4760   7522   9454    338   -391    112       C  
ATOM   3031  CZ  TYR B  71     -10.672   3.291  11.296  1.00 57.38           C  
ANISOU 3031  CZ  TYR B  71     4773   7540   9488    339   -350    149       C  
ATOM   3032  OH  TYR B  71      -9.950   4.017  12.196  1.00 57.53           O  
ANISOU 3032  OH  TYR B  71     4783   7527   9546    301   -344    230       O  
ATOM   3033  N   TYR B  72     -15.267  -0.754   9.768  1.00 57.89           N  
ANISOU 3033  N   TYR B  72     4885   7571   9540    328   -417   -348       N  
ATOM   3034  CA  TYR B  72     -16.338  -0.654  10.798  1.00 56.63           C  
ANISOU 3034  CA  TYR B  72     4713   7345   9458    276   -440   -367       C  
ATOM   3035  C   TYR B  72     -16.875  -2.037  11.193  1.00 56.76           C  
ANISOU 3035  C   TYR B  72     4751   7288   9525    236   -420   -473       C  
ATOM   3036  O   TYR B  72     -17.406  -2.142  12.315  1.00 56.51           O  
ANISOU 3036  O   TYR B  72     4716   7182   9572    194   -416   -473       O  
ATOM   3037  CB  TYR B  72     -17.451   0.286  10.326  1.00 56.33           C  
ANISOU 3037  CB  TYR B  72     4637   7376   9389    273   -500   -363       C  
ATOM   3038  CG  TYR B  72     -17.012   1.725  10.239  1.00 55.59           C  
ANISOU 3038  CG  TYR B  72     4534   7319   9269    304   -513   -247       C  
ATOM   3039  CD1 TYR B  72     -16.837   2.356   9.018  1.00 55.87           C  
ANISOU 3039  CD1 TYR B  72     4560   7454   9214    348   -533   -211       C  
ATOM   3040  CD2 TYR B  72     -16.726   2.445  11.386  1.00 54.55           C  
ANISOU 3040  CD2 TYR B  72     4408   7117   9201    286   -501   -171       C  
ATOM   3041  CE1 TYR B  72     -16.407   3.670   8.940  1.00 55.50           C  
ANISOU 3041  CE1 TYR B  72     4513   7426   9148    371   -538    -98       C  
ATOM   3042  CE2 TYR B  72     -16.299   3.762  11.326  1.00 54.46           C  
ANISOU 3042  CE2 TYR B  72     4398   7123   9171    304   -510    -68       C  
ATOM   3043  CZ  TYR B  72     -16.137   4.377  10.098  1.00 54.80           C  
ANISOU 3043  CZ  TYR B  72     4434   7255   9130    346   -526    -29       C  
ATOM   3044  OH  TYR B  72     -15.712   5.673  10.048  1.00 54.56           O  
ANISOU 3044  OH  TYR B  72     4413   7229   9087    358   -528     76       O  
ATOM   3045  N   HIS B  73     -16.752  -3.049  10.325  1.00 57.29           N  
ANISOU 3045  N   HIS B  73     4845   7372   9551    248   -404   -561       N  
ATOM   3046  CA  HIS B  73     -17.212  -4.442  10.583  1.00 57.51           C  
ANISOU 3046  CA  HIS B  73     4908   7318   9625    206   -378   -669       C  
ATOM   3047  C   HIS B  73     -18.738  -4.479  10.727  1.00 58.69           C  
ANISOU 3047  C   HIS B  73     5023   7472   9805    136   -424   -738       C  
ATOM   3048  O   HIS B  73     -19.225  -5.163  11.652  1.00 59.36           O  
ANISOU 3048  O   HIS B  73     5119   7463   9970     83   -402   -773       O  
ATOM   3049  CB  HIS B  73     -16.521  -5.012  11.832  1.00 56.20           C  
ANISOU 3049  CB  HIS B  73     4776   7034   9541    205   -320   -628       C  
ATOM   3050  CG  HIS B  73     -15.236  -5.702  11.546  1.00 55.74           C  
ANISOU 3050  CG  HIS B  73     4762   6957   9459    266   -263   -619       C  
ATOM   3051  ND1 HIS B  73     -14.677  -6.598  12.432  1.00 55.26           N  
ANISOU 3051  ND1 HIS B  73     4743   6791   9461    275   -205   -610       N  
ATOM   3052  CD2 HIS B  73     -14.419  -5.651  10.476  1.00 55.75           C  
ANISOU 3052  CD2 HIS B  73     4769   7033   9377    327   -251   -614       C  
ATOM   3053  CE1 HIS B  73     -13.562  -7.068  11.922  1.00 55.54           C  
ANISOU 3053  CE1 HIS B  73     4806   6838   9456    345   -160   -600       C  
ATOM   3054  NE2 HIS B  73     -13.382  -6.502  10.721  1.00 55.95           N  
ANISOU 3054  NE2 HIS B  73     4836   7001   9418    375   -186   -605       N  
ATOM   3055  N   THR B  74     -19.468  -3.766   9.864  1.00 59.73           N  
ANISOU 3055  N   THR B  74     5107   7714   9871    139   -485   -752       N  
ATOM   3056  CA  THR B  74     -20.955  -3.780   9.833  1.00 60.51           C  
ANISOU 3056  CA  THR B  74     5155   7850   9985     80   -536   -820       C  
ATOM   3057  C   THR B  74     -21.463  -3.201   8.509  1.00 61.81           C  
ANISOU 3057  C   THR B  74     5277   8161  10044    106   -599   -843       C  
ATOM   3058  O   THR B  74     -20.853  -2.233   8.002  1.00 60.79           O  
ANISOU 3058  O   THR B  74     5144   8098   9854    173   -610   -756       O  
ATOM   3059  CB  THR B  74     -21.561  -3.055  11.042  1.00 59.70           C  
ANISOU 3059  CB  THR B  74     5014   7708   9958     57   -543   -753       C  
ATOM   3060  OG1 THR B  74     -22.955  -3.375  11.076  1.00 60.34           O  
ANISOU 3060  OG1 THR B  74     5046   7817  10064     -6   -578   -832       O  
ATOM   3061  CG2 THR B  74     -21.358  -1.556  11.000  1.00 59.06           C  
ANISOU 3061  CG2 THR B  74     4906   7688   9846    115   -570   -640       C  
ATOM   3062  N   THR B  75     -22.556  -3.786   8.005  1.00 63.90           N  
ANISOU 3062  N   THR B  75     5511   8475  10291     51   -640   -955       N  
ATOM   3063  CA  THR B  75     -23.215  -3.467   6.710  1.00 65.49           C  
ANISOU 3063  CA  THR B  75     5666   8829  10386     65   -709  -1002       C  
ATOM   3064  C   THR B  75     -24.501  -2.658   6.947  1.00 64.99           C  
ANISOU 3064  C   THR B  75     5513   8841  10336     50   -769   -978       C  
ATOM   3065  O   THR B  75     -25.181  -2.364   5.949  1.00 65.37           O  
ANISOU 3065  O   THR B  75     5510   9029  10297     63   -833  -1012       O  
ATOM   3066  CB  THR B  75     -23.485  -4.758   5.924  1.00 67.16           C  
ANISOU 3066  CB  THR B  75     5905   9053  10559     10   -714  -1156       C  
ATOM   3067  OG1 THR B  75     -24.025  -5.720   6.831  1.00 68.01           O  
ANISOU 3067  OG1 THR B  75     6022   9045  10770    -80   -686  -1227       O  
ATOM   3068  CG2 THR B  75     -22.245  -5.326   5.269  1.00 67.04           C  
ANISOU 3068  CG2 THR B  75     5970   9013  10487     59   -666  -1177       C  
ATOM   3069  N   ASP B  76     -24.808  -2.315   8.206  1.00 64.62           N  
ANISOU 3069  N   ASP B  76     5449   8715  10388     30   -748   -920       N  
ATOM   3070  CA  ASP B  76     -25.954  -1.456   8.627  1.00 65.22           C  
ANISOU 3070  CA  ASP B  76     5442   8849  10488     31   -791   -880       C  
ATOM   3071  C   ASP B  76     -25.845  -0.098   7.935  1.00 65.24           C  
ANISOU 3071  C   ASP B  76     5422   8956  10410    125   -830   -782       C  
ATOM   3072  O   ASP B  76     -25.113   0.773   8.399  1.00 64.61           O  
ANISOU 3072  O   ASP B  76     5376   8824  10349    178   -801   -672       O  
ATOM   3073  CB  ASP B  76     -25.986  -1.299  10.152  1.00 64.82           C  
ANISOU 3073  CB  ASP B  76     5400   8678  10550      8   -744   -824       C  
ATOM   3074  CG  ASP B  76     -26.914  -0.213  10.677  1.00 65.23           C  
ANISOU 3074  CG  ASP B  76     5383   8775  10625     36   -772   -758       C  
ATOM   3075  OD1 ASP B  76     -27.546   0.485   9.852  1.00 65.82           O  
ANISOU 3075  OD1 ASP B  76     5400   8977  10630     81   -831   -745       O  
ATOM   3076  OD2 ASP B  76     -26.994  -0.073  11.915  1.00 65.32           O  
ANISOU 3076  OD2 ASP B  76     5401   8696  10720     20   -734   -718       O  
ATOM   3077  N   PRO B  77     -26.578   0.149   6.824  1.00 66.49           N  
ANISOU 3077  N   PRO B  77     5521   9264  10475    148   -897   -815       N  
ATOM   3078  CA  PRO B  77     -26.332   1.333   5.996  1.00 66.80           C  
ANISOU 3078  CA  PRO B  77     5553   9402  10423    245   -928   -718       C  
ATOM   3079  C   PRO B  77     -26.723   2.687   6.620  1.00 66.15           C  
ANISOU 3079  C   PRO B  77     5442   9314  10375    306   -935   -597       C  
ATOM   3080  O   PRO B  77     -26.629   3.681   5.916  1.00 65.74           O  
ANISOU 3080  O   PRO B  77     5386   9341  10250    387   -961   -514       O  
ATOM   3081  CB  PRO B  77     -27.181   1.074   4.736  1.00 68.41           C  
ANISOU 3081  CB  PRO B  77     5695   9775  10521    244  -1002   -799       C  
ATOM   3082  CG  PRO B  77     -27.506  -0.408   4.791  1.00 68.84           C  
ANISOU 3082  CG  PRO B  77     5751   9798  10606    137   -998   -953       C  
ATOM   3083  CD  PRO B  77     -27.646  -0.698   6.270  1.00 67.83           C  
ANISOU 3083  CD  PRO B  77     5631   9523  10618     79   -947   -944       C  
ATOM   3084  N   SER B  78     -27.139   2.704   7.894  1.00 65.45           N  
ANISOU 3084  N   SER B  78     5341   9132  10393    270   -908   -588       N  
ATOM   3085  CA  SER B  78     -27.432   3.935   8.681  1.00 64.65           C  
ANISOU 3085  CA  SER B  78     5229   8997  10337    326   -900   -481       C  
ATOM   3086  C   SER B  78     -26.232   4.323   9.562  1.00 63.19           C  
ANISOU 3086  C   SER B  78     5130   8668  10209    332   -836   -402       C  
ATOM   3087  O   SER B  78     -26.148   5.508   9.948  1.00 62.62           O  
ANISOU 3087  O   SER B  78     5076   8566  10151    390   -828   -302       O  
ATOM   3088  CB  SER B  78     -28.680   3.769   9.516  1.00 64.25           C  
ANISOU 3088  CB  SER B  78     5105   8949  10355    289   -909   -521       C  
ATOM   3089  OG  SER B  78     -28.410   3.029  10.698  1.00 63.42           O  
ANISOU 3089  OG  SER B  78     5034   8714  10347    215   -853   -554       O  
ATOM   3090  N   PHE B  79     -25.346   3.369   9.874  1.00 62.03           N  
ANISOU 3090  N   PHE B  79     5035   8437  10094    277   -793   -445       N  
ATOM   3091  CA  PHE B  79     -24.274   3.506  10.898  1.00 61.11           C  
ANISOU 3091  CA  PHE B  79     4987   8189  10043    267   -734   -386       C  
ATOM   3092  C   PHE B  79     -23.666   4.913  10.854  1.00 60.02           C  
ANISOU 3092  C   PHE B  79     4882   8040   9882    333   -730   -263       C  
ATOM   3093  O   PHE B  79     -23.819   5.654  11.848  1.00 59.41           O  
ANISOU 3093  O   PHE B  79     4817   7894   9863    341   -714   -209       O  
ATOM   3094  CB  PHE B  79     -23.185   2.443  10.715  1.00 61.36           C  
ANISOU 3094  CB  PHE B  79     5070   8174  10070    233   -696   -429       C  
ATOM   3095  CG  PHE B  79     -22.195   2.371  11.852  1.00 61.00           C  
ANISOU 3095  CG  PHE B  79     5077   8005  10093    215   -640   -381       C  
ATOM   3096  CD1 PHE B  79     -22.465   1.616  12.985  1.00 60.92           C  
ANISOU 3096  CD1 PHE B  79     5072   7908  10166    160   -609   -422       C  
ATOM   3097  CD2 PHE B  79     -20.994   3.065  11.797  1.00 61.08           C  
ANISOU 3097  CD2 PHE B  79     5129   7994  10082    250   -618   -291       C  
ATOM   3098  CE1 PHE B  79     -21.555   1.554  14.031  1.00 60.53           C  
ANISOU 3098  CE1 PHE B  79     5068   7759  10168    149   -562   -375       C  
ATOM   3099  CE2 PHE B  79     -20.083   2.999  12.842  1.00 60.28           C  
ANISOU 3099  CE2 PHE B  79     5067   7797  10037    230   -574   -249       C  
ATOM   3100  CZ  PHE B  79     -20.364   2.244  13.958  1.00 59.93           C  
ANISOU 3100  CZ  PHE B  79     5028   7673  10068    184   -548   -291       C  
ATOM   3101  N   LEU B  80     -23.013   5.265   9.738  1.00 59.60           N  
ANISOU 3101  N   LEU B  80     4847   8051   9746    376   -741   -224       N  
ATOM   3102  CA  LEU B  80     -22.163   6.483   9.607  1.00 58.61           C  
ANISOU 3102  CA  LEU B  80     4766   7904   9598    425   -726   -103       C  
ATOM   3103  C   LEU B  80     -22.988   7.748   9.871  1.00 58.02           C  
ANISOU 3103  C   LEU B  80     4678   7831   9535    476   -748    -34       C  
ATOM   3104  O   LEU B  80     -22.448   8.667  10.514  1.00 57.61           O  
ANISOU 3104  O   LEU B  80     4674   7694   9520    485   -720     48       O  
ATOM   3105  CB  LEU B  80     -21.501   6.533   8.225  1.00 59.18           C  
ANISOU 3105  CB  LEU B  80     4848   8067   9567    463   -735    -79       C  
ATOM   3106  CG  LEU B  80     -19.980   6.374   8.243  1.00 59.04           C  
ANISOU 3106  CG  LEU B  80     4881   8002   9548    447   -685    -38       C  
ATOM   3107  CD1 LEU B  80     -19.561   5.022   7.683  1.00 59.27           C  
ANISOU 3107  CD1 LEU B  80     4911   8066   9542    425   -672   -131       C  
ATOM   3108  CD2 LEU B  80     -19.306   7.503   7.478  1.00 59.37           C  
ANISOU 3108  CD2 LEU B  80     4948   8083   9526    498   -680     76       C  
ATOM   3109  N   GLY B  81     -24.235   7.795   9.394  1.00 58.08           N  
ANISOU 3109  N   GLY B  81     4623   7932   9511    508   -794    -68       N  
ATOM   3110  CA  GLY B  81     -25.189   8.880   9.699  1.00 57.47           C  
ANISOU 3110  CA  GLY B  81     4522   7862   9449    569   -813    -11       C  
ATOM   3111  C   GLY B  81     -25.298   9.126  11.195  1.00 55.99           C  
ANISOU 3111  C   GLY B  81     4359   7552   9362    540   -776     -3       C  
ATOM   3112  O   GLY B  81     -25.306  10.303  11.596  1.00 55.61           O  
ANISOU 3112  O   GLY B  81     4348   7448   9333    589   -763     79       O  
ATOM   3113  N   ARG B  82     -25.342   8.051  11.991  1.00 55.25           N  
ANISOU 3113  N   ARG B  82     4253   7411   9328    465   -756    -84       N  
ATOM   3114  CA  ARG B  82     -25.652   8.074  13.448  1.00 54.60           C  
ANISOU 3114  CA  ARG B  82     4179   7232   9334    434   -723    -93       C  
ATOM   3115  C   ARG B  82     -24.360   8.224  14.263  1.00 53.57           C  
ANISOU 3115  C   ARG B  82     4128   6981   9243    399   -676    -51       C  
ATOM   3116  O   ARG B  82     -24.401   8.916  15.302  1.00 53.81           O  
ANISOU 3116  O   ARG B  82     4192   6931   9322    405   -652    -14       O  
ATOM   3117  CB  ARG B  82     -26.432   6.814  13.833  1.00 54.59           C  
ANISOU 3117  CB  ARG B  82     4118   7252   9371    370   -724   -197       C  
ATOM   3118  CG  ARG B  82     -27.697   6.607  13.011  1.00 55.57           C  
ANISOU 3118  CG  ARG B  82     4150   7510   9453    390   -776   -247       C  
ATOM   3119  CD  ARG B  82     -28.551   5.453  13.488  1.00 55.69           C  
ANISOU 3119  CD  ARG B  82     4103   7540   9516    314   -774   -346       C  
ATOM   3120  NE  ARG B  82     -27.978   4.164  13.126  1.00 55.62           N  
ANISOU 3120  NE  ARG B  82     4114   7517   9501    239   -765   -423       N  
ATOM   3121  CZ  ARG B  82     -27.138   3.453  13.875  1.00 54.84           C  
ANISOU 3121  CZ  ARG B  82     4076   7306   9454    185   -715   -438       C  
ATOM   3122  NH1 ARG B  82     -26.748   3.887  15.064  1.00 53.93           N  
ANISOU 3122  NH1 ARG B  82     4004   7090   9397    188   -672   -383       N  
ATOM   3123  NH2 ARG B  82     -26.691   2.293  13.426  1.00 55.09           N  
ANISOU 3123  NH2 ARG B  82     4127   7329   9475    132   -707   -510       N  
ATOM   3124  N   TYR B  83     -23.267   7.599  13.817  1.00 52.53           N  
ANISOU 3124  N   TYR B  83     4025   6846   9087    367   -664    -59       N  
ATOM   3125  CA  TYR B  83     -21.893   7.803  14.349  1.00 51.42           C  
ANISOU 3125  CA  TYR B  83     3948   6620   8966    339   -627     -7       C  
ATOM   3126  C   TYR B  83     -21.554   9.298  14.288  1.00 51.14           C  
ANISOU 3126  C   TYR B  83     3957   6555   8917    382   -626     92       C  
ATOM   3127  O   TYR B  83     -21.293   9.903  15.349  1.00 50.14           O  
ANISOU 3127  O   TYR B  83     3872   6338   8839    365   -603    126       O  
ATOM   3128  CB  TYR B  83     -20.902   6.945  13.556  1.00 51.49           C  
ANISOU 3128  CB  TYR B  83     3965   6665   8934    320   -618    -27       C  
ATOM   3129  CG  TYR B  83     -19.443   7.238  13.801  1.00 51.00           C  
ANISOU 3129  CG  TYR B  83     3951   6552   8873    303   -586     37       C  
ATOM   3130  CD1 TYR B  83     -18.964   7.459  15.081  1.00 50.34           C  
ANISOU 3130  CD1 TYR B  83     3900   6377   8851    267   -559     63       C  
ATOM   3131  CD2 TYR B  83     -18.534   7.267  12.753  1.00 51.25           C  
ANISOU 3131  CD2 TYR B  83     3991   6638   8841    321   -582     72       C  
ATOM   3132  CE1 TYR B  83     -17.624   7.721  15.313  1.00 50.16           C  
ANISOU 3132  CE1 TYR B  83     3909   6322   8827    245   -535    121       C  
ATOM   3133  CE2 TYR B  83     -17.189   7.526  12.969  1.00 50.84           C  
ANISOU 3133  CE2 TYR B  83     3970   6553   8792    301   -551    135       C  
ATOM   3134  CZ  TYR B  83     -16.736   7.753  14.255  1.00 50.06           C  
ANISOU 3134  CZ  TYR B  83     3895   6366   8756    260   -531    158       C  
ATOM   3135  OH  TYR B  83     -15.424   8.003  14.497  1.00 49.72           O  
ANISOU 3135  OH  TYR B  83     3872   6304   8714    233   -506    218       O  
ATOM   3136  N   MET B  84     -21.587   9.864  13.077  1.00 51.84           N  
ANISOU 3136  N   MET B  84     4041   6717   8938    434   -650    137       N  
ATOM   3137  CA  MET B  84     -21.303  11.294  12.784  1.00 52.76           C  
ANISOU 3137  CA  MET B  84     4204   6808   9033    480   -648    240       C  
ATOM   3138  C   MET B  84     -22.202  12.190  13.639  1.00 53.12           C  
ANISOU 3138  C   MET B  84     4265   6791   9126    513   -647    259       C  
ATOM   3139  O   MET B  84     -21.676  13.125  14.266  1.00 52.60           O  
ANISOU 3139  O   MET B  84     4264   6629   9091    505   -622    319       O  
ATOM   3140  CB  MET B  84     -21.551  11.608  11.307  1.00 54.08           C  
ANISOU 3140  CB  MET B  84     4349   7084   9113    544   -678    276       C  
ATOM   3141  CG  MET B  84     -20.500  11.041  10.382  1.00 54.96           C  
ANISOU 3141  CG  MET B  84     4464   7253   9165    524   -670    280       C  
ATOM   3142  SD  MET B  84     -18.898  11.865  10.576  1.00 55.94           S  
ANISOU 3142  SD  MET B  84     4658   7296   9299    490   -626    384       S  
ATOM   3143  CE  MET B  84     -18.038  10.711  11.644  1.00 54.70           C  
ANISOU 3143  CE  MET B  84     4498   7080   9204    405   -595    317       C  
ATOM   3144  N   SER B  85     -23.510  11.917  13.646  1.00 54.00           N  
ANISOU 3144  N   SER B  85     4316   6959   9241    549   -671    209       N  
ATOM   3145  CA  SER B  85     -24.513  12.634  14.477  1.00 54.62           C  
ANISOU 3145  CA  SER B  85     4394   6994   9363    592   -666    217       C  
ATOM   3146  C   SER B  85     -24.020  12.684  15.925  1.00 53.44           C  
ANISOU 3146  C   SER B  85     4298   6722   9284    535   -626    206       C  
ATOM   3147  O   SER B  85     -23.698  13.791  16.400  1.00 53.74           O  
ANISOU 3147  O   SER B  85     4407   6670   9340    552   -605    266       O  
ATOM   3148  CB  SER B  85     -25.872  11.991  14.377  1.00 55.65           C  
ANISOU 3148  CB  SER B  85     4433   7218   9493    614   -694    148       C  
ATOM   3149  OG  SER B  85     -26.401  12.128  13.066  1.00 57.25           O  
ANISOU 3149  OG  SER B  85     4586   7543   9622    677   -738    164       O  
ATOM   3150  N   ALA B  86     -23.927  11.517  16.570  1.00 52.27           N  
ANISOU 3150  N   ALA B  86     4122   6568   9170    467   -614    133       N  
ATOM   3151  CA  ALA B  86     -23.458  11.341  17.964  1.00 51.46           C  
ANISOU 3151  CA  ALA B  86     4059   6367   9123    410   -579    116       C  
ATOM   3152  C   ALA B  86     -22.188  12.168  18.184  1.00 51.23           C  
ANISOU 3152  C   ALA B  86     4112   6259   9094    386   -562    183       C  
ATOM   3153  O   ALA B  86     -22.158  12.950  19.157  1.00 50.50           O  
ANISOU 3153  O   ALA B  86     4073   6080   9034    383   -542    202       O  
ATOM   3154  CB  ALA B  86     -23.218   9.879  18.246  1.00 50.90           C  
ANISOU 3154  CB  ALA B  86     3955   6314   9072    344   -570     47       C  
ATOM   3155  N   LEU B  87     -21.201  12.008  17.291  1.00 51.22           N  
ANISOU 3155  N   LEU B  87     4117   6290   9053    368   -568    214       N  
ATOM   3156  CA  LEU B  87     -19.880  12.691  17.344  1.00 51.33           C  
ANISOU 3156  CA  LEU B  87     4192   6247   9061    331   -553    280       C  
ATOM   3157  C   LEU B  87     -20.080  14.192  17.573  1.00 51.96           C  
ANISOU 3157  C   LEU B  87     4338   6252   9152    364   -546    342       C  
ATOM   3158  O   LEU B  87     -19.484  14.735  18.526  1.00 51.52           O  
ANISOU 3158  O   LEU B  87     4339   6105   9128    318   -527    357       O  
ATOM   3159  CB  LEU B  87     -19.133  12.440  16.031  1.00 51.80           C  
ANISOU 3159  CB  LEU B  87     4234   6381   9064    335   -562    313       C  
ATOM   3160  CG  LEU B  87     -17.764  13.111  15.909  1.00 51.99           C  
ANISOU 3160  CG  LEU B  87     4306   6369   9078    294   -544    389       C  
ATOM   3161  CD1 LEU B  87     -16.797  12.585  16.962  1.00 51.23           C  
ANISOU 3161  CD1 LEU B  87     4218   6228   9018    218   -525    368       C  
ATOM   3162  CD2 LEU B  87     -17.193  12.908  14.515  1.00 52.45           C  
ANISOU 3162  CD2 LEU B  87     4341   6516   9070    313   -548    425       C  
ATOM   3163  N   ASN B  88     -20.916  14.813  16.735  1.00 53.05           N  
ANISOU 3163  N   ASN B  88     4468   6428   9261    444   -562    374       N  
ATOM   3164  CA  ASN B  88     -21.151  16.282  16.674  1.00 53.91           C  
ANISOU 3164  CA  ASN B  88     4645   6466   9371    497   -554    446       C  
ATOM   3165  C   ASN B  88     -21.386  16.833  18.089  1.00 53.71           C  
ANISOU 3165  C   ASN B  88     4676   6328   9402    481   -529    424       C  
ATOM   3166  O   ASN B  88     -21.108  18.033  18.307  1.00 54.07           O  
ANISOU 3166  O   ASN B  88     4806   6276   9459    488   -511    478       O  
ATOM   3167  CB  ASN B  88     -22.306  16.610  15.722  1.00 54.80           C  
ANISOU 3167  CB  ASN B  88     4719   6655   9444    602   -577    469       C  
ATOM   3168  CG  ASN B  88     -22.242  18.010  15.148  1.00 55.89           C  
ANISOU 3168  CG  ASN B  88     4929   6742   9563    664   -568    569       C  
ATOM   3169  OD1 ASN B  88     -21.289  18.747  15.381  1.00 55.99           O  
ANISOU 3169  OD1 ASN B  88     5022   6659   9591    616   -543    621       O  
ATOM   3170  ND2 ASN B  88     -23.260  18.388  14.393  1.00 57.38           N  
ANISOU 3170  ND2 ASN B  88     5088   6996   9715    769   -588    599       N  
ATOM   3171  N   HIS B  89     -21.886  15.990  19.003  1.00 53.19           N  
ANISOU 3171  N   HIS B  89     4569   6273   9367    461   -526    347       N  
ATOM   3172  CA  HIS B  89     -22.114  16.301  20.441  1.00 52.74           C  
ANISOU 3172  CA  HIS B  89     4556   6125   9354    442   -500    313       C  
ATOM   3173  C   HIS B  89     -20.870  15.935  21.259  1.00 51.85           C  
ANISOU 3173  C   HIS B  89     4476   5965   9258    339   -489    299       C  
ATOM   3174  O   HIS B  89     -20.386  16.809  22.004  1.00 52.42           O  
ANISOU 3174  O   HIS B  89     4628   5941   9347    308   -473    315       O  
ATOM   3175  CB  HIS B  89     -23.342  15.552  20.985  1.00 52.41           C  
ANISOU 3175  CB  HIS B  89     4446   6132   9332    475   -498    245       C  
ATOM   3176  CG  HIS B  89     -24.625  15.835  20.273  1.00 53.15           C  
ANISOU 3176  CG  HIS B  89     4489   6293   9409    575   -513    254       C  
ATOM   3177  ND1 HIS B  89     -25.728  16.361  20.921  1.00 53.30           N  
ANISOU 3177  ND1 HIS B  89     4509   6291   9450    644   -495    241       N  
ATOM   3178  CD2 HIS B  89     -24.997  15.643  18.988  1.00 53.41           C  
ANISOU 3178  CD2 HIS B  89     4463   6426   9401    621   -545    274       C  
ATOM   3179  CE1 HIS B  89     -26.716  16.491  20.059  1.00 54.04           C  
ANISOU 3179  CE1 HIS B  89     4540   6471   9519    730   -517    257       C  
ATOM   3180  NE2 HIS B  89     -26.293  16.057  18.867  1.00 53.87           N  
ANISOU 3180  NE2 HIS B  89     4483   6527   9457    715   -550    276       N  
ATOM   3181  N   THR B  90     -20.377  14.696  21.122  1.00 50.65           N  
ANISOU 3181  N   THR B  90     4265   5878   9098    291   -497    268       N  
ATOM   3182  CA  THR B  90     -19.356  14.079  22.017  1.00 49.51           C  
ANISOU 3182  CA  THR B  90     4130   5712   8970    207   -487    247       C  
ATOM   3183  C   THR B  90     -18.074  14.918  21.994  1.00 49.72           C  
ANISOU 3183  C   THR B  90     4216   5688   8987    151   -486    304       C  
ATOM   3184  O   THR B  90     -17.322  14.861  22.983  1.00 49.46           O  
ANISOU 3184  O   THR B  90     4209   5617   8967     85   -479    292       O  
ATOM   3185  CB  THR B  90     -19.059  12.616  21.652  1.00 48.75           C  
ANISOU 3185  CB  THR B  90     3963   5694   8863    184   -492    214       C  
ATOM   3186  OG1 THR B  90     -18.596  12.542  20.305  1.00 48.24           O  
ANISOU 3186  OG1 THR B  90     3876   5691   8762    197   -507    249       O  
ATOM   3187  CG2 THR B  90     -20.258  11.710  21.830  1.00 48.75           C  
ANISOU 3187  CG2 THR B  90     3907   5735   8880    214   -491    150       C  
ATOM   3188  N   LYS B  91     -17.849  15.670  20.913  1.00 49.94           N  
ANISOU 3188  N   LYS B  91     4263   5720   8991    174   -492    365       N  
ATOM   3189  CA  LYS B  91     -16.660  16.542  20.722  1.00 49.87           C  
ANISOU 3189  CA  LYS B  91     4307   5665   8974    115   -487    430       C  
ATOM   3190  C   LYS B  91     -16.805  17.849  21.522  1.00 50.02           C  
ANISOU 3190  C   LYS B  91     4422   5563   9020    103   -474    441       C  
ATOM   3191  O   LYS B  91     -15.785  18.541  21.682  1.00 49.95           O  
ANISOU 3191  O   LYS B  91     4464   5501   9014     28   -470    479       O  
ATOM   3192  CB  LYS B  91     -16.448  16.799  19.227  1.00 50.27           C  
ANISOU 3192  CB  LYS B  91     4342   5770   8986    149   -493    496       C  
ATOM   3193  CG  LYS B  91     -17.498  17.672  18.560  1.00 51.35           C  
ANISOU 3193  CG  LYS B  91     4509   5887   9112    240   -494    530       C  
ATOM   3194  CD  LYS B  91     -17.206  17.933  17.105  1.00 52.08           C  
ANISOU 3194  CD  LYS B  91     4589   6040   9157    273   -498    603       C  
ATOM   3195  CE  LYS B  91     -18.030  19.070  16.542  1.00 53.15           C  
ANISOU 3195  CE  LYS B  91     4776   6136   9283    359   -495    660       C  
ATOM   3196  NZ  LYS B  91     -17.456  19.583  15.275  1.00 54.17           N  
ANISOU 3196  NZ  LYS B  91     4918   6297   9365    371   -490    753       N  
ATOM   3197  N   LYS B  92     -18.008  18.180  22.003  1.00 50.19           N  
ANISOU 3197  N   LYS B  92     4468   5543   9058    171   -467    407       N  
ATOM   3198  CA  LYS B  92     -18.262  19.362  22.879  1.00 51.00           C  
ANISOU 3198  CA  LYS B  92     4669   5521   9185    172   -448    403       C  
ATOM   3199  C   LYS B  92     -18.235  18.929  24.352  1.00 49.99           C  
ANISOU 3199  C   LYS B  92     4549   5369   9074    125   -442    331       C  
ATOM   3200  O   LYS B  92     -18.160  19.813  25.227  1.00 50.10           O  
ANISOU 3200  O   LYS B  92     4650   5282   9101    100   -427    315       O  
ATOM   3201  CB  LYS B  92     -19.598  20.022  22.525  1.00 51.99           C  
ANISOU 3201  CB  LYS B  92     4817   5622   9315    290   -437    414       C  
ATOM   3202  CG  LYS B  92     -19.713  20.532  21.094  1.00 53.08           C  
ANISOU 3202  CG  LYS B  92     4952   5786   9427    351   -443    492       C  
ATOM   3203  CD  LYS B  92     -21.119  20.974  20.735  1.00 54.16           C  
ANISOU 3203  CD  LYS B  92     5085   5931   9562    482   -438    502       C  
ATOM   3204  CE  LYS B  92     -21.217  21.634  19.374  1.00 55.36           C  
ANISOU 3204  CE  LYS B  92     5248   6102   9682    550   -443    592       C  
ATOM   3205  NZ  LYS B  92     -22.590  21.537  18.823  1.00 56.03           N  
ANISOU 3205  NZ  LYS B  92     5273   6266   9748    679   -455    593       N  
ATOM   3206  N   TRP B  93     -18.303  17.620  24.608  1.00 48.79           N  
ANISOU 3206  N   TRP B  93     4315   5303   8919    115   -450    289       N  
ATOM   3207  CA  TRP B  93     -18.088  17.002  25.944  1.00 48.45           C  
ANISOU 3207  CA  TRP B  93     4268   5256   8883     64   -444    233       C  
ATOM   3208  C   TRP B  93     -16.637  17.221  26.385  1.00 48.42           C  
ANISOU 3208  C   TRP B  93     4296   5231   8870    -41   -455    250       C  
ATOM   3209  O   TRP B  93     -15.745  17.257  25.514  1.00 48.84           O  
ANISOU 3209  O   TRP B  93     4329   5315   8911    -77   -468    301       O  
ATOM   3210  CB  TRP B  93     -18.402  15.503  25.908  1.00 47.77           C  
ANISOU 3210  CB  TRP B  93     4088   5265   8797     77   -447    199       C  
ATOM   3211  CG  TRP B  93     -19.838  15.149  25.685  1.00 47.42           C  
ANISOU 3211  CG  TRP B  93     3999   5253   8762    160   -438    170       C  
ATOM   3212  CD1 TRP B  93     -20.879  15.990  25.419  1.00 48.00           C  
ANISOU 3212  CD1 TRP B  93     4095   5299   8842    239   -430    176       C  
ATOM   3213  CD2 TRP B  93     -20.383  13.820  25.670  1.00 46.90           C  
ANISOU 3213  CD2 TRP B  93     3852   5263   8703    171   -436    131       C  
ATOM   3214  NE1 TRP B  93     -22.038  15.277  25.266  1.00 48.03           N  
ANISOU 3214  NE1 TRP B  93     4026   5369   8853    295   -426    143       N  
ATOM   3215  CE2 TRP B  93     -21.765  13.943  25.413  1.00 47.31           C  
ANISOU 3215  CE2 TRP B  93     3873   5336   8764    248   -430    113       C  
ATOM   3216  CE3 TRP B  93     -19.840  12.544  25.862  1.00 46.23           C  
ANISOU 3216  CE3 TRP B  93     3720   5224   8619    125   -436    112       C  
ATOM   3217  CZ2 TRP B  93     -22.608  12.836  25.352  1.00 46.89           C  
ANISOU 3217  CZ2 TRP B  93     3740   5353   8723    263   -426     71       C  
ATOM   3218  CZ3 TRP B  93     -20.675  11.451  25.797  1.00 46.16           C  
ANISOU 3218  CZ3 TRP B  93     3646   5268   8624    145   -427     72       C  
ATOM   3219  CH2 TRP B  93     -22.040  11.597  25.546  1.00 46.42           C  
ANISOU 3219  CH2 TRP B  93     3646   5323   8667    206   -423     49       C  
ATOM   3220  N   LYS B  94     -16.407  17.329  27.692  1.00 48.13           N  
ANISOU 3220  N   LYS B  94     4298   5154   8832    -89   -452    209       N  
ATOM   3221  CA  LYS B  94     -15.047  17.433  28.275  1.00 48.04           C  
ANISOU 3221  CA  LYS B  94     4303   5142   8806   -195   -469    217       C  
ATOM   3222  C   LYS B  94     -14.642  16.053  28.798  1.00 46.79           C  
ANISOU 3222  C   LYS B  94     4068   5074   8636   -215   -476    197       C  
ATOM   3223  O   LYS B  94     -15.430  15.452  29.554  1.00 46.98           O  
ANISOU 3223  O   LYS B  94     4081   5106   8663   -176   -462    153       O  
ATOM   3224  CB  LYS B  94     -15.028  18.528  29.345  1.00 49.22           C  
ANISOU 3224  CB  LYS B  94     4554   5191   8954   -237   -464    182       C  
ATOM   3225  CG  LYS B  94     -15.517  19.892  28.869  1.00 50.39           C  
ANISOU 3225  CG  LYS B  94     4794   5232   9120   -204   -448    201       C  
ATOM   3226  CD  LYS B  94     -14.921  20.316  27.538  1.00 50.88           C  
ANISOU 3226  CD  LYS B  94     4848   5296   9187   -221   -455    277       C  
ATOM   3227  CE  LYS B  94     -15.369  21.684  27.069  1.00 51.94           C  
ANISOU 3227  CE  LYS B  94     5081   5314   9338   -186   -434    307       C  
ATOM   3228  NZ  LYS B  94     -14.661  22.084  25.829  1.00 52.36           N  
ANISOU 3228  NZ  LYS B  94     5128   5374   9391   -215   -438    390       N  
ATOM   3229  N   TYR B  95     -13.479  15.561  28.366  1.00 45.65           N  
ANISOU 3229  N   TYR B  95     3871   4994   8478   -267   -493    236       N  
ATOM   3230  CA  TYR B  95     -12.843  14.309  28.845  1.00 44.44           C  
ANISOU 3230  CA  TYR B  95     3650   4923   8311   -286   -499    231       C  
ATOM   3231  C   TYR B  95     -11.643  14.670  29.710  1.00 44.00           C  
ANISOU 3231  C   TYR B  95     3609   4875   8231   -380   -521    238       C  
ATOM   3232  O   TYR B  95     -10.514  14.660  29.236  1.00 43.78           O  
ANISOU 3232  O   TYR B  95     3543   4899   8193   -432   -536    283       O  
ATOM   3233  CB  TYR B  95     -12.453  13.441  27.650  1.00 44.25           C  
ANISOU 3233  CB  TYR B  95     3550   4976   8285   -260   -498    269       C  
ATOM   3234  CG  TYR B  95     -13.604  13.192  26.717  1.00 44.11           C  
ANISOU 3234  CG  TYR B  95     3518   4957   8283   -178   -484    258       C  
ATOM   3235  CD1 TYR B  95     -14.501  12.170  26.961  1.00 43.90           C  
ANISOU 3235  CD1 TYR B  95     3459   4951   8268   -127   -469    215       C  
ATOM   3236  CD2 TYR B  95     -13.827  14.006  25.622  1.00 44.62           C  
ANISOU 3236  CD2 TYR B  95     3602   5003   8347   -155   -486    291       C  
ATOM   3237  CE1 TYR B  95     -15.580  11.942  26.124  1.00 44.20           C  
ANISOU 3237  CE1 TYR B  95     3475   5000   8318    -62   -462    200       C  
ATOM   3238  CE2 TYR B  95     -14.893  13.787  24.766  1.00 44.74           C  
ANISOU 3238  CE2 TYR B  95     3597   5034   8368    -79   -480    281       C  
ATOM   3239  CZ  TYR B  95     -15.780  12.755  25.024  1.00 44.67           C  
ANISOU 3239  CZ  TYR B  95     3548   5053   8370    -35   -471    231       C  
ATOM   3240  OH  TYR B  95     -16.848  12.528  24.206  1.00 44.91           O  
ANISOU 3240  OH  TYR B  95     3549   5110   8403     30   -470    216       O  
ATOM   3241  N   PRO B  96     -11.848  15.053  30.991  1.00 43.76           N  
ANISOU 3241  N   PRO B  96     3632   4803   8188   -408   -524    193       N  
ATOM   3242  CA  PRO B  96     -10.727  15.287  31.894  1.00 43.94           C  
ANISOU 3242  CA  PRO B  96     3662   4853   8180   -500   -552    191       C  
ATOM   3243  C   PRO B  96     -10.026  13.975  32.278  1.00 43.48           C  
ANISOU 3243  C   PRO B  96     3519   4902   8099   -498   -561    210       C  
ATOM   3244  O   PRO B  96     -10.656  12.922  32.254  1.00 42.70           O  
ANISOU 3244  O   PRO B  96     3384   4829   8009   -425   -539    203       O  
ATOM   3245  CB  PRO B  96     -11.368  15.965  33.116  1.00 44.23           C  
ANISOU 3245  CB  PRO B  96     3785   4816   8202   -509   -548    128       C  
ATOM   3246  CG  PRO B  96     -12.799  15.488  33.099  1.00 43.82           C  
ANISOU 3246  CG  PRO B  96     3737   4740   8172   -405   -512    100       C  
ATOM   3247  CD  PRO B  96     -13.145  15.317  31.633  1.00 43.63           C  
ANISOU 3247  CD  PRO B  96     3673   4722   8182   -351   -501    140       C  
ATOM   3248  N   GLN B  97      -8.724  14.074  32.565  1.00 43.50           N  
ANISOU 3248  N   GLN B  97     3489   4966   8073   -578   -592    237       N  
ATOM   3249  CA  GLN B  97      -7.965  13.076  33.353  1.00 42.96           C  
ANISOU 3249  CA  GLN B  97     3356   4997   7969   -586   -607    251       C  
ATOM   3250  C   GLN B  97      -8.469  13.159  34.792  1.00 42.43           C  
ANISOU 3250  C   GLN B  97     3344   4906   7872   -590   -611    196       C  
ATOM   3251  O   GLN B  97      -8.483  14.271  35.350  1.00 42.64           O  
ANISOU 3251  O   GLN B  97     3441   4875   7883   -654   -628    157       O  
ATOM   3252  CB  GLN B  97      -6.457  13.350  33.294  1.00 43.88           C  
ANISOU 3252  CB  GLN B  97     3419   5194   8059   -676   -644    294       C  
ATOM   3253  CG  GLN B  97      -5.833  13.143  31.917  1.00 43.75           C  
ANISOU 3253  CG  GLN B  97     3336   5224   8063   -667   -635    356       C  
ATOM   3254  CD  GLN B  97      -6.088  11.756  31.385  1.00 42.98           C  
ANISOU 3254  CD  GLN B  97     3178   5174   7976   -564   -605    377       C  
ATOM   3255  OE1 GLN B  97      -6.653  11.585  30.304  1.00 42.61           O  
ANISOU 3255  OE1 GLN B  97     3132   5098   7957   -508   -578    384       O  
ATOM   3256  NE2 GLN B  97      -5.704  10.757  32.168  1.00 42.56           N  
ANISOU 3256  NE2 GLN B  97     3080   5191   7897   -537   -608    385       N  
ATOM   3257  N   VAL B  98      -8.897  12.032  35.354  1.00 41.57           N  
ANISOU 3257  N   VAL B  98     3208   4832   7753   -524   -590    192       N  
ATOM   3258  CA  VAL B  98      -9.205  11.920  36.805  1.00 41.76           C  
ANISOU 3258  CA  VAL B  98     3269   4861   7735   -525   -592    153       C  
ATOM   3259  C   VAL B  98      -8.431  10.718  37.347  1.00 41.60           C  
ANISOU 3259  C   VAL B  98     3177   4948   7679   -506   -600    197       C  
ATOM   3260  O   VAL B  98      -8.672   9.600  36.873  1.00 41.02           O  
ANISOU 3260  O   VAL B  98     3058   4893   7633   -434   -569    227       O  
ATOM   3261  CB  VAL B  98     -10.721  11.825  37.063  1.00 41.46           C  
ANISOU 3261  CB  VAL B  98     3284   4748   7720   -454   -547    109       C  
ATOM   3262  CG1 VAL B  98     -11.051  11.989  38.539  1.00 41.87           C  
ANISOU 3262  CG1 VAL B  98     3389   4798   7721   -462   -546     64       C  
ATOM   3263  CG2 VAL B  98     -11.497  12.837  36.231  1.00 41.43           C  
ANISOU 3263  CG2 VAL B  98     3332   4649   7759   -444   -534     84       C  
ATOM   3264  N   ASN B  99      -7.486  10.977  38.254  1.00 42.43           N  
ANISOU 3264  N   ASN B  99     3273   5122   7726   -571   -643    200       N  
ATOM   3265  CA  ASN B  99      -6.632   9.965  38.926  1.00 42.66           C  
ANISOU 3265  CA  ASN B  99     3233   5267   7707   -554   -658    247       C  
ATOM   3266  C   ASN B  99      -6.075   8.977  37.895  1.00 42.11           C  
ANISOU 3266  C   ASN B  99     3078   5249   7671   -501   -642    314       C  
ATOM   3267  O   ASN B  99      -5.969   7.783  38.227  1.00 42.03           O  
ANISOU 3267  O   ASN B  99     3030   5289   7650   -432   -621    352       O  
ATOM   3268  CB  ASN B  99      -7.399   9.246  40.035  1.00 42.88           C  
ANISOU 3268  CB  ASN B  99     3292   5293   7706   -493   -629    231       C  
ATOM   3269  CG  ASN B  99      -6.551   9.063  41.272  1.00 43.83           C  
ANISOU 3269  CG  ASN B  99     3391   5519   7742   -522   -669    247       C  
ATOM   3270  OD1 ASN B  99      -6.250   7.937  41.657  1.00 44.46           O  
ANISOU 3270  OD1 ASN B  99     3422   5669   7799   -462   -657    301       O  
ATOM   3271  ND2 ASN B  99      -6.149  10.166  41.883  1.00 44.44           N  
ANISOU 3271  ND2 ASN B  99     3505   5609   7772   -615   -717    202       N  
ATOM   3272  N   GLY B 100      -5.718   9.470  36.702  1.00 41.87           N  
ANISOU 3272  N   GLY B 100     3025   5204   7677   -530   -647    329       N  
ATOM   3273  CA  GLY B 100      -5.033   8.713  35.636  1.00 41.45           C  
ANISOU 3273  CA  GLY B 100     2891   5209   7647   -489   -634    389       C  
ATOM   3274  C   GLY B 100      -5.955   8.423  34.470  1.00 40.55           C  
ANISOU 3274  C   GLY B 100     2796   5018   7592   -427   -590    378       C  
ATOM   3275  O   GLY B 100      -5.496   8.494  33.313  1.00 40.98           O  
ANISOU 3275  O   GLY B 100     2811   5090   7667   -427   -586    408       O  
ATOM   3276  N   LEU B 101      -7.220   8.123  34.768  1.00 39.70           N  
ANISOU 3276  N   LEU B 101     2742   4833   7506   -377   -557    336       N  
ATOM   3277  CA  LEU B 101      -8.205   7.572  33.805  1.00 38.54           C  
ANISOU 3277  CA  LEU B 101     2603   4627   7411   -310   -515    322       C  
ATOM   3278  C   LEU B 101      -8.923   8.723  33.104  1.00 37.99           C  
ANISOU 3278  C   LEU B 101     2581   4483   7368   -335   -519    287       C  
ATOM   3279  O   LEU B 101      -9.148   9.761  33.761  1.00 37.98           O  
ANISOU 3279  O   LEU B 101     2636   4441   7353   -384   -537    256       O  
ATOM   3280  CB  LEU B 101      -9.179   6.690  34.586  1.00 38.24           C  
ANISOU 3280  CB  LEU B 101     2590   4556   7380   -255   -480    298       C  
ATOM   3281  CG  LEU B 101      -8.519   5.566  35.378  1.00 38.49           C  
ANISOU 3281  CG  LEU B 101     2587   4653   7383   -222   -471    340       C  
ATOM   3282  CD1 LEU B 101      -9.225   5.326  36.701  1.00 38.62           C  
ANISOU 3282  CD1 LEU B 101     2646   4648   7378   -210   -455    319       C  
ATOM   3283  CD2 LEU B 101      -8.468   4.295  34.552  1.00 38.38           C  
ANISOU 3283  CD2 LEU B 101     2535   4643   7402   -153   -433    367       C  
ATOM   3284  N   THR B 102      -9.250   8.548  31.822  1.00 37.55           N  
ANISOU 3284  N   THR B 102     2509   4411   7346   -299   -501    293       N  
ATOM   3285  CA  THR B 102     -10.127   9.477  31.064  1.00 37.84           C  
ANISOU 3285  CA  THR B 102     2589   4378   7409   -298   -499    267       C  
ATOM   3286  C   THR B 102     -11.571   9.260  31.526  1.00 37.83           C  
ANISOU 3286  C   THR B 102     2626   4318   7430   -251   -472    217       C  
ATOM   3287  O   THR B 102     -12.088   8.142  31.333  1.00 37.40           O  
ANISOU 3287  O   THR B 102     2542   4273   7393   -200   -445    209       O  
ATOM   3288  CB  THR B 102     -10.026   9.297  29.544  1.00 37.57           C  
ANISOU 3288  CB  THR B 102     2519   4363   7392   -268   -490    292       C  
ATOM   3289  OG1 THR B 102      -8.675   9.480  29.123  1.00 38.07           O  
ANISOU 3289  OG1 THR B 102     2540   4491   7434   -309   -508    343       O  
ATOM   3290  CG2 THR B 102     -10.906  10.273  28.795  1.00 37.51           C  
ANISOU 3290  CG2 THR B 102     2554   4293   7403   -259   -490    275       C  
ATOM   3291  N   SER B 103     -12.177  10.284  32.131  1.00 38.47           N  
ANISOU 3291  N   SER B 103     2768   4340   7508   -271   -477    183       N  
ATOM   3292  CA  SER B 103     -13.612  10.319  32.513  1.00 38.79           C  
ANISOU 3292  CA  SER B 103     2842   4328   7568   -225   -450    137       C  
ATOM   3293  C   SER B 103     -14.378  11.165  31.493  1.00 39.40           C  
ANISOU 3293  C   SER B 103     2941   4357   7671   -198   -448    129       C  
ATOM   3294  O   SER B 103     -13.795  11.472  30.432  1.00 40.04           O  
ANISOU 3294  O   SER B 103     3005   4451   7754   -210   -464    163       O  
ATOM   3295  CB  SER B 103     -13.779  10.851  33.904  1.00 39.05           C  
ANISOU 3295  CB  SER B 103     2930   4334   7573   -250   -450    106       C  
ATOM   3296  OG  SER B 103     -15.035  10.475  34.438  1.00 38.58           O  
ANISOU 3296  OG  SER B 103     2882   4250   7526   -199   -414     70       O  
ATOM   3297  N   ILE B 104     -15.629  11.524  31.797  1.00 39.90           N  
ANISOU 3297  N   ILE B 104     3036   4374   7749   -157   -427     91       N  
ATOM   3298  CA  ILE B 104     -16.442  12.479  30.986  1.00 40.42           C  
ANISOU 3298  CA  ILE B 104     3129   4392   7833   -118   -425     86       C  
ATOM   3299  C   ILE B 104     -17.211  13.399  31.935  1.00 41.25           C  
ANISOU 3299  C   ILE B 104     3305   4433   7935   -103   -409     48       C  
ATOM   3300  O   ILE B 104     -17.928  12.882  32.810  1.00 41.16           O  
ANISOU 3300  O   ILE B 104     3286   4429   7922    -77   -384     15       O  
ATOM   3301  CB  ILE B 104     -17.394  11.747  30.023  1.00 40.18           C  
ANISOU 3301  CB  ILE B 104     3041   4395   7830    -57   -412     81       C  
ATOM   3302  CG1 ILE B 104     -16.759  10.499  29.405  1.00 39.91           C  
ANISOU 3302  CG1 ILE B 104     2943   4424   7796    -66   -416     99       C  
ATOM   3303  CG2 ILE B 104     -17.885  12.711  28.960  1.00 40.58           C  
ANISOU 3303  CG2 ILE B 104     3109   4420   7889    -19   -421     96       C  
ATOM   3304  CD1 ILE B 104     -17.646   9.790  28.409  1.00 39.87           C  
ANISOU 3304  CD1 ILE B 104     2886   4451   7811    -18   -408     84       C  
ATOM   3305  N   LYS B 105     -17.054  14.713  31.770  1.00 42.48           N  
ANISOU 3305  N   LYS B 105     3528   4522   8088   -116   -419     53       N  
ATOM   3306  CA  LYS B 105     -17.842  15.728  32.516  1.00 43.73           C  
ANISOU 3306  CA  LYS B 105     3766   4604   8244    -87   -398     14       C  
ATOM   3307  C   LYS B 105     -19.319  15.529  32.138  1.00 43.97           C  
ANISOU 3307  C   LYS B 105     3764   4642   8300      9   -369      0       C  
ATOM   3308  O   LYS B 105     -19.609  15.361  30.927  1.00 43.87           O  
ANISOU 3308  O   LYS B 105     3704   4658   8306     46   -377     30       O  
ATOM   3309  CB  LYS B 105     -17.330  17.140  32.215  1.00 44.55           C  
ANISOU 3309  CB  LYS B 105     3955   4624   8347   -121   -412     29       C  
ATOM   3310  CG  LYS B 105     -17.950  18.240  33.067  1.00 45.57           C  
ANISOU 3310  CG  LYS B 105     4186   4659   8470    -98   -388    -16       C  
ATOM   3311  CD  LYS B 105     -18.021  19.587  32.374  1.00 46.44           C  
ANISOU 3311  CD  LYS B 105     4376   4670   8599    -83   -385      5       C  
ATOM   3312  CE  LYS B 105     -18.872  20.592  33.121  1.00 47.32           C  
ANISOU 3312  CE  LYS B 105     4588   4683   8709    -29   -350    -42       C  
ATOM   3313  NZ  LYS B 105     -19.634  21.454  32.186  1.00 48.00           N  
ANISOU 3313  NZ  LYS B 105     4710   4703   8823     59   -330     -8       N  
ATOM   3314  N   TRP B 106     -20.211  15.520  33.133  1.00 44.11           N  
ANISOU 3314  N   TRP B 106     3800   4647   8312     48   -337    -42       N  
ATOM   3315  CA  TRP B 106     -21.607  15.039  32.969  1.00 44.27           C  
ANISOU 3315  CA  TRP B 106     3762   4703   8354    130   -307    -57       C  
ATOM   3316  C   TRP B 106     -22.356  15.882  31.923  1.00 44.67           C  
ANISOU 3316  C   TRP B 106     3818   4729   8426    204   -307    -38       C  
ATOM   3317  O   TRP B 106     -22.244  17.127  31.951  1.00 45.04           O  
ANISOU 3317  O   TRP B 106     3951   4693   8467    218   -305    -33       O  
ATOM   3318  CB  TRP B 106     -22.355  14.985  34.306  1.00 44.63           C  
ANISOU 3318  CB  TRP B 106     3829   4741   8384    156   -266   -102       C  
ATOM   3319  CG  TRP B 106     -23.687  14.338  34.122  1.00 44.49           C  
ANISOU 3319  CG  TRP B 106     3733   4779   8392    223   -235   -111       C  
ATOM   3320  CD1 TRP B 106     -23.988  13.011  34.219  1.00 44.17           C  
ANISOU 3320  CD1 TRP B 106     3610   4808   8364    207   -222   -113       C  
ATOM   3321  CD2 TRP B 106     -24.878  14.990  33.670  1.00 45.36           C  
ANISOU 3321  CD2 TRP B 106     3830   4883   8520    313   -215   -115       C  
ATOM   3322  NE1 TRP B 106     -25.299  12.796  33.900  1.00 44.53           N  
ANISOU 3322  NE1 TRP B 106     3590   4894   8435    270   -197   -123       N  
ATOM   3323  CE2 TRP B 106     -25.873  13.994  33.561  1.00 45.44           C  
ANISOU 3323  CE2 TRP B 106     3740   4972   8551    341   -194   -123       C  
ATOM   3324  CE3 TRP B 106     -25.206  16.318  33.377  1.00 46.04           C  
ANISOU 3324  CE3 TRP B 106     3982   4902   8606    376   -211   -110       C  
ATOM   3325  CZ2 TRP B 106     -27.180  14.296  33.183  1.00 45.83           C  
ANISOU 3325  CZ2 TRP B 106     3741   5053   8618    427   -173   -128       C  
ATOM   3326  CZ3 TRP B 106     -26.495  16.611  32.993  1.00 46.57           C  
ANISOU 3326  CZ3 TRP B 106     4007   4994   8690    475   -188   -110       C  
ATOM   3327  CH2 TRP B 106     -27.467  15.612  32.901  1.00 46.53           C  
ANISOU 3327  CH2 TRP B 106     3890   5086   8703    500   -171   -119       C  
ATOM   3328  N   ALA B 107     -23.106  15.209  31.043  1.00 44.31           N  
ANISOU 3328  N   ALA B 107     3685   4751   8400    249   -309    -27       N  
ATOM   3329  CA  ALA B 107     -23.849  15.807  29.910  1.00 44.75           C  
ANISOU 3329  CA  ALA B 107     3720   4813   8467    326   -316     -1       C  
ATOM   3330  C   ALA B 107     -24.778  14.764  29.269  1.00 44.84           C  
ANISOU 3330  C   ALA B 107     3618   4924   8494    360   -318     -9       C  
ATOM   3331  O   ALA B 107     -24.351  13.615  29.073  1.00 44.31           O  
ANISOU 3331  O   ALA B 107     3496   4909   8430    305   -330    -15       O  
ATOM   3332  CB  ALA B 107     -22.878  16.365  28.900  1.00 44.42           C  
ANISOU 3332  CB  ALA B 107     3713   4745   8419    297   -349     47       C  
ATOM   3333  N   ASP B 108     -26.013  15.160  28.951  1.00 45.50           N  
ANISOU 3333  N   ASP B 108     3667   5034   8586    449   -305    -11       N  
ATOM   3334  CA  ASP B 108     -26.941  14.391  28.079  1.00 45.63           C  
ANISOU 3334  CA  ASP B 108     3570   5153   8611    483   -318    -15       C  
ATOM   3335  C   ASP B 108     -27.008  12.943  28.579  1.00 45.30           C  
ANISOU 3335  C   ASP B 108     3462   5164   8584    417   -306    -53       C  
ATOM   3336  O   ASP B 108     -26.962  12.021  27.735  1.00 45.37           O  
ANISOU 3336  O   ASP B 108     3403   5237   8597    387   -331    -57       O  
ATOM   3337  CB  ASP B 108     -26.512  14.480  26.611  1.00 45.45           C  
ANISOU 3337  CB  ASP B 108     3530   5163   8575    488   -362     23       C  
ATOM   3338  CG  ASP B 108     -26.045  15.865  26.200  1.00 45.94           C  
ANISOU 3338  CG  ASP B 108     3682   5149   8623    526   -370     73       C  
ATOM   3339  OD1 ASP B 108     -26.095  16.769  27.053  1.00 46.79           O  
ANISOU 3339  OD1 ASP B 108     3871   5171   8736    550   -341     70       O  
ATOM   3340  OD2 ASP B 108     -25.623  16.027  25.039  1.00 45.85           O  
ANISOU 3340  OD2 ASP B 108     3665   5161   8595    531   -400    115       O  
ATOM   3341  N   ASN B 109     -27.106  12.771  29.903  1.00 45.27           N  
ANISOU 3341  N   ASN B 109     3484   5130   8584    398   -268    -79       N  
ATOM   3342  CA  ASN B 109     -27.247  11.463  30.598  1.00 44.54           C  
ANISOU 3342  CA  ASN B 109     3341   5074   8506    341   -243   -107       C  
ATOM   3343  C   ASN B 109     -26.061  10.553  30.248  1.00 43.52           C  
ANISOU 3343  C   ASN B 109     3214   4945   8375    262   -268    -97       C  
ATOM   3344  O   ASN B 109     -26.332   9.373  29.961  1.00 43.33           O  
ANISOU 3344  O   ASN B 109     3123   4970   8370    230   -265   -114       O  
ATOM   3345  CB  ASN B 109     -28.570  10.781  30.236  1.00 44.98           C  
ANISOU 3345  CB  ASN B 109     3288   5216   8586    366   -231   -129       C  
ATOM   3346  CG  ASN B 109     -29.776  11.679  30.432  1.00 46.08           C  
ANISOU 3346  CG  ASN B 109     3406   5374   8725    459   -208   -132       C  
ATOM   3347  OD1 ASN B 109     -29.649  12.803  30.913  1.00 46.95           O  
ANISOU 3347  OD1 ASN B 109     3597   5422   8820    509   -194   -121       O  
ATOM   3348  ND2 ASN B 109     -30.951  11.199  30.058  1.00 45.77           N  
ANISOU 3348  ND2 ASN B 109     3260   5425   8704    483   -202   -147       N  
ATOM   3349  N   ASN B 110     -24.815  11.068  30.287  1.00 42.37           N  
ANISOU 3349  N   ASN B 110     3142   4746   8208    232   -289    -73       N  
ATOM   3350  CA  ASN B 110     -23.593  10.354  29.812  1.00 41.43           C  
ANISOU 3350  CA  ASN B 110     3022   4634   8083    171   -314    -54       C  
ATOM   3351  C   ASN B 110     -22.865   9.651  30.972  1.00 40.53           C  
ANISOU 3351  C   ASN B 110     2932   4503   7961    117   -294    -57       C  
ATOM   3352  O   ASN B 110     -21.738   9.176  30.747  1.00 40.28           O  
ANISOU 3352  O   ASN B 110     2907   4476   7920     74   -312    -36       O  
ATOM   3353  CB  ASN B 110     -22.630  11.275  29.047  1.00 41.66           C  
ANISOU 3353  CB  ASN B 110     3099   4635   8092    167   -349    -17       C  
ATOM   3354  CG  ASN B 110     -21.808  12.208  29.920  1.00 42.11           C  
ANISOU 3354  CG  ASN B 110     3243   4625   8130    139   -348     -5       C  
ATOM   3355  OD1 ASN B 110     -21.844  12.135  31.147  1.00 42.63           O  
ANISOU 3355  OD1 ASN B 110     3338   4669   8189    122   -325    -27       O  
ATOM   3356  ND2 ASN B 110     -21.044  13.091  29.297  1.00 42.26           N  
ANISOU 3356  ND2 ASN B 110     3307   4612   8137    127   -373     28       N  
ATOM   3357  N   CYS B 111     -23.462   9.577  32.165  1.00 40.01           N  
ANISOU 3357  N   CYS B 111     2878   4428   7896    124   -257    -78       N  
ATOM   3358  CA  CYS B 111     -22.881   8.867  33.337  1.00 39.36           C  
ANISOU 3358  CA  CYS B 111     2817   4339   7799     81   -235    -76       C  
ATOM   3359  C   CYS B 111     -22.500   7.438  32.927  1.00 38.74           C  
ANISOU 3359  C   CYS B 111     2690   4291   7739     47   -233    -66       C  
ATOM   3360  O   CYS B 111     -21.373   6.999  33.272  1.00 38.82           O  
ANISOU 3360  O   CYS B 111     2722   4297   7731     12   -241    -42       O  
ATOM   3361  CB  CYS B 111     -23.837   8.864  34.527  1.00 39.70           C  
ANISOU 3361  CB  CYS B 111     2864   4381   7837    103   -187    -99       C  
ATOM   3362  SG  CYS B 111     -25.453   8.105  34.199  1.00 39.92           S  
ANISOU 3362  SG  CYS B 111     2798   4458   7908    132   -150   -122       S  
ATOM   3363  N   TYR B 112     -23.380   6.765  32.177  1.00 38.19           N  
ANISOU 3363  N   TYR B 112     2555   4251   7702     57   -225    -85       N  
ATOM   3364  CA  TYR B 112     -23.288   5.318  31.837  1.00 37.76           C  
ANISOU 3364  CA  TYR B 112     2460   4213   7673     25   -212    -90       C  
ATOM   3365  C   TYR B 112     -22.145   5.081  30.832  1.00 37.40           C  
ANISOU 3365  C   TYR B 112     2419   4172   7618     12   -248    -71       C  
ATOM   3366  O   TYR B 112     -21.606   3.954  30.807  1.00 37.07           O  
ANISOU 3366  O   TYR B 112     2371   4127   7586    -11   -234    -65       O  
ATOM   3367  CB  TYR B 112     -24.648   4.783  31.363  1.00 37.58           C  
ANISOU 3367  CB  TYR B 112     2367   4223   7686     30   -194   -126       C  
ATOM   3368  CG  TYR B 112     -24.937   4.972  29.897  1.00 37.20           C  
ANISOU 3368  CG  TYR B 112     2277   4213   7643     46   -234   -143       C  
ATOM   3369  CD1 TYR B 112     -24.939   3.905  29.018  1.00 37.02           C  
ANISOU 3369  CD1 TYR B 112     2216   4211   7639     16   -241   -166       C  
ATOM   3370  CD2 TYR B 112     -25.178   6.231  29.382  1.00 37.25           C  
ANISOU 3370  CD2 TYR B 112     2289   4231   7630     94   -264   -135       C  
ATOM   3371  CE1 TYR B 112     -25.195   4.082  27.668  1.00 37.12           C  
ANISOU 3371  CE1 TYR B 112     2191   4269   7644     32   -281   -184       C  
ATOM   3372  CE2 TYR B 112     -25.425   6.428  28.036  1.00 37.42           C  
ANISOU 3372  CE2 TYR B 112     2273   4296   7647    116   -302   -142       C  
ATOM   3373  CZ  TYR B 112     -25.435   5.350  27.174  1.00 37.32           C  
ANISOU 3373  CZ  TYR B 112     2216   4317   7644     84   -312   -168       C  
ATOM   3374  OH  TYR B 112     -25.684   5.564  25.850  1.00 37.80           O  
ANISOU 3374  OH  TYR B 112     2241   4431   7689    107   -352   -178       O  
ATOM   3375  N   LEU B 113     -21.780   6.094  30.038  1.00 37.48           N  
ANISOU 3375  N   LEU B 113     2443   4188   7609     30   -286    -58       N  
ATOM   3376  CA  LEU B 113     -20.588   6.051  29.146  1.00 37.51           C  
ANISOU 3376  CA  LEU B 113     2454   4201   7595     19   -317    -32       C  
ATOM   3377  C   LEU B 113     -19.324   6.300  29.973  1.00 37.45           C  
ANISOU 3377  C   LEU B 113     2491   4175   7562     -6   -321      4       C  
ATOM   3378  O   LEU B 113     -18.353   5.556  29.781  1.00 37.14           O  
ANISOU 3378  O   LEU B 113     2445   4150   7516    -22   -323     25       O  
ATOM   3379  CB  LEU B 113     -20.704   7.095  28.034  1.00 37.86           C  
ANISOU 3379  CB  LEU B 113     2497   4260   7626     47   -351    -23       C  
ATOM   3380  CG  LEU B 113     -21.637   6.728  26.885  1.00 38.33           C  
ANISOU 3380  CG  LEU B 113     2501   4364   7697     72   -362    -52       C  
ATOM   3381  CD1 LEU B 113     -21.792   7.903  25.930  1.00 38.60           C  
ANISOU 3381  CD1 LEU B 113     2542   4414   7711    111   -393    -31       C  
ATOM   3382  CD2 LEU B 113     -21.134   5.493  26.152  1.00 38.34           C  
ANISOU 3382  CD2 LEU B 113     2474   4390   7700     51   -362    -66       C  
ATOM   3383  N   ALA B 114     -19.331   7.309  30.849  1.00 37.72           N  
ANISOU 3383  N   ALA B 114     2570   4182   7579     -9   -323      8       N  
ATOM   3384  CA  ALA B 114     -18.199   7.604  31.759  1.00 38.01           C  
ANISOU 3384  CA  ALA B 114     2647   4209   7583    -44   -333     34       C  
ATOM   3385  C   ALA B 114     -17.899   6.351  32.585  1.00 37.98           C  
ANISOU 3385  C   ALA B 114     2631   4221   7579    -55   -306     43       C  
ATOM   3386  O   ALA B 114     -16.713   6.031  32.767  1.00 38.32           O  
ANISOU 3386  O   ALA B 114     2673   4285   7599    -75   -320     76       O  
ATOM   3387  CB  ALA B 114     -18.496   8.792  32.642  1.00 38.38           C  
ANISOU 3387  CB  ALA B 114     2751   4220   7612    -45   -333     20       C  
ATOM   3388  N   THR B 115     -18.937   5.653  33.050  1.00 37.94           N  
ANISOU 3388  N   THR B 115     2609   4208   7596    -40   -268     19       N  
ATOM   3389  CA  THR B 115     -18.788   4.426  33.870  1.00 37.79           C  
ANISOU 3389  CA  THR B 115     2585   4193   7580    -47   -233     34       C  
ATOM   3390  C   THR B 115     -18.243   3.310  32.979  1.00 37.63           C  
ANISOU 3390  C   THR B 115     2534   4183   7581    -45   -231     47       C  
ATOM   3391  O   THR B 115     -17.293   2.638  33.410  1.00 37.54           O  
ANISOU 3391  O   THR B 115     2529   4180   7554    -47   -224     84       O  
ATOM   3392  CB  THR B 115     -20.095   4.081  34.583  1.00 37.87           C  
ANISOU 3392  CB  THR B 115     2587   4191   7610    -38   -187      8       C  
ATOM   3393  OG1 THR B 115     -20.370   5.216  35.402  1.00 37.78           O  
ANISOU 3393  OG1 THR B 115     2613   4171   7568    -31   -190     -2       O  
ATOM   3394  CG2 THR B 115     -20.003   2.820  35.415  1.00 38.03           C  
ANISOU 3394  CG2 THR B 115     2608   4206   7635    -46   -143     31       C  
ATOM   3395  N   ALA B 116     -18.796   3.157  31.773  1.00 37.52           N  
ANISOU 3395  N   ALA B 116     2488   4171   7595    -37   -237     19       N  
ATOM   3396  CA  ALA B 116     -18.261   2.253  30.727  1.00 37.55           C  
ANISOU 3396  CA  ALA B 116     2470   4184   7611    -33   -239     20       C  
ATOM   3397  C   ALA B 116     -16.783   2.585  30.467  1.00 37.30           C  
ANISOU 3397  C   ALA B 116     2447   4179   7546    -31   -268     64       C  
ATOM   3398  O   ALA B 116     -15.924   1.715  30.680  1.00 37.14           O  
ANISOU 3398  O   ALA B 116     2427   4164   7520    -23   -253     94       O  
ATOM   3399  CB  ALA B 116     -19.085   2.368  29.466  1.00 37.54           C  
ANISOU 3399  CB  ALA B 116     2436   4196   7629    -25   -254    -21       C  
ATOM   3400  N   LEU B 117     -16.510   3.814  30.029  1.00 37.29           N  
ANISOU 3400  N   LEU B 117     2452   4193   7523    -36   -306     72       N  
ATOM   3401  CA  LEU B 117     -15.179   4.285  29.564  1.00 37.26           C  
ANISOU 3401  CA  LEU B 117     2445   4221   7488    -45   -335    114       C  
ATOM   3402  C   LEU B 117     -14.123   3.923  30.611  1.00 37.39           C  
ANISOU 3402  C   LEU B 117     2468   4255   7480    -57   -332    154       C  
ATOM   3403  O   LEU B 117     -13.117   3.298  30.237  1.00 37.47           O  
ANISOU 3403  O   LEU B 117     2455   4299   7480    -45   -330    186       O  
ATOM   3404  CB  LEU B 117     -15.247   5.798  29.333  1.00 37.33           C  
ANISOU 3404  CB  LEU B 117     2476   4224   7482    -61   -367    117       C  
ATOM   3405  CG  LEU B 117     -14.012   6.432  28.702  1.00 37.55           C  
ANISOU 3405  CG  LEU B 117     2498   4284   7483    -82   -396    160       C  
ATOM   3406  CD1 LEU B 117     -13.760   5.856  27.321  1.00 37.63           C  
ANISOU 3406  CD1 LEU B 117     2473   4330   7495    -55   -394    165       C  
ATOM   3407  CD2 LEU B 117     -14.168   7.941  28.629  1.00 37.78           C  
ANISOU 3407  CD2 LEU B 117     2565   4286   7504   -103   -420    165       C  
ATOM   3408  N   LEU B 118     -14.373   4.271  31.875  1.00 37.41           N  
ANISOU 3408  N   LEU B 118     2499   4242   7471    -73   -328    152       N  
ATOM   3409  CA  LEU B 118     -13.386   4.156  32.980  1.00 37.77           C  
ANISOU 3409  CA  LEU B 118     2552   4318   7478    -89   -335    191       C  
ATOM   3410  C   LEU B 118     -12.963   2.695  33.178  1.00 38.26           C  
ANISOU 3410  C   LEU B 118     2595   4395   7548    -55   -303    221       C  
ATOM   3411  O   LEU B 118     -11.754   2.452  33.315  1.00 38.54           O  
ANISOU 3411  O   LEU B 118     2609   4479   7555    -50   -316    267       O  
ATOM   3412  CB  LEU B 118     -13.991   4.759  34.250  1.00 37.66           C  
ANISOU 3412  CB  LEU B 118     2579   4283   7446   -106   -332    171       C  
ATOM   3413  CG  LEU B 118     -14.074   6.283  34.247  1.00 37.68           C  
ANISOU 3413  CG  LEU B 118     2614   4268   7432   -140   -365    149       C  
ATOM   3414  CD1 LEU B 118     -14.971   6.782  35.359  1.00 37.95           C  
ANISOU 3414  CD1 LEU B 118     2694   4270   7454   -140   -349    115       C  
ATOM   3415  CD2 LEU B 118     -12.690   6.905  34.361  1.00 38.11           C  
ANISOU 3415  CD2 LEU B 118     2667   4364   7448   -185   -407    182       C  
ATOM   3416  N   THR B 119     -13.910   1.756  33.171  1.00 38.80           N  
ANISOU 3416  N   THR B 119     2667   4420   7653    -32   -260    197       N  
ATOM   3417  CA  THR B 119     -13.652   0.315  33.434  1.00 39.39           C  
ANISOU 3417  CA  THR B 119     2739   4484   7740      0   -219    224       C  
ATOM   3418  C   THR B 119     -13.032  -0.362  32.201  1.00 39.76           C  
ANISOU 3418  C   THR B 119     2763   4539   7803     29   -214    229       C  
ATOM   3419  O   THR B 119     -12.314  -1.350  32.406  1.00 40.28           O  
ANISOU 3419  O   THR B 119     2828   4611   7866     66   -189    268       O  
ATOM   3420  CB  THR B 119     -14.913  -0.394  33.941  1.00 39.59           C  
ANISOU 3420  CB  THR B 119     2785   4455   7803      0   -170    196       C  
ATOM   3421  OG1 THR B 119     -14.596  -1.768  34.161  1.00 40.16           O  
ANISOU 3421  OG1 THR B 119     2864   4502   7890     31   -126    228       O  
ATOM   3422  CG2 THR B 119     -16.087  -0.300  32.996  1.00 39.60           C  
ANISOU 3422  CG2 THR B 119     2773   4424   7847    -12   -165    135       C  
ATOM   3423  N   LEU B 120     -13.273   0.135  30.982  1.00 40.02           N  
ANISOU 3423  N   LEU B 120     2780   4576   7847     21   -235    195       N  
ATOM   3424  CA  LEU B 120     -12.634  -0.382  29.733  1.00 40.67           C  
ANISOU 3424  CA  LEU B 120     2841   4678   7932     50   -232    196       C  
ATOM   3425  C   LEU B 120     -11.129  -0.062  29.729  1.00 41.05           C  
ANISOU 3425  C   LEU B 120     2863   4794   7939     61   -255    256       C  
ATOM   3426  O   LEU B 120     -10.396  -0.716  28.965  1.00 40.82           O  
ANISOU 3426  O   LEU B 120     2815   4788   7906    100   -241    272       O  
ATOM   3427  CB  LEU B 120     -13.317   0.228  28.502  1.00 40.96           C  
ANISOU 3427  CB  LEU B 120     2868   4716   7978     37   -253    148       C  
ATOM   3428  CG  LEU B 120     -14.618  -0.451  28.066  1.00 41.47           C  
ANISOU 3428  CG  LEU B 120     2939   4734   8083     35   -229     85       C  
ATOM   3429  CD1 LEU B 120     -15.434   0.451  27.150  1.00 41.36           C  
ANISOU 3429  CD1 LEU B 120     2910   4736   8067     21   -261     45       C  
ATOM   3430  CD2 LEU B 120     -14.336  -1.782  27.382  1.00 41.87           C  
ANISOU 3430  CD2 LEU B 120     2994   4766   8149     65   -195     68       C  
ATOM   3431  N   GLN B 121     -10.699   0.913  30.542  1.00 41.36           N  
ANISOU 3431  N   GLN B 121     2900   4867   7947     26   -289    285       N  
ATOM   3432  CA  GLN B 121      -9.276   1.297  30.762  1.00 41.79           C  
ANISOU 3432  CA  GLN B 121     2920   4998   7959     19   -317    344       C  
ATOM   3433  C   GLN B 121      -8.620   0.406  31.835  1.00 42.22           C  
ANISOU 3433  C   GLN B 121     2968   5079   7995     54   -299    392       C  
ATOM   3434  O   GLN B 121      -7.402   0.588  32.073  1.00 42.66           O  
ANISOU 3434  O   GLN B 121     2982   5213   8012     54   -323    445       O  
ATOM   3435  CB  GLN B 121      -9.190   2.770  31.180  1.00 41.71           C  
ANISOU 3435  CB  GLN B 121     2917   5004   7924    -46   -363    342       C  
ATOM   3436  CG  GLN B 121      -9.496   3.760  30.064  1.00 41.38           C  
ANISOU 3436  CG  GLN B 121     2879   4950   7892    -73   -383    319       C  
ATOM   3437  CD  GLN B 121      -9.710   5.150  30.608  1.00 41.29           C  
ANISOU 3437  CD  GLN B 121     2899   4921   7868   -133   -417    307       C  
ATOM   3438  OE1 GLN B 121      -8.802   5.789  31.135  1.00 41.33           O  
ANISOU 3438  OE1 GLN B 121     2894   4966   7841   -179   -447    336       O  
ATOM   3439  NE2 GLN B 121     -10.941   5.621  30.510  1.00 41.49           N  
ANISOU 3439  NE2 GLN B 121     2963   4884   7917   -133   -412    260       N  
ATOM   3440  N   GLN B 122      -9.378  -0.507  32.460  1.00 42.00           N  
ANISOU 3440  N   GLN B 122     2973   4992   7990     81   -259    381       N  
ATOM   3441  CA  GLN B 122      -8.949  -1.281  33.659  1.00 42.44           C  
ANISOU 3441  CA  GLN B 122     3035   5065   8025    115   -239    432       C  
ATOM   3442  C   GLN B 122      -9.141  -2.795  33.472  1.00 43.01           C  
ANISOU 3442  C   GLN B 122     3128   5079   8132    180   -176    442       C  
ATOM   3443  O   GLN B 122      -8.721  -3.539  34.391  1.00 43.48           O  
ANISOU 3443  O   GLN B 122     3194   5149   8174    223   -153    497       O  
ATOM   3444  CB  GLN B 122      -9.740  -0.813  34.879  1.00 42.31           C  
ANISOU 3444  CB  GLN B 122     3054   5025   7994     77   -243    416       C  
ATOM   3445  CG  GLN B 122      -9.688   0.691  35.091  1.00 42.09           C  
ANISOU 3445  CG  GLN B 122     3024   5030   7935     12   -298    394       C  
ATOM   3446  CD  GLN B 122     -10.601   1.136  36.205  1.00 42.09           C  
ANISOU 3446  CD  GLN B 122     3067   5000   7922    -15   -294    366       C  
ATOM   3447  OE1 GLN B 122     -10.498   0.671  37.334  1.00 42.57           O  
ANISOU 3447  OE1 GLN B 122     3141   5079   7952      0   -280    397       O  
ATOM   3448  NE2 GLN B 122     -11.506   2.048  35.894  1.00 41.78           N  
ANISOU 3448  NE2 GLN B 122     3052   4919   7903    -51   -304    310       N  
ATOM   3449  N   ILE B 123      -9.756  -3.240  32.365  1.00 42.82           N  
ANISOU 3449  N   ILE B 123     3117   4997   8154    188   -150    391       N  
ATOM   3450  CA  ILE B 123      -9.881  -4.682  31.988  1.00 43.16           C  
ANISOU 3450  CA  ILE B 123     3188   4974   8235    244    -90    388       C  
ATOM   3451  C   ILE B 123      -9.210  -4.884  30.625  1.00 43.33           C  
ANISOU 3451  C   ILE B 123     3185   5019   8256    279    -89    376       C  
ATOM   3452  O   ILE B 123      -9.201  -3.927  29.831  1.00 43.01           O  
ANISOU 3452  O   ILE B 123     3118   5020   8203    244   -129    348       O  
ATOM   3453  CB  ILE B 123     -11.350  -5.164  31.988  1.00 43.17           C  
ANISOU 3453  CB  ILE B 123     3233   4878   8289    211    -53    326       C  
ATOM   3454  CG1 ILE B 123     -12.232  -4.375  31.017  1.00 42.77           C  
ANISOU 3454  CG1 ILE B 123     3170   4823   8256    159    -83    251       C  
ATOM   3455  CG2 ILE B 123     -11.924  -5.163  33.398  1.00 43.27           C  
ANISOU 3455  CG2 ILE B 123     3270   4871   8299    190    -38    350       C  
ATOM   3456  CD1 ILE B 123     -13.500  -5.096  30.612  1.00 42.88           C  
ANISOU 3456  CD1 ILE B 123     3211   4757   8324    135    -46    185       C  
ATOM   3457  N   GLU B 124      -8.695  -6.093  30.373  1.00 44.00           N  
ANISOU 3457  N   GLU B 124     3287   5075   8354    351    -40    398       N  
ATOM   3458  CA  GLU B 124      -7.892  -6.452  29.173  1.00 44.76           C  
ANISOU 3458  CA  GLU B 124     3364   5200   8441    406    -28    394       C  
ATOM   3459  C   GLU B 124      -8.848  -6.864  28.048  1.00 44.58           C  
ANISOU 3459  C   GLU B 124     3377   5102   8456    387     -6    303       C  
ATOM   3460  O   GLU B 124      -9.509  -7.899  28.195  1.00 44.52           O  
ANISOU 3460  O   GLU B 124     3425   4997   8491    396     42    273       O  
ATOM   3461  CB  GLU B 124      -6.895  -7.567  29.521  1.00 46.00           C  
ANISOU 3461  CB  GLU B 124     3527   5359   8591    504     19    462       C  
ATOM   3462  CG  GLU B 124      -5.460  -7.300  29.069  1.00 46.57           C  
ANISOU 3462  CG  GLU B 124     3532   5547   8616    559      2    519       C  
ATOM   3463  CD  GLU B 124      -4.412  -7.306  30.181  1.00 47.58           C  
ANISOU 3463  CD  GLU B 124     3615   5759   8703    603     -9    618       C  
ATOM   3464  OE1 GLU B 124      -4.806  -7.508  31.368  1.00 46.91           O  
ANISOU 3464  OE1 GLU B 124     3560   5642   8622    593     -5    645       O  
ATOM   3465  OE2 GLU B 124      -3.196  -7.090  29.868  1.00 47.21           O  
ANISOU 3465  OE2 GLU B 124     3499   5822   8616    646    -24    671       O  
ATOM   3466  N   LEU B 125      -8.879  -6.086  26.961  1.00 44.82           N  
ANISOU 3466  N   LEU B 125     3378   5181   8468    361    -41    264       N  
ATOM   3467  CA  LEU B 125      -9.873  -6.171  25.855  1.00 45.32           C  
ANISOU 3467  CA  LEU B 125     3464   5203   8553    329    -40    173       C  
ATOM   3468  C   LEU B 125      -9.222  -5.768  24.523  1.00 45.74           C  
ANISOU 3468  C   LEU B 125     3484   5327   8565    354    -57    163       C  
ATOM   3469  O   LEU B 125      -8.493  -4.769  24.511  1.00 44.83           O  
ANISOU 3469  O   LEU B 125     3320   5298   8413    345    -94    214       O  
ATOM   3470  CB  LEU B 125     -11.024  -5.214  26.185  1.00 44.85           C  
ANISOU 3470  CB  LEU B 125     3399   5136   8506    250    -81    140       C  
ATOM   3471  CG  LEU B 125     -12.400  -5.844  26.364  1.00 45.07           C  
ANISOU 3471  CG  LEU B 125     3464   5075   8584    210    -56     75       C  
ATOM   3472  CD1 LEU B 125     -12.820  -6.558  25.099  1.00 45.64           C  
ANISOU 3472  CD1 LEU B 125     3555   5116   8668    214    -38     -3       C  
ATOM   3473  CD2 LEU B 125     -12.430  -6.792  27.548  1.00 45.44           C  
ANISOU 3473  CD2 LEU B 125     3549   5054   8661    225     -7    110       C  
ATOM   3474  N   LYS B 126      -9.514  -6.484  23.433  1.00 47.06           N  
ANISOU 3474  N   LYS B 126     3679   5462   8738    376    -31     95       N  
ATOM   3475  CA  LYS B 126      -9.079  -6.095  22.062  1.00 47.99           C  
ANISOU 3475  CA  LYS B 126     3770   5651   8810    397    -45     75       C  
ATOM   3476  C   LYS B 126     -10.259  -6.225  21.094  1.00 47.59           C  
ANISOU 3476  C   LYS B 126     3746   5568   8767    359    -55    -25       C  
ATOM   3477  O   LYS B 126     -10.837  -7.326  20.984  1.00 47.73           O  
ANISOU 3477  O   LYS B 126     3814   5502   8817    362    -18    -89       O  
ATOM   3478  CB  LYS B 126      -7.869  -6.920  21.608  1.00 49.89           C  
ANISOU 3478  CB  LYS B 126     4011   5916   9026    490      1    103       C  
ATOM   3479  CG  LYS B 126      -6.560  -6.593  22.322  1.00 51.12           C  
ANISOU 3479  CG  LYS B 126     4115   6148   9158    530      0    209       C  
ATOM   3480  CD  LYS B 126      -5.960  -5.224  21.985  1.00 51.54           C  
ANISOU 3480  CD  LYS B 126     4099   6316   9166    496    -49    258       C  
ATOM   3481  CE  LYS B 126      -5.013  -4.702  23.050  1.00 51.85           C  
ANISOU 3481  CE  LYS B 126     4085   6421   9193    491    -70    352       C  
ATOM   3482  NZ  LYS B 126      -4.164  -3.598  22.542  1.00 52.17           N  
ANISOU 3482  NZ  LYS B 126     4057   6575   9189    467   -103    402       N  
ATOM   3483  N   PHE B 127     -10.583  -5.124  20.417  1.00 46.89           N  
ANISOU 3483  N   PHE B 127     3623   5545   8646    324   -104    -34       N  
ATOM   3484  CA  PHE B 127     -11.781  -4.963  19.559  1.00 46.99           C  
ANISOU 3484  CA  PHE B 127     3643   5554   8655    283   -131   -119       C  
ATOM   3485  C   PHE B 127     -11.477  -5.484  18.153  1.00 47.55           C  
ANISOU 3485  C   PHE B 127     3726   5659   8681    326   -115   -171       C  
ATOM   3486  O   PHE B 127     -10.546  -4.985  17.524  1.00 47.88           O  
ANISOU 3486  O   PHE B 127     3739   5781   8671    365   -119   -126       O  
ATOM   3487  CB  PHE B 127     -12.223  -3.497  19.542  1.00 46.42           C  
ANISOU 3487  CB  PHE B 127     3533   5538   8566    239   -188    -91       C  
ATOM   3488  CG  PHE B 127     -12.843  -3.023  20.833  1.00 45.94           C  
ANISOU 3488  CG  PHE B 127     3470   5435   8548    193   -203    -68       C  
ATOM   3489  CD1 PHE B 127     -14.063  -3.531  21.260  1.00 46.20           C  
ANISOU 3489  CD1 PHE B 127     3521   5405   8626    155   -196   -126       C  
ATOM   3490  CD2 PHE B 127     -12.214  -2.072  21.619  1.00 45.29           C  
ANISOU 3490  CD2 PHE B 127     3368   5380   8457    183   -222      9       C  
ATOM   3491  CE1 PHE B 127     -14.637  -3.104  22.446  1.00 45.58           C  
ANISOU 3491  CE1 PHE B 127     3441   5295   8581    118   -203   -103       C  
ATOM   3492  CE2 PHE B 127     -12.791  -1.639  22.802  1.00 45.00           C  
ANISOU 3492  CE2 PHE B 127     3337   5307   8451    145   -233     23       C  
ATOM   3493  CZ  PHE B 127     -13.999  -2.157  23.214  1.00 45.46           C  
ANISOU 3493  CZ  PHE B 127     3414   5306   8552    118   -221    -31       C  
ATOM   3494  N   ASN B 128     -12.263  -6.449  17.678  1.00 48.55           N  
ANISOU 3494  N   ASN B 128     3893   5729   8825    313    -97   -267       N  
ATOM   3495  CA  ASN B 128     -12.188  -6.983  16.293  1.00 49.66           C  
ANISOU 3495  CA  ASN B 128     4053   5897   8915    345    -86   -341       C  
ATOM   3496  C   ASN B 128     -12.280  -5.832  15.293  1.00 49.44           C  
ANISOU 3496  C   ASN B 128     3981   5982   8821    340   -138   -332       C  
ATOM   3497  O   ASN B 128     -11.447  -5.750  14.400  1.00 50.44           O  
ANISOU 3497  O   ASN B 128     4099   6177   8886    394   -126   -317       O  
ATOM   3498  CB  ASN B 128     -13.232  -8.078  16.046  1.00 50.68           C  
ANISOU 3498  CB  ASN B 128     4233   5944   9078    305    -70   -457       C  
ATOM   3499  CG  ASN B 128     -12.893  -9.374  16.755  1.00 51.59           C  
ANISOU 3499  CG  ASN B 128     4410   5941   9247    330     -2   -464       C  
ATOM   3500  OD1 ASN B 128     -13.674  -9.877  17.563  1.00 52.12           O  
ANISOU 3500  OD1 ASN B 128     4502   5920   9379    276     10   -486       O  
ATOM   3501  ND2 ASN B 128     -11.718  -9.914  16.475  1.00 52.43           N  
ANISOU 3501  ND2 ASN B 128     4541   6049   9328    416     45   -437       N  
ATOM   3502  N   PRO B 129     -13.256  -4.896  15.382  1.00 49.03           N  
ANISOU 3502  N   PRO B 129     3896   5956   8774    284   -192   -333       N  
ATOM   3503  CA  PRO B 129     -13.321  -3.788  14.429  1.00 48.91           C  
ANISOU 3503  CA  PRO B 129     3845   6043   8694    290   -237   -313       C  
ATOM   3504  C   PRO B 129     -12.096  -2.882  14.534  1.00 48.61           C  
ANISOU 3504  C   PRO B 129     3779   6062   8627    322   -234   -202       C  
ATOM   3505  O   PRO B 129     -11.728  -2.464  15.630  1.00 48.75           O  
ANISOU 3505  O   PRO B 129     3786   6051   8686    306   -232   -134       O  
ATOM   3506  CB  PRO B 129     -14.596  -3.014  14.803  1.00 48.48           C  
ANISOU 3506  CB  PRO B 129     3766   5987   8667    233   -287   -323       C  
ATOM   3507  CG  PRO B 129     -15.381  -3.956  15.691  1.00 48.44           C  
ANISOU 3507  CG  PRO B 129     3784   5886   8734    190   -267   -380       C  
ATOM   3508  CD  PRO B 129     -14.354  -4.847  16.358  1.00 48.56           C  
ANISOU 3508  CD  PRO B 129     3835   5835   8778    222   -208   -351       C  
ATOM   3509  N   PRO B 130     -11.410  -2.578  13.408  1.00 48.43           N  
ANISOU 3509  N   PRO B 130     3742   6126   8532    365   -231   -182       N  
ATOM   3510  CA  PRO B 130     -10.310  -1.615  13.407  1.00 47.76           C  
ANISOU 3510  CA  PRO B 130     3621   6104   8418    381   -230    -75       C  
ATOM   3511  C   PRO B 130     -10.718  -0.247  13.972  1.00 46.98           C  
ANISOU 3511  C   PRO B 130     3502   6007   8341    330   -275    -14       C  
ATOM   3512  O   PRO B 130     -10.009   0.278  14.816  1.00 46.76           O  
ANISOU 3512  O   PRO B 130     3458   5970   8337    313   -272     60       O  
ATOM   3513  CB  PRO B 130      -9.927  -1.424  11.933  1.00 48.29           C  
ANISOU 3513  CB  PRO B 130     3679   6271   8398    424   -226    -78       C  
ATOM   3514  CG  PRO B 130     -10.622  -2.537  11.169  1.00 49.08           C  
ANISOU 3514  CG  PRO B 130     3817   6356   8476    443   -217   -197       C  
ATOM   3515  CD  PRO B 130     -11.652  -3.166  12.084  1.00 48.99           C  
ANISOU 3515  CD  PRO B 130     3830   6240   8541    394   -227   -264       C  
ATOM   3516  N   ALA B 131     -11.845   0.292  13.495  1.00 46.29           N  
ANISOU 3516  N   ALA B 131     3416   5932   8239    309   -316    -49       N  
ATOM   3517  CA  ALA B 131     -12.361   1.629  13.869  1.00 45.54           C  
ANISOU 3517  CA  ALA B 131     3310   5835   8158    275   -356      3       C  
ATOM   3518  C   ALA B 131     -12.533   1.719  15.389  1.00 44.50           C  
ANISOU 3518  C   ALA B 131     3185   5620   8100    234   -356     19       C  
ATOM   3519  O   ALA B 131     -12.315   2.812  15.922  1.00 44.20           O  
ANISOU 3519  O   ALA B 131     3144   5575   8074    210   -372     86       O  
ATOM   3520  CB  ALA B 131     -13.653   1.915  13.147  1.00 45.89           C  
ANISOU 3520  CB  ALA B 131     3351   5907   8178    274   -396    -48       C  
ATOM   3521  N   LEU B 132     -12.901   0.619  16.057  1.00 44.26           N  
ANISOU 3521  N   LEU B 132     3171   5529   8116    227   -335    -38       N  
ATOM   3522  CA  LEU B 132     -13.041   0.557  17.539  1.00 43.69           C  
ANISOU 3522  CA  LEU B 132     3108   5384   8107    194   -328    -23       C  
ATOM   3523  C   LEU B 132     -11.658   0.548  18.197  1.00 43.96           C  
ANISOU 3523  C   LEU B 132     3136   5422   8143    203   -304     49       C  
ATOM   3524  O   LEU B 132     -11.485   1.323  19.158  1.00 44.50           O  
ANISOU 3524  O   LEU B 132     3202   5473   8232    171   -318     99       O  
ATOM   3525  CB  LEU B 132     -13.824  -0.687  17.967  1.00 43.56           C  
ANISOU 3525  CB  LEU B 132     3112   5303   8135    184   -306   -100       C  
ATOM   3526  CG  LEU B 132     -15.338  -0.539  18.101  1.00 43.46           C  
ANISOU 3526  CG  LEU B 132     3094   5269   8150    148   -332   -157       C  
ATOM   3527  CD1 LEU B 132     -15.882  -1.681  18.943  1.00 43.71           C  
ANISOU 3527  CD1 LEU B 132     3145   5222   8239    123   -300   -207       C  
ATOM   3528  CD2 LEU B 132     -15.746   0.799  18.712  1.00 42.82           C  
ANISOU 3528  CD2 LEU B 132     3000   5189   8078    129   -363   -108       C  
ATOM   3529  N   GLN B 133     -10.730  -0.306  17.739  1.00 44.08           N  
ANISOU 3529  N   GLN B 133     3148   5463   8135    247   -268     51       N  
ATOM   3530  CA  GLN B 133      -9.364  -0.417  18.329  1.00 44.27           C  
ANISOU 3530  CA  GLN B 133     3152   5508   8157    266   -244    123       C  
ATOM   3531  C   GLN B 133      -8.693   0.966  18.300  1.00 43.92           C  
ANISOU 3531  C   GLN B 133     3077   5524   8088    235   -272    204       C  
ATOM   3532  O   GLN B 133      -8.286   1.444  19.384  1.00 43.45           O  
ANISOU 3532  O   GLN B 133     3007   5450   8049    200   -283    252       O  
ATOM   3533  CB  GLN B 133      -8.503  -1.468  17.613  1.00 45.07           C  
ANISOU 3533  CB  GLN B 133     3251   5642   8229    333   -198    114       C  
ATOM   3534  CG  GLN B 133      -8.349  -2.778  18.380  1.00 45.16           C  
ANISOU 3534  CG  GLN B 133     3290   5588   8281    366   -156     93       C  
ATOM   3535  CD  GLN B 133      -7.893  -2.588  19.808  1.00 45.01           C  
ANISOU 3535  CD  GLN B 133     3257   5550   8294    348   -160    159       C  
ATOM   3536  OE1 GLN B 133      -8.493  -3.111  20.747  1.00 44.87           O  
ANISOU 3536  OE1 GLN B 133     3269   5456   8320    333   -151    137       O  
ATOM   3537  NE2 GLN B 133      -6.842  -1.805  19.991  1.00 44.88           N  
ANISOU 3537  NE2 GLN B 133     3193   5608   8251    342   -173    239       N  
ATOM   3538  N   ASP B 134      -8.617   1.583  17.113  1.00 43.83           N  
ANISOU 3538  N   ASP B 134     3053   5571   8028    243   -282    216       N  
ATOM   3539  CA  ASP B 134      -8.067   2.947  16.877  1.00 43.78           C  
ANISOU 3539  CA  ASP B 134     3024   5613   7996    208   -303    293       C  
ATOM   3540  C   ASP B 134      -8.569   3.916  17.955  1.00 43.12           C  
ANISOU 3540  C   ASP B 134     2959   5470   7953    147   -337    311       C  
ATOM   3541  O   ASP B 134      -7.731   4.594  18.585  1.00 43.19           O  
ANISOU 3541  O   ASP B 134     2951   5492   7966    106   -344    374       O  
ATOM   3542  CB  ASP B 134      -8.433   3.469  15.482  1.00 44.20           C  
ANISOU 3542  CB  ASP B 134     3079   5716   7998    226   -313    289       C  
ATOM   3543  CG  ASP B 134      -7.571   2.931  14.346  1.00 44.86           C  
ANISOU 3543  CG  ASP B 134     3138   5883   8022    280   -278    300       C  
ATOM   3544  OD1 ASP B 134      -7.777   3.384  13.190  1.00 45.06           O  
ANISOU 3544  OD1 ASP B 134     3164   5961   7994    297   -285    305       O  
ATOM   3545  OD2 ASP B 134      -6.696   2.072  14.618  1.00 44.85           O  
ANISOU 3545  OD2 ASP B 134     3118   5898   8024    311   -243    306       O  
ATOM   3546  N   ALA B 135      -9.884   3.992  18.159  1.00 42.64           N  
ANISOU 3546  N   ALA B 135     2929   5352   7918    139   -357    256       N  
ATOM   3547  CA  ALA B 135     -10.525   4.999  19.038  1.00 42.54           C  
ANISOU 3547  CA  ALA B 135     2940   5284   7938     93   -385    266       C  
ATOM   3548  C   ALA B 135     -10.267   4.662  20.513  1.00 42.04           C  
ANISOU 3548  C   ALA B 135     2882   5177   7912     67   -379    268       C  
ATOM   3549  O   ALA B 135     -10.104   5.612  21.305  1.00 41.81           O  
ANISOU 3549  O   ALA B 135     2867   5124   7894     21   -397    301       O  
ATOM   3550  CB  ALA B 135     -11.999   5.090  18.733  1.00 42.80           C  
ANISOU 3550  CB  ALA B 135     2992   5287   7981    107   -402    208       C  
ATOM   3551  N   TYR B 136     -10.235   3.368  20.855  1.00 41.79           N  
ANISOU 3551  N   TYR B 136     2847   5133   7897     95   -352    234       N  
ATOM   3552  CA  TYR B 136      -9.955   2.821  22.213  1.00 41.68           C  
ANISOU 3552  CA  TYR B 136     2839   5086   7912     84   -340    242       C  
ATOM   3553  C   TYR B 136      -8.532   3.210  22.646  1.00 42.48           C  
ANISOU 3553  C   TYR B 136     2908   5239   7990     66   -344    315       C  
ATOM   3554  O   TYR B 136      -8.320   3.595  23.821  1.00 41.88           O  
ANISOU 3554  O   TYR B 136     2838   5149   7925     28   -359    337       O  
ATOM   3555  CB  TYR B 136     -10.173   1.306  22.197  1.00 41.16           C  
ANISOU 3555  CB  TYR B 136     2780   4995   7863    129   -303    197       C  
ATOM   3556  CG  TYR B 136     -10.005   0.564  23.501  1.00 40.72           C  
ANISOU 3556  CG  TYR B 136     2735   4900   7834    131   -282    207       C  
ATOM   3557  CD1 TYR B 136     -10.458   1.072  24.706  1.00 40.26           C  
ANISOU 3557  CD1 TYR B 136     2694   4807   7796     92   -298    213       C  
ATOM   3558  CD2 TYR B 136      -9.449  -0.704  23.511  1.00 40.91           C  
ANISOU 3558  CD2 TYR B 136     2759   4920   7863    182   -242    208       C  
ATOM   3559  CE1 TYR B 136     -10.326   0.360  25.890  1.00 40.11           C  
ANISOU 3559  CE1 TYR B 136     2686   4759   7793     99   -277    227       C  
ATOM   3560  CE2 TYR B 136      -9.316  -1.431  24.681  1.00 40.83           C  
ANISOU 3560  CE2 TYR B 136     2763   4873   7875    193   -219    226       C  
ATOM   3561  CZ  TYR B 136      -9.756  -0.900  25.877  1.00 40.34           C  
ANISOU 3561  CZ  TYR B 136     2714   4786   7827    151   -238    238       C  
ATOM   3562  OH  TYR B 136      -9.614  -1.629  27.023  1.00 40.16           O  
ANISOU 3562  OH  TYR B 136     2706   4735   7818    167   -214    262       O  
ATOM   3563  N   TYR B 137      -7.574   3.118  21.722  1.00 43.37           N  
ANISOU 3563  N   TYR B 137     2985   5422   8070     90   -332    350       N  
ATOM   3564  CA  TYR B 137      -6.188   3.603  21.940  1.00 44.84           C  
ANISOU 3564  CA  TYR B 137     3125   5679   8231     65   -337    425       C  
ATOM   3565  C   TYR B 137      -6.238   5.117  22.176  1.00 46.43           C  
ANISOU 3565  C   TYR B 137     3339   5869   8432    -11   -374    454       C  
ATOM   3566  O   TYR B 137      -5.782   5.577  23.242  1.00 45.84           O  
ANISOU 3566  O   TYR B 137     3258   5794   8362    -63   -395    480       O  
ATOM   3567  CB  TYR B 137      -5.273   3.230  20.770  1.00 44.37           C  
ANISOU 3567  CB  TYR B 137     3022   5702   8135    111   -310    456       C  
ATOM   3568  CG  TYR B 137      -4.750   1.816  20.788  1.00 43.88           C  
ANISOU 3568  CG  TYR B 137     2941   5660   8069    187   -268    449       C  
ATOM   3569  CD1 TYR B 137      -4.235   1.253  21.944  1.00 43.75           C  
ANISOU 3569  CD1 TYR B 137     2910   5643   8067    198   -262    474       C  
ATOM   3570  CD2 TYR B 137      -4.736   1.044  19.634  1.00 43.78           C  
ANISOU 3570  CD2 TYR B 137     2931   5668   8034    254   -233    419       C  
ATOM   3571  CE1 TYR B 137      -3.734  -0.040  21.957  1.00 44.16           C  
ANISOU 3571  CE1 TYR B 137     2952   5708   8119    280   -219    476       C  
ATOM   3572  CE2 TYR B 137      -4.243  -0.249  19.629  1.00 44.01           C  
ANISOU 3572  CE2 TYR B 137     2954   5703   8061    331   -189    410       C  
ATOM   3573  CZ  TYR B 137      -3.738  -0.796  20.796  1.00 44.27           C  
ANISOU 3573  CZ  TYR B 137     2975   5729   8116    348   -180    443       C  
ATOM   3574  OH  TYR B 137      -3.252  -2.072  20.802  1.00 44.36           O  
ANISOU 3574  OH  TYR B 137     2988   5739   8128    435   -131    441       O  
ATOM   3575  N   ARG B 138      -6.818   5.856  21.225  1.00 49.27           N  
ANISOU 3575  N   ARG B 138     3720   6216   8783    -17   -383    447       N  
ATOM   3576  CA  ARG B 138      -6.888   7.344  21.244  1.00 51.90           C  
ANISOU 3576  CA  ARG B 138     4077   6525   9116    -82   -410    479       C  
ATOM   3577  C   ARG B 138      -7.842   7.814  22.355  1.00 52.07           C  
ANISOU 3577  C   ARG B 138     4152   6460   9172   -113   -431    439       C  
ATOM   3578  O   ARG B 138      -7.792   9.012  22.691  1.00 52.51           O  
ANISOU 3578  O   ARG B 138     4237   6482   9231   -171   -452    462       O  
ATOM   3579  CB  ARG B 138      -7.283   7.881  19.862  1.00 54.42           C  
ANISOU 3579  CB  ARG B 138     4408   6857   9412    -61   -407    489       C  
ATOM   3580  CG  ARG B 138      -6.142   7.869  18.849  1.00 57.00           C  
ANISOU 3580  CG  ARG B 138     4684   7275   9696    -53   -386    548       C  
ATOM   3581  CD  ARG B 138      -6.273   8.873  17.715  1.00 59.14           C  
ANISOU 3581  CD  ARG B 138     4971   7559   9940    -61   -388    589       C  
ATOM   3582  NE  ARG B 138      -6.463  10.244  18.188  1.00 61.18           N  
ANISOU 3582  NE  ARG B 138     5272   7751  10219   -130   -411    619       N  
ATOM   3583  CZ  ARG B 138      -7.485  11.049  17.867  1.00 62.86           C  
ANISOU 3583  CZ  ARG B 138     5541   7902  10438   -121   -424    611       C  
ATOM   3584  NH1 ARG B 138      -8.439  10.655  17.036  1.00 63.49           N  
ANISOU 3584  NH1 ARG B 138     5629   7992  10500    -49   -423    574       N  
ATOM   3585  NH2 ARG B 138      -7.543  12.272  18.367  1.00 63.41           N  
ANISOU 3585  NH2 ARG B 138     5658   7903  10531   -181   -438    640       N  
ATOM   3586  N   ALA B 139      -8.666   6.912  22.906  1.00 52.00           N  
ANISOU 3586  N   ALA B 139     4157   6414   9186    -76   -422    384       N  
ATOM   3587  CA  ALA B 139      -9.494   7.125  24.119  1.00 51.40           C  
ANISOU 3587  CA  ALA B 139     4122   6270   9137    -96   -433    347       C  
ATOM   3588  C   ALA B 139      -8.643   6.978  25.388  1.00 51.79           C  
ANISOU 3588  C   ALA B 139     4160   6335   9183   -133   -439    370       C  
ATOM   3589  O   ALA B 139      -8.839   7.785  26.317  1.00 51.53           O  
ANISOU 3589  O   ALA B 139     4161   6262   9154   -180   -459    363       O  
ATOM   3590  CB  ALA B 139     -10.642   6.154  24.135  1.00 51.06           C  
ANISOU 3590  CB  ALA B 139     4088   6193   9117    -48   -415    286       C  
ATOM   3591  N   ARG B 140      -7.751   5.978  25.436  1.00 52.77           N  
ANISOU 3591  N   ARG B 140     4237   6516   9293   -106   -423    394       N  
ATOM   3592  CA  ARG B 140      -6.814   5.744  26.574  1.00 53.34           C  
ANISOU 3592  CA  ARG B 140     4284   6628   9352   -129   -432    427       C  
ATOM   3593  C   ARG B 140      -5.887   6.956  26.721  1.00 52.98           C  
ANISOU 3593  C   ARG B 140     4223   6621   9284   -209   -464    471       C  
ATOM   3594  O   ARG B 140      -5.683   7.396  27.871  1.00 53.15           O  
ANISOU 3594  O   ARG B 140     4258   6638   9298   -260   -489    470       O  
ATOM   3595  CB  ARG B 140      -6.016   4.445  26.395  1.00 54.61           C  
ANISOU 3595  CB  ARG B 140     4396   6849   9502    -67   -403    453       C  
ATOM   3596  CG  ARG B 140      -6.647   3.225  27.058  1.00 55.84           C  
ANISOU 3596  CG  ARG B 140     4576   6961   9680    -14   -375    421       C  
ATOM   3597  CD  ARG B 140      -5.799   1.965  26.958  1.00 57.51           C  
ANISOU 3597  CD  ARG B 140     4749   7220   9882     54   -342    454       C  
ATOM   3598  NE  ARG B 140      -4.424   2.179  27.420  1.00 59.02           N  
ANISOU 3598  NE  ARG B 140     4880   7504  10038     40   -359    521       N  
ATOM   3599  CZ  ARG B 140      -3.324   2.227  26.651  1.00 59.70           C  
ANISOU 3599  CZ  ARG B 140     4905   7679  10100     54   -355    568       C  
ATOM   3600  NH1 ARG B 140      -3.392   2.061  25.338  1.00 59.54           N  
ANISOU 3600  NH1 ARG B 140     4880   7661  10079     89   -330    555       N  
ATOM   3601  NH2 ARG B 140      -2.143   2.443  27.210  1.00 60.03           N  
ANISOU 3601  NH2 ARG B 140     4883   7814  10111     33   -376    629       N  
ATOM   3602  N   ALA B 141      -5.376   7.476  25.596  1.00 52.84           N  
ANISOU 3602  N   ALA B 141     4180   6639   9255   -223   -463    505       N  
ATOM   3603  CA  ALA B 141      -4.478   8.655  25.495  1.00 53.09           C  
ANISOU 3603  CA  ALA B 141     4194   6704   9270   -308   -487    552       C  
ATOM   3604  C   ALA B 141      -5.166   9.916  26.037  1.00 52.63           C  
ANISOU 3604  C   ALA B 141     4211   6557   9228   -374   -512    525       C  
ATOM   3605  O   ALA B 141      -4.482  10.717  26.714  1.00 52.73           O  
ANISOU 3605  O   ALA B 141     4225   6580   9230   -461   -539    542       O  
ATOM   3606  CB  ALA B 141      -4.049   8.850  24.062  1.00 53.77           C  
ANISOU 3606  CB  ALA B 141     4249   6836   9343   -295   -468    593       C  
ATOM   3607  N   GLY B 142      -6.460  10.087  25.740  1.00 51.90           N  
ANISOU 3607  N   GLY B 142     4178   6382   9158   -335   -503    481       N  
ATOM   3608  CA  GLY B 142      -7.306  11.148  26.328  1.00 51.61           C  
ANISOU 3608  CA  GLY B 142     4219   6251   9138   -371   -518    446       C  
ATOM   3609  C   GLY B 142      -8.328  11.741  25.367  1.00 50.86           C  
ANISOU 3609  C   GLY B 142     4169   6096   9059   -333   -507    436       C  
ATOM   3610  O   GLY B 142      -9.101  12.612  25.823  1.00 51.07           O  
ANISOU 3610  O   GLY B 142     4262   6039   9100   -347   -514    409       O  
ATOM   3611  N   GLU B 143      -8.345  11.320  24.095  1.00 49.81           N  
ANISOU 3611  N   GLU B 143     4002   6006   8918   -283   -491    457       N  
ATOM   3612  CA  GLU B 143      -9.332  11.795  23.089  1.00 49.63           C  
ANISOU 3612  CA  GLU B 143     4011   5945   8899   -236   -485    452       C  
ATOM   3613  C   GLU B 143     -10.421  10.724  22.894  1.00 48.51           C  
ANISOU 3613  C   GLU B 143     3856   5807   8766   -158   -474    396       C  
ATOM   3614  O   GLU B 143     -10.316   9.905  21.952  1.00 48.86           O  
ANISOU 3614  O   GLU B 143     3860   5911   8794   -113   -462    397       O  
ATOM   3615  CB  GLU B 143      -8.603  12.201  21.807  1.00 50.16           C  
ANISOU 3615  CB  GLU B 143     4055   6063   8940   -244   -478    516       C  
ATOM   3616  CG  GLU B 143      -9.522  12.595  20.655  1.00 50.74           C  
ANISOU 3616  CG  GLU B 143     4152   6120   9004   -185   -473    521       C  
ATOM   3617  CD  GLU B 143     -10.834  13.316  20.950  1.00 50.38           C  
ANISOU 3617  CD  GLU B 143     4170   5987   8982   -158   -481    489       C  
ATOM   3618  OE1 GLU B 143     -11.147  13.607  22.132  1.00 49.37           O  
ANISOU 3618  OE1 GLU B 143     4081   5796   8881   -185   -488    455       O  
ATOM   3619  OE2 GLU B 143     -11.545  13.595  19.971  1.00 50.52           O  
ANISOU 3619  OE2 GLU B 143     4198   6009   8986   -103   -480    500       O  
ATOM   3620  N   ALA B 144     -11.446  10.754  23.751  1.00 47.09           N  
ANISOU 3620  N   ALA B 144     3712   5569   8612   -145   -476    347       N  
ATOM   3621  CA  ALA B 144     -12.512   9.729  23.840  1.00 45.97           C  
ANISOU 3621  CA  ALA B 144     3555   5426   8486    -90   -464    289       C  
ATOM   3622  C   ALA B 144     -13.765  10.167  23.069  1.00 45.29           C  
ANISOU 3622  C   ALA B 144     3482   5320   8404    -41   -468    269       C  
ATOM   3623  O   ALA B 144     -14.752   9.407  23.099  1.00 45.44           O  
ANISOU 3623  O   ALA B 144     3483   5342   8437     -4   -461    219       O  
ATOM   3624  CB  ALA B 144     -12.830   9.456  25.289  1.00 45.76           C  
ANISOU 3624  CB  ALA B 144     3547   5360   8479   -106   -459    255       C  
ATOM   3625  N   ALA B 145     -13.731  11.334  22.414  1.00 44.60           N  
ANISOU 3625  N   ALA B 145     3424   5216   8304    -42   -478    310       N  
ATOM   3626  CA  ALA B 145     -14.844  11.882  21.607  1.00 44.07           C  
ANISOU 3626  CA  ALA B 145     3369   5140   8233     13   -485    306       C  
ATOM   3627  C   ALA B 145     -15.216  10.864  20.532  1.00 43.72           C  
ANISOU 3627  C   ALA B 145     3270   5171   8168     60   -486    282       C  
ATOM   3628  O   ALA B 145     -16.398  10.442  20.498  1.00 44.49           O  
ANISOU 3628  O   ALA B 145     3349   5276   8276    100   -489    232       O  
ATOM   3629  CB  ALA B 145     -14.477  13.208  20.996  1.00 44.52           C  
ANISOU 3629  CB  ALA B 145     3468   5170   8275      4   -490    371       C  
ATOM   3630  N   ASN B 146     -14.244  10.462  19.713  1.00 42.80           N  
ANISOU 3630  N   ASN B 146     3126   5113   8020     53   -482    312       N  
ATOM   3631  CA  ASN B 146     -14.459   9.466  18.632  1.00 42.71           C  
ANISOU 3631  CA  ASN B 146     3071   5175   7980     95   -481    282       C  
ATOM   3632  C   ASN B 146     -15.001   8.161  19.224  1.00 41.99           C  
ANISOU 3632  C   ASN B 146     2957   5080   7917     99   -471    208       C  
ATOM   3633  O   ASN B 146     -16.093   7.732  18.808  1.00 42.38           O  
ANISOU 3633  O   ASN B 146     2987   5148   7967    131   -480    156       O  
ATOM   3634  CB  ASN B 146     -13.191   9.193  17.830  1.00 43.18           C  
ANISOU 3634  CB  ASN B 146     3108   5296   8001     88   -468    324       C  
ATOM   3635  CG  ASN B 146     -13.264   9.825  16.463  1.00 44.09           C  
ANISOU 3635  CG  ASN B 146     3223   5461   8066    122   -476    366       C  
ATOM   3636  OD1 ASN B 146     -12.509  10.748  16.156  1.00 45.49           O  
ANISOU 3636  OD1 ASN B 146     3417   5640   8227     99   -471    439       O  
ATOM   3637  ND2 ASN B 146     -14.199   9.355  15.658  1.00 44.07           N  
ANISOU 3637  ND2 ASN B 146     3202   5502   8039    173   -489    320       N  
ATOM   3638  N   PHE B 147     -14.263   7.562  20.159  1.00 40.76           N  
ANISOU 3638  N   PHE B 147     2800   4903   7782     67   -454    206       N  
ATOM   3639  CA  PHE B 147     -14.568   6.238  20.759  1.00 39.69           C  
ANISOU 3639  CA  PHE B 147     2650   4755   7673     69   -435    149       C  
ATOM   3640  C   PHE B 147     -16.003   6.211  21.301  1.00 39.73           C  
ANISOU 3640  C   PHE B 147     2659   4724   7711     75   -439     98       C  
ATOM   3641  O   PHE B 147     -16.673   5.168  21.159  1.00 39.76           O  
ANISOU 3641  O   PHE B 147     2641   4734   7729     84   -429     41       O  
ATOM   3642  CB  PHE B 147     -13.566   5.927  21.866  1.00 38.92           C  
ANISOU 3642  CB  PHE B 147     2558   4638   7590     37   -419    176       C  
ATOM   3643  CG  PHE B 147     -13.750   4.580  22.509  1.00 38.26           C  
ANISOU 3643  CG  PHE B 147     2468   4535   7533     44   -394    134       C  
ATOM   3644  CD1 PHE B 147     -13.718   3.425  21.746  1.00 38.25           C  
ANISOU 3644  CD1 PHE B 147     2449   4556   7525     73   -375    100       C  
ATOM   3645  CD2 PHE B 147     -13.946   4.471  23.875  1.00 37.85           C  
ANISOU 3645  CD2 PHE B 147     2433   4438   7508     22   -385    130       C  
ATOM   3646  CE1 PHE B 147     -13.880   2.185  22.340  1.00 38.25           C  
ANISOU 3646  CE1 PHE B 147     2454   4523   7555     77   -345     65       C  
ATOM   3647  CE2 PHE B 147     -14.098   3.230  24.470  1.00 37.86           C  
ANISOU 3647  CE2 PHE B 147     2433   4417   7534     30   -355    103       C  
ATOM   3648  CZ  PHE B 147     -14.068   2.090  23.701  1.00 38.13           C  
ANISOU 3648  CZ  PHE B 147     2455   4462   7570     56   -335     72       C  
ATOM   3649  N   CYS B 148     -16.452   7.310  21.916  1.00 39.58           N  
ANISOU 3649  N   CYS B 148     2667   4666   7705     68   -450    116       N  
ATOM   3650  CA  CYS B 148     -17.808   7.438  22.511  1.00 39.48           C  
ANISOU 3650  CA  CYS B 148     2655   4625   7721     81   -449     75       C  
ATOM   3651  C   CYS B 148     -18.855   7.325  21.393  1.00 39.77           C  
ANISOU 3651  C   CYS B 148     2655   4710   7745    120   -466     43       C  
ATOM   3652  O   CYS B 148     -19.735   6.460  21.496  1.00 39.61           O  
ANISOU 3652  O   CYS B 148     2601   4701   7744    120   -459    -12       O  
ATOM   3653  CB  CYS B 148     -17.948   8.738  23.296  1.00 39.60           C  
ANISOU 3653  CB  CYS B 148     2714   4587   7743     76   -453    104       C  
ATOM   3654  SG  CYS B 148     -17.151   8.680  24.925  1.00 39.22           S  
ANISOU 3654  SG  CYS B 148     2702   4489   7710     25   -436    113       S  
ATOM   3655  N   ALA B 149     -18.728   8.134  20.340  1.00 40.18           N  
ANISOU 3655  N   ALA B 149     2710   4796   7760    149   -488     80       N  
ATOM   3656  CA  ALA B 149     -19.641   8.146  19.173  1.00 40.74           C  
ANISOU 3656  CA  ALA B 149     2743   4931   7803    193   -511     59       C  
ATOM   3657  C   ALA B 149     -19.822   6.719  18.643  1.00 40.82           C  
ANISOU 3657  C   ALA B 149     2713   4989   7808    182   -509     -5       C  
ATOM   3658  O   ALA B 149     -20.974   6.317  18.379  1.00 40.98           O  
ANISOU 3658  O   ALA B 149     2692   5046   7833    192   -523    -59       O  
ATOM   3659  CB  ALA B 149     -19.104   9.069  18.109  1.00 41.12           C  
ANISOU 3659  CB  ALA B 149     2808   5010   7803    221   -528    122       C  
ATOM   3660  N   LEU B 150     -18.719   5.984  18.498  1.00 40.78           N  
ANISOU 3660  N   LEU B 150     2717   4984   7792    161   -492     -2       N  
ATOM   3661  CA  LEU B 150     -18.718   4.589  17.990  1.00 41.08           C  
ANISOU 3661  CA  LEU B 150     2732   5049   7824    152   -482    -66       C  
ATOM   3662  C   LEU B 150     -19.515   3.704  18.951  1.00 41.22           C  
ANISOU 3662  C   LEU B 150     2741   5023   7898    120   -463   -125       C  
ATOM   3663  O   LEU B 150     -20.320   2.909  18.458  1.00 42.43           O  
ANISOU 3663  O   LEU B 150     2864   5204   8053    112   -469   -192       O  
ATOM   3664  CB  LEU B 150     -17.279   4.094  17.822  1.00 40.95           C  
ANISOU 3664  CB  LEU B 150     2734   5032   7790    148   -458    -39       C  
ATOM   3665  CG  LEU B 150     -16.566   4.598  16.569  1.00 41.40           C  
ANISOU 3665  CG  LEU B 150     2790   5155   7784    177   -470      2       C  
ATOM   3666  CD1 LEU B 150     -15.144   4.068  16.498  1.00 41.27           C  
ANISOU 3666  CD1 LEU B 150     2781   5146   7752    177   -440     31       C  
ATOM   3667  CD2 LEU B 150     -17.334   4.214  15.313  1.00 42.03           C  
ANISOU 3667  CD2 LEU B 150     2844   5306   7819    204   -492    -53       C  
ATOM   3668  N   ILE B 151     -19.330   3.853  20.264  1.00 40.87           N  
ANISOU 3668  N   ILE B 151     2718   4915   7893     99   -441   -100       N  
ATOM   3669  CA  ILE B 151     -20.082   3.060  21.282  1.00 40.99           C  
ANISOU 3669  CA  ILE B 151     2726   4887   7959     69   -415   -143       C  
ATOM   3670  C   ILE B 151     -21.584   3.344  21.126  1.00 41.36           C  
ANISOU 3670  C   ILE B 151     2731   4965   8017     74   -433   -183       C  
ATOM   3671  O   ILE B 151     -22.357   2.371  21.148  1.00 41.60           O  
ANISOU 3671  O   ILE B 151     2732   4998   8073     46   -422   -243       O  
ATOM   3672  CB  ILE B 151     -19.586   3.348  22.712  1.00 40.80           C  
ANISOU 3672  CB  ILE B 151     2736   4803   7961     53   -391   -101       C  
ATOM   3673  CG1 ILE B 151     -18.161   2.830  22.925  1.00 40.84           C  
ANISOU 3673  CG1 ILE B 151     2767   4791   7956     47   -372    -67       C  
ATOM   3674  CG2 ILE B 151     -20.555   2.779  23.742  1.00 40.90           C  
ANISOU 3674  CG2 ILE B 151     2739   4780   8018     29   -364   -136       C  
ATOM   3675  CD1 ILE B 151     -17.448   3.437  24.120  1.00 40.58           C  
ANISOU 3675  CD1 ILE B 151     2764   4726   7927     34   -366    -14       C  
ATOM   3676  N   LEU B 152     -21.972   4.618  20.976  1.00 41.55           N  
ANISOU 3676  N   LEU B 152     2752   5011   8024    110   -459   -148       N  
ATOM   3677  CA  LEU B 152     -23.383   5.069  20.798  1.00 41.99           C  
ANISOU 3677  CA  LEU B 152     2760   5110   8084    134   -478   -172       C  
ATOM   3678  C   LEU B 152     -23.963   4.443  19.522  1.00 43.33           C  
ANISOU 3678  C   LEU B 152     2877   5361   8225    135   -508   -225       C  
ATOM   3679  O   LEU B 152     -25.074   3.887  19.590  1.00 43.73           O  
ANISOU 3679  O   LEU B 152     2874   5443   8298    114   -510   -281       O  
ATOM   3680  CB  LEU B 152     -23.438   6.600  20.730  1.00 41.43           C  
ANISOU 3680  CB  LEU B 152     2710   5038   7991    187   -496   -112       C  
ATOM   3681  CG  LEU B 152     -23.191   7.331  22.048  1.00 40.75           C  
ANISOU 3681  CG  LEU B 152     2674   4874   7931    184   -471    -76       C  
ATOM   3682  CD1 LEU B 152     -23.011   8.819  21.813  1.00 40.77           C  
ANISOU 3682  CD1 LEU B 152     2718   4860   7912    230   -486    -17       C  
ATOM   3683  CD2 LEU B 152     -24.315   7.077  23.041  1.00 40.70           C  
ANISOU 3683  CD2 LEU B 152     2639   4858   7964    179   -447   -112       C  
ATOM   3684  N   ALA B 153     -23.226   4.521  18.411  1.00 44.40           N  
ANISOU 3684  N   ALA B 153     3025   5534   8309    154   -529   -210       N  
ATOM   3685  CA  ALA B 153     -23.621   3.984  17.089  1.00 45.70           C  
ANISOU 3685  CA  ALA B 153     3149   5785   8429    159   -561   -262       C  
ATOM   3686  C   ALA B 153     -23.699   2.456  17.151  1.00 46.76           C  
ANISOU 3686  C   ALA B 153     3276   5900   8590    100   -540   -344       C  
ATOM   3687  O   ALA B 153     -24.742   1.911  16.755  1.00 47.36           O  
ANISOU 3687  O   ALA B 153     3298   6028   8667     75   -560   -413       O  
ATOM   3688  CB  ALA B 153     -22.643   4.437  16.035  1.00 45.97           C  
ANISOU 3688  CB  ALA B 153     3210   5855   8399    195   -577   -218       C  
ATOM   3689  N   TYR B 154     -22.640   1.795  17.635  1.00 47.61           N  
ANISOU 3689  N   TYR B 154     3433   5936   8718     78   -501   -336       N  
ATOM   3690  CA  TYR B 154     -22.524   0.311  17.680  1.00 48.90           C  
ANISOU 3690  CA  TYR B 154     3609   6061   8908     31   -471   -405       C  
ATOM   3691  C   TYR B 154     -23.639  -0.276  18.554  1.00 49.44           C  
ANISOU 3691  C   TYR B 154     3649   6096   9039    -21   -453   -451       C  
ATOM   3692  O   TYR B 154     -23.983  -1.447  18.338  1.00 49.79           O  
ANISOU 3692  O   TYR B 154     3688   6124   9102    -70   -438   -525       O  
ATOM   3693  CB  TYR B 154     -21.144  -0.145  18.171  1.00 48.96           C  
ANISOU 3693  CB  TYR B 154     3676   5999   8927     35   -428   -367       C  
ATOM   3694  CG  TYR B 154     -20.107  -0.293  17.082  1.00 49.80           C  
ANISOU 3694  CG  TYR B 154     3803   6142   8976     69   -432   -361       C  
ATOM   3695  CD1 TYR B 154     -20.296  -1.186  16.037  1.00 50.81           C  
ANISOU 3695  CD1 TYR B 154     3928   6303   9073     62   -438   -439       C  
ATOM   3696  CD2 TYR B 154     -18.933   0.446  17.089  1.00 49.43           C  
ANISOU 3696  CD2 TYR B 154     3778   6100   8902    105   -428   -280       C  
ATOM   3697  CE1 TYR B 154     -19.362  -1.331  15.024  1.00 50.87           C  
ANISOU 3697  CE1 TYR B 154     3956   6350   9020    100   -435   -436       C  
ATOM   3698  CE2 TYR B 154     -17.991   0.314  16.083  1.00 49.68           C  
ANISOU 3698  CE2 TYR B 154     3822   6176   8878    138   -425   -269       C  
ATOM   3699  CZ  TYR B 154     -18.206  -0.578  15.048  1.00 50.33           C  
ANISOU 3699  CZ  TYR B 154     3903   6293   8926    141   -427   -347       C  
ATOM   3700  OH  TYR B 154     -17.289  -0.722  14.052  1.00 51.20           O  
ANISOU 3700  OH  TYR B 154     4027   6452   8975    180   -419   -340       O  
ATOM   3701  N   CYS B 155     -24.173   0.510  19.493  1.00 49.95           N  
ANISOU 3701  N   CYS B 155     3697   6149   9132    -13   -449   -409       N  
ATOM   3702  CA  CYS B 155     -25.240   0.105  20.453  1.00 51.52           C  
ANISOU 3702  CA  CYS B 155     3863   6324   9388    -57   -424   -438       C  
ATOM   3703  C   CYS B 155     -26.621   0.654  20.047  1.00 52.22           C  
ANISOU 3703  C   CYS B 155     3871   6503   9468    -50   -462   -464       C  
ATOM   3704  O   CYS B 155     -27.611   0.332  20.744  1.00 51.69           O  
ANISOU 3704  O   CYS B 155     3760   6434   9445    -88   -442   -490       O  
ATOM   3705  CB  CYS B 155     -24.880   0.572  21.857  1.00 51.24           C  
ANISOU 3705  CB  CYS B 155     3863   6220   9384    -47   -388   -375       C  
ATOM   3706  SG  CYS B 155     -23.369  -0.212  22.470  1.00 51.40           S  
ANISOU 3706  SG  CYS B 155     3962   6150   9417    -57   -343   -343       S  
ATOM   3707  N   ASN B 156     -26.675   1.457  18.975  1.00 52.79           N  
ANISOU 3707  N   ASN B 156     3920   6655   9482      1   -512   -451       N  
ATOM   3708  CA  ASN B 156     -27.901   2.084  18.413  1.00 53.57           C  
ANISOU 3708  CA  ASN B 156     3938   6859   9557     29   -557   -465       C  
ATOM   3709  C   ASN B 156     -28.478   3.082  19.426  1.00 53.07           C  
ANISOU 3709  C   ASN B 156     3861   6781   9522     70   -541   -411       C  
ATOM   3710  O   ASN B 156     -29.611   3.562  19.203  1.00 53.48           O  
ANISOU 3710  O   ASN B 156     3838   6916   9565     99   -567   -418       O  
ATOM   3711  CB  ASN B 156     -28.901   1.019  17.959  1.00 54.91           C  
ANISOU 3711  CB  ASN B 156     4038   7088   9738    -38   -572   -558       C  
ATOM   3712  CG  ASN B 156     -28.243  -0.021  17.076  1.00 55.70           C  
ANISOU 3712  CG  ASN B 156     4172   7178   9811    -79   -578   -620       C  
ATOM   3713  OD1 ASN B 156     -28.257   0.097  15.851  1.00 56.80           O  
ANISOU 3713  OD1 ASN B 156     4291   7403   9885    -57   -626   -645       O  
ATOM   3714  ND2 ASN B 156     -27.626  -1.020  17.689  1.00 55.21           N  
ANISOU 3714  ND2 ASN B 156     4167   7013   9795   -131   -527   -640       N  
ATOM   3715  N   LYS B 157     -27.709   3.416  20.470  1.00 51.79           N  
ANISOU 3715  N   LYS B 157     3767   6524   9385     78   -501   -360       N  
ATOM   3716  CA  LYS B 157     -28.054   4.465  21.464  1.00 51.55           C  
ANISOU 3716  CA  LYS B 157     3747   6466   9373    123   -482   -309       C  
ATOM   3717  C   LYS B 157     -27.988   5.832  20.774  1.00 51.65           C  
ANISOU 3717  C   LYS B 157     3770   6514   9339    206   -518   -255       C  
ATOM   3718  O   LYS B 157     -27.604   5.892  19.588  1.00 51.62           O  
ANISOU 3718  O   LYS B 157     3766   6558   9288    223   -555   -251       O  
ATOM   3719  CB  LYS B 157     -27.106   4.398  22.666  1.00 50.54           C  
ANISOU 3719  CB  LYS B 157     3697   6233   9272    101   -436   -276       C  
ATOM   3720  CG  LYS B 157     -27.235   3.142  23.519  1.00 50.51           C  
ANISOU 3720  CG  LYS B 157     3689   6185   9315     31   -391   -313       C  
ATOM   3721  CD  LYS B 157     -28.033   3.350  24.790  1.00 50.81           C  
ANISOU 3721  CD  LYS B 157     3711   6205   9389     31   -352   -306       C  
ATOM   3722  CE  LYS B 157     -28.584   2.065  25.372  1.00 51.26           C  
ANISOU 3722  CE  LYS B 157     3737   6246   9492    -41   -310   -348       C  
ATOM   3723  NZ  LYS B 157     -29.873   1.687  24.743  1.00 51.94           N  
ANISOU 3723  NZ  LYS B 157     3725   6416   9590    -66   -327   -402       N  
ATOM   3724  N   THR B 158     -28.377   6.890  21.483  1.00 51.83           N  
ANISOU 3724  N   THR B 158     3807   6513   9372    259   -504   -213       N  
ATOM   3725  CA  THR B 158     -28.240   8.299  21.029  1.00 52.10           C  
ANISOU 3725  CA  THR B 158     3875   6549   9371    342   -525   -150       C  
ATOM   3726  C   THR B 158     -27.911   9.181  22.239  1.00 51.44           C  
ANISOU 3726  C   THR B 158     3865   6367   9310    363   -488   -110       C  
ATOM   3727  O   THR B 158     -28.016   8.701  23.396  1.00 50.37           O  
ANISOU 3727  O   THR B 158     3736   6188   9211    323   -449   -134       O  
ATOM   3728  CB  THR B 158     -29.484   8.778  20.261  1.00 53.12           C  
ANISOU 3728  CB  THR B 158     3923   6784   9475    410   -560   -150       C  
ATOM   3729  OG1 THR B 158     -30.651   8.275  20.913  1.00 53.39           O  
ANISOU 3729  OG1 THR B 158     3880   6859   9546    394   -541   -195       O  
ATOM   3730  CG2 THR B 158     -29.496   8.348  18.808  1.00 53.32           C  
ANISOU 3730  CG2 THR B 158     3901   6905   9450    409   -610   -170       C  
ATOM   3731  N   VAL B 159     -27.504  10.420  21.966  1.00 51.49           N  
ANISOU 3731  N   VAL B 159     3931   6339   9292    420   -498    -51       N  
ATOM   3732  CA  VAL B 159     -27.152  11.438  22.997  1.00 51.36           C  
ANISOU 3732  CA  VAL B 159     3999   6224   9291    441   -467    -16       C  
ATOM   3733  C   VAL B 159     -28.435  11.818  23.740  1.00 51.53           C  
ANISOU 3733  C   VAL B 159     3986   6258   9334    497   -441    -32       C  
ATOM   3734  O   VAL B 159     -29.487  11.887  23.083  1.00 52.02           O  
ANISOU 3734  O   VAL B 159     3970   6407   9385    553   -461    -36       O  
ATOM   3735  CB  VAL B 159     -26.479  12.667  22.360  1.00 51.31           C  
ANISOU 3735  CB  VAL B 159     4064   6175   9255    484   -483     49       C  
ATOM   3736  CG1 VAL B 159     -26.198  13.747  23.391  1.00 51.20           C  
ANISOU 3736  CG1 VAL B 159     4142   6052   9256    500   -452     74       C  
ATOM   3737  CG2 VAL B 159     -25.210  12.283  21.613  1.00 50.59           C  
ANISOU 3737  CG2 VAL B 159     3995   6085   9139    430   -502     68       C  
ATOM   3738  N   GLY B 160     -28.350  12.018  25.057  1.00 51.54           N  
ANISOU 3738  N   GLY B 160     4038   6187   9358    483   -400    -41       N  
ATOM   3739  CA  GLY B 160     -29.497  12.401  25.906  1.00 52.73           C  
ANISOU 3739  CA  GLY B 160     4164   6344   9527    539   -364    -56       C  
ATOM   3740  C   GLY B 160     -30.337  11.202  26.323  1.00 52.87           C  
ANISOU 3740  C   GLY B 160     4086   6432   9569    498   -345   -105       C  
ATOM   3741  O   GLY B 160     -31.008  11.292  27.378  1.00 53.24           O  
ANISOU 3741  O   GLY B 160     4123   6469   9633    516   -301   -121       O  
ATOM   3742  N   GLU B 161     -30.313  10.133  25.517  1.00 52.40           N  
ANISOU 3742  N   GLU B 161     3960   6437   9511    442   -374   -131       N  
ATOM   3743  CA  GLU B 161     -30.982   8.832  25.777  1.00 52.18           C  
ANISOU 3743  CA  GLU B 161     3847   6465   9513    377   -357   -181       C  
ATOM   3744  C   GLU B 161     -30.393   8.207  27.044  1.00 51.13           C  
ANISOU 3744  C   GLU B 161     3767   6255   9403    311   -310   -192       C  
ATOM   3745  O   GLU B 161     -29.165   8.283  27.221  1.00 51.33           O  
ANISOU 3745  O   GLU B 161     3876   6208   9416    284   -314   -171       O  
ATOM   3746  CB  GLU B 161     -30.785   7.907  24.573  1.00 52.55           C  
ANISOU 3746  CB  GLU B 161     3846   6571   9549    326   -400   -209       C  
ATOM   3747  CG  GLU B 161     -31.658   6.665  24.583  1.00 53.21           C  
ANISOU 3747  CG  GLU B 161     3834   6721   9663    260   -391   -266       C  
ATOM   3748  CD  GLU B 161     -31.566   5.825  23.319  1.00 53.76           C  
ANISOU 3748  CD  GLU B 161     3858   6851   9715    213   -437   -306       C  
ATOM   3749  OE1 GLU B 161     -32.335   4.847  23.203  1.00 54.77           O  
ANISOU 3749  OE1 GLU B 161     3908   7035   9867    152   -435   -360       O  
ATOM   3750  OE2 GLU B 161     -30.725   6.145  22.450  1.00 53.65           O  
ANISOU 3750  OE2 GLU B 161     3891   6829   9664    234   -472   -285       O  
ATOM   3751  N   LEU B 162     -31.243   7.598  27.873  1.00 50.88           N  
ANISOU 3751  N   LEU B 162     3682   6247   9400    287   -268   -218       N  
ATOM   3752  CA  LEU B 162     -30.846   6.852  29.097  1.00 49.97           C  
ANISOU 3752  CA  LEU B 162     3606   6075   9305    225   -218   -224       C  
ATOM   3753  C   LEU B 162     -30.097   5.587  28.673  1.00 48.75           C  
ANISOU 3753  C   LEU B 162     3456   5903   9164    141   -229   -241       C  
ATOM   3754  O   LEU B 162     -30.320   5.114  27.539  1.00 48.98           O  
ANISOU 3754  O   LEU B 162     3430   5984   9193    122   -265   -267       O  
ATOM   3755  CB  LEU B 162     -32.099   6.502  29.903  1.00 50.73           C  
ANISOU 3755  CB  LEU B 162     3629   6218   9427    223   -167   -243       C  
ATOM   3756  CG  LEU B 162     -32.960   7.691  30.316  1.00 51.73           C  
ANISOU 3756  CG  LEU B 162     3742   6371   9541    319   -148   -229       C  
ATOM   3757  CD1 LEU B 162     -34.328   7.228  30.795  1.00 52.83           C  
ANISOU 3757  CD1 LEU B 162     3775   6591   9707    315   -104   -249       C  
ATOM   3758  CD2 LEU B 162     -32.256   8.515  31.385  1.00 51.61           C  
ANISOU 3758  CD2 LEU B 162     3840   6267   9502    352   -119   -207       C  
ATOM   3759  N   GLY B 163     -29.249   5.051  29.548  1.00 47.03           N  
ANISOU 3759  N   GLY B 163     3301   5617   8950     98   -198   -229       N  
ATOM   3760  CA  GLY B 163     -28.400   3.902  29.193  1.00 46.32           C  
ANISOU 3760  CA  GLY B 163     3229   5498   8870     34   -203   -237       C  
ATOM   3761  C   GLY B 163     -28.070   3.032  30.384  1.00 45.53           C  
ANISOU 3761  C   GLY B 163     3164   5346   8789    -11   -150   -226       C  
ATOM   3762  O   GLY B 163     -28.220   3.509  31.524  1.00 45.10           O  
ANISOU 3762  O   GLY B 163     3137   5274   8725      9   -116   -206       O  
ATOM   3763  N   ASP B 164     -27.626   1.805  30.102  1.00 45.10           N  
ANISOU 3763  N   ASP B 164     3114   5267   8755    -65   -141   -239       N  
ATOM   3764  CA  ASP B 164     -27.259   0.764  31.096  1.00 45.41           C  
ANISOU 3764  CA  ASP B 164     3188   5251   8814   -108    -87   -222       C  
ATOM   3765  C   ASP B 164     -25.799   0.350  30.858  1.00 45.39           C  
ANISOU 3765  C   ASP B 164     3248   5202   8794   -111   -102   -197       C  
ATOM   3766  O   ASP B 164     -25.466  -0.039  29.713  1.00 45.06           O  
ANISOU 3766  O   ASP B 164     3197   5167   8755   -120   -132   -221       O  
ATOM   3767  CB  ASP B 164     -28.213  -0.428  30.990  1.00 45.78           C  
ANISOU 3767  CB  ASP B 164     3179   5305   8910   -172    -52   -259       C  
ATOM   3768  CG  ASP B 164     -28.113  -1.406  32.142  1.00 45.89           C  
ANISOU 3768  CG  ASP B 164     3226   5262   8948   -211     15   -232       C  
ATOM   3769  OD1 ASP B 164     -26.978  -1.709  32.546  1.00 45.59           O  
ANISOU 3769  OD1 ASP B 164     3256   5170   8893   -201     23   -195       O  
ATOM   3770  OD2 ASP B 164     -29.175  -1.852  32.628  1.00 46.66           O  
ANISOU 3770  OD2 ASP B 164     3275   5375   9079   -249     60   -244       O  
ATOM   3771  N   VAL B 165     -24.959   0.429  31.892  1.00 45.61           N  
ANISOU 3771  N   VAL B 165     3335   5194   8801   -100    -82   -151       N  
ATOM   3772  CA  VAL B 165     -23.514   0.064  31.800  1.00 46.10           C  
ANISOU 3772  CA  VAL B 165     3447   5225   8843    -95    -95   -118       C  
ATOM   3773  C   VAL B 165     -23.418  -1.378  31.288  1.00 47.05           C  
ANISOU 3773  C   VAL B 165     3564   5312   8999   -128    -70   -136       C  
ATOM   3774  O   VAL B 165     -22.654  -1.590  30.327  1.00 47.08           O  
ANISOU 3774  O   VAL B 165     3577   5316   8994   -118    -97   -142       O  
ATOM   3775  CB  VAL B 165     -22.780   0.245  33.142  1.00 45.80           C  
ANISOU 3775  CB  VAL B 165     3461   5167   8774    -83    -74    -67       C  
ATOM   3776  CG1 VAL B 165     -21.416  -0.425  33.140  1.00 45.38           C  
ANISOU 3776  CG1 VAL B 165     3443   5091   8705    -79    -77    -28       C  
ATOM   3777  CG2 VAL B 165     -22.649   1.713  33.508  1.00 45.63           C  
ANISOU 3777  CG2 VAL B 165     3458   5166   8711    -55   -106    -58       C  
ATOM   3778  N   ARG B 166     -24.185  -2.306  31.882  1.00 47.91           N  
ANISOU 3778  N   ARG B 166     3663   5392   9147   -166    -16   -145       N  
ATOM   3779  CA  ARG B 166     -24.118  -3.765  31.590  1.00 48.94           C  
ANISOU 3779  CA  ARG B 166     3807   5468   9318   -204     20   -160       C  
ATOM   3780  C   ARG B 166     -24.586  -4.037  30.155  1.00 49.42           C  
ANISOU 3780  C   ARG B 166     3828   5549   9398   -230    -10   -230       C  
ATOM   3781  O   ARG B 166     -23.991  -4.916  29.517  1.00 49.32           O  
ANISOU 3781  O   ARG B 166     3845   5496   9396   -237     -4   -246       O  
ATOM   3782  CB  ARG B 166     -24.939  -4.581  32.594  1.00 49.99           C  
ANISOU 3782  CB  ARG B 166     3939   5564   9491   -247     89   -150       C  
ATOM   3783  CG  ARG B 166     -24.706  -6.084  32.493  1.00 51.09           C  
ANISOU 3783  CG  ARG B 166     4115   5623   9673   -283    138   -152       C  
ATOM   3784  CD  ARG B 166     -25.668  -6.956  33.289  1.00 52.39           C  
ANISOU 3784  CD  ARG B 166     4274   5745   9887   -343    210   -147       C  
ATOM   3785  NE  ARG B 166     -27.067  -6.585  33.118  1.00 53.21           N  
ANISOU 3785  NE  ARG B 166     4297   5904  10013   -390    207   -195       N  
ATOM   3786  CZ  ARG B 166     -27.769  -6.717  31.993  1.00 53.88           C  
ANISOU 3786  CZ  ARG B 166     4328   6020  10125   -435    176   -269       C  
ATOM   3787  NH1 ARG B 166     -27.215  -7.221  30.901  1.00 54.06           N  
ANISOU 3787  NH1 ARG B 166     4375   6014  10151   -441    147   -311       N  
ATOM   3788  NH2 ARG B 166     -29.034  -6.330  31.961  1.00 54.54           N  
ANISOU 3788  NH2 ARG B 166     4328   6170  10223   -470    173   -303       N  
ATOM   3789  N   GLU B 167     -25.609  -3.321  29.676  1.00 50.39           N  
ANISOU 3789  N   GLU B 167     3887   5735   9520   -238    -41   -269       N  
ATOM   3790  CA  GLU B 167     -26.141  -3.445  28.290  1.00 51.39           C  
ANISOU 3790  CA  GLU B 167     3967   5906   9653   -260    -82   -336       C  
ATOM   3791  C   GLU B 167     -25.052  -3.022  27.299  1.00 50.91           C  
ANISOU 3791  C   GLU B 167     3933   5860   9547   -213   -130   -331       C  
ATOM   3792  O   GLU B 167     -24.788  -3.785  26.350  1.00 51.13           O  
ANISOU 3792  O   GLU B 167     3971   5878   9578   -231   -138   -373       O  
ATOM   3793  CB  GLU B 167     -27.409  -2.602  28.117  1.00 52.48           C  
ANISOU 3793  CB  GLU B 167     4025   6125   9789   -259   -107   -362       C  
ATOM   3794  CG  GLU B 167     -28.151  -2.848  26.806  1.00 53.57           C  
ANISOU 3794  CG  GLU B 167     4099   6323   9930   -291   -147   -433       C  
ATOM   3795  CD  GLU B 167     -29.498  -2.145  26.663  1.00 54.19           C  
ANISOU 3795  CD  GLU B 167     4084   6494  10009   -288   -170   -455       C  
ATOM   3796  OE1 GLU B 167     -30.039  -1.678  27.691  1.00 54.27           O  
ANISOU 3796  OE1 GLU B 167     4076   6512  10031   -273   -138   -422       O  
ATOM   3797  OE2 GLU B 167     -30.008  -2.061  25.516  1.00 54.37           O  
ANISOU 3797  OE2 GLU B 167     4050   6590  10016   -295   -219   -504       O  
ATOM   3798  N   THR B 168     -24.439  -1.856  27.524  1.00 50.40           N  
ANISOU 3798  N   THR B 168     3885   5820   9442   -159   -158   -282       N  
ATOM   3799  CA  THR B 168     -23.346  -1.294  26.685  1.00 49.84           C  
ANISOU 3799  CA  THR B 168     3838   5769   9327   -117   -201   -262       C  
ATOM   3800  C   THR B 168     -22.175  -2.280  26.645  1.00 50.22           C  
ANISOU 3800  C   THR B 168     3936   5767   9376   -115   -176   -246       C  
ATOM   3801  O   THR B 168     -21.707  -2.590  25.529  1.00 49.90           O  
ANISOU 3801  O   THR B 168     3898   5741   9318   -105   -195   -272       O  
ATOM   3802  CB  THR B 168     -22.884   0.069  27.209  1.00 49.31           C  
ANISOU 3802  CB  THR B 168     3790   5718   9227    -75   -223   -207       C  
ATOM   3803  OG1 THR B 168     -24.039   0.860  27.490  1.00 49.39           O  
ANISOU 3803  OG1 THR B 168     3762   5760   9243    -68   -229   -219       O  
ATOM   3804  CG2 THR B 168     -21.997   0.802  26.229  1.00 49.24           C  
ANISOU 3804  CG2 THR B 168     3792   5741   9175    -42   -267   -188       C  
ATOM   3805  N   MET B 169     -21.723  -2.742  27.818  1.00 50.71           N  
ANISOU 3805  N   MET B 169     4036   5777   9453   -116   -133   -203       N  
ATOM   3806  CA  MET B 169     -20.632  -3.745  27.963  1.00 51.15           C  
ANISOU 3806  CA  MET B 169     4140   5783   9512   -102   -101   -176       C  
ATOM   3807  C   MET B 169     -20.979  -4.973  27.113  1.00 52.83           C  
ANISOU 3807  C   MET B 169     4357   5957   9757   -131    -79   -239       C  
ATOM   3808  O   MET B 169     -20.074  -5.476  26.410  1.00 53.77           O  
ANISOU 3808  O   MET B 169     4503   6064   9860   -102    -78   -242       O  
ATOM   3809  CB  MET B 169     -20.429  -4.183  29.421  1.00 50.77           C  
ANISOU 3809  CB  MET B 169     4125   5687   9478   -103    -53   -122       C  
ATOM   3810  CG  MET B 169     -19.763  -3.147  30.326  1.00 50.10           C  
ANISOU 3810  CG  MET B 169     4050   5635   9351    -74    -73    -60       C  
ATOM   3811  SD  MET B 169     -18.480  -2.130  29.537  1.00 49.63           S  
ANISOU 3811  SD  MET B 169     3986   5631   9238    -36   -132    -33       S  
ATOM   3812  CE  MET B 169     -17.146  -2.342  30.712  1.00 49.49           C  
ANISOU 3812  CE  MET B 169     4002   5610   9191     -8   -117     46       C  
ATOM   3813  N   SER B 170     -22.238  -5.427  27.162  1.00 53.94           N  
ANISOU 3813  N   SER B 170     4472   6084   9939   -187    -61   -290       N  
ATOM   3814  CA  SER B 170     -22.739  -6.578  26.367  1.00 54.93           C  
ANISOU 3814  CA  SER B 170     4600   6170  10097   -235    -42   -365       C  
ATOM   3815  C   SER B 170     -22.416  -6.342  24.887  1.00 55.78           C  
ANISOU 3815  C   SER B 170     4696   6332  10165   -214    -92   -413       C  
ATOM   3816  O   SER B 170     -21.476  -7.001  24.406  1.00 57.13           O  
ANISOU 3816  O   SER B 170     4914   6466  10325   -185    -77   -416       O  
ATOM   3817  CB  SER B 170     -24.198  -6.839  26.585  1.00 55.69           C  
ANISOU 3817  CB  SER B 170     4650   6270  10237   -309    -28   -413       C  
ATOM   3818  OG  SER B 170     -24.489  -8.198  26.306  1.00 57.18           O  
ANISOU 3818  OG  SER B 170     4868   6385  10472   -368     12   -468       O  
ATOM   3819  N   TYR B 171     -23.098  -5.399  24.217  1.00 55.79           N  
ANISOU 3819  N   TYR B 171     4637   6420  10139   -216   -147   -441       N  
ATOM   3820  CA  TYR B 171     -22.930  -5.107  22.762  1.00 55.78           C  
ANISOU 3820  CA  TYR B 171     4618   6485  10090   -196   -198   -485       C  
ATOM   3821  C   TYR B 171     -21.455  -4.848  22.408  1.00 53.92           C  
ANISOU 3821  C   TYR B 171     4424   6252   9810   -129   -203   -435       C  
ATOM   3822  O   TYR B 171     -21.065  -5.149  21.262  1.00 53.88           O  
ANISOU 3822  O   TYR B 171     4428   6272   9771   -113   -219   -476       O  
ATOM   3823  CB  TYR B 171     -23.740  -3.889  22.309  1.00 56.75           C  
ANISOU 3823  CB  TYR B 171     4673   6705  10181   -185   -255   -490       C  
ATOM   3824  CG  TYR B 171     -25.236  -3.963  22.497  1.00 58.84           C  
ANISOU 3824  CG  TYR B 171     4874   7001  10480   -241   -260   -536       C  
ATOM   3825  CD1 TYR B 171     -25.979  -5.059  22.083  1.00 60.06           C  
ANISOU 3825  CD1 TYR B 171     5011   7143  10665   -313   -248   -619       C  
ATOM   3826  CD2 TYR B 171     -25.922  -2.893  23.054  1.00 59.70           C  
ANISOU 3826  CD2 TYR B 171     4937   7157  10588   -221   -276   -500       C  
ATOM   3827  CE1 TYR B 171     -27.357  -5.102  22.251  1.00 60.92           C  
ANISOU 3827  CE1 TYR B 171     5047   7295  10805   -371   -254   -659       C  
ATOM   3828  CE2 TYR B 171     -27.296  -2.917  23.224  1.00 60.39           C  
ANISOU 3828  CE2 TYR B 171     4953   7288  10703   -263   -278   -537       C  
ATOM   3829  CZ  TYR B 171     -28.019  -4.026  22.823  1.00 61.31           C  
ANISOU 3829  CZ  TYR B 171     5039   7402  10850   -341   -268   -615       C  
ATOM   3830  OH  TYR B 171     -29.375  -4.017  22.998  1.00 62.24           O  
ANISOU 3830  OH  TYR B 171     5073   7577  10995   -388   -271   -648       O  
ATOM   3831  N   LEU B 172     -20.664  -4.280  23.327  1.00 51.89           N  
ANISOU 3831  N   LEU B 172     4187   5982   9547    -94   -193   -353       N  
ATOM   3832  CA  LEU B 172     -19.218  -3.996  23.099  1.00 50.41           C  
ANISOU 3832  CA  LEU B 172     4026   5807   9319    -37   -197   -297       C  
ATOM   3833  C   LEU B 172     -18.453  -5.318  23.011  1.00 50.82           C  
ANISOU 3833  C   LEU B 172     4126   5796   9384    -21   -149   -307       C  
ATOM   3834  O   LEU B 172     -17.659  -5.457  22.066  1.00 51.84           O  
ANISOU 3834  O   LEU B 172     4266   5953   9477     17   -155   -315       O  
ATOM   3835  CB  LEU B 172     -18.650  -3.108  24.213  1.00 48.78           C  
ANISOU 3835  CB  LEU B 172     3824   5604   9105    -18   -200   -214       C  
ATOM   3836  CG  LEU B 172     -18.959  -1.617  24.095  1.00 47.70           C  
ANISOU 3836  CG  LEU B 172     3656   5525   8939    -12   -248   -192       C  
ATOM   3837  CD1 LEU B 172     -18.571  -0.874  25.365  1.00 46.86           C  
ANISOU 3837  CD1 LEU B 172     3565   5405   8832     -9   -245   -128       C  
ATOM   3838  CD2 LEU B 172     -18.265  -1.014  22.888  1.00 47.38           C  
ANISOU 3838  CD2 LEU B 172     3608   5545   8850     19   -283   -181       C  
ATOM   3839  N   PHE B 173     -18.697  -6.256  23.933  1.00 50.72           N  
ANISOU 3839  N   PHE B 173     4145   5703   9422    -44    -98   -306       N  
ATOM   3840  CA  PHE B 173     -17.931  -7.529  24.049  1.00 51.35           C  
ANISOU 3840  CA  PHE B 173     4283   5705   9521    -17    -42   -300       C  
ATOM   3841  C   PHE B 173     -18.242  -8.469  22.869  1.00 51.72           C  
ANISOU 3841  C   PHE B 173     4354   5724   9574    -35    -31   -394       C  
ATOM   3842  O   PHE B 173     -17.520  -9.476  22.721  1.00 51.45           O  
ANISOU 3842  O   PHE B 173     4375   5626   9548      1     15   -398       O  
ATOM   3843  CB  PHE B 173     -18.193  -8.209  25.398  1.00 51.81           C  
ANISOU 3843  CB  PHE B 173     4373   5682   9630    -37     10   -263       C  
ATOM   3844  CG  PHE B 173     -17.839  -7.408  26.630  1.00 51.65           C  
ANISOU 3844  CG  PHE B 173     4339   5689   9596    -18      3   -176       C  
ATOM   3845  CD1 PHE B 173     -17.067  -6.256  26.557  1.00 51.35           C  
ANISOU 3845  CD1 PHE B 173     4272   5730   9507     17    -42   -129       C  
ATOM   3846  CD2 PHE B 173     -18.272  -7.823  27.881  1.00 52.07           C  
ANISOU 3846  CD2 PHE B 173     4411   5688   9683    -41     45   -143       C  
ATOM   3847  CE1 PHE B 173     -16.755  -5.534  27.701  1.00 51.15           C  
ANISOU 3847  CE1 PHE B 173     4241   5728   9466     25    -51    -60       C  
ATOM   3848  CE2 PHE B 173     -17.952  -7.104  29.023  1.00 51.72           C  
ANISOU 3848  CE2 PHE B 173     4358   5675   9616    -24     37    -70       C  
ATOM   3849  CZ  PHE B 173     -17.193  -5.961  28.933  1.00 51.26           C  
ANISOU 3849  CZ  PHE B 173     4274   5693   9506      7    -12    -34       C  
ATOM   3850  N   GLN B 174     -19.269  -8.159  22.063  1.00 52.00           N  
ANISOU 3850  N   GLN B 174     4349   5806   9602    -85    -72   -470       N  
ATOM   3851  CA  GLN B 174     -19.606  -8.883  20.802  1.00 52.98           C  
ANISOU 3851  CA  GLN B 174     4487   5927   9713   -108    -77   -572       C  
ATOM   3852  C   GLN B 174     -18.537  -8.563  19.754  1.00 52.77           C  
ANISOU 3852  C   GLN B 174     4468   5964   9619    -36    -97   -564       C  
ATOM   3853  O   GLN B 174     -18.199  -9.463  18.957  1.00 53.43           O  
ANISOU 3853  O   GLN B 174     4596   6014   9689    -21    -72   -625       O  
ATOM   3854  CB  GLN B 174     -20.967  -8.472  20.226  1.00 53.40           C  
ANISOU 3854  CB  GLN B 174     4479   6046   9763   -176   -127   -645       C  
ATOM   3855  CG  GLN B 174     -22.132  -8.514  21.206  1.00 53.77           C  
ANISOU 3855  CG  GLN B 174     4494   6066   9870   -247   -115   -646       C  
ATOM   3856  CD  GLN B 174     -22.598  -9.912  21.531  1.00 55.00           C  
ANISOU 3856  CD  GLN B 174     4695   6110  10089   -315    -56   -701       C  
ATOM   3857  OE1 GLN B 174     -21.834 -10.873  21.476  1.00 55.73           O  
ANISOU 3857  OE1 GLN B 174     4863   6115  10195   -291     -8   -706       O  
ATOM   3858  NE2 GLN B 174     -23.866 -10.030  21.893  1.00 55.26           N  
ANISOU 3858  NE2 GLN B 174     4683   6146  10165   -399    -56   -737       N  
ATOM   3859  N   HIS B 175     -18.060  -7.312  19.759  1.00 51.92           N  
ANISOU 3859  N   HIS B 175     4318   5940   9468      2   -137   -493       N  
ATOM   3860  CA  HIS B 175     -17.057  -6.744  18.819  1.00 51.96           C  
ANISOU 3860  CA  HIS B 175     4315   6023   9404     66   -159   -466       C  
ATOM   3861  C   HIS B 175     -15.635  -6.973  19.344  1.00 51.90           C  
ANISOU 3861  C   HIS B 175     4335   5990   9392    131   -119   -386       C  
ATOM   3862  O   HIS B 175     -14.682  -6.653  18.618  1.00 51.57           O  
ANISOU 3862  O   HIS B 175     4285   6011   9297    185   -125   -358       O  
ATOM   3863  CB  HIS B 175     -17.290  -5.241  18.627  1.00 51.53           C  
ANISOU 3863  CB  HIS B 175     4203   6062   9311     66   -219   -422       C  
ATOM   3864  CG  HIS B 175     -18.635  -4.884  18.096  1.00 52.22           C  
ANISOU 3864  CG  HIS B 175     4251   6196   9394     20   -263   -486       C  
ATOM   3865  ND1 HIS B 175     -19.068  -5.287  16.845  1.00 53.10           N  
ANISOU 3865  ND1 HIS B 175     4357   6351   9467     10   -284   -572       N  
ATOM   3866  CD2 HIS B 175     -19.627  -4.132  18.619  1.00 51.86           C  
ANISOU 3866  CD2 HIS B 175     4164   6170   9370    -12   -292   -476       C  
ATOM   3867  CE1 HIS B 175     -20.276  -4.814  16.629  1.00 53.07           C  
ANISOU 3867  CE1 HIS B 175     4303   6397   9461    -28   -328   -608       C  
ATOM   3868  NE2 HIS B 175     -20.639  -4.099  17.701  1.00 52.64           N  
ANISOU 3868  NE2 HIS B 175     4226   6329   9446    -39   -331   -548       N  
ATOM   3869  N   ALA B 176     -15.495  -7.460  20.575  1.00 51.86           N  
ANISOU 3869  N   ALA B 176     4355   5911   9438    128    -80   -343       N  
ATOM   3870  CA  ALA B 176     -14.190  -7.747  21.204  1.00 52.19           C  
ANISOU 3870  CA  ALA B 176     4417   5936   9477    193    -42   -261       C  
ATOM   3871  C   ALA B 176     -13.814  -9.199  20.917  1.00 53.68           C  
ANISOU 3871  C   ALA B 176     4668   6042   9683    232     19   -301       C  
ATOM   3872  O   ALA B 176     -14.720 -10.039  20.901  1.00 54.31           O  
ANISOU 3872  O   ALA B 176     4787   6040   9807    184     43   -374       O  
ATOM   3873  CB  ALA B 176     -14.268  -7.485  22.679  1.00 51.58           C  
ANISOU 3873  CB  ALA B 176     4334   5829   9433    175    -36   -193       C  
ATOM   3874  N   ASN B 177     -12.530  -9.479  20.690  1.00 54.94           N  
ANISOU 3874  N   ASN B 177     4839   6222   9813    315     48   -254       N  
ATOM   3875  CA  ASN B 177     -12.037 -10.869  20.522  1.00 56.43           C  
ANISOU 3875  CA  ASN B 177     5097   6324  10020    373    117   -279       C  
ATOM   3876  C   ASN B 177     -11.975 -11.515  21.911  1.00 57.00           C  
ANISOU 3876  C   ASN B 177     5203   6305  10147    382    163   -218       C  
ATOM   3877  O   ASN B 177     -10.980 -11.275  22.625  1.00 56.74           O  
ANISOU 3877  O   ASN B 177     5147   6312  10099    442    169   -118       O  
ATOM   3878  CB  ASN B 177     -10.705 -10.928  19.775  1.00 56.94           C  
ANISOU 3878  CB  ASN B 177     5153   6453  10029    471    136   -247       C  
ATOM   3879  CG  ASN B 177     -10.419 -12.310  19.230  1.00 58.76           C  
ANISOU 3879  CG  ASN B 177     5462   6594  10269    531    206   -306       C  
ATOM   3880  OD1 ASN B 177      -9.521 -12.487  18.410  1.00 60.08           O  
ANISOU 3880  OD1 ASN B 177     5631   6808  10388    611    228   -307       O  
ATOM   3881  ND2 ASN B 177     -11.184 -13.297  19.668  1.00 59.59           N  
ANISOU 3881  ND2 ASN B 177     5636   6566  10436    492    245   -357       N  
ATOM   3882  N   LEU B 178     -13.023 -12.269  22.273  1.00 57.55           N  
ANISOU 3882  N   LEU B 178     5321   6267  10276    319    190   -273       N  
ATOM   3883  CA  LEU B 178     -13.180 -12.981  23.572  1.00 57.99           C  
ANISOU 3883  CA  LEU B 178     5420   6223  10388    316    241   -221       C  
ATOM   3884  C   LEU B 178     -13.276 -14.496  23.349  1.00 59.50           C  
ANISOU 3884  C   LEU B 178     5709   6272  10626    334    318   -274       C  
ATOM   3885  O   LEU B 178     -13.535 -15.214  24.329  1.00 59.67           O  
ANISOU 3885  O   LEU B 178     5778   6192  10700    324    369   -237       O  
ATOM   3886  CB  LEU B 178     -14.460 -12.489  24.253  1.00 57.77           C  
ANISOU 3886  CB  LEU B 178     5363   6189  10395    213    213   -236       C  
ATOM   3887  CG  LEU B 178     -14.393 -11.131  24.944  1.00 56.84           C  
ANISOU 3887  CG  LEU B 178     5173   6174  10246    201    156   -167       C  
ATOM   3888  CD1 LEU B 178     -15.753 -10.789  25.536  1.00 56.64           C  
ANISOU 3888  CD1 LEU B 178     5128   6134  10258    108    140   -194       C  
ATOM   3889  CD2 LEU B 178     -13.324 -11.111  26.029  1.00 56.58           C  
ANISOU 3889  CD2 LEU B 178     5141   6155  10199    270    175    -52       C  
ATOM   3890  N   ASP B 179     -13.058 -14.965  22.119  1.00 60.46           N  
ANISOU 3890  N   ASP B 179     5863   6382  10726    361    330   -355       N  
ATOM   3891  CA  ASP B 179     -13.437 -16.330  21.662  1.00 61.88           C  
ANISOU 3891  CA  ASP B 179     6143   6418  10949    347    394   -446       C  
ATOM   3892  C   ASP B 179     -12.746 -17.408  22.512  1.00 62.64           C  
ANISOU 3892  C   ASP B 179     6319   6392  11086    430    481   -372       C  
ATOM   3893  O   ASP B 179     -13.373 -18.466  22.717  1.00 63.68           O  
ANISOU 3893  O   ASP B 179     6536   6375  11282    386    539   -419       O  
ATOM   3894  CB  ASP B 179     -13.154 -16.492  20.167  1.00 62.68           C  
ANISOU 3894  CB  ASP B 179     6262   6552  11000    377    387   -543       C  
ATOM   3895  CG  ASP B 179     -13.877 -15.462  19.316  1.00 62.22           C  
ANISOU 3895  CG  ASP B 179     6128   6616  10896    301    302   -610       C  
ATOM   3896  OD1 ASP B 179     -13.427 -15.221  18.178  1.00 62.32           O  
ANISOU 3896  OD1 ASP B 179     6129   6705  10844    343    282   -653       O  
ATOM   3897  OD2 ASP B 179     -14.879 -14.899  19.807  1.00 61.99           O  
ANISOU 3897  OD2 ASP B 179     6051   6607  10893    207    260   -612       O  
ATOM   3898  N   SER B 180     -11.524 -17.163  23.000  1.00 62.44           N  
ANISOU 3898  N   SER B 180     6267   6430  11028    544    490   -257       N  
ATOM   3899  CA  SER B 180     -10.739 -18.138  23.810  1.00 63.18           C  
ANISOU 3899  CA  SER B 180     6427   6429  11149    647    570   -169       C  
ATOM   3900  C   SER B 180     -11.236 -18.156  25.265  1.00 63.17           C  
ANISOU 3900  C   SER B 180     6427   6383  11192    603    581    -87       C  
ATOM   3901  O   SER B 180     -10.879 -19.112  25.984  1.00 63.48           O  
ANISOU 3901  O   SER B 180     6538   6315  11265    670    654    -22       O  
ATOM   3902  CB  SER B 180      -9.254 -17.866  23.733  1.00 62.66           C  
ANISOU 3902  CB  SER B 180     6316   6468  11023    786    571    -78       C  
ATOM   3903  OG  SER B 180      -8.858 -16.930  24.721  1.00 61.38           O  
ANISOU 3903  OG  SER B 180     6067   6419  10834    791    523     33       O  
ATOM   3904  N   CYS B 181     -12.018 -17.148  25.684  1.00 62.37           N  
ANISOU 3904  N   CYS B 181     6252   6359  11086    503    516    -87       N  
ATOM   3905  CA  CYS B 181     -12.681 -17.086  27.019  1.00 62.47           C  
ANISOU 3905  CA  CYS B 181     6262   6337  11134    445    525    -25       C  
ATOM   3906  C   CYS B 181     -13.678 -18.242  27.155  1.00 63.70           C  
ANISOU 3906  C   CYS B 181     6510   6321  11369    374    593    -82       C  
ATOM   3907  O   CYS B 181     -14.351 -18.553  26.151  1.00 64.52           O  
ANISOU 3907  O   CYS B 181     6639   6378  11495    305    591   -204       O  
ATOM   3908  CB  CYS B 181     -13.442 -15.785  27.241  1.00 61.60           C  
ANISOU 3908  CB  CYS B 181     6062   6338  11005    351    445    -38       C  
ATOM   3909  SG  CYS B 181     -12.452 -14.294  26.969  1.00 60.51           S  
ANISOU 3909  SG  CYS B 181     5819   6389  10781    401    360     11       S  
ATOM   3910  N   LYS B 182     -13.792 -18.819  28.357  1.00 63.86           N  
ANISOU 3910  N   LYS B 182     6575   6259  11427    382    650      1       N  
ATOM   3911  CA  LYS B 182     -14.577 -20.053  28.629  1.00 64.71           C  
ANISOU 3911  CA  LYS B 182     6784   6185  11615    324    733    -28       C  
ATOM   3912  C   LYS B 182     -14.963 -20.098  30.112  1.00 64.43           C  
ANISOU 3912  C   LYS B 182     6751   6126  11603    301    764     76       C  
ATOM   3913  O   LYS B 182     -14.155 -19.654  30.949  1.00 63.55           O  
ANISOU 3913  O   LYS B 182     6604   6099  11443    389    750    191       O  
ATOM   3914  CB  LYS B 182     -13.744 -21.277  28.233  1.00 66.17           C  
ANISOU 3914  CB  LYS B 182     7078   6241  11820    432    813    -22       C  
ATOM   3915  CG  LYS B 182     -14.457 -22.622  28.306  1.00 67.70           C  
ANISOU 3915  CG  LYS B 182     7397   6226  12101    373    905    -67       C  
ATOM   3916  CD  LYS B 182     -13.500 -23.778  28.495  1.00 69.05           C  
ANISOU 3916  CD  LYS B 182     7681   6264  12291    512    999      0       C  
ATOM   3917  CE  LYS B 182     -14.167 -25.129  28.371  1.00 70.81           C  
ANISOU 3917  CE  LYS B 182     8044   6259  12602    450   1094    -62       C  
ATOM   3918  NZ  LYS B 182     -13.329 -26.205  28.951  1.00 72.28           N  
ANISOU 3918  NZ  LYS B 182     8343   6306  12813    590   1196     43       N  
ATOM   3919  N   ARG B 183     -16.152 -20.627  30.409  1.00 65.53           N  
ANISOU 3919  N   ARG B 183     6927   6160  11808    185    805     36       N  
ATOM   3920  CA  ARG B 183     -16.713 -20.762  31.783  1.00 66.53           C  
ANISOU 3920  CA  ARG B 183     7062   6253  11962    145    847    126       C  
ATOM   3921  C   ARG B 183     -17.442 -22.112  31.888  1.00 67.85           C  
ANISOU 3921  C   ARG B 183     7338   6220  12219     75    945     99       C  
ATOM   3922  O   ARG B 183     -18.122 -22.492  30.909  1.00 67.62           O  
ANISOU 3922  O   ARG B 183     7332   6126  12234    -19    946    -28       O  
ATOM   3923  CB  ARG B 183     -17.634 -19.570  32.083  1.00 66.02           C  
ANISOU 3923  CB  ARG B 183     6888   6319  11875     46    776    102       C  
ATOM   3924  CG  ARG B 183     -18.244 -19.564  33.479  1.00 66.59           C  
ANISOU 3924  CG  ARG B 183     6956   6382  11961      7    815    190       C  
ATOM   3925  CD  ARG B 183     -19.254 -18.445  33.673  1.00 66.56           C  
ANISOU 3925  CD  ARG B 183     6850   6496  11942    -89    753    151       C  
ATOM   3926  NE  ARG B 183     -18.679 -17.163  34.080  1.00 66.36           N  
ANISOU 3926  NE  ARG B 183     6747   6630  11835    -28    679    202       N  
ATOM   3927  CZ  ARG B 183     -19.377 -16.041  34.295  1.00 66.01           C  
ANISOU 3927  CZ  ARG B 183     6618   6698  11765    -85    622    178       C  
ATOM   3928  NH1 ARG B 183     -20.691 -16.021  34.135  1.00 66.80           N  
ANISOU 3928  NH1 ARG B 183     6685   6783  11910   -199    629    108       N  
ATOM   3929  NH2 ARG B 183     -18.760 -14.933  34.666  1.00 65.07           N  
ANISOU 3929  NH2 ARG B 183     6445   6704  11573    -29    560    222       N  
ATOM   3930  N   VAL B 184     -17.293 -22.816  33.017  1.00 68.47           N  
ANISOU 3930  N   VAL B 184     7485   6208  12322    116   1025    216       N  
ATOM   3931  CA  VAL B 184     -18.009 -24.096  33.300  1.00 70.75           C  
ANISOU 3931  CA  VAL B 184     7884   6295  12702     43   1130    212       C  
ATOM   3932  C   VAL B 184     -18.664 -24.010  34.687  1.00 71.48           C  
ANISOU 3932  C   VAL B 184     7958   6395  12804     -6   1166    315       C  
ATOM   3933  O   VAL B 184     -17.933 -23.853  35.693  1.00 70.62           O  
ANISOU 3933  O   VAL B 184     7849   6337  12644    103   1178    452       O  
ATOM   3934  CB  VAL B 184     -17.086 -25.322  33.145  1.00 71.84           C  
ANISOU 3934  CB  VAL B 184     8157   6270  12867    162   1216    255       C  
ATOM   3935  CG1 VAL B 184     -17.791 -26.619  33.522  1.00 73.44           C  
ANISOU 3935  CG1 VAL B 184     8486   6252  13166     85   1331    263       C  
ATOM   3936  CG2 VAL B 184     -16.540 -25.411  31.728  1.00 71.66           C  
ANISOU 3936  CG2 VAL B 184     8152   6242  12831    204   1185    139       C  
ATOM   3937  N   LEU B 185     -19.999 -24.137  34.702  1.00 72.62           N  
ANISOU 3937  N   LEU B 185     8087   6496  13009   -169   1185    248       N  
ATOM   3938  CA  LEU B 185     -20.926 -23.798  35.820  1.00 72.98           C  
ANISOU 3938  CA  LEU B 185     8080   6587  13060   -252   1204    311       C  
ATOM   3939  C   LEU B 185     -21.748 -25.033  36.201  1.00 74.34           C  
ANISOU 3939  C   LEU B 185     8347   6569  13328   -355   1317    323       C  
ATOM   3940  O   LEU B 185     -22.177 -25.754  35.285  1.00 75.26           O  
ANISOU 3940  O   LEU B 185     8517   6562  13513   -443   1342    212       O  
ATOM   3941  CB  LEU B 185     -21.864 -22.678  35.356  1.00 72.41           C  
ANISOU 3941  CB  LEU B 185     7876   6665  12971   -362   1114    208       C  
ATOM   3942  CG  LEU B 185     -21.503 -21.268  35.814  1.00 71.21           C  
ANISOU 3942  CG  LEU B 185     7617   6713  12726   -295   1027    255       C  
ATOM   3943  CD1 LEU B 185     -22.336 -20.237  35.071  1.00 70.56           C  
ANISOU 3943  CD1 LEU B 185     7420   6757  12632   -386    940    140       C  
ATOM   3944  CD2 LEU B 185     -21.686 -21.121  37.319  1.00 71.67           C  
ANISOU 3944  CD2 LEU B 185     7668   6803  12758   -278   1070    383       C  
ATOM   3945  N   ASN B 186     -22.000 -25.227  37.497  1.00 74.26           N  
ANISOU 3945  N   ASN B 186     8354   6542  13319   -354   1382    450       N  
ATOM   3946  CA  ASN B 186     -22.670 -26.435  38.042  1.00 76.36           C  
ANISOU 3946  CA  ASN B 186     8719   6619  13673   -439   1505    495       C  
ATOM   3947  C   ASN B 186     -23.905 -26.007  38.842  1.00 77.10           C  
ANISOU 3947  C   ASN B 186     8728   6787  13777   -568   1519    516       C  
ATOM   3948  O   ASN B 186     -23.860 -24.917  39.440  1.00 76.63           O  
ANISOU 3948  O   ASN B 186     8569   6907  13637   -523   1459    561       O  
ATOM   3949  CB  ASN B 186     -21.698 -27.244  38.897  1.00 76.85           C  
ANISOU 3949  CB  ASN B 186     8900   6574  13723   -293   1590    654       C  
ATOM   3950  CG  ASN B 186     -21.812 -28.737  38.678  1.00 78.56           C  
ANISOU 3950  CG  ASN B 186     9274   6534  14040   -329   1708    653       C  
ATOM   3951  OD1 ASN B 186     -22.891 -29.308  38.810  1.00 79.06           O  
ANISOU 3951  OD1 ASN B 186     9364   6489  14185   -485   1774    624       O  
ATOM   3952  ND2 ASN B 186     -20.702 -29.375  38.346  1.00 79.15           N  
ANISOU 3952  ND2 ASN B 186     9452   6509  14112   -185   1737    685       N  
ATOM   3953  N   VAL B 187     -24.964 -26.828  38.834  1.00 78.82           N  
ANISOU 3953  N   VAL B 187     8984   6874  14090   -724   1598    480       N  
ATOM   3954  CA  VAL B 187     -26.205 -26.643  39.650  1.00 79.14           C  
ANISOU 3954  CA  VAL B 187     8951   6962  14153   -856   1638    511       C  
ATOM   3955  C   VAL B 187     -26.614 -28.005  40.235  1.00 80.96           C  
ANISOU 3955  C   VAL B 187     9306   6980  14474   -930   1780    587       C  
ATOM   3956  O   VAL B 187     -27.096 -28.853  39.462  1.00 81.55           O  
ANISOU 3956  O   VAL B 187     9440   6901  14642  -1052   1820    489       O  
ATOM   3957  CB  VAL B 187     -27.336 -26.007  38.816  1.00 78.63           C  
ANISOU 3957  CB  VAL B 187     8758   7002  14114  -1010   1565    358       C  
ATOM   3958  CG1 VAL B 187     -28.609 -25.823  39.629  1.00 79.13           C  
ANISOU 3958  CG1 VAL B 187     8737   7126  14201  -1139   1610    391       C  
ATOM   3959  CG2 VAL B 187     -26.905 -24.684  38.196  1.00 76.68           C  
ANISOU 3959  CG2 VAL B 187     8404   6950  13781   -930   1431    290       C  
ATOM   3960  N   VAL B 188     -26.416 -28.203  41.545  1.00 81.71           N  
ANISOU 3960  N   VAL B 188     9442   7065  14539   -861   1855    754       N  
ATOM   3961  CA  VAL B 188     -26.688 -29.482  42.270  1.00 84.79           C  
ANISOU 3961  CA  VAL B 188     9961   7251  15005   -908   2002    861       C  
ATOM   3962  C   VAL B 188     -28.016 -29.356  43.035  1.00 86.61           C  
ANISOU 3962  C   VAL B 188    10111   7532  15262  -1062   2056    892       C  
ATOM   3963  O   VAL B 188     -28.054 -28.595  44.025  1.00 86.17           O  
ANISOU 3963  O   VAL B 188     9982   7635  15123  -1002   2044    987       O  
ATOM   3964  CB  VAL B 188     -25.528 -29.845  43.222  1.00 84.86           C  
ANISOU 3964  CB  VAL B 188    10073   7216  14953   -713   2056   1042       C  
ATOM   3965  CG1 VAL B 188     -25.843 -31.066  44.075  1.00 86.71           C  
ANISOU 3965  CG1 VAL B 188    10435   7254  15254   -752   2210   1173       C  
ATOM   3966  CG2 VAL B 188     -24.219 -30.052  42.478  1.00 84.41           C  
ANISOU 3966  CG2 VAL B 188    10091   7107  14874   -556   2014   1020       C  
ATOM   3967  N   CYS B 189     -29.063 -30.065  42.589  1.00 88.97           N  
ANISOU 3967  N   CYS B 189    10422   7710  15672  -1258   2114    810       N  
ATOM   3968  CA  CYS B 189     -30.280 -30.378  43.393  1.00 90.86           C  
ANISOU 3968  CA  CYS B 189    10624   7933  15963  -1414   2209    867       C  
ATOM   3969  C   CYS B 189     -30.148 -31.805  43.939  1.00 93.18           C  
ANISOU 3969  C   CYS B 189    11094   7972  16335  -1433   2361    983       C  
ATOM   3970  O   CYS B 189     -29.661 -32.683  43.199  1.00 93.35           O  
ANISOU 3970  O   CYS B 189    11246   7798  16422  -1428   2388    932       O  
ATOM   3971  CB  CYS B 189     -31.574 -30.234  42.596  1.00 91.39           C  
ANISOU 3971  CB  CYS B 189    10578   8044  16103  -1631   2177    709       C  
ATOM   3972  SG  CYS B 189     -33.071 -30.452  43.603  1.00 92.18           S  
ANISOU 3972  SG  CYS B 189    10598   8171  16255  -1819   2287    782       S  
ATOM   3973  N   LYS B 190     -30.568 -32.016  45.190  1.00 95.00           N  
ANISOU 3973  N   LYS B 190    11333   8204  16557  -1449   2461   1137       N  
ATOM   3974  CA  LYS B 190     -30.427 -33.302  45.925  1.00 97.76           C  
ANISOU 3974  CA  LYS B 190    11852   8323  16967  -1448   2617   1285       C  
ATOM   3975  C   LYS B 190     -31.500 -34.301  45.469  1.00100.30           C  
ANISOU 3975  C   LYS B 190    12218   8455  17436  -1689   2708   1210       C  
ATOM   3976  O   LYS B 190     -31.328 -35.504  45.754  1.00101.62           O  
ANISOU 3976  O   LYS B 190    12552   8379  17677  -1703   2834   1298       O  
ATOM   3977  CB  LYS B 190     -30.531 -33.068  47.434  1.00 97.75           C  
ANISOU 3977  CB  LYS B 190    11830   8420  16888  -1381   2686   1477       C  
ATOM   3978  CG  LYS B 190     -29.503 -32.106  48.020  1.00 95.81           C  
ANISOU 3978  CG  LYS B 190    11543   8366  16492  -1155   2601   1559       C  
ATOM   3979  CD  LYS B 190     -29.800 -31.710  49.453  1.00 95.64           C  
ANISOU 3979  CD  LYS B 190    11474   8479  16383  -1115   2654   1716       C  
ATOM   3980  CE  LYS B 190     -30.218 -32.879  50.322  1.00 97.50           C  
ANISOU 3980  CE  LYS B 190    11827   8535  16680  -1177   2825   1872       C  
ATOM   3981  NZ  LYS B 190     -30.372 -32.485  51.741  1.00 97.40           N  
ANISOU 3981  NZ  LYS B 190    11777   8665  16563  -1111   2876   2035       N  
ATOM   3982  N   THR B 191     -32.557 -33.824  44.796  1.00100.96           N  
ANISOU 3982  N   THR B 191    12157   8645  17558  -1870   2646   1055       N  
ATOM   3983  CA  THR B 191     -33.702 -34.638  44.301  1.00103.49           C  
ANISOU 3983  CA  THR B 191    12481   8825  18012  -2128   2713    960       C  
ATOM   3984  C   THR B 191     -33.469 -35.026  42.835  1.00103.92           C  
ANISOU 3984  C   THR B 191    12593   8762  18130  -2184   2649    771       C  
ATOM   3985  O   THR B 191     -33.393 -36.237  42.553  1.00106.58           O  
ANISOU 3985  O   THR B 191    13093   8835  18566  -2257   2742    760       O  
ATOM   3986  CB  THR B 191     -35.031 -33.891  44.481  1.00103.49           C  
ANISOU 3986  CB  THR B 191    12277   9034  18011  -2291   2685    911       C  
ATOM   3987  OG1 THR B 191     -35.046 -33.323  45.791  1.00103.20           O  
ANISOU 3987  OG1 THR B 191    12184   9141  17885  -2190   2723   1077       O  
ATOM   3988  CG2 THR B 191     -36.239 -34.785  44.297  1.00105.85           C  
ANISOU 3988  CG2 THR B 191    12574   9200  18443  -2560   2778    860       C  
ATOM   3989  N   CYS B 192     -33.363 -34.041  41.938  1.00102.16           N  
ANISOU 3989  N   CYS B 192    12245   8721  17847  -2151   2499    627       N  
ATOM   3990  CA  CYS B 192     -33.155 -34.249  40.478  1.00102.34           C  
ANISOU 3990  CA  CYS B 192    12300   8674  17907  -2196   2421    435       C  
ATOM   3991  C   CYS B 192     -31.737 -34.787  40.238  1.00101.78           C  
ANISOU 3991  C   CYS B 192    12411   8441  17817  -2000   2437    474       C  
ATOM   3992  O   CYS B 192     -31.616 -35.937  39.754  1.00103.41           O  
ANISOU 3992  O   CYS B 192    12777   8396  18115  -2063   2512    427       O  
ATOM   3993  CB  CYS B 192     -33.392 -32.960  39.696  1.00100.97           C  
ANISOU 3993  CB  CYS B 192    11939   8762  17660  -2190   2260    299       C  
ATOM   3994  SG  CYS B 192     -34.722 -31.935  40.378  1.00101.41           S  
ANISOU 3994  SG  CYS B 192    11763   9082  17686  -2304   2234    322       S  
ATOM   3995  N   GLY B 193     -30.717 -33.993  40.589  1.00 98.69           N  
ANISOU 3995  N   GLY B 193    11996   8189  17313  -1773   2373    557       N  
ATOM   3996  CA  GLY B 193     -29.288 -34.324  40.422  1.00 97.56           C  
ANISOU 3996  CA  GLY B 193    11993   7944  17132  -1559   2375    608       C  
ATOM   3997  C   GLY B 193     -28.471 -33.121  39.972  1.00 94.42           C  
ANISOU 3997  C   GLY B 193    11491   7764  16617  -1395   2231    564       C  
ATOM   3998  O   GLY B 193     -28.793 -31.990  40.397  1.00 92.47           O  
ANISOU 3998  O   GLY B 193    11088   7750  16295  -1384   2157    585       O  
ATOM   3999  N   GLN B 194     -27.470 -33.362  39.118  1.00 93.33           N  
ANISOU 3999  N   GLN B 194    11440   7552  16466  -1276   2195    502       N  
ATOM   4000  CA  GLN B 194     -26.393 -32.403  38.745  1.00 91.15           C  
ANISOU 4000  CA  GLN B 194    11103   7448  16081  -1087   2079    492       C  
ATOM   4001  C   GLN B 194     -26.609 -31.910  37.307  1.00 89.88           C  
ANISOU 4001  C   GLN B 194    10865   7367  15917  -1159   1967    287       C  
ATOM   4002  O   GLN B 194     -27.172 -32.686  36.508  1.00 91.23           O  
ANISOU 4002  O   GLN B 194    11098   7389  16174  -1305   1998    160       O  
ATOM   4003  CB  GLN B 194     -25.036 -33.101  38.864  1.00 91.50           C  
ANISOU 4003  CB  GLN B 194    11304   7353  16109   -884   2134    589       C  
ATOM   4004  CG  GLN B 194     -24.039 -32.369  39.748  1.00 90.01           C  
ANISOU 4004  CG  GLN B 194    11070   7324  15805   -675   2097    743       C  
ATOM   4005  CD  GLN B 194     -22.607 -32.705  39.409  1.00 89.97           C  
ANISOU 4005  CD  GLN B 194    11163   7259  15763   -466   2096    783       C  
ATOM   4006  OE1 GLN B 194     -22.326 -33.604  38.619  1.00 90.63           O  
ANISOU 4006  OE1 GLN B 194    11370   7153  15909   -461   2143    712       O  
ATOM   4007  NE2 GLN B 194     -21.682 -31.975  40.011  1.00 88.67           N  
ANISOU 4007  NE2 GLN B 194    10938   7259  15490   -291   2042    894       N  
ATOM   4008  N   GLN B 195     -26.170 -30.685  36.986  1.00 87.24           N  
ANISOU 4008  N   GLN B 195    10406   7256  15485  -1063   1842    255       N  
ATOM   4009  CA  GLN B 195     -26.155 -30.155  35.590  1.00 86.29           C  
ANISOU 4009  CA  GLN B 195    10219   7223  15341  -1092   1731     77       C  
ATOM   4010  C   GLN B 195     -25.041 -29.104  35.414  1.00 83.57           C  
ANISOU 4010  C   GLN B 195     9811   7057  14885   -902   1630    106       C  
ATOM   4011  O   GLN B 195     -24.984 -28.146  36.221  1.00 81.15           O  
ANISOU 4011  O   GLN B 195     9403   6921  14508   -843   1588    197       O  
ATOM   4012  CB  GLN B 195     -27.540 -29.630  35.187  1.00 86.24           C  
ANISOU 4012  CB  GLN B 195    10073   7332  15361  -1292   1675    -42       C  
ATOM   4013  CG  GLN B 195     -27.955 -28.307  35.817  1.00 84.68           C  
ANISOU 4013  CG  GLN B 195     9705   7377  15090  -1278   1603      8       C  
ATOM   4014  CD  GLN B 195     -28.304 -27.280  34.768  1.00 83.63           C  
ANISOU 4014  CD  GLN B 195     9435   7427  14912  -1317   1472   -132       C  
ATOM   4015  OE1 GLN B 195     -29.447 -26.850  34.646  1.00 83.30           O  
ANISOU 4015  OE1 GLN B 195     9273   7488  14887  -1456   1438   -198       O  
ATOM   4016  NE2 GLN B 195     -27.310 -26.889  33.986  1.00 83.42           N  
ANISOU 4016  NE2 GLN B 195     9423   7446  14825  -1189   1399   -176       N  
ATOM   4017  N   GLN B 196     -24.189 -29.283  34.392  1.00 82.57           N  
ANISOU 4017  N   GLN B 196     9741   6890  14739   -814   1596     28       N  
ATOM   4018  CA  GLN B 196     -23.090 -28.340  34.040  1.00 80.32           C  
ANISOU 4018  CA  GLN B 196     9395   6767  14352   -645   1502     41       C  
ATOM   4019  C   GLN B 196     -23.359 -27.715  32.663  1.00 78.95           C  
ANISOU 4019  C   GLN B 196     9139   6701  14154   -708   1396   -132       C  
ATOM   4020  O   GLN B 196     -24.000 -28.375  31.818  1.00 79.53           O  
ANISOU 4020  O   GLN B 196     9258   6667  14291   -837   1413   -265       O  
ATOM   4021  CB  GLN B 196     -21.716 -29.022  34.109  1.00 80.74           C  
ANISOU 4021  CB  GLN B 196     9577   6709  14389   -457   1556    125       C  
ATOM   4022  CG  GLN B 196     -21.446 -30.045  33.009  1.00 82.03           C  
ANISOU 4022  CG  GLN B 196     9870   6688  14606   -461   1599     12       C  
ATOM   4023  CD  GLN B 196     -19.981 -30.201  32.672  1.00 81.29           C  
ANISOU 4023  CD  GLN B 196     9842   6583  14461   -251   1601     55       C  
ATOM   4024  OE1 GLN B 196     -19.098 -29.932  33.482  1.00 80.33           O  
ANISOU 4024  OE1 GLN B 196     9708   6529  14283    -95   1606    203       O  
ATOM   4025  NE2 GLN B 196     -19.710 -30.653  31.458  1.00 81.41           N  
ANISOU 4025  NE2 GLN B 196     9923   6517  14489   -245   1598    -76       N  
ATOM   4026  N   THR B 197     -22.885 -26.480  32.470  1.00 76.93           N  
ANISOU 4026  N   THR B 197     8770   6650  13808   -621   1292   -127       N  
ATOM   4027  CA  THR B 197     -23.016 -25.665  31.231  1.00 76.42           C  
ANISOU 4027  CA  THR B 197     8614   6723  13699   -651   1182   -266       C  
ATOM   4028  C   THR B 197     -21.621 -25.236  30.761  1.00 75.77           C  
ANISOU 4028  C   THR B 197     8539   6712  13538   -472   1135   -241       C  
ATOM   4029  O   THR B 197     -20.828 -24.811  31.624  1.00 74.43           O  
ANISOU 4029  O   THR B 197     8353   6608  13319   -346   1135   -107       O  
ATOM   4030  CB  THR B 197     -23.883 -24.421  31.471  1.00 75.45           C  
ANISOU 4030  CB  THR B 197     8329   6796  13540   -727   1100   -277       C  
ATOM   4031  OG1 THR B 197     -23.528 -23.895  32.750  1.00 74.66           O  
ANISOU 4031  OG1 THR B 197     8199   6767  13400   -642   1113   -126       O  
ATOM   4032  CG2 THR B 197     -25.370 -24.697  31.433  1.00 76.14           C  
ANISOU 4032  CG2 THR B 197     8373   6858  13697   -923   1117   -355       C  
ATOM   4033  N   THR B 198     -21.348 -25.323  29.452  1.00 76.35           N  
ANISOU 4033  N   THR B 198     8629   6782  13595   -465   1096   -365       N  
ATOM   4034  CA  THR B 198     -20.036 -24.997  28.822  1.00 76.07           C  
ANISOU 4034  CA  THR B 198     8602   6812  13488   -303   1058   -356       C  
ATOM   4035  C   THR B 198     -20.192 -23.747  27.943  1.00 74.88           C  
ANISOU 4035  C   THR B 198     8321   6860  13267   -324    938   -439       C  
ATOM   4036  O   THR B 198     -20.324 -23.891  26.705  1.00 75.36           O  
ANISOU 4036  O   THR B 198     8394   6919  13320   -362    907   -572       O  
ATOM   4037  CB  THR B 198     -19.478 -26.204  28.055  1.00 77.30           C  
ANISOU 4037  CB  THR B 198     8903   6790  13677   -254   1127   -420       C  
ATOM   4038  OG1 THR B 198     -19.369 -27.297  28.970  1.00 78.65           O  
ANISOU 4038  OG1 THR B 198     9194   6773  13914   -230   1241   -326       O  
ATOM   4039  CG2 THR B 198     -18.132 -25.932  27.421  1.00 76.54           C  
ANISOU 4039  CG2 THR B 198     8810   6762  13506    -83   1099   -407       C  
ATOM   4040  N   LEU B 199     -20.157 -22.567  28.572  1.00 73.44           N  
ANISOU 4040  N   LEU B 199     8027   6842  13032   -296    876   -360       N  
ATOM   4041  CA  LEU B 199     -20.322 -21.243  27.912  1.00 71.75           C  
ANISOU 4041  CA  LEU B 199     7687   6821  12752   -309    765   -414       C  
ATOM   4042  C   LEU B 199     -18.958 -20.775  27.389  1.00 70.54           C  
ANISOU 4042  C   LEU B 199     7528   6748  12523   -160    728   -383       C  
ATOM   4043  O   LEU B 199     -17.926 -21.134  27.994  1.00 70.10           O  
ANISOU 4043  O   LEU B 199     7525   6650  12457    -39    774   -278       O  
ATOM   4044  CB  LEU B 199     -20.906 -20.231  28.907  1.00 70.73           C  
ANISOU 4044  CB  LEU B 199     7456   6811  12606   -346    728   -341       C  
ATOM   4045  CG  LEU B 199     -22.114 -20.695  29.728  1.00 71.71           C  
ANISOU 4045  CG  LEU B 199     7581   6863  12800   -471    782   -331       C  
ATOM   4046  CD1 LEU B 199     -22.502 -19.641  30.757  1.00 70.40           C  
ANISOU 4046  CD1 LEU B 199     7320   6825  12603   -475    750   -249       C  
ATOM   4047  CD2 LEU B 199     -23.305 -21.035  28.838  1.00 72.26           C  
ANISOU 4047  CD2 LEU B 199     7630   6906  12917   -624    769   -474       C  
ATOM   4048  N   LYS B 200     -18.970 -20.002  26.302  1.00 69.64           N  
ANISOU 4048  N   LYS B 200     7347   6755  12358   -169    647   -467       N  
ATOM   4049  CA  LYS B 200     -17.770 -19.397  25.669  1.00 68.66           C  
ANISOU 4049  CA  LYS B 200     7197   6733  12157    -45    603   -446       C  
ATOM   4050  C   LYS B 200     -18.200 -18.106  24.964  1.00 67.12           C  
ANISOU 4050  C   LYS B 200     6889   6706  11907    -89    502   -500       C  
ATOM   4051  O   LYS B 200     -19.422 -17.903  24.802  1.00 66.84           O  
ANISOU 4051  O   LYS B 200     6808   6689  11896   -209    472   -572       O  
ATOM   4052  CB  LYS B 200     -17.110 -20.400  24.719  1.00 70.40           C  
ANISOU 4052  CB  LYS B 200     7516   6852  12379     15    650   -512       C  
ATOM   4053  CG  LYS B 200     -18.069 -21.298  23.949  1.00 72.37           C  
ANISOU 4053  CG  LYS B 200     7829   6985  12680   -101    676   -655       C  
ATOM   4054  CD  LYS B 200     -17.379 -22.354  23.100  1.00 73.73           C  
ANISOU 4054  CD  LYS B 200     8119   7040  12855    -32    734   -721       C  
ATOM   4055  CE  LYS B 200     -16.966 -23.580  23.887  1.00 75.15           C  
ANISOU 4055  CE  LYS B 200     8425   7028  13099     23    845   -653       C  
ATOM   4056  NZ  LYS B 200     -16.613 -24.706  22.991  1.00 76.91           N  
ANISOU 4056  NZ  LYS B 200     8776   7107  13338     58    908   -750       N  
ATOM   4057  N   GLY B 201     -17.238 -17.261  24.585  1.00 65.59           N  
ANISOU 4057  N   GLY B 201     6647   6630  11641      4    453   -461       N  
ATOM   4058  CA  GLY B 201     -17.501 -15.890  24.110  1.00 64.44           C  
ANISOU 4058  CA  GLY B 201     6396   6646  11440    -19    361   -479       C  
ATOM   4059  C   GLY B 201     -17.983 -14.999  25.245  1.00 63.51           C  
ANISOU 4059  C   GLY B 201     6211   6590  11327    -53    333   -402       C  
ATOM   4060  O   GLY B 201     -17.599 -15.262  26.404  1.00 63.61           O  
ANISOU 4060  O   GLY B 201     6251   6557  11358    -15    378   -306       O  
ATOM   4061  N   VAL B 202     -18.812 -13.997  24.930  1.00 62.60           N  
ANISOU 4061  N   VAL B 202     6015   6577  11192   -116    266   -443       N  
ATOM   4062  CA  VAL B 202     -19.308 -12.951  25.879  1.00 61.85           C  
ANISOU 4062  CA  VAL B 202     5851   6557  11091   -142    233   -382       C  
ATOM   4063  C   VAL B 202     -19.955 -13.617  27.106  1.00 62.57           C  
ANISOU 4063  C   VAL B 202     5971   6557  11243   -192    296   -343       C  
ATOM   4064  O   VAL B 202     -19.636 -13.189  28.234  1.00 62.25           O  
ANISOU 4064  O   VAL B 202     5922   6539  11191   -156    304   -248       O  
ATOM   4065  CB  VAL B 202     -20.301 -11.989  25.196  1.00 61.35           C  
ANISOU 4065  CB  VAL B 202     5705   6596  11007   -205    162   -449       C  
ATOM   4066  CG1 VAL B 202     -20.703 -10.847  26.119  1.00 60.51           C  
ANISOU 4066  CG1 VAL B 202     5536   6564  10888   -212    131   -387       C  
ATOM   4067  CG2 VAL B 202     -19.767 -11.451  23.877  1.00 61.00           C  
ANISOU 4067  CG2 VAL B 202     5639   6634  10902   -162    107   -491       C  
ATOM   4068  N   GLU B 203     -20.829 -14.613  26.895  1.00 63.16           N  
ANISOU 4068  N   GLU B 203     6081   6538  11378   -276    338   -414       N  
ATOM   4069  CA  GLU B 203     -21.617 -15.315  27.954  1.00 63.96           C  
ANISOU 4069  CA  GLU B 203     6208   6547  11544   -345    405   -386       C  
ATOM   4070  C   GLU B 203     -20.698 -15.852  29.068  1.00 63.47           C  
ANISOU 4070  C   GLU B 203     6216   6410  11488   -264    470   -269       C  
ATOM   4071  O   GLU B 203     -21.219 -16.171  30.166  1.00 63.26           O  
ANISOU 4071  O   GLU B 203     6202   6334  11497   -301    521   -213       O  
ATOM   4072  CB  GLU B 203     -22.428 -16.468  27.346  1.00 65.59           C  
ANISOU 4072  CB  GLU B 203     6459   6646  11814   -446    445   -487       C  
ATOM   4073  CG  GLU B 203     -23.775 -16.059  26.766  1.00 65.69           C  
ANISOU 4073  CG  GLU B 203     6386   6733  11839   -561    396   -584       C  
ATOM   4074  CD  GLU B 203     -24.386 -17.064  25.796  1.00 67.41           C  
ANISOU 4074  CD  GLU B 203     6640   6873  12099   -659    410   -710       C  
ATOM   4075  OE1 GLU B 203     -25.473 -17.610  26.099  1.00 68.30           O  
ANISOU 4075  OE1 GLU B 203     6740   6936  12272   -778    444   -747       O  
ATOM   4076  OE2 GLU B 203     -23.782 -17.293  24.727  1.00 67.51           O  
ANISOU 4076  OE2 GLU B 203     6692   6879  12079   -619    389   -775       O  
ATOM   4077  N   ALA B 204     -19.391 -15.965  28.797  1.00 62.68           N  
ANISOU 4077  N   ALA B 204     6156   6309  11351   -154    470   -229       N  
ATOM   4078  CA  ALA B 204     -18.378 -16.569  29.692  1.00 62.34           C  
ANISOU 4078  CA  ALA B 204     6179   6202  11305    -58    529   -119       C  
ATOM   4079  C   ALA B 204     -17.947 -15.586  30.787  1.00 60.89           C  
ANISOU 4079  C   ALA B 204     5942   6123  11070     -9    498    -13       C  
ATOM   4080  O   ALA B 204     -17.536 -16.072  31.860  1.00 61.26           O  
ANISOU 4080  O   ALA B 204     6031   6122  11120     38    550     83       O  
ATOM   4081  CB  ALA B 204     -17.193 -17.018  28.875  1.00 63.03           C  
ANISOU 4081  CB  ALA B 204     6313   6267  11368     40    537   -126       C  
ATOM   4082  N   VAL B 205     -18.024 -14.273  30.528  1.00 59.18           N  
ANISOU 4082  N   VAL B 205     5642   6039  10805    -19    417    -31       N  
ATOM   4083  CA  VAL B 205     -17.451 -13.200  31.403  1.00 57.92           C  
ANISOU 4083  CA  VAL B 205     5433   5986  10585     28    376     54       C  
ATOM   4084  C   VAL B 205     -18.564 -12.353  32.043  1.00 57.28           C  
ANISOU 4084  C   VAL B 205     5298   5960  10506    -46    352     44       C  
ATOM   4085  O   VAL B 205     -18.219 -11.391  32.763  1.00 56.51           O  
ANISOU 4085  O   VAL B 205     5165   5946  10357    -17    316    100       O  
ATOM   4086  CB  VAL B 205     -16.468 -12.308  30.617  1.00 57.00           C  
ANISOU 4086  CB  VAL B 205     5273   5974  10408     87    307     51       C  
ATOM   4087  CG1 VAL B 205     -15.374 -13.124  29.948  1.00 57.42           C  
ANISOU 4087  CG1 VAL B 205     5373   5987  10457    169    335     59       C  
ATOM   4088  CG2 VAL B 205     -17.170 -11.426  29.593  1.00 56.59           C  
ANISOU 4088  CG2 VAL B 205     5163   5989  10347     28    244    -38       C  
ATOM   4089  N   MET B 206     -19.840 -12.675  31.803  1.00 57.42           N  
ANISOU 4089  N   MET B 206     5306   5935  10576   -138    371    -24       N  
ATOM   4090  CA  MET B 206     -20.996 -11.883  32.307  1.00 56.75           C  
ANISOU 4090  CA  MET B 206     5158   5908  10493   -205    353    -40       C  
ATOM   4091  C   MET B 206     -21.962 -12.796  33.068  1.00 58.01           C  
ANISOU 4091  C   MET B 206     5344   5982  10713   -274    430    -30       C  
ATOM   4092  O   MET B 206     -22.291 -13.888  32.560  1.00 59.02           O  
ANISOU 4092  O   MET B 206     5513   6012  10898   -322    474    -77       O  
ATOM   4093  CB  MET B 206     -21.735 -11.182  31.161  1.00 55.82           C  
ANISOU 4093  CB  MET B 206     4975   5858  10374   -254    290   -137       C  
ATOM   4094  CG  MET B 206     -21.096  -9.861  30.763  1.00 54.64           C  
ANISOU 4094  CG  MET B 206     4783   5817  10160   -199    213   -128       C  
ATOM   4095  SD  MET B 206     -21.731  -9.190  29.204  1.00 54.19           S  
ANISOU 4095  SD  MET B 206     4663   5832  10092   -233    142   -231       S  
ATOM   4096  CE  MET B 206     -23.371  -8.669  29.701  1.00 54.68           C  
ANISOU 4096  CE  MET B 206     4656   5936  10181   -308    141   -260       C  
ATOM   4097  N   TYR B 207     -22.375 -12.354  34.257  1.00 58.10           N  
ANISOU 4097  N   TYR B 207     5334   6030  10709   -281    448     28       N  
ATOM   4098  CA  TYR B 207     -23.437 -12.974  35.085  1.00 58.88           C  
ANISOU 4098  CA  TYR B 207     5437   6075  10856   -353    520     45       C  
ATOM   4099  C   TYR B 207     -24.379 -11.873  35.579  1.00 58.73           C  
ANISOU 4099  C   TYR B 207     5338   6159  10814   -385    493     35       C  
ATOM   4100  O   TYR B 207     -23.881 -10.805  36.010  1.00 58.15           O  
ANISOU 4100  O   TYR B 207     5246   6171  10677   -323    448     70       O  
ATOM   4101  CB  TYR B 207     -22.821 -13.736  36.259  1.00 59.71           C  
ANISOU 4101  CB  TYR B 207     5618   6112  10957   -304    591    154       C  
ATOM   4102  CG  TYR B 207     -23.800 -14.520  37.097  1.00 60.86           C  
ANISOU 4102  CG  TYR B 207     5782   6188  11154   -377    679    185       C  
ATOM   4103  CD1 TYR B 207     -24.404 -15.671  36.613  1.00 61.97           C  
ANISOU 4103  CD1 TYR B 207     5957   6211  11375   -459    736    140       C  
ATOM   4104  CD2 TYR B 207     -24.106 -14.126  38.390  1.00 60.89           C  
ANISOU 4104  CD2 TYR B 207     5771   6241  11122   -367    708    259       C  
ATOM   4105  CE1 TYR B 207     -25.293 -16.403  37.386  1.00 63.11           C  
ANISOU 4105  CE1 TYR B 207     6118   6289  11571   -535    822    174       C  
ATOM   4106  CE2 TYR B 207     -24.989 -14.848  39.176  1.00 62.31           C  
ANISOU 4106  CE2 TYR B 207     5965   6362  11345   -432    795    297       C  
ATOM   4107  CZ  TYR B 207     -25.587 -15.990  38.674  1.00 63.43           C  
ANISOU 4107  CZ  TYR B 207     6138   6386  11574   -520    853    257       C  
ATOM   4108  OH  TYR B 207     -26.454 -16.692  39.462  1.00 64.64           O  
ANISOU 4108  OH  TYR B 207     6304   6481  11773   -594    944    300       O  
ATOM   4109  N   MET B 208     -25.690 -12.134  35.494  1.00 58.97           N  
ANISOU 4109  N   MET B 208     5324   6184  10897   -479    522    -13       N  
ATOM   4110  CA  MET B 208     -26.776 -11.331  36.114  1.00 58.31           C  
ANISOU 4110  CA  MET B 208     5164   6186  10804   -512    523    -14       C  
ATOM   4111  C   MET B 208     -27.413 -12.162  37.237  1.00 58.51           C  
ANISOU 4111  C   MET B 208     5210   6153  10864   -562    620     43       C  
ATOM   4112  O   MET B 208     -28.259 -13.017  36.910  1.00 59.75           O  
ANISOU 4112  O   MET B 208     5354   6254  11092   -659    664      2       O  
ATOM   4113  CB  MET B 208     -27.836 -10.969  35.068  1.00 58.84           C  
ANISOU 4113  CB  MET B 208     5144   6312  10900   -580    479   -114       C  
ATOM   4114  CG  MET B 208     -28.884 -10.003  35.583  1.00 58.92           C  
ANISOU 4114  CG  MET B 208     5067   6426  10893   -592    472   -117       C  
ATOM   4115  SD  MET B 208     -28.241  -8.317  35.722  1.00 58.25           S  
ANISOU 4115  SD  MET B 208     4968   6442  10721   -483    395    -97       S  
ATOM   4116  CE  MET B 208     -28.970  -7.817  37.280  1.00 57.91           C  
ANISOU 4116  CE  MET B 208     4902   6448  10652   -472    453    -37       C  
ATOM   4117  N   GLY B 209     -27.011 -11.943  38.497  1.00 57.25           N  
ANISOU 4117  N   GLY B 209     5084   6009  10657   -505    653    135       N  
ATOM   4118  CA  GLY B 209     -27.488 -12.722  39.660  1.00 57.28           C  
ANISOU 4118  CA  GLY B 209     5118   5963  10683   -539    751    210       C  
ATOM   4119  C   GLY B 209     -26.988 -12.177  40.989  1.00 56.38           C  
ANISOU 4119  C   GLY B 209     5030   5902  10488   -459    766    302       C  
ATOM   4120  O   GLY B 209     -27.829 -11.760  41.792  1.00 56.47           O  
ANISOU 4120  O   GLY B 209     4999   5973  10481   -480    799    320       O  
ATOM   4121  N   THR B 210     -25.670 -12.194  41.223  1.00 55.86           N  
ANISOU 4121  N   THR B 210     5028   5823  10371   -371    742    358       N  
ATOM   4122  CA  THR B 210     -25.000 -11.654  42.444  1.00 55.25           C  
ANISOU 4122  CA  THR B 210     4980   5809  10204   -291    740    442       C  
ATOM   4123  C   THR B 210     -23.735 -10.883  42.047  1.00 53.65           C  
ANISOU 4123  C   THR B 210     4785   5659   9940   -212    650    435       C  
ATOM   4124  O   THR B 210     -23.365 -10.933  40.853  1.00 53.21           O  
ANISOU 4124  O   THR B 210     4722   5578   9916   -215    603    378       O  
ATOM   4125  CB  THR B 210     -24.641 -12.751  43.456  1.00 56.60           C  
ANISOU 4125  CB  THR B 210     5227   5908  10370   -266    826    553       C  
ATOM   4126  OG1 THR B 210     -24.085 -12.098  44.599  1.00 56.66           O  
ANISOU 4126  OG1 THR B 210     5248   6001  10277   -193    813    622       O  
ATOM   4127  CG2 THR B 210     -23.655 -13.772  42.930  1.00 56.91           C  
ANISOU 4127  CG2 THR B 210     5336   5846  10441   -229    836    583       C  
ATOM   4128  N   LEU B 211     -23.098 -10.213  43.015  1.00 52.60           N  
ANISOU 4128  N   LEU B 211     4666   5599   9718   -148    628    491       N  
ATOM   4129  CA  LEU B 211     -21.921  -9.325  42.791  1.00 51.62           C  
ANISOU 4129  CA  LEU B 211     4540   5543   9527    -85    540    486       C  
ATOM   4130  C   LEU B 211     -20.623 -10.001  43.274  1.00 51.79           C  
ANISOU 4130  C   LEU B 211     4619   5549   9509    -12    548    578       C  
ATOM   4131  O   LEU B 211     -19.616  -9.928  42.550  1.00 50.50           O  
ANISOU 4131  O   LEU B 211     4455   5391   9338     26    495    570       O  
ATOM   4132  CB  LEU B 211     -22.174  -7.994  43.510  1.00 51.00           C  
ANISOU 4132  CB  LEU B 211     4434   5566   9375    -75    503    470       C  
ATOM   4133  CG  LEU B 211     -23.428  -7.228  43.079  1.00 49.98           C  
ANISOU 4133  CG  LEU B 211     4247   5463   9278   -126    495    387       C  
ATOM   4134  CD1 LEU B 211     -23.524  -5.901  43.810  1.00 49.33           C  
ANISOU 4134  CD1 LEU B 211     4155   5470   9119   -100    461    373       C  
ATOM   4135  CD2 LEU B 211     -23.449  -7.005  41.576  1.00 49.34           C  
ANISOU 4135  CD2 LEU B 211     4129   5366   9251   -149    440    309       C  
ATOM   4136  N   SER B 212     -20.643 -10.638  44.448  1.00 52.80           N  
ANISOU 4136  N   SER B 212     4788   5664   9607     10    614    668       N  
ATOM   4137  CA  SER B 212     -19.473 -11.314  45.067  1.00 53.48           C  
ANISOU 4137  CA  SER B 212     4926   5746   9647     91    628    771       C  
ATOM   4138  C   SER B 212     -19.013 -12.473  44.179  1.00 54.87           C  
ANISOU 4138  C   SER B 212     5139   5812   9896    109    658    782       C  
ATOM   4139  O   SER B 212     -19.802 -13.428  44.003  1.00 55.74           O  
ANISOU 4139  O   SER B 212     5279   5813  10085     61    734    780       O  
ATOM   4140  CB  SER B 212     -19.795 -11.797  46.455  1.00 53.99           C  
ANISOU 4140  CB  SER B 212     5029   5815   9669    108    702    865       C  
ATOM   4141  OG  SER B 212     -18.691 -12.475  47.028  1.00 53.88           O  
ANISOU 4141  OG  SER B 212     5063   5802   9607    194    715    972       O  
ATOM   4142  N   TYR B 213     -17.788 -12.378  43.644  1.00 55.62           N  
ANISOU 4142  N   TYR B 213     5231   5934   9965    174    602    791       N  
ATOM   4143  CA  TYR B 213     -17.077 -13.472  42.931  1.00 56.48           C  
ANISOU 4143  CA  TYR B 213     5383   5952  10124    223    630    817       C  
ATOM   4144  C   TYR B 213     -16.764 -14.558  43.960  1.00 59.18           C  
ANISOU 4144  C   TYR B 213     5793   6241  10451    286    710    942       C  
ATOM   4145  O   TYR B 213     -17.212 -15.712  43.787  1.00 60.74           O  
ANISOU 4145  O   TYR B 213     6050   6303  10725    269    794    958       O  
ATOM   4146  CB  TYR B 213     -15.807 -12.948  42.251  1.00 55.55           C  
ANISOU 4146  CB  TYR B 213     5232   5907   9965    285    550    806       C  
ATOM   4147  CG  TYR B 213     -15.230 -13.816  41.156  1.00 55.24           C  
ANISOU 4147  CG  TYR B 213     5221   5784   9984    325    568    792       C  
ATOM   4148  CD1 TYR B 213     -16.042 -14.429  40.213  1.00 55.23           C  
ANISOU 4148  CD1 TYR B 213     5244   5668  10073    262    608    714       C  
ATOM   4149  CD2 TYR B 213     -13.860 -13.980  41.024  1.00 54.70           C  
ANISOU 4149  CD2 TYR B 213     5150   5760   9873    425    542    850       C  
ATOM   4150  CE1 TYR B 213     -15.514 -15.204  39.192  1.00 55.20           C  
ANISOU 4150  CE1 TYR B 213     5273   5584  10114    300    625    690       C  
ATOM   4151  CE2 TYR B 213     -13.316 -14.753  40.011  1.00 54.85           C  
ANISOU 4151  CE2 TYR B 213     5196   5704   9938    471    563    834       C  
ATOM   4152  CZ  TYR B 213     -14.145 -15.366  39.088  1.00 54.90           C  
ANISOU 4152  CZ  TYR B 213     5239   5588  10033    410    606    751       C  
ATOM   4153  OH  TYR B 213     -13.629 -16.132  38.084  1.00 54.65           O  
ANISOU 4153  OH  TYR B 213     5242   5478  10042    456    630    725       O  
ATOM   4154  N   GLU B 214     -16.061 -14.172  45.031  1.00 60.44           N  
ANISOU 4154  N   GLU B 214     5946   6506  10512    352    685   1026       N  
ATOM   4155  CA  GLU B 214     -15.641 -15.080  46.132  1.00 62.28           C  
ANISOU 4155  CA  GLU B 214     6237   6718  10706    431    750   1161       C  
ATOM   4156  C   GLU B 214     -16.771 -16.075  46.414  1.00 63.72           C  
ANISOU 4156  C   GLU B 214     6481   6764  10965    375    861   1184       C  
ATOM   4157  O   GLU B 214     -16.495 -17.288  46.446  1.00 64.50           O  
ANISOU 4157  O   GLU B 214     6651   6750  11106    425    936   1258       O  
ATOM   4158  CB  GLU B 214     -15.288 -14.279  47.386  1.00 62.50           C  
ANISOU 4158  CB  GLU B 214     6239   6895  10611    464    708   1219       C  
ATOM   4159  CG  GLU B 214     -14.232 -14.948  48.242  1.00 64.00           C  
ANISOU 4159  CG  GLU B 214     6464   7123  10730    582    727   1358       C  
ATOM   4160  CD  GLU B 214     -14.378 -14.701  49.733  1.00 65.18           C  
ANISOU 4160  CD  GLU B 214     6622   7366  10775    601    740   1438       C  
ATOM   4161  OE1 GLU B 214     -15.527 -14.666  50.211  1.00 65.48           O  
ANISOU 4161  OE1 GLU B 214     6678   7371  10830    532    794   1422       O  
ATOM   4162  OE2 GLU B 214     -13.344 -14.550  50.413  1.00 66.14           O  
ANISOU 4162  OE2 GLU B 214     6730   7603  10794    686    695   1517       O  
ATOM   4163  N   GLN B 215     -17.999 -15.572  46.566  1.00 64.75           N  
ANISOU 4163  N   GLN B 215     6582   6902  11116    275    874   1120       N  
ATOM   4164  CA  GLN B 215     -19.206 -16.379  46.889  1.00 66.35           C  
ANISOU 4164  CA  GLN B 215     6823   6995  11389    200    978   1136       C  
ATOM   4165  C   GLN B 215     -19.609 -17.219  45.677  1.00 67.41           C  
ANISOU 4165  C   GLN B 215     6985   6981  11646    141   1015   1066       C  
ATOM   4166  O   GLN B 215     -19.821 -18.428  45.862  1.00 69.54           O  
ANISOU 4166  O   GLN B 215     7330   7117  11975    136   1110   1127       O  
ATOM   4167  CB  GLN B 215     -20.373 -15.492  47.324  1.00 65.79           C  
ANISOU 4167  CB  GLN B 215     6696   6999  11301    114    974   1080       C  
ATOM   4168  CG  GLN B 215     -21.642 -16.285  47.606  1.00 66.75           C  
ANISOU 4168  CG  GLN B 215     6840   7021  11498     27   1081   1094       C  
ATOM   4169  CD  GLN B 215     -22.467 -15.691  48.720  1.00 67.10           C  
ANISOU 4169  CD  GLN B 215     6854   7158  11482     -1   1109   1119       C  
ATOM   4170  OE1 GLN B 215     -22.662 -14.480  48.797  1.00 66.53           O  
ANISOU 4170  OE1 GLN B 215     6720   7203  11355     -9   1043   1055       O  
ATOM   4171  NE2 GLN B 215     -22.964 -16.548  49.598  1.00 68.25           N  
ANISOU 4171  NE2 GLN B 215     7047   7245  11637    -15   1215   1215       N  
ATOM   4172  N   PHE B 216     -19.712 -16.604  44.495  1.00 67.38           N  
ANISOU 4172  N   PHE B 216     6928   6997  11676     96    944    945       N  
ATOM   4173  CA  PHE B 216     -20.131 -17.262  43.227  1.00 68.41           C  
ANISOU 4173  CA  PHE B 216     7074   7005  11911     31    964    855       C  
ATOM   4174  C   PHE B 216     -19.449 -18.629  43.102  1.00 69.77           C  
ANISOU 4174  C   PHE B 216     7345   7036  12126     95   1034    923       C  
ATOM   4175  O   PHE B 216     -20.085 -19.552  42.574  1.00 70.72           O  
ANISOU 4175  O   PHE B 216     7513   7015  12340     24   1099    883       O  
ATOM   4176  CB  PHE B 216     -19.803 -16.377  42.022  1.00 67.77           C  
ANISOU 4176  CB  PHE B 216     6931   6994  11825     27    863    745       C  
ATOM   4177  CG  PHE B 216     -20.302 -16.882  40.691  1.00 68.41           C  
ANISOU 4177  CG  PHE B 216     7018   6978  11996    -44    869    638       C  
ATOM   4178  CD1 PHE B 216     -21.427 -16.330  40.099  1.00 68.32           C  
ANISOU 4178  CD1 PHE B 216     6940   6996  12021   -150    841    532       C  
ATOM   4179  CD2 PHE B 216     -19.635 -17.892  40.014  1.00 69.51           C  
ANISOU 4179  CD2 PHE B 216     7227   7003  12178      0    901    640       C  
ATOM   4180  CE1 PHE B 216     -21.873 -16.781  38.866  1.00 68.97           C  
ANISOU 4180  CE1 PHE B 216     7024   7004  12176   -218    839    429       C  
ATOM   4181  CE2 PHE B 216     -20.088 -18.346  38.783  1.00 69.93           C  
ANISOU 4181  CE2 PHE B 216     7291   6972  12306    -69    904    531       C  
ATOM   4182  CZ  PHE B 216     -21.204 -17.787  38.209  1.00 69.60           C  
ANISOU 4182  CZ  PHE B 216     7180   6969  12294   -182    869    424       C  
ATOM   4183  N   LYS B 217     -18.197 -18.737  43.561  1.00 70.66           N  
ANISOU 4183  N   LYS B 217     7485   7189  12172    223   1021   1019       N  
ATOM   4184  CA  LYS B 217     -17.370 -19.975  43.509  1.00 72.98           C  
ANISOU 4184  CA  LYS B 217     7872   7362  12493    318   1085   1101       C  
ATOM   4185  C   LYS B 217     -17.885 -21.011  44.518  1.00 75.95           C  
ANISOU 4185  C   LYS B 217     8332   7626  12899    310   1202   1208       C  
ATOM   4186  O   LYS B 217     -17.706 -22.220  44.250  1.00 78.27           O  
ANISOU 4186  O   LYS B 217     8721   7758  13260    339   1282   1243       O  
ATOM   4187  CB  LYS B 217     -15.901 -19.656  43.807  1.00 72.42           C  
ANISOU 4187  CB  LYS B 217     7785   7402  12329    463   1030   1181       C  
ATOM   4188  CG  LYS B 217     -15.188 -18.811  42.761  1.00 70.64           C  
ANISOU 4188  CG  LYS B 217     7489   7271  12080    484    928   1094       C  
ATOM   4189  CD  LYS B 217     -13.930 -18.152  43.285  1.00 70.02           C  
ANISOU 4189  CD  LYS B 217     7360   7349  11893    592    858   1169       C  
ATOM   4190  CE  LYS B 217     -13.149 -17.437  42.204  1.00 68.86           C  
ANISOU 4190  CE  LYS B 217     7149   7284  11729    614    770   1094       C  
ATOM   4191  NZ  LYS B 217     -12.162 -16.494  42.775  1.00 68.18           N  
ANISOU 4191  NZ  LYS B 217     6992   7377  11536    675    687   1146       N  
ATOM   4192  N   LYS B 218     -18.477 -20.561  45.633  1.00 76.52           N  
ANISOU 4192  N   LYS B 218     8376   7778  12920    277   1215   1261       N  
ATOM   4193  CA  LYS B 218     -18.902 -21.420  46.774  1.00 77.99           C  
ANISOU 4193  CA  LYS B 218     8634   7887  13110    280   1325   1386       C  
ATOM   4194  C   LYS B 218     -20.340 -21.895  46.544  1.00 78.75           C  
ANISOU 4194  C   LYS B 218     8743   7866  13309    126   1401   1324       C  
ATOM   4195  O   LYS B 218     -20.522 -23.117  46.387  1.00 80.13           O  
ANISOU 4195  O   LYS B 218     9011   7863  13569    106   1496   1358       O  
ATOM   4196  CB  LYS B 218     -18.743 -20.672  48.102  1.00 78.14           C  
ANISOU 4196  CB  LYS B 218     8614   8068  13006    330   1301   1474       C  
ATOM   4197  CG  LYS B 218     -17.426 -19.922  48.238  1.00 78.05           C  
ANISOU 4197  CG  LYS B 218     8558   8208  12887    450   1201   1503       C  
ATOM   4198  CD  LYS B 218     -16.994 -19.613  49.655  1.00 79.18           C  
ANISOU 4198  CD  LYS B 218     8698   8481  12904    529   1196   1624       C  
ATOM   4199  CE  LYS B 218     -15.588 -19.045  49.697  1.00 79.71           C  
ANISOU 4199  CE  LYS B 218     8724   8687  12874    645   1098   1654       C  
ATOM   4200  NZ  LYS B 218     -15.313 -18.294  50.946  1.00 80.15           N  
ANISOU 4200  NZ  LYS B 218     8745   8915  12793    685   1056   1719       N  
ATOM   4201  N   GLY B 219     -21.314 -20.976  46.515  1.00 78.01           N  
ANISOU 4201  N   GLY B 219     8560   7867  13212     22   1362   1238       N  
ATOM   4202  CA  GLY B 219     -22.744 -21.326  46.413  1.00 78.95           C  
ANISOU 4202  CA  GLY B 219     8667   7909  13418   -128   1430   1186       C  
ATOM   4203  C   GLY B 219     -23.663 -20.119  46.314  1.00 78.41           C  
ANISOU 4203  C   GLY B 219     8482   7980  13329   -212   1368   1089       C  
ATOM   4204  O   GLY B 219     -23.535 -19.204  47.146  1.00 77.10           O  
ANISOU 4204  O   GLY B 219     8271   7958  13065   -164   1330   1126       O  
ATOM   4205  N   VAL B 220     -24.562 -20.141  45.325  1.00 79.86           N  
ANISOU 4205  N   VAL B 220     8622   8121  13600   -333   1359    966       N  
ATOM   4206  CA  VAL B 220     -25.754 -19.251  45.171  1.00 80.59           C  
ANISOU 4206  CA  VAL B 220     8604   8316  13700   -436   1328    875       C  
ATOM   4207  C   VAL B 220     -26.981 -20.095  45.557  1.00 82.22           C  
ANISOU 4207  C   VAL B 220     8819   8433  13986   -561   1439    898       C  
ATOM   4208  O   VAL B 220     -26.772 -21.250  45.969  1.00 83.92           O  
ANISOU 4208  O   VAL B 220     9133   8511  14240   -556   1533    987       O  
ATOM   4209  CB  VAL B 220     -25.818 -18.701  43.726  1.00 80.20           C  
ANISOU 4209  CB  VAL B 220     8494   8293  13685   -475   1233    728       C  
ATOM   4210  CG1 VAL B 220     -27.054 -17.855  43.438  1.00 80.14           C  
ANISOU 4210  CG1 VAL B 220     8371   8385  13692   -573   1199    633       C  
ATOM   4211  CG2 VAL B 220     -24.564 -17.916  43.370  1.00 78.58           C  
ANISOU 4211  CG2 VAL B 220     8283   8169  13403   -355   1132    718       C  
ATOM   4212  N   GLN B 221     -28.200 -19.548  45.483  1.00 82.91           N  
ANISOU 4212  N   GLN B 221     8806   8598  14095   -665   1436    829       N  
ATOM   4213  CA  GLN B 221     -29.470 -20.329  45.524  1.00 84.37           C  
ANISOU 4213  CA  GLN B 221     8975   8706  14375   -815   1530    819       C  
ATOM   4214  C   GLN B 221     -30.373 -19.900  44.356  1.00 84.81           C  
ANISOU 4214  C   GLN B 221     8925   8808  14491   -926   1469    667       C  
ATOM   4215  O   GLN B 221     -30.408 -18.692  44.055  1.00 83.26           O  
ANISOU 4215  O   GLN B 221     8641   8754  14237   -886   1375    603       O  
ATOM   4216  CB  GLN B 221     -30.150 -20.156  46.886  1.00 84.57           C  
ANISOU 4216  CB  GLN B 221     8971   8804  14355   -825   1608    917       C  
ATOM   4217  CG  GLN B 221     -30.773 -18.782  47.115  1.00 83.63           C  
ANISOU 4217  CG  GLN B 221     8729   8875  14170   -818   1549    866       C  
ATOM   4218  CD  GLN B 221     -32.237 -18.707  46.743  1.00 83.80           C  
ANISOU 4218  CD  GLN B 221     8640   8934  14262   -961   1575    788       C  
ATOM   4219  OE1 GLN B 221     -33.034 -19.590  47.061  1.00 84.40           O  
ANISOU 4219  OE1 GLN B 221     8722   8937  14408  -1068   1677    827       O  
ATOM   4220  NE2 GLN B 221     -32.612 -17.630  46.072  1.00 82.41           N  
ANISOU 4220  NE2 GLN B 221     8361   8881  14070   -962   1483    681       N  
ATOM   4221  N   ILE B 222     -31.063 -20.857  43.721  1.00 87.79           N  
ANISOU 4221  N   ILE B 222     9314   9067  14975  -1061   1518    613       N  
ATOM   4222  CA  ILE B 222     -32.055 -20.623  42.621  1.00 89.47           C  
ANISOU 4222  CA  ILE B 222     9421   9322  15249  -1188   1468    470       C  
ATOM   4223  C   ILE B 222     -33.156 -21.686  42.698  1.00 91.88           C  
ANISOU 4223  C   ILE B 222     9725   9526  15659  -1360   1570    467       C  
ATOM   4224  O   ILE B 222     -33.067 -22.611  43.505  1.00 92.79           O  
ANISOU 4224  O   ILE B 222     9932   9521  15802  -1374   1678    573       O  
ATOM   4225  CB  ILE B 222     -31.358 -20.611  41.242  1.00 89.16           C  
ANISOU 4225  CB  ILE B 222     9409   9244  15224  -1163   1376    361       C  
ATOM   4226  CG1 ILE B 222     -30.487 -21.853  41.029  1.00 90.65           C  
ANISOU 4226  CG1 ILE B 222     9748   9236  15459  -1139   1430    394       C  
ATOM   4227  CG2 ILE B 222     -30.565 -19.325  41.039  1.00 87.27           C  
ANISOU 4227  CG2 ILE B 222     9129   9142  14887  -1026   1266    343       C  
ATOM   4228  CD1 ILE B 222     -29.903 -21.965  39.637  1.00 90.60           C  
ANISOU 4228  CD1 ILE B 222     9769   9183  15470  -1126   1354    279       C  
ATOM   4229  N   PRO B 223     -34.244 -21.577  41.894  1.00 92.41           N  
ANISOU 4229  N   PRO B 223     9683   9645  15784  -1498   1541    350       N  
ATOM   4230  CA  PRO B 223     -35.191 -22.682  41.719  1.00 94.55           C  
ANISOU 4230  CA  PRO B 223     9955   9804  16164  -1681   1625    323       C  
ATOM   4231  C   PRO B 223     -34.558 -23.886  41.001  1.00 95.32           C  
ANISOU 4231  C   PRO B 223    10195   9688  16333  -1716   1650    287       C  
ATOM   4232  O   PRO B 223     -35.312 -24.754  40.589  1.00 97.06           O  
ANISOU 4232  O   PRO B 223    10419   9810  16647  -1881   1699    230       O  
ATOM   4233  CB  PRO B 223     -36.322 -22.087  40.861  1.00 94.60           C  
ANISOU 4233  CB  PRO B 223     9798   9950  16195  -1794   1554    191       C  
ATOM   4234  CG  PRO B 223     -36.153 -20.584  40.990  1.00 92.48           C  
ANISOU 4234  CG  PRO B 223     9435   9879  15823  -1660   1462    189       C  
ATOM   4235  CD  PRO B 223     -34.666 -20.369  41.169  1.00 90.95           C  
ANISOU 4235  CD  PRO B 223     9360   9636  15558  -1487   1428    246       C  
ATOM   4236  N   GLN B 229     -35.020 -25.873  45.803  1.00 76.59           N  
ANISOU 4236  N   GLN B 229     8035   7101  13962  -1708   2107    850       N  
ATOM   4237  CA  GLN B 229     -33.944 -24.939  45.364  1.00 74.69           C  
ANISOU 4237  CA  GLN B 229     7794   6953  13629  -1537   1980    807       C  
ATOM   4238  C   GLN B 229     -32.792 -25.738  44.733  1.00 74.68           C  
ANISOU 4238  C   GLN B 229     7944   6772  13657  -1468   1971    799       C  
ATOM   4239  O   GLN B 229     -32.971 -26.955  44.509  1.00 76.26           O  
ANISOU 4239  O   GLN B 229     8241   6777  13956  -1568   2056    803       O  
ATOM   4240  CB  GLN B 229     -33.459 -24.095  46.547  1.00 73.80           C  
ANISOU 4240  CB  GLN B 229     7668   6978  13391  -1381   1975    924       C  
ATOM   4241  CG  GLN B 229     -32.662 -24.888  47.577  1.00 74.43           C  
ANISOU 4241  CG  GLN B 229     7893   6942  13443  -1287   2070   1091       C  
ATOM   4242  CD  GLN B 229     -32.852 -24.375  48.984  1.00 74.18           C  
ANISOU 4242  CD  GLN B 229     7830   7039  13316  -1221   2120   1217       C  
ATOM   4243  OE1 GLN B 229     -33.971 -24.140  49.432  1.00 74.20           O  
ANISOU 4243  OE1 GLN B 229     7737   7127  13328  -1317   2169   1221       O  
ATOM   4244  NE2 GLN B 229     -31.753 -24.214  49.703  1.00 73.42           N  
ANISOU 4244  NE2 GLN B 229     7810   6963  13120  -1054   2109   1322       N  
ATOM   4245  N   ALA B 230     -31.665 -25.073  44.445  1.00 72.81           N  
ANISOU 4245  N   ALA B 230     7726   6598  13339  -1307   1875    787       N  
ATOM   4246  CA  ALA B 230     -30.422 -25.679  43.904  1.00 72.43           C  
ANISOU 4246  CA  ALA B 230     7810   6411  13298  -1204   1860    790       C  
ATOM   4247  C   ALA B 230     -29.209 -24.797  44.247  1.00 70.58           C  
ANISOU 4247  C   ALA B 230     7577   6296  12942  -1005   1780    847       C  
ATOM   4248  O   ALA B 230     -29.401 -23.600  44.547  1.00 69.36           O  
ANISOU 4248  O   ALA B 230     7312   6331  12709   -970   1711    834       O  
ATOM   4249  CB  ALA B 230     -30.562 -25.885  42.415  1.00 72.24           C  
ANISOU 4249  CB  ALA B 230     7777   6328  13342  -1288   1798    624       C  
ATOM   4250  N   THR B 231     -28.002 -25.374  44.204  1.00 70.24           N  
ANISOU 4250  N   THR B 231     7654   6146  12885   -881   1792    907       N  
ATOM   4251  CA  THR B 231     -26.712 -24.707  44.531  1.00 68.73           C  
ANISOU 4251  CA  THR B 231     7474   6056  12583   -692   1723    972       C  
ATOM   4252  C   THR B 231     -25.924 -24.462  43.242  1.00 67.40           C  
ANISOU 4252  C   THR B 231     7306   5887  12415   -638   1626    860       C  
ATOM   4253  O   THR B 231     -25.403 -25.446  42.694  1.00 68.57           O  
ANISOU 4253  O   THR B 231     7562   5871  12620   -617   1666    853       O  
ATOM   4254  CB  THR B 231     -25.883 -25.555  45.506  1.00 69.73           C  
ANISOU 4254  CB  THR B 231     7727   6082  12685   -575   1811   1141       C  
ATOM   4255  OG1 THR B 231     -26.661 -25.762  46.684  1.00 71.07           O  
ANISOU 4255  OG1 THR B 231     7893   6259  12848   -630   1904   1246       O  
ATOM   4256  CG2 THR B 231     -24.565 -24.914  45.882  1.00 68.54           C  
ANISOU 4256  CG2 THR B 231     7577   6046  12417   -389   1739   1211       C  
ATOM   4257  N   LYS B 232     -25.838 -23.207  42.786  1.00 65.22           N  
ANISOU 4257  N   LYS B 232     6920   5783  12076   -614   1509    779       N  
ATOM   4258  CA  LYS B 232     -25.008 -22.809  41.615  1.00 64.09           C  
ANISOU 4258  CA  LYS B 232     6767   5669  11915   -549   1411    684       C  
ATOM   4259  C   LYS B 232     -23.585 -22.508  42.096  1.00 63.19           C  
ANISOU 4259  C   LYS B 232     6688   5611  11708   -370   1378    783       C  
ATOM   4260  O   LYS B 232     -23.446 -21.856  43.147  1.00 62.54           O  
ANISOU 4260  O   LYS B 232     6570   5647  11546   -313   1367    870       O  
ATOM   4261  CB  LYS B 232     -25.600 -21.598  40.885  1.00 62.71           C  
ANISOU 4261  CB  LYS B 232     6459   5648  11717   -608   1306    559       C  
ATOM   4262  CG  LYS B 232     -25.020 -21.348  39.500  1.00 61.73           C  
ANISOU 4262  CG  LYS B 232     6325   5533  11594   -581   1220    446       C  
ATOM   4263  CD  LYS B 232     -25.848 -20.420  38.636  1.00 60.90           C  
ANISOU 4263  CD  LYS B 232     6102   5545  11490   -667   1135    315       C  
ATOM   4264  CE  LYS B 232     -26.001 -20.918  37.213  1.00 61.38           C  
ANISOU 4264  CE  LYS B 232     6179   5531  11611   -735   1109    184       C  
ATOM   4265  NZ  LYS B 232     -26.099 -19.805  36.240  1.00 60.07           N  
ANISOU 4265  NZ  LYS B 232     5913   5507  11403   -735    996     80       N  
ATOM   4266  N   TYR B 233     -22.573 -22.981  41.363  1.00 63.37           N  
ANISOU 4266  N   TYR B 233     6778   5560  11740   -285   1363    769       N  
ATOM   4267  CA  TYR B 233     -21.136 -22.714  41.637  1.00 62.73           C  
ANISOU 4267  CA  TYR B 233     6717   5543  11574   -113   1323    852       C  
ATOM   4268  C   TYR B 233     -20.311 -22.822  40.350  1.00 62.22           C  
ANISOU 4268  C   TYR B 233     6670   5448  11521    -57   1272    769       C  
ATOM   4269  O   TYR B 233     -20.636 -23.652  39.474  1.00 62.83           O  
ANISOU 4269  O   TYR B 233     6807   5381  11681   -121   1312    688       O  
ATOM   4270  CB  TYR B 233     -20.585 -23.653  42.713  1.00 64.09           C  
ANISOU 4270  CB  TYR B 233     6991   5624  11735    -19   1418   1014       C  
ATOM   4271  CG  TYR B 233     -20.665 -25.127  42.406  1.00 66.10           C  
ANISOU 4271  CG  TYR B 233     7376   5650  12088    -39   1526   1028       C  
ATOM   4272  CD1 TYR B 233     -21.650 -25.915  42.978  1.00 67.77           C  
ANISOU 4272  CD1 TYR B 233     7642   5738  12370   -144   1632   1068       C  
ATOM   4273  CD2 TYR B 233     -19.740 -25.747  41.579  1.00 66.71           C  
ANISOU 4273  CD2 TYR B 233     7527   5629  12188     50   1530   1006       C  
ATOM   4274  CE1 TYR B 233     -21.730 -27.276  42.726  1.00 69.40           C  
ANISOU 4274  CE1 TYR B 233     7979   5717  12670   -170   1736   1082       C  
ATOM   4275  CE2 TYR B 233     -19.801 -27.109  41.320  1.00 68.53           C  
ANISOU 4275  CE2 TYR B 233     7892   5636  12510     37   1635   1017       C  
ATOM   4276  CZ  TYR B 233     -20.800 -27.876  41.896  1.00 69.79           C  
ANISOU 4276  CZ  TYR B 233     8111   5662  12742    -76   1738   1054       C  
ATOM   4277  OH  TYR B 233     -20.886 -29.214  41.644  1.00 71.64           O  
ANISOU 4277  OH  TYR B 233     8486   5660  13072   -100   1845   1061       O  
ATOM   4278  N   LEU B 234     -19.265 -21.990  40.271  1.00 61.10           N  
ANISOU 4278  N   LEU B 234     6479   5443  11293     55   1188    788       N  
ATOM   4279  CA  LEU B 234     -18.227 -21.984  39.206  1.00 60.15           C  
ANISOU 4279  CA  LEU B 234     6366   5326  11159    141   1139    739       C  
ATOM   4280  C   LEU B 234     -17.363 -23.238  39.353  1.00 61.03           C  
ANISOU 4280  C   LEU B 234     6597   5294  11295    254   1223    828       C  
ATOM   4281  O   LEU B 234     -16.914 -23.510  40.483  1.00 61.10           O  
ANISOU 4281  O   LEU B 234     6640   5311  11265    340   1266    968       O  
ATOM   4282  CB  LEU B 234     -17.384 -20.714  39.365  1.00 58.75           C  
ANISOU 4282  CB  LEU B 234     6095   5345  10879    222   1036    762       C  
ATOM   4283  CG  LEU B 234     -16.329 -20.453  38.290  1.00 58.20           C  
ANISOU 4283  CG  LEU B 234     6006   5322  10783    304    974    713       C  
ATOM   4284  CD1 LEU B 234     -16.942 -20.433  36.897  1.00 57.94           C  
ANISOU 4284  CD1 LEU B 234     5960   5245  10807    210    948    561       C  
ATOM   4285  CD2 LEU B 234     -15.606 -19.148  38.572  1.00 56.93           C  
ANISOU 4285  CD2 LEU B 234     5749   5356  10525    359    876    742       C  
ATOM   4286  N   VAL B 235     -17.154 -23.972  38.257  1.00 61.55           N  
ANISOU 4286  N   VAL B 235     6728   5237  11419    260   1248    749       N  
ATOM   4287  CA  VAL B 235     -16.173 -25.095  38.187  1.00 63.19           C  
ANISOU 4287  CA  VAL B 235     7051   5312  11645    394   1322    821       C  
ATOM   4288  C   VAL B 235     -14.851 -24.536  37.647  1.00 62.56           C  
ANISOU 4288  C   VAL B 235     6920   5358  11491    533   1248    826       C  
ATOM   4289  O   VAL B 235     -13.865 -24.511  38.410  1.00 62.93           O  
ANISOU 4289  O   VAL B 235     6962   5473  11473    671   1249    956       O  
ATOM   4290  CB  VAL B 235     -16.686 -26.268  37.331  1.00 64.35           C  
ANISOU 4290  CB  VAL B 235     7311   5241  11897    323   1401    728       C  
ATOM   4291  CG1 VAL B 235     -15.820 -27.505  37.511  1.00 65.65           C  
ANISOU 4291  CG1 VAL B 235     7612   5242  12087    463   1499    823       C  
ATOM   4292  CG2 VAL B 235     -18.142 -26.587  37.637  1.00 65.15           C  
ANISOU 4292  CG2 VAL B 235     7428   5250  12074    144   1451    688       C  
ATOM   4293  N   GLN B 236     -14.859 -24.066  36.395  1.00 61.56           N  
ANISOU 4293  N   GLN B 236     6746   5274  11366    493   1183    692       N  
ATOM   4294  CA  GLN B 236     -13.662 -23.625  35.632  1.00 60.54           C  
ANISOU 4294  CA  GLN B 236     6572   5249  11178    610   1123    677       C  
ATOM   4295  C   GLN B 236     -13.981 -22.283  34.954  1.00 58.79           C  
ANISOU 4295  C   GLN B 236     6228   5191  10917    526   1010    574       C  
ATOM   4296  O   GLN B 236     -15.041 -22.208  34.297  1.00 58.94           O  
ANISOU 4296  O   GLN B 236     6241   5169  10985    392    999    454       O  
ATOM   4297  CB  GLN B 236     -13.305 -24.741  34.645  1.00 61.57           C  
ANISOU 4297  CB  GLN B 236     6811   5217  11364    662   1189    619       C  
ATOM   4298  CG  GLN B 236     -12.099 -24.465  33.757  1.00 61.26           C  
ANISOU 4298  CG  GLN B 236     6737   5266  11271    787   1145    599       C  
ATOM   4299  CD  GLN B 236     -12.110 -25.346  32.530  1.00 62.16           C  
ANISOU 4299  CD  GLN B 236     6946   5232  11439    790   1195    486       C  
ATOM   4300  OE1 GLN B 236     -12.528 -26.500  32.575  1.00 63.47           O  
ANISOU 4300  OE1 GLN B 236     7237   5196  11680    770   1290    474       O  
ATOM   4301  NE2 GLN B 236     -11.660 -24.802  31.411  1.00 61.45           N  
ANISOU 4301  NE2 GLN B 236     6799   5237  11309    812   1134    398       N  
ATOM   4302  N   GLN B 237     -13.117 -21.269  35.127  1.00 57.33           N  
ANISOU 4302  N   GLN B 237     5950   5185  10647    599    931    622       N  
ATOM   4303  CA  GLN B 237     -13.211 -19.927  34.477  1.00 55.51           C  
ANISOU 4303  CA  GLN B 237     5607   5111  10370    542    825    541       C  
ATOM   4304  C   GLN B 237     -11.898 -19.600  33.758  1.00 55.22           C  
ANISOU 4304  C   GLN B 237     5530   5170  10278    656    781    549       C  
ATOM   4305  O   GLN B 237     -10.847 -19.566  34.436  1.00 55.32           O  
ANISOU 4305  O   GLN B 237     5524   5254  10238    770    780    663       O  
ATOM   4306  CB  GLN B 237     -13.502 -18.839  35.517  1.00 54.40           C  
ANISOU 4306  CB  GLN B 237     5386   5105  10178    500    769    593       C  
ATOM   4307  CG  GLN B 237     -13.679 -17.443  34.932  1.00 52.69           C  
ANISOU 4307  CG  GLN B 237     5066   5031   9920    439    667    516       C  
ATOM   4308  CD  GLN B 237     -14.939 -17.325  34.113  1.00 52.45           C  
ANISOU 4308  CD  GLN B 237     5028   4954   9944    311    657    388       C  
ATOM   4309  OE1 GLN B 237     -16.044 -17.572  34.598  1.00 52.79           O  
ANISOU 4309  OE1 GLN B 237     5088   4936  10032    221    693    373       O  
ATOM   4310  NE2 GLN B 237     -14.781 -16.947  32.857  1.00 51.80           N  
ANISOU 4310  NE2 GLN B 237     4915   4911   9855    302    609    297       N  
ATOM   4311  N   GLU B 238     -11.962 -19.337  32.449  1.00 54.88           N  
ANISOU 4311  N   GLU B 238     5467   5142  10241    624    746    436       N  
ATOM   4312  CA  GLU B 238     -10.809 -18.861  31.635  1.00 54.80           C  
ANISOU 4312  CA  GLU B 238     5403   5243  10174    714    699    432       C  
ATOM   4313  C   GLU B 238     -11.168 -17.526  30.979  1.00 53.10           C  
ANISOU 4313  C   GLU B 238     5091   5159   9924    627    604    354       C  
ATOM   4314  O   GLU B 238     -11.794 -17.538  29.902  1.00 52.67           O  
ANISOU 4314  O   GLU B 238     5046   5070   9895    560    593    238       O  
ATOM   4315  CB  GLU B 238     -10.419 -19.879  30.562  1.00 56.32           C  
ANISOU 4315  CB  GLU B 238     5674   5326  10397    779    758    374       C  
ATOM   4316  CG  GLU B 238      -9.467 -20.947  31.052  1.00 57.94           C  
ANISOU 4316  CG  GLU B 238     5952   5454  10607    927    838    478       C  
ATOM   4317  CD  GLU B 238      -9.441 -22.167  30.154  1.00 59.71           C  
ANISOU 4317  CD  GLU B 238     6292   5512  10884    969    919    407       C  
ATOM   4318  OE1 GLU B 238      -9.129 -22.013  28.957  1.00 59.95           O  
ANISOU 4318  OE1 GLU B 238     6306   5577  10894    986    898    320       O  
ATOM   4319  OE2 GLU B 238      -9.767 -23.263  30.646  1.00 61.62           O  
ANISOU 4319  OE2 GLU B 238     6642   5584  11184    980   1006    435       O  
ATOM   4320  N   SER B 239     -10.779 -16.421  31.615  1.00 51.97           N  
ANISOU 4320  N   SER B 239     4862   5160   9721    630    538    416       N  
ATOM   4321  CA  SER B 239     -10.875 -15.049  31.056  1.00 50.73           C  
ANISOU 4321  CA  SER B 239     4614   5136   9523    570    448    364       C  
ATOM   4322  C   SER B 239      -9.976 -14.114  31.858  1.00 50.14           C  
ANISOU 4322  C   SER B 239     4466   5205   9380    612    393    459       C  
ATOM   4323  O   SER B 239      -9.673 -14.384  33.020  1.00 49.97           O  
ANISOU 4323  O   SER B 239     4455   5186   9342    654    415    552       O  
ATOM   4324  CB  SER B 239     -12.309 -14.567  31.035  1.00 50.20           C  
ANISOU 4324  CB  SER B 239     4536   5047   9489    439    424    284       C  
ATOM   4325  OG  SER B 239     -12.815 -14.397  32.353  1.00 49.92           O  
ANISOU 4325  OG  SER B 239     4500   5010   9455    405    433    344       O  
ATOM   4326  N   PRO B 240      -9.523 -12.996  31.249  1.00 49.54           N  
ANISOU 4326  N   PRO B 240     4312   5252   9257    598    321    437       N  
ATOM   4327  CA  PRO B 240      -8.754 -11.977  31.965  1.00 49.43           C  
ANISOU 4327  CA  PRO B 240     4225   5376   9179    610    261    511       C  
ATOM   4328  C   PRO B 240      -9.580 -11.225  33.023  1.00 49.12           C  
ANISOU 4328  C   PRO B 240     4174   5357   9132    528    230    517       C  
ATOM   4329  O   PRO B 240      -9.027 -10.849  34.049  1.00 49.08           O  
ANISOU 4329  O   PRO B 240     4141   5427   9080    550    207    594       O  
ATOM   4330  CB  PRO B 240      -8.282 -11.028  30.854  1.00 48.88           C  
ANISOU 4330  CB  PRO B 240     4090   5403   9076    595    203    468       C  
ATOM   4331  CG  PRO B 240      -9.279 -11.228  29.732  1.00 48.66           C  
ANISOU 4331  CG  PRO B 240     4097   5298   9094    538    215    357       C  
ATOM   4332  CD  PRO B 240      -9.705 -12.677  29.826  1.00 49.27           C  
ANISOU 4332  CD  PRO B 240     4261   5231   9227    567    296    342       C  
ATOM   4333  N   PHE B 241     -10.873 -11.020  32.756  1.00 49.14           N  
ANISOU 4333  N   PHE B 241     4194   5301   9176    438    230    435       N  
ATOM   4334  CA  PHE B 241     -11.834 -10.372  33.690  1.00 49.15           C  
ANISOU 4334  CA  PHE B 241     4188   5309   9175    362    212    430       C  
ATOM   4335  C   PHE B 241     -13.112 -11.209  33.811  1.00 49.45           C  
ANISOU 4335  C   PHE B 241     4281   5226   9281    310    272    387       C  
ATOM   4336  O   PHE B 241     -13.453 -11.963  32.884  1.00 49.62           O  
ANISOU 4336  O   PHE B 241     4335   5165   9350    301    305    326       O  
ATOM   4337  CB  PHE B 241     -12.193  -8.957  33.228  1.00 48.32           C  
ANISOU 4337  CB  PHE B 241     4027   5283   9048    296    139    374       C  
ATOM   4338  CG  PHE B 241     -13.049  -8.891  31.986  1.00 48.17           C  
ANISOU 4338  CG  PHE B 241     4006   5225   9069    245    133    275       C  
ATOM   4339  CD1 PHE B 241     -14.404  -8.605  32.067  1.00 48.06           C  
ANISOU 4339  CD1 PHE B 241     3992   5180   9088    168    132    216       C  
ATOM   4340  CD2 PHE B 241     -12.495  -9.109  30.734  1.00 48.30           C  
ANISOU 4340  CD2 PHE B 241     4017   5249   9084    277    127    242       C  
ATOM   4341  CE1 PHE B 241     -15.182  -8.536  30.922  1.00 48.01           C  
ANISOU 4341  CE1 PHE B 241     3974   5155   9110    124    119    127       C  
ATOM   4342  CE2 PHE B 241     -13.275  -9.048  29.591  1.00 48.18           C  
ANISOU 4342  CE2 PHE B 241     3999   5211   9095    232    116    150       C  
ATOM   4343  CZ  PHE B 241     -14.617  -8.758  29.686  1.00 48.13           C  
ANISOU 4343  CZ  PHE B 241     3988   5179   9119    154    109     93       C  
ATOM   4344  N   VAL B 242     -13.799 -11.060  34.939  1.00 49.27           N  
ANISOU 4344  N   VAL B 242     4265   5196   9256    272    287    415       N  
ATOM   4345  CA  VAL B 242     -15.221 -11.470  35.095  1.00 49.85           C  
ANISOU 4345  CA  VAL B 242     4366   5185   9389    194    331    366       C  
ATOM   4346  C   VAL B 242     -16.022 -10.216  35.472  1.00 49.18           C  
ANISOU 4346  C   VAL B 242     4230   5174   9281    129    283    334       C  
ATOM   4347  O   VAL B 242     -15.462  -9.349  36.177  1.00 49.18           O  
ANISOU 4347  O   VAL B 242     4204   5261   9219    152    241    380       O  
ATOM   4348  CB  VAL B 242     -15.368 -12.618  36.114  1.00 50.97           C  
ANISOU 4348  CB  VAL B 242     4571   5238   9555    216    413    438       C  
ATOM   4349  CG1 VAL B 242     -14.606 -13.858  35.669  1.00 51.83           C  
ANISOU 4349  CG1 VAL B 242     4740   5259   9692    289    467    466       C  
ATOM   4350  CG2 VAL B 242     -14.943 -12.212  37.513  1.00 51.02           C  
ANISOU 4350  CG2 VAL B 242     4570   5316   9498    253    406    533       C  
ATOM   4351  N   MET B 243     -17.251 -10.102  34.958  1.00 48.59           N  
ANISOU 4351  N   MET B 243     4140   5069   9251     53    285    254       N  
ATOM   4352  CA  MET B 243     -18.227  -9.030  35.284  1.00 47.75           C  
ANISOU 4352  CA  MET B 243     3987   5019   9133     -2    254    219       C  
ATOM   4353  C   MET B 243     -19.349  -9.650  36.118  1.00 48.85           C  
ANISOU 4353  C   MET B 243     4145   5101   9313    -52    320    227       C  
ATOM   4354  O   MET B 243     -19.916 -10.680  35.685  1.00 49.46           O  
ANISOU 4354  O   MET B 243     4246   5091   9453    -91    370    195       O  
ATOM   4355  CB  MET B 243     -18.816  -8.423  34.009  1.00 46.88           C  
ANISOU 4355  CB  MET B 243     3833   4936   9041    -44    206    127       C  
ATOM   4356  CG  MET B 243     -19.724  -7.237  34.260  1.00 46.19           C  
ANISOU 4356  CG  MET B 243     3698   4911   8939    -82    171     96       C  
ATOM   4357  SD  MET B 243     -20.249  -6.410  32.730  1.00 45.27           S  
ANISOU 4357  SD  MET B 243     3527   4842   8829   -109    107      6       S  
ATOM   4358  CE  MET B 243     -21.101  -4.993  33.417  1.00 45.13           C  
ANISOU 4358  CE  MET B 243     3470   4892   8785   -124     78      1       C  
ATOM   4359  N   MET B 244     -19.637  -9.062  37.277  1.00 49.25           N  
ANISOU 4359  N   MET B 244     4186   5198   9326    -54    325    268       N  
ATOM   4360  CA  MET B 244     -20.668  -9.557  38.221  1.00 50.67           C  
ANISOU 4360  CA  MET B 244     4377   5340   9532    -96    393    290       C  
ATOM   4361  C   MET B 244     -21.735  -8.472  38.402  1.00 51.14           C  
ANISOU 4361  C   MET B 244     4382   5467   9582   -139    369    242       C  
ATOM   4362  O   MET B 244     -21.394  -7.413  38.976  1.00 51.66           O  
ANISOU 4362  O   MET B 244     4437   5607   9584   -108    329    260       O  
ATOM   4363  CB  MET B 244     -20.040  -9.902  39.575  1.00 51.17           C  
ANISOU 4363  CB  MET B 244     4485   5407   9548    -44    431    393       C  
ATOM   4364  CG  MET B 244     -19.014 -11.015  39.509  1.00 51.84           C  
ANISOU 4364  CG  MET B 244     4627   5427   9642     14    464    454       C  
ATOM   4365  SD  MET B 244     -19.603 -12.465  38.604  1.00 53.17           S  
ANISOU 4365  SD  MET B 244     4836   5450   9914    -33    533    411       S  
ATOM   4366  CE  MET B 244     -21.067 -12.877  39.549  1.00 53.84           C  
ANISOU 4366  CE  MET B 244     4924   5492  10039   -115    613    424       C  
ATOM   4367  N   SER B 245     -22.966  -8.728  37.935  1.00 51.23           N  
ANISOU 4367  N   SER B 245     4358   5452   9652   -208    394    182       N  
ATOM   4368  CA  SER B 245     -24.082  -7.746  37.890  1.00 50.84           C  
ANISOU 4368  CA  SER B 245     4244   5470   9602   -243    372    129       C  
ATOM   4369  C   SER B 245     -25.309  -8.289  38.635  1.00 51.62           C  
ANISOU 4369  C   SER B 245     4324   5548   9738   -301    448    139       C  
ATOM   4370  O   SER B 245     -25.681  -9.460  38.411  1.00 52.41           O  
ANISOU 4370  O   SER B 245     4440   5571   9901   -354    502    134       O  
ATOM   4371  CB  SER B 245     -24.433  -7.383  36.469  1.00 50.46           C  
ANISOU 4371  CB  SER B 245     4147   5441   9581   -268    317     44       C  
ATOM   4372  OG  SER B 245     -23.290  -7.425  35.630  1.00 49.98           O  
ANISOU 4372  OG  SER B 245     4113   5370   9505   -229    272     40       O  
ATOM   4373  N   ALA B 246     -25.931  -7.453  39.467  1.00 51.12           N  
ANISOU 4373  N   ALA B 246     4231   5552   9639   -293    456    149       N  
ATOM   4374  CA  ALA B 246     -27.125  -7.791  40.273  1.00 52.00           C  
ANISOU 4374  CA  ALA B 246     4313   5667   9775   -341    531    164       C  
ATOM   4375  C   ALA B 246     -28.073  -6.596  40.290  1.00 51.68           C  
ANISOU 4375  C   ALA B 246     4201   5718   9715   -337    506    117       C  
ATOM   4376  O   ALA B 246     -27.622  -5.454  40.225  1.00 51.22           O  
ANISOU 4376  O   ALA B 246     4145   5710   9603   -281    446    103       O  
ATOM   4377  CB  ALA B 246     -26.705  -8.183  41.669  1.00 52.38           C  
ANISOU 4377  CB  ALA B 246     4421   5700   9780   -309    590    255       C  
ATOM   4378  N   PRO B 247     -29.405  -6.810  40.392  1.00 51.87           N  
ANISOU 4378  N   PRO B 247     4160   5765   9783   -395    555     95       N  
ATOM   4379  CA  PRO B 247     -30.343  -5.702  40.563  1.00 51.35           C  
ANISOU 4379  CA  PRO B 247     4024   5790   9694   -375    545     63       C  
ATOM   4380  C   PRO B 247     -29.851  -4.770  41.667  1.00 50.48           C  
ANISOU 4380  C   PRO B 247     3960   5719   9498   -298    543    103       C  
ATOM   4381  O   PRO B 247     -29.607  -5.220  42.785  1.00 50.53           O  
ANISOU 4381  O   PRO B 247     4015   5710   9475   -290    600    167       O  
ATOM   4382  CB  PRO B 247     -31.653  -6.406  40.943  1.00 52.41           C  
ANISOU 4382  CB  PRO B 247     4095   5936   9882   -450    626     67       C  
ATOM   4383  CG  PRO B 247     -31.547  -7.751  40.263  1.00 53.07           C  
ANISOU 4383  CG  PRO B 247     4194   5931  10038   -530    645     57       C  
ATOM   4384  CD  PRO B 247     -30.082  -8.118  40.389  1.00 52.84           C  
ANISOU 4384  CD  PRO B 247     4270   5826   9978   -481    627    103       C  
ATOM   4385  N   PRO B 248     -29.689  -3.456  41.387  1.00 49.38           N  
ANISOU 4385  N   PRO B 248     3813   5630   9316   -242    479     66       N  
ATOM   4386  CA  PRO B 248     -28.988  -2.544  42.293  1.00 49.03           C  
ANISOU 4386  CA  PRO B 248     3829   5609   9188   -175    462     91       C  
ATOM   4387  C   PRO B 248     -29.380  -2.724  43.765  1.00 49.55           C  
ANISOU 4387  C   PRO B 248     3916   5699   9211   -165    541    141       C  
ATOM   4388  O   PRO B 248     -30.558  -2.740  44.024  1.00 51.03           O  
ANISOU 4388  O   PRO B 248     4045   5923   9420   -182    595    131       O  
ATOM   4389  CB  PRO B 248     -29.429  -1.159  41.795  1.00 48.78           C  
ANISOU 4389  CB  PRO B 248     3763   5629   9140   -133    412     34       C  
ATOM   4390  CG  PRO B 248     -29.663  -1.359  40.314  1.00 48.66           C  
ANISOU 4390  CG  PRO B 248     3693   5605   9188   -164    366    -11       C  
ATOM   4391  CD  PRO B 248     -30.198  -2.772  40.189  1.00 49.24           C  
ANISOU 4391  CD  PRO B 248     3732   5649   9327   -240    421      0       C  
ATOM   4392  N   ALA B 249     -28.404  -2.848  44.672  1.00 49.40           N  
ANISOU 4392  N   ALA B 249     3972   5668   9126   -137    546    194       N  
ATOM   4393  CA  ALA B 249     -28.629  -3.066  46.124  1.00 50.26           C  
ANISOU 4393  CA  ALA B 249     4113   5805   9179   -121    619    250       C  
ATOM   4394  C   ALA B 249     -27.376  -2.701  46.928  1.00 49.91           C  
ANISOU 4394  C   ALA B 249     4149   5774   9040    -72    585    286       C  
ATOM   4395  O   ALA B 249     -26.274  -2.821  46.368  1.00 49.09           O  
ANISOU 4395  O   ALA B 249     4074   5639   8937    -68    523    292       O  
ATOM   4396  CB  ALA B 249     -29.037  -4.501  46.365  1.00 50.97           C  
ANISOU 4396  CB  ALA B 249     4193   5851   9322   -175    700    307       C  
ATOM   4397  N   GLN B 250     -27.551  -2.296  48.195  1.00 50.84           N  
ANISOU 4397  N   GLN B 250     4297   5943   9074    -39    624    309       N  
ATOM   4398  CA  GLN B 250     -26.454  -1.850  49.102  1.00 51.51           C  
ANISOU 4398  CA  GLN B 250     4456   6061   9053      3    589    335       C  
ATOM   4399  C   GLN B 250     -25.473  -3.007  49.310  1.00 51.87           C  
ANISOU 4399  C   GLN B 250     4537   6075   9093      0    594    418       C  
ATOM   4400  O   GLN B 250     -25.931  -4.135  49.580  1.00 52.53           O  
ANISOU 4400  O   GLN B 250     4614   6128   9215    -22    671    477       O  
ATOM   4401  CB  GLN B 250     -26.975  -1.346  50.451  1.00 52.64           C  
ANISOU 4401  CB  GLN B 250     4625   6270   9105     37    642    342       C  
ATOM   4402  CG  GLN B 250     -27.307   0.135  50.449  1.00 53.03           C  
ANISOU 4402  CG  GLN B 250     4679   6353   9115     70    607    258       C  
ATOM   4403  CD  GLN B 250     -28.375   0.435  49.426  1.00 53.75           C  
ANISOU 4403  CD  GLN B 250     4696   6426   9297     57    614    204       C  
ATOM   4404  OE1 GLN B 250     -28.123   1.093  48.417  1.00 53.97           O  
ANISOU 4404  OE1 GLN B 250     4714   6430   9362     58    544    152       O  
ATOM   4405  NE2 GLN B 250     -29.573  -0.081  49.662  1.00 54.52           N  
ANISOU 4405  NE2 GLN B 250     4738   6544   9433     43    698    220       N  
ATOM   4406  N   TYR B 251     -24.172  -2.715  49.206  1.00 51.63           N  
ANISOU 4406  N   TYR B 251     4544   6055   9017     21    518    425       N  
ATOM   4407  CA  TYR B 251     -23.083  -3.718  49.090  1.00 51.80           C  
ANISOU 4407  CA  TYR B 251     4590   6047   9044     30    505    496       C  
ATOM   4408  C   TYR B 251     -21.736  -3.047  49.363  1.00 51.64           C  
ANISOU 4408  C   TYR B 251     4602   6081   8936     61    421    500       C  
ATOM   4409  O   TYR B 251     -21.259  -2.313  48.483  1.00 51.77           O  
ANISOU 4409  O   TYR B 251     4603   6093   8971     51    347    444       O  
ATOM   4410  CB  TYR B 251     -23.116  -4.328  47.689  1.00 51.37           C  
ANISOU 4410  CB  TYR B 251     4500   5916   9100     -2    492    475       C  
ATOM   4411  CG  TYR B 251     -22.109  -5.418  47.440  1.00 51.75           C  
ANISOU 4411  CG  TYR B 251     4574   5921   9168     13    491    542       C  
ATOM   4412  CD1 TYR B 251     -21.968  -6.481  48.316  1.00 52.72           C  
ANISOU 4412  CD1 TYR B 251     4734   6027   9270     34    558    635       C  
ATOM   4413  CD2 TYR B 251     -21.321  -5.405  46.303  1.00 51.51           C  
ANISOU 4413  CD2 TYR B 251     4531   5864   9176     14    428    516       C  
ATOM   4414  CE1 TYR B 251     -21.057  -7.496  48.076  1.00 53.19           C  
ANISOU 4414  CE1 TYR B 251     4821   6040   9350     62    562    701       C  
ATOM   4415  CE2 TYR B 251     -20.403  -6.410  46.048  1.00 51.68           C  
ANISOU 4415  CE2 TYR B 251     4574   5844   9214     41    432    576       C  
ATOM   4416  CZ  TYR B 251     -20.273  -7.461  46.936  1.00 52.67           C  
ANISOU 4416  CZ  TYR B 251     4740   5948   9322     67    499    669       C  
ATOM   4417  OH  TYR B 251     -19.374  -8.455  46.684  1.00 53.44           O  
ANISOU 4417  OH  TYR B 251     4863   6000   9438    106    508    732       O  
ATOM   4418  N   GLU B 252     -21.153  -3.302  50.537  1.00 52.02           N  
ANISOU 4418  N   GLU B 252     4689   6183   8890     95    433    567       N  
ATOM   4419  CA  GLU B 252     -19.916  -2.644  51.040  1.00 51.82           C  
ANISOU 4419  CA  GLU B 252     4691   6235   8762    119    354    572       C  
ATOM   4420  C   GLU B 252     -18.704  -3.229  50.300  1.00 50.81           C  
ANISOU 4420  C   GLU B 252     4549   6090   8663    131    304    614       C  
ATOM   4421  O   GLU B 252     -18.421  -4.427  50.488  1.00 51.18           O  
ANISOU 4421  O   GLU B 252     4605   6114   8725    160    348    701       O  
ATOM   4422  CB  GLU B 252     -19.860  -2.814  52.561  1.00 53.35           C  
ANISOU 4422  CB  GLU B 252     4925   6502   8841    153    391    631       C  
ATOM   4423  CG  GLU B 252     -18.505  -2.557  53.194  1.00 54.16           C  
ANISOU 4423  CG  GLU B 252     5050   6695   8833    179    318    664       C  
ATOM   4424  CD  GLU B 252     -18.461  -2.843  54.691  1.00 55.89           C  
ANISOU 4424  CD  GLU B 252     5308   6996   8930    218    356    731       C  
ATOM   4425  OE1 GLU B 252     -19.478  -2.571  55.389  1.00 56.71           O  
ANISOU 4425  OE1 GLU B 252     5432   7111   9001    217    417    709       O  
ATOM   4426  OE2 GLU B 252     -17.415  -3.349  55.164  1.00 56.52           O  
ANISOU 4426  OE2 GLU B 252     5396   7136   8943    255    327    810       O  
ATOM   4427  N   LEU B 253     -18.032  -2.413  49.477  1.00 49.39           N  
ANISOU 4427  N   LEU B 253     4350   5921   8495    112    220    558       N  
ATOM   4428  CA  LEU B 253     -16.852  -2.813  48.655  1.00 48.40           C  
ANISOU 4428  CA  LEU B 253     4201   5792   8397    125    169    589       C  
ATOM   4429  C   LEU B 253     -15.586  -2.782  49.525  1.00 48.28           C  
ANISOU 4429  C   LEU B 253     4196   5875   8274    157    121    648       C  
ATOM   4430  O   LEU B 253     -15.215  -1.689  50.000  1.00 47.92           O  
ANISOU 4430  O   LEU B 253     4157   5899   8148    136     60    604       O  
ATOM   4431  CB  LEU B 253     -16.714  -1.874  47.450  1.00 47.27           C  
ANISOU 4431  CB  LEU B 253     4029   5627   8301     87    105    507       C  
ATOM   4432  CG  LEU B 253     -17.896  -1.855  46.482  1.00 46.77           C  
ANISOU 4432  CG  LEU B 253     3947   5484   8339     60    140    447       C  
ATOM   4433  CD1 LEU B 253     -17.722  -0.766  45.435  1.00 46.09           C  
ANISOU 4433  CD1 LEU B 253     3839   5392   8279     31     73    374       C  
ATOM   4434  CD2 LEU B 253     -18.082  -3.208  45.816  1.00 46.69           C  
ANISOU 4434  CD2 LEU B 253     3923   5403   8413     68    192    487       C  
ATOM   4435  N   LYS B 254     -14.961  -3.945  49.726  1.00 48.26           N  
ANISOU 4435  N   LYS B 254     4194   5876   8267    208    147    745       N  
ATOM   4436  CA  LYS B 254     -13.676  -4.097  50.462  1.00 48.62           C  
ANISOU 4436  CA  LYS B 254     4233   6025   8212    252    100    818       C  
ATOM   4437  C   LYS B 254     -12.530  -3.683  49.533  1.00 47.47           C  
ANISOU 4437  C   LYS B 254     4041   5914   8081    243     17    799       C  
ATOM   4438  O   LYS B 254     -12.542  -4.092  48.353  1.00 46.53           O  
ANISOU 4438  O   LYS B 254     3901   5718   8058    243     29    787       O  
ATOM   4439  CB  LYS B 254     -13.454  -5.543  50.922  1.00 49.50           C  
ANISOU 4439  CB  LYS B 254     4363   6119   8323    324    166    938       C  
ATOM   4440  CG  LYS B 254     -14.571  -6.177  51.743  1.00 50.18           C  
ANISOU 4440  CG  LYS B 254     4495   6160   8410    333    264    976       C  
ATOM   4441  CD  LYS B 254     -14.363  -7.672  51.950  1.00 51.02           C  
ANISOU 4441  CD  LYS B 254     4626   6215   8542    400    337   1096       C  
ATOM   4442  CE  LYS B 254     -15.639  -8.490  51.919  1.00 51.21           C  
ANISOU 4442  CE  LYS B 254     4684   6120   8651    378    446   1109       C  
ATOM   4443  NZ  LYS B 254     -16.197  -8.698  53.277  1.00 52.07           N  
ANISOU 4443  NZ  LYS B 254     4831   6269   8681    395    508   1171       N  
ATOM   4444  N   HIS B 255     -11.572  -2.913  50.049  1.00 47.32           N  
ANISOU 4444  N   HIS B 255     4003   6009   7965    232    -61    795       N  
ATOM   4445  CA  HIS B 255     -10.362  -2.476  49.305  1.00 46.87           C  
ANISOU 4445  CA  HIS B 255     3891   6008   7907    217   -143    787       C  
ATOM   4446  C   HIS B 255      -9.674  -3.700  48.689  1.00 46.79           C  
ANISOU 4446  C   HIS B 255     3850   5979   7947    288   -117    874       C  
ATOM   4447  O   HIS B 255      -9.510  -4.709  49.404  1.00 47.53           O  
ANISOU 4447  O   HIS B 255     3960   6091   8008    359    -73    967       O  
ATOM   4448  CB  HIS B 255      -9.422  -1.671  50.212  1.00 47.38           C  
ANISOU 4448  CB  HIS B 255     3939   6214   7846    194   -225    787       C  
ATOM   4449  CG  HIS B 255      -8.127  -1.350  49.556  1.00 47.19           C  
ANISOU 4449  CG  HIS B 255     3849   6264   7817    178   -302    796       C  
ATOM   4450  ND1 HIS B 255      -6.917  -1.618  50.154  1.00 48.02           N  
ANISOU 4450  ND1 HIS B 255     3906   6504   7833    214   -352    870       N  
ATOM   4451  CD2 HIS B 255      -7.852  -0.835  48.340  1.00 46.54           C  
ANISOU 4451  CD2 HIS B 255     3732   6145   7805    135   -334    747       C  
ATOM   4452  CE1 HIS B 255      -5.944  -1.263  49.338  1.00 47.98           C  
ANISOU 4452  CE1 HIS B 255     3835   6546   7847    188   -410    865       C  
ATOM   4453  NE2 HIS B 255      -6.490  -0.779  48.217  1.00 46.95           N  
ANISOU 4453  NE2 HIS B 255     3716   6309   7814    140   -399    791       N  
ATOM   4454  N   GLY B 256      -9.342  -3.618  47.398  1.00 45.96           N  
ANISOU 4454  N   GLY B 256     3710   5834   7919    274   -136    844       N  
ATOM   4455  CA  GLY B 256      -8.492  -4.584  46.675  1.00 45.99           C  
ANISOU 4455  CA  GLY B 256     3678   5833   7962    342   -124    911       C  
ATOM   4456  C   GLY B 256      -9.054  -5.996  46.673  1.00 46.19           C  
ANISOU 4456  C   GLY B 256     3746   5755   8046    409    -28    971       C  
ATOM   4457  O   GLY B 256      -8.244  -6.935  46.664  1.00 47.08           O  
ANISOU 4457  O   GLY B 256     3846   5887   8153    492    -10   1058       O  
ATOM   4458  N   THR B 257     -10.383  -6.149  46.681  1.00 45.64           N  
ANISOU 4458  N   THR B 257     3726   5582   8033    375     32    928       N  
ATOM   4459  CA  THR B 257     -11.104  -7.442  46.507  1.00 45.45           C  
ANISOU 4459  CA  THR B 257     3748   5435   8086    411    129    965       C  
ATOM   4460  C   THR B 257     -11.768  -7.470  45.130  1.00 44.15           C  
ANISOU 4460  C   THR B 257     3580   5163   8031    366    147    882       C  
ATOM   4461  O   THR B 257     -12.462  -8.447  44.836  1.00 44.18           O  
ANISOU 4461  O   THR B 257     3620   5056   8108    374    222    890       O  
ATOM   4462  CB  THR B 257     -12.160  -7.642  47.600  1.00 46.04           C  
ANISOU 4462  CB  THR B 257     3872   5483   8139    396    190    982       C  
ATOM   4463  OG1 THR B 257     -13.060  -6.533  47.535  1.00 45.68           O  
ANISOU 4463  OG1 THR B 257     3822   5436   8098    317    168    882       O  
ATOM   4464  CG2 THR B 257     -11.561  -7.745  48.984  1.00 47.03           C  
ANISOU 4464  CG2 THR B 257     4006   5713   8147    448    180   1071       C  
ATOM   4465  N   PHE B 258     -11.554  -6.424  44.333  1.00 43.10           N  
ANISOU 4465  N   PHE B 258     3407   5065   7904    318     79    807       N  
ATOM   4466  CA  PHE B 258     -12.214  -6.172  43.027  1.00 42.28           C  
ANISOU 4466  CA  PHE B 258     3292   4883   7886    270     80    719       C  
ATOM   4467  C   PHE B 258     -11.370  -5.153  42.260  1.00 41.51           C  
ANISOU 4467  C   PHE B 258     3146   4857   7769    248      0    681       C  
ATOM   4468  O   PHE B 258     -10.606  -4.423  42.911  1.00 41.59           O  
ANISOU 4468  O   PHE B 258     3134   4966   7700    242    -57    702       O  
ATOM   4469  CB  PHE B 258     -13.647  -5.664  43.237  1.00 42.14           C  
ANISOU 4469  CB  PHE B 258     3295   4820   7894    207    104    652       C  
ATOM   4470  CG  PHE B 258     -13.756  -4.239  43.730  1.00 41.81           C  
ANISOU 4470  CG  PHE B 258     3242   4850   7791    162     46    604       C  
ATOM   4471  CD1 PHE B 258     -14.056  -3.205  42.855  1.00 41.09           C  
ANISOU 4471  CD1 PHE B 258     3131   4753   7728    114      2    523       C  
ATOM   4472  CD2 PHE B 258     -13.538  -3.927  45.064  1.00 42.27           C  
ANISOU 4472  CD2 PHE B 258     3318   4981   7760    172     36    640       C  
ATOM   4473  CE1 PHE B 258     -14.131  -1.894  43.302  1.00 40.88           C  
ANISOU 4473  CE1 PHE B 258     3107   4777   7649     76    -45    478       C  
ATOM   4474  CE2 PHE B 258     -13.609  -2.615  45.507  1.00 42.10           C  
ANISOU 4474  CE2 PHE B 258     3298   5017   7681    129    -15    587       C  
ATOM   4475  CZ  PHE B 258     -13.912  -1.602  44.628  1.00 41.38           C  
ANISOU 4475  CZ  PHE B 258     3192   4903   7625     82    -53    505       C  
ATOM   4476  N   THR B 259     -11.505  -5.106  40.935  1.00 40.92           N  
ANISOU 4476  N   THR B 259     3054   4734   7759    231     -6    628       N  
ATOM   4477  CA  THR B 259     -10.880  -4.063  40.084  1.00 40.69           C  
ANISOU 4477  CA  THR B 259     2981   4759   7719    200    -75    588       C  
ATOM   4478  C   THR B 259     -11.667  -2.764  40.272  1.00 40.40           C  
ANISOU 4478  C   THR B 259     2952   4727   7669    129   -109    519       C  
ATOM   4479  O   THR B 259     -11.172  -1.860  40.976  1.00 40.93           O  
ANISOU 4479  O   THR B 259     3012   4868   7670    104   -159    523       O  
ATOM   4480  CB  THR B 259     -10.807  -4.495  38.616  1.00 40.50           C  
ANISOU 4480  CB  THR B 259     2943   4686   7760    213    -63    559       C  
ATOM   4481  OG1 THR B 259      -9.881  -5.580  38.552  1.00 41.31           O  
ANISOU 4481  OG1 THR B 259     3040   4795   7860    289    -35    628       O  
ATOM   4482  CG2 THR B 259     -10.372  -3.378  37.692  1.00 40.00           C  
ANISOU 4482  CG2 THR B 259     2839   4669   7689    174   -125    517       C  
ATOM   4483  N   CYS B 260     -12.859  -2.684  39.682  1.00 39.72           N  
ANISOU 4483  N   CYS B 260     2880   4567   7644    100    -82    456       N  
ATOM   4484  CA  CYS B 260     -13.752  -1.505  39.772  1.00 39.26           C  
ANISOU 4484  CA  CYS B 260     2830   4502   7582     48   -103    390       C  
ATOM   4485  C   CYS B 260     -15.210  -1.974  39.827  1.00 39.82           C  
ANISOU 4485  C   CYS B 260     2919   4502   7706     38    -43    356       C  
ATOM   4486  O   CYS B 260     -15.459  -3.203  39.762  1.00 40.09           O  
ANISOU 4486  O   CYS B 260     2963   4487   7781     60     11    382       O  
ATOM   4487  CB  CYS B 260     -13.524  -0.564  38.599  1.00 38.25           C  
ANISOU 4487  CB  CYS B 260     2678   4383   7472     20   -154    344       C  
ATOM   4488  SG  CYS B 260     -13.888  -1.346  37.011  1.00 37.29           S  
ANISOU 4488  SG  CYS B 260     2537   4202   7430     34   -129    316       S  
ATOM   4489  N   ALA B 261     -16.129  -1.018  39.966  1.00 39.98           N  
ANISOU 4489  N   ALA B 261     2946   4518   7727      7    -51    302       N  
ATOM   4490  CA  ALA B 261     -17.578  -1.246  40.127  1.00 40.24           C  
ANISOU 4490  CA  ALA B 261     2982   4505   7801     -6      1    268       C  
ATOM   4491  C   ALA B 261     -18.335  -0.145  39.389  1.00 40.24           C  
ANISOU 4491  C   ALA B 261     2965   4500   7823    -29    -27    199       C  
ATOM   4492  O   ALA B 261     -17.686   0.809  38.905  1.00 40.58           O  
ANISOU 4492  O   ALA B 261     3006   4567   7843    -35    -84    184       O  
ATOM   4493  CB  ALA B 261     -17.926  -1.262  41.593  1.00 40.69           C  
ANISOU 4493  CB  ALA B 261     3068   4582   7808      0     36    295       C  
ATOM   4494  N   SER B 262     -19.655  -0.298  39.301  1.00 40.34           N  
ANISOU 4494  N   SER B 262     2963   4484   7878    -40     13    164       N  
ATOM   4495  CA  SER B 262     -20.620   0.740  38.867  1.00 40.14           C  
ANISOU 4495  CA  SER B 262     2920   4461   7868    -47     -1    105       C  
ATOM   4496  C   SER B 262     -21.702   0.874  39.943  1.00 40.23           C  
ANISOU 4496  C   SER B 262     2938   4479   7867    -44     49     97       C  
ATOM   4497  O   SER B 262     -22.333  -0.141  40.260  1.00 40.22           O  
ANISOU 4497  O   SER B 262     2923   4461   7897    -55    107    113       O  
ATOM   4498  CB  SER B 262     -21.208   0.393  37.529  1.00 40.27           C  
ANISOU 4498  CB  SER B 262     2894   4458   7949    -58     -4     69       C  
ATOM   4499  OG  SER B 262     -22.251  -0.562  37.674  1.00 40.97           O  
ANISOU 4499  OG  SER B 262     2959   4525   8084    -76     53     61       O  
ATOM   4500  N   GLU B 263     -21.882   2.073  40.499  1.00 40.29           N  
ANISOU 4500  N   GLU B 263     2969   4507   7830    -32     33     73       N  
ATOM   4501  CA  GLU B 263     -22.903   2.354  41.539  1.00 40.91           C  
ANISOU 4501  CA  GLU B 263     3056   4600   7887    -19     83     60       C  
ATOM   4502  C   GLU B 263     -24.043   3.154  40.893  1.00 40.83           C  
ANISOU 4502  C   GLU B 263     3012   4588   7911     -4     84      7       C  
ATOM   4503  O   GLU B 263     -23.762   4.196  40.271  1.00 40.15           O  
ANISOU 4503  O   GLU B 263     2939   4495   7818      7     33    -19       O  
ATOM   4504  CB  GLU B 263     -22.228   3.003  42.754  1.00 41.35           C  
ANISOU 4504  CB  GLU B 263     3172   4682   7856     -8     71     72       C  
ATOM   4505  CG  GLU B 263     -22.345   4.514  42.845  1.00 41.52           C  
ANISOU 4505  CG  GLU B 263     3228   4703   7842      5     38     21       C  
ATOM   4506  CD  GLU B 263     -23.652   5.009  43.438  1.00 42.15           C  
ANISOU 4506  CD  GLU B 263     3308   4789   7915     36     91    -12       C  
ATOM   4507  OE1 GLU B 263     -23.825   6.248  43.594  1.00 42.13           O  
ANISOU 4507  OE1 GLU B 263     3345   4777   7883     57     75    -56       O  
ATOM   4508  OE2 GLU B 263     -24.499   4.147  43.730  1.00 42.63           O  
ANISOU 4508  OE2 GLU B 263     3331   4862   8003     38    153      5       O  
ATOM   4509  N   TYR B 264     -25.277   2.652  41.023  1.00 41.35           N  
ANISOU 4509  N   TYR B 264     3032   4664   8015     -5    141      0       N  
ATOM   4510  CA  TYR B 264     -26.531   3.258  40.495  1.00 41.40           C  
ANISOU 4510  CA  TYR B 264     2987   4687   8054     15    151    -44       C  
ATOM   4511  C   TYR B 264     -27.402   3.734  41.663  1.00 42.10           C  
ANISOU 4511  C   TYR B 264     3084   4804   8107     47    208    -52       C  
ATOM   4512  O   TYR B 264     -27.837   2.886  42.459  1.00 42.66           O  
ANISOU 4512  O   TYR B 264     3140   4888   8178     30    270    -24       O  
ATOM   4513  CB  TYR B 264     -27.291   2.235  39.645  1.00 41.32           C  
ANISOU 4513  CB  TYR B 264     2901   4681   8117    -18    171    -50       C  
ATOM   4514  CG  TYR B 264     -28.324   2.798  38.701  1.00 41.15           C  
ANISOU 4514  CG  TYR B 264     2812   4689   8131      0    155    -93       C  
ATOM   4515  CD1 TYR B 264     -29.659   2.890  39.058  1.00 41.43           C  
ANISOU 4515  CD1 TYR B 264     2790   4768   8183     13    205   -108       C  
ATOM   4516  CD2 TYR B 264     -27.964   3.212  37.429  1.00 40.76           C  
ANISOU 4516  CD2 TYR B 264     2752   4635   8097      6     91   -113       C  
ATOM   4517  CE1 TYR B 264     -30.605   3.398  38.181  1.00 41.65           C  
ANISOU 4517  CE1 TYR B 264     2745   4837   8240     37    187   -142       C  
ATOM   4518  CE2 TYR B 264     -28.898   3.723  36.542  1.00 40.87           C  
ANISOU 4518  CE2 TYR B 264     2703   4686   8136     30     73   -145       C  
ATOM   4519  CZ  TYR B 264     -30.226   3.816  36.916  1.00 41.22           C  
ANISOU 4519  CZ  TYR B 264     2686   4779   8197     48    118   -160       C  
ATOM   4520  OH  TYR B 264     -31.135   4.320  36.028  1.00 41.10           O  
ANISOU 4520  OH  TYR B 264     2598   4813   8202     79     96   -186       O  
ATOM   4521  N   THR B 265     -27.632   5.043  41.772  1.00 42.47           N  
ANISOU 4521  N   THR B 265     3158   4853   8122     95    191    -85       N  
ATOM   4522  CA  THR B 265     -28.652   5.650  42.672  1.00 43.27           C  
ANISOU 4522  CA  THR B 265     3261   4985   8194    142    248   -105       C  
ATOM   4523  C   THR B 265     -29.794   6.137  41.787  1.00 43.61           C  
ANISOU 4523  C   THR B 265     3231   5050   8286    180    250   -135       C  
ATOM   4524  O   THR B 265     -29.548   6.268  40.580  1.00 43.18           O  
ANISOU 4524  O   THR B 265     3155   4982   8269    172    194   -144       O  
ATOM   4525  CB  THR B 265     -28.047   6.756  43.544  1.00 43.55           C  
ANISOU 4525  CB  THR B 265     3392   5002   8152    174    234   -125       C  
ATOM   4526  OG1 THR B 265     -27.185   6.118  44.485  1.00 43.64           O  
ANISOU 4526  OG1 THR B 265     3449   5019   8112    141    241    -91       O  
ATOM   4527  CG2 THR B 265     -29.070   7.562  44.314  1.00 44.61           C  
ANISOU 4527  CG2 THR B 265     3537   5159   8253    238    289   -157       C  
ATOM   4528  N   GLY B 266     -30.982   6.363  42.358  1.00 44.57           N  
ANISOU 4528  N   GLY B 266     3314   5215   8404    222    312   -147       N  
ATOM   4529  CA  GLY B 266     -32.188   6.781  41.617  1.00 45.15           C  
ANISOU 4529  CA  GLY B 266     3302   5331   8519    267    320   -170       C  
ATOM   4530  C   GLY B 266     -32.876   5.573  41.012  1.00 45.35           C  
ANISOU 4530  C   GLY B 266     3219   5400   8611    208    337   -157       C  
ATOM   4531  O   GLY B 266     -32.206   4.540  40.877  1.00 44.82           O  
ANISOU 4531  O   GLY B 266     3160   5304   8563    137    326   -136       O  
ATOM   4532  N   ASN B 267     -34.162   5.681  40.666  1.00 46.47           N  
ANISOU 4532  N   ASN B 267     3260   5609   8786    237    364   -171       N  
ATOM   4533  CA  ASN B 267     -35.060   4.496  40.582  1.00 47.21           C  
ANISOU 4533  CA  ASN B 267     3245   5758   8932    172    409   -161       C  
ATOM   4534  C   ASN B 267     -35.633   4.289  39.179  1.00 47.55           C  
ANISOU 4534  C   ASN B 267     3188   5845   9033    151    361   -184       C  
ATOM   4535  O   ASN B 267     -35.589   3.127  38.705  1.00 47.79           O  
ANISOU 4535  O   ASN B 267     3177   5871   9108     61    356   -183       O  
ATOM   4536  CB  ASN B 267     -36.160   4.563  41.636  1.00 47.99           C  
ANISOU 4536  CB  ASN B 267     3295   5921   9015    204    498   -152       C  
ATOM   4537  CG  ASN B 267     -35.944   3.507  42.691  1.00 48.26           C  
ANISOU 4537  CG  ASN B 267     3356   5939   9040    139    563   -115       C  
ATOM   4538  OD1 ASN B 267     -35.561   3.815  43.815  1.00 48.69           O  
ANISOU 4538  OD1 ASN B 267     3491   5977   9033    172    600    -99       O  
ATOM   4539  ND2 ASN B 267     -36.130   2.256  42.310  1.00 48.67           N  
ANISOU 4539  ND2 ASN B 267     3349   5991   9150     45    576   -100       N  
ATOM   4540  N   TYR B 268     -36.176   5.334  38.551  1.00 47.69           N  
ANISOU 4540  N   TYR B 268     3169   5905   9045    231    330   -204       N  
ATOM   4541  CA  TYR B 268     -36.951   5.204  37.290  1.00 47.95           C  
ANISOU 4541  CA  TYR B 268     3086   6011   9121    224    289   -224       C  
ATOM   4542  C   TYR B 268     -36.204   5.873  36.143  1.00 47.20           C  
ANISOU 4542  C   TYR B 268     3037   5880   9016    257    202   -233       C  
ATOM   4543  O   TYR B 268     -35.534   5.165  35.392  1.00 47.02           O  
ANISOU 4543  O   TYR B 268     3025   5827   9012    187    158   -240       O  
ATOM   4544  CB  TYR B 268     -38.352   5.786  37.463  1.00 49.10           C  
ANISOU 4544  CB  TYR B 268     3128   6259   9268    298    329   -228       C  
ATOM   4545  CG  TYR B 268     -39.196   5.027  38.449  1.00 49.83           C  
ANISOU 4545  CG  TYR B 268     3150   6404   9376    253    417   -216       C  
ATOM   4546  CD1 TYR B 268     -39.561   3.712  38.211  1.00 50.28           C  
ANISOU 4546  CD1 TYR B 268     3125   6491   9485    135    432   -218       C  
ATOM   4547  CD2 TYR B 268     -39.609   5.617  39.628  1.00 50.34           C  
ANISOU 4547  CD2 TYR B 268     3237   6485   9401    326    490   -203       C  
ATOM   4548  CE1 TYR B 268     -40.338   3.007  39.116  1.00 51.28           C  
ANISOU 4548  CE1 TYR B 268     3189   6664   9629     86    519   -200       C  
ATOM   4549  CE2 TYR B 268     -40.385   4.928  40.543  1.00 51.39           C  
ANISOU 4549  CE2 TYR B 268     3305   6675   9545    287    578   -185       C  
ATOM   4550  CZ  TYR B 268     -40.752   3.619  40.286  1.00 51.78           C  
ANISOU 4550  CZ  TYR B 268     3267   6754   9650    164    593   -179       C  
ATOM   4551  OH  TYR B 268     -41.525   2.950  41.186  1.00 52.75           O  
ANISOU 4551  OH  TYR B 268     3326   6930   9786    119    685   -155       O  
ATOM   4552  N   GLN B 269     -36.303   7.199  36.059  1.00 47.32           N  
ANISOU 4552  N   GLN B 269     3086   5892   8999    363    187   -232       N  
ATOM   4553  CA  GLN B 269     -35.929   8.022  34.876  1.00 46.65           C  
ANISOU 4553  CA  GLN B 269     3023   5795   8906    415    113   -233       C  
ATOM   4554  C   GLN B 269     -34.919   9.090  35.288  1.00 45.60           C  
ANISOU 4554  C   GLN B 269     3032   5563   8731    466    102   -222       C  
ATOM   4555  O   GLN B 269     -34.543   9.915  34.425  1.00 45.44           O  
ANISOU 4555  O   GLN B 269     3048   5517   8700    514     49   -215       O  
ATOM   4556  CB  GLN B 269     -37.177   8.676  34.281  1.00 47.77           C  
ANISOU 4556  CB  GLN B 269     3061   6035   9054    503    108   -235       C  
ATOM   4557  CG  GLN B 269     -38.361   8.710  35.235  1.00 48.76           C  
ANISOU 4557  CG  GLN B 269     3112   6231   9182    545    186   -235       C  
ATOM   4558  CD  GLN B 269     -39.392   9.708  34.782  1.00 50.07           C  
ANISOU 4558  CD  GLN B 269     3205   6477   9340    669    183   -229       C  
ATOM   4559  OE1 GLN B 269     -40.004  10.403  35.590  1.00 51.01           O  
ANISOU 4559  OE1 GLN B 269     3328   6612   9441    761    242   -223       O  
ATOM   4560  NE2 GLN B 269     -39.581   9.790  33.475  1.00 50.42           N  
ANISOU 4560  NE2 GLN B 269     3185   6577   9395    682    115   -228       N  
ATOM   4561  N   CYS B 270     -34.515   9.082  36.560  1.00 44.83           N  
ANISOU 4561  N   CYS B 270     3011   5415   8607    454    149   -221       N  
ATOM   4562  CA  CYS B 270     -33.407   9.921  37.075  1.00 44.11           C  
ANISOU 4562  CA  CYS B 270     3058   5227   8472    472    136   -218       C  
ATOM   4563  C   CYS B 270     -32.528   9.095  38.017  1.00 43.02           C  
ANISOU 4563  C   CYS B 270     2977   5050   8316    391    155   -211       C  
ATOM   4564  O   CYS B 270     -32.406   9.455  39.204  1.00 43.21           O  
ANISOU 4564  O   CYS B 270     3069   5050   8299    411    197   -217       O  
ATOM   4565  CB  CYS B 270     -33.932  11.193  37.729  1.00 45.07           C  
ANISOU 4565  CB  CYS B 270     3231   5331   8562    578    174   -230       C  
ATOM   4566  SG  CYS B 270     -35.606  11.081  38.418  1.00 45.42           S  
ANISOU 4566  SG  CYS B 270     3167   5477   8613    644    258   -237       S  
ATOM   4567  N   GLY B 271     -31.951   8.019  37.483  1.00 41.68           N  
ANISOU 4567  N   GLY B 271     2782   4879   8173    309    126   -200       N  
ATOM   4568  CA  GLY B 271     -30.889   7.244  38.140  1.00 41.02           C  
ANISOU 4568  CA  GLY B 271     2759   4753   8073    239    130   -183       C  
ATOM   4569  C   GLY B 271     -29.516   7.716  37.698  1.00 40.09           C  
ANISOU 4569  C   GLY B 271     2722   4575   7932    225     68   -175       C  
ATOM   4570  O   GLY B 271     -29.381   8.176  36.562  1.00 39.44           O  
ANISOU 4570  O   GLY B 271     2629   4490   7867    241     18   -178       O  
ATOM   4571  N   HIS B 272     -28.523   7.608  38.573  1.00 39.99           N  
ANISOU 4571  N   HIS B 272     2786   4526   7881    194     70   -162       N  
ATOM   4572  CA  HIS B 272     -27.121   8.012  38.296  1.00 39.82           C  
ANISOU 4572  CA  HIS B 272     2837   4458   7835    169     13   -150       C  
ATOM   4573  C   HIS B 272     -26.180   6.814  38.490  1.00 39.24           C  
ANISOU 4573  C   HIS B 272     2765   4383   7760    106      8   -120       C  
ATOM   4574  O   HIS B 272     -26.312   6.102  39.508  1.00 38.96           O  
ANISOU 4574  O   HIS B 272     2732   4360   7709     91     55   -106       O  
ATOM   4575  CB  HIS B 272     -26.755   9.219  39.173  1.00 40.33           C  
ANISOU 4575  CB  HIS B 272     2994   4484   7843    198     13   -167       C  
ATOM   4576  CG  HIS B 272     -25.504   9.915  38.754  1.00 40.16           C  
ANISOU 4576  CG  HIS B 272     3038   4417   7801    173    -46   -161       C  
ATOM   4577  ND1 HIS B 272     -25.229  10.210  37.430  1.00 39.97           N  
ANISOU 4577  ND1 HIS B 272     2996   4381   7809    173    -93   -151       N  
ATOM   4578  CD2 HIS B 272     -24.461  10.380  39.472  1.00 40.20           C  
ANISOU 4578  CD2 HIS B 272     3123   4395   7757    141    -68   -163       C  
ATOM   4579  CE1 HIS B 272     -24.073  10.835  37.354  1.00 39.63           C  
ANISOU 4579  CE1 HIS B 272     3017   4300   7740    141   -135   -143       C  
ATOM   4580  NE2 HIS B 272     -23.591  10.958  38.591  1.00 39.98           N  
ANISOU 4580  NE2 HIS B 272     3119   4334   7735    118   -123   -153       N  
ATOM   4581  N   TYR B 273     -25.283   6.588  37.528  1.00 39.00           N  
ANISOU 4581  N   TYR B 273     2733   4340   7744     78    -41   -106       N  
ATOM   4582  CA  TYR B 273     -24.084   5.724  37.692  1.00 39.03           C  
ANISOU 4582  CA  TYR B 273     2756   4336   7736     34    -55    -74       C  
ATOM   4583  C   TYR B 273     -22.926   6.583  38.194  1.00 38.96           C  
ANISOU 4583  C   TYR B 273     2818   4309   7672     26    -92    -64       C  
ATOM   4584  O   TYR B 273     -22.712   7.653  37.607  1.00 39.16           O  
ANISOU 4584  O   TYR B 273     2869   4315   7694     37   -129    -78       O  
ATOM   4585  CB  TYR B 273     -23.620   5.107  36.376  1.00 38.78           C  
ANISOU 4585  CB  TYR B 273     2687   4305   7741     13    -89    -65       C  
ATOM   4586  CG  TYR B 273     -24.350   3.869  35.938  1.00 39.35           C  
ANISOU 4586  CG  TYR B 273     2697   4389   7863     -4    -57    -72       C  
ATOM   4587  CD1 TYR B 273     -25.263   3.919  34.897  1.00 39.73           C  
ANISOU 4587  CD1 TYR B 273     2687   4460   7948      3    -67   -103       C  
ATOM   4588  CD2 TYR B 273     -24.100   2.640  36.525  1.00 39.76           C  
ANISOU 4588  CD2 TYR B 273     2751   4430   7924    -33    -20    -48       C  
ATOM   4589  CE1 TYR B 273     -25.928   2.787  34.459  1.00 39.84           C  
ANISOU 4589  CE1 TYR B 273     2644   4485   8008    -27    -43   -119       C  
ATOM   4590  CE2 TYR B 273     -24.756   1.495  36.097  1.00 40.11           C  
ANISOU 4590  CE2 TYR B 273     2748   4471   8019    -61     11    -58       C  
ATOM   4591  CZ  TYR B 273     -25.672   1.572  35.061  1.00 40.05           C  
ANISOU 4591  CZ  TYR B 273     2681   4487   8049    -64     -2    -99       C  
ATOM   4592  OH  TYR B 273     -26.320   0.463  34.610  1.00 40.72           O  
ANISOU 4592  OH  TYR B 273     2718   4569   8182   -105     23   -120       O  
ATOM   4593  N   LYS B 274     -22.229   6.136  39.239  1.00 39.10           N  
ANISOU 4593  N   LYS B 274     2869   4338   7650      5    -81    -40       N  
ATOM   4594  CA  LYS B 274     -20.864   6.604  39.598  1.00 39.15           C  
ANISOU 4594  CA  LYS B 274     2925   4346   7605    -20   -126    -24       C  
ATOM   4595  C   LYS B 274     -19.919   5.411  39.475  1.00 38.99           C  
ANISOU 4595  C   LYS B 274     2878   4346   7587    -42   -133     23       C  
ATOM   4596  O   LYS B 274     -20.383   4.266  39.632  1.00 38.91           O  
ANISOU 4596  O   LYS B 274     2839   4341   7604    -36    -89     41       O  
ATOM   4597  CB  LYS B 274     -20.761   7.149  41.026  1.00 39.76           C  
ANISOU 4597  CB  LYS B 274     3061   4432   7613    -20   -114    -36       C  
ATOM   4598  CG  LYS B 274     -21.696   8.293  41.378  1.00 40.39           C  
ANISOU 4598  CG  LYS B 274     3179   4485   7680     11    -95    -86       C  
ATOM   4599  CD  LYS B 274     -21.420   8.885  42.744  1.00 41.17           C  
ANISOU 4599  CD  LYS B 274     3348   4592   7700      6    -89   -107       C  
ATOM   4600  CE  LYS B 274     -22.465   9.902  43.151  1.00 41.93           C  
ANISOU 4600  CE  LYS B 274     3486   4659   7785     53    -55   -159       C  
ATOM   4601  NZ  LYS B 274     -21.966  10.789  44.225  1.00 42.70           N  
ANISOU 4601  NZ  LYS B 274     3673   4748   7803     39    -67   -196       N  
ATOM   4602  N   HIS B 275     -18.640   5.678  39.232  1.00 39.11           N  
ANISOU 4602  N   HIS B 275     2906   4376   7578    -66   -183     44       N  
ATOM   4603  CA  HIS B 275     -17.589   4.637  39.120  1.00 39.02           C  
ANISOU 4603  CA  HIS B 275     2870   4393   7562    -75   -192     95       C  
ATOM   4604  C   HIS B 275     -16.855   4.537  40.457  1.00 39.49           C  
ANISOU 4604  C   HIS B 275     2958   4492   7552    -83   -197    123       C  
ATOM   4605  O   HIS B 275     -16.547   5.592  41.032  1.00 39.70           O  
ANISOU 4605  O   HIS B 275     3024   4530   7528   -106   -227    100       O  
ATOM   4606  CB  HIS B 275     -16.659   4.965  37.956  1.00 38.69           C  
ANISOU 4606  CB  HIS B 275     2809   4358   7534    -91   -242    105       C  
ATOM   4607  CG  HIS B 275     -15.840   3.800  37.529  1.00 38.71           C  
ANISOU 4607  CG  HIS B 275     2775   4383   7548    -82   -239    150       C  
ATOM   4608  ND1 HIS B 275     -16.422   2.603  37.164  1.00 38.70           N  
ANISOU 4608  ND1 HIS B 275     2750   4358   7593    -59   -195    155       N  
ATOM   4609  CD2 HIS B 275     -14.504   3.646  37.397  1.00 38.59           C  
ANISOU 4609  CD2 HIS B 275     2744   4410   7507    -90   -271    192       C  
ATOM   4610  CE1 HIS B 275     -15.476   1.757  36.820  1.00 38.78           C  
ANISOU 4610  CE1 HIS B 275     2742   4387   7605    -46   -197    195       C  
ATOM   4611  NE2 HIS B 275     -14.287   2.374  36.952  1.00 38.66           N  
ANISOU 4611  NE2 HIS B 275     2725   4418   7544    -60   -244    222       N  
ATOM   4612  N   ILE B 276     -16.634   3.319  40.952  1.00 39.79           N  
ANISOU 4612  N   ILE B 276     2983   4550   7585    -66   -165    171       N  
ATOM   4613  CA  ILE B 276     -15.723   3.058  42.105  1.00 40.43           C  
ANISOU 4613  CA  ILE B 276     3081   4687   7593    -65   -176    215       C  
ATOM   4614  C   ILE B 276     -14.583   2.156  41.610  1.00 40.12           C  
ANISOU 4614  C   ILE B 276     3005   4676   7562    -51   -192    274       C  
ATOM   4615  O   ILE B 276     -14.873   1.082  41.066  1.00 39.61           O  
ANISOU 4615  O   ILE B 276     2921   4578   7551    -25   -151    296       O  
ATOM   4616  CB  ILE B 276     -16.477   2.476  43.319  1.00 41.15           C  
ANISOU 4616  CB  ILE B 276     3195   4782   7656    -42   -117    231       C  
ATOM   4617  CG1 ILE B 276     -17.328   3.530  44.039  1.00 41.45           C  
ANISOU 4617  CG1 ILE B 276     3274   4815   7660    -50   -107    174       C  
ATOM   4618  CG2 ILE B 276     -15.497   1.827  44.285  1.00 41.76           C  
ANISOU 4618  CG2 ILE B 276     3278   4922   7666    -27   -123    297       C  
ATOM   4619  CD1 ILE B 276     -18.523   4.023  43.263  1.00 41.10           C  
ANISOU 4619  CD1 ILE B 276     3220   4716   7679    -46    -86    120       C  
ATOM   4620  N   THR B 277     -13.340   2.619  41.778  1.00 40.38           N  
ANISOU 4620  N   THR B 277     3028   4771   7542    -71   -248    296       N  
ATOM   4621  CA  THR B 277     -12.081   1.969  41.317  1.00 40.28           C  
ANISOU 4621  CA  THR B 277     2971   4806   7525    -54   -272    355       C  
ATOM   4622  C   THR B 277     -11.203   1.686  42.538  1.00 40.86           C  
ANISOU 4622  C   THR B 277     3043   4964   7517    -42   -290    409       C  
ATOM   4623  O   THR B 277     -10.970   2.629  43.313  1.00 41.17           O  
ANISOU 4623  O   THR B 277     3103   5047   7492    -83   -330    384       O  
ATOM   4624  CB  THR B 277     -11.353   2.834  40.277  1.00 39.82           C  
ANISOU 4624  CB  THR B 277     2885   4763   7479    -92   -326    337       C  
ATOM   4625  OG1 THR B 277     -10.226   2.099  39.815  1.00 40.03           O  
ANISOU 4625  OG1 THR B 277     2863   4841   7505    -64   -337    395       O  
ATOM   4626  CG2 THR B 277     -10.861   4.167  40.796  1.00 40.10           C  
ANISOU 4626  CG2 THR B 277     2939   4836   7457   -153   -383    308       C  
ATOM   4627  N   SER B 278     -10.770   0.433  42.713  1.00 41.28           N  
ANISOU 4627  N   SER B 278     3077   5036   7570     14   -259    479       N  
ATOM   4628  CA  SER B 278      -9.841  -0.005  43.790  1.00 42.21           C  
ANISOU 4628  CA  SER B 278     3183   5247   7608     44   -275    549       C  
ATOM   4629  C   SER B 278      -8.391   0.201  43.329  1.00 42.73           C  
ANISOU 4629  C   SER B 278     3187   5401   7647     38   -336    584       C  
ATOM   4630  O   SER B 278      -7.961  -0.468  42.367  1.00 42.30           O  
ANISOU 4630  O   SER B 278     3097   5332   7642     77   -321    615       O  
ATOM   4631  CB  SER B 278     -10.097  -1.433  44.192  1.00 42.43           C  
ANISOU 4631  CB  SER B 278     3224   5247   7650    117   -207    617       C  
ATOM   4632  OG  SER B 278      -9.476  -1.725  45.435  1.00 43.19           O  
ANISOU 4632  OG  SER B 278     3320   5432   7656    148   -218    682       O  
ATOM   4633  N   LYS B 279      -7.681   1.122  43.980  1.00 43.76           N  
ANISOU 4633  N   LYS B 279     3304   5621   7700    -12   -402    574       N  
ATOM   4634  CA  LYS B 279      -6.235   1.382  43.761  1.00 44.89           C  
ANISOU 4634  CA  LYS B 279     3377   5875   7804    -30   -466    612       C  
ATOM   4635  C   LYS B 279      -5.543   1.213  45.118  1.00 46.25           C  
ANISOU 4635  C   LYS B 279     3533   6167   7870    -16   -499    661       C  
ATOM   4636  O   LYS B 279      -5.786   0.163  45.755  1.00 46.44           O  
ANISOU 4636  O   LYS B 279     3574   6190   7879     60   -451    720       O  
ATOM   4637  CB  LYS B 279      -6.064   2.748  43.090  1.00 44.75           C  
ANISOU 4637  CB  LYS B 279     3354   5848   7801   -124   -518    544       C  
ATOM   4638  CG  LYS B 279      -6.750   2.869  41.734  1.00 44.12           C  
ANISOU 4638  CG  LYS B 279     3286   5660   7814   -125   -485    505       C  
ATOM   4639  CD  LYS B 279      -6.714   4.271  41.162  1.00 44.26           C  
ANISOU 4639  CD  LYS B 279     3315   5655   7844   -213   -529    444       C  
ATOM   4640  CE  LYS B 279      -7.047   4.329  39.684  1.00 43.78           C  
ANISOU 4640  CE  LYS B 279     3246   5525   7864   -206   -507    428       C  
ATOM   4641  NZ  LYS B 279      -6.167   5.282  38.964  1.00 44.00           N  
ANISOU 4641  NZ  LYS B 279     3238   5590   7890   -274   -556    426       N  
ATOM   4642  N   GLU B 280      -4.737   2.187  45.558  1.00 47.37           N  
ANISOU 4642  N   GLU B 280     3648   6408   7941    -90   -576    640       N  
ATOM   4643  CA  GLU B 280      -4.025   2.121  46.866  1.00 48.96           C  
ANISOU 4643  CA  GLU B 280     3829   6746   8028    -86   -621    680       C  
ATOM   4644  C   GLU B 280      -5.046   2.399  47.974  1.00 49.44           C  
ANISOU 4644  C   GLU B 280     3976   6769   8040    -97   -599    633       C  
ATOM   4645  O   GLU B 280      -4.828   1.922  49.099  1.00 50.29           O  
ANISOU 4645  O   GLU B 280     4085   6962   8060    -56   -603    681       O  
ATOM   4646  CB  GLU B 280      -2.815   3.064  46.906  1.00 49.67           C  
ANISOU 4646  CB  GLU B 280     3853   6958   8059   -176   -714    666       C  
ATOM   4647  CG  GLU B 280      -3.146   4.515  47.212  1.00 49.91           C  
ANISOU 4647  CG  GLU B 280     3941   6960   8063   -295   -759    561       C  
ATOM   4648  CD  GLU B 280      -3.724   5.321  46.061  1.00 49.12           C  
ANISOU 4648  CD  GLU B 280     3876   6729   8058   -351   -742    492       C  
ATOM   4649  OE1 GLU B 280      -3.945   4.747  44.974  1.00 48.30           O  
ANISOU 4649  OE1 GLU B 280     3752   6557   8041   -299   -696    520       O  
ATOM   4650  OE2 GLU B 280      -3.947   6.531  46.256  1.00 49.57           O  
ANISOU 4650  OE2 GLU B 280     3984   6750   8097   -445   -775    410       O  
ATOM   4651  N   THR B 281      -6.101   3.158  47.641  1.00 49.26           N  
ANISOU 4651  N   THR B 281     4019   6628   8069   -145   -575    545       N  
ATOM   4652  CA  THR B 281      -7.345   3.365  48.437  1.00 49.16           C  
ANISOU 4652  CA  THR B 281     4091   6549   8037   -141   -530    494       C  
ATOM   4653  C   THR B 281      -8.544   3.220  47.487  1.00 48.05           C  
ANISOU 4653  C   THR B 281     3983   6262   8009   -121   -462    460       C  
ATOM   4654  O   THR B 281      -8.313   2.889  46.310  1.00 47.43           O  
ANISOU 4654  O   THR B 281     3864   6145   8010   -109   -455    480       O  
ATOM   4655  CB  THR B 281      -7.294   4.717  49.161  1.00 49.88           C  
ANISOU 4655  CB  THR B 281     4227   6672   8051   -229   -587    408       C  
ATOM   4656  OG1 THR B 281      -8.485   4.878  49.927  1.00 50.27           O  
ANISOU 4656  OG1 THR B 281     4357   6664   8078   -212   -537    362       O  
ATOM   4657  CG2 THR B 281      -7.146   5.891  48.218  1.00 49.63           C  
ANISOU 4657  CG2 THR B 281     4200   6582   8072   -315   -626    337       C  
ATOM   4658  N   LEU B 282      -9.771   3.446  47.969  1.00 48.07           N  
ANISOU 4658  N   LEU B 282     4051   6196   8015   -117   -414    411       N  
ATOM   4659  CA  LEU B 282     -11.016   3.396  47.147  1.00 47.29           C  
ANISOU 4659  CA  LEU B 282     3977   5973   8018   -103   -353    373       C  
ATOM   4660  C   LEU B 282     -11.351   4.797  46.627  1.00 46.80           C  
ANISOU 4660  C   LEU B 282     3946   5855   7979   -167   -384    282       C  
ATOM   4661  O   LEU B 282     -11.734   5.657  47.440  1.00 47.12           O  
ANISOU 4661  O   LEU B 282     4043   5897   7963   -196   -392    223       O  
ATOM   4662  CB  LEU B 282     -12.180   2.845  47.977  1.00 47.74           C  
ANISOU 4662  CB  LEU B 282     4077   5996   8064    -59   -278    378       C  
ATOM   4663  CG  LEU B 282     -12.190   1.332  48.196  1.00 48.18           C  
ANISOU 4663  CG  LEU B 282     4113   6058   8135      9   -221    470       C  
ATOM   4664  CD1 LEU B 282     -13.522   0.889  48.768  1.00 48.25           C  
ANISOU 4664  CD1 LEU B 282     4162   6012   8158     36   -138    467       C  
ATOM   4665  CD2 LEU B 282     -11.897   0.578  46.906  1.00 47.88           C  
ANISOU 4665  CD2 LEU B 282     4030   5970   8191     31   -210    503       C  
ATOM   4666  N   TYR B 283     -11.206   5.003  45.319  1.00 46.11           N  
ANISOU 4666  N   TYR B 283     3828   5720   7969   -183   -397    273       N  
ATOM   4667  CA  TYR B 283     -11.545   6.260  44.606  1.00 45.90           C  
ANISOU 4667  CA  TYR B 283     3832   5628   7980   -234   -419    201       C  
ATOM   4668  C   TYR B 283     -12.928   6.091  43.976  1.00 44.95           C  
ANISOU 4668  C   TYR B 283     3726   5413   7938   -194   -358    173       C  
ATOM   4669  O   TYR B 283     -13.131   5.084  43.273  1.00 44.58           O  
ANISOU 4669  O   TYR B 283     3639   5346   7951   -155   -324    212       O  
ATOM   4670  CB  TYR B 283     -10.518   6.574  43.513  1.00 46.25           C  
ANISOU 4670  CB  TYR B 283     3827   5689   8055   -273   -469    218       C  
ATOM   4671  CG  TYR B 283      -9.146   7.003  43.981  1.00 47.38           C  
ANISOU 4671  CG  TYR B 283     3944   5930   8127   -332   -538    235       C  
ATOM   4672  CD1 TYR B 283      -8.208   6.078  44.410  1.00 47.71           C  
ANISOU 4672  CD1 TYR B 283     3928   6074   8124   -304   -554    307       C  
ATOM   4673  CD2 TYR B 283      -8.765   8.337  43.951  1.00 47.98           C  
ANISOU 4673  CD2 TYR B 283     4051   5997   8181   -417   -589    181       C  
ATOM   4674  CE1 TYR B 283      -6.945   6.470  44.823  1.00 48.63           C  
ANISOU 4674  CE1 TYR B 283     4006   6299   8172   -360   -622    324       C  
ATOM   4675  CE2 TYR B 283      -7.504   8.745  44.355  1.00 48.69           C  
ANISOU 4675  CE2 TYR B 283     4109   6183   8208   -487   -656    192       C  
ATOM   4676  CZ  TYR B 283      -6.586   7.808  44.793  1.00 49.13           C  
ANISOU 4676  CZ  TYR B 283     4094   6358   8215   -459   -676    264       C  
ATOM   4677  OH  TYR B 283      -5.338   8.211  45.185  1.00 49.81           O  
ANISOU 4677  OH  TYR B 283     4134   6555   8234   -529   -747    276       O  
ATOM   4678  N   CYS B 284     -13.845   7.029  44.230  1.00 44.63           N  
ANISOU 4678  N   CYS B 284     3742   5318   7897   -204   -343    107       N  
ATOM   4679  CA  CYS B 284     -15.165   7.111  43.551  1.00 43.52           C  
ANISOU 4679  CA  CYS B 284     3607   5098   7828   -170   -294     75       C  
ATOM   4680  C   CYS B 284     -15.129   8.237  42.516  1.00 42.56           C  
ANISOU 4680  C   CYS B 284     3498   4923   7747   -199   -328     36       C  
ATOM   4681  O   CYS B 284     -15.113   9.418  42.921  1.00 43.41           O  
ANISOU 4681  O   CYS B 284     3666   5007   7820   -231   -350    -13       O  
ATOM   4682  CB  CYS B 284     -16.305   7.351  44.530  1.00 44.21           C  
ANISOU 4682  CB  CYS B 284     3741   5167   7888   -142   -245     36       C  
ATOM   4683  SG  CYS B 284     -17.863   7.721  43.682  1.00 44.68           S  
ANISOU 4683  SG  CYS B 284     3798   5147   8029   -103   -197     -7       S  
ATOM   4684  N   ILE B 285     -15.081   7.874  41.233  1.00 41.02           N  
ANISOU 4684  N   ILE B 285     3256   4709   7618   -190   -330     59       N  
ATOM   4685  CA  ILE B 285     -15.206   8.822  40.089  1.00 39.98           C  
ANISOU 4685  CA  ILE B 285     3133   4526   7531   -204   -352     34       C  
ATOM   4686  C   ILE B 285     -16.697   9.012  39.797  1.00 39.39           C  
ANISOU 4686  C   ILE B 285     3069   4395   7500   -155   -306     -1       C  
ATOM   4687  O   ILE B 285     -17.420   8.005  39.620  1.00 38.89           O  
ANISOU 4687  O   ILE B 285     2965   4338   7473   -118   -266     11       O  
ATOM   4688  CB  ILE B 285     -14.433   8.333  38.848  1.00 39.45           C  
ANISOU 4688  CB  ILE B 285     3006   4479   7502   -211   -375     78       C  
ATOM   4689  CG1 ILE B 285     -12.931   8.216  39.133  1.00 39.65           C  
ANISOU 4689  CG1 ILE B 285     3010   4574   7482   -256   -419    117       C  
ATOM   4690  CG2 ILE B 285     -14.730   9.232  37.651  1.00 39.19           C  
ANISOU 4690  CG2 ILE B 285     2983   4396   7512   -215   -388     59       C  
ATOM   4691  CD1 ILE B 285     -12.081   7.879  37.925  1.00 39.18           C  
ANISOU 4691  CD1 ILE B 285     2893   4541   7453   -262   -440    160       C  
ATOM   4692  N   ASP B 286     -17.120  10.273  39.769  1.00 39.01           N  
ANISOU 4692  N   ASP B 286     3076   4295   7450   -157   -313    -45       N  
ATOM   4693  CA  ASP B 286     -18.462  10.721  39.335  1.00 38.36           C  
ANISOU 4693  CA  ASP B 286     3002   4164   7409   -104   -278    -76       C  
ATOM   4694  C   ASP B 286     -18.259  11.695  38.174  1.00 38.07           C  
ANISOU 4694  C   ASP B 286     2980   4081   7402   -113   -309    -77       C  
ATOM   4695  O   ASP B 286     -18.389  12.911  38.401  1.00 38.83           O  
ANISOU 4695  O   ASP B 286     3147   4122   7484   -116   -315   -110       O  
ATOM   4696  CB  ASP B 286     -19.205  11.357  40.507  1.00 38.82           C  
ANISOU 4696  CB  ASP B 286     3122   4199   7427    -81   -245   -123       C  
ATOM   4697  CG  ASP B 286     -20.619  11.762  40.154  1.00 38.84           C  
ANISOU 4697  CG  ASP B 286     3122   4165   7468    -13   -203   -151       C  
ATOM   4698  OD1 ASP B 286     -20.943  11.739  38.948  1.00 38.37           O  
ANISOU 4698  OD1 ASP B 286     3020   4095   7462      7   -211   -136       O  
ATOM   4699  OD2 ASP B 286     -21.375  12.089  41.083  1.00 39.22           O  
ANISOU 4699  OD2 ASP B 286     3207   4205   7489     20   -163   -186       O  
ATOM   4700  N   GLY B 287     -17.916  11.184  36.989  1.00 37.17           N  
ANISOU 4700  N   GLY B 287     2809   3986   7325   -115   -327    -42       N  
ATOM   4701  CA  GLY B 287     -17.552  12.021  35.830  1.00 36.95           C  
ANISOU 4701  CA  GLY B 287     2790   3927   7319   -127   -357    -28       C  
ATOM   4702  C   GLY B 287     -16.289  12.820  36.115  1.00 37.23           C  
ANISOU 4702  C   GLY B 287     2872   3952   7320   -200   -398    -21       C  
ATOM   4703  O   GLY B 287     -15.206  12.222  36.065  1.00 36.88           O  
ANISOU 4703  O   GLY B 287     2788   3963   7261   -243   -423     12       O  
ATOM   4704  N   ALA B 288     -16.425  14.108  36.451  1.00 37.85           N  
ANISOU 4704  N   ALA B 288     3032   3962   7386   -215   -402    -53       N  
ATOM   4705  CA  ALA B 288     -15.305  15.054  36.695  1.00 38.32           C  
ANISOU 4705  CA  ALA B 288     3147   3996   7416   -299   -440    -56       C  
ATOM   4706  C   ALA B 288     -15.046  15.242  38.194  1.00 38.82           C  
ANISOU 4706  C   ALA B 288     3262   4067   7421   -338   -445   -100       C  
ATOM   4707  O   ALA B 288     -14.034  15.878  38.520  1.00 39.28           O  
ANISOU 4707  O   ALA B 288     3355   4122   7447   -423   -483   -108       O  
ATOM   4708  CB  ALA B 288     -15.582  16.382  36.033  1.00 38.74           C  
ANISOU 4708  CB  ALA B 288     3270   3955   7495   -296   -439    -64       C  
ATOM   4709  N   LEU B 289     -15.914  14.733  39.072  1.00 38.96           N  
ANISOU 4709  N   LEU B 289     3282   4099   7420   -284   -409   -129       N  
ATOM   4710  CA  LEU B 289     -15.701  14.800  40.542  1.00 39.79           C  
ANISOU 4710  CA  LEU B 289     3434   4227   7456   -313   -411   -168       C  
ATOM   4711  C   LEU B 289     -14.954  13.538  40.971  1.00 39.71           C  
ANISOU 4711  C   LEU B 289     3350   4322   7416   -332   -426   -126       C  
ATOM   4712  O   LEU B 289     -15.024  12.523  40.249  1.00 38.79           O  
ANISOU 4712  O   LEU B 289     3156   4241   7340   -298   -415    -77       O  
ATOM   4713  CB  LEU B 289     -17.029  14.930  41.296  1.00 40.20           C  
ANISOU 4713  CB  LEU B 289     3528   4247   7497   -239   -355   -215       C  
ATOM   4714  CG  LEU B 289     -18.078  15.889  40.722  1.00 40.49           C  
ANISOU 4714  CG  LEU B 289     3614   4192   7577   -178   -324   -243       C  
ATOM   4715  CD1 LEU B 289     -19.109  16.238  41.787  1.00 41.06           C  
ANISOU 4715  CD1 LEU B 289     3746   4239   7616   -119   -273   -300       C  
ATOM   4716  CD2 LEU B 289     -17.456  17.157  40.155  1.00 41.00           C  
ANISOU 4716  CD2 LEU B 289     3748   4174   7653   -230   -357   -253       C  
ATOM   4717  N   LEU B 290     -14.255  13.622  42.099  1.00 40.78           N  
ANISOU 4717  N   LEU B 290     3512   4503   7479   -383   -452   -144       N  
ATOM   4718  CA  LEU B 290     -13.399  12.538  42.633  1.00 41.08           C  
ANISOU 4718  CA  LEU B 290     3485   4646   7474   -400   -473    -97       C  
ATOM   4719  C   LEU B 290     -13.509  12.546  44.154  1.00 42.07           C  
ANISOU 4719  C   LEU B 290     3658   4810   7516   -402   -467   -134       C  
ATOM   4720  O   LEU B 290     -13.357  13.620  44.749  1.00 42.63           O  
ANISOU 4720  O   LEU B 290     3806   4849   7540   -451   -489   -195       O  
ATOM   4721  CB  LEU B 290     -11.953  12.765  42.187  1.00 41.45           C  
ANISOU 4721  CB  LEU B 290     3497   4740   7512   -481   -535    -66       C  
ATOM   4722  CG  LEU B 290     -10.979  11.629  42.514  1.00 41.56           C  
ANISOU 4722  CG  LEU B 290     3430   4871   7490   -485   -558     -4       C  
ATOM   4723  CD1 LEU B 290     -11.391  10.338  41.814  1.00 40.80           C  
ANISOU 4723  CD1 LEU B 290     3266   4786   7448   -406   -517     51       C  
ATOM   4724  CD2 LEU B 290      -9.549  12.006  42.148  1.00 41.82           C  
ANISOU 4724  CD2 LEU B 290     3422   4961   7506   -571   -621     22       C  
ATOM   4725  N   THR B 291     -13.776  11.379  44.733  1.00 42.49           N  
ANISOU 4725  N   THR B 291     3671   4925   7548   -351   -436    -97       N  
ATOM   4726  CA  THR B 291     -13.874  11.143  46.194  1.00 43.56           C  
ANISOU 4726  CA  THR B 291     3839   5116   7594   -341   -424   -113       C  
ATOM   4727  C   THR B 291     -12.857  10.056  46.538  1.00 43.77           C  
ANISOU 4727  C   THR B 291     3797   5252   7581   -348   -451    -41       C  
ATOM   4728  O   THR B 291     -12.462   9.328  45.615  1.00 42.98           O  
ANISOU 4728  O   THR B 291     3628   5164   7538   -334   -455     18       O  
ATOM   4729  CB  THR B 291     -15.326  10.810  46.570  1.00 43.65           C  
ANISOU 4729  CB  THR B 291     3871   5091   7621   -263   -346   -129       C  
ATOM   4730  OG1 THR B 291     -16.004  12.061  46.695  1.00 44.09           O  
ANISOU 4730  OG1 THR B 291     4007   5068   7673   -262   -334   -207       O  
ATOM   4731  CG2 THR B 291     -15.482  10.014  47.851  1.00 44.13           C  
ANISOU 4731  CG2 THR B 291     3934   5226   7607   -231   -316   -108       C  
ATOM   4732  N   LYS B 292     -12.442   9.982  47.803  1.00 45.02           N  
ANISOU 4732  N   LYS B 292     3977   5489   7640   -362   -470    -46       N  
ATOM   4733  CA  LYS B 292     -11.597   8.886  48.336  1.00 45.77           C  
ANISOU 4733  CA  LYS B 292     4011   5697   7682   -347   -488     30       C  
ATOM   4734  C   LYS B 292     -12.090   8.494  49.726  1.00 46.73           C  
ANISOU 4734  C   LYS B 292     4170   5868   7715   -306   -453     29       C  
ATOM   4735  O   LYS B 292     -12.372   9.405  50.530  1.00 47.04           O  
ANISOU 4735  O   LYS B 292     4283   5900   7687   -333   -461    -45       O  
ATOM   4736  CB  LYS B 292     -10.135   9.313  48.478  1.00 46.84           C  
ANISOU 4736  CB  LYS B 292     4117   5920   7758   -426   -574     36       C  
ATOM   4737  CG  LYS B 292      -9.593  10.239  47.400  1.00 46.79           C  
ANISOU 4737  CG  LYS B 292     4102   5864   7808   -499   -618      9       C  
ATOM   4738  CD  LYS B 292      -8.101  10.408  47.493  1.00 47.63           C  
ANISOU 4738  CD  LYS B 292     4154   6079   7864   -576   -698     34       C  
ATOM   4739  CE  LYS B 292      -7.595  10.468  48.918  1.00 48.81           C  
ANISOU 4739  CE  LYS B 292     4319   6338   7888   -605   -739     17       C  
ATOM   4740  NZ  LYS B 292      -6.160  10.835  48.960  1.00 49.80           N  
ANISOU 4740  NZ  LYS B 292     4386   6571   7964   -699   -825     28       N  
ATOM   4741  N   SER B 293     -12.135   7.190  50.003  1.00 47.40           N  
ANISOU 4741  N   SER B 293     4211   6001   7797   -243   -415    111       N  
ATOM   4742  CA  SER B 293     -12.421   6.620  51.345  1.00 48.86           C  
ANISOU 4742  CA  SER B 293     4421   6254   7889   -199   -382    138       C  
ATOM   4743  C   SER B 293     -11.583   5.357  51.564  1.00 49.55           C  
ANISOU 4743  C   SER B 293     4444   6431   7950   -159   -389    246       C  
ATOM   4744  O   SER B 293     -11.144   4.762  50.563  1.00 48.86           O  
ANISOU 4744  O   SER B 293     4298   6325   7941   -147   -393    298       O  
ATOM   4745  CB  SER B 293     -13.899   6.349  51.518  1.00 48.85           C  
ANISOU 4745  CB  SER B 293     4453   6180   7925   -144   -290    124       C  
ATOM   4746  OG  SER B 293     -14.422   5.591  50.431  1.00 48.05           O  
ANISOU 4746  OG  SER B 293     4306   6008   7943   -111   -244    164       O  
ATOM   4747  N   SER B 294     -11.360   4.994  52.831  1.00 51.20           N  
ANISOU 4747  N   SER B 294     4668   6736   8046   -134   -389    280       N  
ATOM   4748  CA  SER B 294     -10.826   3.677  53.276  1.00 52.17           C  
ANISOU 4748  CA  SER B 294     4747   6941   8134    -69   -373    396       C  
ATOM   4749  C   SER B 294     -11.804   2.555  52.882  1.00 52.55           C  
ANISOU 4749  C   SER B 294     4791   6898   8274     -1   -275    453       C  
ATOM   4750  O   SER B 294     -11.332   1.403  52.727  1.00 52.70           O  
ANISOU 4750  O   SER B 294     4769   6939   8314     51   -256    551       O  
ATOM   4751  CB  SER B 294     -10.537   3.680  54.763  1.00 53.12           C  
ANISOU 4751  CB  SER B 294     4895   7181   8103    -56   -392    411       C  
ATOM   4752  OG  SER B 294     -10.714   2.388  55.328  1.00 53.25           O  
ANISOU 4752  OG  SER B 294     4902   7230   8098     27   -330    519       O  
ATOM   4753  N   GLU B 295     -13.106   2.868  52.742  1.00 53.10           N  
ANISOU 4753  N   GLU B 295     4903   6875   8398     -1   -212    395       N  
ATOM   4754  CA  GLU B 295     -14.141   1.943  52.191  1.00 53.04           C  
ANISOU 4754  CA  GLU B 295     4885   6772   8494     40   -123    431       C  
ATOM   4755  C   GLU B 295     -15.312   2.713  51.565  1.00 52.38           C  
ANISOU 4755  C   GLU B 295     4822   6593   8487     15    -92    342       C  
ATOM   4756  O   GLU B 295     -15.535   3.867  51.961  1.00 52.63           O  
ANISOU 4756  O   GLU B 295     4897   6631   8468    -13   -116    262       O  
ATOM   4757  CB  GLU B 295     -14.683   1.009  53.272  1.00 54.09           C  
ANISOU 4757  CB  GLU B 295     5040   6933   8575     94    -47    501       C  
ATOM   4758  CG  GLU B 295     -15.219  -0.282  52.687  1.00 54.15           C  
ANISOU 4758  CG  GLU B 295     5024   6862   8686    132     30    571       C  
ATOM   4759  CD  GLU B 295     -15.525  -1.382  53.684  1.00 55.45           C  
ANISOU 4759  CD  GLU B 295     5210   7052   8807    186    106    666       C  
ATOM   4760  OE1 GLU B 295     -15.338  -2.564  53.315  1.00 55.87           O  
ANISOU 4760  OE1 GLU B 295     5244   7063   8918    221    144    749       O  
ATOM   4761  OE2 GLU B 295     -15.970  -1.061  54.813  1.00 56.26           O  
ANISOU 4761  OE2 GLU B 295     5351   7208   8815    194    131    658       O  
ATOM   4762  N   TYR B 296     -16.026   2.074  50.629  1.00 51.87           N  
ANISOU 4762  N   TYR B 296     4727   6443   8534     30    -40    356       N  
ATOM   4763  CA  TYR B 296     -17.280   2.563  49.992  1.00 51.57           C  
ANISOU 4763  CA  TYR B 296     4694   6323   8576     21      0    289       C  
ATOM   4764  C   TYR B 296     -18.426   1.634  50.396  1.00 51.10           C  
ANISOU 4764  C   TYR B 296     4630   6237   8546     53     97    327       C  
ATOM   4765  O   TYR B 296     -18.197   0.417  50.544  1.00 50.93           O  
ANISOU 4765  O   TYR B 296     4594   6219   8538     77    132    409       O  
ATOM   4766  CB  TYR B 296     -17.170   2.612  48.462  1.00 51.41           C  
ANISOU 4766  CB  TYR B 296     4632   6239   8662      1    -27    270       C  
ATOM   4767  CG  TYR B 296     -18.373   3.195  47.756  1.00 51.50           C  
ANISOU 4767  CG  TYR B 296     4639   6181   8746     -3      0    204       C  
ATOM   4768  CD1 TYR B 296     -18.352   4.487  47.254  1.00 51.78           C  
ANISOU 4768  CD1 TYR B 296     4693   6193   8786    -28    -46    133       C  
ATOM   4769  CD2 TYR B 296     -19.543   2.467  47.600  1.00 51.81           C  
ANISOU 4769  CD2 TYR B 296     4655   6181   8847     15     75    215       C  
ATOM   4770  CE1 TYR B 296     -19.455   5.041  46.618  1.00 51.88           C  
ANISOU 4770  CE1 TYR B 296     4700   6150   8860    -19    -21     80       C  
ATOM   4771  CE2 TYR B 296     -20.655   3.005  46.967  1.00 52.01           C  
ANISOU 4771  CE2 TYR B 296     4664   6161   8933     14     98    158       C  
ATOM   4772  CZ  TYR B 296     -20.616   4.298  46.472  1.00 52.10           C  
ANISOU 4772  CZ  TYR B 296     4694   6155   8945      4     49     92       C  
ATOM   4773  OH  TYR B 296     -21.713   4.836  45.850  1.00 51.61           O  
ANISOU 4773  OH  TYR B 296     4614   6055   8938     18     71     44       O  
ATOM   4774  N   LYS B 297     -19.620   2.206  50.562  1.00 50.85           N  
ANISOU 4774  N   LYS B 297     4613   6179   8527     56    142    270       N  
ATOM   4775  CA  LYS B 297     -20.894   1.476  50.803  1.00 50.74           C  
ANISOU 4775  CA  LYS B 297     4583   6140   8556     75    239    294       C  
ATOM   4776  C   LYS B 297     -22.004   2.199  50.040  1.00 49.37           C  
ANISOU 4776  C   LYS B 297     4386   5916   8454     68    255    218       C  
ATOM   4777  O   LYS B 297     -22.077   3.434  50.158  1.00 49.51           O  
ANISOU 4777  O   LYS B 297     4437   5941   8434     71    223    149       O  
ATOM   4778  CB  LYS B 297     -21.206   1.421  52.299  1.00 52.09           C  
ANISOU 4778  CB  LYS B 297     4794   6374   8621    102    290    318       C  
ATOM   4779  CG  LYS B 297     -22.540   0.784  52.658  1.00 53.09           C  
ANISOU 4779  CG  LYS B 297     4902   6486   8783    117    396    343       C  
ATOM   4780  CD  LYS B 297     -23.236   1.490  53.801  1.00 54.26           C  
ANISOU 4780  CD  LYS B 297     5089   6687   8840    144    440    308       C  
ATOM   4781  CE  LYS B 297     -24.381   0.694  54.389  1.00 55.19           C  
ANISOU 4781  CE  LYS B 297     5185   6813   8970    159    552    358       C  
ATOM   4782  NZ  LYS B 297     -24.494   0.911  55.852  1.00 56.38           N  
ANISOU 4782  NZ  LYS B 297     5387   7044   8989    194    593    373       N  
ATOM   4783  N   GLY B 298     -22.817   1.468  49.276  1.00 48.07           N  
ANISOU 4783  N   GLY B 298     4170   5706   8389     60    301    231       N  
ATOM   4784  CA  GLY B 298     -23.847   2.075  48.412  1.00 47.35           C  
ANISOU 4784  CA  GLY B 298     4040   5579   8369     57    309    167       C  
ATOM   4785  C   GLY B 298     -24.387   1.106  47.366  1.00 46.34           C  
ANISOU 4785  C   GLY B 298     3849   5406   8351     33    336    185       C  
ATOM   4786  O   GLY B 298     -23.929  -0.031  47.269  1.00 46.23           O  
ANISOU 4786  O   GLY B 298     3829   5373   8362     18    350    243       O  
ATOM   4787  N   PRO B 299     -25.389   1.537  46.564  1.00 45.31           N  
ANISOU 4787  N   PRO B 299     3671   5259   8283     31    343    133       N  
ATOM   4788  CA  PRO B 299     -26.064   0.647  45.621  1.00 44.73           C  
ANISOU 4788  CA  PRO B 299     3533   5154   8308      0    370    137       C  
ATOM   4789  C   PRO B 299     -25.209   0.332  44.384  1.00 43.19           C  
ANISOU 4789  C   PRO B 299     3327   4919   8161    -21    306    135       C  
ATOM   4790  O   PRO B 299     -25.206   1.110  43.449  1.00 42.39           O  
ANISOU 4790  O   PRO B 299     3210   4813   8083    -16    254     88       O  
ATOM   4791  CB  PRO B 299     -27.360   1.405  45.273  1.00 45.04           C  
ANISOU 4791  CB  PRO B 299     3522   5213   8378     15    389     81       C  
ATOM   4792  CG  PRO B 299     -27.019   2.867  45.491  1.00 45.00           C  
ANISOU 4792  CG  PRO B 299     3567   5220   8311     57    342     36       C  
ATOM   4793  CD  PRO B 299     -25.957   2.893  46.572  1.00 45.25           C  
ANISOU 4793  CD  PRO B 299     3672   5265   8253     62    330     67       C  
ATOM   4794  N   ILE B 300     -24.516  -0.810  44.424  1.00 42.66           N  
ANISOU 4794  N   ILE B 300     3274   4827   8106    -37    318    191       N  
ATOM   4795  CA  ILE B 300     -23.632  -1.315  43.332  1.00 41.74           C  
ANISOU 4795  CA  ILE B 300     3152   4673   8032    -50    271    197       C  
ATOM   4796  C   ILE B 300     -24.445  -2.302  42.500  1.00 41.68           C  
ANISOU 4796  C   ILE B 300     3098   4623   8115    -88    310    185       C  
ATOM   4797  O   ILE B 300     -25.274  -3.012  43.085  1.00 42.61           O  
ANISOU 4797  O   ILE B 300     3204   4731   8255   -108    382    207       O  
ATOM   4798  CB  ILE B 300     -22.352  -1.975  43.878  1.00 41.64           C  
ANISOU 4798  CB  ILE B 300     3184   4661   7976    -33    263    265       C  
ATOM   4799  CG1 ILE B 300     -21.769  -1.223  45.078  1.00 41.86           C  
ANISOU 4799  CG1 ILE B 300     3256   4746   7903     -6    244    284       C  
ATOM   4800  CG2 ILE B 300     -21.326  -2.143  42.767  1.00 41.08           C  
ANISOU 4800  CG2 ILE B 300     3106   4568   7930    -32    206    263       C  
ATOM   4801  CD1 ILE B 300     -21.555   0.253  44.845  1.00 41.49           C  
ANISOU 4801  CD1 ILE B 300     3217   4725   7820     -3    178    223       C  
ATOM   4802  N   THR B 301     -24.198  -2.340  41.191  1.00 41.08           N  
ANISOU 4802  N   THR B 301     2998   4524   8086   -100    264    150       N  
ATOM   4803  CA  THR B 301     -24.956  -3.155  40.205  1.00 41.13           C  
ANISOU 4803  CA  THR B 301     2958   4494   8173   -143    285    118       C  
ATOM   4804  C   THR B 301     -24.003  -3.943  39.295  1.00 40.77           C  
ANISOU 4804  C   THR B 301     2931   4402   8155   -148    259    126       C  
ATOM   4805  O   THR B 301     -24.436  -4.972  38.756  1.00 41.29           O  
ANISOU 4805  O   THR B 301     2983   4421   8283   -187    293    113       O  
ATOM   4806  CB  THR B 301     -25.908  -2.275  39.387  1.00 40.94           C  
ANISOU 4806  CB  THR B 301     2874   4506   8172   -149    254     51       C  
ATOM   4807  OG1 THR B 301     -26.544  -3.122  38.432  1.00 41.14           O  
ANISOU 4807  OG1 THR B 301     2854   4508   8269   -198    266     18       O  
ATOM   4808  CG2 THR B 301     -25.224  -1.131  38.667  1.00 40.35           C  
ANISOU 4808  CG2 THR B 301     2808   4453   8067   -116    175     25       C  
ATOM   4809  N   ASP B 302     -22.784  -3.449  39.080  1.00 40.18           N  
ANISOU 4809  N   ASP B 302     2884   4343   8038   -112    203    141       N  
ATOM   4810  CA  ASP B 302     -21.701  -4.181  38.374  1.00 40.05           C  
ANISOU 4810  CA  ASP B 302     2887   4293   8034    -99    184    161       C  
ATOM   4811  C   ASP B 302     -20.471  -4.213  39.281  1.00 39.77           C  
ANISOU 4811  C   ASP B 302     2896   4277   7937    -57    177    231       C  
ATOM   4812  O   ASP B 302     -20.194  -3.202  39.950  1.00 39.76           O  
ANISOU 4812  O   ASP B 302     2902   4328   7874    -42    145    238       O  
ATOM   4813  CB  ASP B 302     -21.340  -3.532  37.034  1.00 39.77           C  
ANISOU 4813  CB  ASP B 302     2827   4277   8005    -95    118    113       C  
ATOM   4814  CG  ASP B 302     -22.487  -3.424  36.041  1.00 40.10           C  
ANISOU 4814  CG  ASP B 302     2820   4318   8096   -130    112     44       C  
ATOM   4815  OD1 ASP B 302     -23.358  -4.332  36.027  1.00 40.78           O  
ANISOU 4815  OD1 ASP B 302     2891   4369   8233   -169    162     27       O  
ATOM   4816  OD2 ASP B 302     -22.492  -2.439  35.273  1.00 40.00           O  
ANISOU 4816  OD2 ASP B 302     2783   4343   8070   -119     57      9       O  
ATOM   4817  N   VAL B 303     -19.765  -5.336  39.313  1.00 39.75           N  
ANISOU 4817  N   VAL B 303     2921   4234   7946    -37    206    280       N  
ATOM   4818  CA  VAL B 303     -18.399  -5.400  39.901  1.00 39.66           C  
ANISOU 4818  CA  VAL B 303     2937   4256   7875     13    185    349       C  
ATOM   4819  C   VAL B 303     -17.532  -6.224  38.949  1.00 39.60           C  
ANISOU 4819  C   VAL B 303     2934   4213   7897     41    182    362       C  
ATOM   4820  O   VAL B 303     -17.990  -7.289  38.493  1.00 39.31           O  
ANISOU 4820  O   VAL B 303     2912   4098   7922     28    232    351       O  
ATOM   4821  CB  VAL B 303     -18.416  -5.940  41.342  1.00 40.14           C  
ANISOU 4821  CB  VAL B 303     3033   4320   7898     33    238    422       C  
ATOM   4822  CG1 VAL B 303     -17.081  -5.737  42.034  1.00 40.18           C  
ANISOU 4822  CG1 VAL B 303     3052   4390   7823     83    202    487       C  
ATOM   4823  CG2 VAL B 303     -19.527  -5.306  42.162  1.00 40.22           C  
ANISOU 4823  CG2 VAL B 303     3037   4353   7889      3    261    399       C  
ATOM   4824  N   PHE B 304     -16.368  -5.671  38.595  1.00 39.63           N  
ANISOU 4824  N   PHE B 304     2924   4272   7859     71    123    376       N  
ATOM   4825  CA  PHE B 304     -15.351  -6.299  37.718  1.00 40.04           C  
ANISOU 4825  CA  PHE B 304     2974   4312   7924    112    115    394       C  
ATOM   4826  C   PHE B 304     -14.248  -6.891  38.600  1.00 41.06           C  
ANISOU 4826  C   PHE B 304     3123   4469   8007    175    129    487       C  
ATOM   4827  O   PHE B 304     -13.869  -6.265  39.611  1.00 40.78           O  
ANISOU 4827  O   PHE B 304     3082   4504   7905    181    102    525       O  
ATOM   4828  CB  PHE B 304     -14.854  -5.284  36.690  1.00 39.22           C  
ANISOU 4828  CB  PHE B 304     2832   4263   7806    103     46    352       C  
ATOM   4829  CG  PHE B 304     -15.937  -4.791  35.771  1.00 38.72           C  
ANISOU 4829  CG  PHE B 304     2750   4176   7784     54     34    269       C  
ATOM   4830  CD1 PHE B 304     -16.199  -5.437  34.574  1.00 38.73           C  
ANISOU 4830  CD1 PHE B 304     2748   4132   7835     49     47    224       C  
ATOM   4831  CD2 PHE B 304     -16.713  -3.696  36.112  1.00 38.47           C  
ANISOU 4831  CD2 PHE B 304     2705   4171   7738     18      9    235       C  
ATOM   4832  CE1 PHE B 304     -17.199  -4.985  33.726  1.00 38.47           C  
ANISOU 4832  CE1 PHE B 304     2690   4094   7832      7     30    150       C  
ATOM   4833  CE2 PHE B 304     -17.719  -3.252  35.266  1.00 38.33           C  
ANISOU 4833  CE2 PHE B 304     2664   4142   7756    -14     -1    167       C  
ATOM   4834  CZ  PHE B 304     -17.959  -3.895  34.074  1.00 38.22           C  
ANISOU 4834  CZ  PHE B 304     2638   4096   7788    -21      5    126       C  
ATOM   4835  N   TYR B 305     -13.792  -8.093  38.239  1.00 42.52           N  
ANISOU 4835  N   TYR B 305     3333   4597   8224    224    173    521       N  
ATOM   4836  CA  TYR B 305     -12.824  -8.918  39.006  1.00 44.07           C  
ANISOU 4836  CA  TYR B 305     3552   4805   8387    302    202    620       C  
ATOM   4837  C   TYR B 305     -11.764  -9.478  38.046  1.00 45.28           C  
ANISOU 4837  C   TYR B 305     3697   4955   8552    366    200    636       C  
ATOM   4838  O   TYR B 305     -12.131 -10.125  37.039  1.00 45.71           O  
ANISOU 4838  O   TYR B 305     3774   4924   8670    360    233    585       O  
ATOM   4839  CB  TYR B 305     -13.545 -10.055  39.738  1.00 44.51           C  
ANISOU 4839  CB  TYR B 305     3665   4765   8478    308    288    660       C  
ATOM   4840  CG  TYR B 305     -14.490  -9.663  40.847  1.00 44.19           C  
ANISOU 4840  CG  TYR B 305     3635   4738   8417    261    305    665       C  
ATOM   4841  CD1 TYR B 305     -14.050  -9.540  42.155  1.00 44.48           C  
ANISOU 4841  CD1 TYR B 305     3679   4841   8377    298    303    745       C  
ATOM   4842  CD2 TYR B 305     -15.841  -9.482  40.606  1.00 43.78           C  
ANISOU 4842  CD2 TYR B 305     3581   4636   8416    184    327    593       C  
ATOM   4843  CE1 TYR B 305     -14.918  -9.208  43.183  1.00 44.46           C  
ANISOU 4843  CE1 TYR B 305     3689   4853   8348    261    326    749       C  
ATOM   4844  CE2 TYR B 305     -16.721  -9.146  41.623  1.00 43.75           C  
ANISOU 4844  CE2 TYR B 305     3581   4648   8391    149    351    600       C  
ATOM   4845  CZ  TYR B 305     -16.260  -9.010  42.920  1.00 44.13           C  
ANISOU 4845  CZ  TYR B 305     3644   4760   8361    188    353    677       C  
ATOM   4846  OH  TYR B 305     -17.111  -8.680  43.940  1.00 44.14           O  
ANISOU 4846  OH  TYR B 305     3653   4783   8333    158    381    683       O  
ATOM   4847  N   LYS B 306     -10.490  -9.240  38.363  1.00 46.56           N  
ANISOU 4847  N   LYS B 306     3825   5214   8651    425    162    702       N  
ATOM   4848  CA  LYS B 306      -9.301  -9.716  37.602  1.00 47.73           C  
ANISOU 4848  CA  LYS B 306     3952   5387   8795    503    160    735       C  
ATOM   4849  C   LYS B 306      -9.256 -11.252  37.644  1.00 49.05           C  
ANISOU 4849  C   LYS B 306     4182   5446   9005    579    246    782       C  
ATOM   4850  O   LYS B 306      -9.576 -11.804  38.712  1.00 49.40           O  
ANISOU 4850  O   LYS B 306     4269   5455   9044    596    290    841       O  
ATOM   4851  CB  LYS B 306      -8.050  -9.094  38.235  1.00 48.23           C  
ANISOU 4851  CB  LYS B 306     3955   5593   8774    541    102    806       C  
ATOM   4852  CG  LYS B 306      -6.892  -8.799  37.292  1.00 48.52           C  
ANISOU 4852  CG  LYS B 306     3930   5711   8793    576     63    811       C  
ATOM   4853  CD  LYS B 306      -5.750  -8.069  37.974  1.00 48.77           C  
ANISOU 4853  CD  LYS B 306     3891   5896   8741    589     -2    875       C  
ATOM   4854  CE  LYS B 306      -4.607  -7.771  37.028  1.00 49.20           C  
ANISOU 4854  CE  LYS B 306     3874   6038   8779    617    -35    884       C  
ATOM   4855  NZ  LYS B 306      -4.985  -6.763  36.008  1.00 48.61           N  
ANISOU 4855  NZ  LYS B 306     3781   5960   8727    531    -73    797       N  
ATOM   4856  N   GLU B 307      -8.885 -11.919  36.543  1.00 49.98           N  
ANISOU 4856  N   GLU B 307     4314   5512   9163    626    275    758       N  
ATOM   4857  CA  GLU B 307      -8.742 -13.404  36.503  1.00 51.96           C  
ANISOU 4857  CA  GLU B 307     4637   5647   9456    708    362    799       C  
ATOM   4858  C   GLU B 307      -7.861 -13.851  35.331  1.00 52.57           C  
ANISOU 4858  C   GLU B 307     4708   5721   9545    784    373    785       C  
ATOM   4859  O   GLU B 307      -7.805 -13.133  34.331  1.00 52.11           O  
ANISOU 4859  O   GLU B 307     4604   5711   9483    744    326    714       O  
ATOM   4860  CB  GLU B 307     -10.113 -14.078  36.396  1.00 52.89           C  
ANISOU 4860  CB  GLU B 307     4829   5612   9652    638    424    738       C  
ATOM   4861  CG  GLU B 307     -10.129 -15.520  36.888  1.00 54.42           C  
ANISOU 4861  CG  GLU B 307     5112   5678   9886    705    519    804       C  
ATOM   4862  CD  GLU B 307     -10.027 -15.688  38.398  1.00 55.33           C  
ANISOU 4862  CD  GLU B 307     5241   5821   9958    740    540    917       C  
ATOM   4863  OE1 GLU B 307      -9.574 -14.743  39.079  1.00 55.21           O  
ANISOU 4863  OE1 GLU B 307     5161   5948   9868    741    474    956       O  
ATOM   4864  OE2 GLU B 307     -10.406 -16.764  38.896  1.00 56.44           O  
ANISOU 4864  OE2 GLU B 307     5463   5841  10139    764    624    965       O  
ATOM   4865  N   ASN B 308      -7.202 -15.008  35.480  1.00 53.95           N  
ANISOU 4865  N   ASN B 308     4929   5839   9728    899    439    857       N  
ATOM   4866  CA  ASN B 308      -6.409 -15.712  34.431  1.00 54.55           C  
ANISOU 4866  CA  ASN B 308     5020   5885   9820    994    475    848       C  
ATOM   4867  C   ASN B 308      -7.014 -17.106  34.192  1.00 55.11           C  
ANISOU 4867  C   ASN B 308     5209   5760   9967   1019    574    823       C  
ATOM   4868  O   ASN B 308      -7.397 -17.405  33.039  1.00 54.54           O  
ANISOU 4868  O   ASN B 308     5173   5607   9940    989    594    722       O  
ATOM   4869  CB  ASN B 308      -4.928 -15.830  34.823  1.00 55.53           C  
ANISOU 4869  CB  ASN B 308     5089   6127   9881   1128    467    963       C  
ATOM   4870  CG  ASN B 308      -3.984 -15.064  33.916  1.00 55.55           C  
ANISOU 4870  CG  ASN B 308     4998   6267   9841   1147    410    944       C  
ATOM   4871  OD1 ASN B 308      -3.222 -14.212  34.372  1.00 55.69           O  
ANISOU 4871  OD1 ASN B 308     4922   6443   9793   1149    343    999       O  
ATOM   4872  ND2 ASN B 308      -4.013 -15.370  32.628  1.00 55.20           N  
ANISOU 4872  ND2 ASN B 308     4977   6165   9830   1159    436    866       N  
ATOM   4873  N   SER B 309      -7.079 -17.921  35.251  1.00 55.66           N  
ANISOU 4873  N   SER B 309     5341   5758  10049   1069    634    913       N  
ATOM   4874  CA  SER B 309      -7.480 -19.352  35.224  1.00 56.86           C  
ANISOU 4874  CA  SER B 309     5617   5714  10272   1109    740    919       C  
ATOM   4875  C   SER B 309      -7.957 -19.772  36.621  1.00 57.44           C  
ANISOU 4875  C   SER B 309     5738   5735  10350   1103    783   1012       C  
ATOM   4876  O   SER B 309      -7.121 -19.787  37.548  1.00 57.40           O  
ANISOU 4876  O   SER B 309     5706   5819  10284   1202    777   1137       O  
ATOM   4877  CB  SER B 309      -6.328 -20.209  34.741  1.00 57.99           C  
ANISOU 4877  CB  SER B 309     5790   5831  10410   1269    791    969       C  
ATOM   4878  OG  SER B 309      -6.789 -21.390  34.100  1.00 58.80           O  
ANISOU 4878  OG  SER B 309     6014   5733  10591   1279    881    910       O  
ATOM   4879  N   TYR B 310      -9.253 -20.067  36.777  1.00 57.79           N  
ANISOU 4879  N   TYR B 310     5844   5654  10458    989    822    957       N  
ATOM   4880  CA  TYR B 310      -9.829 -20.627  38.029  1.00 59.05           C  
ANISOU 4880  CA  TYR B 310     6065   5739  10632    977    883   1044       C  
ATOM   4881  C   TYR B 310     -10.230 -22.088  37.827  1.00 60.31           C  
ANISOU 4881  C   TYR B 310     6358   5676  10879    996    998   1044       C  
ATOM   4882  O   TYR B 310     -10.613 -22.463  36.705  1.00 60.60           O  
ANISOU 4882  O   TYR B 310     6437   5609  10979    947   1019    930       O  
ATOM   4883  CB  TYR B 310     -11.063 -19.863  38.510  1.00 58.61           C  
ANISOU 4883  CB  TYR B 310     5975   5711  10582    827    851    993       C  
ATOM   4884  CG  TYR B 310     -11.560 -20.336  39.853  1.00 59.83           C  
ANISOU 4884  CG  TYR B 310     6179   5816  10735    822    911   1092       C  
ATOM   4885  CD1 TYR B 310     -10.835 -20.093  41.010  1.00 60.27           C  
ANISOU 4885  CD1 TYR B 310     6205   5988  10705    909    893   1220       C  
ATOM   4886  CD2 TYR B 310     -12.731 -21.067  39.969  1.00 61.14           C  
ANISOU 4886  CD2 TYR B 310     6421   5825  10981    730    990   1063       C  
ATOM   4887  CE1 TYR B 310     -11.272 -20.536  42.249  1.00 61.24           C  
ANISOU 4887  CE1 TYR B 310     6377   6074  10817    912    951   1318       C  
ATOM   4888  CE2 TYR B 310     -13.188 -21.513  41.202  1.00 62.10           C  
ANISOU 4888  CE2 TYR B 310     6590   5903  11100    725   1053   1163       C  
ATOM   4889  CZ  TYR B 310     -12.454 -21.250  42.346  1.00 62.07           C  
ANISOU 4889  CZ  TYR B 310     6560   6018  11005    821   1035   1293       C  
ATOM   4890  OH  TYR B 310     -12.894 -21.688  43.561  1.00 62.58           O  
ANISOU 4890  OH  TYR B 310     6672   6048  11056    821   1099   1396       O  
ATOM   4891  N   THR B 311     -10.134 -22.877  38.899  1.00 61.25           N  
ANISOU 4891  N   THR B 311     6546   5727  10999   1063   1071   1170       N  
ATOM   4892  CA  THR B 311     -10.716 -24.241  39.008  1.00 62.82           C  
ANISOU 4892  CA  THR B 311     6883   5697  11286   1057   1191   1189       C  
ATOM   4893  C   THR B 311     -11.116 -24.480  40.471  1.00 63.85           C  
ANISOU 4893  C   THR B 311     7045   5816  11399   1054   1238   1316       C  
ATOM   4894  O   THR B 311     -10.360 -24.059  41.376  1.00 63.83           O  
ANISOU 4894  O   THR B 311     6987   5959  11305   1148   1201   1432       O  
ATOM   4895  CB  THR B 311      -9.769 -25.304  38.435  1.00 63.72           C  
ANISOU 4895  CB  THR B 311     7083   5701  11426   1208   1259   1222       C  
ATOM   4896  OG1 THR B 311      -9.217 -24.828  37.206  1.00 62.70           O  
ANISOU 4896  OG1 THR B 311     6896   5645  11281   1228   1199   1121       O  
ATOM   4897  CG2 THR B 311     -10.465 -26.623  38.181  1.00 65.08           C  
ANISOU 4897  CG2 THR B 311     7408   5615  11704   1171   1377   1192       C  
ATOM   4898  N   THR B 312     -12.282 -25.099  40.686  1.00 64.83           N  
ANISOU 4898  N   THR B 312     7247   5783  11601    942   1314   1292       N  
ATOM   4899  CA  THR B 312     -12.896 -25.340  42.019  1.00 65.57           C  
ANISOU 4899  CA  THR B 312     7373   5853  11686    911   1369   1400       C  
ATOM   4900  C   THR B 312     -12.286 -26.586  42.662  1.00 67.61           C  
ANISOU 4900  C   THR B 312     7749   5982  11955   1052   1475   1552       C  
ATOM   4901  O   THR B 312     -11.874 -27.494  41.912  1.00 68.73           O  
ANISOU 4901  O   THR B 312     7980   5976  12156   1120   1534   1533       O  
ATOM   4902  CB  THR B 312     -14.413 -25.533  41.924  1.00 65.66           C  
ANISOU 4902  CB  THR B 312     7416   5747  11784    725   1415   1314       C  
ATOM   4903  OG1 THR B 312     -14.901 -25.558  43.266  1.00 65.90           O  
ANISOU 4903  OG1 THR B 312     7454   5800  11785    705   1457   1426       O  
ATOM   4904  CG2 THR B 312     -14.815 -26.801  41.198  1.00 67.05           C  
ANISOU 4904  CG2 THR B 312     7719   5681  12076    686   1514   1260       C  
ATOM   4905  N   THR B 313     -12.273 -26.632  43.998  1.00 68.47           N  
ANISOU 4905  N   THR B 313     7864   6143  12007   1096   1502   1695       N  
ATOM   4906  CA  THR B 313     -11.871 -27.819  44.800  1.00 70.59           C  
ANISOU 4906  CA  THR B 313     8251   6287  12283   1223   1613   1861       C  
ATOM   4907  C   THR B 313     -13.127 -28.597  45.230  1.00 72.37           C  
ANISOU 4907  C   THR B 313     8577   6323  12596   1098   1724   1874       C  
ATOM   4908  O   THR B 313     -12.976 -29.541  46.033  1.00 74.43           O  
ANISOU 4908  O   THR B 313     8941   6474  12862   1183   1824   2022       O  
ATOM   4909  CB  THR B 313     -10.970 -27.411  45.975  1.00 70.34           C  
ANISOU 4909  CB  THR B 313     8160   6445  12120   1363   1571   2019       C  
ATOM   4910  OG1 THR B 313     -11.730 -26.639  46.903  1.00 69.17           O  
ANISOU 4910  OG1 THR B 313     7951   6413  11918   1260   1538   2032       O  
ATOM   4911  CG2 THR B 313      -9.757 -26.618  45.536  1.00 69.40           C  
ANISOU 4911  CG2 THR B 313     7929   6519  11918   1467   1460   2002       C  
ATOM   4912  N   ILE B 314     -14.312 -28.225  44.717  1.00 72.04           N  
ANISOU 4912  N   ILE B 314     8505   6248  12618    906   1709   1731       N  
ATOM   4913  CA  ILE B 314     -15.587 -28.995  44.864  1.00 73.11           C  
ANISOU 4913  CA  ILE B 314     8727   6193  12857    757   1813   1712       C  
ATOM   4914  C   ILE B 314     -15.602 -30.104  43.804  1.00 74.31           C  
ANISOU 4914  C   ILE B 314     9001   6107  13124    745   1888   1637       C  
ATOM   4915  O   ILE B 314     -15.581 -29.833  42.601  1.00 73.21           O  
ANISOU 4915  O   ILE B 314     8831   5968  13017    700   1831   1485       O  
ATOM   4916  CB  ILE B 314     -16.823 -28.078  44.747  1.00 72.04           C  
ANISOU 4916  CB  ILE B 314     8489   6147  12735    563   1758   1590       C  
ATOM   4917  CG1 ILE B 314     -16.943 -27.125  45.940  1.00 71.39           C  
ANISOU 4917  CG1 ILE B 314     8313   6266  12544    571   1710   1672       C  
ATOM   4918  CG2 ILE B 314     -18.093 -28.898  44.558  1.00 73.12           C  
ANISOU 4918  CG2 ILE B 314     8702   6086  12993    395   1857   1537       C  
ATOM   4919  CD1 ILE B 314     -17.991 -26.044  45.761  1.00 70.03           C  
ANISOU 4919  CD1 ILE B 314     8026   6211  12369    412   1641   1549       C  
TER    4920      ILE B 314                                                      
ATOM   4921  N   THR C   4     -34.811 -12.416  -8.294  1.00 88.93           N  
ANISOU 4921  N   THR C   4     9153  12305  12331     19   -686  -1043       N  
ATOM   4922  CA  THR C   4     -36.036 -11.797  -7.700  1.00 88.03           C  
ANISOU 4922  CA  THR C   4     9096  12061  12289    -32   -724   -917       C  
ATOM   4923  C   THR C   4     -36.726 -12.817  -6.785  1.00 86.25           C  
ANISOU 4923  C   THR C   4     8942  11655  12174     29   -764   -961       C  
ATOM   4924  O   THR C   4     -36.937 -13.953  -7.244  1.00 86.03           O  
ANISOU 4924  O   THR C   4     8942  11610  12132     68   -775  -1073       O  
ATOM   4925  CB  THR C   4     -36.986 -11.283  -8.792  1.00 89.04           C  
ANISOU 4925  CB  THR C   4     9233  12259  12336   -112   -741   -856       C  
ATOM   4926  OG1 THR C   4     -37.601 -12.413  -9.411  1.00 90.01           O  
ANISOU 4926  OG1 THR C   4     9383  12376  12437    -88   -769   -964       O  
ATOM   4927  CG2 THR C   4     -36.298 -10.438  -9.843  1.00 90.42           C  
ANISOU 4927  CG2 THR C   4     9354  12616  12383   -172   -697   -821       C  
ATOM   4928  N   ILE C   5     -37.064 -12.423  -5.549  1.00 85.09           N  
ANISOU 4928  N   ILE C   5     8825  11375  12127     31   -780   -878       N  
ATOM   4929  CA  ILE C   5     -37.612 -13.326  -4.486  1.00 85.02           C  
ANISOU 4929  CA  ILE C   5     8889  11187  12225     87   -809   -907       C  
ATOM   4930  C   ILE C   5     -39.117 -13.076  -4.337  1.00 83.84           C  
ANISOU 4930  C   ILE C   5     8788  10947  12120     20   -846   -834       C  
ATOM   4931  O   ILE C   5     -39.640 -12.221  -5.073  1.00 83.88           O  
ANISOU 4931  O   ILE C   5     8766  11035  12067    -51   -853   -765       O  
ATOM   4932  CB  ILE C   5     -36.869 -13.150  -3.143  1.00 85.16           C  
ANISOU 4932  CB  ILE C   5     8903  11134  12318    146   -799   -878       C  
ATOM   4933  CG1 ILE C   5     -37.038 -11.743  -2.557  1.00 84.08           C  
ANISOU 4933  CG1 ILE C   5     8740  10994  12211     78   -796   -743       C  
ATOM   4934  CG2 ILE C   5     -35.403 -13.538  -3.288  1.00 86.28           C  
ANISOU 4934  CG2 ILE C   5     8988  11378  12413    227   -768   -971       C  
ATOM   4935  CD1 ILE C   5     -36.776 -11.659  -1.068  1.00 82.67           C  
ANISOU 4935  CD1 ILE C   5     8577  10710  12124    125   -801   -710       C  
ATOM   4936  N   LYS C   6     -39.770 -13.790  -3.409  1.00 82.55           N  
ANISOU 4936  N   LYS C   6     8693  10625  12048     44   -867   -848       N  
ATOM   4937  CA  LYS C   6     -41.245 -13.760  -3.203  1.00 81.46           C  
ANISOU 4937  CA  LYS C   6     8595  10400  11954    -17   -900   -805       C  
ATOM   4938  C   LYS C   6     -41.567 -13.464  -1.730  1.00 78.24           C  
ANISOU 4938  C   LYS C   6     8222   9854  11651     -9   -908   -727       C  
ATOM   4939  O   LYS C   6     -41.457 -14.388  -0.904  1.00 77.04           O  
ANISOU 4939  O   LYS C   6     8130   9579  11559     42   -904   -775       O  
ATOM   4940  CB  LYS C   6     -41.849 -15.087  -3.674  1.00 83.17           C  
ANISOU 4940  CB  LYS C   6     8866  10568  12167    -17   -909   -923       C  
ATOM   4941  CG  LYS C   6     -43.337 -15.028  -3.985  1.00 84.61           C  
ANISOU 4941  CG  LYS C   6     9058  10738  12352   -101   -940   -907       C  
ATOM   4942  CD  LYS C   6     -43.776 -15.901  -5.147  1.00 86.84           C  
ANISOU 4942  CD  LYS C   6     9346  11082  12568   -130   -946  -1026       C  
ATOM   4943  CE  LYS C   6     -44.973 -15.331  -5.887  1.00 87.82           C  
ANISOU 4943  CE  LYS C   6     9427  11299  12640   -211   -981   -991       C  
ATOM   4944  NZ  LYS C   6     -45.951 -16.374  -6.285  1.00 88.89           N  
ANISOU 4944  NZ  LYS C   6     9593  11406  12775   -262   -993  -1104       N  
ATOM   4945  N   VAL C   7     -41.964 -12.222  -1.427  1.00 76.04           N  
ANISOU 4945  N   VAL C   7     7913   9592  11387    -57   -917   -612       N  
ATOM   4946  CA  VAL C   7     -42.316 -11.743  -0.054  1.00 75.22           C  
ANISOU 4946  CA  VAL C   7     7830   9374  11376    -58   -924   -532       C  
ATOM   4947  C   VAL C   7     -43.692 -11.055  -0.101  1.00 74.47           C  
ANISOU 4947  C   VAL C   7     7731   9264  11296   -127   -954   -458       C  
ATOM   4948  O   VAL C   7     -44.386 -11.200  -1.133  1.00 75.73           O  
ANISOU 4948  O   VAL C   7     7879   9493  11399   -164   -973   -485       O  
ATOM   4949  CB  VAL C   7     -41.220 -10.821   0.524  1.00 74.95           C  
ANISOU 4949  CB  VAL C   7     7754   9374  11349    -35   -900   -474       C  
ATOM   4950  CG1 VAL C   7     -39.862 -11.503   0.536  1.00 75.56           C  
ANISOU 4950  CG1 VAL C   7     7818   9489  11401     41   -875   -557       C  
ATOM   4951  CG2 VAL C   7     -41.141  -9.483  -0.197  1.00 74.79           C  
ANISOU 4951  CG2 VAL C   7     7682   9462  11272    -93   -891   -392       C  
ATOM   4952  N   PHE C   8     -44.080 -10.352   0.973  1.00 72.15           N  
ANISOU 4952  N   PHE C   8     7442   8895  11074   -138   -960   -376       N  
ATOM   4953  CA  PHE C   8     -45.421  -9.728   1.139  1.00 70.08           C  
ANISOU 4953  CA  PHE C   8     7175   8610  10840   -188   -990   -312       C  
ATOM   4954  C   PHE C   8     -45.304  -8.257   1.557  1.00 66.57           C  
ANISOU 4954  C   PHE C   8     6703   8177  10414   -198   -987   -199       C  
ATOM   4955  O   PHE C   8     -44.467  -7.944   2.420  1.00 65.25           O  
ANISOU 4955  O   PHE C   8     6535   7969  10286   -173   -963   -176       O  
ATOM   4956  CB  PHE C   8     -46.246 -10.481   2.187  1.00 70.95           C  
ANISOU 4956  CB  PHE C   8     7332   8593  11031   -196   -998   -338       C  
ATOM   4957  CG  PHE C   8     -46.719 -11.853   1.780  1.00 72.72           C  
ANISOU 4957  CG  PHE C   8     7598   8787  11245   -210  -1001   -444       C  
ATOM   4958  CD1 PHE C   8     -47.259 -12.082   0.522  1.00 74.35           C  
ANISOU 4958  CD1 PHE C   8     7779   9087  11381   -246  -1019   -494       C  
ATOM   4959  CD2 PHE C   8     -46.661 -12.912   2.674  1.00 73.45           C  
ANISOU 4959  CD2 PHE C   8     7760   8752  11395   -191   -984   -494       C  
ATOM   4960  CE1 PHE C   8     -47.708 -13.343   0.163  1.00 75.68           C  
ANISOU 4960  CE1 PHE C   8     7987   9224  11543   -271  -1016   -603       C  
ATOM   4961  CE2 PHE C   8     -47.110 -14.173   2.312  1.00 74.59           C  
ANISOU 4961  CE2 PHE C   8     7956   8850  11534   -214   -979   -594       C  
ATOM   4962  CZ  PHE C   8     -47.633 -14.386   1.058  1.00 75.64           C  
ANISOU 4962  CZ  PHE C   8     8058   9077  11602   -258   -994   -653       C  
ATOM   4963  N   THR C   9     -46.149  -7.404   0.966  1.00 64.16           N  
ANISOU 4963  N   THR C   9     6376   7924  10078   -229  -1012   -136       N  
ATOM   4964  CA  THR C   9     -46.373  -5.982   1.346  1.00 62.06           C  
ANISOU 4964  CA  THR C   9     6098   7645   9835   -239  -1014    -25       C  
ATOM   4965  C   THR C   9     -47.821  -5.834   1.840  1.00 61.38           C  
ANISOU 4965  C   THR C   9     6012   7509   9799   -250  -1052     -1       C  
ATOM   4966  O   THR C   9     -48.684  -6.608   1.372  1.00 61.39           O  
ANISOU 4966  O   THR C   9     6008   7537   9780   -265  -1079    -60       O  
ATOM   4967  CB  THR C   9     -46.023  -5.041   0.184  1.00 61.68           C  
ANISOU 4967  CB  THR C   9     6034   7702   9697   -251  -1008     35       C  
ATOM   4968  OG1 THR C   9     -47.082  -4.997  -0.769  1.00 61.69           O  
ANISOU 4968  OG1 THR C   9     6026   7773   9640   -259  -1049     45       O  
ATOM   4969  CG2 THR C   9     -44.763  -5.452  -0.541  1.00 62.25           C  
ANISOU 4969  CG2 THR C   9     6096   7854   9701   -249   -973    -15       C  
ATOM   4970  N   THR C  10     -48.069  -4.893   2.762  1.00 60.39           N  
ANISOU 4970  N   THR C  10     5887   7320   9736   -247  -1051     71       N  
ATOM   4971  CA  THR C  10     -49.397  -4.621   3.387  1.00 59.67           C  
ANISOU 4971  CA  THR C  10     5786   7185   9699   -252  -1082     95       C  
ATOM   4972  C   THR C  10     -49.337  -3.300   4.164  1.00 58.42           C  
ANISOU 4972  C   THR C  10     5630   6974   9592   -241  -1072    185       C  
ATOM   4973  O   THR C  10     -48.249  -2.982   4.673  1.00 57.50           O  
ANISOU 4973  O   THR C  10     5527   6823   9497   -239  -1035    202       O  
ATOM   4974  CB  THR C  10     -49.817  -5.773   4.313  1.00 59.51           C  
ANISOU 4974  CB  THR C  10     5781   7087   9740   -266  -1079     20       C  
ATOM   4975  OG1 THR C  10     -51.128  -5.537   4.828  1.00 58.79           O  
ANISOU 4975  OG1 THR C  10     5670   6975   9691   -281  -1106     33       O  
ATOM   4976  CG2 THR C  10     -48.859  -5.967   5.469  1.00 59.07           C  
ANISOU 4976  CG2 THR C  10     5755   6946   9743   -250  -1044     17       C  
ATOM   4977  N   VAL C  11     -50.460  -2.572   4.252  1.00 58.08           N  
ANISOU 4977  N   VAL C  11     5571   6929   9565   -231  -1105    233       N  
ATOM   4978  CA  VAL C  11     -50.610  -1.344   5.098  1.00 56.97           C  
ANISOU 4978  CA  VAL C  11     5437   6723   9484   -215  -1098    309       C  
ATOM   4979  C   VAL C  11     -51.267  -1.719   6.428  1.00 55.70           C  
ANISOU 4979  C   VAL C  11     5265   6488   9408   -221  -1100    274       C  
ATOM   4980  O   VAL C  11     -50.965  -1.044   7.420  1.00 54.90           O  
ANISOU 4980  O   VAL C  11     5173   6318   9366   -216  -1078    307       O  
ATOM   4981  CB  VAL C  11     -51.400  -0.216   4.405  1.00 57.57           C  
ANISOU 4981  CB  VAL C  11     5510   6839   9524   -183  -1131    388       C  
ATOM   4982  CG1 VAL C  11     -50.695   0.278   3.154  1.00 58.33           C  
ANISOU 4982  CG1 VAL C  11     5630   7000   9531   -181  -1121    439       C  
ATOM   4983  CG2 VAL C  11     -52.835  -0.606   4.093  1.00 58.31           C  
ANISOU 4983  CG2 VAL C  11     5562   6991   9602   -167  -1184    355       C  
ATOM   4984  N   ASP C  12     -52.121  -2.749   6.435  1.00 55.77           N  
ANISOU 4984  N   ASP C  12     5255   6514   9417   -239  -1121    205       N  
ATOM   4985  CA  ASP C  12     -52.968  -3.140   7.595  1.00 55.72           C  
ANISOU 4985  CA  ASP C  12     5236   6452   9480   -256  -1122    171       C  
ATOM   4986  C   ASP C  12     -52.553  -4.505   8.162  1.00 55.48           C  
ANISOU 4986  C   ASP C  12     5238   6369   9469   -287  -1095     98       C  
ATOM   4987  O   ASP C  12     -53.056  -4.844   9.250  1.00 55.18           O  
ANISOU 4987  O   ASP C  12     5205   6273   9487   -307  -1084     77       O  
ATOM   4988  CB  ASP C  12     -54.455  -3.154   7.220  1.00 56.67           C  
ANISOU 4988  CB  ASP C  12     5307   6637   9584   -261  -1165    150       C  
ATOM   4989  CG  ASP C  12     -54.801  -3.926   5.954  1.00 57.53           C  
ANISOU 4989  CG  ASP C  12     5399   6841   9617   -279  -1191     95       C  
ATOM   4990  OD1 ASP C  12     -53.869  -4.453   5.302  1.00 57.59           O  
ANISOU 4990  OD1 ASP C  12     5438   6861   9583   -286  -1174     75       O  
ATOM   4991  OD2 ASP C  12     -56.007  -3.982   5.621  1.00 58.05           O  
ANISOU 4991  OD2 ASP C  12     5413   6979   9663   -286  -1227     66       O  
ATOM   4992  N   ASN C  13     -51.702  -5.266   7.460  1.00 55.82           N  
ANISOU 4992  N   ASN C  13     5308   6433   9467   -288  -1083     60       N  
ATOM   4993  CA  ASN C  13     -51.275  -6.636   7.865  1.00 55.94           C  
ANISOU 4993  CA  ASN C  13     5369   6391   9494   -302  -1059    -11       C  
ATOM   4994  C   ASN C  13     -52.502  -7.560   7.938  1.00 56.18           C  
ANISOU 4994  C   ASN C  13     5400   6412   9534   -354  -1068    -75       C  
ATOM   4995  O   ASN C  13     -52.488  -8.508   8.752  1.00 56.32           O  
ANISOU 4995  O   ASN C  13     5465   6345   9586   -375  -1043   -116       O  
ATOM   4996  CB  ASN C  13     -50.516  -6.614   9.196  1.00 55.84           C  
ANISOU 4996  CB  ASN C  13     5387   6292   9536   -281  -1028      7       C  
ATOM   4997  CG  ASN C  13     -49.886  -7.943   9.557  1.00 56.16           C  
ANISOU 4997  CG  ASN C  13     5486   6271   9578   -271  -1005    -51       C  
ATOM   4998  OD1 ASN C  13     -49.475  -8.705   8.684  1.00 56.76           O  
ANISOU 4998  OD1 ASN C  13     5581   6373   9609   -265  -1004   -102       O  
ATOM   4999  ND2 ASN C  13     -49.805  -8.227  10.847  1.00 56.01           N  
ANISOU 4999  ND2 ASN C  13     5502   6172   9607   -264   -986    -46       N  
ATOM   5000  N   ILE C  14     -53.527  -7.281   7.124  1.00 55.43           N  
ANISOU 5000  N   ILE C  14     5253   6402   9405   -374  -1102    -84       N  
ATOM   5001  CA  ILE C  14     -54.733  -8.138   6.933  1.00 54.67           C  
ANISOU 5001  CA  ILE C  14     5138   6331   9301   -436  -1113   -163       C  
ATOM   5002  C   ILE C  14     -54.873  -8.436   5.437  1.00 54.85           C  
ANISOU 5002  C   ILE C  14     5135   6461   9243   -444  -1140   -208       C  
ATOM   5003  O   ILE C  14     -55.044  -9.620   5.089  1.00 55.13           O  
ANISOU 5003  O   ILE C  14     5196   6490   9261   -493  -1128   -298       O  
ATOM   5004  CB  ILE C  14     -55.979  -7.455   7.532  1.00 54.53           C  
ANISOU 5004  CB  ILE C  14     5063   6338   9318   -451  -1133   -142       C  
ATOM   5005  CG1 ILE C  14     -55.883  -7.390   9.061  1.00 53.52           C  
ANISOU 5005  CG1 ILE C  14     4964   6104   9265   -457  -1100   -116       C  
ATOM   5006  CG2 ILE C  14     -57.253  -8.135   7.049  1.00 55.51           C  
ANISOU 5006  CG2 ILE C  14     5140   6535   9415   -517  -1151   -227       C  
ATOM   5007  CD1 ILE C  14     -57.206  -7.453   9.797  1.00 53.31           C  
ANISOU 5007  CD1 ILE C  14     4896   6086   9273   -508  -1100   -147       C  
ATOM   5008  N   ASN C  15     -54.801  -7.400   4.595  1.00 54.71           N  
ANISOU 5008  N   ASN C  15     5077   6535   9175   -398  -1172   -147       N  
ATOM   5009  CA  ASN C  15     -54.765  -7.510   3.112  1.00 55.54           C  
ANISOU 5009  CA  ASN C  15     5157   6757   9187   -393  -1199   -173       C  
ATOM   5010  C   ASN C  15     -53.304  -7.698   2.687  1.00 55.68           C  
ANISOU 5010  C   ASN C  15     5223   6756   9175   -366  -1170   -165       C  
ATOM   5011  O   ASN C  15     -52.557  -6.700   2.715  1.00 56.02           O  
ANISOU 5011  O   ASN C  15     5272   6797   9215   -323  -1163    -79       O  
ATOM   5012  CB  ASN C  15     -55.423  -6.298   2.443  1.00 55.71           C  
ANISOU 5012  CB  ASN C  15     5122   6885   9160   -350  -1247   -103       C  
ATOM   5013  CG  ASN C  15     -56.874  -6.119   2.841  1.00 55.85           C  
ANISOU 5013  CG  ASN C  15     5077   6941   9201   -365  -1279   -123       C  
ATOM   5014  OD1 ASN C  15     -57.782  -6.431   2.071  1.00 56.37           O  
ANISOU 5014  OD1 ASN C  15     5087   7120   9210   -385  -1316   -182       O  
ATOM   5015  ND2 ASN C  15     -57.105  -5.635   4.050  1.00 54.83           N  
ANISOU 5015  ND2 ASN C  15     4951   6730   9152   -357  -1266    -84       N  
ATOM   5016  N   LEU C  16     -52.917  -8.933   2.335  1.00 56.01           N  
ANISOU 5016  N   LEU C  16     5298   6784   9198   -392  -1150   -257       N  
ATOM   5017  CA  LEU C  16     -51.506  -9.354   2.110  1.00 55.74           C  
ANISOU 5017  CA  LEU C  16     5310   6724   9146   -362  -1117   -273       C  
ATOM   5018  C   LEU C  16     -51.228  -9.457   0.610  1.00 56.94           C  
ANISOU 5018  C   LEU C  16     5438   6999   9196   -358  -1131   -305       C  
ATOM   5019  O   LEU C  16     -51.612 -10.467  -0.003  1.00 57.34           O  
ANISOU 5019  O   LEU C  16     5491   7080   9213   -393  -1136   -405       O  
ATOM   5020  CB  LEU C  16     -51.253 -10.697   2.802  1.00 55.57           C  
ANISOU 5020  CB  LEU C  16     5351   6589   9171   -380  -1084   -355       C  
ATOM   5021  CG  LEU C  16     -51.351 -10.688   4.327  1.00 54.86           C  
ANISOU 5021  CG  LEU C  16     5296   6375   9171   -379  -1063   -320       C  
ATOM   5022  CD1 LEU C  16     -51.055 -12.065   4.891  1.00 55.06           C  
ANISOU 5022  CD1 LEU C  16     5404   6287   9230   -388  -1030   -394       C  
ATOM   5023  CD2 LEU C  16     -50.414  -9.655   4.936  1.00 54.28           C  
ANISOU 5023  CD2 LEU C  16     5217   6285   9122   -325  -1053   -229       C  
ATOM   5024  N   HIS C  17     -50.536  -8.457   0.063  1.00 58.33           N  
ANISOU 5024  N   HIS C  17     5596   7241   9323   -323  -1132   -228       N  
ATOM   5025  CA  HIS C  17     -50.240  -8.311  -1.386  1.00 60.18           C  
ANISOU 5025  CA  HIS C  17     5807   7609   9447   -317  -1144   -236       C  
ATOM   5026  C   HIS C  17     -48.897  -8.982  -1.689  1.00 61.49           C  
ANISOU 5026  C   HIS C  17     6000   7774   9587   -301  -1104   -292       C  
ATOM   5027  O   HIS C  17     -47.931  -8.722  -0.943  1.00 61.22           O  
ANISOU 5027  O   HIS C  17     5987   7675   9599   -275  -1071   -257       O  
ATOM   5028  CB  HIS C  17     -50.307  -6.829  -1.780  1.00 60.05           C  
ANISOU 5028  CB  HIS C  17     5769   7657   9389   -292  -1162   -113       C  
ATOM   5029  CG  HIS C  17     -51.579  -6.175  -1.351  1.00 59.87           C  
ANISOU 5029  CG  HIS C  17     5721   7626   9401   -288  -1201    -62       C  
ATOM   5030  ND1 HIS C  17     -52.647  -6.000  -2.207  1.00 60.29           N  
ANISOU 5030  ND1 HIS C  17     5730   7790   9385   -286  -1252    -66       N  
ATOM   5031  CD2 HIS C  17     -51.970  -5.688  -0.153  1.00 59.05           C  
ANISOU 5031  CD2 HIS C  17     5621   7425   9388   -281  -1200    -16       C  
ATOM   5032  CE1 HIS C  17     -53.632  -5.413  -1.558  1.00 60.18           C  
ANISOU 5032  CE1 HIS C  17     5693   7750   9420   -272  -1280    -24       C  
ATOM   5033  NE2 HIS C  17     -53.243  -5.215  -0.296  1.00 59.08           N  
ANISOU 5033  NE2 HIS C  17     5584   7481   9381   -272  -1247      6       N  
ATOM   5034  N   THR C  18     -48.857  -9.815  -2.735  1.00 63.51           N  
ANISOU 5034  N   THR C  18     6250   8109   9771   -313  -1107   -384       N  
ATOM   5035  CA  THR C  18     -47.717 -10.704  -3.090  1.00 64.98           C  
ANISOU 5035  CA  THR C  18     6460   8299   9930   -293  -1072   -469       C  
ATOM   5036  C   THR C  18     -46.862 -10.005  -4.152  1.00 66.46           C  
ANISOU 5036  C   THR C  18     6615   8617  10016   -278  -1061   -430       C  
ATOM   5037  O   THR C  18     -47.431  -9.559  -5.166  1.00 67.04           O  
ANISOU 5037  O   THR C  18     6658   8808  10005   -297  -1089   -406       O  
ATOM   5038  CB  THR C  18     -48.217 -12.083  -3.543  1.00 65.84           C  
ANISOU 5038  CB  THR C  18     6587   8404  10025   -321  -1077   -605       C  
ATOM   5039  OG1 THR C  18     -48.520 -12.039  -4.938  1.00 66.33           O  
ANISOU 5039  OG1 THR C  18     6606   8618   9976   -341  -1099   -640       O  
ATOM   5040  CG2 THR C  18     -49.437 -12.539  -2.770  1.00 65.82           C  
ANISOU 5040  CG2 THR C  18     6602   8309  10096   -365  -1093   -631       C  
ATOM   5041  N   GLN C  19     -45.551  -9.916  -3.920  1.00 67.24           N  
ANISOU 5041  N   GLN C  19     6720   8706  10119   -247  -1020   -425       N  
ATOM   5042  CA  GLN C  19     -44.626  -9.091  -4.739  1.00 68.95           C  
ANISOU 5042  CA  GLN C  19     6909   9041  10248   -246   -996   -375       C  
ATOM   5043  C   GLN C  19     -43.339  -9.879  -5.034  1.00 70.51           C  
ANISOU 5043  C   GLN C  19     7100   9278  10413   -215   -956   -471       C  
ATOM   5044  O   GLN C  19     -42.902 -10.661  -4.163  1.00 69.42           O  
ANISOU 5044  O   GLN C  19     6986   9040  10348   -176   -942   -531       O  
ATOM   5045  CB  GLN C  19     -44.369  -7.777  -3.999  1.00 68.14           C  
ANISOU 5045  CB  GLN C  19     6806   8895  10189   -250   -982   -248       C  
ATOM   5046  CG  GLN C  19     -45.596  -6.878  -3.898  1.00 67.46           C  
ANISOU 5046  CG  GLN C  19     6724   8791  10118   -268  -1022   -150       C  
ATOM   5047  CD  GLN C  19     -45.428  -5.579  -4.648  1.00 68.12           C  
ANISOU 5047  CD  GLN C  19     6803   8957  10123   -283  -1015    -39       C  
ATOM   5048  OE1 GLN C  19     -44.894  -5.538  -5.755  1.00 68.36           O  
ANISOU 5048  OE1 GLN C  19     6821   9104  10047   -294   -998    -49       O  
ATOM   5049  NE2 GLN C  19     -45.887  -4.497  -4.040  1.00 67.95           N  
ANISOU 5049  NE2 GLN C  19     6797   8870  10149   -282  -1024     67       N  
ATOM   5050  N   VAL C  20     -42.775  -9.683  -6.233  1.00 73.04           N  
ANISOU 5050  N   VAL C  20     7389   9742  10621   -226   -939   -485       N  
ATOM   5051  CA  VAL C  20     -41.498 -10.297  -6.710  1.00 75.17           C  
ANISOU 5051  CA  VAL C  20     7636  10087  10838   -196   -898   -579       C  
ATOM   5052  C   VAL C  20     -40.448  -9.183  -6.824  1.00 76.39           C  
ANISOU 5052  C   VAL C  20     7756  10320  10948   -215   -854   -501       C  
ATOM   5053  O   VAL C  20     -40.471  -8.441  -7.829  1.00 77.50           O  
ANISOU 5053  O   VAL C  20     7879  10577  10988   -258   -846   -444       O  
ATOM   5054  CB  VAL C  20     -41.693 -11.051  -8.044  1.00 76.39           C  
ANISOU 5054  CB  VAL C  20     7776  10358  10890   -205   -906   -679       C  
ATOM   5055  CG1 VAL C  20     -40.371 -11.399  -8.715  1.00 76.95           C  
ANISOU 5055  CG1 VAL C  20     7811  10542  10884   -179   -861   -760       C  
ATOM   5056  CG2 VAL C  20     -42.539 -12.304  -7.867  1.00 76.15           C  
ANISOU 5056  CG2 VAL C  20     7783  10240  10910   -194   -936   -785       C  
ATOM   5057  N   VAL C  21     -39.561  -9.080  -5.830  1.00 77.37           N  
ANISOU 5057  N   VAL C  21     7872  10386  11139   -187   -826   -499       N  
ATOM   5058  CA  VAL C  21     -38.575  -7.965  -5.687  1.00 78.37           C  
ANISOU 5058  CA  VAL C  21     7964  10569  11243   -219   -779   -428       C  
ATOM   5059  C   VAL C  21     -37.189  -8.454  -6.116  1.00 79.73           C  
ANISOU 5059  C   VAL C  21     8083  10858  11354   -192   -733   -529       C  
ATOM   5060  O   VAL C  21     -36.866  -9.628  -5.840  1.00 79.12           O  
ANISOU 5060  O   VAL C  21     8005  10751  11306   -119   -740   -643       O  
ATOM   5061  CB  VAL C  21     -38.545  -7.401  -4.253  1.00 78.20           C  
ANISOU 5061  CB  VAL C  21     7956  10421  11333   -213   -778   -362       C  
ATOM   5062  CG1 VAL C  21     -39.831  -6.662  -3.927  1.00 77.94           C  
ANISOU 5062  CG1 VAL C  21     7965  10298  11347   -246   -815   -253       C  
ATOM   5063  CG2 VAL C  21     -38.259  -8.466  -3.201  1.00 77.71           C  
ANISOU 5063  CG2 VAL C  21     7903  10264  11356   -137   -789   -448       C  
ATOM   5064  N   ASP C  22     -36.406  -7.557  -6.730  1.00 80.96           N  
ANISOU 5064  N   ASP C  22     8197  11135  11426   -250   -684   -487       N  
ATOM   5065  CA  ASP C  22     -35.056  -7.826  -7.296  1.00 82.12           C  
ANISOU 5065  CA  ASP C  22     8276  11432  11492   -243   -631   -579       C  
ATOM   5066  C   ASP C  22     -34.001  -7.666  -6.193  1.00 82.59           C  
ANISOU 5066  C   ASP C  22     8291  11472  11615   -216   -600   -603       C  
ATOM   5067  O   ASP C  22     -34.251  -6.902  -5.235  1.00 82.19           O  
ANISOU 5067  O   ASP C  22     8263  11321  11643   -243   -605   -514       O  
ATOM   5068  CB  ASP C  22     -34.779  -6.900  -8.486  1.00 82.34           C  
ANISOU 5068  CB  ASP C  22     8285  11606  11392   -333   -587   -517       C  
ATOM   5069  CG  ASP C  22     -33.636  -7.351  -9.378  1.00 82.75           C  
ANISOU 5069  CG  ASP C  22     8266  11838  11337   -330   -537   -627       C  
ATOM   5070  OD1 ASP C  22     -33.181  -8.502  -9.222  1.00 82.35           O  
ANISOU 5070  OD1 ASP C  22     8185  11799  11306   -244   -546   -762       O  
ATOM   5071  OD2 ASP C  22     -33.216  -6.545 -10.226  1.00 83.17           O  
ANISOU 5071  OD2 ASP C  22     8300  12016  11285   -413   -487   -577       O  
ATOM   5072  N   MET C  23     -32.861  -8.349  -6.341  1.00 83.28           N  
ANISOU 5072  N   MET C  23     8314  11664  11664   -163   -571   -725       N  
ATOM   5073  CA  MET C  23     -31.771  -8.403  -5.330  1.00 82.91           C  
ANISOU 5073  CA  MET C  23     8208  11627  11664   -114   -549   -777       C  
ATOM   5074  C   MET C  23     -30.851  -7.198  -5.530  1.00 83.84           C  
ANISOU 5074  C   MET C  23     8258  11872  11723   -216   -481   -734       C  
ATOM   5075  O   MET C  23     -30.616  -6.473  -4.545  1.00 84.63           O  
ANISOU 5075  O   MET C  23     8349  11920  11887   -245   -469   -681       O  
ATOM   5076  CB  MET C  23     -30.949  -9.691  -5.456  1.00 83.51           C  
ANISOU 5076  CB  MET C  23     8239  11772  11718      1   -551   -936       C  
ATOM   5077  CG  MET C  23     -31.781 -10.933  -5.742  1.00 83.87           C  
ANISOU 5077  CG  MET C  23     8356  11726  11785     78   -600   -998       C  
ATOM   5078  SD  MET C  23     -33.167 -11.153  -4.597  1.00 82.00           S  
ANISOU 5078  SD  MET C  23     8229  11245  11682     98   -663   -916       S  
ATOM   5079  CE  MET C  23     -32.278 -11.569  -3.099  1.00 80.94           C  
ANISOU 5079  CE  MET C  23     8074  11047  11629    210   -667   -961       C  
ATOM   5080  N   SER C  24     -30.357  -7.009  -6.760  1.00 85.21           N  
ANISOU 5080  N   SER C  24     8390  12208  11776   -274   -434   -761       N  
ATOM   5081  CA  SER C  24     -29.442  -5.909  -7.175  1.00 86.50           C  
ANISOU 5081  CA  SER C  24     8493  12512  11859   -392   -355   -728       C  
ATOM   5082  C   SER C  24     -29.900  -4.587  -6.550  1.00 87.14           C  
ANISOU 5082  C   SER C  24     8628  12483  11997   -488   -343   -580       C  
ATOM   5083  O   SER C  24     -29.053  -3.882  -5.961  1.00 87.37           O  
ANISOU 5083  O   SER C  24     8604  12551  12041   -546   -293   -579       O  
ATOM   5084  CB  SER C  24     -29.368  -5.801  -8.681  1.00 87.05           C  
ANISOU 5084  CB  SER C  24     8555  12727  11790   -456   -318   -731       C  
ATOM   5085  OG  SER C  24     -28.826  -4.549  -9.079  1.00 86.87           O  
ANISOU 5085  OG  SER C  24     8514  12795  11696   -595   -241   -654       O  
ATOM   5086  N   MET C  25     -31.194  -4.280  -6.684  1.00 88.11           N  
ANISOU 5086  N   MET C  25     8848  12478  12149   -503   -387   -468       N  
ATOM   5087  CA  MET C  25     -31.847  -3.062  -6.138  1.00 87.35           C  
ANISOU 5087  CA  MET C  25     8820  12255  12112   -576   -386   -322       C  
ATOM   5088  C   MET C  25     -32.303  -3.347  -4.705  1.00 84.11           C  
ANISOU 5088  C   MET C  25     8429  11686  11841   -503   -438   -322       C  
ATOM   5089  O   MET C  25     -32.593  -4.521  -4.391  1.00 81.88           O  
ANISOU 5089  O   MET C  25     8147  11361  11602   -398   -491   -401       O  
ATOM   5090  CB  MET C  25     -33.049  -2.655  -6.999  1.00 89.54           C  
ANISOU 5090  CB  MET C  25     9186  12489  12345   -606   -415   -209       C  
ATOM   5091  CG  MET C  25     -32.675  -2.340  -8.443  1.00 92.49           C  
ANISOU 5091  CG  MET C  25     9552  13021  12569   -678   -365   -194       C  
ATOM   5092  SD  MET C  25     -34.104  -2.013  -9.515  1.00 96.00           S  
ANISOU 5092  SD  MET C  25    10092  13438  12943   -685   -413    -73       S  
ATOM   5093  CE  MET C  25     -34.239  -0.232  -9.352  1.00 96.39           C  
ANISOU 5093  CE  MET C  25    10222  13406  12993   -794   -365    108       C  
ATOM   5094  N   THR C  26     -32.347  -2.306  -3.871  1.00 82.48           N  
ANISOU 5094  N   THR C  26     8244  11393  11698   -562   -420   -239       N  
ATOM   5095  CA  THR C  26     -32.858  -2.361  -2.478  1.00 80.21           C  
ANISOU 5095  CA  THR C  26     7981  10953  11539   -509   -465   -221       C  
ATOM   5096  C   THR C  26     -34.379  -2.502  -2.540  1.00 77.58           C  
ANISOU 5096  C   THR C  26     7735  10490  11248   -475   -531   -145       C  
ATOM   5097  O   THR C  26     -34.935  -2.368  -3.647  1.00 76.66           O  
ANISOU 5097  O   THR C  26     7655  10412  11059   -501   -536    -99       O  
ATOM   5098  CB  THR C  26     -32.522  -1.106  -1.659  1.00 80.90           C  
ANISOU 5098  CB  THR C  26     8069  10992  11676   -594   -422   -156       C  
ATOM   5099  OG1 THR C  26     -33.499  -0.114  -1.982  1.00 81.49           O  
ANISOU 5099  OG1 THR C  26     8234  10973  11756   -654   -425    -20       O  
ATOM   5100  CG2 THR C  26     -31.127  -0.561  -1.889  1.00 82.02           C  
ANISOU 5100  CG2 THR C  26     8132  11278  11751   -680   -339   -204       C  
ATOM   5101  N   TYR C  27     -35.016  -2.738  -1.393  1.00 75.19           N  
ANISOU 5101  N   TYR C  27     7460  10054  11054   -421   -577   -135       N  
ATOM   5102  CA  TYR C  27     -36.487  -2.647  -1.223  1.00 74.05           C  
ANISOU 5102  CA  TYR C  27     7389   9782  10964   -403   -633    -57       C  
ATOM   5103  C   TYR C  27     -36.947  -1.247  -1.656  1.00 74.84           C  
ANISOU 5103  C   TYR C  27     7537   9858  11039   -485   -612     72       C  
ATOM   5104  O   TYR C  27     -37.801  -1.142  -2.562  1.00 76.79           O  
ANISOU 5104  O   TYR C  27     7826  10114  11234   -488   -638    127       O  
ATOM   5105  CB  TYR C  27     -36.893  -2.913   0.228  1.00 72.06           C  
ANISOU 5105  CB  TYR C  27     7149   9400  10828   -352   -668    -64       C  
ATOM   5106  CG  TYR C  27     -36.758  -4.339   0.699  1.00 70.39           C  
ANISOU 5106  CG  TYR C  27     6924   9172  10648   -258   -699   -168       C  
ATOM   5107  CD1 TYR C  27     -35.833  -4.686   1.670  1.00 69.87           C  
ANISOU 5107  CD1 TYR C  27     6816   9111  10618   -212   -687   -233       C  
ATOM   5108  CD2 TYR C  27     -37.574  -5.338   0.199  1.00 69.48           C  
ANISOU 5108  CD2 TYR C  27     6843   9032  10523   -214   -742   -204       C  
ATOM   5109  CE1 TYR C  27     -35.715  -5.988   2.126  1.00 69.08           C  
ANISOU 5109  CE1 TYR C  27     6721   8982  10544   -114   -717   -319       C  
ATOM   5110  CE2 TYR C  27     -37.464  -6.647   0.639  1.00 69.17           C  
ANISOU 5110  CE2 TYR C  27     6812   8956  10514   -131   -765   -297       C  
ATOM   5111  CZ  TYR C  27     -36.534  -6.972   1.608  1.00 68.72           C  
ANISOU 5111  CZ  TYR C  27     6724   8892  10492    -75   -753   -349       C  
ATOM   5112  OH  TYR C  27     -36.418  -8.257   2.044  1.00 68.68           O  
ANISOU 5112  OH  TYR C  27     6741   8839  10512     17   -775   -431       O  
ATOM   5113  N   GLY C  28     -36.371  -0.210  -1.036  1.00 73.99           N  
ANISOU 5113  N   GLY C  28     7425   9723  10963   -547   -564    115       N  
ATOM   5114  CA  GLY C  28     -36.782   1.203  -1.173  1.00 73.40           C  
ANISOU 5114  CA  GLY C  28     7414   9585  10888   -621   -539    241       C  
ATOM   5115  C   GLY C  28     -37.064   1.588  -2.614  1.00 73.14           C  
ANISOU 5115  C   GLY C  28     7424   9620  10743   -657   -527    310       C  
ATOM   5116  O   GLY C  28     -38.242   1.801  -2.946  1.00 72.04           O  
ANISOU 5116  O   GLY C  28     7344   9423  10604   -626   -576    388       O  
ATOM   5117  N   GLN C  29     -36.011   1.683  -3.429  1.00 73.86           N  
ANISOU 5117  N   GLN C  29     7481   9842  10737   -720   -465    281       N  
ATOM   5118  CA  GLN C  29     -36.073   1.950  -4.894  1.00 74.89           C  
ANISOU 5118  CA  GLN C  29     7645  10071  10738   -760   -444    335       C  
ATOM   5119  C   GLN C  29     -37.424   1.467  -5.438  1.00 74.14           C  
ANISOU 5119  C   GLN C  29     7592   9950  10627   -683   -525    369       C  
ATOM   5120  O   GLN C  29     -38.136   2.276  -6.065  1.00 75.32           O  
ANISOU 5120  O   GLN C  29     7815  10075  10728   -698   -534    487       O  
ATOM   5121  CB  GLN C  29     -34.917   1.261  -5.630  1.00 75.74           C  
ANISOU 5121  CB  GLN C  29     7674  10353  10750   -783   -398    228       C  
ATOM   5122  CG  GLN C  29     -33.614   1.222  -4.838  1.00 75.90           C  
ANISOU 5122  CG  GLN C  29     7611  10418  10806   -817   -342    136       C  
ATOM   5123  CD  GLN C  29     -32.403   0.845  -5.657  1.00 77.08           C  
ANISOU 5123  CD  GLN C  29     7682  10757  10846   -858   -282     43       C  
ATOM   5124  OE1 GLN C  29     -32.507   0.437  -6.810  1.00 78.47           O  
ANISOU 5124  OE1 GLN C  29     7860  11032  10920   -851   -284     33       O  
ATOM   5125  NE2 GLN C  29     -31.234   0.970  -5.050  1.00 76.42           N  
ANISOU 5125  NE2 GLN C  29     7519  10736  10780   -900   -227    -32       N  
ATOM   5126  N   GLN C  30     -37.773   0.209  -5.155  1.00 72.61           N  
ANISOU 5126  N   GLN C  30     7356   9759  10474   -601   -581    269       N  
ATOM   5127  CA  GLN C  30     -38.941  -0.514  -5.728  1.00 71.41           C  
ANISOU 5127  CA  GLN C  30     7221   9612  10297   -537   -654    260       C  
ATOM   5128  C   GLN C  30     -40.238  -0.041  -5.057  1.00 70.47           C  
ANISOU 5128  C   GLN C  30     7153   9357  10263   -502   -710    343       C  
ATOM   5129  O   GLN C  30     -41.195   0.272  -5.791  1.00 71.91           O  
ANISOU 5129  O   GLN C  30     7375   9554  10391   -486   -749    414       O  
ATOM   5130  CB  GLN C  30     -38.765  -2.022  -5.544  1.00 70.51           C  
ANISOU 5130  CB  GLN C  30     7051   9529  10207   -474   -682    115       C  
ATOM   5131  CG  GLN C  30     -37.378  -2.526  -5.922  1.00 71.24           C  
ANISOU 5131  CG  GLN C  30     7081   9746  10239   -490   -627     15       C  
ATOM   5132  CD  GLN C  30     -37.222  -4.007  -5.683  1.00 71.06           C  
ANISOU 5132  CD  GLN C  30     7020   9733  10247   -412   -656   -124       C  
ATOM   5133  OE1 GLN C  30     -38.074  -4.805  -6.061  1.00 71.21           O  
ANISOU 5133  OE1 GLN C  30     7056   9739  10258   -371   -706   -162       O  
ATOM   5134  NE2 GLN C  30     -36.123  -4.389  -5.053  1.00 70.73           N  
ANISOU 5134  NE2 GLN C  30     6926   9712  10236   -391   -623   -206       N  
ATOM   5135  N   PHE C  31     -40.250   0.028  -3.720  1.00 68.51           N  
ANISOU 5135  N   PHE C  31     6900   8994  10136   -488   -714    332       N  
ATOM   5136  CA  PHE C  31     -41.468   0.118  -2.869  1.00 66.63           C  
ANISOU 5136  CA  PHE C  31     6689   8631   9995   -442   -772    369       C  
ATOM   5137  C   PHE C  31     -41.630   1.489  -2.196  1.00 65.39           C  
ANISOU 5137  C   PHE C  31     6580   8368   9895   -471   -751    476       C  
ATOM   5138  O   PHE C  31     -42.758   1.766  -1.725  1.00 66.03           O  
ANISOU 5138  O   PHE C  31     6689   8363  10036   -432   -798    524       O  
ATOM   5139  CB  PHE C  31     -41.411  -0.950  -1.773  1.00 66.13           C  
ANISOU 5139  CB  PHE C  31     6588   8511  10025   -398   -792    267       C  
ATOM   5140  CG  PHE C  31     -41.670  -2.369  -2.217  1.00 66.37           C  
ANISOU 5140  CG  PHE C  31     6594   8593  10029   -355   -827    163       C  
ATOM   5141  CD1 PHE C  31     -42.059  -2.669  -3.517  1.00 67.17           C  
ANISOU 5141  CD1 PHE C  31     6696   8794  10030   -355   -847    155       C  
ATOM   5142  CD2 PHE C  31     -41.554  -3.410  -1.308  1.00 65.51           C  
ANISOU 5142  CD2 PHE C  31     6468   8426   9994   -313   -840     73       C  
ATOM   5143  CE1 PHE C  31     -42.307  -3.979  -3.897  1.00 67.04           C  
ANISOU 5143  CE1 PHE C  31     6660   8816   9994   -322   -875     48       C  
ATOM   5144  CE2 PHE C  31     -41.800  -4.719  -1.691  1.00 65.42           C  
ANISOU 5144  CE2 PHE C  31     6449   8441   9963   -277   -866    -23       C  
ATOM   5145  CZ  PHE C  31     -42.185  -4.998  -2.982  1.00 66.32           C  
ANISOU 5145  CZ  PHE C  31     6562   8652   9984   -286   -883    -40       C  
ATOM   5146  N   GLY C  32     -40.570   2.301  -2.129  1.00 63.73           N  
ANISOU 5146  N   GLY C  32     6377   8166   9670   -540   -680    505       N  
ATOM   5147  CA  GLY C  32     -40.508   3.492  -1.259  1.00 62.40           C  
ANISOU 5147  CA  GLY C  32     6248   7883   9575   -577   -648    577       C  
ATOM   5148  C   GLY C  32     -40.282   3.072   0.190  1.00 60.40           C  
ANISOU 5148  C   GLY C  32     5951   7562   9436   -557   -655    502       C  
ATOM   5149  O   GLY C  32     -39.721   2.008   0.433  1.00 59.71           O  
ANISOU 5149  O   GLY C  32     5802   7531   9352   -533   -659    399       O  
ATOM   5150  N   PRO C  33     -40.718   3.866   1.196  1.00 59.56           N  
ANISOU 5150  N   PRO C  33     5876   7335   9420   -558   -657    550       N  
ATOM   5151  CA  PRO C  33     -40.599   3.458   2.597  1.00 58.61           C  
ANISOU 5151  CA  PRO C  33     5714   7155   9400   -534   -667    483       C  
ATOM   5152  C   PRO C  33     -41.163   2.042   2.824  1.00 57.31           C  
ANISOU 5152  C   PRO C  33     5514   7004   9256   -457   -728    407       C  
ATOM   5153  O   PRO C  33     -42.363   1.851   2.684  1.00 56.93           O  
ANISOU 5153  O   PRO C  33     5490   6919   9221   -414   -781    435       O  
ATOM   5154  CB  PRO C  33     -41.401   4.526   3.367  1.00 58.48           C  
ANISOU 5154  CB  PRO C  33     5749   7007   9462   -533   -676    560       C  
ATOM   5155  CG  PRO C  33     -41.379   5.740   2.463  1.00 59.41           C  
ANISOU 5155  CG  PRO C  33     5938   7112   9521   -584   -638    665       C  
ATOM   5156  CD  PRO C  33     -41.352   5.186   1.050  1.00 60.16           C  
ANISOU 5156  CD  PRO C  33     6031   7321   9502   -576   -649    670       C  
ATOM   5157  N   THR C  34     -40.277   1.090   3.131  1.00 56.26           N  
ANISOU 5157  N   THR C  34     5327   6927   9119   -442   -716    309       N  
ATOM   5158  CA  THR C  34     -40.589  -0.333   3.436  1.00 55.69           C  
ANISOU 5158  CA  THR C  34     5233   6856   9068   -373   -761    227       C  
ATOM   5159  C   THR C  34     -40.169  -0.618   4.885  1.00 55.14           C  
ANISOU 5159  C   THR C  34     5139   6731   9078   -348   -758    178       C  
ATOM   5160  O   THR C  34     -39.152  -0.048   5.310  1.00 54.73           O  
ANISOU 5160  O   THR C  34     5056   6708   9029   -383   -713    167       O  
ATOM   5161  CB  THR C  34     -39.897  -1.264   2.428  1.00 55.60           C  
ANISOU 5161  CB  THR C  34     5193   6959   8972   -360   -752    154       C  
ATOM   5162  OG1 THR C  34     -40.072  -0.727   1.115  1.00 55.50           O  
ANISOU 5162  OG1 THR C  34     5200   7013   8874   -399   -742    209       O  
ATOM   5163  CG2 THR C  34     -40.424  -2.681   2.473  1.00 55.13           C  
ANISOU 5163  CG2 THR C  34     5135   6885   8924   -294   -798     80       C  
ATOM   5164  N   TYR C  35     -40.925  -1.446   5.616  1.00 55.29           N  
ANISOU 5164  N   TYR C  35     5171   6682   9152   -294   -800    151       N  
ATOM   5165  CA  TYR C  35     -40.651  -1.800   7.037  1.00 55.78           C  
ANISOU 5165  CA  TYR C  35     5221   6690   9284   -260   -803    112       C  
ATOM   5166  C   TYR C  35     -40.901  -3.294   7.280  1.00 55.42           C  
ANISOU 5166  C   TYR C  35     5188   6621   9245   -194   -835     44       C  
ATOM   5167  O   TYR C  35     -41.732  -3.886   6.581  1.00 55.42           O  
ANISOU 5167  O   TYR C  35     5215   6614   9227   -187   -862     39       O  
ATOM   5168  CB  TYR C  35     -41.509  -0.955   7.982  1.00 56.18           C  
ANISOU 5168  CB  TYR C  35     5292   6641   9409   -277   -813    173       C  
ATOM   5169  CG  TYR C  35     -41.386   0.539   7.809  1.00 57.12           C  
ANISOU 5169  CG  TYR C  35     5419   6752   9531   -339   -780    243       C  
ATOM   5170  CD1 TYR C  35     -40.548   1.295   8.618  1.00 56.79           C  
ANISOU 5170  CD1 TYR C  35     5352   6705   9518   -375   -741    236       C  
ATOM   5171  CD2 TYR C  35     -42.134   1.209   6.853  1.00 58.27           C  
ANISOU 5171  CD2 TYR C  35     5600   6891   9648   -361   -789    315       C  
ATOM   5172  CE1 TYR C  35     -40.444   2.669   8.469  1.00 57.24           C  
ANISOU 5172  CE1 TYR C  35     5430   6737   9581   -441   -703    298       C  
ATOM   5173  CE2 TYR C  35     -42.040   2.583   6.689  1.00 58.47           C  
ANISOU 5173  CE2 TYR C  35     5652   6888   9674   -413   -756    388       C  
ATOM   5174  CZ  TYR C  35     -41.192   3.317   7.500  1.00 58.11           C  
ANISOU 5174  CZ  TYR C  35     5591   6822   9664   -458   -709    378       C  
ATOM   5175  OH  TYR C  35     -41.096   4.670   7.340  1.00 58.97           O  
ANISOU 5175  OH  TYR C  35     5740   6888   9778   -517   -669    446       O  
ATOM   5176  N   LEU C  36     -40.201  -3.867   8.262  1.00 55.61           N  
ANISOU 5176  N   LEU C  36     5199   6635   9295   -147   -831     -6       N  
ATOM   5177  CA  LEU C  36     -40.242  -5.310   8.621  1.00 56.72           C  
ANISOU 5177  CA  LEU C  36     5368   6740   9441    -74   -853    -70       C  
ATOM   5178  C   LEU C  36     -40.180  -5.428  10.144  1.00 57.31           C  
ANISOU 5178  C   LEU C  36     5452   6749   9574    -38   -859    -70       C  
ATOM   5179  O   LEU C  36     -39.076  -5.282  10.697  1.00 58.31           O  
ANISOU 5179  O   LEU C  36     5536   6927   9690     -9   -842   -100       O  
ATOM   5180  CB  LEU C  36     -39.052  -6.024   7.966  1.00 57.60           C  
ANISOU 5180  CB  LEU C  36     5450   6947   9488    -27   -839   -146       C  
ATOM   5181  CG  LEU C  36     -38.740  -7.441   8.458  1.00 57.73           C  
ANISOU 5181  CG  LEU C  36     5499   6927   9507     67   -855   -217       C  
ATOM   5182  CD1 LEU C  36     -39.821  -8.428   8.036  1.00 57.69           C  
ANISOU 5182  CD1 LEU C  36     5564   6842   9511     72   -879   -231       C  
ATOM   5183  CD2 LEU C  36     -37.380  -7.901   7.951  1.00 58.03           C  
ANISOU 5183  CD2 LEU C  36     5489   7076   9482    123   -837   -295       C  
ATOM   5184  N   ASP C  37     -41.322  -5.674  10.785  1.00 58.75           N  
ANISOU 5184  N   ASP C  37     5681   6833   9808    -42   -881    -42       N  
ATOM   5185  CA  ASP C  37     -41.438  -5.834  12.259  1.00 59.63           C  
ANISOU 5185  CA  ASP C  37     5810   6876   9969    -12   -886    -36       C  
ATOM   5186  C   ASP C  37     -40.780  -4.621  12.932  1.00 59.11           C  
ANISOU 5186  C   ASP C  37     5689   6849   9920    -37   -865    -13       C  
ATOM   5187  O   ASP C  37     -39.969  -4.828  13.858  1.00 59.62           O  
ANISOU 5187  O   ASP C  37     5735   6933   9983      9   -861    -43       O  
ATOM   5188  CB  ASP C  37     -40.833  -7.168  12.711  1.00 61.26           C  
ANISOU 5188  CB  ASP C  37     6052   7065  10159     75   -893    -93       C  
ATOM   5189  CG  ASP C  37     -41.331  -8.365  11.912  1.00 63.22           C  
ANISOU 5189  CG  ASP C  37     6359   7274  10387     93   -905   -129       C  
ATOM   5190  OD1 ASP C  37     -42.564  -8.611  11.924  1.00 62.80           O  
ANISOU 5190  OD1 ASP C  37     6351   7146  10364     50   -916   -109       O  
ATOM   5191  OD2 ASP C  37     -40.485  -9.034  11.266  1.00 64.56           O  
ANISOU 5191  OD2 ASP C  37     6525   7494  10508    146   -901   -186       O  
ATOM   5192  N   GLY C  38     -41.096  -3.412  12.447  1.00 58.29           N  
ANISOU 5192  N   GLY C  38     5563   6757   9824   -107   -852     34       N  
ATOM   5193  CA  GLY C  38     -40.649  -2.124  13.016  1.00 57.66           C  
ANISOU 5193  CA  GLY C  38     5445   6694   9768   -152   -826     59       C  
ATOM   5194  C   GLY C  38     -39.447  -1.545  12.284  1.00 57.85           C  
ANISOU 5194  C   GLY C  38     5420   6818   9742   -186   -790     39       C  
ATOM   5195  O   GLY C  38     -39.501  -0.352  11.920  1.00 58.72           O  
ANISOU 5195  O   GLY C  38     5525   6928   9858   -256   -764     84       O  
ATOM   5196  N   ALA C  39     -38.398  -2.357  12.092  1.00 56.91           N  
ANISOU 5196  N   ALA C  39     5269   6779   9573   -136   -786    -26       N  
ATOM   5197  CA  ALA C  39     -37.092  -1.990  11.490  1.00 56.00           C  
ANISOU 5197  CA  ALA C  39     5090   6786   9401   -163   -748    -68       C  
ATOM   5198  C   ALA C  39     -37.285  -1.323  10.120  1.00 54.81           C  
ANISOU 5198  C   ALA C  39     4950   6662   9213   -237   -725    -24       C  
ATOM   5199  O   ALA C  39     -38.003  -1.898   9.276  1.00 54.06           O  
ANISOU 5199  O   ALA C  39     4896   6545   9098   -219   -749     -8       O  
ATOM   5200  CB  ALA C  39     -36.233  -3.229  11.373  1.00 56.39           C  
ANISOU 5200  CB  ALA C  39     5114   6909   9402    -73   -760   -148       C  
ATOM   5201  N   ASP C  40     -36.647  -0.167   9.904  1.00 53.71           N  
ANISOU 5201  N   ASP C  40     4779   6571   9058   -320   -677     -9       N  
ATOM   5202  CA  ASP C  40     -36.623   0.541   8.595  1.00 53.66           C  
ANISOU 5202  CA  ASP C  40     4787   6600   9000   -395   -644     36       C  
ATOM   5203  C   ASP C  40     -35.622  -0.165   7.672  1.00 54.24           C  
ANISOU 5203  C   ASP C  40     4812   6806   8990   -379   -626    -32       C  
ATOM   5204  O   ASP C  40     -34.404  -0.015   7.897  1.00 55.00           O  
ANISOU 5204  O   ASP C  40     4836   7003   9057   -399   -589    -95       O  
ATOM   5205  CB  ASP C  40     -36.297   2.028   8.762  1.00 53.63           C  
ANISOU 5205  CB  ASP C  40     4782   6582   9012   -497   -591     78       C  
ATOM   5206  CG  ASP C  40     -36.356   2.822   7.465  1.00 54.11           C  
ANISOU 5206  CG  ASP C  40     4881   6661   9018   -575   -554    143       C  
ATOM   5207  OD1 ASP C  40     -36.228   2.208   6.391  1.00 54.34           O  
ANISOU 5207  OD1 ASP C  40     4906   6763   8978   -558   -558    131       O  
ATOM   5208  OD2 ASP C  40     -36.533   4.052   7.537  1.00 54.37           O  
ANISOU 5208  OD2 ASP C  40     4952   6630   9075   -650   -519    207       O  
ATOM   5209  N   VAL C  41     -36.125  -0.878   6.658  1.00 54.28           N  
ANISOU 5209  N   VAL C  41     4848   6822   8954   -347   -651    -27       N  
ATOM   5210  CA  VAL C  41     -35.317  -1.708   5.714  1.00 55.28           C  
ANISOU 5210  CA  VAL C  41     4934   7069   8998   -317   -640   -100       C  
ATOM   5211  C   VAL C  41     -35.458  -1.158   4.285  1.00 56.36           C  
ANISOU 5211  C   VAL C  41     5091   7259   9064   -389   -613    -51       C  
ATOM   5212  O   VAL C  41     -35.362  -1.954   3.330  1.00 56.06           O  
ANISOU 5212  O   VAL C  41     5047   7291   8962   -357   -621    -93       O  
ATOM   5213  CB  VAL C  41     -35.713  -3.196   5.818  1.00 54.88           C  
ANISOU 5213  CB  VAL C  41     4905   6987   8957   -209   -692   -156       C  
ATOM   5214  CG1 VAL C  41     -35.757  -3.654   7.268  1.00 54.21           C  
ANISOU 5214  CG1 VAL C  41     4824   6829   8941   -141   -719   -179       C  
ATOM   5215  CG2 VAL C  41     -37.032  -3.505   5.128  1.00 54.94           C  
ANISOU 5215  CG2 VAL C  41     4982   6924   8968   -208   -728   -108       C  
ATOM   5216  N   THR C  42     -35.625   0.162   4.145  1.00 57.76           N  
ANISOU 5216  N   THR C  42     5295   7405   9245   -480   -578     32       N  
ATOM   5217  CA  THR C  42     -35.721   0.888   2.846  1.00 59.23           C  
ANISOU 5217  CA  THR C  42     5515   7634   9356   -555   -545     98       C  
ATOM   5218  C   THR C  42     -34.382   0.814   2.103  1.00 61.34           C  
ANISOU 5218  C   THR C  42     5715   8059   9532   -601   -486     33       C  
ATOM   5219  O   THR C  42     -34.391   0.506   0.897  1.00 61.15           O  
ANISOU 5219  O   THR C  42     5697   8112   9423   -606   -481     33       O  
ATOM   5220  CB  THR C  42     -36.108   2.360   3.047  1.00 58.66           C  
ANISOU 5220  CB  THR C  42     5498   7471   9315   -636   -514    203       C  
ATOM   5221  OG1 THR C  42     -37.174   2.422   3.991  1.00 57.44           O  
ANISOU 5221  OG1 THR C  42     5384   7185   9255   -588   -564    241       O  
ATOM   5222  CG2 THR C  42     -36.531   3.042   1.765  1.00 59.23           C  
ANISOU 5222  CG2 THR C  42     5634   7554   9315   -688   -496    296       C  
ATOM   5223  N   LYS C  43     -33.287   1.109   2.808  1.00 64.07           N  
ANISOU 5223  N   LYS C  43     5992   8460   9889   -636   -442    -25       N  
ATOM   5224  CA  LYS C  43     -31.927   1.297   2.233  1.00 66.76           C  
ANISOU 5224  CA  LYS C  43     6255   8962  10145   -705   -372    -91       C  
ATOM   5225  C   LYS C  43     -31.270  -0.067   1.989  1.00 67.68           C  
ANISOU 5225  C   LYS C  43     6297   9201  10217   -607   -395   -212       C  
ATOM   5226  O   LYS C  43     -30.483  -0.170   1.034  1.00 69.22           O  
ANISOU 5226  O   LYS C  43     6442   9539  10319   -644   -351   -259       O  
ATOM   5227  CB  LYS C  43     -31.089   2.177   3.165  1.00 67.70           C  
ANISOU 5227  CB  LYS C  43     6325   9098  10300   -785   -319   -116       C  
ATOM   5228  CG  LYS C  43     -31.611   3.598   3.331  1.00 68.62           C  
ANISOU 5228  CG  LYS C  43     6522   9092  10456   -891   -283     -5       C  
ATOM   5229  CD  LYS C  43     -30.978   4.357   4.479  1.00 69.82           C  
ANISOU 5229  CD  LYS C  43     6632   9232  10665   -957   -244    -40       C  
ATOM   5230  CE  LYS C  43     -31.405   5.810   4.525  1.00 70.91           C  
ANISOU 5230  CE  LYS C  43     6860   9246  10836  -1072   -196     62       C  
ATOM   5231  NZ  LYS C  43     -30.583   6.597   5.476  1.00 71.67           N  
ANISOU 5231  NZ  LYS C  43     6905   9356  10970  -1164   -139      8       N  
ATOM   5232  N   ILE C  44     -31.595  -1.076   2.802  1.00 67.43           N  
ANISOU 5232  N   ILE C  44     6264   9111  10245   -486   -458   -259       N  
ATOM   5233  CA  ILE C  44     -30.956  -2.424   2.738  1.00 68.04           C  
ANISOU 5233  CA  ILE C  44     6282   9279  10289   -372   -483   -377       C  
ATOM   5234  C   ILE C  44     -31.599  -3.207   1.586  1.00 68.69           C  
ANISOU 5234  C   ILE C  44     6412   9362  10324   -333   -510   -376       C  
ATOM   5235  O   ILE C  44     -32.714  -2.850   1.184  1.00 68.74           O  
ANISOU 5235  O   ILE C  44     6498   9275  10344   -368   -530   -283       O  
ATOM   5236  CB  ILE C  44     -31.040  -3.155   4.097  1.00 67.30           C  
ANISOU 5236  CB  ILE C  44     6186   9110  10274   -259   -535   -418       C  
ATOM   5237  CG1 ILE C  44     -32.307  -4.003   4.241  1.00 66.00           C  
ANISOU 5237  CG1 ILE C  44     6114   8800  10161   -180   -600   -382       C  
ATOM   5238  CG2 ILE C  44     -30.880  -2.179   5.258  1.00 66.87           C  
ANISOU 5238  CG2 ILE C  44     6113   9013  10280   -314   -518   -385       C  
ATOM   5239  CD1 ILE C  44     -32.370  -4.781   5.538  1.00 65.38           C  
ANISOU 5239  CD1 ILE C  44     6046   8646  10149    -71   -645   -417       C  
ATOM   5240  N   LYS C  45     -30.904  -4.221   1.065  1.00 70.79           N  
ANISOU 5240  N   LYS C  45     6627   9739  10531   -260   -511   -482       N  
ATOM   5241  CA  LYS C  45     -31.322  -5.010  -0.128  1.00 71.74           C  
ANISOU 5241  CA  LYS C  45     6778   9888  10590   -228   -529   -507       C  
ATOM   5242  C   LYS C  45     -31.943  -6.323   0.341  1.00 71.16           C  
ANISOU 5242  C   LYS C  45     6754   9709  10572   -102   -593   -554       C  
ATOM   5243  O   LYS C  45     -31.679  -6.775   1.452  1.00 71.06           O  
ANISOU 5243  O   LYS C  45     6733   9645  10619    -22   -616   -590       O  
ATOM   5244  CB  LYS C  45     -30.127  -5.204  -1.070  1.00 72.97           C  
ANISOU 5244  CB  LYS C  45     6845  10239  10639   -241   -478   -601       C  
ATOM   5245  CG  LYS C  45     -29.434  -3.902  -1.452  1.00 73.62           C  
ANISOU 5245  CG  LYS C  45     6879  10426  10664   -382   -402   -559       C  
ATOM   5246  CD  LYS C  45     -28.436  -3.994  -2.580  1.00 74.92           C  
ANISOU 5246  CD  LYS C  45     6965  10789  10709   -420   -344   -637       C  
ATOM   5247  CE  LYS C  45     -27.914  -2.630  -2.987  1.00 75.76           C  
ANISOU 5247  CE  LYS C  45     7049  10975  10758   -584   -261   -576       C  
ATOM   5248  NZ  LYS C  45     -27.189  -2.672  -4.279  1.00 77.05           N  
ANISOU 5248  NZ  LYS C  45     7158  11324  10793   -640   -202   -628       N  
ATOM   5249  N   PRO C  46     -32.808  -6.967  -0.473  1.00 71.39           N  
ANISOU 5249  N   PRO C  46     6842   9700  10582    -84   -623   -553       N  
ATOM   5250  CA  PRO C  46     -33.589  -8.110   0.000  1.00 71.00           C  
ANISOU 5250  CA  PRO C  46     6860   9522  10594      8   -678   -583       C  
ATOM   5251  C   PRO C  46     -32.732  -9.352   0.289  1.00 71.42           C  
ANISOU 5251  C   PRO C  46     6888   9604  10641    135   -686   -708       C  
ATOM   5252  O   PRO C  46     -32.344 -10.034  -0.635  1.00 71.81           O  
ANISOU 5252  O   PRO C  46     6919   9741  10625    170   -677   -792       O  
ATOM   5253  CB  PRO C  46     -34.604  -8.385  -1.126  1.00 71.27           C  
ANISOU 5253  CB  PRO C  46     6946   9544  10589    -25   -697   -566       C  
ATOM   5254  CG  PRO C  46     -34.491  -7.199  -2.072  1.00 71.85           C  
ANISOU 5254  CG  PRO C  46     6991   9722  10586   -134   -659   -496       C  
ATOM   5255  CD  PRO C  46     -33.104  -6.623  -1.872  1.00 72.10           C  
ANISOU 5255  CD  PRO C  46     6940   9869  10584   -158   -603   -524       C  
ATOM   5256  N   HIS C  47     -32.457  -9.601   1.572  1.00 71.54           N  
ANISOU 5256  N   HIS C  47     6907   9550  10722    207   -704   -717       N  
ATOM   5257  CA  HIS C  47     -31.859 -10.861   2.094  1.00 72.57           C  
ANISOU 5257  CA  HIS C  47     7045   9663  10864    355   -725   -817       C  
ATOM   5258  C   HIS C  47     -32.865 -12.000   1.891  1.00 72.46           C  
ANISOU 5258  C   HIS C  47     7140   9510  10881    403   -761   -835       C  
ATOM   5259  O   HIS C  47     -34.066 -11.700   1.761  1.00 73.75           O  
ANISOU 5259  O   HIS C  47     7362   9580  11077    322   -776   -760       O  
ATOM   5260  CB  HIS C  47     -31.453 -10.698   3.565  1.00 72.81           C  
ANISOU 5260  CB  HIS C  47     7062   9649  10951    411   -739   -799       C  
ATOM   5261  CG  HIS C  47     -30.392 -11.645   4.011  1.00 73.78           C  
ANISOU 5261  CG  HIS C  47     7152   9825  11054    563   -750   -903       C  
ATOM   5262  ND1 HIS C  47     -30.672 -12.757   4.781  1.00 73.75           N  
ANISOU 5262  ND1 HIS C  47     7237   9686  11096    689   -789   -923       N  
ATOM   5263  CD2 HIS C  47     -29.057 -11.649   3.805  1.00 74.15           C  
ANISOU 5263  CD2 HIS C  47     7090  10047  11037    616   -726   -994       C  
ATOM   5264  CE1 HIS C  47     -29.555 -13.406   5.032  1.00 74.41           C  
ANISOU 5264  CE1 HIS C  47     7273   9854  11144    826   -794  -1016       C  
ATOM   5265  NE2 HIS C  47     -28.550 -12.747   4.442  1.00 75.10           N  
ANISOU 5265  NE2 HIS C  47     7230  10140  11164    786   -758  -1066       N  
ATOM   5266  N   ASN C  48     -32.396 -13.253   1.872  1.00 72.10           N  
ANISOU 5266  N   ASN C  48     7120   9451  10824    528   -773   -937       N  
ATOM   5267  CA  ASN C  48     -33.183 -14.432   1.415  1.00 71.76           C  
ANISOU 5267  CA  ASN C  48     7176   9294  10792    566   -793   -984       C  
ATOM   5268  C   ASN C  48     -33.945 -15.071   2.584  1.00 70.40           C  
ANISOU 5268  C   ASN C  48     7116   8923  10709    614   -824   -946       C  
ATOM   5269  O   ASN C  48     -34.862 -15.872   2.314  1.00 70.52           O  
ANISOU 5269  O   ASN C  48     7225   8821  10747    604   -837   -964       O  
ATOM   5270  CB  ASN C  48     -32.285 -15.446   0.702  1.00 72.91           C  
ANISOU 5270  CB  ASN C  48     7303   9520  10877    674   -783  -1119       C  
ATOM   5271  CG  ASN C  48     -31.621 -14.869  -0.531  1.00 73.26           C  
ANISOU 5271  CG  ASN C  48     7242   9767  10827    615   -747  -1160       C  
ATOM   5272  OD1 ASN C  48     -32.041 -13.834  -1.045  1.00 72.83           O  
ANISOU 5272  OD1 ASN C  48     7154   9770  10748    484   -731  -1083       O  
ATOM   5273  ND2 ASN C  48     -30.582 -15.528  -1.011  1.00 74.49           N  
ANISOU 5273  ND2 ASN C  48     7346  10033  10923    713   -732  -1280       N  
ATOM   5274  N   SER C  49     -33.597 -14.720   3.826  1.00 69.17           N  
ANISOU 5274  N   SER C  49     6950   8737  10595    654   -833   -899       N  
ATOM   5275  CA  SER C  49     -34.266 -15.192   5.068  1.00 68.45           C  
ANISOU 5275  CA  SER C  49     6959   8467  10580    693   -858   -849       C  
ATOM   5276  C   SER C  49     -35.681 -14.604   5.177  1.00 67.69           C  
ANISOU 5276  C   SER C  49     6907   8277  10535    561   -865   -754       C  
ATOM   5277  O   SER C  49     -36.416 -15.008   6.099  1.00 66.09           O  
ANISOU 5277  O   SER C  49     6791   7926  10392    570   -880   -714       O  
ATOM   5278  CB  SER C  49     -33.448 -14.841   6.282  1.00 67.89           C  
ANISOU 5278  CB  SER C  49     6845   8425  10523    766   -865   -827       C  
ATOM   5279  OG  SER C  49     -32.063 -14.962   6.008  1.00 68.18           O  
ANISOU 5279  OG  SER C  49     6791   8616  10497    860   -855   -912       O  
ATOM   5280  N   HIS C  50     -36.032 -13.670   4.286  1.00 68.28           N  
ANISOU 5280  N   HIS C  50     6923   8440  10581    447   -853   -719       N  
ATOM   5281  CA  HIS C  50     -37.340 -12.964   4.237  1.00 67.94           C  
ANISOU 5281  CA  HIS C  50     6902   8338  10573    328   -862   -631       C  
ATOM   5282  C   HIS C  50     -38.372 -13.780   3.451  1.00 69.66           C  
ANISOU 5282  C   HIS C  50     7187   8492  10787    294   -873   -668       C  
ATOM   5283  O   HIS C  50     -39.583 -13.499   3.607  1.00 69.78           O  
ANISOU 5283  O   HIS C  50     7235   8436  10841    217   -887   -611       O  
ATOM   5284  CB  HIS C  50     -37.177 -11.576   3.605  1.00 67.12           C  
ANISOU 5284  CB  HIS C  50     6711   8359  10430    236   -844   -574       C  
ATOM   5285  CG  HIS C  50     -36.163 -10.717   4.277  1.00 66.12           C  
ANISOU 5285  CG  HIS C  50     6513   8305  10303    245   -825   -549       C  
ATOM   5286  ND1 HIS C  50     -35.127 -10.124   3.589  1.00 66.22           N  
ANISOU 5286  ND1 HIS C  50     6438   8473  10248    225   -793   -575       N  
ATOM   5287  CD2 HIS C  50     -36.021 -10.349   5.567  1.00 65.61           C  
ANISOU 5287  CD2 HIS C  50     6446   8188  10293    265   -830   -508       C  
ATOM   5288  CE1 HIS C  50     -34.394  -9.419   4.425  1.00 66.26           C  
ANISOU 5288  CE1 HIS C  50     6388   8517  10269    225   -778   -555       C  
ATOM   5289  NE2 HIS C  50     -34.917  -9.546   5.645  1.00 65.83           N  
ANISOU 5289  NE2 HIS C  50     6384   8339  10289    254   -803   -515       N  
ATOM   5290  N   GLU C  51     -37.923 -14.723   2.612  1.00 71.39           N  
ANISOU 5290  N   GLU C  51     7420   8745  10958    347   -866   -768       N  
ATOM   5291  CA  GLU C  51     -38.822 -15.524   1.738  1.00 72.19           C  
ANISOU 5291  CA  GLU C  51     7578   8805  11046    308   -872   -825       C  
ATOM   5292  C   GLU C  51     -40.117 -15.789   2.519  1.00 71.14           C  
ANISOU 5292  C   GLU C  51     7526   8515  10987    257   -888   -779       C  
ATOM   5293  O   GLU C  51     -40.055 -16.460   3.574  1.00 70.31           O  
ANISOU 5293  O   GLU C  51     7496   8281  10935    318   -888   -780       O  
ATOM   5294  CB  GLU C  51     -38.140 -16.810   1.258  1.00 74.14           C  
ANISOU 5294  CB  GLU C  51     7864   9043  11260    404   -862   -949       C  
ATOM   5295  CG  GLU C  51     -38.656 -17.307  -0.087  1.00 75.46           C  
ANISOU 5295  CG  GLU C  51     8039   9257  11375    352   -860  -1027       C  
ATOM   5296  CD  GLU C  51     -38.074 -16.614  -1.311  1.00 76.54           C  
ANISOU 5296  CD  GLU C  51     8072   9590  11418    320   -847  -1044       C  
ATOM   5297  OE1 GLU C  51     -38.747 -16.622  -2.365  1.00 77.33           O  
ANISOU 5297  OE1 GLU C  51     8163   9748  11470    247   -852  -1069       O  
ATOM   5298  OE2 GLU C  51     -36.949 -16.075  -1.215  1.00 76.85           O  
ANISOU 5298  OE2 GLU C  51     8039   9734  11426    365   -831  -1036       O  
ATOM   5299  N   GLY C  52     -41.225 -15.206   2.054  1.00 70.42           N  
ANISOU 5299  N   GLY C  52     7416   8445  10894    151   -901   -734       N  
ATOM   5300  CA  GLY C  52     -42.560 -15.348   2.662  1.00 70.35           C  
ANISOU 5300  CA  GLY C  52     7463   8320  10947     85   -914   -697       C  
ATOM   5301  C   GLY C  52     -42.653 -14.643   4.003  1.00 69.53           C  
ANISOU 5301  C   GLY C  52     7358   8152  10906     88   -918   -602       C  
ATOM   5302  O   GLY C  52     -43.136 -15.277   4.965  1.00 69.38           O  
ANISOU 5302  O   GLY C  52     7417   8000  10945     95   -916   -598       O  
ATOM   5303  N   LYS C  53     -42.213 -13.379   4.064  1.00 69.31           N  
ANISOU 5303  N   LYS C  53     7252   8216  10866     77   -918   -529       N  
ATOM   5304  CA  LYS C  53     -42.360 -12.486   5.249  1.00 68.04           C  
ANISOU 5304  CA  LYS C  53     7076   8014  10761     65   -921   -438       C  
ATOM   5305  C   LYS C  53     -43.208 -11.261   4.881  1.00 66.02           C  
ANISOU 5305  C   LYS C  53     6769   7811  10503    -19   -934   -361       C  
ATOM   5306  O   LYS C  53     -43.308 -10.937   3.677  1.00 64.64           O  
ANISOU 5306  O   LYS C  53     6556   7733  10268    -53   -938   -368       O  
ATOM   5307  CB  LYS C  53     -40.993 -12.061   5.796  1.00 69.02           C  
ANISOU 5307  CB  LYS C  53     7157   8188  10877    132   -907   -428       C  
ATOM   5308  CG  LYS C  53     -40.335 -13.055   6.747  1.00 70.56           C  
ANISOU 5308  CG  LYS C  53     7410   8304  11096    233   -903   -470       C  
ATOM   5309  CD  LYS C  53     -39.475 -12.386   7.808  1.00 71.51           C  
ANISOU 5309  CD  LYS C  53     7486   8450  11233    277   -899   -431       C  
ATOM   5310  CE  LYS C  53     -39.042 -13.317   8.921  1.00 72.58           C  
ANISOU 5310  CE  LYS C  53     7687   8496  11392    381   -904   -453       C  
ATOM   5311  NZ  LYS C  53     -37.824 -14.079   8.555  1.00 74.06           N  
ANISOU 5311  NZ  LYS C  53     7866   8742  11529    494   -900   -536       N  
ATOM   5312  N   THR C  54     -43.771 -10.602   5.901  1.00 64.39           N  
ANISOU 5312  N   THR C  54     6563   7544  10356    -44   -940   -291       N  
ATOM   5313  CA  THR C  54     -44.781  -9.513   5.788  1.00 62.95           C  
ANISOU 5313  CA  THR C  54     6347   7382  10188   -110   -957   -217       C  
ATOM   5314  C   THR C  54     -44.118  -8.159   6.070  1.00 61.06           C  
ANISOU 5314  C   THR C  54     6058   7189   9951   -112   -944   -145       C  
ATOM   5315  O   THR C  54     -43.640  -7.960   7.202  1.00 59.28           O  
ANISOU 5315  O   THR C  54     5835   6916   9770    -86   -933   -126       O  
ATOM   5316  CB  THR C  54     -45.965  -9.778   6.727  1.00 62.60           C  
ANISOU 5316  CB  THR C  54     6339   7235  10208   -140   -968   -202       C  
ATOM   5317  OG1 THR C  54     -46.199 -11.188   6.750  1.00 63.03           O  
ANISOU 5317  OG1 THR C  54     6458   7221  10267   -132   -964   -279       O  
ATOM   5318  CG2 THR C  54     -47.221  -9.045   6.307  1.00 62.41           C  
ANISOU 5318  CG2 THR C  54     6281   7245  10184   -199   -993   -161       C  
ATOM   5319  N   PHE C  55     -44.123  -7.267   5.072  1.00 60.84           N  
ANISOU 5319  N   PHE C  55     5993   7249   9873   -145   -945   -105       N  
ATOM   5320  CA  PHE C  55     -43.441  -5.946   5.079  1.00 60.42           C  
ANISOU 5320  CA  PHE C  55     5903   7243   9810   -163   -923    -39       C  
ATOM   5321  C   PHE C  55     -44.472  -4.820   4.945  1.00 59.31           C  
ANISOU 5321  C   PHE C  55     5760   7091   9683   -204   -941     45       C  
ATOM   5322  O   PHE C  55     -45.199  -4.805   3.943  1.00 59.66           O  
ANISOU 5322  O   PHE C  55     5803   7183   9680   -220   -963     55       O  
ATOM   5323  CB  PHE C  55     -42.428  -5.863   3.933  1.00 61.62           C  
ANISOU 5323  CB  PHE C  55     6025   7509   9876   -166   -900    -64       C  
ATOM   5324  CG  PHE C  55     -41.214  -6.745   4.087  1.00 62.42           C  
ANISOU 5324  CG  PHE C  55     6115   7641   9960   -114   -879   -147       C  
ATOM   5325  CD1 PHE C  55     -40.009  -6.222   4.530  1.00 62.77           C  
ANISOU 5325  CD1 PHE C  55     6118   7729  10000   -106   -846   -148       C  
ATOM   5326  CD2 PHE C  55     -41.274  -8.099   3.795  1.00 63.17           C  
ANISOU 5326  CD2 PHE C  55     6238   7722  10040    -71   -891   -231       C  
ATOM   5327  CE1 PHE C  55     -38.892  -7.032   4.676  1.00 63.33           C  
ANISOU 5327  CE1 PHE C  55     6168   7844  10049    -43   -832   -230       C  
ATOM   5328  CE2 PHE C  55     -40.157  -8.908   3.941  1.00 63.59           C  
ANISOU 5328  CE2 PHE C  55     6284   7800  10076     -4   -875   -309       C  
ATOM   5329  CZ  PHE C  55     -38.968  -8.373   4.381  1.00 63.74           C  
ANISOU 5329  CZ  PHE C  55     6253   7876  10087     15   -848   -308       C  
ATOM   5330  N   TYR C  56     -44.519  -3.897   5.910  1.00 58.30           N  
ANISOU 5330  N   TYR C  56     5629   6909   9613   -213   -932    102       N  
ATOM   5331  CA  TYR C  56     -45.342  -2.661   5.838  1.00 58.42           C  
ANISOU 5331  CA  TYR C  56     5645   6907   9644   -239   -944    187       C  
ATOM   5332  C   TYR C  56     -44.788  -1.772   4.721  1.00 59.01           C  
ANISOU 5332  C   TYR C  56     5716   7057   9647   -264   -923    237       C  
ATOM   5333  O   TYR C  56     -43.564  -1.767   4.525  1.00 59.82           O  
ANISOU 5333  O   TYR C  56     5803   7208   9716   -276   -886    213       O  
ATOM   5334  CB  TYR C  56     -45.369  -1.931   7.183  1.00 57.98           C  
ANISOU 5334  CB  TYR C  56     5590   6771   9666   -241   -932    221       C  
ATOM   5335  CG  TYR C  56     -46.324  -2.524   8.188  1.00 58.08           C  
ANISOU 5335  CG  TYR C  56     5612   6711   9743   -226   -956    199       C  
ATOM   5336  CD1 TYR C  56     -47.687  -2.265   8.126  1.00 57.91           C  
ANISOU 5336  CD1 TYR C  56     5590   6670   9741   -231   -988    226       C  
ATOM   5337  CD2 TYR C  56     -45.871  -3.351   9.203  1.00 57.97           C  
ANISOU 5337  CD2 TYR C  56     5606   6654   9763   -206   -945    149       C  
ATOM   5338  CE1 TYR C  56     -48.571  -2.805   9.047  1.00 57.30           C  
ANISOU 5338  CE1 TYR C  56     5516   6537   9717   -231  -1003    201       C  
ATOM   5339  CE2 TYR C  56     -46.743  -3.901  10.131  1.00 57.57           C  
ANISOU 5339  CE2 TYR C  56     5573   6536   9765   -202   -960    133       C  
ATOM   5340  CZ  TYR C  56     -48.099  -3.629  10.053  1.00 57.06           C  
ANISOU 5340  CZ  TYR C  56     5503   6456   9720   -222   -985    156       C  
ATOM   5341  OH  TYR C  56     -48.957  -4.177  10.961  1.00 55.99           O  
ANISOU 5341  OH  TYR C  56     5379   6263   9629   -230   -992    135       O  
ATOM   5342  N   VAL C  57     -45.659  -1.068   3.996  1.00 59.45           N  
ANISOU 5342  N   VAL C  57     5785   7129   9674   -271   -946    301       N  
ATOM   5343  CA  VAL C  57     -45.255  -0.082   2.950  1.00 60.89           C  
ANISOU 5343  CA  VAL C  57     5982   7369   9782   -295   -925    371       C  
ATOM   5344  C   VAL C  57     -46.120   1.169   3.094  1.00 61.74           C  
ANISOU 5344  C   VAL C  57     6120   7420   9917   -289   -940    468       C  
ATOM   5345  O   VAL C  57     -46.999   1.181   3.967  1.00 61.31           O  
ANISOU 5345  O   VAL C  57     6061   7297   9934   -265   -968    467       O  
ATOM   5346  CB  VAL C  57     -45.352  -0.665   1.527  1.00 61.73           C  
ANISOU 5346  CB  VAL C  57     6082   7583   9787   -293   -942    348       C  
ATOM   5347  CG1 VAL C  57     -44.573  -1.965   1.405  1.00 61.66           C  
ANISOU 5347  CG1 VAL C  57     6048   7621   9758   -287   -929    242       C  
ATOM   5348  CG2 VAL C  57     -46.794  -0.844   1.076  1.00 62.03           C  
ANISOU 5348  CG2 VAL C  57     6121   7637   9811   -265  -1001    360       C  
ATOM   5349  N   LEU C  58     -45.866   2.178   2.261  1.00 63.69           N  
ANISOU 5349  N   LEU C  58     6401   7692  10104   -308   -919    548       N  
ATOM   5350  CA  LEU C  58     -46.605   3.464   2.270  1.00 64.94           C  
ANISOU 5350  CA  LEU C  58     6607   7789  10278   -291   -930    651       C  
ATOM   5351  C   LEU C  58     -47.768   3.352   1.296  1.00 66.16           C  
ANISOU 5351  C   LEU C  58     6763   8004  10367   -241   -991    682       C  
ATOM   5352  O   LEU C  58     -47.616   2.763   0.230  1.00 67.11           O  
ANISOU 5352  O   LEU C  58     6872   8227  10399   -245  -1000    659       O  
ATOM   5353  CB  LEU C  58     -45.655   4.596   1.863  1.00 65.86           C  
ANISOU 5353  CB  LEU C  58     6774   7892  10356   -343   -869    725       C  
ATOM   5354  CG  LEU C  58     -45.869   5.922   2.593  1.00 65.86           C  
ANISOU 5354  CG  LEU C  58     6827   7772  10424   -346   -848    801       C  
ATOM   5355  CD1 LEU C  58     -45.441   5.811   4.052  1.00 64.92           C  
ANISOU 5355  CD1 LEU C  58     6674   7583  10408   -368   -824    738       C  
ATOM   5356  CD2 LEU C  58     -45.125   7.052   1.894  1.00 66.84           C  
ANISOU 5356  CD2 LEU C  58     7022   7883  10490   -402   -787    887       C  
ATOM   5357  N   PRO C  59     -48.969   3.867   1.644  1.00 67.60           N  
ANISOU 5357  N   PRO C  59     6953   8139  10590   -188  -1035    724       N  
ATOM   5358  CA  PRO C  59     -49.979   4.196   0.643  1.00 69.65           C  
ANISOU 5358  CA  PRO C  59     7225   8463  10775   -131  -1089    781       C  
ATOM   5359  C   PRO C  59     -49.355   5.060  -0.466  1.00 72.02           C  
ANISOU 5359  C   PRO C  59     7591   8793  10978   -144  -1058    877       C  
ATOM   5360  O   PRO C  59     -49.354   6.271  -0.356  1.00 72.46           O  
ANISOU 5360  O   PRO C  59     7715   8770  11047   -131  -1038    973       O  
ATOM   5361  CB  PRO C  59     -51.058   4.941   1.445  1.00 69.43           C  
ANISOU 5361  CB  PRO C  59     7202   8354  10822    -72  -1122    820       C  
ATOM   5362  CG  PRO C  59     -50.920   4.395   2.849  1.00 67.97           C  
ANISOU 5362  CG  PRO C  59     6978   8099  10747   -102  -1104    741       C  
ATOM   5363  CD  PRO C  59     -49.446   4.093   3.013  1.00 66.98           C  
ANISOU 5363  CD  PRO C  59     6863   7962  10624   -173  -1040    709       C  
ATOM   5364  N   ASN C  60     -48.782   4.393  -1.470  1.00 74.22           N  
ANISOU 5364  N   ASN C  60     7856   9182  11163   -175  -1048    845       N  
ATOM   5365  CA  ASN C  60     -48.338   4.983  -2.760  1.00 76.77           C  
ANISOU 5365  CA  ASN C  60     8233   9573  11362   -188  -1027    928       C  
ATOM   5366  C   ASN C  60     -49.118   4.257  -3.865  1.00 77.11           C  
ANISOU 5366  C   ASN C  60     8237   9757  11303   -143  -1091    899       C  
ATOM   5367  O   ASN C  60     -48.489   3.743  -4.810  1.00 78.07           O  
ANISOU 5367  O   ASN C  60     8348   9984  11329   -179  -1072    870       O  
ATOM   5368  CB  ASN C  60     -46.812   4.941  -2.907  1.00 78.19           C  
ANISOU 5368  CB  ASN C  60     8423   9768  11517   -276   -945    908       C  
ATOM   5369  CG  ASN C  60     -46.198   3.606  -2.533  1.00 79.53           C  
ANISOU 5369  CG  ASN C  60     8517   9984  11717   -307   -935    772       C  
ATOM   5370  OD1 ASN C  60     -46.835   2.561  -2.670  1.00 80.86           O  
ANISOU 5370  OD1 ASN C  60     8634  10207  11880   -274   -986    694       O  
ATOM   5371  ND2 ASN C  60     -44.961   3.628  -2.054  1.00 79.06           N  
ANISOU 5371  ND2 ASN C  60     8449   9902  11688   -369   -869    738       N  
ATOM   5372  N   ASP C  61     -50.448   4.220  -3.714  1.00 76.26           N  
ANISOU 5372  N   ASP C  61     8102   9658  11215    -71  -1162    898       N  
ATOM   5373  CA  ASP C  61     -51.405   3.433  -4.540  1.00 76.37           C  
ANISOU 5373  CA  ASP C  61     8056   9809  11150    -29  -1233    844       C  
ATOM   5374  C   ASP C  61     -52.822   3.602  -3.963  1.00 75.20           C  
ANISOU 5374  C   ASP C  61     7871   9641  11058     44  -1300    841       C  
ATOM   5375  O   ASP C  61     -52.959   3.732  -2.722  1.00 73.30           O  
ANISOU 5375  O   ASP C  61     7623   9287  10940     39  -1287    822       O  
ATOM   5376  CB  ASP C  61     -50.975   1.962  -4.611  1.00 76.10           C  
ANISOU 5376  CB  ASP C  61     7959   9840  11116    -86  -1222    704       C  
ATOM   5377  CG  ASP C  61     -52.058   0.973  -5.026  1.00 76.67           C  
ANISOU 5377  CG  ASP C  61     7957  10020  11152    -63  -1289    610       C  
ATOM   5378  OD1 ASP C  61     -51.940  -0.205  -4.636  1.00 76.83           O  
ANISOU 5378  OD1 ASP C  61     7934  10037  11218   -106  -1281    490       O  
ATOM   5379  OD2 ASP C  61     -52.998   1.373  -5.747  1.00 76.94           O  
ANISOU 5379  OD2 ASP C  61     7982  10143  11109     -3  -1348    655       O  
ATOM   5380  N   ASP C  62     -53.831   3.605  -4.841  1.00 75.03           N  
ANISOU 5380  N   ASP C  62     7820   9741  10945    110  -1370    854       N  
ATOM   5381  CA  ASP C  62     -55.279   3.646  -4.490  1.00 73.98           C  
ANISOU 5381  CA  ASP C  62     7628   9639  10841    185  -1443    831       C  
ATOM   5382  C   ASP C  62     -55.601   2.541  -3.473  1.00 71.64           C  
ANISOU 5382  C   ASP C  62     7253   9314  10650    130  -1441    695       C  
ATOM   5383  O   ASP C  62     -55.960   2.881  -2.321  1.00 71.00           O  
ANISOU 5383  O   ASP C  62     7168   9130  10679    144  -1436    697       O  
ATOM   5384  CB  ASP C  62     -56.154   3.519  -5.741  1.00 74.78           C  
ANISOU 5384  CB  ASP C  62     7688   9918  10806    249  -1517    833       C  
ATOM   5385  CG  ASP C  62     -56.836   4.812  -6.141  1.00 75.86           C  
ANISOU 5385  CG  ASP C  62     7874  10063  10885    369  -1564    966       C  
ATOM   5386  OD1 ASP C  62     -58.081   4.841  -6.111  1.00 76.84           O  
ANISOU 5386  OD1 ASP C  62     7930  10265  11000    449  -1638    941       O  
ATOM   5387  OD2 ASP C  62     -56.120   5.775  -6.478  1.00 76.21           O  
ANISOU 5387  OD2 ASP C  62     8024  10037  10892    382  -1525   1092       O  
ATOM   5388  N   THR C  63     -55.464   1.271  -3.879  1.00 69.35           N  
ANISOU 5388  N   THR C  63     6913   9108  10326     70  -1441    581       N  
ATOM   5389  CA  THR C  63     -55.756   0.065  -3.055  1.00 66.75           C  
ANISOU 5389  CA  THR C  63     6525   8754  10082      9  -1434    447       C  
ATOM   5390  C   THR C  63     -55.385   0.339  -1.593  1.00 65.21           C  
ANISOU 5390  C   THR C  63     6357   8395  10022    -10  -1389    461       C  
ATOM   5391  O   THR C  63     -56.252   0.137  -0.720  1.00 65.03           O  
ANISOU 5391  O   THR C  63     6291   8343  10073     -8  -1408    415       O  
ATOM   5392  CB  THR C  63     -55.007  -1.166  -3.582  1.00 65.47           C  
ANISOU 5392  CB  THR C  63     6355   8637   9880    -62  -1404    348       C  
ATOM   5393  OG1 THR C  63     -55.386  -1.370  -4.943  1.00 65.64           O  
ANISOU 5393  OG1 THR C  63     6347   8821   9770    -44  -1447    331       O  
ATOM   5394  CG2 THR C  63     -55.291  -2.419  -2.784  1.00 64.44           C  
ANISOU 5394  CG2 THR C  63     6187   8465   9831   -124  -1392    218       C  
ATOM   5395  N   LEU C  64     -54.159   0.822  -1.365  1.00 64.15           N  
ANISOU 5395  N   LEU C  64     6289   8172   9910    -32  -1330    521       N  
ATOM   5396  CA  LEU C  64     -53.513   0.966  -0.032  1.00 62.37           C  
ANISOU 5396  CA  LEU C  64     6090   7803   9801    -63  -1279    521       C  
ATOM   5397  C   LEU C  64     -53.854   2.325   0.594  1.00 61.72           C  
ANISOU 5397  C   LEU C  64     6041   7635   9772    -11  -1281    619       C  
ATOM   5398  O   LEU C  64     -53.713   2.443   1.826  1.00 60.11           O  
ANISOU 5398  O   LEU C  64     5840   7327   9670    -28  -1254    606       O  
ATOM   5399  CB  LEU C  64     -52.002   0.801  -0.211  1.00 62.18           C  
ANISOU 5399  CB  LEU C  64     6109   7755   9762   -113  -1217    522       C  
ATOM   5400  CG  LEU C  64     -51.565  -0.484  -0.912  1.00 62.21           C  
ANISOU 5400  CG  LEU C  64     6087   7842   9707   -152  -1211    425       C  
ATOM   5401  CD1 LEU C  64     -50.079  -0.438  -1.246  1.00 62.15           C  
ANISOU 5401  CD1 LEU C  64     6113   7835   9666   -187  -1152    436       C  
ATOM   5402  CD2 LEU C  64     -51.898  -1.705  -0.064  1.00 61.22           C  
ANISOU 5402  CD2 LEU C  64     5928   7676   9655   -181  -1213    314       C  
ATOM   5403  N   ARG C  65     -54.255   3.312  -0.215  1.00 62.40           N  
ANISOU 5403  N   ARG C  65     6158   7761   9789     52  -1312    714       N  
ATOM   5404  CA  ARG C  65     -54.857   4.581   0.279  1.00 63.09           C  
ANISOU 5404  CA  ARG C  65     6278   7773   9921    124  -1328    802       C  
ATOM   5405  C   ARG C  65     -56.223   4.262   0.904  1.00 62.73           C  
ANISOU 5405  C   ARG C  65     6152   7757   9923    166  -1382    738       C  
ATOM   5406  O   ARG C  65     -56.534   4.848   1.956  1.00 62.47           O  
ANISOU 5406  O   ARG C  65     6122   7629   9981    190  -1374    752       O  
ATOM   5407  CB  ARG C  65     -54.966   5.623  -0.840  1.00 64.99           C  
ANISOU 5407  CB  ARG C  65     6581   8049  10060    193  -1349    922       C  
ATOM   5408  CG  ARG C  65     -53.833   6.640  -0.856  1.00 65.68           C  
ANISOU 5408  CG  ARG C  65     6775   8029  10151    164  -1281   1023       C  
ATOM   5409  CD  ARG C  65     -53.936   7.631  -2.004  1.00 67.42           C  
ANISOU 5409  CD  ARG C  65     7076   8278  10263    228  -1297   1150       C  
ATOM   5410  NE  ARG C  65     -53.147   7.229  -3.164  1.00 68.16           N  
ANISOU 5410  NE  ARG C  65     7188   8467  10241    176  -1274   1160       N  
ATOM   5411  CZ  ARG C  65     -51.837   7.443  -3.318  1.00 68.37           C  
ANISOU 5411  CZ  ARG C  65     7273   8450  10253     90  -1196   1189       C  
ATOM   5412  NH1 ARG C  65     -51.134   8.061  -2.381  1.00 67.93           N  
ANISOU 5412  NH1 ARG C  65     7263   8254  10292     41  -1132   1209       N  
ATOM   5413  NH2 ARG C  65     -51.228   7.032  -4.417  1.00 69.00           N  
ANISOU 5413  NH2 ARG C  65     7357   8639  10219     50  -1180   1189       N  
ATOM   5414  N   VAL C  66     -56.981   3.340   0.298  1.00 62.93           N  
ANISOU 5414  N   VAL C  66     6104   7916   9891    165  -1430    661       N  
ATOM   5415  CA  VAL C  66     -58.339   2.907   0.756  1.00 62.80           C  
ANISOU 5415  CA  VAL C  66     5994   7961   9904    189  -1481    581       C  
ATOM   5416  C   VAL C  66     -58.202   1.991   1.981  1.00 62.10           C  
ANISOU 5416  C   VAL C  66     5877   7799   9919    104  -1440    485       C  
ATOM   5417  O   VAL C  66     -58.846   2.287   3.008  1.00 61.80           O  
ANISOU 5417  O   VAL C  66     5810   7711   9960    122  -1443    472       O  
ATOM   5418  CB  VAL C  66     -59.123   2.197  -0.364  1.00 62.94           C  
ANISOU 5418  CB  VAL C  66     5941   8156   9816    199  -1540    520       C  
ATOM   5419  CG1 VAL C  66     -60.507   1.793   0.117  1.00 63.27           C  
ANISOU 5419  CG1 VAL C  66     5879   8274   9887    212  -1586    430       C  
ATOM   5420  CG2 VAL C  66     -59.211   3.041  -1.627  1.00 63.89           C  
ANISOU 5420  CG2 VAL C  66     6095   8362   9817    288  -1582    620       C  
ATOM   5421  N   GLU C  67     -57.414   0.914   1.860  1.00 61.68           N  
ANISOU 5421  N   GLU C  67     5833   7741   9859     21  -1403    420       N  
ATOM   5422  CA  GLU C  67     -57.169  -0.098   2.927  1.00 60.87           C  
ANISOU 5422  CA  GLU C  67     5721   7565   9839    -56  -1362    332       C  
ATOM   5423  C   GLU C  67     -56.627   0.584   4.196  1.00 59.95           C  
ANISOU 5423  C   GLU C  67     5646   7309   9821    -53  -1319    380       C  
ATOM   5424  O   GLU C  67     -57.220   0.364   5.274  1.00 60.52           O  
ANISOU 5424  O   GLU C  67     5687   7340   9967    -69  -1314    336       O  
ATOM   5425  CB  GLU C  67     -56.213  -1.187   2.429  1.00 60.54           C  
ANISOU 5425  CB  GLU C  67     5705   7533   9763   -119  -1330    275       C  
ATOM   5426  CG  GLU C  67     -56.852  -2.151   1.439  1.00 61.36           C  
ANISOU 5426  CG  GLU C  67     5759   7764   9788   -144  -1365    189       C  
ATOM   5427  CD  GLU C  67     -55.901  -3.162   0.818  1.00 61.05           C  
ANISOU 5427  CD  GLU C  67     5750   7738   9707   -194  -1335    130       C  
ATOM   5428  OE1 GLU C  67     -54.806  -3.349   1.374  1.00 61.54           O  
ANISOU 5428  OE1 GLU C  67     5862   7704   9814   -215  -1285    137       O  
ATOM   5429  OE2 GLU C  67     -56.253  -3.756  -0.220  1.00 60.80           O  
ANISOU 5429  OE2 GLU C  67     5686   7820   9592   -208  -1363     72       O  
ATOM   5430  N   ALA C  68     -55.552   1.375   4.084  1.00 58.89           N  
ANISOU 5430  N   ALA C  68     5577   7113   9684    -41  -1285    460       N  
ATOM   5431  CA  ALA C  68     -54.927   2.101   5.217  1.00 57.61           C  
ANISOU 5431  CA  ALA C  68     5454   6826   9607    -45  -1241    500       C  
ATOM   5432  C   ALA C  68     -55.997   2.940   5.928  1.00 57.11           C  
ANISOU 5432  C   ALA C  68     5366   6733   9598      9  -1268    525       C  
ATOM   5433  O   ALA C  68     -56.229   2.707   7.130  1.00 55.68           O  
ANISOU 5433  O   ALA C  68     5162   6495   9495    -12  -1251    481       O  
ATOM   5434  CB  ALA C  68     -53.774   2.954   4.741  1.00 57.57           C  
ANISOU 5434  CB  ALA C  68     5516   6784   9573    -45  -1205    582       C  
ATOM   5435  N   PHE C  69     -56.648   3.856   5.203  1.00 57.93           N  
ANISOU 5435  N   PHE C  69     5475   6879   9656     86  -1309    592       N  
ATOM   5436  CA  PHE C  69     -57.729   4.727   5.736  1.00 58.08           C  
ANISOU 5436  CA  PHE C  69     5469   6881   9717    163  -1342    616       C  
ATOM   5437  C   PHE C  69     -58.831   3.851   6.349  1.00 58.02           C  
ANISOU 5437  C   PHE C  69     5367   6936   9740    143  -1368    514       C  
ATOM   5438  O   PHE C  69     -59.267   4.165   7.466  1.00 57.42           O  
ANISOU 5438  O   PHE C  69     5269   6806   9742    153  -1358    495       O  
ATOM   5439  CB  PHE C  69     -58.283   5.672   4.666  1.00 58.76           C  
ANISOU 5439  CB  PHE C  69     5576   7023   9727    263  -1392    700       C  
ATOM   5440  CG  PHE C  69     -59.497   6.433   5.128  1.00 59.49           C  
ANISOU 5440  CG  PHE C  69     5629   7119   9852    359  -1436    710       C  
ATOM   5441  CD1 PHE C  69     -59.424   7.274   6.228  1.00 59.32           C  
ANISOU 5441  CD1 PHE C  69     5639   6974   9923    380  -1405    733       C  
ATOM   5442  CD2 PHE C  69     -60.727   6.268   4.506  1.00 60.72           C  
ANISOU 5442  CD2 PHE C  69     5707   7415   9947    429  -1507    681       C  
ATOM   5443  CE1 PHE C  69     -60.549   7.947   6.682  1.00 59.97           C  
ANISOU 5443  CE1 PHE C  69     5681   7066  10039    475  -1444    731       C  
ATOM   5444  CE2 PHE C  69     -61.851   6.946   4.957  1.00 61.06           C  
ANISOU 5444  CE2 PHE C  69     5702   7476  10019    527  -1549    680       C  
ATOM   5445  CZ  PHE C  69     -61.760   7.784   6.044  1.00 60.85           C  
ANISOU 5445  CZ  PHE C  69     5713   7319  10088    553  -1517    705       C  
ATOM   5446  N   GLU C  70     -59.243   2.775   5.665  1.00 59.06           N  
ANISOU 5446  N   GLU C  70     5447   7180   9813    108  -1395    444       N  
ATOM   5447  CA  GLU C  70     -60.312   1.848   6.145  1.00 60.07           C  
ANISOU 5447  CA  GLU C  70     5486   7377   9960     68  -1412    337       C  
ATOM   5448  C   GLU C  70     -59.916   1.239   7.500  1.00 58.79           C  
ANISOU 5448  C   GLU C  70     5337   7113   9888    -10  -1356    287       C  
ATOM   5449  O   GLU C  70     -60.833   0.979   8.312  1.00 59.26           O  
ANISOU 5449  O   GLU C  70     5335   7190   9989    -29  -1358    227       O  
ATOM   5450  CB  GLU C  70     -60.615   0.737   5.129  1.00 61.34           C  
ANISOU 5450  CB  GLU C  70     5604   7661  10041     22  -1438    264       C  
ATOM   5451  CG  GLU C  70     -61.694   1.095   4.112  1.00 63.11           C  
ANISOU 5451  CG  GLU C  70     5760   8037  10181     97  -1511    264       C  
ATOM   5452  CD  GLU C  70     -62.388  -0.092   3.456  1.00 64.52           C  
ANISOU 5452  CD  GLU C  70     5861   8353  10297     35  -1537    152       C  
ATOM   5453  OE1 GLU C  70     -62.625  -1.098   4.155  1.00 65.04           O  
ANISOU 5453  OE1 GLU C  70     5899   8401  10412    -59  -1505     56       O  
ATOM   5454  OE2 GLU C  70     -62.696  -0.010   2.246  1.00 65.81           O  
ANISOU 5454  OE2 GLU C  70     5997   8645  10362     80  -1588    158       O  
ATOM   5455  N   TYR C  71     -58.613   1.024   7.735  1.00 57.27           N  
ANISOU 5455  N   TYR C  71     5215   6828   9715    -52  -1306    309       N  
ATOM   5456  CA  TYR C  71     -58.049   0.332   8.927  1.00 55.44           C  
ANISOU 5456  CA  TYR C  71     5006   6506   9551   -120  -1254    267       C  
ATOM   5457  C   TYR C  71     -57.663   1.343  10.018  1.00 54.05           C  
ANISOU 5457  C   TYR C  71     4858   6229   9447    -92  -1226    318       C  
ATOM   5458  O   TYR C  71     -58.050   1.141  11.187  1.00 53.68           O  
ANISOU 5458  O   TYR C  71     4790   6146   9459   -117  -1207    279       O  
ATOM   5459  CB  TYR C  71     -56.846  -0.521   8.513  1.00 55.26           C  
ANISOU 5459  CB  TYR C  71     5036   6459   9499   -167  -1223    252       C  
ATOM   5460  CG  TYR C  71     -56.399  -1.524   9.546  1.00 54.78           C  
ANISOU 5460  CG  TYR C  71     4999   6327   9487   -227  -1180    196       C  
ATOM   5461  CD1 TYR C  71     -57.209  -2.589   9.901  1.00 55.21           C  
ANISOU 5461  CD1 TYR C  71     5027   6399   9551   -282  -1178    117       C  
ATOM   5462  CD2 TYR C  71     -55.164  -1.421  10.165  1.00 54.18           C  
ANISOU 5462  CD2 TYR C  71     4974   6169   9442   -231  -1139    222       C  
ATOM   5463  CE1 TYR C  71     -56.814  -3.518  10.850  1.00 54.65           C  
ANISOU 5463  CE1 TYR C  71     4995   6251   9517   -332  -1137     77       C  
ATOM   5464  CE2 TYR C  71     -54.753  -2.341  11.116  1.00 53.79           C  
ANISOU 5464  CE2 TYR C  71     4951   6058   9426   -269  -1105    178       C  
ATOM   5465  CZ  TYR C  71     -55.580  -3.398  11.462  1.00 53.76           C  
ANISOU 5465  CZ  TYR C  71     4936   6058   9431   -317  -1103    111       C  
ATOM   5466  OH  TYR C  71     -55.193  -4.315  12.400  1.00 52.85           O  
ANISOU 5466  OH  TYR C  71     4864   5872   9344   -351  -1067     77       O  
ATOM   5467  N   TYR C  72     -56.921   2.394   9.652  1.00 52.88           N  
ANISOU 5467  N   TYR C  72     4760   6039   9291    -50  -1218    398       N  
ATOM   5468  CA  TYR C  72     -56.313   3.375  10.593  1.00 51.70           C  
ANISOU 5468  CA  TYR C  72     4649   5788   9207    -38  -1182    442       C  
ATOM   5469  C   TYR C  72     -57.251   4.572  10.817  1.00 51.19           C  
ANISOU 5469  C   TYR C  72     4568   5710   9170     37  -1209    480       C  
ATOM   5470  O   TYR C  72     -57.142   5.203  11.879  1.00 50.29           O  
ANISOU 5470  O   TYR C  72     4464   5519   9124     42  -1182    484       O  
ATOM   5471  CB  TYR C  72     -54.926   3.786  10.088  1.00 51.66           C  
ANISOU 5471  CB  TYR C  72     4710   5741   9177    -53  -1148    496       C  
ATOM   5472  CG  TYR C  72     -53.948   2.641  10.012  1.00 50.98           C  
ANISOU 5472  CG  TYR C  72     4634   5667   9069   -113  -1121    450       C  
ATOM   5473  CD1 TYR C  72     -53.551   2.108   8.796  1.00 51.25           C  
ANISOU 5473  CD1 TYR C  72     4679   5767   9027   -123  -1130    450       C  
ATOM   5474  CD2 TYR C  72     -53.447   2.062  11.164  1.00 50.35           C  
ANISOU 5474  CD2 TYR C  72     4554   5537   9039   -151  -1087    404       C  
ATOM   5475  CE1 TYR C  72     -52.672   1.041   8.727  1.00 50.79           C  
ANISOU 5475  CE1 TYR C  72     4629   5717   8949   -166  -1106    400       C  
ATOM   5476  CE2 TYR C  72     -52.561   0.997  11.113  1.00 49.98           C  
ANISOU 5476  CE2 TYR C  72     4521   5497   8969   -187  -1066    361       C  
ATOM   5477  CZ  TYR C  72     -52.175   0.482   9.891  1.00 50.09           C  
ANISOU 5477  CZ  TYR C  72     4545   5572   8914   -193  -1075    356       C  
ATOM   5478  OH  TYR C  72     -51.313  -0.573   9.858  1.00 49.74           O  
ANISOU 5478  OH  TYR C  72     4516   5532   8850   -217  -1054    308       O  
ATOM   5479  N   HIS C  73     -58.133   4.873   9.856  1.00 51.67           N  
ANISOU 5479  N   HIS C  73     4603   5849   9178    100  -1261    503       N  
ATOM   5480  CA  HIS C  73     -59.169   5.947   9.919  1.00 52.08           C  
ANISOU 5480  CA  HIS C  73     4634   5909   9244    197  -1299    535       C  
ATOM   5481  C   HIS C  73     -58.522   7.323   9.738  1.00 52.92           C  
ANISOU 5481  C   HIS C  73     4829   5914   9361    249  -1280    634       C  
ATOM   5482  O   HIS C  73     -59.250   8.334   9.845  1.00 53.33           O  
ANISOU 5482  O   HIS C  73     4886   5944   9433    341  -1305    669       O  
ATOM   5483  CB  HIS C  73     -59.987   5.867  11.218  1.00 51.05           C  
ANISOU 5483  CB  HIS C  73     4439   5769   9185    194  -1294    468       C  
ATOM   5484  CG  HIS C  73     -61.199   5.006  11.110  1.00 51.13           C  
ANISOU 5484  CG  HIS C  73     4352   5905   9170    185  -1332    388       C  
ATOM   5485  ND1 HIS C  73     -62.173   4.980  12.088  1.00 50.98           N  
ANISOU 5485  ND1 HIS C  73     4259   5912   9197    189  -1335    325       N  
ATOM   5486  CD2 HIS C  73     -61.613   4.161  10.141  1.00 51.42           C  
ANISOU 5486  CD2 HIS C  73     4346   6055   9134    165  -1367    353       C  
ATOM   5487  CE1 HIS C  73     -63.123   4.140  11.735  1.00 51.28           C  
ANISOU 5487  CE1 HIS C  73     4213   6074   9194    164  -1366    253       C  
ATOM   5488  NE2 HIS C  73     -62.805   3.625  10.546  1.00 51.50           N  
ANISOU 5488  NE2 HIS C  73     4259   6156   9151    149  -1387    267       N  
ATOM   5489  N   THR C  74     -57.224   7.357   9.422  1.00 52.78           N  
ANISOU 5489  N   THR C  74     4882   5841   9328    194  -1236    673       N  
ATOM   5490  CA  THR C  74     -56.417   8.598   9.313  1.00 53.27           C  
ANISOU 5490  CA  THR C  74     5040   5797   9403    209  -1199    759       C  
ATOM   5491  C   THR C  74     -55.761   8.638   7.930  1.00 53.66           C  
ANISOU 5491  C   THR C  74     5144   5882   9360    200  -1199    825       C  
ATOM   5492  O   THR C  74     -55.434   7.562   7.401  1.00 53.40           O  
ANISOU 5492  O   THR C  74     5080   5932   9277    149  -1203    785       O  
ATOM   5493  CB  THR C  74     -55.416   8.692  10.470  1.00 52.55           C  
ANISOU 5493  CB  THR C  74     4970   5610   9386    133  -1134    730       C  
ATOM   5494  OG1 THR C  74     -54.648   9.878  10.268  1.00 53.54           O  
ANISOU 5494  OG1 THR C  74     5187   5637   9517    132  -1094    806       O  
ATOM   5495  CG2 THR C  74     -54.505   7.489  10.572  1.00 51.92           C  
ANISOU 5495  CG2 THR C  74     4867   5568   9290     43  -1106    674       C  
ATOM   5496  N   THR C  75     -55.606   9.839   7.372  1.00 54.46           N  
ANISOU 5496  N   THR C  75     5332   5920   9439    250  -1191    923       N  
ATOM   5497  CA  THR C  75     -55.073  10.087   6.006  1.00 55.36           C  
ANISOU 5497  CA  THR C  75     5513   6065   9454    251  -1189   1005       C  
ATOM   5498  C   THR C  75     -53.676  10.727   6.117  1.00 55.48           C  
ANISOU 5498  C   THR C  75     5616   5977   9486    169  -1108   1049       C  
ATOM   5499  O   THR C  75     -53.026  10.915   5.064  1.00 56.41           O  
ANISOU 5499  O   THR C  75     5793   6116   9523    143  -1088   1112       O  
ATOM   5500  CB  THR C  75     -56.093  10.914   5.206  1.00 56.77           C  
ANISOU 5500  CB  THR C  75     5726   6265   9579    378  -1247   1087       C  
ATOM   5501  OG1 THR C  75     -57.348  10.862   5.889  1.00 56.24           O  
ANISOU 5501  OG1 THR C  75     5581   6226   9561    455  -1298   1034       O  
ATOM   5502  CG2 THR C  75     -56.279  10.433   3.783  1.00 57.33           C  
ANISOU 5502  CG2 THR C  75     5787   6468   9525    403  -1291   1117       C  
ATOM   5503  N   ASP C  76     -53.229  11.032   7.343  1.00 54.57           N  
ANISOU 5503  N   ASP C  76     5503   5765   9465    122  -1061   1010       N  
ATOM   5504  CA  ASP C  76     -51.903  11.629   7.662  1.00 54.38           C  
ANISOU 5504  CA  ASP C  76     5543   5649   9468     31   -979   1027       C  
ATOM   5505  C   ASP C  76     -50.800  10.704   7.151  1.00 53.86           C  
ANISOU 5505  C   ASP C  76     5451   5667   9345    -59   -950    992       C  
ATOM   5506  O   ASP C  76     -50.650   9.588   7.644  1.00 53.35           O  
ANISOU 5506  O   ASP C  76     5307   5665   9297    -89   -958    905       O  
ATOM   5507  CB  ASP C  76     -51.769  11.870   9.170  1.00 53.68           C  
ANISOU 5507  CB  ASP C  76     5430   5477   9487      1   -948    963       C  
ATOM   5508  CG  ASP C  76     -50.366  12.233   9.634  1.00 53.41           C  
ANISOU 5508  CG  ASP C  76     5431   5383   9480   -106   -867    947       C  
ATOM   5509  OD1 ASP C  76     -49.583  12.732   8.801  1.00 54.39           O  
ANISOU 5509  OD1 ASP C  76     5625   5490   9551   -154   -825   1007       O  
ATOM   5510  OD2 ASP C  76     -50.071  12.017  10.828  1.00 52.11           O  
ANISOU 5510  OD2 ASP C  76     5218   5196   9383   -145   -845    871       O  
ATOM   5511  N   PRO C  77     -49.959  11.142   6.186  1.00 54.17           N  
ANISOU 5511  N   PRO C  77     5559   5708   9314   -104   -909   1057       N  
ATOM   5512  CA  PRO C  77     -48.997  10.243   5.550  1.00 53.69           C  
ANISOU 5512  CA  PRO C  77     5465   5747   9185   -176   -886   1021       C  
ATOM   5513  C   PRO C  77     -47.704  10.050   6.361  1.00 52.95           C  
ANISOU 5513  C   PRO C  77     5344   5636   9135   -275   -819    952       C  
ATOM   5514  O   PRO C  77     -46.819   9.357   5.884  1.00 52.79           O  
ANISOU 5514  O   PRO C  77     5295   5701   9061   -330   -796    916       O  
ATOM   5515  CB  PRO C  77     -48.736  10.954   4.216  1.00 54.84           C  
ANISOU 5515  CB  PRO C  77     5699   5901   9233   -179   -867   1126       C  
ATOM   5516  CG  PRO C  77     -48.844  12.426   4.560  1.00 55.71           C  
ANISOU 5516  CG  PRO C  77     5911   5863   9390   -168   -833   1207       C  
ATOM   5517  CD  PRO C  77     -49.861  12.518   5.679  1.00 55.21           C  
ANISOU 5517  CD  PRO C  77     5808   5741   9425    -93   -876   1167       C  
ATOM   5518  N   SER C  78     -47.627  10.661   7.550  1.00 52.19           N  
ANISOU 5518  N   SER C  78     5255   5443   9131   -292   -792    930       N  
ATOM   5519  CA  SER C  78     -46.529  10.492   8.539  1.00 51.25           C  
ANISOU 5519  CA  SER C  78     5095   5316   9060   -374   -738    852       C  
ATOM   5520  C   SER C  78     -46.865   9.370   9.532  1.00 50.05           C  
ANISOU 5520  C   SER C  78     4854   5206   8956   -344   -777    760       C  
ATOM   5521  O   SER C  78     -45.942   8.916  10.240  1.00 48.98           O  
ANISOU 5521  O   SER C  78     4673   5097   8840   -395   -746    689       O  
ATOM   5522  CB  SER C  78     -46.242  11.797   9.253  1.00 51.77           C  
ANISOU 5522  CB  SER C  78     5221   5258   9190   -414   -684    874       C  
ATOM   5523  OG  SER C  78     -47.193  12.069  10.276  1.00 51.10           O  
ANISOU 5523  OG  SER C  78     5125   5102   9189   -353   -715    855       O  
ATOM   5524  N   PHE C  79     -48.134   8.938   9.581  1.00 50.09           N  
ANISOU 5524  N   PHE C  79     4836   5221   8973   -266   -841    760       N  
ATOM   5525  CA  PHE C  79     -48.663   7.990  10.597  1.00 48.91           C  
ANISOU 5525  CA  PHE C  79     4616   5091   8873   -241   -874    683       C  
ATOM   5526  C   PHE C  79     -47.847   6.697  10.567  1.00 48.43           C  
ANISOU 5526  C   PHE C  79     4508   5113   8779   -276   -868    614       C  
ATOM   5527  O   PHE C  79     -47.291   6.311  11.613  1.00 47.94           O  
ANISOU 5527  O   PHE C  79     4413   5045   8757   -299   -848    554       O  
ATOM   5528  CB  PHE C  79     -50.148   7.677  10.386  1.00 48.79           C  
ANISOU 5528  CB  PHE C  79     4579   5098   8857   -165   -939    691       C  
ATOM   5529  CG  PHE C  79     -50.682   6.713  11.416  1.00 47.77           C  
ANISOU 5529  CG  PHE C  79     4388   4988   8775   -157   -962    614       C  
ATOM   5530  CD1 PHE C  79     -50.990   7.148  12.696  1.00 47.37           C  
ANISOU 5530  CD1 PHE C  79     4324   4874   8801   -152   -951    589       C  
ATOM   5531  CD2 PHE C  79     -50.808   5.364  11.130  1.00 47.20           C  
ANISOU 5531  CD2 PHE C  79     4276   4990   8666   -163   -986    564       C  
ATOM   5532  CE1 PHE C  79     -51.439   6.261  13.660  1.00 46.66           C  
ANISOU 5532  CE1 PHE C  79     4182   4801   8743   -152   -964    523       C  
ATOM   5533  CE2 PHE C  79     -51.256   4.478  12.095  1.00 46.77           C  
ANISOU 5533  CE2 PHE C  79     4179   4939   8650   -166   -997    498       C  
ATOM   5534  CZ  PHE C  79     -51.571   4.928  13.358  1.00 46.49           C  
ANISOU 5534  CZ  PHE C  79     4132   4847   8685   -162   -986    482       C  
ATOM   5535  N   LEU C  80     -47.793   6.048   9.404  1.00 48.84           N  
ANISOU 5535  N   LEU C  80     4558   5242   8755   -270   -886    622       N  
ATOM   5536  CA  LEU C  80     -47.072   4.762   9.217  1.00 49.03           C  
ANISOU 5536  CA  LEU C  80     4544   5344   8741   -289   -884    555       C  
ATOM   5537  C   LEU C  80     -45.653   4.911   9.764  1.00 48.23           C  
ANISOU 5537  C   LEU C  80     4431   5244   8648   -342   -828    520       C  
ATOM   5538  O   LEU C  80     -45.313   4.195  10.725  1.00 47.07           O  
ANISOU 5538  O   LEU C  80     4248   5101   8535   -338   -827    455       O  
ATOM   5539  CB  LEU C  80     -47.053   4.396   7.731  1.00 50.44           C  
ANISOU 5539  CB  LEU C  80     4733   5603   8828   -285   -899    577       C  
ATOM   5540  CG  LEU C  80     -48.193   3.499   7.261  1.00 50.95           C  
ANISOU 5540  CG  LEU C  80     4776   5714   8869   -241   -958    555       C  
ATOM   5541  CD1 LEU C  80     -49.546   3.979   7.770  1.00 51.07           C  
ANISOU 5541  CD1 LEU C  80     4788   5681   8936   -196   -996    581       C  
ATOM   5542  CD2 LEU C  80     -48.190   3.430   5.750  1.00 52.05           C  
ANISOU 5542  CD2 LEU C  80     4930   5935   8911   -237   -971    587       C  
ATOM   5543  N   GLY C  81     -44.880   5.822   9.168  1.00 48.57           N  
ANISOU 5543  N   GLY C  81     4506   5290   8659   -390   -783    562       N  
ATOM   5544  CA  GLY C  81     -43.579   6.271   9.689  1.00 48.70           C  
ANISOU 5544  CA  GLY C  81     4508   5310   8686   -456   -723    531       C  
ATOM   5545  C   GLY C  81     -43.519   6.129  11.199  1.00 48.15           C  
ANISOU 5545  C   GLY C  81     4401   5202   8690   -448   -723    473       C  
ATOM   5546  O   GLY C  81     -42.778   5.256  11.666  1.00 48.74           O  
ANISOU 5546  O   GLY C  81     4425   5336   8755   -444   -720    402       O  
ATOM   5547  N   ARG C  82     -44.313   6.915  11.932  1.00 48.07           N  
ANISOU 5547  N   ARG C  82     4416   5102   8747   -434   -730    500       N  
ATOM   5548  CA  ARG C  82     -44.236   7.038  13.417  1.00 47.61           C  
ANISOU 5548  CA  ARG C  82     4327   5005   8757   -437   -721    450       C  
ATOM   5549  C   ARG C  82     -44.652   5.729  14.101  1.00 47.09           C  
ANISOU 5549  C   ARG C  82     4218   4970   8701   -384   -764    397       C  
ATOM   5550  O   ARG C  82     -44.052   5.410  15.151  1.00 46.41           O  
ANISOU 5550  O   ARG C  82     4095   4900   8635   -390   -752    339       O  
ATOM   5551  CB  ARG C  82     -45.098   8.203  13.905  1.00 47.76           C  
ANISOU 5551  CB  ARG C  82     4387   4919   8840   -429   -719    492       C  
ATOM   5552  CG  ARG C  82     -44.530   9.575  13.569  1.00 48.45           C  
ANISOU 5552  CG  ARG C  82     4529   4948   8931   -492   -662    533       C  
ATOM   5553  CD  ARG C  82     -45.637  10.558  13.253  1.00 48.80           C  
ANISOU 5553  CD  ARG C  82     4644   4894   9004   -451   -677    611       C  
ATOM   5554  NE  ARG C  82     -46.711  10.477  14.234  1.00 47.98           N  
ANISOU 5554  NE  ARG C  82     4516   4749   8963   -388   -716    588       N  
ATOM   5555  CZ  ARG C  82     -47.998  10.678  13.983  1.00 48.11           C  
ANISOU 5555  CZ  ARG C  82     4553   4730   8993   -312   -762    632       C  
ATOM   5556  NH1 ARG C  82     -48.414  10.973  12.763  1.00 48.90           N  
ANISOU 5556  NH1 ARG C  82     4704   4829   9045   -279   -780    708       N  
ATOM   5557  NH2 ARG C  82     -48.876  10.583  14.964  1.00 47.76           N  
ANISOU 5557  NH2 ARG C  82     4475   4664   9005   -267   -789    597       N  
ATOM   5558  N   TYR C  83     -45.639   5.008  13.549  1.00 47.53           N  
ANISOU 5558  N   TYR C  83     4281   5034   8740   -338   -810    414       N  
ATOM   5559  CA  TYR C  83     -46.133   3.712  14.096  1.00 47.02           C  
ANISOU 5559  CA  TYR C  83     4194   4989   8683   -299   -845    367       C  
ATOM   5560  C   TYR C  83     -44.983   2.697  14.056  1.00 46.87           C  
ANISOU 5560  C   TYR C  83     4152   5034   8620   -300   -833    313       C  
ATOM   5561  O   TYR C  83     -44.620   2.131  15.107  1.00 45.84           O  
ANISOU 5561  O   TYR C  83     4002   4905   8508   -284   -831    267       O  
ATOM   5562  CB  TYR C  83     -47.393   3.228  13.363  1.00 46.94           C  
ANISOU 5562  CB  TYR C  83     4193   4983   8657   -267   -889    389       C  
ATOM   5563  CG  TYR C  83     -47.836   1.833  13.741  1.00 46.23           C  
ANISOU 5563  CG  TYR C  83     4090   4909   8566   -247   -914    339       C  
ATOM   5564  CD1 TYR C  83     -47.915   1.449  15.072  1.00 45.50           C  
ANISOU 5564  CD1 TYR C  83     3987   4784   8515   -242   -909    304       C  
ATOM   5565  CD2 TYR C  83     -48.154   0.887  12.774  1.00 46.06           C  
ANISOU 5565  CD2 TYR C  83     4073   4930   8496   -238   -939    325       C  
ATOM   5566  CE1 TYR C  83     -48.289   0.165  15.432  1.00 45.23           C  
ANISOU 5566  CE1 TYR C  83     3958   4750   8476   -230   -924    264       C  
ATOM   5567  CE2 TYR C  83     -48.534  -0.401  13.119  1.00 45.70           C  
ANISOU 5567  CE2 TYR C  83     4030   4883   8451   -230   -954    276       C  
ATOM   5568  CZ  TYR C  83     -48.606  -0.762  14.454  1.00 45.40           C  
ANISOU 5568  CZ  TYR C  83     3992   4802   8456   -227   -944    249       C  
ATOM   5569  OH  TYR C  83     -48.982  -2.022  14.825  1.00 44.99           O  
ANISOU 5569  OH  TYR C  83     3958   4733   8402   -224   -952    208       O  
ATOM   5570  N   MET C  84     -44.402   2.497  12.875  1.00 47.82           N  
ANISOU 5570  N   MET C  84     4276   5213   8681   -310   -826    318       N  
ATOM   5571  CA  MET C  84     -43.209   1.634  12.695  1.00 48.72           C  
ANISOU 5571  CA  MET C  84     4364   5400   8747   -303   -812    262       C  
ATOM   5572  C   MET C  84     -42.132   2.082  13.690  1.00 48.72           C  
ANISOU 5572  C   MET C  84     4329   5417   8765   -324   -777    225       C  
ATOM   5573  O   MET C  84     -41.658   1.221  14.461  1.00 48.87           O  
ANISOU 5573  O   MET C  84     4324   5460   8782   -284   -785    172       O  
ATOM   5574  CB  MET C  84     -42.676   1.719  11.263  1.00 50.15           C  
ANISOU 5574  CB  MET C  84     4548   5648   8858   -327   -797    276       C  
ATOM   5575  CG  MET C  84     -43.638   1.171  10.227  1.00 51.01           C  
ANISOU 5575  CG  MET C  84     4682   5764   8934   -304   -834    299       C  
ATOM   5576  SD  MET C  84     -43.926  -0.607  10.410  1.00 52.12           S  
ANISOU 5576  SD  MET C  84     4822   5913   9067   -250   -869    228       S  
ATOM   5577  CE  MET C  84     -45.498  -0.600  11.273  1.00 51.82           C  
ANISOU 5577  CE  MET C  84     4801   5789   9097   -238   -903    251       C  
ATOM   5578  N   SER C  85     -41.793   3.378  13.695  1.00 48.88           N  
ANISOU 5578  N   SER C  85     4349   5422   8800   -383   -739    252       N  
ATOM   5579  CA  SER C  85     -40.842   4.010  14.649  1.00 49.16           C  
ANISOU 5579  CA  SER C  85     4346   5474   8856   -421   -701    212       C  
ATOM   5580  C   SER C  85     -41.163   3.540  16.069  1.00 48.63           C  
ANISOU 5580  C   SER C  85     4262   5380   8833   -376   -725    176       C  
ATOM   5581  O   SER C  85     -40.336   2.822  16.667  1.00 49.09           O  
ANISOU 5581  O   SER C  85     4279   5502   8868   -345   -727    117       O  
ATOM   5582  CB  SER C  85     -40.872   5.514  14.577  1.00 49.67           C  
ANISOU 5582  CB  SER C  85     4438   5483   8951   -493   -660    253       C  
ATOM   5583  OG  SER C  85     -40.119   5.986  13.475  1.00 50.94           O  
ANISOU 5583  OG  SER C  85     4605   5689   9058   -552   -619    271       O  
ATOM   5584  N   ALA C  86     -42.325   3.940  16.585  1.00 47.87           N  
ANISOU 5584  N   ALA C  86     4195   5198   8792   -368   -742    212       N  
ATOM   5585  CA  ALA C  86     -42.836   3.495  17.898  1.00 46.89           C  
ANISOU 5585  CA  ALA C  86     4063   5046   8706   -330   -764    187       C  
ATOM   5586  C   ALA C  86     -42.567   1.994  18.046  1.00 46.15           C  
ANISOU 5586  C   ALA C  86     3964   4997   8574   -271   -790    151       C  
ATOM   5587  O   ALA C  86     -41.898   1.613  19.022  1.00 45.25           O  
ANISOU 5587  O   ALA C  86     3821   4918   8451   -245   -788    106       O  
ATOM   5588  CB  ALA C  86     -44.308   3.810  18.014  1.00 46.72           C  
ANISOU 5588  CB  ALA C  86     4074   4945   8732   -319   -786    231       C  
ATOM   5589  N   LEU C  87     -43.036   1.197  17.077  1.00 46.10           N  
ANISOU 5589  N   LEU C  87     3985   4988   8540   -248   -813    169       N  
ATOM   5590  CA  LEU C  87     -43.155  -0.284  17.179  1.00 46.18           C  
ANISOU 5590  CA  LEU C  87     4016   5004   8526   -192   -840    142       C  
ATOM   5591  C   LEU C  87     -41.771  -0.926  17.336  1.00 46.36           C  
ANISOU 5591  C   LEU C  87     4011   5101   8501   -152   -832     89       C  
ATOM   5592  O   LEU C  87     -41.651  -1.865  18.154  1.00 46.28           O  
ANISOU 5592  O   LEU C  87     4017   5083   8484    -96   -846     63       O  
ATOM   5593  CB  LEU C  87     -43.888  -0.831  15.947  1.00 46.22           C  
ANISOU 5593  CB  LEU C  87     4052   4999   8508   -191   -860    162       C  
ATOM   5594  CG  LEU C  87     -44.017  -2.356  15.875  1.00 45.95           C  
ANISOU 5594  CG  LEU C  87     4051   4957   8449   -145   -880    129       C  
ATOM   5595  CD1 LEU C  87     -44.571  -2.930  17.173  1.00 45.40           C  
ANISOU 5595  CD1 LEU C  87     4008   4830   8411   -123   -888    123       C  
ATOM   5596  CD2 LEU C  87     -44.881  -2.772  14.694  1.00 46.21           C  
ANISOU 5596  CD2 LEU C  87     4108   4984   8464   -158   -899    141       C  
ATOM   5597  N   ASN C  88     -40.767  -0.441  16.597  1.00 46.76           N  
ANISOU 5597  N   ASN C  88     4025   5223   8517   -178   -808     73       N  
ATOM   5598  CA  ASN C  88     -39.382  -0.992  16.612  1.00 47.15           C  
ANISOU 5598  CA  ASN C  88     4030   5369   8513   -138   -799     11       C  
ATOM   5599  C   ASN C  88     -38.866  -1.102  18.057  1.00 46.51           C  
ANISOU 5599  C   ASN C  88     3920   5310   8440    -98   -803    -24       C  
ATOM   5600  O   ASN C  88     -38.150  -2.081  18.351  1.00 46.37           O  
ANISOU 5600  O   ASN C  88     3892   5342   8382    -19   -818    -69       O  
ATOM   5601  CB  ASN C  88     -38.426  -0.167  15.748  1.00 47.87           C  
ANISOU 5601  CB  ASN C  88     4073   5543   8570   -197   -761     -2       C  
ATOM   5602  CG  ASN C  88     -37.202  -0.951  15.326  1.00 49.00           C  
ANISOU 5602  CG  ASN C  88     4171   5797   8647   -149   -758    -68       C  
ATOM   5603  OD1 ASN C  88     -37.030  -2.105  15.715  1.00 49.34           O  
ANISOU 5603  OD1 ASN C  88     4226   5848   8673    -58   -786   -102       O  
ATOM   5604  ND2 ASN C  88     -36.346  -0.336  14.528  1.00 49.88           N  
ANISOU 5604  ND2 ASN C  88     4236   5995   8720   -207   -720    -87       N  
ATOM   5605  N   HIS C  89     -39.236  -0.148  18.918  1.00 46.01           N  
ANISOU 5605  N   HIS C  89     3846   5210   8423   -144   -791     -8       N  
ATOM   5606  CA  HIS C  89     -38.856  -0.078  20.356  1.00 45.83           C  
ANISOU 5606  CA  HIS C  89     3792   5213   8407   -118   -793    -42       C  
ATOM   5607  C   HIS C  89     -39.734  -1.016  21.202  1.00 45.05           C  
ANISOU 5607  C   HIS C  89     3750   5044   8322    -56   -825    -20       C  
ATOM   5608  O   HIS C  89     -39.156  -1.802  21.980  1.00 44.72           O  
ANISOU 5608  O   HIS C  89     3704   5042   8244     18   -841    -50       O  
ATOM   5609  CB  HIS C  89     -38.907   1.380  20.847  1.00 45.81           C  
ANISOU 5609  CB  HIS C  89     3758   5199   8447   -201   -762    -41       C  
ATOM   5610  CG  HIS C  89     -37.821   2.242  20.290  1.00 46.58           C  
ANISOU 5610  CG  HIS C  89     3799   5376   8524   -268   -721    -76       C  
ATOM   5611  ND1 HIS C  89     -36.780   2.721  21.069  1.00 47.03           N  
ANISOU 5611  ND1 HIS C  89     3782   5523   8563   -291   -700   -143       N  
ATOM   5612  CD2 HIS C  89     -37.592   2.694  19.037  1.00 46.96           C  
ANISOU 5612  CD2 HIS C  89     3850   5433   8556   -325   -695    -57       C  
ATOM   5613  CE1 HIS C  89     -35.965   3.441  20.321  1.00 47.44           C  
ANISOU 5613  CE1 HIS C  89     3795   5634   8596   -367   -657   -167       C  
ATOM   5614  NE2 HIS C  89     -36.435   3.432  19.069  1.00 47.48           N  
ANISOU 5614  NE2 HIS C  89     3850   5589   8600   -388   -652   -111       N  
ATOM   5615  N   THR C  90     -41.066  -0.947  21.058  1.00 44.57           N  
ANISOU 5615  N   THR C  90     3741   4888   8305    -85   -832     29       N  
ATOM   5616  CA  THR C  90     -42.055  -1.561  21.995  1.00 43.98           C  
ANISOU 5616  CA  THR C  90     3715   4744   8251    -60   -849     50       C  
ATOM   5617  C   THR C  90     -42.140  -3.079  21.812  1.00 43.91           C  
ANISOU 5617  C   THR C  90     3767   4709   8207      5   -870     49       C  
ATOM   5618  O   THR C  90     -42.642  -3.736  22.732  1.00 44.10           O  
ANISOU 5618  O   THR C  90     3835   4687   8231     33   -877     60       O  
ATOM   5619  CB  THR C  90     -43.455  -0.959  21.850  1.00 43.74           C  
ANISOU 5619  CB  THR C  90     3705   4638   8276   -116   -847     91       C  
ATOM   5620  OG1 THR C  90     -43.958  -1.294  20.556  1.00 43.59           O  
ANISOU 5620  OG1 THR C  90     3713   4596   8251   -127   -857    113       O  
ATOM   5621  CG2 THR C  90     -43.463   0.538  22.063  1.00 44.04           C  
ANISOU 5621  CG2 THR C  90     3701   4677   8354   -172   -825     94       C  
ATOM   5622  N   LYS C  91     -41.673  -3.615  20.683  1.00 43.94           N  
ANISOU 5622  N   LYS C  91     3778   4737   8179     26   -874     35       N  
ATOM   5623  CA  LYS C  91     -41.505  -5.081  20.483  1.00 44.20           C  
ANISOU 5623  CA  LYS C  91     3871   4747   8174    100   -890     21       C  
ATOM   5624  C   LYS C  91     -40.282  -5.586  21.274  1.00 44.52           C  
ANISOU 5624  C   LYS C  91     3896   4850   8167    192   -898    -15       C  
ATOM   5625  O   LYS C  91     -40.053  -6.803  21.258  1.00 44.58           O  
ANISOU 5625  O   LYS C  91     3963   4832   8141    271   -912    -27       O  
ATOM   5626  CB  LYS C  91     -41.395  -5.404  18.988  1.00 44.35           C  
ANISOU 5626  CB  LYS C  91     3895   4781   8172     92   -891      8       C  
ATOM   5627  CG  LYS C  91     -40.084  -5.002  18.321  1.00 44.78           C  
ANISOU 5627  CG  LYS C  91     3882   4945   8188    105   -881    -30       C  
ATOM   5628  CD  LYS C  91     -39.930  -5.545  16.914  1.00 45.09           C  
ANISOU 5628  CD  LYS C  91     3933   5005   8194    111   -882    -49       C  
ATOM   5629  CE  LYS C  91     -38.493  -5.605  16.437  1.00 45.33           C  
ANISOU 5629  CE  LYS C  91     3903   5150   8169    154   -873   -104       C  
ATOM   5630  NZ  LYS C  91     -37.989  -4.262  16.075  1.00 45.16           N  
ANISOU 5630  NZ  LYS C  91     3805   5206   8146     75   -844   -101       N  
ATOM   5631  N   LYS C  92     -39.511  -4.692  21.911  1.00 44.98           N  
ANISOU 5631  N   LYS C  92     3878   4992   8219    185   -890    -38       N  
ATOM   5632  CA  LYS C  92     -38.323  -5.031  22.748  1.00 45.49           C  
ANISOU 5632  CA  LYS C  92     3907   5145   8232    274   -902    -81       C  
ATOM   5633  C   LYS C  92     -38.665  -4.891  24.236  1.00 44.59           C  
ANISOU 5633  C   LYS C  92     3804   5012   8124    286   -908    -63       C  
ATOM   5634  O   LYS C  92     -37.949  -5.498  25.056  1.00 44.66           O  
ANISOU 5634  O   LYS C  92     3815   5071   8081    383   -927    -83       O  
ATOM   5635  CB  LYS C  92     -37.124  -4.126  22.432  1.00 46.54           C  
ANISOU 5635  CB  LYS C  92     3929   5410   8341    249   -887   -135       C  
ATOM   5636  CG  LYS C  92     -36.779  -3.938  20.957  1.00 47.37           C  
ANISOU 5636  CG  LYS C  92     4008   5551   8439    209   -870   -151       C  
ATOM   5637  CD  LYS C  92     -35.573  -3.022  20.730  1.00 48.25           C  
ANISOU 5637  CD  LYS C  92     4010   5798   8522    167   -844   -208       C  
ATOM   5638  CE  LYS C  92     -35.223  -2.797  19.269  1.00 48.65           C  
ANISOU 5638  CE  LYS C  92     4037   5890   8556    118   -821   -220       C  
ATOM   5639  NZ  LYS C  92     -34.832  -1.388  19.003  1.00 48.93           N  
ANISOU 5639  NZ  LYS C  92     4005   5979   8604      0   -777   -230       N  
ATOM   5640  N   TRP C  93     -39.685  -4.094  24.574  1.00 43.47           N  
ANISOU 5640  N   TRP C  93     3666   4811   8037    199   -893    -30       N  
ATOM   5641  CA  TRP C  93     -40.198  -3.954  25.963  1.00 43.36           C  
ANISOU 5641  CA  TRP C  93     3667   4774   8031    199   -894    -13       C  
ATOM   5642  C   TRP C  93     -40.761  -5.300  26.420  1.00 43.64           C  
ANISOU 5642  C   TRP C  93     3808   4729   8043    262   -907     22       C  
ATOM   5643  O   TRP C  93     -41.076  -6.136  25.551  1.00 44.44           O  
ANISOU 5643  O   TRP C  93     3972   4766   8145    274   -910     37       O  
ATOM   5644  CB  TRP C  93     -41.284  -2.880  26.079  1.00 42.80           C  
ANISOU 5644  CB  TRP C  93     3583   4651   8029     96   -873      9       C  
ATOM   5645  CG  TRP C  93     -40.848  -1.466  25.861  1.00 42.84           C  
ANISOU 5645  CG  TRP C  93     3505   4709   8063     28   -853    -20       C  
ATOM   5646  CD1 TRP C  93     -39.576  -0.987  25.729  1.00 43.36           C  
ANISOU 5646  CD1 TRP C  93     3498   4878   8099     30   -845    -71       C  
ATOM   5647  CD2 TRP C  93     -41.718  -0.324  25.774  1.00 42.61           C  
ANISOU 5647  CD2 TRP C  93     3464   4628   8097    -56   -833     -2       C  
ATOM   5648  NE1 TRP C  93     -39.598   0.371  25.552  1.00 43.35           N  
ANISOU 5648  NE1 TRP C  93     3448   4880   8140    -59   -816    -84       N  
ATOM   5649  CE2 TRP C  93     -40.897   0.807  25.581  1.00 42.90           C  
ANISOU 5649  CE2 TRP C  93     3433   4724   8143   -106   -810    -39       C  
ATOM   5650  CE3 TRP C  93     -43.107  -0.149  25.837  1.00 42.23           C  
ANISOU 5650  CE3 TRP C  93     3454   4493   8098    -93   -831     36       C  
ATOM   5651  CZ2 TRP C  93     -41.428   2.089  25.449  1.00 42.73           C  
ANISOU 5651  CZ2 TRP C  93     3398   4656   8179   -184   -785    -31       C  
ATOM   5652  CZ3 TRP C  93     -43.630   1.119  25.716  1.00 41.80           C  
ANISOU 5652  CZ3 TRP C  93     3373   4409   8098   -158   -812     40       C  
ATOM   5653  CH2 TRP C  93     -42.799   2.222  25.524  1.00 42.30           C  
ANISOU 5653  CH2 TRP C  93     3386   4512   8172   -200   -789     11       C  
ATOM   5654  N   LYS C  94     -40.923  -5.475  27.733  1.00 43.61           N  
ANISOU 5654  N   LYS C  94     3827   4723   8017    291   -910     36       N  
ATOM   5655  CA  LYS C  94     -41.566  -6.664  28.351  1.00 43.71           C  
ANISOU 5655  CA  LYS C  94     3955   4647   8006    334   -913     81       C  
ATOM   5656  C   LYS C  94     -43.017  -6.308  28.722  1.00 42.92           C  
ANISOU 5656  C   LYS C  94     3879   4470   7956    235   -890    114       C  
ATOM   5657  O   LYS C  94     -43.265  -5.157  29.153  1.00 42.31           O  
ANISOU 5657  O   LYS C  94     3728   4433   7913    175   -879    100       O  
ATOM   5658  CB  LYS C  94     -40.740  -7.117  29.560  1.00 44.45           C  
ANISOU 5658  CB  LYS C  94     4060   4803   8026    439   -932     78       C  
ATOM   5659  CG  LYS C  94     -39.272  -7.407  29.276  1.00 45.18           C  
ANISOU 5659  CG  LYS C  94     4108   4997   8061    549   -959     33       C  
ATOM   5660  CD  LYS C  94     -38.998  -8.824  28.814  1.00 45.97           C  
ANISOU 5660  CD  LYS C  94     4311   5033   8122    654   -974     50       C  
ATOM   5661  CE  LYS C  94     -37.517  -9.138  28.752  1.00 46.94           C  
ANISOU 5661  CE  LYS C  94     4382   5275   8177    786  -1006      0       C  
ATOM   5662  NZ  LYS C  94     -37.264 -10.598  28.692  1.00 47.86           N  
ANISOU 5662  NZ  LYS C  94     4620   5319   8243    919  -1024     23       N  
ATOM   5663  N   TYR C  95     -43.946  -7.253  28.551  1.00 42.55           N  
ANISOU 5663  N   TYR C  95     3930   4320   7916    216   -879    150       N  
ATOM   5664  CA  TYR C  95     -45.378  -7.104  28.925  1.00 41.69           C  
ANISOU 5664  CA  TYR C  95     3846   4147   7847    123   -854    175       C  
ATOM   5665  C   TYR C  95     -45.786  -8.270  29.812  1.00 42.15           C  
ANISOU 5665  C   TYR C  95     4019   4134   7861    147   -840    213       C  
ATOM   5666  O   TYR C  95     -46.433  -9.200  29.339  1.00 42.75           O  
ANISOU 5666  O   TYR C  95     4182   4118   7941    120   -825    231       O  
ATOM   5667  CB  TYR C  95     -46.258  -7.033  27.679  1.00 40.93           C  
ANISOU 5667  CB  TYR C  95     3746   4002   7803     48   -847    172       C  
ATOM   5668  CG  TYR C  95     -45.881  -5.938  26.719  1.00 40.24           C  
ANISOU 5668  CG  TYR C  95     3565   3972   7750     26   -859    146       C  
ATOM   5669  CD1 TYR C  95     -46.407  -4.667  26.846  1.00 39.98           C  
ANISOU 5669  CD1 TYR C  95     3458   3966   7765    -34   -851    141       C  
ATOM   5670  CD2 TYR C  95     -44.989  -6.171  25.690  1.00 40.37           C  
ANISOU 5670  CD2 TYR C  95     3573   4014   7748     68   -873    128       C  
ATOM   5671  CE1 TYR C  95     -46.075  -3.655  25.959  1.00 39.65           C  
ANISOU 5671  CE1 TYR C  95     3350   3962   7752    -56   -856    127       C  
ATOM   5672  CE2 TYR C  95     -44.641  -5.171  24.798  1.00 40.14           C  
ANISOU 5672  CE2 TYR C  95     3468   4038   7745     39   -876    111       C  
ATOM   5673  CZ  TYR C  95     -45.185  -3.909  24.934  1.00 39.60           C  
ANISOU 5673  CZ  TYR C  95     3340   3983   7723    -24   -867    114       C  
ATOM   5674  OH  TYR C  95     -44.845  -2.916  24.069  1.00 39.57           O  
ANISOU 5674  OH  TYR C  95     3278   4015   7739    -54   -865    106       O  
ATOM   5675  N   PRO C  96     -45.418  -8.258  31.113  1.00 42.49           N  
ANISOU 5675  N   PRO C  96     4071   4217   7856    194   -840    227       N  
ATOM   5676  CA  PRO C  96     -45.786  -9.338  32.028  1.00 43.64           C  
ANISOU 5676  CA  PRO C  96     4338   4293   7948    218   -823    275       C  
ATOM   5677  C   PRO C  96     -47.223  -9.202  32.565  1.00 44.13           C  
ANISOU 5677  C   PRO C  96     4418   4310   8037    103   -783    293       C  
ATOM   5678  O   PRO C  96     -47.706  -8.095  32.706  1.00 44.15           O  
ANISOU 5678  O   PRO C  96     4321   4367   8084     37   -778    267       O  
ATOM   5679  CB  PRO C  96     -44.748  -9.180  33.146  1.00 43.77           C  
ANISOU 5679  CB  PRO C  96     4333   4401   7895    318   -845    276       C  
ATOM   5680  CG  PRO C  96     -44.524  -7.683  33.212  1.00 42.88           C  
ANISOU 5680  CG  PRO C  96     4070   4397   7822    274   -853    226       C  
ATOM   5681  CD  PRO C  96     -44.634  -7.205  31.778  1.00 42.16           C  
ANISOU 5681  CD  PRO C  96     3925   4291   7801    222   -856    196       C  
ATOM   5682  N   GLN C  97     -47.878 -10.330  32.845  1.00 45.25           N  
ANISOU 5682  N   GLN C  97     4687   4352   8153     78   -753    334       N  
ATOM   5683  CA  GLN C  97     -49.209 -10.358  33.507  1.00 45.87           C  
ANISOU 5683  CA  GLN C  97     4790   4397   8240    -32   -707    350       C  
ATOM   5684  C   GLN C  97     -48.985 -10.040  34.990  1.00 46.06           C  
ANISOU 5684  C   GLN C  97     4807   4486   8207     -1   -702    371       C  
ATOM   5685  O   GLN C  97     -48.039 -10.620  35.571  1.00 46.64           O  
ANISOU 5685  O   GLN C  97     4948   4564   8208    108   -720    404       O  
ATOM   5686  CB  GLN C  97     -49.894 -11.712  33.290  1.00 46.92           C  
ANISOU 5686  CB  GLN C  97     5069   4401   8357    -80   -669    382       C  
ATOM   5687  CG  GLN C  97     -50.092 -12.074  31.823  1.00 46.89           C  
ANISOU 5687  CG  GLN C  97     5072   4342   8403   -111   -676    351       C  
ATOM   5688  CD  GLN C  97     -51.285 -11.389  31.203  1.00 46.63           C  
ANISOU 5688  CD  GLN C  97     4944   4336   8437   -235   -662    310       C  
ATOM   5689  OE1 GLN C  97     -51.146 -10.540  30.322  1.00 45.75           O  
ANISOU 5689  OE1 GLN C  97     4726   4284   8373   -233   -693    274       O  
ATOM   5690  NE2 GLN C  97     -52.473 -11.762  31.661  1.00 47.56           N  
ANISOU 5690  NE2 GLN C  97     5100   4415   8553   -344   -614    315       N  
ATOM   5691  N   VAL C  98     -49.799  -9.139  35.557  1.00 45.49           N  
ANISOU 5691  N   VAL C  98     4651   4470   8163    -83   -682    349       N  
ATOM   5692  CA  VAL C  98     -49.697  -8.647  36.968  1.00 45.72           C  
ANISOU 5692  CA  VAL C  98     4650   4580   8142    -68   -674    354       C  
ATOM   5693  C   VAL C  98     -51.105  -8.575  37.580  1.00 45.91           C  
ANISOU 5693  C   VAL C  98     4676   4593   8174   -188   -621    355       C  
ATOM   5694  O   VAL C  98     -51.906  -7.725  37.137  1.00 45.29           O  
ANISOU 5694  O   VAL C  98     4498   4541   8168   -265   -615    308       O  
ATOM   5695  CB  VAL C  98     -48.991  -7.279  37.026  1.00 45.00           C  
ANISOU 5695  CB  VAL C  98     4415   4601   8079    -33   -708    299       C  
ATOM   5696  CG1 VAL C  98     -48.613  -6.905  38.452  1.00 45.45           C  
ANISOU 5696  CG1 VAL C  98     4448   4751   8070      2   -707    297       C  
ATOM   5697  CG2 VAL C  98     -47.775  -7.233  36.111  1.00 44.58           C  
ANISOU 5697  CG2 VAL C  98     4337   4566   8036     51   -752    282       C  
ATOM   5698  N   ASN C  99     -51.391  -9.434  38.562  1.00 46.78           N  
ANISOU 5698  N   ASN C  99     4897   4669   8209   -199   -585    407       N  
ATOM   5699  CA  ASN C  99     -52.747  -9.656  39.135  1.00 47.33           C  
ANISOU 5699  CA  ASN C  99     4993   4719   8272   -324   -523    414       C  
ATOM   5700  C   ASN C  99     -53.805  -9.597  38.020  1.00 47.15           C  
ANISOU 5700  C   ASN C  99     4928   4653   8333   -431   -506    373       C  
ATOM   5701  O   ASN C  99     -54.780  -8.825  38.169  1.00 47.11           O  
ANISOU 5701  O   ASN C  99     4821   4708   8368   -515   -485    327       O  
ATOM   5702  CB  ASN C  99     -53.039  -8.667  40.263  1.00 47.38           C  
ANISOU 5702  CB  ASN C  99     4902   4839   8261   -348   -511    384       C  
ATOM   5703  CG  ASN C  99     -54.301  -9.005  41.023  1.00 48.37           C  
ANISOU 5703  CG  ASN C  99     5062   4959   8356   -466   -443    394       C  
ATOM   5704  OD1 ASN C  99     -55.198  -8.173  41.132  1.00 48.82           O  
ANISOU 5704  OD1 ASN C  99     5008   5080   8459   -544   -424    337       O  
ATOM   5705  ND2 ASN C  99     -54.386 -10.220  41.540  1.00 49.67           N  
ANISOU 5705  ND2 ASN C  99     5382   5046   8440   -480   -404    464       N  
ATOM   5706  N   GLY C 100     -53.601 -10.371  36.941  1.00 47.25           N  
ANISOU 5706  N   GLY C 100     5010   4575   8366   -419   -516    385       N  
ATOM   5707  CA  GLY C 100     -54.571 -10.607  35.849  1.00 47.15           C  
ANISOU 5707  CA  GLY C 100     4982   4515   8414   -519   -499    350       C  
ATOM   5708  C   GLY C 100     -54.488  -9.588  34.716  1.00 46.34           C  
ANISOU 5708  C   GLY C 100     4746   4467   8393   -502   -546    296       C  
ATOM   5709  O   GLY C 100     -55.292  -9.717  33.759  1.00 46.40           O  
ANISOU 5709  O   GLY C 100     4729   4454   8446   -575   -539    264       O  
ATOM   5710  N   LEU C 101     -53.557  -8.624  34.788  1.00 45.24           N  
ANISOU 5710  N   LEU C 101     4526   4396   8265   -412   -591    285       N  
ATOM   5711  CA  LEU C 101     -53.523  -7.425  33.904  1.00 44.18           C  
ANISOU 5711  CA  LEU C 101     4262   4318   8203   -403   -627    238       C  
ATOM   5712  C   LEU C 101     -52.176  -7.328  33.188  1.00 43.84           C  
ANISOU 5712  C   LEU C 101     4218   4276   8162   -304   -673    243       C  
ATOM   5713  O   LEU C 101     -51.132  -7.432  33.863  1.00 44.33           O  
ANISOU 5713  O   LEU C 101     4308   4361   8175   -223   -687    262       O  
ATOM   5714  CB  LEU C 101     -53.778  -6.173  34.750  1.00 43.91           C  
ANISOU 5714  CB  LEU C 101     4123   4373   8188   -412   -625    207       C  
ATOM   5715  CG  LEU C 101     -55.177  -6.058  35.358  1.00 44.04           C  
ANISOU 5715  CG  LEU C 101     4107   4414   8211   -509   -582    185       C  
ATOM   5716  CD1 LEU C 101     -55.242  -4.927  36.368  1.00 43.75           C  
ANISOU 5716  CD1 LEU C 101     3981   4460   8179   -500   -578    153       C  
ATOM   5717  CD2 LEU C 101     -56.228  -5.865  34.277  1.00 43.70           C  
ANISOU 5717  CD2 LEU C 101     4006   4366   8228   -574   -583    149       C  
ATOM   5718  N   THR C 102     -52.200  -7.119  31.870  1.00 43.52           N  
ANISOU 5718  N   THR C 102     4141   4223   8169   -310   -696    222       N  
ATOM   5719  CA  THR C 102     -50.974  -6.944  31.054  1.00 43.34           C  
ANISOU 5719  CA  THR C 102     4103   4213   8149   -229   -735    219       C  
ATOM   5720  C   THR C 102     -50.398  -5.570  31.383  1.00 42.83           C  
ANISOU 5720  C   THR C 102     3935   4230   8107   -199   -753    195       C  
ATOM   5721  O   THR C 102     -51.082  -4.570  31.105  1.00 42.80           O  
ANISOU 5721  O   THR C 102     3852   4251   8158   -246   -753    171       O  
ATOM   5722  CB  THR C 102     -51.220  -7.084  29.547  1.00 43.43           C  
ANISOU 5722  CB  THR C 102     4105   4196   8197   -252   -750    204       C  
ATOM   5723  OG1 THR C 102     -52.054  -8.214  29.281  1.00 44.35           O  
ANISOU 5723  OG1 THR C 102     4304   4242   8305   -311   -724    209       O  
ATOM   5724  CG2 THR C 102     -49.924  -7.231  28.782  1.00 43.45           C  
ANISOU 5724  CG2 THR C 102     4116   4206   8185   -171   -780    203       C  
ATOM   5725  N   SER C 103     -49.215  -5.546  31.996  1.00 42.77           N  
ANISOU 5725  N   SER C 103     3930   4263   8056   -123   -767    198       N  
ATOM   5726  CA  SER C 103     -48.471  -4.314  32.356  1.00 42.31           C  
ANISOU 5726  CA  SER C 103     3778   4286   8010    -99   -781    165       C  
ATOM   5727  C   SER C 103     -47.275  -4.143  31.414  1.00 42.03           C  
ANISOU 5727  C   SER C 103     3715   4278   7975    -46   -809    150       C  
ATOM   5728  O   SER C 103     -47.209  -4.854  30.393  1.00 42.43           O  
ANISOU 5728  O   SER C 103     3810   4284   8026    -34   -817    163       O  
ATOM   5729  CB  SER C 103     -48.041  -4.351  33.790  1.00 42.62           C  
ANISOU 5729  CB  SER C 103     3823   4377   7992    -62   -776    166       C  
ATOM   5730  OG  SER C 103     -47.776  -3.035  34.248  1.00 42.66           O  
ANISOU 5730  OG  SER C 103     3730   4455   8023    -75   -777    121       O  
ATOM   5731  N   ILE C 104     -46.384  -3.206  31.730  1.00 41.60           N  
ANISOU 5731  N   ILE C 104     3585   4300   7919    -24   -817    116       N  
ATOM   5732  CA  ILE C 104     -45.093  -2.996  31.015  1.00 41.51           C  
ANISOU 5732  CA  ILE C 104     3535   4340   7896     20   -837     91       C  
ATOM   5733  C   ILE C 104     -44.026  -2.735  32.073  1.00 42.05           C  
ANISOU 5733  C   ILE C 104     3559   4505   7911     73   -845     58       C  
ATOM   5734  O   ILE C 104     -44.240  -1.801  32.871  1.00 42.25           O  
ANISOU 5734  O   ILE C 104     3530   4567   7955     33   -832     30       O  
ATOM   5735  CB  ILE C 104     -45.179  -1.816  30.028  1.00 40.87           C  
ANISOU 5735  CB  ILE C 104     3387   4259   7879    -37   -831     70       C  
ATOM   5736  CG1 ILE C 104     -46.534  -1.750  29.314  1.00 40.48           C  
ANISOU 5736  CG1 ILE C 104     3360   4134   7884    -96   -824     96       C  
ATOM   5737  CG2 ILE C 104     -44.014  -1.864  29.051  1.00 40.73           C  
ANISOU 5737  CG2 ILE C 104     3348   4283   7844     -4   -844     53       C  
ATOM   5738  CD1 ILE C 104     -46.711  -0.544  28.419  1.00 40.07           C  
ANISOU 5738  CD1 ILE C 104     3256   4077   7889   -141   -820     87       C  
ATOM   5739  N   LYS C 105     -42.945  -3.525  32.086  1.00 42.72           N  
ANISOU 5739  N   LYS C 105     3664   4636   7932    163   -868     55       N  
ATOM   5740  CA  LYS C 105     -41.729  -3.241  32.899  1.00 43.37           C  
ANISOU 5740  CA  LYS C 105     3682   4840   7955    223   -884     10       C  
ATOM   5741  C   LYS C 105     -41.229  -1.846  32.500  1.00 42.90           C  
ANISOU 5741  C   LYS C 105     3513   4843   7941    157   -872    -49       C  
ATOM   5742  O   LYS C 105     -41.320  -1.505  31.303  1.00 41.94           O  
ANISOU 5742  O   LYS C 105     3382   4683   7870    111   -863    -48       O  
ATOM   5743  CB  LYS C 105     -40.661  -4.325  32.700  1.00 44.19           C  
ANISOU 5743  CB  LYS C 105     3819   4983   7985    342   -914     13       C  
ATOM   5744  CG  LYS C 105     -39.411  -4.170  33.563  1.00 45.04           C  
ANISOU 5744  CG  LYS C 105     3856   5237   8019    421   -937    -36       C  
ATOM   5745  CD  LYS C 105     -38.449  -5.339  33.459  1.00 45.97           C  
ANISOU 5745  CD  LYS C 105     4015   5393   8057    562   -972    -29       C  
ATOM   5746  CE  LYS C 105     -37.019  -4.972  33.791  1.00 46.76           C  
ANISOU 5746  CE  LYS C 105     4001   5668   8094    631   -998   -104       C  
ATOM   5747  NZ  LYS C 105     -36.369  -4.234  32.679  1.00 46.66           N  
ANISOU 5747  NZ  LYS C 105     3893   5713   8123    574   -986   -166       N  
ATOM   5748  N   TRP C 106     -40.772  -1.043  33.460  1.00 43.42           N  
ANISOU 5748  N   TRP C 106     3506   5000   7991    144   -867   -101       N  
ATOM   5749  CA  TRP C 106     -40.454   0.385  33.198  1.00 44.08           C  
ANISOU 5749  CA  TRP C 106     3499   5121   8126     59   -844   -161       C  
ATOM   5750  C   TRP C 106     -39.256   0.507  32.239  1.00 44.62           C  
ANISOU 5750  C   TRP C 106     3515   5257   8180     67   -847   -199       C  
ATOM   5751  O   TRP C 106     -38.225  -0.170  32.460  1.00 44.41           O  
ANISOU 5751  O   TRP C 106     3464   5329   8078    154   -873   -224       O  
ATOM   5752  CB  TRP C 106     -40.229   1.179  34.487  1.00 44.85           C  
ANISOU 5752  CB  TRP C 106     3531   5302   8206     36   -834   -220       C  
ATOM   5753  CG  TRP C 106     -40.071   2.631  34.165  1.00 45.23           C  
ANISOU 5753  CG  TRP C 106     3510   5354   8319    -63   -801   -277       C  
ATOM   5754  CD1 TRP C 106     -41.048   3.581  34.146  1.00 45.16           C  
ANISOU 5754  CD1 TRP C 106     3510   5258   8389   -142   -772   -275       C  
ATOM   5755  CD2 TRP C 106     -38.878   3.275  33.691  1.00 46.03           C  
ANISOU 5755  CD2 TRP C 106     3534   5539   8414    -95   -790   -344       C  
ATOM   5756  NE1 TRP C 106     -40.538   4.783  33.736  1.00 45.52           N  
ANISOU 5756  NE1 TRP C 106     3501   5313   8479   -219   -743   -330       N  
ATOM   5757  CE2 TRP C 106     -39.210   4.625  33.448  1.00 46.04           C  
ANISOU 5757  CE2 TRP C 106     3513   5485   8494   -202   -750   -373       C  
ATOM   5758  CE3 TRP C 106     -37.566   2.844  33.462  1.00 46.21           C  
ANISOU 5758  CE3 TRP C 106     3503   5682   8370    -45   -808   -385       C  
ATOM   5759  CZ2 TRP C 106     -38.272   5.547  32.994  1.00 46.32           C  
ANISOU 5759  CZ2 TRP C 106     3484   5572   8543   -274   -720   -439       C  
ATOM   5760  CZ3 TRP C 106     -36.644   3.755  33.005  1.00 46.72           C  
ANISOU 5760  CZ3 TRP C 106     3487   5816   8446   -117   -781   -457       C  
ATOM   5761  CH2 TRP C 106     -36.994   5.086  32.776  1.00 46.87           C  
ANISOU 5761  CH2 TRP C 106     3495   5770   8544   -238   -734   -481       C  
ATOM   5762  N   ALA C 107     -39.393   1.375  31.229  1.00 44.68           N  
ANISOU 5762  N   ALA C 107     3503   5219   8252    -15   -821   -204       N  
ATOM   5763  CA  ALA C 107     -38.434   1.578  30.116  1.00 45.08           C  
ANISOU 5763  CA  ALA C 107     3512   5318   8297    -32   -814   -232       C  
ATOM   5764  C   ALA C 107     -38.948   2.706  29.210  1.00 45.50           C  
ANISOU 5764  C   ALA C 107     3568   5290   8428   -138   -778   -219       C  
ATOM   5765  O   ALA C 107     -40.133   2.657  28.831  1.00 45.07           O  
ANISOU 5765  O   ALA C 107     3578   5123   8422   -154   -778   -159       O  
ATOM   5766  CB  ALA C 107     -38.257   0.287  29.349  1.00 44.61           C  
ANISOU 5766  CB  ALA C 107     3504   5246   8199     50   -841   -194       C  
ATOM   5767  N   ASP C 108     -38.097   3.693  28.896  1.00 46.41           N  
ANISOU 5767  N   ASP C 108     3619   5463   8551   -209   -747   -275       N  
ATOM   5768  CA  ASP C 108     -38.407   4.829  27.981  1.00 46.68           C  
ANISOU 5768  CA  ASP C 108     3666   5419   8650   -309   -707   -260       C  
ATOM   5769  C   ASP C 108     -39.580   5.650  28.539  1.00 46.30           C  
ANISOU 5769  C   ASP C 108     3653   5266   8672   -351   -693   -239       C  
ATOM   5770  O   ASP C 108     -40.589   5.835  27.801  1.00 46.19           O  
ANISOU 5770  O   ASP C 108     3699   5143   8707   -365   -692   -175       O  
ATOM   5771  CB  ASP C 108     -38.720   4.334  26.566  1.00 46.63           C  
ANISOU 5771  CB  ASP C 108     3713   5355   8648   -298   -715   -196       C  
ATOM   5772  CG  ASP C 108     -37.639   3.458  25.966  1.00 47.04           C  
ANISOU 5772  CG  ASP C 108     3734   5506   8632   -246   -729   -219       C  
ATOM   5773  OD1 ASP C 108     -36.667   3.155  26.682  1.00 48.33           O  
ANISOU 5773  OD1 ASP C 108     3833   5787   8741   -206   -738   -282       O  
ATOM   5774  OD2 ASP C 108     -37.775   3.090  24.788  1.00 46.99           O  
ANISOU 5774  OD2 ASP C 108     3763   5468   8623   -242   -731   -180       O  
ATOM   5775  N   ASN C 109     -39.450   6.115  29.788  1.00 45.89           N  
ANISOU 5775  N   ASN C 109     3559   5257   8619   -365   -685   -296       N  
ATOM   5776  CA  ASN C 109     -40.481   6.899  30.523  1.00 45.39           C  
ANISOU 5776  CA  ASN C 109     3516   5113   8615   -397   -670   -296       C  
ATOM   5777  C   ASN C 109     -41.878   6.416  30.121  1.00 44.41           C  
ANISOU 5777  C   ASN C 109     3464   4882   8526   -361   -691   -214       C  
ATOM   5778  O   ASN C 109     -42.749   7.276  29.917  1.00 44.61           O  
ANISOU 5778  O   ASN C 109     3518   4814   8618   -398   -673   -195       O  
ATOM   5779  CB  ASN C 109     -40.352   8.407  30.268  1.00 45.55           C  
ANISOU 5779  CB  ASN C 109     3529   5081   8697   -497   -620   -332       C  
ATOM   5780  CG  ASN C 109     -38.953   8.940  30.487  1.00 45.77           C  
ANISOU 5780  CG  ASN C 109     3481   5216   8692   -558   -590   -422       C  
ATOM   5781  OD1 ASN C 109     -38.200   8.396  31.288  1.00 45.69           O  
ANISOU 5781  OD1 ASN C 109     3407   5334   8618   -521   -609   -478       O  
ATOM   5782  ND2 ASN C 109     -38.598  10.001  29.780  1.00 45.74           N  
ANISOU 5782  ND2 ASN C 109     3486   5165   8727   -652   -541   -437       N  
ATOM   5783  N   ASN C 110     -42.079   5.095  30.024  1.00 43.70           N  
ANISOU 5783  N   ASN C 110     3404   4806   8392   -290   -726   -171       N  
ATOM   5784  CA  ASN C 110     -43.334   4.464  29.528  1.00 42.42           C  
ANISOU 5784  CA  ASN C 110     3306   4557   8254   -264   -745   -101       C  
ATOM   5785  C   ASN C 110     -44.287   4.192  30.697  1.00 41.77           C  
ANISOU 5785  C   ASN C 110     3236   4460   8174   -245   -750    -99       C  
ATOM   5786  O   ASN C 110     -45.265   3.456  30.481  1.00 42.10           O  
ANISOU 5786  O   ASN C 110     3323   4450   8219   -225   -765    -51       O  
ATOM   5787  CB  ASN C 110     -43.059   3.157  28.783  1.00 42.25           C  
ANISOU 5787  CB  ASN C 110     3319   4549   8184   -209   -771    -64       C  
ATOM   5788  CG  ASN C 110     -42.461   2.097  29.684  1.00 42.77           C  
ANISOU 5788  CG  ASN C 110     3384   4686   8179   -140   -792    -80       C  
ATOM   5789  OD1 ASN C 110     -42.203   2.348  30.860  1.00 43.25           O  
ANISOU 5789  OD1 ASN C 110     3411   4801   8220   -134   -788   -119       O  
ATOM   5790  ND2 ASN C 110     -42.199   0.921  29.139  1.00 42.84           N  
ANISOU 5790  ND2 ASN C 110     3433   4699   8146    -82   -814    -53       N  
ATOM   5791  N   CYS C 111     -44.023   4.750  31.884  1.00 41.33           N  
ANISOU 5791  N   CYS C 111     3137   4453   8111   -258   -737   -154       N  
ATOM   5792  CA  CYS C 111     -44.832   4.523  33.114  1.00 40.83           C  
ANISOU 5792  CA  CYS C 111     3079   4395   8039   -244   -737   -159       C  
ATOM   5793  C   CYS C 111     -46.289   4.957  32.876  1.00 40.18           C  
ANISOU 5793  C   CYS C 111     3021   4222   8023   -270   -728   -132       C  
ATOM   5794  O   CYS C 111     -47.197   4.259  33.360  1.00 39.80           O  
ANISOU 5794  O   CYS C 111     2998   4162   7960   -254   -734   -107       O  
ATOM   5795  CB  CYS C 111     -44.220   5.221  34.326  1.00 41.13           C  
ANISOU 5795  CB  CYS C 111     3058   4512   8058   -261   -722   -235       C  
ATOM   5796  SG  CYS C 111     -44.434   7.020  34.343  1.00 41.44           S  
ANISOU 5796  SG  CYS C 111     3060   4500   8183   -340   -682   -294       S  
ATOM   5797  N   TYR C 112     -46.507   6.050  32.138  1.00 39.92           N  
ANISOU 5797  N   TYR C 112     2982   4129   8056   -308   -713   -136       N  
ATOM   5798  CA  TYR C 112     -47.853   6.570  31.780  1.00 39.43           C  
ANISOU 5798  CA  TYR C 112     2936   3987   8056   -316   -710   -112       C  
ATOM   5799  C   TYR C 112     -48.529   5.587  30.822  1.00 39.03           C  
ANISOU 5799  C   TYR C 112     2926   3907   7996   -293   -735    -48       C  
ATOM   5800  O   TYR C 112     -49.705   5.276  31.064  1.00 39.45           O  
ANISOU 5800  O   TYR C 112     2984   3942   8059   -287   -740    -36       O  
ATOM   5801  CB  TYR C 112     -47.780   7.989  31.208  1.00 39.62           C  
ANISOU 5801  CB  TYR C 112     2958   3949   8145   -349   -688   -127       C  
ATOM   5802  CG  TYR C 112     -47.397   8.099  29.753  1.00 39.53           C  
ANISOU 5802  CG  TYR C 112     2978   3898   8141   -356   -693    -80       C  
ATOM   5803  CD1 TYR C 112     -48.344   8.374  28.781  1.00 39.51           C  
ANISOU 5803  CD1 TYR C 112     3008   3826   8176   -341   -705    -30       C  
ATOM   5804  CD2 TYR C 112     -46.079   7.963  29.348  1.00 39.64           C  
ANISOU 5804  CD2 TYR C 112     2984   3959   8119   -376   -686    -90       C  
ATOM   5805  CE1 TYR C 112     -47.997   8.488  27.445  1.00 39.61           C  
ANISOU 5805  CE1 TYR C 112     3052   3810   8186   -347   -709     16       C  
ATOM   5806  CE2 TYR C 112     -45.714   8.070  28.017  1.00 39.77           C  
ANISOU 5806  CE2 TYR C 112     3028   3948   8134   -389   -685    -49       C  
ATOM   5807  CZ  TYR C 112     -46.677   8.334  27.061  1.00 39.81           C  
ANISOU 5807  CZ  TYR C 112     3074   3878   8174   -375   -697      7       C  
ATOM   5808  OH  TYR C 112     -46.313   8.434  25.750  1.00 40.18           O  
ANISOU 5808  OH  TYR C 112     3149   3906   8209   -387   -696     51       O  
ATOM   5809  N   LEU C 113     -47.803   5.088  29.813  1.00 38.53           N  
ANISOU 5809  N   LEU C 113     2884   3848   7906   -284   -748    -19       N  
ATOM   5810  CA  LEU C 113     -48.319   4.106  28.816  1.00 38.10           C  
ANISOU 5810  CA  LEU C 113     2868   3770   7836   -266   -771     32       C  
ATOM   5811  C   LEU C 113     -48.781   2.833  29.530  1.00 37.88           C  
ANISOU 5811  C   LEU C 113     2865   3759   7766   -247   -779     40       C  
ATOM   5812  O   LEU C 113     -49.884   2.347  29.220  1.00 37.34           O  
ANISOU 5812  O   LEU C 113     2817   3662   7709   -254   -786     63       O  
ATOM   5813  CB  LEU C 113     -47.241   3.768  27.782  1.00 37.95           C  
ANISOU 5813  CB  LEU C 113     2863   3769   7786   -258   -779     47       C  
ATOM   5814  CG  LEU C 113     -47.581   4.194  26.359  1.00 38.11           C  
ANISOU 5814  CG  LEU C 113     2899   3745   7832   -270   -785     85       C  
ATOM   5815  CD1 LEU C 113     -46.429   3.912  25.413  1.00 38.10           C  
ANISOU 5815  CD1 LEU C 113     2904   3776   7794   -269   -786     91       C  
ATOM   5816  CD2 LEU C 113     -48.852   3.503  25.885  1.00 38.10           C  
ANISOU 5816  CD2 LEU C 113     2923   3716   7837   -258   -807    117       C  
ATOM   5817  N   ALA C 114     -47.948   2.309  30.432  1.00 37.96           N  
ANISOU 5817  N   ALA C 114     2876   3820   7726   -225   -777     22       N  
ATOM   5818  CA  ALA C 114     -48.275   1.158  31.305  1.00 37.97           C  
ANISOU 5818  CA  ALA C 114     2915   3833   7677   -205   -778     35       C  
ATOM   5819  C   ALA C 114     -49.613   1.410  32.009  1.00 37.92           C  
ANISOU 5819  C   ALA C 114     2899   3810   7699   -239   -762     29       C  
ATOM   5820  O   ALA C 114     -50.414   0.470  32.095  1.00 38.04           O  
ANISOU 5820  O   ALA C 114     2954   3802   7694   -249   -759     54       O  
ATOM   5821  CB  ALA C 114     -47.172   0.934  32.305  1.00 38.24           C  
ANISOU 5821  CB  ALA C 114     2940   3936   7653   -168   -779     11       C  
ATOM   5822  N   THR C 115     -49.838   2.636  32.490  1.00 38.02           N  
ANISOU 5822  N   THR C 115     2858   3831   7754   -259   -748     -9       N  
ATOM   5823  CA  THR C 115     -50.982   3.001  33.369  1.00 38.17           C  
ANISOU 5823  CA  THR C 115     2853   3855   7795   -283   -730    -32       C  
ATOM   5824  C   THR C 115     -52.268   3.042  32.533  1.00 37.69           C  
ANISOU 5824  C   THR C 115     2789   3751   7778   -300   -735    -14       C  
ATOM   5825  O   THR C 115     -53.287   2.491  32.988  1.00 37.45           O  
ANISOU 5825  O   THR C 115     2762   3730   7736   -322   -724    -14       O  
ATOM   5826  CB  THR C 115     -50.681   4.300  34.127  1.00 38.53           C  
ANISOU 5826  CB  THR C 115     2845   3924   7870   -291   -713    -90       C  
ATOM   5827  OG1 THR C 115     -49.365   4.176  34.668  1.00 38.55           O  
ANISOU 5827  OG1 THR C 115     2842   3981   7823   -275   -715   -109       O  
ATOM   5828  CG2 THR C 115     -51.663   4.583  35.245  1.00 39.01           C  
ANISOU 5828  CG2 THR C 115     2875   4008   7936   -307   -692   -125       C  
ATOM   5829  N   ALA C 116     -52.211   3.655  31.349  1.00 37.34           N  
ANISOU 5829  N   ALA C 116     2740   3670   7776   -292   -750      0       N  
ATOM   5830  CA  ALA C 116     -53.302   3.672  30.348  1.00 37.23           C  
ANISOU 5830  CA  ALA C 116     2722   3628   7793   -295   -765     19       C  
ATOM   5831  C   ALA C 116     -53.712   2.232  30.008  1.00 37.24           C  
ANISOU 5831  C   ALA C 116     2762   3633   7752   -311   -772     46       C  
ATOM   5832  O   ALA C 116     -54.937   1.965  29.917  1.00 37.12           O  
ANISOU 5832  O   ALA C 116     2729   3626   7746   -333   -771     39       O  
ATOM   5833  CB  ALA C 116     -52.858   4.426  29.120  1.00 37.00           C  
ANISOU 5833  CB  ALA C 116     2698   3563   7795   -277   -781     41       C  
ATOM   5834  N   LEU C 117     -52.723   1.344  29.844  1.00 36.97           N  
ANISOU 5834  N   LEU C 117     2776   3597   7673   -301   -777     68       N  
ATOM   5835  CA  LEU C 117     -52.910  -0.056  29.380  1.00 37.00           C  
ANISOU 5835  CA  LEU C 117     2835   3584   7637   -312   -781     93       C  
ATOM   5836  C   LEU C 117     -53.599  -0.873  30.480  1.00 37.29           C  
ANISOU 5836  C   LEU C 117     2897   3628   7642   -345   -756     88       C  
ATOM   5837  O   LEU C 117     -54.519  -1.653  30.149  1.00 37.41           O  
ANISOU 5837  O   LEU C 117     2933   3629   7651   -385   -749     91       O  
ATOM   5838  CB  LEU C 117     -51.548  -0.643  29.003  1.00 36.91           C  
ANISOU 5838  CB  LEU C 117     2868   3567   7587   -275   -793    111       C  
ATOM   5839  CG  LEU C 117     -51.582  -1.979  28.262  1.00 37.11           C  
ANISOU 5839  CG  LEU C 117     2958   3562   7579   -276   -800    133       C  
ATOM   5840  CD1 LEU C 117     -52.346  -1.859  26.956  1.00 36.96           C  
ANISOU 5840  CD1 LEU C 117     2921   3531   7588   -300   -816    135       C  
ATOM   5841  CD2 LEU C 117     -50.169  -2.474  27.998  1.00 37.27           C  
ANISOU 5841  CD2 LEU C 117     3012   3587   7560   -224   -811    142       C  
ATOM   5842  N   LEU C 118     -53.172  -0.701  31.734  1.00 37.37           N  
ANISOU 5842  N   LEU C 118     2905   3665   7629   -334   -739     77       N  
ATOM   5843  CA  LEU C 118     -53.808  -1.325  32.926  1.00 37.83           C  
ANISOU 5843  CA  LEU C 118     2986   3737   7649   -367   -708     74       C  
ATOM   5844  C   LEU C 118     -55.255  -0.821  33.041  1.00 38.28           C  
ANISOU 5844  C   LEU C 118     2984   3815   7745   -417   -692     42       C  
ATOM   5845  O   LEU C 118     -56.170  -1.663  33.207  1.00 38.55           O  
ANISOU 5845  O   LEU C 118     3042   3846   7756   -472   -669     45       O  
ATOM   5846  CB  LEU C 118     -52.994  -0.988  34.181  1.00 37.81           C  
ANISOU 5846  CB  LEU C 118     2976   3777   7611   -337   -700     63       C  
ATOM   5847  CG  LEU C 118     -51.658  -1.715  34.320  1.00 37.81           C  
ANISOU 5847  CG  LEU C 118     3035   3777   7552   -281   -714     90       C  
ATOM   5848  CD1 LEU C 118     -50.711  -0.942  35.222  1.00 37.98           C  
ANISOU 5848  CD1 LEU C 118     3011   3863   7554   -244   -718     59       C  
ATOM   5849  CD2 LEU C 118     -51.853  -3.125  34.847  1.00 38.23           C  
ANISOU 5849  CD2 LEU C 118     3183   3802   7538   -285   -696    131       C  
ATOM   5850  N   THR C 119     -55.450   0.499  32.939  1.00 38.37           N  
ANISOU 5850  N   THR C 119     2921   3845   7810   -399   -702     10       N  
ATOM   5851  CA  THR C 119     -56.778   1.175  32.982  1.00 38.73           C  
ANISOU 5851  CA  THR C 119     2896   3919   7898   -422   -695    -27       C  
ATOM   5852  C   THR C 119     -57.694   0.601  31.889  1.00 38.73           C  
ANISOU 5852  C   THR C 119     2894   3913   7907   -449   -707    -20       C  
ATOM   5853  O   THR C 119     -58.732   0.018  32.239  1.00 38.79           O  
ANISOU 5853  O   THR C 119     2888   3951   7897   -505   -684    -40       O  
ATOM   5854  CB  THR C 119     -56.635   2.694  32.824  1.00 38.66           C  
ANISOU 5854  CB  THR C 119     2831   3908   7950   -378   -709    -55       C  
ATOM   5855  OG1 THR C 119     -55.786   3.190  33.860  1.00 38.83           O  
ANISOU 5855  OG1 THR C 119     2850   3943   7960   -364   -694    -75       O  
ATOM   5856  CG2 THR C 119     -57.968   3.409  32.879  1.00 39.20           C  
ANISOU 5856  CG2 THR C 119     2828   4006   8060   -378   -706    -97       C  
ATOM   5857  N   LEU C 120     -57.308   0.766  30.620  1.00 38.50           N  
ANISOU 5857  N   LEU C 120     2875   3854   7899   -418   -741      3       N  
ATOM   5858  CA  LEU C 120     -58.122   0.418  29.426  1.00 38.95           C  
ANISOU 5858  CA  LEU C 120     2917   3917   7964   -434   -762      4       C  
ATOM   5859  C   LEU C 120     -58.692  -1.001  29.563  1.00 39.88           C  
ANISOU 5859  C   LEU C 120     3074   4039   8038   -505   -737      1       C  
ATOM   5860  O   LEU C 120     -59.908  -1.184  29.299  1.00 40.53           O  
ANISOU 5860  O   LEU C 120     3109   4165   8125   -549   -733    -32       O  
ATOM   5861  CB  LEU C 120     -57.253   0.564  28.176  1.00 38.58           C  
ANISOU 5861  CB  LEU C 120     2900   3835   7923   -393   -795     40       C  
ATOM   5862  CG  LEU C 120     -57.207   1.981  27.607  1.00 38.61           C  
ANISOU 5862  CG  LEU C 120     2860   3834   7973   -339   -819     43       C  
ATOM   5863  CD1 LEU C 120     -55.918   2.241  26.847  1.00 38.27           C  
ANISOU 5863  CD1 LEU C 120     2859   3754   7928   -307   -834     80       C  
ATOM   5864  CD2 LEU C 120     -58.413   2.239  26.719  1.00 38.94           C  
ANISOU 5864  CD2 LEU C 120     2851   3910   8031   -329   -845     32       C  
ATOM   5865  N   GLN C 121     -57.863  -1.955  29.991  1.00 39.97           N  
ANISOU 5865  N   GLN C 121     3170   4008   8006   -517   -719     30       N  
ATOM   5866  CA  GLN C 121     -58.261  -3.365  30.248  1.00 40.54           C  
ANISOU 5866  CA  GLN C 121     3311   4059   8034   -586   -686     35       C  
ATOM   5867  C   GLN C 121     -59.516  -3.413  31.135  1.00 41.09           C  
ANISOU 5867  C   GLN C 121     3336   4178   8096   -658   -647     -3       C  
ATOM   5868  O   GLN C 121     -60.420  -4.180  30.798  1.00 41.68           O  
ANISOU 5868  O   GLN C 121     3415   4263   8159   -734   -627    -25       O  
ATOM   5869  CB  GLN C 121     -57.087  -4.126  30.871  1.00 40.72           C  
ANISOU 5869  CB  GLN C 121     3432   4028   8009   -560   -674     76       C  
ATOM   5870  CG  GLN C 121     -55.988  -4.471  29.870  1.00 40.37           C  
ANISOU 5870  CG  GLN C 121     3438   3940   7960   -505   -705    104       C  
ATOM   5871  CD  GLN C 121     -54.679  -4.864  30.509  1.00 40.30           C  
ANISOU 5871  CD  GLN C 121     3497   3904   7909   -445   -705    137       C  
ATOM   5872  OE1 GLN C 121     -53.825  -5.472  29.881  1.00 40.55           O  
ANISOU 5872  OE1 GLN C 121     3585   3900   7922   -404   -721    156       O  
ATOM   5873  NE2 GLN C 121     -54.502  -4.522  31.771  1.00 40.68           N  
ANISOU 5873  NE2 GLN C 121     3536   3981   7937   -434   -688    138       N  
ATOM   5874  N   GLN C 122     -59.578  -2.596  32.194  1.00 41.21           N  
ANISOU 5874  N   GLN C 122     3304   4233   8119   -641   -633    -19       N  
ATOM   5875  CA  GLN C 122     -60.618  -2.635  33.261  1.00 41.86           C  
ANISOU 5875  CA  GLN C 122     3347   4373   8184   -706   -588    -57       C  
ATOM   5876  C   GLN C 122     -61.821  -1.730  32.950  1.00 42.50           C  
ANISOU 5876  C   GLN C 122     3305   4532   8311   -709   -599   -118       C  
ATOM   5877  O   GLN C 122     -62.594  -1.477  33.890  1.00 42.43           O  
ANISOU 5877  O   GLN C 122     3242   4586   8293   -746   -566   -160       O  
ATOM   5878  CB  GLN C 122     -60.037  -2.138  34.586  1.00 41.55           C  
ANISOU 5878  CB  GLN C 122     3312   4350   8126   -676   -571    -52       C  
ATOM   5879  CG  GLN C 122     -58.983  -3.046  35.192  1.00 41.49           C  
ANISOU 5879  CG  GLN C 122     3417   4290   8056   -666   -556      2       C  
ATOM   5880  CD  GLN C 122     -58.085  -2.273  36.127  1.00 41.32           C  
ANISOU 5880  CD  GLN C 122     3380   4293   8024   -604   -563      2       C  
ATOM   5881  OE1 GLN C 122     -58.196  -2.369  37.346  1.00 41.50           O  
ANISOU 5881  OE1 GLN C 122     3412   4353   8001   -625   -529     -1       O  
ATOM   5882  NE2 GLN C 122     -57.189  -1.482  35.558  1.00 40.86           N  
ANISOU 5882  NE2 GLN C 122     3297   4221   8004   -532   -604      3       N  
ATOM   5883  N   ILE C 123     -61.980  -1.247  31.714  1.00 43.19           N  
ANISOU 5883  N   ILE C 123     3349   4622   8438   -666   -645   -124       N  
ATOM   5884  CA  ILE C 123     -62.950  -0.159  31.379  1.00 44.16           C  
ANISOU 5884  CA  ILE C 123     3357   4815   8606   -629   -669   -174       C  
ATOM   5885  C   ILE C 123     -63.761  -0.571  30.143  1.00 45.50           C  
ANISOU 5885  C   ILE C 123     3490   5022   8775   -653   -695   -194       C  
ATOM   5886  O   ILE C 123     -63.154  -0.909  29.119  1.00 45.16           O  
ANISOU 5886  O   ILE C 123     3497   4930   8729   -633   -724   -156       O  
ATOM   5887  CB  ILE C 123     -62.199   1.186  31.229  1.00 43.70           C  
ANISOU 5887  CB  ILE C 123     3284   4724   8595   -525   -705   -158       C  
ATOM   5888  CG1 ILE C 123     -62.811   2.268  32.118  1.00 44.10           C  
ANISOU 5888  CG1 ILE C 123     3254   4825   8675   -494   -693   -211       C  
ATOM   5889  CG2 ILE C 123     -62.088   1.655  29.784  1.00 43.65           C  
ANISOU 5889  CG2 ILE C 123     3269   4698   8617   -465   -757   -135       C  
ATOM   5890  CD1 ILE C 123     -62.662   2.004  33.598  1.00 44.28           C  
ANISOU 5890  CD1 ILE C 123     3293   4866   8666   -540   -643   -228       C  
ATOM   5891  N   GLU C 124     -65.095  -0.589  30.252  1.00 47.93           N  
ANISOU 5891  N   GLU C 124     3705   5425   9079   -698   -681   -259       N  
ATOM   5892  CA  GLU C 124     -65.994  -1.021  29.148  1.00 49.35           C  
ANISOU 5892  CA  GLU C 124     3831   5668   9250   -731   -704   -295       C  
ATOM   5893  C   GLU C 124     -65.811  -0.012  28.011  1.00 49.37           C  
ANISOU 5893  C   GLU C 124     3799   5671   9288   -614   -772   -275       C  
ATOM   5894  O   GLU C 124     -66.183   1.165  28.202  1.00 49.95           O  
ANISOU 5894  O   GLU C 124     3801   5781   9396   -532   -794   -295       O  
ATOM   5895  CB  GLU C 124     -67.440  -1.146  29.635  1.00 51.11           C  
ANISOU 5895  CB  GLU C 124     3946   6013   9458   -801   -672   -380       C  
ATOM   5896  CG  GLU C 124     -68.375  -1.856  28.662  1.00 52.54           C  
ANISOU 5896  CG  GLU C 124     4072   6273   9614   -869   -682   -431       C  
ATOM   5897  CD  GLU C 124     -68.180  -3.363  28.525  1.00 53.51           C  
ANISOU 5897  CD  GLU C 124     4292   6341   9696   -998   -638   -421       C  
ATOM   5898  OE1 GLU C 124     -68.350  -4.095  29.539  1.00 54.05           O  
ANISOU 5898  OE1 GLU C 124     4405   6396   9735  -1103   -569   -431       O  
ATOM   5899  OE2 GLU C 124     -67.861  -3.811  27.399  1.00 53.54           O  
ANISOU 5899  OE2 GLU C 124     4334   6312   9694   -993   -670   -404       O  
ATOM   5900  N   LEU C 125     -65.189  -0.442  26.909  1.00 48.91           N  
ANISOU 5900  N   LEU C 125     3799   5564   9218   -603   -802   -233       N  
ATOM   5901  CA  LEU C 125     -64.869   0.432  25.750  1.00 48.80           C  
ANISOU 5901  CA  LEU C 125     3774   5541   9226   -499   -864   -198       C  
ATOM   5902  C   LEU C 125     -64.651  -0.416  24.494  1.00 48.75           C  
ANISOU 5902  C   LEU C 125     3806   5528   9187   -527   -887   -183       C  
ATOM   5903  O   LEU C 125     -64.492  -1.644  24.615  1.00 48.29           O  
ANISOU 5903  O   LEU C 125     3805   5443   9100   -620   -852   -190       O  
ATOM   5904  CB  LEU C 125     -63.612   1.240  26.082  1.00 48.40           C  
ANISOU 5904  CB  LEU C 125     3789   5394   9205   -429   -866   -138       C  
ATOM   5905  CG  LEU C 125     -63.464   2.565  25.340  1.00 48.60           C  
ANISOU 5905  CG  LEU C 125     3795   5407   9265   -317   -914   -109       C  
ATOM   5906  CD1 LEU C 125     -63.820   3.728  26.246  1.00 48.93           C  
ANISOU 5906  CD1 LEU C 125     3788   5454   9348   -261   -906   -136       C  
ATOM   5907  CD2 LEU C 125     -62.054   2.731  24.798  1.00 48.55           C  
ANISOU 5907  CD2 LEU C 125     3877   5308   9259   -287   -923    -41       C  
ATOM   5908  N   LYS C 126     -64.654   0.236  23.331  1.00 49.51           N  
ANISOU 5908  N   LYS C 126     3878   5646   9286   -447   -942   -161       N  
ATOM   5909  CA  LYS C 126     -64.266  -0.363  22.026  1.00 50.09           C  
ANISOU 5909  CA  LYS C 126     3990   5713   9326   -453   -971   -139       C  
ATOM   5910  C   LYS C 126     -63.933   0.771  21.043  1.00 49.43           C  
ANISOU 5910  C   LYS C 126     3902   5626   9252   -339  -1025    -87       C  
ATOM   5911  O   LYS C 126     -64.689   1.764  21.010  1.00 50.02           O  
ANISOU 5911  O   LYS C 126     3905   5755   9344   -264  -1054    -99       O  
ATOM   5912  CB  LYS C 126     -65.380  -1.298  21.538  1.00 51.73           C  
ANISOU 5912  CB  LYS C 126     4137   6020   9497   -535   -971   -211       C  
ATOM   5913  CG  LYS C 126     -66.519  -0.654  20.754  1.00 52.85           C  
ANISOU 5913  CG  LYS C 126     4162   6291   9627   -476  -1025   -251       C  
ATOM   5914  CD  LYS C 126     -66.275  -0.625  19.251  1.00 53.54           C  
ANISOU 5914  CD  LYS C 126     4258   6403   9679   -427  -1079   -224       C  
ATOM   5915  CE  LYS C 126     -67.547  -0.748  18.437  1.00 55.06           C  
ANISOU 5915  CE  LYS C 126     4336   6751   9831   -428  -1120   -295       C  
ATOM   5916  NZ  LYS C 126     -68.135  -2.108  18.524  1.00 55.56           N  
ANISOU 5916  NZ  LYS C 126     4378   6865   9865   -574  -1081   -378       N  
ATOM   5917  N   PHE C 127     -62.841   0.630  20.286  1.00 48.10           N  
ANISOU 5917  N   PHE C 127     3811   5396   9069   -323  -1036    -32       N  
ATOM   5918  CA  PHE C 127     -62.292   1.681  19.387  1.00 47.71           C  
ANISOU 5918  CA  PHE C 127     3783   5322   9022   -227  -1075     30       C  
ATOM   5919  C   PHE C 127     -62.944   1.586  18.002  1.00 47.89           C  
ANISOU 5919  C   PHE C 127     3763   5434   8998   -199  -1126     23       C  
ATOM   5920  O   PHE C 127     -63.343   0.480  17.576  1.00 47.95           O  
ANISOU 5920  O   PHE C 127     3752   5497   8968   -269  -1126    -23       O  
ATOM   5921  CB  PHE C 127     -60.760   1.612  19.331  1.00 46.87           C  
ANISOU 5921  CB  PHE C 127     3772   5119   8917   -231  -1054     86       C  
ATOM   5922  CG  PHE C 127     -60.097   1.994  20.630  1.00 46.08           C  
ANISOU 5922  CG  PHE C 127     3702   4947   8858   -237  -1014     94       C  
ATOM   5923  CD1 PHE C 127     -60.133   3.303  21.083  1.00 46.07           C  
ANISOU 5923  CD1 PHE C 127     3685   4918   8899   -175  -1015    111       C  
ATOM   5924  CD2 PHE C 127     -59.479   1.038  21.420  1.00 45.73           C  
ANISOU 5924  CD2 PHE C 127     3702   4864   8806   -300   -975     81       C  
ATOM   5925  CE1 PHE C 127     -59.556   3.650  22.294  1.00 45.85           C  
ANISOU 5925  CE1 PHE C 127     3677   4836   8905   -186   -978    106       C  
ATOM   5926  CE2 PHE C 127     -58.892   1.388  22.625  1.00 45.53           C  
ANISOU 5926  CE2 PHE C 127     3698   4790   8809   -301   -942     85       C  
ATOM   5927  CZ  PHE C 127     -58.933   2.693  23.060  1.00 45.71           C  
ANISOU 5927  CZ  PHE C 127     3696   4798   8874   -249   -944     93       C  
ATOM   5928  N   ASN C 128     -63.067   2.741  17.340  1.00 47.82           N  
ANISOU 5928  N   ASN C 128     3742   5437   8988    -97  -1168     69       N  
ATOM   5929  CA  ASN C 128     -63.714   2.894  16.010  1.00 48.45           C  
ANISOU 5929  CA  ASN C 128     3779   5612   9016    -41  -1226     74       C  
ATOM   5930  C   ASN C 128     -62.736   2.539  14.894  1.00 47.94           C  
ANISOU 5930  C   ASN C 128     3786   5522   8906    -51  -1235    123       C  
ATOM   5931  O   ASN C 128     -63.170   2.023  13.866  1.00 48.45           O  
ANISOU 5931  O   ASN C 128     3818   5677   8913    -57  -1269    101       O  
ATOM   5932  CB  ASN C 128     -64.339   4.281  15.851  1.00 49.30           C  
ANISOU 5932  CB  ASN C 128     3852   5742   9138     84  -1267    105       C  
ATOM   5933  CG  ASN C 128     -65.585   4.437  16.698  1.00 50.02           C  
ANISOU 5933  CG  ASN C 128     3840   5908   9254     97  -1270     31       C  
ATOM   5934  OD1 ASN C 128     -66.471   3.583  16.671  1.00 50.34           O  
ANISOU 5934  OD1 ASN C 128     3800   6060   9266     38  -1275    -46       O  
ATOM   5935  ND2 ASN C 128     -65.661   5.510  17.468  1.00 50.55           N  
ANISOU 5935  ND2 ASN C 128     3911   5921   9374    168  -1261     46       N  
ATOM   5936  N   PRO C 129     -61.411   2.798  15.028  1.00 46.96           N  
ANISOU 5936  N   PRO C 129     3750   5289   8800    -55  -1204    182       N  
ATOM   5937  CA  PRO C 129     -60.427   2.253  14.091  1.00 46.40           C  
ANISOU 5937  CA  PRO C 129     3740   5204   8685    -82  -1201    212       C  
ATOM   5938  C   PRO C 129     -60.262   0.751  14.311  1.00 45.48           C  
ANISOU 5938  C   PRO C 129     3631   5094   8555   -179  -1174    150       C  
ATOM   5939  O   PRO C 129     -60.064   0.324  15.448  1.00 44.97           O  
ANISOU 5939  O   PRO C 129     3582   4975   8528   -228  -1133    124       O  
ATOM   5940  CB  PRO C 129     -59.113   2.991  14.408  1.00 45.94           C  
ANISOU 5940  CB  PRO C 129     3759   5038   8656    -66  -1169    276       C  
ATOM   5941  CG  PRO C 129     -59.507   4.111  15.358  1.00 46.12           C  
ANISOU 5941  CG  PRO C 129     3766   5016   8739    -17  -1161    288       C  
ATOM   5942  CD  PRO C 129     -60.782   3.659  16.038  1.00 46.38           C  
ANISOU 5942  CD  PRO C 129     3717   5116   8787    -34  -1170    215       C  
ATOM   5943  N   PRO C 130     -60.375  -0.100  13.261  1.00 45.29           N  
ANISOU 5943  N   PRO C 130     3601   5132   8472   -209  -1193    122       N  
ATOM   5944  CA  PRO C 130     -60.069  -1.524  13.397  1.00 44.97           C  
ANISOU 5944  CA  PRO C 130     3592   5072   8420   -298  -1161     66       C  
ATOM   5945  C   PRO C 130     -58.646  -1.716  13.952  1.00 44.12           C  
ANISOU 5945  C   PRO C 130     3568   4857   8335   -308  -1120    101       C  
ATOM   5946  O   PRO C 130     -58.497  -2.431  14.929  1.00 43.70           O  
ANISOU 5946  O   PRO C 130     3542   4751   8308   -357  -1082     72       O  
ATOM   5947  CB  PRO C 130     -60.224  -2.089  11.974  1.00 45.35           C  
ANISOU 5947  CB  PRO C 130     3629   5203   8399   -307  -1194     42       C  
ATOM   5948  CG  PRO C 130     -61.125  -1.103  11.262  1.00 45.94           C  
ANISOU 5948  CG  PRO C 130     3634   5375   8445   -232  -1250     63       C  
ATOM   5949  CD  PRO C 130     -60.850   0.239  11.910  1.00 45.89           C  
ANISOU 5949  CD  PRO C 130     3644   5303   8487   -158  -1246    137       C  
ATOM   5950  N   ALA C 131     -57.660  -1.045  13.339  1.00 43.69           N  
ANISOU 5950  N   ALA C 131     3550   4782   8265   -259  -1126    161       N  
ATOM   5951  CA  ALA C 131     -56.250  -0.960  13.788  1.00 42.98           C  
ANISOU 5951  CA  ALA C 131     3523   4614   8193   -257  -1090    194       C  
ATOM   5952  C   ALA C 131     -56.181  -0.970  15.316  1.00 42.66           C  
ANISOU 5952  C   ALA C 131     3490   4510   8208   -275  -1057    182       C  
ATOM   5953  O   ALA C 131     -55.459  -1.831  15.873  1.00 41.87           O  
ANISOU 5953  O   ALA C 131     3433   4366   8109   -304  -1027    162       O  
ATOM   5954  CB  ALA C 131     -55.612   0.287  13.234  1.00 42.92           C  
ANISOU 5954  CB  ALA C 131     3530   4598   8178   -204  -1098    264       C  
ATOM   5955  N   LEU C 132     -56.920  -0.057  15.956  1.00 43.14           N  
ANISOU 5955  N   LEU C 132     3509   4572   8307   -251  -1062    191       N  
ATOM   5956  CA  LEU C 132     -56.889   0.169  17.428  1.00 43.20           C  
ANISOU 5956  CA  LEU C 132     3516   4530   8366   -262  -1031    182       C  
ATOM   5957  C   LEU C 132     -57.825  -0.803  18.159  1.00 43.56           C  
ANISOU 5957  C   LEU C 132     3540   4594   8416   -319  -1017    124       C  
ATOM   5958  O   LEU C 132     -57.621  -0.979  19.371  1.00 43.23           O  
ANISOU 5958  O   LEU C 132     3514   4510   8399   -341   -984    114       O  
ATOM   5959  CB  LEU C 132     -57.263   1.621  17.751  1.00 43.33           C  
ANISOU 5959  CB  LEU C 132     3503   4539   8422   -209  -1041    211       C  
ATOM   5960  CG  LEU C 132     -56.124   2.548  18.181  1.00 43.00           C  
ANISOU 5960  CG  LEU C 132     3499   4430   8407   -187  -1016    250       C  
ATOM   5961  CD1 LEU C 132     -56.660   3.665  19.065  1.00 43.34           C  
ANISOU 5961  CD1 LEU C 132     3514   4448   8503   -155  -1010    249       C  
ATOM   5962  CD2 LEU C 132     -55.018   1.806  18.915  1.00 42.56           C  
ANISOU 5962  CD2 LEU C 132     3481   4340   8349   -225   -982    235       C  
ATOM   5963  N   GLN C 133     -58.810  -1.400  17.482  1.00 44.65           N  
ANISOU 5963  N   GLN C 133     3641   4797   8527   -349  -1037     85       N  
ATOM   5964  CA  GLN C 133     -59.636  -2.490  18.079  1.00 45.52           C  
ANISOU 5964  CA  GLN C 133     3739   4920   8633   -428  -1013     23       C  
ATOM   5965  C   GLN C 133     -58.794  -3.774  18.152  1.00 45.78           C  
ANISOU 5965  C   GLN C 133     3859   4890   8645   -475   -982     13       C  
ATOM   5966  O   GLN C 133     -58.635  -4.301  19.273  1.00 45.99           O  
ANISOU 5966  O   GLN C 133     3926   4862   8686   -511   -942      6       O  
ATOM   5967  CB  GLN C 133     -60.952  -2.712  17.326  1.00 46.09           C  
ANISOU 5967  CB  GLN C 133     3737   5094   8680   -454  -1041    -29       C  
ATOM   5968  CG  GLN C 133     -62.179  -2.256  18.106  1.00 46.26           C  
ANISOU 5968  CG  GLN C 133     3675   5174   8726   -464  -1039    -66       C  
ATOM   5969  CD  GLN C 133     -62.478  -3.114  19.311  1.00 46.32           C  
ANISOU 5969  CD  GLN C 133     3702   5150   8747   -554   -985   -107       C  
ATOM   5970  OE1 GLN C 133     -62.640  -2.622  20.424  1.00 46.52           O  
ANISOU 5970  OE1 GLN C 133     3710   5160   8804   -547   -962   -104       O  
ATOM   5971  NE2 GLN C 133     -62.555  -4.415  19.103  1.00 46.78           N  
ANISOU 5971  NE2 GLN C 133     3801   5194   8776   -642   -959   -147       N  
ATOM   5972  N   ASP C 134     -58.266  -4.256  17.021  1.00 46.06           N  
ANISOU 5972  N   ASP C 134     3925   4931   8644   -469   -998     13       N  
ATOM   5973  CA  ASP C 134     -57.498  -5.530  16.970  1.00 46.07           C  
ANISOU 5973  CA  ASP C 134     4010   4869   8623   -502   -971     -4       C  
ATOM   5974  C   ASP C 134     -56.423  -5.475  18.057  1.00 45.25           C  
ANISOU 5974  C   ASP C 134     3963   4689   8540   -471   -943     33       C  
ATOM   5975  O   ASP C 134     -56.550  -6.210  19.046  1.00 45.43           O  
ANISOU 5975  O   ASP C 134     4030   4661   8569   -510   -908     18       O  
ATOM   5976  CB  ASP C 134     -56.916  -5.804  15.581  1.00 46.51           C  
ANISOU 5976  CB  ASP C 134     4083   4951   8637   -480   -995     -6       C  
ATOM   5977  CG  ASP C 134     -57.966  -6.054  14.509  1.00 47.76           C  
ANISOU 5977  CG  ASP C 134     4187   5195   8762   -515  -1023    -54       C  
ATOM   5978  OD1 ASP C 134     -57.587  -6.097  13.323  1.00 48.38           O  
ANISOU 5978  OD1 ASP C 134     4266   5314   8800   -492  -1048    -54       O  
ATOM   5979  OD2 ASP C 134     -59.157  -6.198  14.863  1.00 48.78           O  
ANISOU 5979  OD2 ASP C 134     4267   5363   8901   -567  -1020    -96       O  
ATOM   5980  N   ALA C 135     -55.446  -4.580  17.914  1.00 44.97           N  
ANISOU 5980  N   ALA C 135     3923   4651   8509   -407   -955     78       N  
ATOM   5981  CA  ALA C 135     -54.284  -4.452  18.824  1.00 44.57           C  
ANISOU 5981  CA  ALA C 135     3913   4550   8470   -372   -933    105       C  
ATOM   5982  C   ALA C 135     -54.753  -4.479  20.285  1.00 44.77           C  
ANISOU 5982  C   ALA C 135     3940   4547   8522   -396   -907    100       C  
ATOM   5983  O   ALA C 135     -53.985  -4.965  21.132  1.00 44.43           O  
ANISOU 5983  O   ALA C 135     3950   4459   8471   -382   -884    108       O  
ATOM   5984  CB  ALA C 135     -53.522  -3.196  18.504  1.00 44.05           C  
ANISOU 5984  CB  ALA C 135     3818   4505   8414   -322   -947    144       C  
ATOM   5985  N   TYR C 136     -55.977  -4.011  20.557  1.00 45.43           N  
ANISOU 5985  N   TYR C 136     3967   4666   8629   -426   -910     85       N  
ATOM   5986  CA  TYR C 136     -56.579  -3.912  21.915  1.00 46.11           C  
ANISOU 5986  CA  TYR C 136     4039   4742   8736   -455   -882     75       C  
ATOM   5987  C   TYR C 136     -57.003  -5.295  22.440  1.00 46.81           C  
ANISOU 5987  C   TYR C 136     4186   4796   8803   -524   -847     48       C  
ATOM   5988  O   TYR C 136     -56.917  -5.527  23.664  1.00 46.42           O  
ANISOU 5988  O   TYR C 136     4169   4715   8753   -538   -816     55       O  
ATOM   5989  CB  TYR C 136     -57.760  -2.937  21.890  1.00 46.56           C  
ANISOU 5989  CB  TYR C 136     4007   4861   8822   -456   -899     60       C  
ATOM   5990  CG  TYR C 136     -58.340  -2.569  23.234  1.00 46.79           C  
ANISOU 5990  CG  TYR C 136     4006   4897   8875   -475   -872     45       C  
ATOM   5991  CD1 TYR C 136     -57.527  -2.365  24.338  1.00 46.83           C  
ANISOU 5991  CD1 TYR C 136     4043   4861   8887   -456   -849     65       C  
ATOM   5992  CD2 TYR C 136     -59.702  -2.378  23.393  1.00 46.99           C  
ANISOU 5992  CD2 TYR C 136     3959   4983   8912   -508   -872      4       C  
ATOM   5993  CE1 TYR C 136     -58.052  -2.009  25.569  1.00 46.84           C  
ANISOU 5993  CE1 TYR C 136     4014   4878   8905   -473   -824     48       C  
ATOM   5994  CE2 TYR C 136     -60.243  -2.019  24.616  1.00 47.33           C  
ANISOU 5994  CE2 TYR C 136     3966   5042   8972   -525   -846    -15       C  
ATOM   5995  CZ  TYR C 136     -59.414  -1.833  25.707  1.00 47.16           C  
ANISOU 5995  CZ  TYR C 136     3986   4974   8957   -508   -820      8       C  
ATOM   5996  OH  TYR C 136     -59.935  -1.473  26.913  1.00 47.72           O  
ANISOU 5996  OH  TYR C 136     4021   5069   9040   -526   -793    -15       O  
ATOM   5997  N   TYR C 137     -57.476  -6.188  21.568  1.00 47.83           N  
ANISOU 5997  N   TYR C 137     4334   4928   8910   -571   -849     15       N  
ATOM   5998  CA  TYR C 137     -57.822  -7.581  21.952  1.00 49.15           C  
ANISOU 5998  CA  TYR C 137     4577   5041   9055   -647   -809    -11       C  
ATOM   5999  C   TYR C 137     -56.526  -8.335  22.253  1.00 50.12           C  
ANISOU 5999  C   TYR C 137     4808   5078   9156   -602   -794     19       C  
ATOM   6000  O   TYR C 137     -56.447  -8.953  23.334  1.00 50.79           O  
ANISOU 6000  O   TYR C 137     4963   5105   9230   -623   -757     32       O  
ATOM   6001  CB  TYR C 137     -58.651  -8.293  20.881  1.00 49.49           C  
ANISOU 6001  CB  TYR C 137     4607   5114   9081   -715   -813    -66       C  
ATOM   6002  CG  TYR C 137     -60.105  -7.897  20.833  1.00 49.84           C  
ANISOU 6002  CG  TYR C 137     4550   5249   9135   -776   -817   -113       C  
ATOM   6003  CD1 TYR C 137     -60.887  -7.864  21.977  1.00 49.97           C  
ANISOU 6003  CD1 TYR C 137     4545   5277   9163   -833   -781   -128       C  
ATOM   6004  CD2 TYR C 137     -60.706  -7.563  19.630  1.00 50.45           C  
ANISOU 6004  CD2 TYR C 137     4549   5415   9203   -774   -858   -146       C  
ATOM   6005  CE1 TYR C 137     -62.225  -7.500  21.926  1.00 51.04           C  
ANISOU 6005  CE1 TYR C 137     4574   5514   9304   -884   -784   -181       C  
ATOM   6006  CE2 TYR C 137     -62.042  -7.203  19.558  1.00 51.12           C  
ANISOU 6006  CE2 TYR C 137     4529   5601   9290   -817   -867   -196       C  
ATOM   6007  CZ  TYR C 137     -62.808  -7.172  20.711  1.00 51.62           C  
ANISOU 6007  CZ  TYR C 137     4564   5679   9369   -873   -830   -217       C  
ATOM   6008  OH  TYR C 137     -64.125  -6.818  20.630  1.00 52.17           O  
ANISOU 6008  OH  TYR C 137     4518   5866   9438   -911   -839   -277       O  
ATOM   6009  N   ARG C 138     -55.546  -8.251  21.342  1.00 50.99           N  
ANISOU 6009  N   ARG C 138     4929   5187   9255   -538   -823     31       N  
ATOM   6010  CA  ARG C 138     -54.237  -8.953  21.436  1.00 51.86           C  
ANISOU 6010  CA  ARG C 138     5129   5234   9341   -477   -817     50       C  
ATOM   6011  C   ARG C 138     -53.457  -8.412  22.640  1.00 51.87           C  
ANISOU 6011  C   ARG C 138     5133   5228   9345   -420   -811     90       C  
ATOM   6012  O   ARG C 138     -52.653  -9.176  23.190  1.00 51.89           O  
ANISOU 6012  O   ARG C 138     5219   5175   9321   -378   -798    105       O  
ATOM   6013  CB  ARG C 138     -53.472  -8.830  20.113  1.00 52.69           C  
ANISOU 6013  CB  ARG C 138     5219   5369   9431   -428   -849     43       C  
ATOM   6014  CG  ARG C 138     -54.006  -9.735  19.009  1.00 54.47           C  
ANISOU 6014  CG  ARG C 138     5469   5588   9638   -479   -850     -4       C  
ATOM   6015  CD  ARG C 138     -53.558  -9.302  17.621  1.00 56.01           C  
ANISOU 6015  CD  ARG C 138     5618   5847   9817   -443   -885    -12       C  
ATOM   6016  NE  ARG C 138     -52.181  -9.697  17.305  1.00 57.48           N  
ANISOU 6016  NE  ARG C 138     5854   6009   9977   -370   -887     -7       N  
ATOM   6017  CZ  ARG C 138     -51.282  -8.965  16.627  1.00 57.72           C  
ANISOU 6017  CZ  ARG C 138     5840   6096   9993   -314   -909      9       C  
ATOM   6018  NH1 ARG C 138     -51.571  -7.750  16.187  1.00 57.81           N  
ANISOU 6018  NH1 ARG C 138     5771   6177  10016   -318   -931     34       N  
ATOM   6019  NH2 ARG C 138     -50.069  -9.447  16.412  1.00 58.04           N  
ANISOU 6019  NH2 ARG C 138     5921   6124  10007   -251   -907      1       N  
ATOM   6020  N   ALA C 139     -53.718  -7.162  23.046  1.00 52.69           N  
ANISOU 6020  N   ALA C 139     5153   5388   9478   -415   -822    102       N  
ATOM   6021  CA  ALA C 139     -53.147  -6.497  24.245  1.00 53.57           C  
ANISOU 6021  CA  ALA C 139     5251   5507   9596   -375   -814    127       C  
ATOM   6022  C   ALA C 139     -53.651  -7.163  25.531  1.00 55.20           C  
ANISOU 6022  C   ALA C 139     5510   5675   9786   -413   -778    132       C  
ATOM   6023  O   ALA C 139     -52.811  -7.471  26.402  1.00 54.52           O  
ANISOU 6023  O   ALA C 139     5476   5566   9672   -365   -769    155       O  
ATOM   6024  CB  ALA C 139     -53.492  -5.029  24.240  1.00 53.16           C  
ANISOU 6024  CB  ALA C 139     5102   5513   9583   -371   -830    129       C  
ATOM   6025  N   ARG C 140     -54.970  -7.360  25.648  1.00 58.01           N  
ANISOU 6025  N   ARG C 140     5850   6037  10154   -495   -757    110       N  
ATOM   6026  CA  ARG C 140     -55.634  -8.041  26.799  1.00 60.10           C  
ANISOU 6026  CA  ARG C 140     6165   6268  10399   -556   -712    111       C  
ATOM   6027  C   ARG C 140     -55.136  -9.491  26.905  1.00 59.95           C  
ANISOU 6027  C   ARG C 140     6283   6156  10337   -555   -688    129       C  
ATOM   6028  O   ARG C 140     -55.100 -10.018  28.033  1.00 60.90           O  
ANISOU 6028  O   ARG C 140     6476   6235  10426   -564   -654    155       O  
ATOM   6029  CB  ARG C 140     -57.162  -7.953  26.672  1.00 62.71           C  
ANISOU 6029  CB  ARG C 140     6436   6642  10750   -654   -694     70       C  
ATOM   6030  CG  ARG C 140     -57.744  -6.667  27.250  1.00 64.69           C  
ANISOU 6030  CG  ARG C 140     6576   6969  11031   -650   -701     58       C  
ATOM   6031  CD  ARG C 140     -59.171  -6.334  26.850  1.00 66.36           C  
ANISOU 6031  CD  ARG C 140     6696   7251  11265   -716   -701      8       C  
ATOM   6032  NE  ARG C 140     -60.155  -7.037  27.663  1.00 68.01           N  
ANISOU 6032  NE  ARG C 140     6922   7465  11454   -817   -649    -17       N  
ATOM   6033  CZ  ARG C 140     -61.140  -7.806  27.194  1.00 70.97           C  
ANISOU 6033  CZ  ARG C 140     7293   7853  11817   -914   -626    -63       C  
ATOM   6034  NH1 ARG C 140     -61.306  -7.981  25.891  1.00 71.38           N  
ANISOU 6034  NH1 ARG C 140     7322   7922  11876   -917   -657    -89       N  
ATOM   6035  NH2 ARG C 140     -61.971  -8.396  28.041  1.00 72.72           N  
ANISOU 6035  NH2 ARG C 140     7532   8079  12017  -1015   -569    -86       N  
ATOM   6036  N   ALA C 141     -54.742 -10.101  25.783  1.00 58.89           N  
ANISOU 6036  N   ALA C 141     6188   5987  10198   -538   -704    116       N  
ATOM   6037  CA  ALA C 141     -54.177 -11.468  25.712  1.00 59.46           C  
ANISOU 6037  CA  ALA C 141     6397   5960  10234   -519   -685    126       C  
ATOM   6038  C   ALA C 141     -52.736 -11.504  26.251  1.00 59.45           C  
ANISOU 6038  C   ALA C 141     6443   5942  10203   -396   -703    166       C  
ATOM   6039  O   ALA C 141     -52.283 -12.608  26.615  1.00 60.47           O  
ANISOU 6039  O   ALA C 141     6698   5984  10294   -362   -683    188       O  
ATOM   6040  CB  ALA C 141     -54.245 -11.970  24.292  1.00 60.07           C  
ANISOU 6040  CB  ALA C 141     6483   6023  10317   -536   -699     86       C  
ATOM   6041  N   GLY C 142     -52.036 -10.360  26.290  1.00 58.10           N  
ANISOU 6041  N   GLY C 142     6177   5852  10045   -331   -737    173       N  
ATOM   6042  CA  GLY C 142     -50.644 -10.242  26.777  1.00 56.48           C  
ANISOU 6042  CA  GLY C 142     5985   5663   9808   -219   -757    197       C  
ATOM   6043  C   GLY C 142     -49.715  -9.654  25.723  1.00 54.88           C  
ANISOU 6043  C   GLY C 142     5716   5519   9617   -160   -795    177       C  
ATOM   6044  O   GLY C 142     -48.643  -9.121  26.099  1.00 54.87           O  
ANISOU 6044  O   GLY C 142     5677   5571   9600    -84   -813    183       O  
ATOM   6045  N   GLU C 143     -50.109  -9.740  24.449  1.00 52.79           N  
ANISOU 6045  N   GLU C 143     5432   5252   9372   -198   -803    151       N  
ATOM   6046  CA  GLU C 143     -49.310  -9.301  23.277  1.00 51.43           C  
ANISOU 6046  CA  GLU C 143     5206   5132   9201   -155   -832    132       C  
ATOM   6047  C   GLU C 143     -49.644  -7.836  22.957  1.00 49.89           C  
ANISOU 6047  C   GLU C 143     4898   5013   9044   -188   -847    133       C  
ATOM   6048  O   GLU C 143     -50.465  -7.594  22.048  1.00 49.71           O  
ANISOU 6048  O   GLU C 143     4840   5004   9041   -241   -854    120       O  
ATOM   6049  CB  GLU C 143     -49.606 -10.260  22.127  1.00 51.85           C  
ANISOU 6049  CB  GLU C 143     5311   5142   9245   -179   -831    103       C  
ATOM   6050  CG  GLU C 143     -48.761 -10.015  20.899  1.00 52.26           C  
ANISOU 6050  CG  GLU C 143     5322   5247   9286   -134   -856     82       C  
ATOM   6051  CD  GLU C 143     -49.601  -9.913  19.642  1.00 52.43           C  
ANISOU 6051  CD  GLU C 143     5308   5291   9320   -200   -865     56       C  
ATOM   6052  OE1 GLU C 143     -50.111 -10.961  19.193  1.00 52.82           O  
ANISOU 6052  OE1 GLU C 143     5422   5286   9359   -236   -853     25       O  
ATOM   6053  OE2 GLU C 143     -49.774  -8.780  19.144  1.00 51.91           O  
ANISOU 6053  OE2 GLU C 143     5154   5295   9271   -217   -882     65       O  
ATOM   6054  N   ALA C 144     -49.001  -6.894  23.657  1.00 48.41           N  
ANISOU 6054  N   ALA C 144     4658   4873   8863   -154   -851    146       N  
ATOM   6055  CA  ALA C 144     -49.464  -5.492  23.815  1.00 47.13           C  
ANISOU 6055  CA  ALA C 144     4409   4754   8741   -189   -854    151       C  
ATOM   6056  C   ALA C 144     -48.517  -4.486  23.150  1.00 45.84           C  
ANISOU 6056  C   ALA C 144     4186   4647   8584   -161   -868    149       C  
ATOM   6057  O   ALA C 144     -48.726  -3.279  23.351  1.00 45.42           O  
ANISOU 6057  O   ALA C 144     4074   4617   8564   -182   -867    154       O  
ATOM   6058  CB  ALA C 144     -49.610  -5.187  25.285  1.00 47.02           C  
ANISOU 6058  CB  ALA C 144     4389   4742   8731   -190   -838    158       C  
ATOM   6059  N   ALA C 145     -47.529  -4.950  22.389  1.00 45.35           N  
ANISOU 6059  N   ALA C 145     4139   4602   8488   -119   -877    138       N  
ATOM   6060  CA  ALA C 145     -46.507  -4.092  21.745  1.00 44.95           C  
ANISOU 6060  CA  ALA C 145     4034   4611   8432   -102   -882    132       C  
ATOM   6061  C   ALA C 145     -47.174  -3.133  20.756  1.00 44.04           C  
ANISOU 6061  C   ALA C 145     3880   4506   8346   -151   -887    148       C  
ATOM   6062  O   ALA C 145     -47.109  -1.922  20.989  1.00 44.17           O  
ANISOU 6062  O   ALA C 145     3853   4539   8391   -169   -880    159       O  
ATOM   6063  CB  ALA C 145     -45.462  -4.946  21.069  1.00 45.53           C  
ANISOU 6063  CB  ALA C 145     4132   4708   8458    -49   -888    110       C  
ATOM   6064  N   ASN C 146     -47.815  -3.680  19.719  1.00 43.89           N  
ANISOU 6064  N   ASN C 146     3882   4474   8317   -168   -899    149       N  
ATOM   6065  CA  ASN C 146     -48.396  -2.949  18.555  1.00 43.15           C  
ANISOU 6065  CA  ASN C 146     3759   4403   8232   -197   -911    166       C  
ATOM   6066  C   ASN C 146     -49.464  -1.976  19.046  1.00 42.28           C  
ANISOU 6066  C   ASN C 146     3617   4278   8169   -224   -913    187       C  
ATOM   6067  O   ASN C 146     -49.591  -0.892  18.462  1.00 42.65           O  
ANISOU 6067  O   ASN C 146     3635   4340   8228   -230   -918    212       O  
ATOM   6068  CB  ASN C 146     -48.998  -3.910  17.528  1.00 43.14           C  
ANISOU 6068  CB  ASN C 146     3784   4400   8204   -210   -926    150       C  
ATOM   6069  CG  ASN C 146     -48.262  -5.228  17.528  1.00 43.58           C  
ANISOU 6069  CG  ASN C 146     3894   4439   8226   -178   -920    118       C  
ATOM   6070  OD1 ASN C 146     -48.314  -5.964  18.515  1.00 43.58           O  
ANISOU 6070  OD1 ASN C 146     3936   4391   8229   -167   -909    109       O  
ATOM   6071  ND2 ASN C 146     -47.522  -5.498  16.465  1.00 44.03           N  
ANISOU 6071  ND2 ASN C 146     3951   4532   8243   -157   -925    102       N  
ATOM   6072  N   PHE C 147     -50.202  -2.367  20.081  1.00 41.26           N  
ANISOU 6072  N   PHE C 147     3497   4119   8059   -238   -906    176       N  
ATOM   6073  CA  PHE C 147     -51.237  -1.525  20.721  1.00 40.61           C  
ANISOU 6073  CA  PHE C 147     3378   4030   8021   -258   -905    183       C  
ATOM   6074  C   PHE C 147     -50.590  -0.259  21.285  1.00 40.46           C  
ANISOU 6074  C   PHE C 147     3330   4012   8028   -244   -893    195       C  
ATOM   6075  O   PHE C 147     -51.077   0.848  20.969  1.00 41.16           O  
ANISOU 6075  O   PHE C 147     3391   4100   8147   -246   -899    212       O  
ATOM   6076  CB  PHE C 147     -51.966  -2.296  21.819  1.00 40.31           C  
ANISOU 6076  CB  PHE C 147     3358   3968   7987   -281   -891    164       C  
ATOM   6077  CG  PHE C 147     -53.154  -1.551  22.364  1.00 40.19           C  
ANISOU 6077  CG  PHE C 147     3296   3961   8011   -303   -890    159       C  
ATOM   6078  CD1 PHE C 147     -54.154  -1.104  21.516  1.00 40.20           C  
ANISOU 6078  CD1 PHE C 147     3259   3989   8026   -311   -912    160       C  
ATOM   6079  CD2 PHE C 147     -53.259  -1.280  23.715  1.00 40.01           C  
ANISOU 6079  CD2 PHE C 147     3264   3931   8007   -308   -869    150       C  
ATOM   6080  CE1 PHE C 147     -55.240  -0.408  22.009  1.00 40.35           C  
ANISOU 6080  CE1 PHE C 147     3227   4024   8078   -317   -914    149       C  
ATOM   6081  CE2 PHE C 147     -54.350  -0.583  24.208  1.00 40.23           C  
ANISOU 6081  CE2 PHE C 147     3243   3973   8069   -323   -867    138       C  
ATOM   6082  CZ  PHE C 147     -55.334  -0.147  23.353  1.00 40.49           C  
ANISOU 6082  CZ  PHE C 147     3235   4031   8118   -325   -889    135       C  
ATOM   6083  N   CYS C 148     -49.535  -0.422  22.090  1.00 39.75           N  
ANISOU 6083  N   CYS C 148     3249   3928   7926   -229   -877    182       N  
ATOM   6084  CA  CYS C 148     -48.780   0.691  22.720  1.00 39.31           C  
ANISOU 6084  CA  CYS C 148     3163   3883   7890   -227   -860    177       C  
ATOM   6085  C   CYS C 148     -48.214   1.582  21.612  1.00 39.23           C  
ANISOU 6085  C   CYS C 148     3142   3883   7881   -235   -858    196       C  
ATOM   6086  O   CYS C 148     -48.322   2.813  21.722  1.00 38.78           O  
ANISOU 6086  O   CYS C 148     3067   3807   7860   -250   -846    205       O  
ATOM   6087  CB  CYS C 148     -47.682   0.161  23.634  1.00 39.26           C  
ANISOU 6087  CB  CYS C 148     3162   3902   7852   -203   -849    152       C  
ATOM   6088  SG  CYS C 148     -48.325  -0.682  25.104  1.00 39.39           S  
ANISOU 6088  SG  CYS C 148     3203   3902   7862   -196   -844    141       S  
ATOM   6089  N   ALA C 149     -47.671   0.964  20.564  1.00 39.70           N  
ANISOU 6089  N   ALA C 149     3218   3967   7900   -226   -867    201       N  
ATOM   6090  CA  ALA C 149     -47.084   1.646  19.388  1.00 40.28           C  
ANISOU 6090  CA  ALA C 149     3287   4060   7957   -239   -861    222       C  
ATOM   6091  C   ALA C 149     -48.171   2.459  18.681  1.00 40.56           C  
ANISOU 6091  C   ALA C 149     3327   4066   8017   -248   -874    263       C  
ATOM   6092  O   ALA C 149     -47.874   3.588  18.249  1.00 41.06           O  
ANISOU 6092  O   ALA C 149     3393   4117   8091   -263   -859    290       O  
ATOM   6093  CB  ALA C 149     -46.455   0.637  18.458  1.00 40.49           C  
ANISOU 6093  CB  ALA C 149     3328   4125   7929   -223   -869    211       C  
ATOM   6094  N   LEU C 150     -49.381   1.902  18.579  1.00 40.76           N  
ANISOU 6094  N   LEU C 150     3355   4083   8048   -238