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***  OXIDOREDUCTASE 31-OCT-14 3X1B  ***

elNémo ID: 20081917414145086

Job options:

ID        	=	 20081917414145086
JOBID     	=	 OXIDOREDUCTASE 31-OCT-14 3X1B
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    OXIDOREDUCTASE                          31-OCT-14   3X1B              
TITLE     CRYSTAL STRUCTURE OF LACCASE FROM LENTINUS SP. AT 1.8 A RESOLUTION    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LACCASE;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.10.3.2                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LENTINUS;                                       
SOURCE   3 ORGANISM_TAXID: 5357                                                 
KEYWDS    OXIDOREDUCTASE, MULTICOPPER OXIDASE, GLYCOSYLATION                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.Y.JENG,L.F.SHYUR,A.H.J.WANG                                         
REVDAT   1   10-DEC-14 3X1B    0                                                
JRNL        AUTH   W.C.LIU,M.MAESTRE-REYNA,W.Y.JENG,C.C.LEE,C.A.HSU,T.N.WEN,    
JRNL        AUTH 2 A.H.J.WANG,L.F.SHYUR                                         
JRNL        TITL   CRYSTAL STRUCTURE OF LACCASE FROM LENTINUS SP. AT 1.8 A      
JRNL        TITL 2 RESOLUTION                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 114401                         
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) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.145                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5728                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 15524                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 857                          
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7628                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 335                                     
REMARK   3   SOLVENT ATOMS            : 1116                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.22000                                              
REMARK   3    B22 (A**2) : -2.19000                                             
REMARK   3    B33 (A**2) : 0.97000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.154         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.104         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.077         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.608         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8280 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11304 ; 1.410 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   998 ; 6.492 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   356 ;34.687 ;24.157       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1048 ;12.140 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;18.876 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1317 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6336 ; 0.007 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  5000 ; 1.164 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8106 ; 1.964 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3248 ; 2.822 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3198 ; 4.094 ; 4.500       
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):  8248 ; 1.463 ; 3.000       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    22        A   521                          
REMARK   3    RESIDUE RANGE :   A   601        A   617                          
REMARK   3    RESIDUE RANGE :   A   701        A  1319                          
REMARK   3    ORIGIN FOR THE GROUP (A):  84.1508  35.3043  53.7828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0025 T22:   0.0101                                     
REMARK   3      T33:   0.0328 T12:   0.0000                                     
REMARK   3      T13:   0.0001 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0008 L22:   0.0080                                     
REMARK   3      L33:   0.0034 L12:   0.0013                                     
REMARK   3      L13:   0.0012 L23:  -0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0001 S12:  -0.0007 S13:   0.0004                       
REMARK   3      S21:   0.0015 S22:   0.0004 S23:  -0.0003                       
REMARK   3      S31:  -0.0004 S32:  -0.0003 S33:  -0.0005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    22        B   521                          
REMARK   3    RESIDUE RANGE :   B   601        B   618                          
REMARK   3    RESIDUE RANGE :   B   701        B  1197                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.3663  76.5115  49.9755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0024 T22:   0.0103                                     
REMARK   3      T33:   0.0321 T12:   0.0001                                     
REMARK   3      T13:   0.0003 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0011 L22:   0.0097                                     
REMARK   3      L33:   0.0014 L12:   0.0030                                     
REMARK   3      L13:   0.0003 L23:   0.0014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:  -0.0001 S13:  -0.0011                       
REMARK   3      S21:   0.0011 S22:   0.0005 S23:  -0.0013                       
REMARK   3      S31:   0.0005 S32:  -0.0001 S33:  -0.0003                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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                                                           
REMARK   4                                                                      
REMARK   4 3X1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB097053.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90000                            
REMARK 200  MONOCHROMATOR                  : LN2-COOLED DOUBLE CRYSTAL          
REMARK 200                                   SI(111) MONOCHROMATOR              
REMARK 200  OPTICS                         : HORIZONTAL FOCUSING MIRROR         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114514                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.600                              
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: 1KYA                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% ISOPROPANOL, 20% POLYETHYLENE        
REMARK 280  GLYCOL 4000, 100 MM SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 298K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       49.63300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       94.33800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.63300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       94.33800            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     PHE A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     VAL A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     PHE A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     PHE B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     THR B    12                                                      
REMARK 465     LEU B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     VAL B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     PHE B    20                                                      
REMARK 465     ALA B    21                                                      
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   O    HOH B   707     O    HOH B  1062              1.90            
REMARK 500   O6   BMA B   609     O5   MAN B   610              2.05            
REMARK 500   O3   BMA B   609     C2   MAN B   613              2.11            
REMARK 500   O    HOH A  1130     O    HOH A  1192              2.13            
REMARK 500   O    HOH B   950     O    HOH B   970              2.13            
REMARK 500   OE1  GLU A   170     O    HOH A  1037              2.16            
REMARK 500   OD2  ASP B    44     O    HOH B  1085              2.17            
REMARK 500   C3   BMA B   609     C1   MAN B   613              2.18            
REMARK 500   OD2  ASP A    44     O    HOH A  1110              2.19            
REMARK 500   O3   NAG A   601     O    HOH A  1110              2.19            
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    LEU A  79      130.46     76.43                                   
REMARK 500    SER A 134     -134.33     46.01                                   
REMARK 500    LEU A 185       56.58   -112.98                                   
REMARK 500    ASP A 227      -75.06   -157.07                                   
REMARK 500    THR A 357      -51.84   -125.59                                   
REMARK 500    ASN A 458       72.33   -151.00                                   
REMARK 500    LEU B  79      127.36     75.80                                   
REMARK 500    SER B 134     -135.82     50.92                                   
REMARK 500    ASN B 162     -167.06   -160.18                                   
REMARK 500    ASP B 227      -72.06   -156.35                                   
REMARK 500    ASP B 276     -179.29   -174.88                                   
REMARK 500    GLU B 440      -61.47   -103.22                                   
REMARK 500    ASP B 441       44.24   -140.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1290        DISTANCE =  5.47 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 614  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 420   NE2                                                    
REMARK 620 2 HIS A  85   NE2 177.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 615  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 420   NE2                                                    
REMARK 620 2 HIS B  85   NE2 179.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 616  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 474   NE2                                                    
REMARK 620 2 HIS A 422   NE2 117.9                                              
REMARK 620 3 HIS A 132   NE2 119.6 114.1                                        
REMARK 620 4 HOH A 713   O   101.6 102.4  95.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 616  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  87   ND1                                                    
REMARK 620 2 HIS B 130   NE2 135.8                                              
REMARK 620 3 HIS B 476   NE2 105.3 115.0                                        
REMARK 620 4 HOH B 718   O   113.6  92.3  78.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 615  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  87   ND1                                                    
REMARK 620 2 HIS A 130   NE2 135.5                                              
REMARK 620 3 HIS A 476   NE2 104.8 115.4                                        
REMARK 620 4 HOH A 713   O   115.5  92.1  77.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 617  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 422   NE2                                                    
REMARK 620 2 HIS B 474   NE2 118.2                                              
REMARK 620 3 HIS B 132   NE2 116.3 116.4                                        
REMARK 620 4 HOH B 718   O   103.4  99.0  97.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 618  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 480   ND1                                                    
REMARK 620 2 HIS B 417   ND1 106.3                                              
REMARK 620 3 CYS B 475   SG  134.2 118.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 617  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 417   ND1                                                    
REMARK 620 2 HIS A 480   ND1 108.2                                              
REMARK 620 3 CYS A 475   SG  120.9 129.8                                        
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 CU A 614                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 615                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 616                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 617                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 615                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 616                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 617                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 618                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  75 RESIDUES 601 TO 606                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 613 BOUND   
REMARK 800  TO ASN A 238                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  458 RESIDUES 607 TO 612                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800  75 RESIDUES 601 TO 606                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 614 BOUND   
REMARK 800  TO ASN B 238                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800  458 RESIDUES 607 TO 613                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE DATABASE REFERENCES FOR THIS PROTEIN DOES NOT           
REMARK 999 CURRENTLY EXIST.                                                     
DBREF  3X1B A    1   521  PDB    3X1B     3X1B             1    521             
DBREF  3X1B B    1   521  PDB    3X1B     3X1B             1    521             
SEQRES   1 A  521  MET LYS ALA LEU SER PHE LEU THR PRO ILE VAL THR LEU          
SEQRES   2 A  521  ALA LEU VAL ALA GLY ALA PHE ALA SER VAL GLY PRO VAL          
SEQRES   3 A  521  ALA ASN LEU LYS ILE GLY ASN ALA ALA VAL SER PRO ASP          
SEQRES   4 A  521  GLY TYR THR ARG ASP ALA VAL VAL VAL ASN GLY ALA THR          
SEQRES   5 A  521  PRO GLY PRO LEU ILE VAL GLY ASN LYS GLY ASP ASN PHE          
SEQRES   6 A  521  ARG LEU ASN VAL ILE ASP GLU LEU THR ASN HIS THR MET          
SEQRES   7 A  521  LEU LYS SER THR SER ILE HIS TRP HIS GLY PHE PHE GLN          
SEQRES   8 A  521  HIS GLY THR ASN TRP ALA ASP GLY GLY ALA PHE VAL ASN          
SEQRES   9 A  521  GLN CYS PRO ILE SER SER GLY HIS SER PHE SER TYR ASN          
SEQRES  10 A  521  PHE GLN ALA LYS ASP GLN ALA GLY THR PHE TRP TYR HIS          
SEQRES  11 A  521  SER HIS LEU SER THR GLN TYR CYS ASP GLY LEU ARG GLY          
SEQRES  12 A  521  PRO PHE VAL VAL TYR ASP PRO LYS ASP PRO HIS LYS LYS          
SEQRES  13 A  521  LEU TYR ASP VAL ASP ASN GLU SER THR VAL ILE THR LEU          
SEQRES  14 A  521  GLU ASP TRP TYR HIS THR ALA ALA ARG LEU GLY PRO ARG          
SEQRES  15 A  521  PHE PRO LEU GLY SER ASP SER THR LEU ILE ASN GLY LEU          
SEQRES  16 A  521  GLY ARG SER ALA THR THR ALA THR GLY ASP LEU ALA VAL          
SEQRES  17 A  521  ILE LYS VAL THR ARG GLY LYS ARG TYR ARG PHE ARG LEU          
SEQRES  18 A  521  VAL SER LEU SER CYS ASP PRO PHE TYR THR PHE SER ILE          
SEQRES  19 A  521  ASP GLY HIS ASN MET THR ILE ILE GLU ALA ASP ALA VAL          
SEQRES  20 A  521  ASN THR LYS PRO HIS THR VAL ASP SER LEU GLU ILE PHE          
SEQRES  21 A  521  ALA GLY GLN ARG TYR SER PHE ILE LEU ASN ALA ASN GLN          
SEQRES  22 A  521  PRO VAL ASP ASN TYR TRP VAL ARG ALA ASN PRO ASN PHE          
SEQRES  23 A  521  GLY ASN VAL GLY PHE THR ASN GLY ILE ASN SER ALA ILE          
SEQRES  24 A  521  LEU ARG TYR ASP GLY ALA ALA VAL ALA GLU PRO ALA THR          
SEQRES  25 A  521  ALA ILE PRO PRO ALA SER VAL THR PRO LEU LEU GLU THR          
SEQRES  26 A  521  ASP LEU HIS PRO LEU VAL SER THR PRO VAL PRO GLY SER          
SEQRES  27 A  521  PRO VAL ALA GLY GLY VAL ASP LYS ALA LEU ASN PHE VAL          
SEQRES  28 A  521  PHE ASN PHE ASP GLY THR ASN PHE PHE ILE ASN ASP ALA          
SEQRES  29 A  521  THR PHE THR PRO PRO SER VAL PRO VAL LEU LEU GLN ILE          
SEQRES  30 A  521  LEU SER GLY ALA GLN ALA ALA GLN ASP LEU LEU PRO SER          
SEQRES  31 A  521  GLY SER VAL ILE PRO LEU PRO ALA LEU SER THR ILE GLU          
SEQRES  32 A  521  LEU SER PHE PRO ALA THR ALA ASN ALA PRO GLY VAL PRO          
SEQRES  33 A  521  HIS PRO PHE HIS LEU HIS GLY HIS THR PHE ALA VAL VAL          
SEQRES  34 A  521  ARG SER ALA GLY SER THR ALA TYR ASN TYR GLU ASP PRO          
SEQRES  35 A  521  VAL TRP ARG ASP VAL VAL SER THR GLY THR PRO ALA ALA          
SEQRES  36 A  521  GLY ASP ASN VAL THR ILE ARG PHE VAL THR ASP ASN PRO          
SEQRES  37 A  521  GLY PRO TRP PHE LEU HIS CYS HIS ILE ASP PHE HIS LEU          
SEQRES  38 A  521  GLU ALA GLY PHE ALA VAL VAL PHE ALA GLU ASP LEU PRO          
SEQRES  39 A  521  GLY THR PRO ALA ALA ASN PRO VAL PRO GLN SER TRP SER          
SEQRES  40 A  521  ASP LEU CYS PRO ILE TYR ASP ALA LEU ALA GLU ASP ASP          
SEQRES  41 A  521  GLN                                                          
SEQRES   1 B  521  MET LYS ALA LEU SER PHE LEU THR PRO ILE VAL THR LEU          
SEQRES   2 B  521  ALA LEU VAL ALA GLY ALA PHE ALA SER VAL GLY PRO VAL          
SEQRES   3 B  521  ALA ASN LEU LYS ILE GLY ASN ALA ALA VAL SER PRO ASP          
SEQRES   4 B  521  GLY TYR THR ARG ASP ALA VAL VAL VAL ASN GLY ALA THR          
SEQRES   5 B  521  PRO GLY PRO LEU ILE VAL GLY ASN LYS GLY ASP ASN PHE          
SEQRES   6 B  521  ARG LEU ASN VAL ILE ASP GLU LEU THR ASN HIS THR MET          
SEQRES   7 B  521  LEU LYS SER THR SER ILE HIS TRP HIS GLY PHE PHE GLN          
SEQRES   8 B  521  HIS GLY THR ASN TRP ALA ASP GLY GLY ALA PHE VAL ASN          
SEQRES   9 B  521  GLN CYS PRO ILE SER SER GLY HIS SER PHE SER TYR ASN          
SEQRES  10 B  521  PHE GLN ALA LYS ASP GLN ALA GLY THR PHE TRP TYR HIS          
SEQRES  11 B  521  SER HIS LEU SER THR GLN TYR CYS ASP GLY LEU ARG GLY          
SEQRES  12 B  521  PRO PHE VAL VAL TYR ASP PRO LYS ASP PRO HIS LYS LYS          
SEQRES  13 B  521  LEU TYR ASP VAL ASP ASN GLU SER THR VAL ILE THR LEU          
SEQRES  14 B  521  GLU ASP TRP TYR HIS THR ALA ALA ARG LEU GLY PRO ARG          
SEQRES  15 B  521  PHE PRO LEU GLY SER ASP SER THR LEU ILE ASN GLY LEU          
SEQRES  16 B  521  GLY ARG SER ALA THR THR ALA THR GLY ASP LEU ALA VAL          
SEQRES  17 B  521  ILE LYS VAL THR ARG GLY LYS ARG TYR ARG PHE ARG LEU          
SEQRES  18 B  521  VAL SER LEU SER CYS ASP PRO PHE TYR THR PHE SER ILE          
SEQRES  19 B  521  ASP GLY HIS ASN MET THR ILE ILE GLU ALA ASP ALA VAL          
SEQRES  20 B  521  ASN THR LYS PRO HIS THR VAL ASP SER LEU GLU ILE PHE          
SEQRES  21 B  521  ALA GLY GLN ARG TYR SER PHE ILE LEU ASN ALA ASN GLN          
SEQRES  22 B  521  PRO VAL ASP ASN TYR TRP VAL ARG ALA ASN PRO ASN PHE          
SEQRES  23 B  521  GLY ASN VAL GLY PHE THR ASN GLY ILE ASN SER ALA ILE          
SEQRES  24 B  521  LEU ARG TYR ASP GLY ALA ALA VAL ALA GLU PRO ALA THR          
SEQRES  25 B  521  ALA ILE PRO PRO ALA SER VAL THR PRO LEU LEU GLU THR          
SEQRES  26 B  521  ASP LEU HIS PRO LEU VAL SER THR PRO VAL PRO GLY SER          
SEQRES  27 B  521  PRO VAL ALA GLY GLY VAL ASP LYS ALA LEU ASN PHE VAL          
SEQRES  28 B  521  PHE ASN PHE ASP GLY THR ASN PHE PHE ILE ASN ASP ALA          
SEQRES  29 B  521  THR PHE THR PRO PRO SER VAL PRO VAL LEU LEU GLN ILE          
SEQRES  30 B  521  LEU SER GLY ALA GLN ALA ALA GLN ASP LEU LEU PRO SER          
SEQRES  31 B  521  GLY SER VAL ILE PRO LEU PRO ALA LEU SER THR ILE GLU          
SEQRES  32 B  521  LEU SER PHE PRO ALA THR ALA ASN ALA PRO GLY VAL PRO          
SEQRES  33 B  521  HIS PRO PHE HIS LEU HIS GLY HIS THR PHE ALA VAL VAL          
SEQRES  34 B  521  ARG SER ALA GLY SER THR ALA TYR ASN TYR GLU ASP PRO          
SEQRES  35 B  521  VAL TRP ARG ASP VAL VAL SER THR GLY THR PRO ALA ALA          
SEQRES  36 B  521  GLY ASP ASN VAL THR ILE ARG PHE VAL THR ASP ASN PRO          
SEQRES  37 B  521  GLY PRO TRP PHE LEU HIS CYS HIS ILE ASP PHE HIS LEU          
SEQRES  38 B  521  GLU ALA GLY PHE ALA VAL VAL PHE ALA GLU ASP LEU PRO          
SEQRES  39 B  521  GLY THR PRO ALA ALA ASN PRO VAL PRO GLN SER TRP SER          
SEQRES  40 B  521  ASP LEU CYS PRO ILE TYR ASP ALA LEU ALA GLU ASP ASP          
SEQRES  41 B  521  GLN                                                          
MODRES 3X1B ASN A   75  ASN  GLYCOSYLATION SITE                                 
MODRES 3X1B ASN B  238  ASN  GLYCOSYLATION SITE                                 
MODRES 3X1B ASN A  238  ASN  GLYCOSYLATION SITE                                 
MODRES 3X1B ASN B  458  ASN  GLYCOSYLATION SITE                                 
MODRES 3X1B ASN B   75  ASN  GLYCOSYLATION SITE                                 
MODRES 3X1B ASN A  458  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    BMA  A 603      11                                                       
HET    MAN  A 604      11                                                       
HET    MAN  A 605      11                                                       
HET    MAN  A 606      11                                                       
HET    NAG  A 607      14                                                       
HET    NAG  A 608      14                                                       
HET    BMA  A 609      11                                                       
HET    MAN  A 610      11                                                       
HET    MAN  A 611      11                                                       
HET    MAN  A 612      11                                                       
HET    NAG  A 613      14                                                       
HET     CU  A 614       1                                                       
HET     CU  A 615       1                                                       
HET     CU  A 616       1                                                       
HET     CU  A 617       1                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    BMA  B 603      11                                                       
HET    MAN  B 604      11                                                       
HET    MAN  B 605      11                                                       
HET    MAN  B 606      11                                                       
HET    NAG  B 607      14                                                       
HET    NAG  B 608      14                                                       
HET    BMA  B 609      11                                                       
HET    MAN  B 610      11                                                       
HET    MAN  B 611      11                                                       
HET    MAN  B 612      11                                                       
HET    MAN  B 613      11                                                       
HET    NAG  B 614      14                                                       
HET     CU  B 615       1                                                       
HET     CU  B 616       1                                                       
HET     CU  B 617       1                                                       
HET     CU  B 618       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CU COPPER (II) ION                                                  
FORMUL   3  NAG    10(C8 H15 N O6)                                              
FORMUL   3  BMA    4(C6 H12 O6)                                                 
FORMUL   3  MAN    13(C6 H12 O6)                                                
FORMUL   6   CU    8(CU 2+)                                                     
FORMUL  17  HOH   *1116(H2 O)                                                   
HELIX    1   1 ASN A   75  LEU A   79  5                                   5    
HELIX    2   2 THR A   94  ASP A   98  5                                   5    
HELIX    3   3 THR A  135  GLY A  140  5                                   6    
HELIX    4   4 HIS A  154  TYR A  158  5                                   5    
HELIX    5   5 ASN A  162  SER A  164  5                                   3    
HELIX    6   6 PHE A  291  ILE A  295  5                                   5    
HELIX    7   7 LEU A  323  LEU A  327  5                                   5    
HELIX    8   8 PRO A  372  SER A  379  1                                   8    
HELIX    9   9 THR A  452  GLY A  456  5                                   5    
HELIX   10  10 ILE A  477  ALA A  483  1                                   7    
HELIX   11  11 GLY A  495  ASN A  500  1                                   6    
HELIX   12  12 PRO A  503  ALA A  515  1                                  13    
HELIX   13  13 ALA A  517  GLN A  521  5                                   5    
HELIX   14  14 ASN B   75  LEU B   79  5                                   5    
HELIX   15  15 THR B   94  ASP B   98  5                                   5    
HELIX   16  16 THR B  135  GLY B  140  5                                   6    
HELIX   17  17 HIS B  154  TYR B  158  5                                   5    
HELIX   18  18 ASN B  162  SER B  164  5                                   3    
HELIX   19  19 PHE B  291  ILE B  295  5                                   5    
HELIX   20  20 LEU B  323  LEU B  327  5                                   5    
HELIX   21  21 PRO B  372  SER B  379  1                                   8    
HELIX   22  22 ALA B  383  LEU B  387  5                                   5    
HELIX   23  23 THR B  452  GLY B  456  5                                   5    
HELIX   24  24 ILE B  477  ALA B  483  1                                   7    
HELIX   25  25 GLY B  495  ASN B  500  1                                   6    
HELIX   26  26 PRO B  503  ALA B  515  1                                  13    
HELIX   27  27 ALA B  517  GLN B  521  5                                   5    
SHEET    1   A 4 ARG A  43  VAL A  48  0                                        
SHEET    2   A 4 VAL A  26  VAL A  36 -1  N  GLY A  32   O  VAL A  47           
SHEET    3   A 4 ASN A  64  ASP A  71  1  O  ILE A  70   N  ILE A  31           
SHEET    4   A 4 HIS A 112  GLN A 119 -1  O  PHE A 118   N  PHE A  65           
SHEET    1   B 4 ILE A  57  ASN A  60  0                                        
SHEET    2   B 4 ARG A 142  TYR A 148  1  O  TYR A 148   N  GLY A  59           
SHEET    3   B 4 GLY A 125  SER A 131 -1  N  PHE A 127   O  PHE A 145           
SHEET    4   B 4 ILE A  84  HIS A  87 -1  N  HIS A  85   O  HIS A 130           
SHEET    1   C 6 SER A 189  ILE A 192  0                                        
SHEET    2   C 6 VAL A 166  TRP A 172 -1  N  GLU A 170   O  LEU A 191           
SHEET    3   C 6 ARG A 216  SER A 223  1  O  ARG A 220   N  ILE A 167           
SHEET    4   C 6 ARG A 264  ASN A 270 -1  O  TYR A 265   N  LEU A 221           
SHEET    5   C 6 MET A 239  ALA A 244 -1  N  THR A 240   O  ILE A 268           
SHEET    6   C 6 VAL A 247  VAL A 254 -1  O  VAL A 254   N  MET A 239           
SHEET    1   D 5 VAL A 208  VAL A 211  0                                        
SHEET    2   D 5 SER A 297  TYR A 302  1  O  ILE A 299   N  ILE A 209           
SHEET    3   D 5 ASN A 277  PRO A 284 -1  N  TYR A 278   O  LEU A 300           
SHEET    4   D 5 TYR A 230  ILE A 234 -1  N  SER A 233   O  ARG A 281           
SHEET    5   D 5 LEU A 257  ILE A 259 -1  O  LEU A 257   N  PHE A 232           
SHEET    1   E 2 GLY A 287  VAL A 289  0                                        
SHEET    2   E 2 GLY B 287  VAL B 289 -1  O  GLY B 287   N  VAL A 289           
SHEET    1   F 5 LYS A 346  ASN A 349  0                                        
SHEET    2   F 5 THR A 401  PRO A 407  1  O  GLU A 403   N  LEU A 348           
SHEET    3   F 5 ASN A 458  VAL A 464 -1  O  PHE A 463   N  ILE A 402           
SHEET    4   F 5 PHE A 426  ARG A 430 -1  N  ALA A 427   O  ARG A 462           
SHEET    5   F 5 TRP A 444  ARG A 445 -1  O  ARG A 445   N  PHE A 426           
SHEET    1   G 2 PHE A 352  PHE A 354  0                                        
SHEET    2   G 2 PHE A 359  ILE A 361 -1  O  PHE A 360   N  ASN A 353           
SHEET    1   H 5 VAL A 393  LEU A 396  0                                        
SHEET    2   H 5 ALA A 486  GLU A 491  1  O  VAL A 488   N  ILE A 394           
SHEET    3   H 5 GLY A 469  CYS A 475 -1  N  TRP A 471   O  PHE A 489           
SHEET    4   H 5 PRO A 418  LEU A 421 -1  N  HIS A 420   O  HIS A 474           
SHEET    5   H 5 VAL A 447  SER A 449 -1  O  VAL A 448   N  PHE A 419           
SHEET    1   I 4 ARG B  43  VAL B  48  0                                        
SHEET    2   I 4 VAL B  26  VAL B  36 -1  N  GLY B  32   O  VAL B  47           
SHEET    3   I 4 ASN B  64  ASP B  71  1  O  ILE B  70   N  ILE B  31           
SHEET    4   I 4 SER B 113  GLN B 119 -1  O  PHE B 118   N  PHE B  65           
SHEET    1   J 4 ILE B  57  ASN B  60  0                                        
SHEET    2   J 4 ARG B 142  TYR B 148  1  O  TYR B 148   N  GLY B  59           
SHEET    3   J 4 GLY B 125  SER B 131 -1  N  PHE B 127   O  PHE B 145           
SHEET    4   J 4 ILE B  84  HIS B  87 -1  N  HIS B  85   O  HIS B 130           
SHEET    1   K 6 SER B 189  ILE B 192  0                                        
SHEET    2   K 6 VAL B 166  TRP B 172 -1  N  GLU B 170   O  LEU B 191           
SHEET    3   K 6 ARG B 216  SER B 223  1  O  ARG B 220   N  ILE B 167           
SHEET    4   K 6 ARG B 264  ASN B 270 -1  O  TYR B 265   N  LEU B 221           
SHEET    5   K 6 MET B 239  ALA B 244 -1  N  THR B 240   O  ILE B 268           
SHEET    6   K 6 VAL B 247  VAL B 254 -1  O  VAL B 254   N  MET B 239           
SHEET    1   L 5 VAL B 208  VAL B 211  0                                        
SHEET    2   L 5 SER B 297  TYR B 302  1  O  ILE B 299   N  ILE B 209           
SHEET    3   L 5 ASN B 277  PRO B 284 -1  N  TYR B 278   O  LEU B 300           
SHEET    4   L 5 TYR B 230  ILE B 234 -1  N  SER B 233   O  ARG B 281           
SHEET    5   L 5 LEU B 257  ILE B 259 -1  O  LEU B 257   N  PHE B 232           
SHEET    1   M 5 LYS B 346  ASN B 349  0                                        
SHEET    2   M 5 THR B 401  PRO B 407  1  O  GLU B 403   N  LEU B 348           
SHEET    3   M 5 ASN B 458  VAL B 464 -1  O  PHE B 463   N  ILE B 402           
SHEET    4   M 5 PHE B 426  ARG B 430 -1  N  ALA B 427   O  ARG B 462           
SHEET    5   M 5 TRP B 444  ARG B 445 -1  O  ARG B 445   N  PHE B 426           
SHEET    1   N 2 PHE B 352  PHE B 354  0                                        
SHEET    2   N 2 PHE B 359  ILE B 361 -1  O  PHE B 360   N  ASN B 353           
SHEET    1   O 5 VAL B 393  LEU B 396  0                                        
SHEET    2   O 5 ALA B 486  GLU B 491  1  O  VAL B 488   N  ILE B 394           
SHEET    3   O 5 GLY B 469  CYS B 475 -1  N  TRP B 471   O  PHE B 489           
SHEET    4   O 5 PRO B 418  LEU B 421 -1  N  HIS B 420   O  HIS B 474           
SHEET    5   O 5 VAL B 447  SER B 449 -1  O  VAL B 448   N  PHE B 419           
SSBOND   1 CYS A  106    CYS A  510                          1555   1555  2.07  
SSBOND   2 CYS A  138    CYS A  226                          1555   1555  2.02  
SSBOND   3 CYS B  106    CYS B  510                          1555   1555  2.09  
SSBOND   4 CYS B  138    CYS B  226                          1555   1555  2.04  
LINK         O6  BMA B 609                 C1  MAN B 610     1555   1555  1.37  
LINK         O6  BMA A 603                 C1  MAN A 604     1555   1555  1.42  
LINK         O6  BMA A 609                 C1  MAN A 610     1555   1555  1.42  
LINK         O6  BMA B 603                 C1  MAN B 604     1555   1555  1.42  
LINK         O4  NAG A 602                 C1  BMA A 603     1555   1555  1.43  
LINK         O4  NAG B 608                 C1  BMA B 609     1555   1555  1.43  
LINK         O4  NAG A 601                 C1  NAG A 602     1555   1555  1.43  
LINK         O4  NAG A 608                 C1  BMA A 609     1555   1555  1.43  
LINK         O3  BMA B 609                 C1  MAN B 613     1555   1555  1.43  
LINK         O3  BMA B 603                 C1  MAN B 606     1555   1555  1.43  
LINK         O4  NAG B 602                 C1  BMA B 603     1555   1555  1.43  
LINK         O4  NAG B 601                 C1  NAG B 602     1555   1555  1.43  
LINK         ND2 ASN A  75                 C1  NAG A 601     1555   1555  1.44  
LINK         O6  MAN A 610                 C1  MAN A 612     1555   1555  1.44  
LINK         O4  NAG B 607                 C1  NAG B 608     1555   1555  1.44  
LINK         ND2 ASN B 238                 C1  NAG B 614     1555   1555  1.44  
LINK         ND2 ASN A 238                 C1  NAG A 613     1555   1555  1.44  
LINK         O6  MAN A 604                 C1  MAN A 606     1555   1555  1.44  
LINK         ND2 ASN B 458                 C1  NAG B 607     1555   1555  1.44  
LINK         ND2 ASN B  75                 C1  NAG B 601     1555   1555  1.44  
LINK         O3  MAN A 604                 C1  MAN A 605     1555   1555  1.44  
LINK         ND2 ASN A 458                 C1  NAG A 607     1555   1555  1.44  
LINK         O4  NAG A 607                 C1  NAG A 608     1555   1555  1.44  
LINK         O3  MAN B 604                 C1  MAN B 605     1555   1555  1.45  
LINK         O6  MAN B 610                 C1  MAN B 612     1555   1555  1.45  
LINK         O3  MAN B 610                 C1  MAN B 611     1555   1555  1.45  
LINK         O3  MAN A 610                 C1  MAN A 611     1555   1555  1.45  
LINK         NE2 HIS A 420                CU    CU A 614     1555   1555  1.98  
LINK         NE2 HIS A  85                CU    CU A 614     1555   1555  1.98  
LINK         NE2 HIS B 420                CU    CU B 615     1555   1555  1.98  
LINK         NE2 HIS B  85                CU    CU B 615     1555   1555  1.99  
LINK         NE2 HIS A 474                CU    CU A 616     1555   1555  1.99  
LINK         ND1 HIS B  87                CU    CU B 616     1555   1555  2.00  
LINK         ND1 HIS A  87                CU    CU A 615     1555   1555  2.00  
LINK         NE2 HIS B 422                CU    CU B 617     1555   1555  2.00  
LINK         NE2 HIS B 474                CU    CU B 617     1555   1555  2.00  
LINK         NE2 HIS A 422                CU    CU A 616     1555   1555  2.00  
LINK         NE2 HIS B 132                CU    CU B 617     1555   1555  2.00  
LINK         NE2 HIS B 130                CU    CU B 616     1555   1555  2.00  
LINK         ND1 HIS B 480                CU    CU B 618     1555   1555  2.00  
LINK         NE2 HIS A 130                CU    CU A 615     1555   1555  2.00  
LINK         ND1 HIS A 417                CU    CU A 617     1555   1555  2.01  
LINK         ND1 HIS A 480                CU    CU A 617     1555   1555  2.01  
LINK         ND1 HIS B 417                CU    CU B 618     1555   1555  2.01  
LINK         NE2 HIS A 132                CU    CU A 616     1555   1555  2.01  
LINK         NE2 HIS B 476                CU    CU B 616     1555   1555  2.02  
LINK         NE2 HIS A 476                CU    CU A 615     1555   1555  2.03  
LINK         SG  CYS A 475                CU    CU A 617     1555   1555  2.27  
LINK         SG  CYS B 475                CU    CU B 618     1555   1555  2.28  
LINK        CU    CU B 617                 O   HOH B 718     1555   1555  2.43  
LINK        CU    CU A 616                 O   HOH A 713     1555   1555  2.46  
LINK        CU    CU A 615                 O   HOH A 713     1555   1555  2.59  
LINK        CU    CU B 616                 O   HOH B 718     1555   1555  2.61  
CISPEP   1 GLY A   24    PRO A   25          0         8.15                     
CISPEP   2 THR A   52    PRO A   53          0        -4.42                     
CISPEP   3 LEU A  388    PRO A  389          0         3.15                     
CISPEP   4 VAL A  415    PRO A  416          0        -4.33                     
CISPEP   5 GLY B   24    PRO B   25          0         3.07                     
CISPEP   6 THR B   52    PRO B   53          0        -6.46                     
CISPEP   7 LEU B  388    PRO B  389          0         3.00                     
CISPEP   8 VAL B  415    PRO B  416          0        -1.92                     
SITE     1 AC1  5 HIS A  85  HIS A  87  HIS A 420  HIS A 422                    
SITE     2 AC1  5 HOH A 746                                                     
SITE     1 AC2  5 HIS A  87  TRP A 128  HIS A 130  HIS A 476                    
SITE     2 AC2  5 HOH A 713                                                     
SITE     1 AC3  4 HIS A 132  HIS A 422  HIS A 474  HOH A 713                    
SITE     1 AC4  3 HIS A 417  CYS A 475  HIS A 480                               
SITE     1 AC5  5 HIS B  85  HIS B  87  HIS B 420  HIS B 422                    
SITE     2 AC5  5 HOH B 704                                                     
SITE     1 AC6  5 HIS B  87  TRP B 128  HIS B 130  HIS B 476                    
SITE     2 AC6  5 HOH B 718                                                     
SITE     1 AC7  4 HIS B 132  HIS B 422  HIS B 474  HOH B 718                    
SITE     1 AC8  4 HIS B 417  CYS B 475  ILE B 477  HIS B 480                    
SITE     1 AC9 39 TYR A  41  ARG A  43  ASP A  44  ASN A  75                    
SITE     2 AC9 39 MET A  78  HIS A 174  THR A 175  ALA A 176                    
SITE     3 AC9 39 LEU A 179  THR A 201  GLY A 214  LYS A 215                    
SITE     4 AC9 39 HOH A 707  HOH A 737  HOH A 815  HOH A 845                    
SITE     5 AC9 39 HOH A 882  HOH A 894  HOH A 911  HOH A1010                    
SITE     6 AC9 39 HOH A1011  HOH A1058  HOH A1078  HOH A1087                    
SITE     7 AC9 39 HOH A1110  HOH A1112  HOH A1116  HOH A1119                    
SITE     8 AC9 39 HOH A1120  HOH A1128  HOH A1166  HOH A1189                    
SITE     9 AC9 39 HOH A1222  HOH A1241  HOH A1243  HOH A1244                    
SITE    10 AC9 39 ALA B 202  ASN B 293  HOH B1124                               
SITE     1 BC1  1 ASN A 238                                                     
SITE     1 BC2 21 GLY A 342  VAL A 344  ASP A 345  LYS A 346                    
SITE     2 BC2 21 ALA A 347  ASN A 349  SER A 405  ASN A 458                    
SITE     3 BC2 21 HOH A 778  HOH A 859  HOH A 901  HOH A 975                    
SITE     4 BC2 21 HOH A1138  HOH A1142  HOH A1145  HOH A1154                    
SITE     5 BC2 21 HOH A1159  HOH A1168  HOH A1265  HOH A1286                    
SITE     6 BC2 21 HOH A1287                                                     
SITE     1 BC3 17 TYR B  41  ARG B  43  ASP B  44  ASN B  75                    
SITE     2 BC3 17 MET B  78  HIS B 174  THR B 175  ALA B 176                    
SITE     3 BC3 17 LEU B 179  HOH B1084  HOH B1085  HOH B1086                    
SITE     4 BC3 17 HOH B1100  HOH B1108  HOH B1118  HOH B1132                    
SITE     5 BC3 17 HOH B1193                                                     
SITE     1 BC4  3 GLY B 236  ASN B 238  HOH B 919                               
SITE     1 BC5 17 GLY B 342  VAL B 344  LYS B 346  ALA B 347                    
SITE     2 BC5 17 LEU B 348  ASN B 349  SER B 405  ASN B 458                    
SITE     3 BC5 17 HOH B 829  HOH B 872  HOH B 948  HOH B 987                    
SITE     4 BC5 17 HOH B 997  HOH B1056  HOH B1147  HOH B1151                    
SITE     5 BC5 17 HOH B1164                                                     
CRYST1   99.266  188.676   65.414  90.00  90.00  90.00 P 21 21 2     8          
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      0.010074  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005300  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015287        0.00000                         
ATOM      1  N   SER A  22      98.204  31.354  68.089  1.00 25.14           N  
ANISOU    1  N   SER A  22     1355   2761   5435    308   -319    449       N  
ATOM      2  CA  SER A  22      97.598  30.632  66.925  1.00 25.46           C  
ANISOU    2  CA  SER A  22     1285   2814   5572    346   -355    403       C  
ATOM      3  C   SER A  22      97.568  29.128  67.172  1.00 25.16           C  
ANISOU    3  C   SER A  22     1263   2771   5523    366   -327    403       C  
ATOM      4  O   SER A  22      98.267  28.620  68.055  1.00 25.79           O  
ANISOU    4  O   SER A  22     1396   2762   5639    289   -402    367       O  
ATOM      5  CB  SER A  22      98.402  30.909  65.657  1.00 25.40           C  
ANISOU    5  CB  SER A  22     1300   2826   5522    461   -356    437       C  
ATOM      6  OG  SER A  22      99.763  30.517  65.843  1.00 28.40           O  
ANISOU    6  OG  SER A  22     1490   3458   5840    304   -415    436       O  
ATOM      7  N   VAL A  23      96.778  28.416  66.373  1.00 25.19           N  
ANISOU    7  N   VAL A  23     1284   2789   5495    361   -266    374       N  
ATOM      8  CA  VAL A  23      96.679  26.957  66.462  1.00 24.76           C  
ANISOU    8  CA  VAL A  23     1279   2699   5430    476   -176    391       C  
ATOM      9  C   VAL A  23      96.759  26.360  65.060  1.00 25.12           C  
ANISOU    9  C   VAL A  23     1377   2688   5479    534   -166    370       C  
ATOM     10  O   VAL A  23      96.612  27.075  64.064  1.00 24.48           O  
ANISOU   10  O   VAL A  23     1274   2564   5460    692   -310    390       O  
ATOM     11  CB  VAL A  23      95.357  26.495  67.141  1.00 25.09           C  
ANISOU   11  CB  VAL A  23     1302   2819   5409    424   -175    381       C  
ATOM     12  CG1 VAL A  23      95.208  27.138  68.528  1.00 27.07           C  
ANISOU   12  CG1 VAL A  23     1864   2970   5450    355    -49    365       C  
ATOM     13  CG2 VAL A  23      94.129  26.812  66.267  1.00 23.25           C  
ANISOU   13  CG2 VAL A  23      788   2634   5410    411     33    534       C  
ATOM     14  N   GLY A  24      97.002  25.053  64.990  1.00 25.24           N  
ANISOU   14  N   GLY A  24     1383   2715   5489    589   -126    388       N  
ATOM     15  CA  GLY A  24      96.985  24.345  63.718  1.00 25.31           C  
ANISOU   15  CA  GLY A  24     1352   2674   5587    617    -77    272       C  
ATOM     16  C   GLY A  24      98.399  24.029  63.264  1.00 25.94           C  
ANISOU   16  C   GLY A  24     1367   2868   5620    499    -60    260       C  
ATOM     17  O   GLY A  24      99.378  24.588  63.803  1.00 26.17           O  
ANISOU   17  O   GLY A  24     1398   2852   5693    407    -34    360       O  
ATOM     18  N   PRO A  25      98.516  23.163  62.241  1.00 26.02           N  
ANISOU   18  N   PRO A  25     1383   2798   5703    514    -33    152       N  
ATOM     19  CA  PRO A  25      97.430  22.619  61.410  1.00 25.63           C  
ANISOU   19  CA  PRO A  25     1281   2770   5685    533     -9    124       C  
ATOM     20  C   PRO A  25      96.629  21.466  62.037  1.00 25.85           C  
ANISOU   20  C   PRO A  25     1382   2750   5687    561     17    108       C  
ATOM     21  O   PRO A  25      95.576  21.090  61.513  1.00 26.41           O  
ANISOU   21  O   PRO A  25     1444   2767   5821    517    105     37       O  
ATOM     22  CB  PRO A  25      98.179  22.118  60.173  1.00 25.80           C  
ANISOU   22  CB  PRO A  25     1330   2819   5652    506    -40     97       C  
ATOM     23  CG  PRO A  25      99.526  21.678  60.736  1.00 26.60           C  
ANISOU   23  CG  PRO A  25     1476   2885   5744    542    -81     69       C  
ATOM     24  CD  PRO A  25      99.838  22.831  61.671  1.00 26.26           C  
ANISOU   24  CD  PRO A  25     1351   2916   5710    503    -92    146       C  
ATOM     25  N   VAL A  26      97.109  20.913  63.148  1.00 25.73           N  
ANISOU   25  N   VAL A  26     1438   2597   5741    608     77    154       N  
ATOM     26  CA  VAL A  26      96.336  19.948  63.927  1.00 25.49           C  
ANISOU   26  CA  VAL A  26     1471   2602   5612    591     98    199       C  
ATOM     27  C   VAL A  26      95.949  20.640  65.223  1.00 25.59           C  
ANISOU   27  C   VAL A  26     1413   2729   5580    497     62    244       C  
ATOM     28  O   VAL A  26      96.830  21.059  65.986  1.00 25.88           O  
ANISOU   28  O   VAL A  26     1358   2930   5545    512      6    223       O  
ATOM     29  CB  VAL A  26      97.191  18.713  64.260  1.00 26.06           C  
ANISOU   29  CB  VAL A  26     1645   2573   5681    524     96    217       C  
ATOM     30  CG1 VAL A  26      96.421  17.758  65.178  1.00 26.17           C  
ANISOU   30  CG1 VAL A  26     1614   2682   5644    566    149    329       C  
ATOM     31  CG2 VAL A  26      97.608  18.033  62.966  1.00 25.94           C  
ANISOU   31  CG2 VAL A  26     1603   2587   5667    691    199    193       C  
ATOM     32  N   ALA A  27      94.649  20.760  65.474  1.00 24.46           N  
ANISOU   32  N   ALA A  27     1259   2586   5447    505     12    286       N  
ATOM     33  CA  ALA A  27      94.185  21.492  66.643  1.00 24.20           C  
ANISOU   33  CA  ALA A  27     1247   2585   5362    407     58    311       C  
ATOM     34  C   ALA A  27      92.766  21.096  67.044  1.00 23.88           C  
ANISOU   34  C   ALA A  27     1192   2610   5271    325    -54    328       C  
ATOM     35  O   ALA A  27      91.981  20.641  66.217  1.00 23.88           O  
ANISOU   35  O   ALA A  27     1186   2659   5226    349    -21    350       O  
ATOM     36  CB  ALA A  27      94.206  23.001  66.360  1.00 24.37           C  
ANISOU   36  CB  ALA A  27     1327   2540   5389    379    100    289       C  
ATOM     37  N   ASN A  28      92.464  21.320  68.319  1.00 23.48           N  
ANISOU   37  N   ASN A  28     1184   2589   5145    337   -158    362       N  
ATOM     38  CA  ASN A  28      91.112  21.326  68.845  1.00 23.24           C  
ANISOU   38  CA  ASN A  28     1236   2531   5061    417   -247    410       C  
ATOM     39  C   ASN A  28      90.537  22.736  68.813  1.00 22.97           C  
ANISOU   39  C   ASN A  28     1259   2463   5003    364   -280    376       C  
ATOM     40  O   ASN A  28      91.219  23.704  69.169  1.00 23.81           O  
ANISOU   40  O   ASN A  28     1485   2476   5083    480   -352    317       O  
ATOM     41  CB  ASN A  28      91.106  20.824  70.287  1.00 23.94           C  
ANISOU   41  CB  ASN A  28     1363   2610   5120    416   -295    368       C  
ATOM     42  CG  ASN A  28      91.429  19.356  70.388  1.00 25.19           C  
ANISOU   42  CG  ASN A  28     1633   2737   5198    510   -428    421       C  
ATOM     43  OD1 ASN A  28      91.172  18.578  69.465  1.00 25.95           O  
ANISOU   43  OD1 ASN A  28     1667   2968   5224    464   -454    337       O  
ATOM     44  ND2 ASN A  28      92.000  18.962  71.517  1.00 29.76           N  
ANISOU   44  ND2 ASN A  28     2928   3161   5218    363   -766    344       N  
ATOM     45  N   LEU A  29      89.301  22.844  68.343  1.00 22.21           N  
ANISOU   45  N   LEU A  29     1163   2417   4858    358   -301    410       N  
ATOM     46  CA  LEU A  29      88.549  24.100  68.363  1.00 21.17           C  
ANISOU   46  CA  LEU A  29     1088   2302   4653    301   -326    378       C  
ATOM     47  C   LEU A  29      87.283  23.921  69.193  1.00 21.19           C  
ANISOU   47  C   LEU A  29     1077   2396   4576    368   -409    359       C  
ATOM     48  O   LEU A  29      86.302  23.351  68.713  1.00 21.61           O  
ANISOU   48  O   LEU A  29     1028   2455   4726    175   -263    252       O  
ATOM     49  CB  LEU A  29      88.208  24.558  66.942  1.00 21.04           C  
ANISOU   49  CB  LEU A  29      887   2467   4639    220   -342    385       C  
ATOM     50  CG  LEU A  29      89.409  24.747  66.001  1.00 21.96           C  
ANISOU   50  CG  LEU A  29     1386   2421   4535    123   -322    490       C  
ATOM     51  CD1 LEU A  29      88.924  24.850  64.565  1.00 22.44           C  
ANISOU   51  CD1 LEU A  29     1570   2398   4557     14   -579    753       C  
ATOM     52  CD2 LEU A  29      90.293  25.946  66.386  1.00 22.63           C  
ANISOU   52  CD2 LEU A  29     1471   2566   4559    146   -495    585       C  
ATOM     53  N   LYS A  30      87.313  24.407  70.433  1.00 21.29           N  
ANISOU   53  N   LYS A  30     1190   2367   4530    475   -406    367       N  
ATOM     54  CA  LYS A  30      86.184  24.278  71.347  1.00 21.09           C  
ANISOU   54  CA  LYS A  30     1200   2464   4347    483   -461    327       C  
ATOM     55  C   LYS A  30      85.215  25.418  71.057  1.00 20.75           C  
ANISOU   55  C   LYS A  30     1215   2335   4332    401   -427    253       C  
ATOM     56  O   LYS A  30      85.578  26.597  71.132  1.00 21.10           O  
ANISOU   56  O   LYS A  30     1154   2387   4476    348   -356    193       O  
ATOM     57  CB  LYS A  30      86.637  24.334  72.808  1.00 21.78           C  
ANISOU   57  CB  LYS A  30     1488   2474   4314    616   -534    337       C  
ATOM     58  CG  LYS A  30      87.381  23.077  73.265  1.00 24.66           C  
ANISOU   58  CG  LYS A  30     2030   3087   4253    778   -661    490       C  
ATOM     59  CD  LYS A  30      88.071  23.233  74.611  1.00 32.15           C  
ANISOU   59  CD  LYS A  30     3529   4376   4310    783   -782    872       C  
ATOM     60  CE  LYS A  30      87.123  22.982  75.766  1.00 35.18           C  
ANISOU   60  CE  LYS A  30     4004   4930   4433    634   -865   1199       C  
ATOM     61  NZ  LYS A  30      87.866  22.260  76.855  1.00 39.29           N  
ANISOU   61  NZ  LYS A  30     4798   5092   5038    978  -1142   1528       N  
ATOM     62  N   ILE A  31      83.986  25.057  70.695  1.00 20.02           N  
ANISOU   62  N   ILE A  31     1137   2196   4273    270   -299    180       N  
ATOM     63  CA  ILE A  31      82.969  26.035  70.341  1.00 19.69           C  
ANISOU   63  CA  ILE A  31     1122   2204   4154    233   -305    185       C  
ATOM     64  C   ILE A  31      82.044  26.151  71.539  1.00 19.71           C  
ANISOU   64  C   ILE A  31     1250   2217   4021    192   -264    183       C  
ATOM     65  O   ILE A  31      81.418  25.168  71.912  1.00 20.77           O  
ANISOU   65  O   ILE A  31     1469   2235   4184     21   -268    161       O  
ATOM     66  CB  ILE A  31      82.157  25.577  69.107  1.00 19.37           C  
ANISOU   66  CB  ILE A  31     1110   2164   4086    330   -310    158       C  
ATOM     67  CG1 ILE A  31      83.105  25.191  67.962  1.00 19.52           C  
ANISOU   67  CG1 ILE A  31     1071   1991   4352     27   -115    126       C  
ATOM     68  CG2 ILE A  31      81.155  26.674  68.704  1.00 19.68           C  
ANISOU   68  CG2 ILE A  31     1081   2049   4348    364   -249     79       C  
ATOM     69  CD1 ILE A  31      84.066  26.316  67.521  1.00 18.26           C  
ANISOU   69  CD1 ILE A  31      933   1902   4100    147    215    184       C  
ATOM     70  N   GLY A  32      81.992  27.322  72.165  1.00 20.01           N  
ANISOU   70  N   GLY A  32     1376   2217   4007    216   -137    246       N  
ATOM     71  CA  GLY A  32      81.194  27.516  73.377  1.00 19.16           C  
ANISOU   71  CA  GLY A  32     1285   2167   3827    291   -131    132       C  
ATOM     72  C   GLY A  32      80.477  28.850  73.431  1.00 19.17           C  
ANISOU   72  C   GLY A  32     1324   2232   3726    250   -102    110       C  
ATOM     73  O   GLY A  32      80.643  29.718  72.567  1.00 18.68           O  
ANISOU   73  O   GLY A  32     1297   2228   3571    318    -45     73       O  
ATOM     74  N   ASN A  33      79.652  29.013  74.457  1.00 19.01           N  
ANISOU   74  N   ASN A  33     1255   2312   3655    285   -113    136       N  
ATOM     75  CA  ASN A  33      79.029  30.308  74.681  1.00 19.27           C  
ANISOU   75  CA  ASN A  33     1360   2275   3686    205   -166    105       C  
ATOM     76  C   ASN A  33      79.776  31.043  75.769  1.00 19.66           C  
ANISOU   76  C   ASN A  33     1348   2370   3752    163   -256    140       C  
ATOM     77  O   ASN A  33      80.203  30.419  76.740  1.00 19.96           O  
ANISOU   77  O   ASN A  33     1461   2393   3727    178   -329    225       O  
ATOM     78  CB  ASN A  33      77.568  30.161  75.098  1.00 18.65           C  
ANISOU   78  CB  ASN A  33     1204   2289   3592     99   -147    155       C  
ATOM     79  CG  ASN A  33      76.723  29.539  74.015  1.00 19.75           C  
ANISOU   79  CG  ASN A  33     1399   2402   3700     11    -88    239       C  
ATOM     80  OD1 ASN A  33      76.185  28.454  74.203  1.00 19.86           O  
ANISOU   80  OD1 ASN A  33     1668   2298   3578     22    239    759       O  
ATOM     81  ND2 ASN A  33      76.621  30.208  72.864  1.00 18.55           N  
ANISOU   81  ND2 ASN A  33     1032   2542   3474    -60   -181    200       N  
ATOM     82  N   ALA A  34      79.913  32.357  75.610  1.00 20.19           N  
ANISOU   82  N   ALA A  34     1494   2371   3803    156   -253     95       N  
ATOM     83  CA  ALA A  34      80.572  33.193  76.610  1.00 20.45           C  
ANISOU   83  CA  ALA A  34     1594   2355   3818     64   -296      3       C  
ATOM     84  C   ALA A  34      80.050  34.616  76.520  1.00 21.11           C  
ANISOU   84  C   ALA A  34     1731   2432   3857     18   -261     43       C  
ATOM     85  O   ALA A  34      79.674  35.067  75.436  1.00 21.12           O  
ANISOU   85  O   ALA A  34     1804   2341   3878    -13   -223    120       O  
ATOM     86  CB  ALA A  34      82.093  33.191  76.415  1.00 21.22           C  
ANISOU   86  CB  ALA A  34     1702   2505   3856     35   -279    -50       C  
ATOM     87  N   ALA A  35      80.052  35.319  77.649  1.00 21.17           N  
ANISOU   87  N   ALA A  35     1812   2438   3794    -25   -184     36       N  
ATOM     88  CA  ALA A  35      79.828  36.763  77.649  1.00 21.38           C  
ANISOU   88  CA  ALA A  35     1915   2399   3807   -192    -90    149       C  
ATOM     89  C   ALA A  35      81.114  37.461  77.207  1.00 21.52           C  
ANISOU   89  C   ALA A  35     1843   2519   3813   -174    -93    165       C  
ATOM     90  O   ALA A  35      82.203  37.163  77.716  1.00 21.33           O  
ANISOU   90  O   ALA A  35     1742   2512   3848   -305   -151    293       O  
ATOM     91  CB  ALA A  35      79.431  37.244  79.032  1.00 22.55           C  
ANISOU   91  CB  ALA A  35     2218   2455   3893   -215    -83    134       C  
ATOM     92  N   VAL A  36      80.985  38.367  76.242  1.00 20.24           N  
ANISOU   92  N   VAL A  36     1698   2343   3647   -182    -87     84       N  
ATOM     93  CA  VAL A  36      82.137  39.073  75.684  1.00 20.41           C  
ANISOU   93  CA  VAL A  36     1809   2425   3518   -138    -97     64       C  
ATOM     94  C   VAL A  36      81.859  40.573  75.620  1.00 20.49           C  
ANISOU   94  C   VAL A  36     1753   2459   3572   -220    -87    -33       C  
ATOM     95  O   VAL A  36      80.703  40.993  75.661  1.00 19.20           O  
ANISOU   95  O   VAL A  36     1615   2312   3367    -91   -123    -97       O  
ATOM     96  CB  VAL A  36      82.512  38.539  74.285  1.00 19.88           C  
ANISOU   96  CB  VAL A  36     1778   2363   3410   -130   -121     48       C  
ATOM     97  CG1 VAL A  36      82.861  37.063  74.357  1.00 20.96           C  
ANISOU   97  CG1 VAL A  36     2156   2558   3248    123   -290    197       C  
ATOM     98  CG2 VAL A  36      81.376  38.749  73.280  1.00 20.86           C  
ANISOU   98  CG2 VAL A  36     1841   2407   3676   -174   -190    112       C  
ATOM     99  N   SER A  37      82.904  41.387  75.522  1.00 20.65           N  
ANISOU   99  N   SER A  37     1598   2666   3581   -303   -129    -34       N  
ATOM    100  CA  SER A  37      82.667  42.829  75.395  1.00 21.68           C  
ANISOU  100  CA  SER A  37     1666   2812   3756   -359    -74   -131       C  
ATOM    101  C   SER A  37      83.656  43.494  74.436  1.00 20.40           C  
ANISOU  101  C   SER A  37     1346   2687   3715   -371    -46    -92       C  
ATOM    102  O   SER A  37      84.467  44.323  74.862  1.00 21.07           O  
ANISOU  102  O   SER A  37     1334   2743   3926   -363   -145    -58       O  
ATOM    103  CB  SER A  37      82.644  43.509  76.766  1.00 22.96           C  
ANISOU  103  CB  SER A  37     1758   3092   3872   -354   -172    -97       C  
ATOM    104  OG  SER A  37      83.915  43.388  77.348  1.00 27.20           O  
ANISOU  104  OG  SER A  37     2334   3662   4337   -437   -162   -337       O  
ATOM    105  N   PRO A  38      83.602  43.126  73.140  1.00 19.63           N  
ANISOU  105  N   PRO A  38     1144   2673   3641   -413     25    -78       N  
ATOM    106  CA  PRO A  38      84.652  43.616  72.225  1.00 19.10           C  
ANISOU  106  CA  PRO A  38     1151   2580   3524   -448    104    -63       C  
ATOM    107  C   PRO A  38      84.599  45.122  71.958  1.00 18.69           C  
ANISOU  107  C   PRO A  38     1117   2565   3419   -412    121    -82       C  
ATOM    108  O   PRO A  38      85.615  45.737  71.603  1.00 17.78           O  
ANISOU  108  O   PRO A  38     1047   2383   3323   -309    148   -147       O  
ATOM    109  CB  PRO A  38      84.368  42.855  70.930  1.00 18.48           C  
ANISOU  109  CB  PRO A  38      976   2598   3447   -361      4   -119       C  
ATOM    110  CG  PRO A  38      82.872  42.532  71.002  1.00 18.86           C  
ANISOU  110  CG  PRO A  38      989   2573   3603   -568    145   -156       C  
ATOM    111  CD  PRO A  38      82.655  42.218  72.457  1.00 19.30           C  
ANISOU  111  CD  PRO A  38     1145   2646   3541   -484     47    -88       C  
ATOM    112  N   ASP A  39      83.412  45.705  72.110  1.00 18.32           N  
ANISOU  112  N   ASP A  39     1123   2548   3288   -424     96      1       N  
ATOM    113  CA  ASP A  39      83.267  47.144  71.965  1.00 18.64           C  
ANISOU  113  CA  ASP A  39     1229   2562   3288   -524     68     -8       C  
ATOM    114  C   ASP A  39      82.853  47.802  73.270  1.00 19.72           C  
ANISOU  114  C   ASP A  39     1444   2639   3407   -623     12    -34       C  
ATOM    115  O   ASP A  39      82.231  48.874  73.263  1.00 19.42           O  
ANISOU  115  O   ASP A  39     1372   2649   3357   -511    -42    -80       O  
ATOM    116  CB  ASP A  39      82.254  47.466  70.863  1.00 17.78           C  
ANISOU  116  CB  ASP A  39      851   2647   3255   -434     36     30       C  
ATOM    117  CG  ASP A  39      80.895  46.854  71.137  1.00 17.53           C  
ANISOU  117  CG  ASP A  39     1263   2251   3144   -510    -94    -65       C  
ATOM    118  OD1 ASP A  39      80.689  46.263  72.217  1.00 16.73           O  
ANISOU  118  OD1 ASP A  39      919   2357   3077    -12     12     40       O  
ATOM    119  OD2 ASP A  39      80.017  46.990  70.268  1.00 17.28           O  
ANISOU  119  OD2 ASP A  39     1656   2330   2580   -408   -321   -187       O  
ATOM    120  N   GLY A  40      83.199  47.141  74.374  1.00 20.77           N  
ANISOU  120  N   GLY A  40     1625   2730   3534   -646    -42    -30       N  
ATOM    121  CA  GLY A  40      82.905  47.637  75.708  1.00 21.54           C  
ANISOU  121  CA  GLY A  40     1809   2805   3569   -679    151    -49       C  
ATOM    122  C   GLY A  40      81.474  47.461  76.189  1.00 22.44           C  
ANISOU  122  C   GLY A  40     1916   2956   3651   -539    100    -44       C  
ATOM    123  O   GLY A  40      81.123  47.994  77.245  1.00 23.79           O  
ANISOU  123  O   GLY A  40     2129   3259   3650   -594    172    -36       O  
ATOM    124  N   TYR A  41      80.649  46.760  75.411  1.00 21.76           N  
ANISOU  124  N   TYR A  41     1861   2796   3608   -594    106    -18       N  
ATOM    125  CA  TYR A  41      79.295  46.375  75.812  1.00 21.39           C  
ANISOU  125  CA  TYR A  41     1884   2777   3464   -539    124     77       C  
ATOM    126  C   TYR A  41      79.297  44.848  75.934  1.00 21.09           C  
ANISOU  126  C   TYR A  41     1964   2729   3319   -516     78     77       C  
ATOM    127  O   TYR A  41      79.700  44.155  75.008  1.00 20.16           O  
ANISOU  127  O   TYR A  41     2002   2662   2993   -515     36    168       O  
ATOM    128  CB  TYR A  41      78.254  46.801  74.764  1.00 21.67           C  
ANISOU  128  CB  TYR A  41     1852   2769   3611   -528    244     62       C  
ATOM    129  CG  TYR A  41      76.849  46.291  75.059  1.00 23.73           C  
ANISOU  129  CG  TYR A  41     1893   3073   4049   -408    291    -29       C  
ATOM    130  CD1 TYR A  41      76.107  46.827  76.109  1.00 26.98           C  
ANISOU  130  CD1 TYR A  41     2262   3511   4475   -457    605   -169       C  
ATOM    131  CD2 TYR A  41      76.276  45.254  74.310  1.00 23.05           C  
ANISOU  131  CD2 TYR A  41     1765   2847   4145   -341    354    -53       C  
ATOM    132  CE1 TYR A  41      74.823  46.359  76.403  1.00 27.27           C  
ANISOU  132  CE1 TYR A  41     1935   3581   4845   -514    807   -420       C  
ATOM    133  CE2 TYR A  41      75.001  44.782  74.591  1.00 24.97           C  
ANISOU  133  CE2 TYR A  41     2224   2824   4440   -559    683   -191       C  
ATOM    134  CZ  TYR A  41      74.281  45.343  75.635  1.00 27.15           C  
ANISOU  134  CZ  TYR A  41     2031   3398   4884   -596    854   -232       C  
ATOM    135  OH  TYR A  41      73.025  44.875  75.922  1.00 29.62           O  
ANISOU  135  OH  TYR A  41     2381   3641   5232   -865   1021   -112       O  
ATOM    136  N   THR A  42      78.841  44.327  77.070  1.00 20.79           N  
ANISOU  136  N   THR A  42     2067   2672   3160   -488    -69    123       N  
ATOM    137  CA  THR A  42      78.800  42.887  77.318  1.00 20.27           C  
ANISOU  137  CA  THR A  42     1955   2571   3173   -415   -194     34       C  
ATOM    138  C   THR A  42      77.562  42.212  76.712  1.00 20.00           C  
ANISOU  138  C   THR A  42     1909   2438   3250   -407    -86     38       C  
ATOM    139  O   THR A  42      76.411  42.588  76.984  1.00 19.76           O  
ANISOU  139  O   THR A  42     1728   2410   3369   -340    -87     -6       O  
ATOM    140  CB  THR A  42      78.881  42.638  78.839  1.00 20.91           C  
ANISOU  140  CB  THR A  42     2105   2606   3231   -464   -182     65       C  
ATOM    141  OG1 THR A  42      80.120  43.186  79.312  1.00 22.84           O  
ANISOU  141  OG1 THR A  42     2231   3228   3219   -284   -469    -45       O  
ATOM    142  CG2 THR A  42      78.821  41.148  79.201  1.00 22.39           C  
ANISOU  142  CG2 THR A  42     2476   2606   3423   -329   -244     10       C  
ATOM    143  N   ARG A  43      77.804  41.215  75.869  1.00 19.05           N  
ANISOU  143  N   ARG A  43     1737   2256   3241   -375    -85    -10       N  
ATOM    144  CA  ARG A  43      76.708  40.370  75.389  1.00 18.29           C  
ANISOU  144  CA  ARG A  43     1531   2223   3192   -275   -130     21       C  
ATOM    145  C   ARG A  43      77.156  38.911  75.269  1.00 18.47           C  
ANISOU  145  C   ARG A  43     1532   2207   3278   -313    -59     10       C  
ATOM    146  O   ARG A  43      78.353  38.608  75.170  1.00 17.41           O  
ANISOU  146  O   ARG A  43     1357   2044   3211   -289     19     67       O  
ATOM    147  CB  ARG A  43      76.178  40.892  74.051  1.00 18.48           C  
ANISOU  147  CB  ARG A  43     1604   2232   3184   -260    -90     42       C  
ATOM    148  CG  ARG A  43      77.218  40.869  72.924  1.00 17.04           C  
ANISOU  148  CG  ARG A  43     1172   2261   3040    -82   -278     50       C  
ATOM    149  CD  ARG A  43      76.513  40.718  71.575  1.00 17.96           C  
ANISOU  149  CD  ARG A  43     1403   2218   3201   -203   -500   -227       C  
ATOM    150  NE  ARG A  43      76.117  39.337  71.308  1.00 15.08           N  
ANISOU  150  NE  ARG A  43      473   2107   3148   -178   -290    -49       N  
ATOM    151  CZ  ARG A  43      75.657  38.899  70.137  1.00 15.39           C  
ANISOU  151  CZ  ARG A  43     1089   2068   2689    -58    139    -55       C  
ATOM    152  NH1 ARG A  43      75.506  39.737  69.120  1.00 17.17           N  
ANISOU  152  NH1 ARG A  43     1102   1881   3539      4    274    190       N  
ATOM    153  NH2 ARG A  43      75.316  37.621  69.989  1.00 14.32           N  
ANISOU  153  NH2 ARG A  43     1130   2006   2305    -48    157    198       N  
ATOM    154  N   ASP A  44      76.188  38.002  75.292  1.00 18.83           N  
ANISOU  154  N   ASP A  44     1469   2292   3393   -293     45     64       N  
ATOM    155  CA  ASP A  44      76.469  36.585  75.083  1.00 19.30           C  
ANISOU  155  CA  ASP A  44     1504   2339   3489   -207    191    -34       C  
ATOM    156  C   ASP A  44      76.791  36.320  73.622  1.00 19.24           C  
ANISOU  156  C   ASP A  44     1493   2300   3518   -172    220   -104       C  
ATOM    157  O   ASP A  44      76.124  36.852  72.731  1.00 19.48           O  
ANISOU  157  O   ASP A  44     1548   2243   3608    -75    315   -112       O  
ATOM    158  CB  ASP A  44      75.267  35.744  75.524  1.00 19.99           C  
ANISOU  158  CB  ASP A  44     1472   2517   3604   -195    181     48       C  
ATOM    159  CG  ASP A  44      74.993  35.923  76.996  1.00 22.67           C  
ANISOU  159  CG  ASP A  44     1813   3007   3793   -186    218    119       C  
ATOM    160  OD1 ASP A  44      75.935  35.669  77.775  1.00 24.03           O  
ANISOU  160  OD1 ASP A  44     1934   3326   3866   -160    145    155       O  
ATOM    161  OD2 ASP A  44      73.892  36.389  77.371  1.00 27.17           O  
ANISOU  161  OD2 ASP A  44     2270   3758   4293   -154    388    102       O  
ATOM    162  N   ALA A  45      77.785  35.468  73.389  1.00 17.70           N  
ANISOU  162  N   ALA A  45     1212   2070   3441   -176    274   -216       N  
ATOM    163  CA  ALA A  45      78.230  35.199  72.031  1.00 18.01           C  
ANISOU  163  CA  ALA A  45     1373   2079   3388   -128    298   -196       C  
ATOM    164  C   ALA A  45      78.605  33.728  71.846  1.00 18.49           C  
ANISOU  164  C   ALA A  45     1373   2192   3459    -47    267   -158       C  
ATOM    165  O   ALA A  45      78.555  32.942  72.797  1.00 19.11           O  
ANISOU  165  O   ALA A  45     1710   2184   3364     18    233   -194       O  
ATOM    166  CB  ALA A  45      79.422  36.088  71.691  1.00 17.33           C  
ANISOU  166  CB  ALA A  45     1272   1904   3410   -163    311   -266       C  
ATOM    167  N   VAL A  46      78.914  33.356  70.604  1.00 17.57           N  
ANISOU  167  N   VAL A  46      991   2273   3411    -25    238   -155       N  
ATOM    168  CA  VAL A  46      79.504  32.063  70.291  1.00 17.43           C  
ANISOU  168  CA  VAL A  46      698   2281   3643      6     68    -59       C  
ATOM    169  C   VAL A  46      81.006  32.325  70.121  1.00 18.26           C  
ANISOU  169  C   VAL A  46      631   2442   3864      8     38    114       C  
ATOM    170  O   VAL A  46      81.408  33.186  69.326  1.00 18.16           O  
ANISOU  170  O   VAL A  46      412   2522   3964     13    -29    267       O  
ATOM    171  CB  VAL A  46      78.905  31.494  68.990  1.00 17.44           C  
ANISOU  171  CB  VAL A  46      732   2257   3635     77    178   -199       C  
ATOM    172  CG1 VAL A  46      79.602  30.171  68.593  1.00 18.93           C  
ANISOU  172  CG1 VAL A  46     1151   2262   3777    274    122    -81       C  
ATOM    173  CG2 VAL A  46      77.385  31.309  69.146  1.00 16.98           C  
ANISOU  173  CG2 VAL A  46      766   2043   3640   -389    -17   -281       C  
ATOM    174  N   VAL A  47      81.838  31.595  70.862  1.00 18.27           N  
ANISOU  174  N   VAL A  47      536   2459   3945     48    -33    140       N  
ATOM    175  CA  VAL A  47      83.289  31.833  70.837  1.00 18.50           C  
ANISOU  175  CA  VAL A  47      573   2421   4036    110   -105     26       C  
ATOM    176  C   VAL A  47      84.045  30.556  70.472  1.00 18.66           C  
ANISOU  176  C   VAL A  47      593   2466   4030     84   -144     38       C  
ATOM    177  O   VAL A  47      83.502  29.456  70.546  1.00 18.99           O  
ANISOU  177  O   VAL A  47      527   2513   4174    214     -4    195       O  
ATOM    178  CB  VAL A  47      83.795  32.367  72.201  1.00 19.10           C  
ANISOU  178  CB  VAL A  47      748   2395   4111    162   -153     29       C  
ATOM    179  CG1 VAL A  47      83.127  33.719  72.566  1.00 20.06           C  
ANISOU  179  CG1 VAL A  47     1018   2335   4269    132   -109   -137       C  
ATOM    180  CG2 VAL A  47      83.537  31.340  73.305  1.00 19.41           C  
ANISOU  180  CG2 VAL A  47      844   2437   4091   -129     39     68       C  
ATOM    181  N   VAL A  48      85.308  30.708  70.088  1.00 18.51           N  
ANISOU  181  N   VAL A  48      596   2443   3992    150   -128     42       N  
ATOM    182  CA  VAL A  48      86.154  29.611  69.667  1.00 19.01           C  
ANISOU  182  CA  VAL A  48      700   2407   4114    165   -269     43       C  
ATOM    183  C   VAL A  48      87.383  29.648  70.561  1.00 19.89           C  
ANISOU  183  C   VAL A  48      873   2562   4120    174   -346     88       C  
ATOM    184  O   VAL A  48      88.105  30.660  70.575  1.00 19.36           O  
ANISOU  184  O   VAL A  48      761   2427   4167    157   -424     82       O  
ATOM    185  CB  VAL A  48      86.587  29.828  68.191  1.00 18.84           C  
ANISOU  185  CB  VAL A  48      756   2372   4030    262   -343      3       C  
ATOM    186  CG1 VAL A  48      87.493  28.686  67.707  1.00 18.48           C  
ANISOU  186  CG1 VAL A  48      514   2208   4297    263   -166     30       C  
ATOM    187  CG2 VAL A  48      85.327  29.971  67.327  1.00 19.44           C  
ANISOU  187  CG2 VAL A  48      553   2531   4302    182   -362     53       C  
ATOM    188  N   ASN A  49      87.626  28.558  71.293  1.00 20.55           N  
ANISOU  188  N   ASN A  49      899   2681   4225    242   -372     88       N  
ATOM    189  CA  ASN A  49      88.688  28.547  72.305  1.00 21.43           C  
ANISOU  189  CA  ASN A  49     1132   2784   4226    223   -373     39       C  
ATOM    190  C   ASN A  49      88.633  29.777  73.212  1.00 21.97           C  
ANISOU  190  C   ASN A  49     1245   2862   4239    181   -390     54       C  
ATOM    191  O   ASN A  49      89.661  30.403  73.507  1.00 21.88           O  
ANISOU  191  O   ASN A  49     1155   2910   4247    221   -339    -33       O  
ATOM    192  CB  ASN A  49      90.065  28.373  71.643  1.00 21.63           C  
ANISOU  192  CB  ASN A  49     1143   2793   4281    216   -309     98       C  
ATOM    193  CG  ASN A  49      90.221  27.002  71.012  1.00 21.48           C  
ANISOU  193  CG  ASN A  49     1107   2858   4193    144   -327     87       C  
ATOM    194  OD1 ASN A  49      89.398  26.121  71.253  1.00 21.91           O  
ANISOU  194  OD1 ASN A  49     1455   2697   4170     91   -356    305       O  
ATOM    195  ND2 ASN A  49      91.274  26.802  70.220  1.00 22.47           N  
ANISOU  195  ND2 ASN A  49     1180   2919   4440    286   -137     68       N  
ATOM    196  N   GLY A  50      87.411  30.131  73.608  1.00 21.42           N  
ANISOU  196  N   GLY A  50     1281   2796   4061    165   -313    112       N  
ATOM    197  CA  GLY A  50      87.177  31.211  74.556  1.00 21.65           C  
ANISOU  197  CA  GLY A  50     1520   2569   4137     66   -426    218       C  
ATOM    198  C   GLY A  50      87.138  32.606  73.955  1.00 22.20           C  
ANISOU  198  C   GLY A  50     1717   2649   4066     21   -353    237       C  
ATOM    199  O   GLY A  50      86.875  33.561  74.690  1.00 23.22           O  
ANISOU  199  O   GLY A  50     2122   2537   4160    -68   -536    177       O  
ATOM    200  N   ALA A  51      87.351  32.742  72.645  1.00 21.04           N  
ANISOU  200  N   ALA A  51     1511   2554   3927   -147   -323    276       N  
ATOM    201  CA  ALA A  51      87.462  34.073  72.044  1.00 20.42           C  
ANISOU  201  CA  ALA A  51     1317   2665   3774   -168   -247    315       C  
ATOM    202  C   ALA A  51      86.585  34.290  70.824  1.00 19.42           C  
ANISOU  202  C   ALA A  51     1083   2540   3755   -183   -176    286       C  
ATOM    203  O   ALA A  51      86.345  33.361  70.055  1.00 18.43           O  
ANISOU  203  O   ALA A  51     1051   2486   3463   -233   -207    260       O  
ATOM    204  CB  ALA A  51      88.928  34.339  71.644  1.00 20.55           C  
ANISOU  204  CB  ALA A  51     1273   2678   3857   -281   -234    447       C  
ATOM    205  N   THR A  52      86.136  35.530  70.643  1.00 18.27           N  
ANISOU  205  N   THR A  52      807   2493   3642   -213   -113    254       N  
ATOM    206  CA  THR A  52      85.638  35.964  69.357  1.00 18.21           C  
ANISOU  206  CA  THR A  52      887   2477   3554   -139    -50    234       C  
ATOM    207  C   THR A  52      86.233  37.338  69.042  1.00 18.19           C  
ANISOU  207  C   THR A  52      994   2503   3413   -192    -28    126       C  
ATOM    208  O   THR A  52      86.239  38.223  69.895  1.00 18.56           O  
ANISOU  208  O   THR A  52     1125   2545   3381   -228   -123     74       O  
ATOM    209  CB  THR A  52      84.076  35.997  69.310  1.00 18.41           C  
ANISOU  209  CB  THR A  52      816   2548   3629    -47    -86    165       C  
ATOM    210  OG1 THR A  52      83.652  36.355  67.995  1.00 18.32           O  
ANISOU  210  OG1 THR A  52      598   2494   3866    -19    -26    101       O  
ATOM    211  CG2 THR A  52      83.520  37.023  70.282  1.00 19.12           C  
ANISOU  211  CG2 THR A  52     1092   2556   3616    224    -33    269       C  
ATOM    212  N   PRO A  53      86.745  37.525  67.819  1.00 17.81           N  
ANISOU  212  N   PRO A  53     1065   2412   3288   -193     42    179       N  
ATOM    213  CA  PRO A  53      86.863  36.498  66.795  1.00 18.15           C  
ANISOU  213  CA  PRO A  53     1159   2418   3318    -62     21    183       C  
ATOM    214  C   PRO A  53      87.778  35.369  67.266  1.00 18.05           C  
ANISOU  214  C   PRO A  53     1016   2271   3570     11    -85    123       C  
ATOM    215  O   PRO A  53      88.545  35.535  68.241  1.00 17.59           O  
ANISOU  215  O   PRO A  53      812   2156   3715    131    -83     21       O  
ATOM    216  CB  PRO A  53      87.534  37.228  65.625  1.00 18.19           C  
ANISOU  216  CB  PRO A  53     1246   2441   3224   -243     99    263       C  
ATOM    217  CG  PRO A  53      88.154  38.421  66.179  1.00 18.41           C  
ANISOU  217  CG  PRO A  53     1213   2688   3093   -194    222    199       C  
ATOM    218  CD  PRO A  53      87.458  38.765  67.463  1.00 19.22           C  
ANISOU  218  CD  PRO A  53     1400   2613   3289   -143    133    211       C  
ATOM    219  N   GLY A  54      87.676  34.230  66.588  1.00 17.48           N  
ANISOU  219  N   GLY A  54      786   2256   3597    175    -55      8       N  
ATOM    220  CA  GLY A  54      88.388  33.022  67.008  1.00 18.07           C  
ANISOU  220  CA  GLY A  54      729   2185   3949    144    -48    -55       C  
ATOM    221  C   GLY A  54      89.875  33.149  66.739  1.00 18.78           C  
ANISOU  221  C   GLY A  54      714   2167   4252    154    -79    -43       C  
ATOM    222  O   GLY A  54      90.309  34.074  66.050  1.00 18.74           O  
ANISOU  222  O   GLY A  54      663   2172   4286    170    -40   -207       O  
ATOM    223  N   PRO A  55      90.671  32.213  67.275  1.00 19.20           N  
ANISOU  223  N   PRO A  55      608   2180   4507    160   -113     -3       N  
ATOM    224  CA  PRO A  55      92.108  32.251  67.090  1.00 19.71           C  
ANISOU  224  CA  PRO A  55      639   2207   4641     87    -26     30       C  
ATOM    225  C   PRO A  55      92.492  32.092  65.619  1.00 19.69           C  
ANISOU  225  C   PRO A  55      594   2197   4687     11    -70     59       C  
ATOM    226  O   PRO A  55      91.755  31.489  64.842  1.00 20.42           O  
ANISOU  226  O   PRO A  55      523   2516   4719    -53    -95     94       O  
ATOM    227  CB  PRO A  55      92.594  31.047  67.913  1.00 19.35           C  
ANISOU  227  CB  PRO A  55      598   2213   4538    110    -41     17       C  
ATOM    228  CG  PRO A  55      91.419  30.091  67.856  1.00 19.80           C  
ANISOU  228  CG  PRO A  55      516   2243   4762    236     46     53       C  
ATOM    229  CD  PRO A  55      90.236  31.010  68.004  1.00 19.03           C  
ANISOU  229  CD  PRO A  55      463   2169   4599    168    -71     53       C  
ATOM    230  N   LEU A  56      93.642  32.648  65.258  1.00 20.48           N  
ANISOU  230  N   LEU A  56      597   2254   4928    -47    -33     60       N  
ATOM    231  CA  LEU A  56      94.281  32.407  63.977  1.00 20.37           C  
ANISOU  231  CA  LEU A  56      534   2191   5012    -76     -3    -12       C  
ATOM    232  C   LEU A  56      94.620  30.918  63.839  1.00 21.25           C  
ANISOU  232  C   LEU A  56      663   2287   5120      7     30    -19       C  
ATOM    233  O   LEU A  56      95.313  30.352  64.680  1.00 21.44           O  
ANISOU  233  O   LEU A  56      806   2223   5113    -52    -37    -80       O  
ATOM    234  CB  LEU A  56      95.560  33.257  63.871  1.00 20.78           C  
ANISOU  234  CB  LEU A  56      511   2339   5044   -149     73    115       C  
ATOM    235  CG  LEU A  56      96.405  33.023  62.607  1.00 20.99           C  
ANISOU  235  CG  LEU A  56      412   2395   5166    -87     -8     94       C  
ATOM    236  CD1 LEU A  56      95.580  33.392  61.350  1.00 21.19           C  
ANISOU  236  CD1 LEU A  56      290   2781   4978    102    108    185       C  
ATOM    237  CD2 LEU A  56      97.717  33.824  62.680  1.00 20.33           C  
ANISOU  237  CD2 LEU A  56      293   2587   4842   -141     -5     60       C  
ATOM    238  N   ILE A  57      94.128  30.282  62.780  1.00 20.40           N  
ANISOU  238  N   ILE A  57      503   2093   5156    -52     51   -158       N  
ATOM    239  CA  ILE A  57      94.565  28.934  62.426  1.00 21.07           C  
ANISOU  239  CA  ILE A  57      580   2224   5200    205    177    -82       C  
ATOM    240  C   ILE A  57      95.674  29.043  61.394  1.00 21.62           C  
ANISOU  240  C   ILE A  57      650   2273   5292    277    169    -94       C  
ATOM    241  O   ILE A  57      95.561  29.829  60.450  1.00 22.31           O  
ANISOU  241  O   ILE A  57      705   2344   5425    511    272    -51       O  
ATOM    242  CB  ILE A  57      93.397  28.116  61.836  1.00 21.19           C  
ANISOU  242  CB  ILE A  57      680   2160   5211    135    236   -179       C  
ATOM    243  CG1 ILE A  57      92.258  28.044  62.860  1.00 21.59           C  
ANISOU  243  CG1 ILE A  57      586   2323   5293     24    226    -52       C  
ATOM    244  CG2 ILE A  57      93.877  26.724  61.383  1.00 22.39           C  
ANISOU  244  CG2 ILE A  57     1045   2363   5098    479    202   -184       C  
ATOM    245  CD1 ILE A  57      91.011  27.333  62.359  1.00 21.48           C  
ANISOU  245  CD1 ILE A  57      299   2599   5261    152    145     44       C  
ATOM    246  N   VAL A  58      96.745  28.273  61.580  1.00 21.94           N  
ANISOU  246  N   VAL A  58      777   2197   5361    420    239   -106       N  
ATOM    247  CA  VAL A  58      97.898  28.340  60.681  1.00 22.54           C  
ANISOU  247  CA  VAL A  58      789   2407   5365    374    260     24       C  
ATOM    248  C   VAL A  58      98.338  26.974  60.155  1.00 23.54           C  
ANISOU  248  C   VAL A  58      904   2480   5561    441    302     53       C  
ATOM    249  O   VAL A  58      98.052  25.927  60.744  1.00 24.02           O  
ANISOU  249  O   VAL A  58     1146   2391   5588    385    318     89       O  
ATOM    250  CB  VAL A  58      99.112  29.042  61.340  1.00 23.19           C  
ANISOU  250  CB  VAL A  58     1005   2491   5312    438    168     87       C  
ATOM    251  CG1 VAL A  58      98.784  30.493  61.648  1.00 21.86           C  
ANISOU  251  CG1 VAL A  58      650   2747   4906    308    141    -52       C  
ATOM    252  CG2 VAL A  58      99.583  28.279  62.585  1.00 24.07           C  
ANISOU  252  CG2 VAL A  58      823   2958   5363    462     35    131       C  
ATOM    253  N   GLY A  59      99.013  26.996  59.011  1.00 23.74           N  
ANISOU  253  N   GLY A  59      939   2473   5606    538    348     -6       N  
ATOM    254  CA  GLY A  59      99.726  25.832  58.491  1.00 24.85           C  
ANISOU  254  CA  GLY A  59      970   2621   5850    574    324     -3       C  
ATOM    255  C   GLY A  59     100.536  26.332  57.317  1.00 25.09           C  
ANISOU  255  C   GLY A  59      975   2683   5872    662    368    -20       C  
ATOM    256  O   GLY A  59     100.544  27.539  57.046  1.00 24.72           O  
ANISOU  256  O   GLY A  59      882   2646   5861    782    361    -13       O  
ATOM    257  N   ASN A  60     101.241  25.418  56.653  1.00 25.71           N  
ANISOU  257  N   ASN A  60     1014   2744   6011    695    369    -17       N  
ATOM    258  CA  ASN A  60     102.006  25.729  55.446  1.00 26.03           C  
ANISOU  258  CA  ASN A  60     1059   2785   6046    695    366     57       C  
ATOM    259  C   ASN A  60     101.386  25.103  54.209  1.00 25.84           C  
ANISOU  259  C   ASN A  60     1007   2758   6052    749    347     71       C  
ATOM    260  O   ASN A  60     100.621  24.142  54.302  1.00 26.02           O  
ANISOU  260  O   ASN A  60     1130   2666   6090    696    364    103       O  
ATOM    261  CB  ASN A  60     103.438  25.192  55.546  1.00 25.35           C  
ANISOU  261  CB  ASN A  60      942   2715   5972    799    242     36       C  
ATOM    262  CG  ASN A  60     104.209  25.773  56.712  1.00 27.23           C  
ANISOU  262  CG  ASN A  60     1420   3036   5887    751    183     61       C  
ATOM    263  OD1 ASN A  60     104.909  25.050  57.425  1.00 30.65           O  
ANISOU  263  OD1 ASN A  60     2086   3853   5705    742     25    173       O  
ATOM    264  ND2 ASN A  60     104.115  27.076  56.895  1.00 25.08           N  
ANISOU  264  ND2 ASN A  60     1318   2978   5232    535    110   -102       N  
ATOM    265  N   LYS A  61     101.732  25.650  53.049  1.00 26.29           N  
ANISOU  265  N   LYS A  61     1040   2831   6116    697    482     45       N  
ATOM    266  CA  LYS A  61     101.251  25.124  51.778  1.00 27.44           C  
ANISOU  266  CA  LYS A  61     1339   2886   6197    610    521     29       C  
ATOM    267  C   LYS A  61     101.434  23.605  51.736  1.00 27.79           C  
ANISOU  267  C   LYS A  61     1405   2851   6300    579    483     55       C  
ATOM    268  O   LYS A  61     102.507  23.082  52.054  1.00 27.98           O  
ANISOU  268  O   LYS A  61     1512   2769   6347    611    511    -97       O  
ATOM    269  CB  LYS A  61     101.993  25.808  50.619  1.00 28.06           C  
ANISOU  269  CB  LYS A  61     1457   2999   6205    600    591    108       C  
ATOM    270  CG  LYS A  61     101.521  25.387  49.238  1.00 28.77           C  
ANISOU  270  CG  LYS A  61     1643   3211   6075    518    728     30       C  
ATOM    271  CD  LYS A  61     102.422  25.961  48.154  1.00 33.05           C  
ANISOU  271  CD  LYS A  61     2655   3673   6230    362    833    134       C  
ATOM    272  CE  LYS A  61     101.736  25.833  46.801  1.00 35.36           C  
ANISOU  272  CE  LYS A  61     3230   4026   6178    487    955    101       C  
ATOM    273  NZ  LYS A  61     102.668  26.193  45.702  1.00 38.28           N  
ANISOU  273  NZ  LYS A  61     3478   4476   6591    411   1202    192       N  
ATOM    274  N   GLY A  62     100.360  22.904  51.384  1.00 28.38           N  
ANISOU  274  N   GLY A  62     1570   2828   6384    557    352     35       N  
ATOM    275  CA  GLY A  62     100.362  21.447  51.280  1.00 29.01           C  
ANISOU  275  CA  GLY A  62     1699   2859   6462    495    372     42       C  
ATOM    276  C   GLY A  62     100.088  20.662  52.552  1.00 28.98           C  
ANISOU  276  C   GLY A  62     1706   2843   6460    474    365     35       C  
ATOM    277  O   GLY A  62      99.958  19.429  52.500  1.00 28.92           O  
ANISOU  277  O   GLY A  62     1700   2890   6397    436    425     26       O  
ATOM    278  N   ASP A  63     100.029  21.351  53.691  1.00 28.36           N  
ANISOU  278  N   ASP A  63     1600   2699   6476    495    368    -11       N  
ATOM    279  CA  ASP A  63      99.815  20.670  54.969  1.00 28.72           C  
ANISOU  279  CA  ASP A  63     1726   2684   6501    540    223     -5       C  
ATOM    280  C   ASP A  63      98.454  19.963  55.030  1.00 28.50           C  
ANISOU  280  C   ASP A  63     1675   2640   6513    593    196    -11       C  
ATOM    281  O   ASP A  63      97.468  20.404  54.421  1.00 28.24           O  
ANISOU  281  O   ASP A  63     1681   2613   6433    515     99      1       O  
ATOM    282  CB  ASP A  63      99.911  21.640  56.153  1.00 28.61           C  
ANISOU  282  CB  ASP A  63     1736   2568   6563    544    220    -45       C  
ATOM    283  CG  ASP A  63     101.341  21.922  56.599  1.00 28.95           C  
ANISOU  283  CG  ASP A  63     1800   2606   6594    628    213    -12       C  
ATOM    284  OD1 ASP A  63     102.310  21.347  56.044  1.00 29.43           O  
ANISOU  284  OD1 ASP A  63     1787   2660   6733    623    199    -68       O  
ATOM    285  OD2 ASP A  63     101.490  22.751  57.529  1.00 27.83           O  
ANISOU  285  OD2 ASP A  63     1674   2319   6578    605    167     37       O  
ATOM    286  N   ASN A  64      98.416  18.861  55.778  1.00 28.43           N  
ANISOU  286  N   ASN A  64     1712   2616   6474    652    151      0       N  
ATOM    287  CA  ASN A  64      97.158  18.219  56.126  1.00 28.29           C  
ANISOU  287  CA  ASN A  64     1632   2692   6425    800    256    -18       C  
ATOM    288  C   ASN A  64      96.686  18.823  57.435  1.00 28.21           C  
ANISOU  288  C   ASN A  64     1622   2746   6351    779    180     71       C  
ATOM    289  O   ASN A  64      97.446  18.882  58.405  1.00 28.69           O  
ANISOU  289  O   ASN A  64     1521   2980   6399    948    190    105       O  
ATOM    290  CB  ASN A  64      97.309  16.709  56.269  1.00 29.51           C  
ANISOU  290  CB  ASN A  64     1880   2802   6528    763    245    -63       C  
ATOM    291  CG  ASN A  64      97.715  16.045  54.968  1.00 31.28           C  
ANISOU  291  CG  ASN A  64     2216   3017   6650    842    327   -240       C  
ATOM    292  OD1 ASN A  64      98.766  15.406  54.891  1.00 36.57           O  
ANISOU  292  OD1 ASN A  64     3082   3690   7122   1159    266   -531       O  
ATOM    293  ND2 ASN A  64      96.905  16.219  53.932  1.00 29.78           N  
ANISOU  293  ND2 ASN A  64     2084   2850   6378    568    339   -563       N  
ATOM    294  N   PHE A  65      95.456  19.328  57.411  1.00 26.46           N  
ANISOU  294  N   PHE A  65     1331   2519   6203    686    255    171       N  
ATOM    295  CA  PHE A  65      94.815  19.924  58.566  1.00 25.92           C  
ANISOU  295  CA  PHE A  65     1385   2432   6031    644    251    192       C  
ATOM    296  C   PHE A  65      93.896  18.872  59.166  1.00 25.75           C  
ANISOU  296  C   PHE A  65     1419   2403   5963    637    254    220       C  
ATOM    297  O   PHE A  65      93.222  18.151  58.431  1.00 25.89           O  
ANISOU  297  O   PHE A  65     1344   2597   5895    504    180    159       O  
ATOM    298  CB  PHE A  65      93.991  21.148  58.138  1.00 25.87           C  
ANISOU  298  CB  PHE A  65     1534   2293   6002    564    255    213       C  
ATOM    299  CG  PHE A  65      94.847  22.309  57.761  1.00 25.68           C  
ANISOU  299  CG  PHE A  65     1409   2352   5995    562    265    292       C  
ATOM    300  CD1 PHE A  65      95.366  22.412  56.479  1.00 25.98           C  
ANISOU  300  CD1 PHE A  65     1454   2352   6063    437    398    393       C  
ATOM    301  CD2 PHE A  65      95.191  23.253  58.711  1.00 24.32           C  
ANISOU  301  CD2 PHE A  65     1166   2012   6059    669    252    283       C  
ATOM    302  CE1 PHE A  65      96.203  23.458  56.140  1.00 27.08           C  
ANISOU  302  CE1 PHE A  65     2108   2216   5962    405    360    571       C  
ATOM    303  CE2 PHE A  65      96.032  24.303  58.382  1.00 24.77           C  
ANISOU  303  CE2 PHE A  65     1393   2162   5855    412    231    514       C  
ATOM    304  CZ  PHE A  65      96.536  24.409  57.091  1.00 26.08           C  
ANISOU  304  CZ  PHE A  65     1653   2355   5899    419    246    401       C  
ATOM    305  N   ARG A  66      93.910  18.778  60.494  1.00 25.21           N  
ANISOU  305  N   ARG A  66     1344   2387   5845    730    245    272       N  
ATOM    306  CA  ARG A  66      92.973  17.937  61.234  1.00 25.03           C  
ANISOU  306  CA  ARG A  66     1337   2415   5758    642    244    255       C  
ATOM    307  C   ARG A  66      92.442  18.881  62.305  1.00 24.76           C  
ANISOU  307  C   ARG A  66     1296   2459   5650    541    186    309       C  
ATOM    308  O   ARG A  66      93.092  19.144  63.320  1.00 24.20           O  
ANISOU  308  O   ARG A  66     1028   2491   5673    503    184    275       O  
ATOM    309  CB  ARG A  66      93.661  16.720  61.857  1.00 25.76           C  
ANISOU  309  CB  ARG A  66     1531   2449   5807    601    215    275       C  
ATOM    310  CG  ARG A  66      94.426  15.863  60.849  1.00 28.91           C  
ANISOU  310  CG  ARG A  66     2158   2838   5988    805    308    171       C  
ATOM    311  CD  ARG A  66      94.999  14.573  61.445  1.00 33.41           C  
ANISOU  311  CD  ARG A  66     3237   2853   6601    703    313    169       C  
ATOM    312  NE  ARG A  66      93.958  13.784  62.096  1.00 37.44           N  
ANISOU  312  NE  ARG A  66     3832   3423   6968    472    470    224       N  
ATOM    313  CZ  ARG A  66      93.167  12.909  61.478  1.00 40.42           C  
ANISOU  313  CZ  ARG A  66     4410   3884   7061    244    464    144       C  
ATOM    314  NH1 ARG A  66      93.298  12.684  60.174  1.00 40.51           N  
ANISOU  314  NH1 ARG A  66     4470   3913   7006    443    680     -5       N  
ATOM    315  NH2 ARG A  66      92.234  12.257  62.170  1.00 41.82           N  
ANISOU  315  NH2 ARG A  66     4553   4255   7080    181    540    361       N  
ATOM    316  N   LEU A  67      91.260  19.421  62.043  1.00 23.92           N  
ANISOU  316  N   LEU A  67     1222   2355   5509    500     93    344       N  
ATOM    317  CA  LEU A  67      90.709  20.454  62.905  1.00 23.27           C  
ANISOU  317  CA  LEU A  67     1187   2405   5247    387    113    380       C  
ATOM    318  C   LEU A  67      89.508  19.850  63.623  1.00 23.01           C  
ANISOU  318  C   LEU A  67     1210   2371   5161    343    -28    412       C  
ATOM    319  O   LEU A  67      88.446  19.665  63.037  1.00 22.38           O  
ANISOU  319  O   LEU A  67      994   2419   5089    254     -4    393       O  
ATOM    320  CB  LEU A  67      90.366  21.718  62.094  1.00 23.12           C  
ANISOU  320  CB  LEU A  67     1129   2410   5243    319    137    408       C  
ATOM    321  CG  LEU A  67      91.590  22.365  61.423  1.00 23.87           C  
ANISOU  321  CG  LEU A  67     1452   2421   5194     -9    -71    330       C  
ATOM    322  CD1 LEU A  67      91.180  23.455  60.422  1.00 23.55           C  
ANISOU  322  CD1 LEU A  67     1685   2307   4954   -109    149    290       C  
ATOM    323  CD2 LEU A  67      92.563  22.924  62.471  1.00 23.59           C  
ANISOU  323  CD2 LEU A  67     1069   2658   5236   -170   -123    505       C  
ATOM    324  N   ASN A  68      89.708  19.531  64.899  1.00 22.91           N  
ANISOU  324  N   ASN A  68     1221   2410   5072    359    -99    447       N  
ATOM    325  CA  ASN A  68      88.715  18.822  65.684  1.00 22.45           C  
ANISOU  325  CA  ASN A  68     1213   2379   4936    353   -229    407       C  
ATOM    326  C   ASN A  68      87.780  19.817  66.364  1.00 22.01           C  
ANISOU  326  C   ASN A  68     1158   2327   4876    326   -273    343       C  
ATOM    327  O   ASN A  68      88.149  20.493  67.328  1.00 22.71           O  
ANISOU  327  O   ASN A  68     1117   2588   4924    463   -337    288       O  
ATOM    328  CB  ASN A  68      89.418  17.919  66.701  1.00 22.94           C  
ANISOU  328  CB  ASN A  68     1366   2381   4969    378   -240    462       C  
ATOM    329  CG  ASN A  68      88.441  17.098  67.512  1.00 23.12           C  
ANISOU  329  CG  ASN A  68     1431   2468   4884    319   -396    490       C  
ATOM    330  OD1 ASN A  68      87.436  16.642  66.986  1.00 24.96           O  
ANISOU  330  OD1 ASN A  68     1936   2570   4976     90   -668    323       O  
ATOM    331  ND2 ASN A  68      88.717  16.929  68.803  1.00 24.33           N  
ANISOU  331  ND2 ASN A  68     1845   2707   4689    522   -447    531       N  
ATOM    332  N   VAL A  69      86.567  19.914  65.832  1.00 20.88           N  
ANISOU  332  N   VAL A  69     1010   2197   4723    337   -267    251       N  
ATOM    333  CA  VAL A  69      85.611  20.912  66.270  1.00 20.87           C  
ANISOU  333  CA  VAL A  69     1063   2256   4610    267   -215    181       C  
ATOM    334  C   VAL A  69      84.781  20.267  67.376  1.00 20.92           C  
ANISOU  334  C   VAL A  69     1020   2366   4562    259   -210    162       C  
ATOM    335  O   VAL A  69      84.092  19.262  67.163  1.00 21.77           O  
ANISOU  335  O   VAL A  69     1263   2420   4588    238   -145    123       O  
ATOM    336  CB  VAL A  69      84.763  21.400  65.078  1.00 20.40           C  
ANISOU  336  CB  VAL A  69     1026   2190   4535    308   -174    133       C  
ATOM    337  CG1 VAL A  69      83.601  22.280  65.551  1.00 20.56           C  
ANISOU  337  CG1 VAL A  69     1096   2114   4600    280   -186     84       C  
ATOM    338  CG2 VAL A  69      85.660  22.178  64.117  1.00 20.59           C  
ANISOU  338  CG2 VAL A  69     1221   2058   4542    270   -101     -6       C  
ATOM    339  N   ILE A  70      84.901  20.837  68.570  1.00 20.49           N  
ANISOU  339  N   ILE A  70      909   2373   4502    285   -258    202       N  
ATOM    340  CA  ILE A  70      84.285  20.285  69.767  1.00 19.95           C  
ANISOU  340  CA  ILE A  70      786   2349   4442    266   -262    241       C  
ATOM    341  C   ILE A  70      83.139  21.210  70.152  1.00 20.03           C  
ANISOU  341  C   ILE A  70      796   2339   4474    207   -296    266       C  
ATOM    342  O   ILE A  70      83.373  22.357  70.563  1.00 19.37           O  
ANISOU  342  O   ILE A  70      619   2193   4546    179   -229    237       O  
ATOM    343  CB  ILE A  70      85.309  20.219  70.918  1.00 20.09           C  
ANISOU  343  CB  ILE A  70      784   2396   4453    345   -253    311       C  
ATOM    344  CG1 ILE A  70      86.508  19.357  70.494  1.00 20.93           C  
ANISOU  344  CG1 ILE A  70     1007   2341   4602    419   -241     82       C  
ATOM    345  CG2 ILE A  70      84.640  19.644  72.166  1.00 21.19           C  
ANISOU  345  CG2 ILE A  70     1047   2547   4454    400   -117    283       C  
ATOM    346  CD1 ILE A  70      87.689  19.337  71.456  1.00 23.07           C  
ANISOU  346  CD1 ILE A  70     1277   2575   4912    967   -385    188       C  
ATOM    347  N   ASP A  71      81.907  20.718  69.999  1.00 19.89           N  
ANISOU  347  N   ASP A  71      763   2296   4498    112   -215    318       N  
ATOM    348  CA  ASP A  71      80.735  21.571  70.210  1.00 20.00           C  
ANISOU  348  CA  ASP A  71      922   2301   4376    117   -211    293       C  
ATOM    349  C   ASP A  71      80.294  21.509  71.671  1.00 20.64           C  
ANISOU  349  C   ASP A  71     1079   2412   4352     46   -202    298       C  
ATOM    350  O   ASP A  71      79.768  20.475  72.100  1.00 21.21           O  
ANISOU  350  O   ASP A  71     1347   2432   4276      2   -208    359       O  
ATOM    351  CB  ASP A  71      79.590  21.135  69.293  1.00 19.54           C  
ANISOU  351  CB  ASP A  71      871   2197   4354    155   -216    293       C  
ATOM    352  CG  ASP A  71      78.371  22.049  69.389  1.00 20.86           C  
ANISOU  352  CG  ASP A  71     1145   2252   4528    267   -228    307       C  
ATOM    353  OD1 ASP A  71      78.340  22.938  70.271  1.00 21.10           O  
ANISOU  353  OD1 ASP A  71     1099   2236   4682    513   -324    201       O  
ATOM    354  OD2 ASP A  71      77.426  21.866  68.588  1.00 20.69           O  
ANISOU  354  OD2 ASP A  71      972   2218   4672    -98      1    346       O  
ATOM    355  N   GLU A  72      80.478  22.614  72.399  1.00 20.66           N  
ANISOU  355  N   GLU A  72     1058   2444   4348     40   -189    237       N  
ATOM    356  CA  GLU A  72      80.100  22.740  73.809  1.00 21.86           C  
ANISOU  356  CA  GLU A  72     1269   2607   4429    129   -290    180       C  
ATOM    357  C   GLU A  72      79.000  23.795  74.012  1.00 21.52           C  
ANISOU  357  C   GLU A  72     1352   2474   4350    106   -183    193       C  
ATOM    358  O   GLU A  72      78.790  24.263  75.135  1.00 22.04           O  
ANISOU  358  O   GLU A  72     1522   2538   4312     63   -171    189       O  
ATOM    359  CB  GLU A  72      81.310  23.108  74.679  1.00 22.90           C  
ANISOU  359  CB  GLU A  72     1354   2792   4554    271   -353    190       C  
ATOM    360  CG  GLU A  72      82.513  22.185  74.494  1.00 26.83           C  
ANISOU  360  CG  GLU A  72     1765   3435   4991    533   -721    -33       C  
ATOM    361  CD  GLU A  72      83.614  22.430  75.502  1.00 31.68           C  
ANISOU  361  CD  GLU A  72     2359   4160   5519    605  -1062    -80       C  
ATOM    362  OE1 GLU A  72      83.752  23.569  75.995  1.00 35.03           O  
ANISOU  362  OE1 GLU A  72     2679   4828   5800    446  -1107   -416       O  
ATOM    363  OE2 GLU A  72      84.367  21.476  75.787  1.00 33.33           O  
ANISOU  363  OE2 GLU A  72     2460   4872   5332    802  -1506     70       O  
ATOM    364  N   LEU A  73      78.288  24.151  72.943  1.00 20.25           N  
ANISOU  364  N   LEU A  73     1265   2300   4126     84   -131    263       N  
ATOM    365  CA  LEU A  73      77.259  25.202  73.007  1.00 20.28           C  
ANISOU  365  CA  LEU A  73     1369   2274   4059     29     -9    268       C  
ATOM    366  C   LEU A  73      76.064  24.804  73.869  1.00 20.37           C  
ANISOU  366  C   LEU A  73     1366   2295   4079     16      6    247       C  
ATOM    367  O   LEU A  73      75.604  23.662  73.803  1.00 20.57           O  
ANISOU  367  O   LEU A  73     1486   2279   4048    -25    167    202       O  
ATOM    368  CB  LEU A  73      76.775  25.569  71.595  1.00 20.00           C  
ANISOU  368  CB  LEU A  73     1248   2277   4073     79      2    272       C  
ATOM    369  CG  LEU A  73      77.865  26.201  70.720  1.00 19.73           C  
ANISOU  369  CG  LEU A  73     1464   2073   3958   -114     33    226       C  
ATOM    370  CD1 LEU A  73      77.471  26.159  69.241  1.00 18.70           C  
ANISOU  370  CD1 LEU A  73     1091   2218   3796     21     78    476       C  
ATOM    371  CD2 LEU A  73      78.139  27.620  71.202  1.00 19.31           C  
ANISOU  371  CD2 LEU A  73      960   2009   4365   -252    209    138       C  
ATOM    372  N   THR A  74      75.552  25.744  74.660  1.00 20.27           N  
ANISOU  372  N   THR A  74     1373   2295   4031    -23     -8    269       N  
ATOM    373  CA  THR A  74      74.399  25.479  75.518  1.00 21.02           C  
ANISOU  373  CA  THR A  74     1616   2341   4028     65      0    323       C  
ATOM    374  C   THR A  74      73.223  26.389  75.210  1.00 20.60           C  
ANISOU  374  C   THR A  74     1496   2360   3971    -28     38    324       C  
ATOM    375  O   THR A  74      72.130  26.184  75.727  1.00 21.38           O  
ANISOU  375  O   THR A  74     1518   2609   3993     58    136    479       O  
ATOM    376  CB  THR A  74      74.757  25.630  77.007  1.00 21.65           C  
ANISOU  376  CB  THR A  74     1718   2419   4086     19     21    322       C  
ATOM    377  OG1 THR A  74      75.209  26.971  77.250  1.00 24.21           O  
ANISOU  377  OG1 THR A  74     2379   2510   4307    265     -2    233       O  
ATOM    378  CG2 THR A  74      75.886  24.669  77.365  1.00 22.94           C  
ANISOU  378  CG2 THR A  74     1855   2665   4195    274      3    437       C  
ATOM    379  N   ASN A  75      73.435  27.395  74.366  1.00 19.43           N  
ANISOU  379  N   ASN A  75     1386   2208   3788      6    -37    234       N  
ATOM    380  CA  ASN A  75      72.409  28.405  74.179  1.00 18.89           C  
ANISOU  380  CA  ASN A  75     1252   2078   3848    -46    -73    210       C  
ATOM    381  C   ASN A  75      71.644  28.251  72.859  1.00 18.73           C  
ANISOU  381  C   ASN A  75     1072   2057   3986   -121    -67    197       C  
ATOM    382  O   ASN A  75      72.188  28.548  71.794  1.00 18.61           O  
ANISOU  382  O   ASN A  75     1051   1867   4152   -294    -53    277       O  
ATOM    383  CB  ASN A  75      73.057  29.784  74.314  1.00 18.69           C  
ANISOU  383  CB  ASN A  75     1229   2105   3765    109   -145    124       C  
ATOM    384  CG  ASN A  75      72.033  30.895  74.323  1.00 20.53           C  
ANISOU  384  CG  ASN A  75     1614   2084   4102    237   -143     66       C  
ATOM    385  OD1 ASN A  75      70.998  30.782  73.668  1.00 22.86           O  
ANISOU  385  OD1 ASN A  75     1854   2319   4511    549   -344    -42       O  
ATOM    386  ND2 ASN A  75      72.308  31.965  75.065  1.00 19.27           N  
ANISOU  386  ND2 ASN A  75     1633   2113   3573    206    318   -106       N  
ATOM    387  N   HIS A  76      70.402  27.760  72.914  1.00 18.52           N  
ANISOU  387  N   HIS A  76      817   2092   4125   -129     -6    275       N  
ATOM    388  CA  HIS A  76      69.638  27.538  71.677  1.00 19.48           C  
ANISOU  388  CA  HIS A  76      897   2254   4247   -170     73    172       C  
ATOM    389  C   HIS A  76      69.359  28.826  70.886  1.00 19.36           C  
ANISOU  389  C   HIS A  76      903   2276   4177   -113    139    169       C  
ATOM    390  O   HIS A  76      69.160  28.796  69.666  1.00 19.79           O  
ANISOU  390  O   HIS A  76      982   2327   4208    -70    231     87       O  
ATOM    391  CB  HIS A  76      68.323  26.801  71.988  1.00 20.09           C  
ANISOU  391  CB  HIS A  76      833   2371   4428   -230     41    208       C  
ATOM    392  CG  HIS A  76      67.412  26.640  70.806  1.00 22.03           C  
ANISOU  392  CG  HIS A  76     1210   2516   4644   -189    -37    165       C  
ATOM    393  ND1 HIS A  76      67.739  25.876  69.704  1.00 22.19           N  
ANISOU  393  ND1 HIS A  76     1256   2293   4879   -297   -279   -110       N  
ATOM    394  CD2 HIS A  76      66.185  27.157  70.554  1.00 23.81           C  
ANISOU  394  CD2 HIS A  76     1478   2448   5120    -52    -93     72       C  
ATOM    395  CE1 HIS A  76      66.758  25.943  68.820  1.00 23.73           C  
ANISOU  395  CE1 HIS A  76     1625   2305   5086    -66   -136     59       C  
ATOM    396  NE2 HIS A  76      65.798  26.705  69.315  1.00 23.58           N  
ANISOU  396  NE2 HIS A  76     1471   2463   5023     -6    -91    190       N  
ATOM    397  N   THR A  77      69.306  29.964  71.566  1.00 19.02           N  
ANISOU  397  N   THR A  77      904   2171   4151    -57    163    181       N  
ATOM    398  CA  THR A  77      69.032  31.233  70.884  1.00 19.88           C  
ANISOU  398  CA  THR A  77     1138   2194   4221     86    192    130       C  
ATOM    399  C   THR A  77      70.100  31.579  69.842  1.00 19.01           C  
ANISOU  399  C   THR A  77     1011   2119   4093    122    126    152       C  
ATOM    400  O   THR A  77      69.837  32.284  68.869  1.00 19.24           O  
ANISOU  400  O   THR A  77     1106   2068   4135    219    188    142       O  
ATOM    401  CB  THR A  77      68.877  32.383  71.897  1.00 20.45           C  
ANISOU  401  CB  THR A  77     1303   2237   4227    146    245    157       C  
ATOM    402  OG1 THR A  77      67.802  32.040  72.774  1.00 21.03           O  
ANISOU  402  OG1 THR A  77     1240   2349   4398    134    396    110       O  
ATOM    403  CG2 THR A  77      68.532  33.706  71.200  1.00 21.26           C  
ANISOU  403  CG2 THR A  77     1514   2099   4464    140    276    166       C  
ATOM    404  N   MET A  78      71.308  31.064  70.044  1.00 18.26           N  
ANISOU  404  N   MET A  78      933   1982   4021    156     55     86       N  
ATOM    405  CA  MET A  78      72.371  31.267  69.084  1.00 17.40           C  
ANISOU  405  CA  MET A  78      891   1883   3837    108    -33     63       C  
ATOM    406  C   MET A  78      72.727  29.951  68.391  1.00 17.07           C  
ANISOU  406  C   MET A  78      904   1846   3733    150    -43     96       C  
ATOM    407  O   MET A  78      73.740  29.883  67.694  1.00 16.47           O  
ANISOU  407  O   MET A  78      903   1667   3686    138    -37    111       O  
ATOM    408  CB  MET A  78      73.587  31.897  69.797  1.00 17.54           C  
ANISOU  408  CB  MET A  78     1017   1877   3767     59   -164    -52       C  
ATOM    409  CG  MET A  78      73.213  33.259  70.415  1.00 17.08           C  
ANISOU  409  CG  MET A  78      991   1942   3556     80    -88    -96       C  
ATOM    410  SD  MET A  78      74.620  34.158  71.100  1.00 17.05           S  
ANISOU  410  SD  MET A  78     1307   2242   2929   -100   -182     -1       S  
ATOM    411  CE  MET A  78      74.852  33.293  72.640  1.00 16.20           C  
ANISOU  411  CE  MET A  78      851   2284   3019    134   -671    345       C  
ATOM    412  N   LEU A  79      71.888  28.939  68.620  1.00 16.46           N  
ANISOU  412  N   LEU A  79      772   1870   3609    170     42    163       N  
ATOM    413  CA  LEU A  79      71.989  27.556  68.118  1.00 16.93           C  
ANISOU  413  CA  LEU A  79      968   1980   3481    143    136    256       C  
ATOM    414  C   LEU A  79      73.023  26.709  68.847  1.00 17.17           C  
ANISOU  414  C   LEU A  79      972   2017   3535    106    163    264       C  
ATOM    415  O   LEU A  79      74.177  27.114  69.015  1.00 17.45           O  
ANISOU  415  O   LEU A  79      875   2081   3673    100    149    269       O  
ATOM    416  CB  LEU A  79      72.170  27.451  66.588  1.00 17.26           C  
ANISOU  416  CB  LEU A  79     1037   2089   3429    152    205    106       C  
ATOM    417  CG  LEU A  79      71.162  28.212  65.712  1.00 16.68           C  
ANISOU  417  CG  LEU A  79     1122   2132   3081    180    329    221       C  
ATOM    418  CD1 LEU A  79      71.505  28.140  64.216  1.00 17.62           C  
ANISOU  418  CD1 LEU A  79     1344   2289   3059    277    383   -108       C  
ATOM    419  CD2 LEU A  79      69.697  27.793  65.963  1.00 16.77           C  
ANISOU  419  CD2 LEU A  79     1342   1871   3158    148    405   -211       C  
ATOM    420  N   LYS A  80      72.601  25.520  69.265  1.00 17.77           N  
ANISOU  420  N   LYS A  80     1063   2082   3606    106    226    424       N  
ATOM    421  CA  LYS A  80      73.496  24.636  70.012  1.00 18.91           C  
ANISOU  421  CA  LYS A  80     1255   2175   3752     71    288    460       C  
ATOM    422  C   LYS A  80      74.315  23.783  69.058  1.00 18.90           C  
ANISOU  422  C   LYS A  80     1183   2136   3860     26    239    418       C  
ATOM    423  O   LYS A  80      75.347  23.251  69.446  1.00 19.29           O  
ANISOU  423  O   LYS A  80     1221   2198   3908     23    182    393       O  
ATOM    424  CB  LYS A  80      72.703  23.722  70.943  1.00 18.71           C  
ANISOU  424  CB  LYS A  80     1245   2162   3700    -33    392    496       C  
ATOM    425  CG  LYS A  80      71.973  24.426  72.085  1.00 21.76           C  
ANISOU  425  CG  LYS A  80     1890   2370   4007    173    507    593       C  
ATOM    426  CD  LYS A  80      71.501  23.352  73.063  1.00 24.71           C  
ANISOU  426  CD  LYS A  80     2245   3122   4021   -254    975    711       C  
ATOM    427  CE  LYS A  80      70.455  23.874  74.013  1.00 26.24           C  
ANISOU  427  CE  LYS A  80     2944   3016   4009    -57    925    774       C  
ATOM    428  NZ  LYS A  80      70.123  22.864  75.069  1.00 29.80           N  
ANISOU  428  NZ  LYS A  80     3413   3786   4121    -77    967   1103       N  
ATOM    429  N   SER A  81      73.850  23.658  67.816  1.00 18.96           N  
ANISOU  429  N   SER A  81     1113   2161   3929    -46    173    345       N  
ATOM    430  CA  SER A  81      74.544  22.884  66.789  1.00 18.96           C  
ANISOU  430  CA  SER A  81      965   2265   3973   -107    205    312       C  
ATOM    431  C   SER A  81      75.497  23.830  66.069  1.00 19.15           C  
ANISOU  431  C   SER A  81     1007   2214   4053    -58    156    288       C  
ATOM    432  O   SER A  81      75.396  25.060  66.227  1.00 19.18           O  
ANISOU  432  O   SER A  81      960   2244   4084     78    261    268       O  
ATOM    433  CB  SER A  81      73.517  22.300  65.809  1.00 19.43           C  
ANISOU  433  CB  SER A  81     1110   2283   3990   -244    263    321       C  
ATOM    434  OG  SER A  81      72.532  21.588  66.542  1.00 20.10           O  
ANISOU  434  OG  SER A  81     1123   2476   4034   -125    429    126       O  
ATOM    435  N   THR A  82      76.410  23.269  65.278  1.00 18.48           N  
ANISOU  435  N   THR A  82      752   2167   4103    -31     77    261       N  
ATOM    436  CA  THR A  82      77.280  24.105  64.468  1.00 19.44           C  
ANISOU  436  CA  THR A  82     1037   2121   4229     11     33    170       C  
ATOM    437  C   THR A  82      77.795  23.349  63.239  1.00 19.29           C  
ANISOU  437  C   THR A  82      960   2161   4208     27     57    155       C  
ATOM    438  O   THR A  82      77.686  22.131  63.141  1.00 19.74           O  
ANISOU  438  O   THR A  82     1042   2186   4273     -7    -17    114       O  
ATOM    439  CB  THR A  82      78.447  24.676  65.316  1.00 18.92           C  
ANISOU  439  CB  THR A  82      929   2016   4241     79    -46    221       C  
ATOM    440  OG1 THR A  82      79.058  25.789  64.637  1.00 19.28           O  
ANISOU  440  OG1 THR A  82     1084   1927   4312    -73    -87   -107       O  
ATOM    441  CG2 THR A  82      79.515  23.603  65.633  1.00 21.01           C  
ANISOU  441  CG2 THR A  82     1360   2176   4447    299   -245    201       C  
ATOM    442  N   SER A  83      78.342  24.084  62.284  1.00 19.27           N  
ANISOU  442  N   SER A  83      958   2199   4162     57     15    125       N  
ATOM    443  CA  SER A  83      78.989  23.479  61.127  1.00 18.99           C  
ANISOU  443  CA  SER A  83      922   2183   4109     94     94     89       C  
ATOM    444  C   SER A  83      80.017  24.505  60.669  1.00 18.90           C  
ANISOU  444  C   SER A  83      833   2259   4086    108    105     87       C  
ATOM    445  O   SER A  83      79.660  25.669  60.504  1.00 19.27           O  
ANISOU  445  O   SER A  83      895   2185   4241    102    212      1       O  
ATOM    446  CB  SER A  83      77.932  23.252  60.043  1.00 19.40           C  
ANISOU  446  CB  SER A  83      971   2195   4204     79     77    -21       C  
ATOM    447  OG  SER A  83      78.495  22.555  58.947  1.00 20.22           O  
ANISOU  447  OG  SER A  83     1416   1982   4283    246    293     21       O  
ATOM    448  N   ILE A  84      81.281  24.126  60.491  1.00 18.94           N  
ANISOU  448  N   ILE A  84      847   2377   3969    102    120    121       N  
ATOM    449  CA  ILE A  84      82.295  25.131  60.153  1.00 18.39           C  
ANISOU  449  CA  ILE A  84      804   2439   3743     77    184    152       C  
ATOM    450  C   ILE A  84      82.760  24.998  58.716  1.00 18.57           C  
ANISOU  450  C   ILE A  84      849   2379   3826    117    136     77       C  
ATOM    451  O   ILE A  84      83.164  23.918  58.276  1.00 18.62           O  
ANISOU  451  O   ILE A  84      855   2380   3840    130    195     31       O  
ATOM    452  CB  ILE A  84      83.570  25.023  61.020  1.00 19.27           C  
ANISOU  452  CB  ILE A  84      983   2664   3672    -10    219    246       C  
ATOM    453  CG1 ILE A  84      83.239  24.791  62.502  1.00 23.32           C  
ANISOU  453  CG1 ILE A  84     1778   3155   3928    249    333    242       C  
ATOM    454  CG2 ILE A  84      84.529  26.208  60.775  1.00 18.93           C  
ANISOU  454  CG2 ILE A  84      804   2695   3691    -91   -164    -15       C  
ATOM    455  CD1 ILE A  84      82.390  25.827  63.136  1.00 25.03           C  
ANISOU  455  CD1 ILE A  84     2051   3242   4216    420    451    111       C  
ATOM    456  N   HIS A  85      82.769  26.131  58.023  1.00 18.47           N  
ANISOU  456  N   HIS A  85      871   2278   3868    202    217     17       N  
ATOM    457  CA  HIS A  85      83.270  26.201  56.662  1.00 17.96           C  
ANISOU  457  CA  HIS A  85      766   2154   3902    191    261    -29       C  
ATOM    458  C   HIS A  85      84.659  26.842  56.663  1.00 17.93           C  
ANISOU  458  C   HIS A  85      786   2152   3875    287    321    -66       C  
ATOM    459  O   HIS A  85      84.898  27.831  57.366  1.00 17.22           O  
ANISOU  459  O   HIS A  85      634   2213   3692    157    255    -83       O  
ATOM    460  CB  HIS A  85      82.260  26.979  55.818  1.00 19.10           C  
ANISOU  460  CB  HIS A  85      866   2392   3996     94    286    -19       C  
ATOM    461  CG  HIS A  85      82.767  27.327  54.459  1.00 21.34           C  
ANISOU  461  CG  HIS A  85     1355   2564   4188     17    267   -150       C  
ATOM    462  ND1 HIS A  85      83.211  26.370  53.571  1.00 20.90           N  
ANISOU  462  ND1 HIS A  85     1127   2350   4462    -97    221   -245       N  
ATOM    463  CD2 HIS A  85      82.952  28.526  53.857  1.00 20.66           C  
ANISOU  463  CD2 HIS A  85      724   2885   4239    145    125    -60       C  
ATOM    464  CE1 HIS A  85      83.613  26.960  52.462  1.00 22.14           C  
ANISOU  464  CE1 HIS A  85     1280   2715   4415   -157     45   -192       C  
ATOM    465  NE2 HIS A  85      83.477  28.264  52.619  1.00 22.81           N  
ANISOU  465  NE2 HIS A  85     1078   3203   4386    -88    -71    -47       N  
ATOM    466  N   TRP A  86      85.570  26.289  55.864  1.00 17.72           N  
ANISOU  466  N   TRP A  86      710   2123   3900    357    300   -182       N  
ATOM    467  CA  TRP A  86      86.938  26.794  55.762  1.00 18.12           C  
ANISOU  467  CA  TRP A  86      885   2075   3923    464    434    -89       C  
ATOM    468  C   TRP A  86      86.989  27.583  54.455  1.00 19.06           C  
ANISOU  468  C   TRP A  86     1063   2226   3950    500    396   -128       C  
ATOM    469  O   TRP A  86      87.098  27.005  53.368  1.00 20.23           O  
ANISOU  469  O   TRP A  86     1381   2321   3984    604    516    -71       O  
ATOM    470  CB  TRP A  86      87.918  25.610  55.850  1.00 18.20           C  
ANISOU  470  CB  TRP A  86      803   2115   3995    497    454   -143       C  
ATOM    471  CG  TRP A  86      87.430  24.636  56.895  1.00 17.71           C  
ANISOU  471  CG  TRP A  86      791   2097   3840    526    502   -171       C  
ATOM    472  CD1 TRP A  86      86.654  23.530  56.686  1.00 20.09           C  
ANISOU  472  CD1 TRP A  86     1439   2084   4108    468    471   -323       C  
ATOM    473  CD2 TRP A  86      87.588  24.749  58.318  1.00 19.58           C  
ANISOU  473  CD2 TRP A  86     1199   2248   3990    505    286   -316       C  
ATOM    474  NE1 TRP A  86      86.341  22.931  57.889  1.00 19.65           N  
ANISOU  474  NE1 TRP A  86     1380   2039   4046    394    338   -199       N  
ATOM    475  CE2 TRP A  86      86.904  23.659  58.905  1.00 18.93           C  
ANISOU  475  CE2 TRP A  86     1185   2145   3863    578    391   -263       C  
ATOM    476  CE3 TRP A  86      88.248  25.661  59.152  1.00 18.76           C  
ANISOU  476  CE3 TRP A  86      985   2293   3849    473    186   -244       C  
ATOM    477  CZ2 TRP A  86      86.874  23.447  60.291  1.00 20.12           C  
ANISOU  477  CZ2 TRP A  86     1224   2317   4102    391     98   -265       C  
ATOM    478  CZ3 TRP A  86      88.197  25.464  60.535  1.00 19.37           C  
ANISOU  478  CZ3 TRP A  86     1049   2320   3990    434    128    -92       C  
ATOM    479  CH2 TRP A  86      87.516  24.363  61.089  1.00 20.21           C  
ANISOU  479  CH2 TRP A  86     1244   2280   4151    540    242   -237       C  
ATOM    480  N   HIS A  87      86.818  28.900  54.563  1.00 18.41           N  
ANISOU  480  N   HIS A  87     1012   2117   3865    511    356    -25       N  
ATOM    481  CA  HIS A  87      86.457  29.696  53.394  1.00 19.17           C  
ANISOU  481  CA  HIS A  87     1191   2262   3828    471    430    -51       C  
ATOM    482  C   HIS A  87      87.655  29.865  52.482  1.00 19.47           C  
ANISOU  482  C   HIS A  87     1210   2317   3870    431    437    -64       C  
ATOM    483  O   HIS A  87      88.669  30.453  52.890  1.00 19.54           O  
ANISOU  483  O   HIS A  87      992   2607   3824    363    522     -9       O  
ATOM    484  CB  HIS A  87      85.910  31.065  53.810  1.00 18.54           C  
ANISOU  484  CB  HIS A  87     1243   2182   3619    422    431   -128       C  
ATOM    485  CG  HIS A  87      85.510  31.943  52.662  1.00 20.13           C  
ANISOU  485  CG  HIS A  87     1672   2412   3564    426    423   -192       C  
ATOM    486  ND1 HIS A  87      84.261  32.521  52.565  1.00 19.77           N  
ANISOU  486  ND1 HIS A  87     1757   2658   3096    362    474   -541       N  
ATOM    487  CD2 HIS A  87      86.207  32.366  51.579  1.00 19.61           C  
ANISOU  487  CD2 HIS A  87     1865   2505   3078    407    380   -370       C  
ATOM    488  CE1 HIS A  87      84.207  33.266  51.474  1.00 21.27           C  
ANISOU  488  CE1 HIS A  87     1948   2637   3497    157    569   -413       C  
ATOM    489  NE2 HIS A  87      85.374  33.183  50.854  1.00 20.38           N  
ANISOU  489  NE2 HIS A  87     1907   2603   3233    413    579   -234       N  
ATOM    490  N   GLY A  88      87.511  29.372  51.251  1.00 19.88           N  
ANISOU  490  N   GLY A  88     1272   2200   4079    462    409    -63       N  
ATOM    491  CA  GLY A  88      88.555  29.521  50.240  1.00 20.78           C  
ANISOU  491  CA  GLY A  88     1405   2303   4186    347    428   -151       C  
ATOM    492  C   GLY A  88      89.224  28.210  49.871  1.00 21.27           C  
ANISOU  492  C   GLY A  88     1441   2323   4319    349    401   -216       C  
ATOM    493  O   GLY A  88      89.852  28.112  48.814  1.00 21.57           O  
ANISOU  493  O   GLY A  88     1506   2385   4304    142    448    -76       O  
ATOM    494  N   PHE A  89      89.126  27.202  50.737  1.00 21.36           N  
ANISOU  494  N   PHE A  89     1491   2252   4370    257    452   -288       N  
ATOM    495  CA  PHE A  89      89.756  25.895  50.452  1.00 22.19           C  
ANISOU  495  CA  PHE A  89     1536   2389   4505    356    453   -380       C  
ATOM    496  C   PHE A  89      88.973  25.095  49.405  1.00 22.17           C  
ANISOU  496  C   PHE A  89     1583   2328   4510    324    522   -421       C  
ATOM    497  O   PHE A  89      87.742  25.012  49.471  1.00 22.42           O  
ANISOU  497  O   PHE A  89     1615   2429   4473    362    729   -307       O  
ATOM    498  CB  PHE A  89      89.920  25.079  51.739  1.00 21.17           C  
ANISOU  498  CB  PHE A  89     1293   2379   4372    352    338   -440       C  
ATOM    499  CG  PHE A  89      90.986  25.623  52.638  1.00 23.94           C  
ANISOU  499  CG  PHE A  89     1354   2983   4757    229    298   -531       C  
ATOM    500  CD1 PHE A  89      92.319  25.318  52.393  1.00 25.85           C  
ANISOU  500  CD1 PHE A  89     1136   3742   4944    241   -332   -640       C  
ATOM    501  CD2 PHE A  89      90.666  26.485  53.680  1.00 24.04           C  
ANISOU  501  CD2 PHE A  89     1335   3037   4760      1   -239   -640       C  
ATOM    502  CE1 PHE A  89      93.318  25.846  53.190  1.00 27.48           C  
ANISOU  502  CE1 PHE A  89     1119   4002   5318   -158    -30   -983       C  
ATOM    503  CE2 PHE A  89      91.658  27.022  54.478  1.00 24.18           C  
ANISOU  503  CE2 PHE A  89      848   3229   5109     22   -390   -613       C  
ATOM    504  CZ  PHE A  89      92.982  26.694  54.235  1.00 26.67           C  
ANISOU  504  CZ  PHE A  89     1207   3695   5228     24    112   -846       C  
ATOM    505  N   PHE A  90      89.667  24.523  48.425  1.00 22.64           N  
ANISOU  505  N   PHE A  90     1696   2363   4541    285    651   -455       N  
ATOM    506  CA  PHE A  90      88.971  23.792  47.361  1.00 23.80           C  
ANISOU  506  CA  PHE A  90     1839   2549   4652    289    664   -496       C  
ATOM    507  C   PHE A  90      88.286  22.502  47.816  1.00 24.12           C  
ANISOU  507  C   PHE A  90     1887   2513   4762    358    634   -564       C  
ATOM    508  O   PHE A  90      87.296  22.078  47.203  1.00 23.88           O  
ANISOU  508  O   PHE A  90     1699   2503   4871    304    603   -577       O  
ATOM    509  CB  PHE A  90      89.893  23.498  46.167  1.00 24.22           C  
ANISOU  509  CB  PHE A  90     1914   2621   4667    292    726   -514       C  
ATOM    510  CG  PHE A  90      90.499  24.722  45.553  1.00 25.92           C  
ANISOU  510  CG  PHE A  90     2213   2951   4684    113    671   -342       C  
ATOM    511  CD1 PHE A  90      89.827  25.938  45.575  1.00 27.79           C  
ANISOU  511  CD1 PHE A  90     2630   3069   4860    -11    658   -177       C  
ATOM    512  CD2 PHE A  90      91.755  24.655  44.954  1.00 27.26           C  
ANISOU  512  CD2 PHE A  90     2545   3313   4498     94    910   -301       C  
ATOM    513  CE1 PHE A  90      90.404  27.081  45.014  1.00 29.68           C  
ANISOU  513  CE1 PHE A  90     3104   3219   4952    -28    639     41       C  
ATOM    514  CE2 PHE A  90      92.338  25.786  44.387  1.00 28.94           C  
ANISOU  514  CE2 PHE A  90     3219   3153   4623    105    707   -232       C  
ATOM    515  CZ  PHE A  90      91.657  26.999  44.408  1.00 29.51           C  
ANISOU  515  CZ  PHE A  90     3111   3297   4801    168    676   -136       C  
ATOM    516  N   GLN A  91      88.809  21.892  48.879  1.00 24.13           N  
ANISOU  516  N   GLN A  91     1886   2501   4780    506    631   -631       N  
ATOM    517  CA  GLN A  91      88.252  20.642  49.419  1.00 24.76           C  
ANISOU  517  CA  GLN A  91     1934   2656   4817    601    668   -702       C  
ATOM    518  C   GLN A  91      88.131  19.533  48.369  1.00 25.53           C  
ANISOU  518  C   GLN A  91     2141   2717   4840    630    629   -747       C  
ATOM    519  O   GLN A  91      87.174  18.747  48.381  1.00 24.69           O  
ANISOU  519  O   GLN A  91     1962   2696   4720    641    751   -805       O  
ATOM    520  CB  GLN A  91      86.896  20.902  50.100  1.00 24.65           C  
ANISOU  520  CB  GLN A  91     1941   2684   4739    712    679   -698       C  
ATOM    521  CG  GLN A  91      86.982  21.900  51.243  1.00 23.98           C  
ANISOU  521  CG  GLN A  91     1765   2426   4917    676    520   -657       C  
ATOM    522  CD  GLN A  91      87.610  21.325  52.507  1.00 24.11           C  
ANISOU  522  CD  GLN A  91     1879   2120   5159    733    520   -489       C  
ATOM    523  OE1 GLN A  91      88.055  20.176  52.536  1.00 26.50           O  
ANISOU  523  OE1 GLN A  91     2310   2165   5592    751    357   -224       O  
ATOM    524  NE2 GLN A  91      87.640  22.127  53.565  1.00 22.41           N  
ANISOU  524  NE2 GLN A  91     1528   1878   5107    315     82   -421       N  
ATOM    525  N   HIS A  92      89.111  19.465  47.467  1.00 25.93           N  
ANISOU  525  N   HIS A  92     2260   2748   4842    740    607   -828       N  
ATOM    526  CA  HIS A  92      89.096  18.459  46.414  1.00 27.84           C  
ANISOU  526  CA  HIS A  92     2674   2948   4953    688    418   -863       C  
ATOM    527  C   HIS A  92      89.113  17.056  47.020  1.00 27.19           C  
ANISOU  527  C   HIS A  92     2576   2835   4918    652    405   -865       C  
ATOM    528  O   HIS A  92      90.031  16.690  47.761  1.00 26.16           O  
ANISOU  528  O   HIS A  92     2422   2568   4950    804    394   -882       O  
ATOM    529  CB  HIS A  92      90.277  18.640  45.449  1.00 28.89           C  
ANISOU  529  CB  HIS A  92     2787   3157   5032    680    436   -975       C  
ATOM    530  CG  HIS A  92      90.107  17.887  44.169  1.00 35.40           C  
ANISOU  530  CG  HIS A  92     3977   4093   5378    789    166   -937       C  
ATOM    531  ND1 HIS A  92      90.545  16.590  44.001  1.00 40.45           N  
ANISOU  531  ND1 HIS A  92     4989   4456   5922    967   -112   -962       N  
ATOM    532  CD2 HIS A  92      89.500  18.233  43.007  1.00 39.47           C  
ANISOU  532  CD2 HIS A  92     4503   4704   5790   1016   -147   -754       C  
ATOM    533  CE1 HIS A  92      90.234  16.175  42.784  1.00 42.03           C  
ANISOU  533  CE1 HIS A  92     5313   4762   5893    869   -327   -869       C  
ATOM    534  NE2 HIS A  92      89.595  17.152  42.163  1.00 41.72           N  
ANISOU  534  NE2 HIS A  92     5042   4840   5968    926   -378   -906       N  
ATOM    535  N   GLY A  93      88.070  16.286  46.720  1.00 26.89           N  
ANISOU  535  N   GLY A  93     2596   2751   4870    649    344   -825       N  
ATOM    536  CA  GLY A  93      87.910  14.955  47.287  1.00 26.19           C  
ANISOU  536  CA  GLY A  93     2539   2662   4747    575    254   -710       C  
ATOM    537  C   GLY A  93      87.551  14.931  48.762  1.00 25.89           C  
ANISOU  537  C   GLY A  93     2480   2629   4728    559    216   -633       C  
ATOM    538  O   GLY A  93      87.484  13.853  49.353  1.00 25.98           O  
ANISOU  538  O   GLY A  93     2621   2596   4652    566    173   -601       O  
ATOM    539  N   THR A  94      87.315  16.098  49.361  1.00 24.64           N  
ANISOU  539  N   THR A  94     2303   2496   4561    520    206   -564       N  
ATOM    540  CA  THR A  94      86.884  16.170  50.757  1.00 23.57           C  
ANISOU  540  CA  THR A  94     2037   2428   4487    518    219   -470       C  
ATOM    541  C   THR A  94      85.662  17.079  50.895  1.00 23.53           C  
ANISOU  541  C   THR A  94     2075   2482   4383    459    239   -477       C  
ATOM    542  O   THR A  94      85.537  17.854  51.852  1.00 23.14           O  
ANISOU  542  O   THR A  94     2066   2418   4307    460    105   -457       O  
ATOM    543  CB  THR A  94      88.022  16.597  51.726  1.00 23.56           C  
ANISOU  543  CB  THR A  94     2086   2337   4527    547    252   -459       C  
ATOM    544  OG1 THR A  94      88.560  17.863  51.331  1.00 21.64           O  
ANISOU  544  OG1 THR A  94     1571   2222   4429    500    164   -402       O  
ATOM    545  CG2 THR A  94      89.165  15.562  51.781  1.00 24.20           C  
ANISOU  545  CG2 THR A  94     1851   2650   4693    591    326   -339       C  
ATOM    546  N   ASN A  95      84.749  16.970  49.932  1.00 22.57           N  
ANISOU  546  N   ASN A  95     1899   2449   4225    407    283   -421       N  
ATOM    547  CA  ASN A  95      83.518  17.759  49.928  1.00 22.46           C  
ANISOU  547  CA  ASN A  95     1949   2385   4199    369    410   -409       C  
ATOM    548  C   ASN A  95      82.799  17.708  51.273  1.00 21.89           C  
ANISOU  548  C   ASN A  95     1834   2296   4185    339    479   -368       C  
ATOM    549  O   ASN A  95      82.220  18.709  51.691  1.00 21.48           O  
ANISOU  549  O   ASN A  95     1807   2189   4165    245    470   -365       O  
ATOM    550  CB  ASN A  95      82.567  17.324  48.801  1.00 22.35           C  
ANISOU  550  CB  ASN A  95     1972   2288   4230    420    338   -446       C  
ATOM    551  CG  ASN A  95      81.310  18.175  48.730  1.00 22.40           C  
ANISOU  551  CG  ASN A  95     1983   2322   4205    297    409   -491       C  
ATOM    552  OD1 ASN A  95      80.344  17.940  49.460  1.00 22.08           O  
ANISOU  552  OD1 ASN A  95     2342   1892   4154      4    496   -520       O  
ATOM    553  ND2 ASN A  95      81.316  19.174  47.844  1.00 22.18           N  
ANISOU  553  ND2 ASN A  95     1872   2189   4367    334    485   -493       N  
ATOM    554  N   TRP A  96      82.857  16.549  51.926  1.00 21.18           N  
ANISOU  554  N   TRP A  96     1618   2252   4175    360    484   -321       N  
ATOM    555  CA  TRP A  96      82.212  16.308  53.215  1.00 21.04           C  
ANISOU  555  CA  TRP A  96     1675   2102   4216    287    483   -270       C  
ATOM    556  C   TRP A  96      82.742  17.202  54.335  1.00 20.91           C  
ANISOU  556  C   TRP A  96     1588   2071   4284    321    498   -277       C  
ATOM    557  O   TRP A  96      82.138  17.281  55.408  1.00 21.15           O  
ANISOU  557  O   TRP A  96     1469   2171   4393    270    647   -231       O  
ATOM    558  CB  TRP A  96      82.367  14.833  53.605  1.00 20.61           C  
ANISOU  558  CB  TRP A  96     1635   2057   4136    317    497   -311       C  
ATOM    559  CG  TRP A  96      83.796  14.398  53.813  1.00 21.64           C  
ANISOU  559  CG  TRP A  96     1805   2097   4318    265    468   -243       C  
ATOM    560  CD1 TRP A  96      84.606  13.775  52.902  1.00 20.98           C  
ANISOU  560  CD1 TRP A  96     1726   2139   4103    262    580   -237       C  
ATOM    561  CD2 TRP A  96      84.579  14.561  55.000  1.00 21.97           C  
ANISOU  561  CD2 TRP A  96     1842   2168   4336    140    482   -262       C  
ATOM    562  NE1 TRP A  96      85.841  13.528  53.455  1.00 22.43           N  
ANISOU  562  NE1 TRP A  96     2006   2205   4309     99    516   -156       N  
ATOM    563  CE2 TRP A  96      85.852  14.005  54.740  1.00 22.55           C  
ANISOU  563  CE2 TRP A  96     2068   2081   4418    286    350   -251       C  
ATOM    564  CE3 TRP A  96      84.331  15.129  56.254  1.00 22.34           C  
ANISOU  564  CE3 TRP A  96     1936   2147   4403     75    425   -285       C  
ATOM    565  CZ2 TRP A  96      86.879  14.013  55.689  1.00 24.39           C  
ANISOU  565  CZ2 TRP A  96     2399   2250   4615    207    339   -202       C  
ATOM    566  CZ3 TRP A  96      85.339  15.112  57.205  1.00 22.78           C  
ANISOU  566  CZ3 TRP A  96     1857   2074   4723    229    387   -135       C  
ATOM    567  CH2 TRP A  96      86.601  14.568  56.913  1.00 23.12           C  
ANISOU  567  CH2 TRP A  96     2032   2178   4574    359    337   -181       C  
ATOM    568  N   ALA A  97      83.883  17.845  54.094  1.00 20.16           N  
ANISOU  568  N   ALA A  97     1363   1984   4311    301    473   -286       N  
ATOM    569  CA  ALA A  97      84.546  18.700  55.080  1.00 20.16           C  
ANISOU  569  CA  ALA A  97     1366   1995   4298    358    353   -338       C  
ATOM    570  C   ALA A  97      84.294  20.185  54.814  1.00 20.52           C  
ANISOU  570  C   ALA A  97     1414   2058   4322    354    322   -392       C  
ATOM    571  O   ALA A  97      84.766  21.043  55.558  1.00 21.29           O  
ANISOU  571  O   ALA A  97     1683   2065   4340    329    214   -342       O  
ATOM    572  CB  ALA A  97      86.074  18.423  55.068  1.00 20.04           C  
ANISOU  572  CB  ALA A  97     1354   1989   4268    369    386   -413       C  
ATOM    573  N   ASP A  98      83.580  20.496  53.736  1.00 20.48           N  
ANISOU  573  N   ASP A  98     1453   2030   4298    384    259   -341       N  
ATOM    574  CA  ASP A  98      83.392  21.889  53.317  1.00 21.16           C  
ANISOU  574  CA  ASP A  98     1542   2124   4373    320    253   -429       C  
ATOM    575  C   ASP A  98      82.553  22.736  54.284  1.00 20.90           C  
ANISOU  575  C   ASP A  98     1439   2143   4357    319    228   -399       C  
ATOM    576  O   ASP A  98      82.740  23.943  54.376  1.00 21.80           O  
ANISOU  576  O   ASP A  98     1629   2171   4481    276    215   -477       O  
ATOM    577  CB  ASP A  98      82.818  21.966  51.901  1.00 20.01           C  
ANISOU  577  CB  ASP A  98     1443   1953   4207    311    174   -383       C  
ATOM    578  CG  ASP A  98      82.957  23.352  51.287  1.00 21.54           C  
ANISOU  578  CG  ASP A  98     1525   2091   4565    265    169   -468       C  
ATOM    579  OD1 ASP A  98      84.020  24.011  51.428  1.00 23.38           O  
ANISOU  579  OD1 ASP A  98     1794   2204   4884     26    280   -353       O  
ATOM    580  OD2 ASP A  98      81.988  23.778  50.634  1.00 21.71           O  
ANISOU  580  OD2 ASP A  98     1282   2130   4834     99    163   -231       O  
ATOM    581  N   GLY A  99      81.637  22.109  55.010  1.00 21.14           N  
ANISOU  581  N   GLY A  99     1316   2330   4386    223    213   -400       N  
ATOM    582  CA  GLY A  99      80.967  22.784  56.110  1.00 20.45           C  
ANISOU  582  CA  GLY A  99     1222   2259   4288    269    283   -391       C  
ATOM    583  C   GLY A  99      79.638  23.478  55.846  1.00 20.30           C  
ANISOU  583  C   GLY A  99     1067   2380   4263    116    253   -365       C  
ATOM    584  O   GLY A  99      79.038  24.014  56.773  1.00 20.17           O  
ANISOU  584  O   GLY A  99     1266   2314   4084     89    248   -462       O  
ATOM    585  N   GLY A 100      79.144  23.475  54.612  1.00 20.12           N  
ANISOU  585  N   GLY A 100      979   2383   4280     92    268   -281       N  
ATOM    586  CA  GLY A 100      77.850  24.106  54.352  1.00 20.44           C  
ANISOU  586  CA  GLY A 100      946   2516   4302    102    230   -333       C  
ATOM    587  C   GLY A 100      76.732  23.301  55.000  1.00 19.86           C  
ANISOU  587  C   GLY A 100      942   2391   4213     66    252   -306       C  
ATOM    588  O   GLY A 100      76.530  22.136  54.637  1.00 20.61           O  
ANISOU  588  O   GLY A 100      969   2531   4329    109    111   -261       O  
ATOM    589  N   ALA A 101      76.015  23.883  55.961  1.00 19.22           N  
ANISOU  589  N   ALA A 101      742   2345   4213    170    257   -316       N  
ATOM    590  CA  ALA A 101      74.976  23.099  56.642  1.00 19.36           C  
ANISOU  590  CA  ALA A 101     1013   2219   4123    114    274   -376       C  
ATOM    591  C   ALA A 101      73.888  22.641  55.671  1.00 19.23           C  
ANISOU  591  C   ALA A 101      973   2313   4019    178    211   -339       C  
ATOM    592  O   ALA A 101      73.372  23.449  54.911  1.00 19.01           O  
ANISOU  592  O   ALA A 101     1070   2034   4117    202    247   -380       O  
ATOM    593  CB  ALA A 101      74.339  23.869  57.797  1.00 19.78           C  
ANISOU  593  CB  ALA A 101     1140   2391   3981    128    317   -402       C  
ATOM    594  N   PHE A 102      73.585  21.342  55.682  1.00 19.48           N  
ANISOU  594  N   PHE A 102      979   2370   4051     36     54   -271       N  
ATOM    595  CA  PHE A 102      72.542  20.723  54.844  1.00 20.59           C  
ANISOU  595  CA  PHE A 102     1119   2586   4116    104    109   -276       C  
ATOM    596  C   PHE A 102      72.898  20.694  53.358  1.00 20.85           C  
ANISOU  596  C   PHE A 102     1249   2526   4145     81    114   -278       C  
ATOM    597  O   PHE A 102      72.065  20.389  52.500  1.00 21.50           O  
ANISOU  597  O   PHE A 102     1319   2659   4190     -1    122   -214       O  
ATOM    598  CB  PHE A 102      71.174  21.350  55.137  1.00 20.28           C  
ANISOU  598  CB  PHE A 102      924   2698   4083    121     86   -228       C  
ATOM    599  CG  PHE A 102      70.818  21.303  56.594  1.00 22.56           C  
ANISOU  599  CG  PHE A 102     1151   3164   4254    186     30   -207       C  
ATOM    600  CD1 PHE A 102      70.425  20.108  57.194  1.00 22.16           C  
ANISOU  600  CD1 PHE A 102      881   3275   4261    117     34    -74       C  
ATOM    601  CD2 PHE A 102      70.938  22.444  57.378  1.00 22.42           C  
ANISOU  601  CD2 PHE A 102     1044   3153   4320    233    225   -226       C  
ATOM    602  CE1 PHE A 102      70.128  20.057  58.558  1.00 22.78           C  
ANISOU  602  CE1 PHE A 102      944   3263   4445    358     88    -46       C  
ATOM    603  CE2 PHE A 102      70.668  22.403  58.749  1.00 23.17           C  
ANISOU  603  CE2 PHE A 102      921   3558   4324    367    327    -51       C  
ATOM    604  CZ  PHE A 102      70.246  21.205  59.340  1.00 22.26           C  
ANISOU  604  CZ  PHE A 102      850   3280   4326    360    -69     12       C  
ATOM    605  N   VAL A 103      74.161  20.991  53.072  1.00 21.06           N  
ANISOU  605  N   VAL A 103     1418   2404   4178     17    259   -303       N  
ATOM    606  CA  VAL A 103      74.715  20.811  51.732  1.00 20.79           C  
ANISOU  606  CA  VAL A 103     1518   2203   4175    141    217   -282       C  
ATOM    607  C   VAL A 103      75.841  19.786  51.781  1.00 21.19           C  
ANISOU  607  C   VAL A 103     1654   2184   4213    121    197   -327       C  
ATOM    608  O   VAL A 103      75.778  18.749  51.120  1.00 21.92           O  
ANISOU  608  O   VAL A 103     1969   2193   4167    198    211   -368       O  
ATOM    609  CB  VAL A 103      75.187  22.140  51.108  1.00 20.47           C  
ANISOU  609  CB  VAL A 103     1428   2275   4072    252    231   -279       C  
ATOM    610  CG1 VAL A 103      75.848  21.860  49.755  1.00 19.77           C  
ANISOU  610  CG1 VAL A 103     1319   2069   4124    106    331    -92       C  
ATOM    611  CG2 VAL A 103      73.962  23.070  50.954  1.00 20.66           C  
ANISOU  611  CG2 VAL A 103     1645   1927   4278    411    211   -301       C  
ATOM    612  N   ASN A 104      76.848  20.066  52.598  1.00 20.50           N  
ANISOU  612  N   ASN A 104     1485   2105   4199     89    169   -257       N  
ATOM    613  CA  ASN A 104      77.982  19.173  52.755  1.00 20.15           C  
ANISOU  613  CA  ASN A 104     1413   2020   4220     43    248   -311       C  
ATOM    614  C   ASN A 104      77.938  18.261  53.968  1.00 20.04           C  
ANISOU  614  C   ASN A 104     1383   2043   4186     19    175   -301       C  
ATOM    615  O   ASN A 104      78.662  17.261  54.000  1.00 20.34           O  
ANISOU  615  O   ASN A 104     1591   1965   4172     30    239   -482       O  
ATOM    616  CB  ASN A 104      79.269  19.995  52.761  1.00 19.72           C  
ANISOU  616  CB  ASN A 104     1318   2078   4097     17    155   -247       C  
ATOM    617  CG  ASN A 104      79.330  20.924  51.575  1.00 19.44           C  
ANISOU  617  CG  ASN A 104     1273   2073   4037     30    378   -296       C  
ATOM    618  OD1 ASN A 104      79.578  20.503  50.437  1.00 22.69           O  
ANISOU  618  OD1 ASN A 104     2030   2648   3941    338    182   -342       O  
ATOM    619  ND2 ASN A 104      79.045  22.183  51.822  1.00 16.34           N  
ANISOU  619  ND2 ASN A 104      779   2061   3366    151    607   -487       N  
ATOM    620  N   GLN A 105      77.107  18.604  54.950  1.00 20.21           N  
ANISOU  620  N   GLN A 105     1367   2021   4289     16    162   -288       N  
ATOM    621  CA  GLN A 105      76.943  17.804  56.170  1.00 20.38           C  
ANISOU  621  CA  GLN A 105     1315   2075   4350    -47     93   -202       C  
ATOM    622  C   GLN A 105      75.665  18.198  56.917  1.00 20.84           C  
ANISOU  622  C   GLN A 105     1369   2087   4461    -23    117   -128       C  
ATOM    623  O   GLN A 105      75.111  19.281  56.672  1.00 20.67           O  
ANISOU  623  O   GLN A 105     1389   2104   4360     -6    108    -94       O  
ATOM    624  CB  GLN A 105      78.134  18.048  57.114  1.00 20.19           C  
ANISOU  624  CB  GLN A 105     1193   2117   4360    -88    150   -275       C  
ATOM    625  CG  GLN A 105      78.172  19.475  57.671  1.00 19.71           C  
ANISOU  625  CG  GLN A 105     1167   1922   4398   -104     85   -203       C  
ATOM    626  CD  GLN A 105      79.211  19.647  58.756  1.00 19.91           C  
ANISOU  626  CD  GLN A 105     1678   1792   4095   -202    231   -395       C  
ATOM    627  OE1 GLN A 105      80.336  20.058  58.474  1.00 19.89           O  
ANISOU  627  OE1 GLN A 105     1535   2100   3920     81    281   -180       O  
ATOM    628  NE2 GLN A 105      78.855  19.313  59.996  1.00 21.00           N  
ANISOU  628  NE2 GLN A 105     1639   1964   4374   -311    390     72       N  
ATOM    629  N   CYS A 106      75.214  17.346  57.839  1.00 21.03           N  
ANISOU  629  N   CYS A 106     1414   2023   4553   -113      7    -99       N  
ATOM    630  CA  CYS A 106      74.296  17.795  58.885  1.00 21.47           C  
ANISOU  630  CA  CYS A 106     1477   2042   4637    -93    -28     -7       C  
ATOM    631  C   CYS A 106      75.152  18.460  59.950  1.00 20.54           C  
ANISOU  631  C   CYS A 106     1352   1894   4556      2    -69     16       C  
ATOM    632  O   CYS A 106      76.333  18.127  60.088  1.00 20.30           O  
ANISOU  632  O   CYS A 106     1361   1813   4538    141     34     15       O  
ATOM    633  CB  CYS A 106      73.535  16.639  59.551  1.00 22.51           C  
ANISOU  633  CB  CYS A 106     1703   2131   4718   -150    -69     -6       C  
ATOM    634  SG  CYS A 106      72.112  16.036  58.627  1.00 28.18           S  
ANISOU  634  SG  CYS A 106     2239   2856   5611   -260   -108     54       S  
ATOM    635  N   PRO A 107      74.556  19.374  60.729  1.00 20.29           N  
ANISOU  635  N   PRO A 107     1260   1943   4504    107    -90     84       N  
ATOM    636  CA  PRO A 107      75.301  20.058  61.782  1.00 20.07           C  
ANISOU  636  CA  PRO A 107     1313   1885   4427    134   -131    101       C  
ATOM    637  C   PRO A 107      75.848  19.098  62.831  1.00 20.83           C  
ANISOU  637  C   PRO A 107     1431   2019   4461     19   -108    117       C  
ATOM    638  O   PRO A 107      75.265  18.033  63.062  1.00 21.56           O  
ANISOU  638  O   PRO A 107     1692   2046   4454     83    -94    164       O  
ATOM    639  CB  PRO A 107      74.252  20.984  62.409  1.00 19.96           C  
ANISOU  639  CB  PRO A 107     1273   1957   4353    202   -103    138       C  
ATOM    640  CG  PRO A 107      73.261  21.223  61.280  1.00 20.07           C  
ANISOU  640  CG  PRO A 107     1221   1940   4461     46   -156     74       C  
ATOM    641  CD  PRO A 107      73.175  19.880  60.608  1.00 20.35           C  
ANISOU  641  CD  PRO A 107     1258   2006   4467    221    -72     25       C  
ATOM    642  N   ILE A 108      76.968  19.489  63.433  1.00 20.73           N  
ANISOU  642  N   ILE A 108     1355   2066   4455     -4   -124    108       N  
ATOM    643  CA  ILE A 108      77.499  18.854  64.637  1.00 20.44           C  
ANISOU  643  CA  ILE A 108     1274   2076   4415   -161    -55    114       C  
ATOM    644  C   ILE A 108      76.543  19.194  65.777  1.00 20.07           C  
ANISOU  644  C   ILE A 108     1231   2009   4386   -147     80    116       C  
ATOM    645  O   ILE A 108      76.081  20.332  65.872  1.00 19.97           O  
ANISOU  645  O   ILE A 108     1070   2093   4425    -45    202    208       O  
ATOM    646  CB  ILE A 108      78.908  19.414  65.008  1.00 19.82           C  
ANISOU  646  CB  ILE A 108     1122   1986   4422   -190    -98    168       C  
ATOM    647  CG1 ILE A 108      79.862  19.328  63.817  1.00 19.53           C  
ANISOU  647  CG1 ILE A 108     1099   2084   4235   -371   -196     71       C  
ATOM    648  CG2 ILE A 108      79.482  18.662  66.211  1.00 19.51           C  
ANISOU  648  CG2 ILE A 108     1103   2076   4233   -284   -227    -19       C  
ATOM    649  CD1 ILE A 108      81.204  20.094  63.988  1.00 19.08           C  
ANISOU  649  CD1 ILE A 108     1016   2306   3926   -369    -65    135       C  
ATOM    650  N   SER A 109      76.285  18.229  66.653  1.00 19.83           N  
ANISOU  650  N   SER A 109     1255   1973   4304   -180    170     86       N  
ATOM    651  CA  SER A 109      75.380  18.430  67.784  1.00 20.29           C  
ANISOU  651  CA  SER A 109     1458   2000   4250   -236    172     44       C  
ATOM    652  C   SER A 109      76.143  18.736  69.063  1.00 20.42           C  
ANISOU  652  C   SER A 109     1529   1982   4248   -203    141     74       C  
ATOM    653  O   SER A 109      77.278  18.288  69.261  1.00 20.18           O  
ANISOU  653  O   SER A 109     1535   1866   4266   -122    264     35       O  
ATOM    654  CB  SER A 109      74.503  17.196  67.999  1.00 19.95           C  
ANISOU  654  CB  SER A 109     1320   2052   4208   -275    157     73       C  
ATOM    655  OG  SER A 109      73.761  16.905  66.830  1.00 21.14           O  
ANISOU  655  OG  SER A 109     1543   2225   4262   -473    231    -96       O  
ATOM    656  N   SER A 110      75.526  19.510  69.946  1.00 20.48           N  
ANISOU  656  N   SER A 110     1711   1937   4131   -185     91     75       N  
ATOM    657  CA  SER A 110      76.216  19.869  71.184  1.00 21.27           C  
ANISOU  657  CA  SER A 110     1832   2084   4162   -131    -15     79       C  
ATOM    658  C   SER A 110      76.586  18.590  71.938  1.00 21.86           C  
ANISOU  658  C   SER A 110     1829   2198   4276   -142    -44    137       C  
ATOM    659  O   SER A 110      75.854  17.598  71.901  1.00 22.32           O  
ANISOU  659  O   SER A 110     1881   2205   4393   -128   -101    184       O  
ATOM    660  CB  SER A 110      75.346  20.776  72.055  1.00 21.34           C  
ANISOU  660  CB  SER A 110     1931   2050   4126   -193    -74    -45       C  
ATOM    661  OG  SER A 110      76.113  21.212  73.169  1.00 22.05           O  
ANISOU  661  OG  SER A 110     2270   2385   3719     34   -128   -213       O  
ATOM    662  N   GLY A 111      77.730  18.628  72.614  1.00 22.14           N  
ANISOU  662  N   GLY A 111     1732   2279   4400    -95     -8    225       N  
ATOM    663  CA  GLY A 111      78.238  17.490  73.366  1.00 21.49           C  
ANISOU  663  CA  GLY A 111     1734   2073   4358    -61    -27    195       C  
ATOM    664  C   GLY A 111      78.982  16.500  72.492  1.00 21.77           C  
ANISOU  664  C   GLY A 111     1677   2148   4445    -83    -37    195       C  
ATOM    665  O   GLY A 111      79.334  15.417  72.959  1.00 21.33           O  
ANISOU  665  O   GLY A 111     1658   2062   4384    -47    -57    179       O  
ATOM    666  N   HIS A 112      79.213  16.869  71.234  1.00 21.22           N  
ANISOU  666  N   HIS A 112     1607   2040   4415   -120    -45    196       N  
ATOM    667  CA  HIS A 112      79.918  16.018  70.276  1.00 21.45           C  
ANISOU  667  CA  HIS A 112     1594   2018   4538   -181    -49    129       C  
ATOM    668  C   HIS A 112      81.072  16.764  69.629  1.00 21.56           C  
ANISOU  668  C   HIS A 112     1586   2097   4506   -109     -7    167       C  
ATOM    669  O   HIS A 112      81.110  18.007  69.651  1.00 21.05           O  
ANISOU  669  O   HIS A 112     1522   2014   4459   -120    100    188       O  
ATOM    670  CB  HIS A 112      78.970  15.540  69.170  1.00 21.40           C  
ANISOU  670  CB  HIS A 112     1616   2040   4472   -138   -108    154       C  
ATOM    671  CG  HIS A 112      77.816  14.727  69.670  1.00 22.74           C  
ANISOU  671  CG  HIS A 112     1703   1970   4967   -297   -118     24       C  
ATOM    672  ND1 HIS A 112      76.698  15.295  70.246  1.00 23.19           N  
ANISOU  672  ND1 HIS A 112     1784   1846   5181   -291    -95   -182       N  
ATOM    673  CD2 HIS A 112      77.600  13.388  69.665  1.00 21.35           C  
ANISOU  673  CD2 HIS A 112     1492   1545   5075   -170   -267    133       C  
ATOM    674  CE1 HIS A 112      75.859  14.336  70.605  1.00 22.19           C  
ANISOU  674  CE1 HIS A 112     1733   1765   4932   -370   -525   -169       C  
ATOM    675  NE2 HIS A 112      76.382  13.171  70.262  1.00 21.28           N  
ANISOU  675  NE2 HIS A 112     1477   1725   4881   -454   -621   -152       N  
ATOM    676  N   SER A 113      81.981  15.987  69.036  1.00 21.71           N  
ANISOU  676  N   SER A 113     1521   2144   4583    -79    -66    183       N  
ATOM    677  CA  SER A 113      83.098  16.509  68.259  1.00 21.65           C  
ANISOU  677  CA  SER A 113     1481   2204   4538    -52    -99    160       C  
ATOM    678  C   SER A 113      83.046  15.970  66.828  1.00 21.65           C  
ANISOU  678  C   SER A 113     1397   2254   4576    -56   -133    135       C  
ATOM    679  O   SER A 113      82.452  14.925  66.572  1.00 21.78           O  
ANISOU  679  O   SER A 113     1285   2348   4640    -41   -175     47       O  
ATOM    680  CB  SER A 113      84.427  16.112  68.901  1.00 22.08           C  
ANISOU  680  CB  SER A 113     1479   2378   4530   -139    -91     76       C  
ATOM    681  OG  SER A 113      84.480  16.589  70.238  1.00 24.88           O  
ANISOU  681  OG  SER A 113     2188   2585   4677    -76   -176    -26       O  
ATOM    682  N   PHE A 114      83.686  16.679  65.906  1.00 21.57           N  
ANISOU  682  N   PHE A 114     1273   2344   4575     -7   -141    118       N  
ATOM    683  CA  PHE A 114      83.787  16.233  64.519  1.00 21.15           C  
ANISOU  683  CA  PHE A 114     1159   2254   4620     16    -58    106       C  
ATOM    684  C   PHE A 114      85.074  16.792  63.925  1.00 21.48           C  
ANISOU  684  C   PHE A 114     1146   2233   4779     10    -72     94       C  
ATOM    685  O   PHE A 114      85.311  18.010  63.979  1.00 21.77           O  
ANISOU  685  O   PHE A 114     1223   2211   4834    -70    -87    151       O  
ATOM    686  CB  PHE A 114      82.585  16.711  63.696  1.00 20.60           C  
ANISOU  686  CB  PHE A 114     1170   2153   4502     62    -71    120       C  
ATOM    687  CG  PHE A 114      82.631  16.262  62.262  1.00 21.99           C  
ANISOU  687  CG  PHE A 114     1615   2243   4496    -76     -6    199       C  
ATOM    688  CD1 PHE A 114      82.603  14.901  61.947  1.00 22.83           C  
ANISOU  688  CD1 PHE A 114     1626   2496   4549    170     40     15       C  
ATOM    689  CD2 PHE A 114      82.740  17.190  61.233  1.00 22.25           C  
ANISOU  689  CD2 PHE A 114     1655   2366   4433    106   -180    233       C  
ATOM    690  CE1 PHE A 114      82.669  14.464  60.625  1.00 21.76           C  
ANISOU  690  CE1 PHE A 114     1421   2348   4499    103   -108     58       C  
ATOM    691  CE2 PHE A 114      82.815  16.767  59.910  1.00 23.34           C  
ANISOU  691  CE2 PHE A 114     1887   2573   4406    -47    120    243       C  
ATOM    692  CZ  PHE A 114      82.784  15.400  59.604  1.00 22.66           C  
ANISOU  692  CZ  PHE A 114     1408   2628   4570    147     11    237       C  
ATOM    693  N   SER A 115      85.872  15.913  63.327  1.00 20.81           N  
ANISOU  693  N   SER A 115      861   2168   4876     56    -51    100       N  
ATOM    694  CA  SER A 115      87.187  16.306  62.828  1.00 22.15           C  
ANISOU  694  CA  SER A 115     1089   2319   5007    173    105     34       C  
ATOM    695  C   SER A 115      87.172  16.635  61.338  1.00 22.16           C  
ANISOU  695  C   SER A 115     1072   2302   5046    207    236    -48       C  
ATOM    696  O   SER A 115      86.843  15.778  60.510  1.00 23.51           O  
ANISOU  696  O   SER A 115     1440   2327   5165    138    280    -74       O  
ATOM    697  CB  SER A 115      88.226  15.229  63.125  1.00 21.87           C  
ANISOU  697  CB  SER A 115      893   2358   5057    154     54     43       C  
ATOM    698  OG  SER A 115      89.521  15.784  62.962  1.00 23.73           O  
ANISOU  698  OG  SER A 115     1199   2781   5034    167     -8     56       O  
ATOM    699  N   TYR A 116      87.494  17.882  61.006  1.00 21.77           N  
ANISOU  699  N   TYR A 116      993   2180   5096    396    296   -137       N  
ATOM    700  CA  TYR A 116      87.603  18.274  59.611  1.00 21.57           C  
ANISOU  700  CA  TYR A 116      917   2118   5158    452    288   -103       C  
ATOM    701  C   TYR A 116      89.029  18.014  59.160  1.00 22.90           C  
ANISOU  701  C   TYR A 116     1084   2293   5322    422    339   -181       C  
ATOM    702  O   TYR A 116      89.960  18.686  59.617  1.00 22.80           O  
ANISOU  702  O   TYR A 116      875   2393   5394    466    334   -210       O  
ATOM    703  CB  TYR A 116      87.236  19.745  59.425  1.00 20.98           C  
ANISOU  703  CB  TYR A 116      838   2080   5053    344    301   -172       C  
ATOM    704  CG  TYR A 116      85.773  20.071  59.658  1.00 20.51           C  
ANISOU  704  CG  TYR A 116      912   1927   4951    384    350    -34       C  
ATOM    705  CD1 TYR A 116      85.298  20.346  60.939  1.00 19.72           C  
ANISOU  705  CD1 TYR A 116      569   1932   4991    147    801   -177       C  
ATOM    706  CD2 TYR A 116      84.866  20.127  58.601  1.00 17.60           C  
ANISOU  706  CD2 TYR A 116      641   1508   4537     49    267    -57       C  
ATOM    707  CE1 TYR A 116      83.958  20.694  61.154  1.00 19.90           C  
ANISOU  707  CE1 TYR A 116      538   2104   4916    206    282    141       C  
ATOM    708  CE2 TYR A 116      83.531  20.502  58.811  1.00 18.72           C  
ANISOU  708  CE2 TYR A 116      705   1868   4537      6    398    120       C  
ATOM    709  CZ  TYR A 116      83.081  20.776  60.091  1.00 18.94           C  
ANISOU  709  CZ  TYR A 116      498   1989   4709    192    432   -110       C  
ATOM    710  OH  TYR A 116      81.768  21.130  60.353  1.00 16.96           O  
ANISOU  710  OH  TYR A 116      534   1922   3986    340    558     47       O  
ATOM    711  N   ASN A 117      89.189  17.023  58.287  1.00 23.85           N  
ANISOU  711  N   ASN A 117     1196   2351   5515    518    351   -243       N  
ATOM    712  CA  ASN A 117      90.509  16.571  57.850  1.00 24.49           C  
ANISOU  712  CA  ASN A 117     1286   2444   5575    425    439   -250       C  
ATOM    713  C   ASN A 117      90.653  16.824  56.361  1.00 25.00           C  
ANISOU  713  C   ASN A 117     1374   2500   5624    439    511   -292       C  
ATOM    714  O   ASN A 117      89.986  16.185  55.540  1.00 26.02           O  
ANISOU  714  O   ASN A 117     1618   2626   5642    440    573   -312       O  
ATOM    715  CB  ASN A 117      90.707  15.083  58.154  1.00 24.30           C  
ANISOU  715  CB  ASN A 117     1214   2391   5625    359    422   -205       C  
ATOM    716  CG  ASN A 117      90.366  14.727  59.590  1.00 25.74           C  
ANISOU  716  CG  ASN A 117     1600   2440   5738    275    227   -214       C  
ATOM    717  OD1 ASN A 117      90.550  15.530  60.511  1.00 24.88           O  
ANISOU  717  OD1 ASN A 117     1171   2290   5992    247     57   -216       O  
ATOM    718  ND2 ASN A 117      89.840  13.517  59.785  1.00 28.03           N  
ANISOU  718  ND2 ASN A 117     2335   2493   5821    257    211    -20       N  
ATOM    719  N   PHE A 118      91.506  17.784  56.019  1.00 25.45           N  
ANISOU  719  N   PHE A 118     1447   2566   5654    497    548   -351       N  
ATOM    720  CA  PHE A 118      91.609  18.199  54.627  1.00 25.85           C  
ANISOU  720  CA  PHE A 118     1481   2693   5649    438    528   -372       C  
ATOM    721  C   PHE A 118      92.991  18.767  54.378  1.00 26.25           C  
ANISOU  721  C   PHE A 118     1436   2815   5723    452    535   -454       C  
ATOM    722  O   PHE A 118      93.752  18.995  55.324  1.00 26.28           O  
ANISOU  722  O   PHE A 118     1539   2823   5624    304    516   -479       O  
ATOM    723  CB  PHE A 118      90.510  19.213  54.259  1.00 25.33           C  
ANISOU  723  CB  PHE A 118     1288   2674   5660    446    531   -424       C  
ATOM    724  CG  PHE A 118      90.533  20.479  55.079  1.00 25.04           C  
ANISOU  724  CG  PHE A 118     1271   2698   5544    414    439   -326       C  
ATOM    725  CD1 PHE A 118      91.297  21.568  54.681  1.00 25.65           C  
ANISOU  725  CD1 PHE A 118     1468   2708   5566    307    371   -337       C  
ATOM    726  CD2 PHE A 118      89.791  20.582  56.245  1.00 24.14           C  
ANISOU  726  CD2 PHE A 118     1007   2700   5462    465    351   -317       C  
ATOM    727  CE1 PHE A 118      91.324  22.743  55.435  1.00 25.18           C  
ANISOU  727  CE1 PHE A 118     1164   2838   5562    363    416   -262       C  
ATOM    728  CE2 PHE A 118      89.810  21.748  57.008  1.00 24.25           C  
ANISOU  728  CE2 PHE A 118     1109   2766   5338    254    137   -250       C  
ATOM    729  CZ  PHE A 118      90.583  22.831  56.604  1.00 25.09           C  
ANISOU  729  CZ  PHE A 118     1383   2845   5302    365    394   -303       C  
ATOM    730  N   GLN A 119      93.299  19.004  53.107  1.00 26.75           N  
ANISOU  730  N   GLN A 119     1544   2916   5704    445    540   -509       N  
ATOM    731  CA  GLN A 119      94.643  19.422  52.720  1.00 27.88           C  
ANISOU  731  CA  GLN A 119     1600   3085   5906    464    559   -546       C  
ATOM    732  C   GLN A 119      94.643  20.783  52.019  1.00 28.49           C  
ANISOU  732  C   GLN A 119     1721   3141   5961    451    540   -576       C  
ATOM    733  O   GLN A 119      93.741  21.072  51.223  1.00 28.73           O  
ANISOU  733  O   GLN A 119     1714   3253   5947    414    475   -559       O  
ATOM    734  CB  GLN A 119      95.300  18.357  51.834  1.00 28.01           C  
ANISOU  734  CB  GLN A 119     1661   3160   5820    494    586   -555       C  
ATOM    735  CG  GLN A 119      96.788  18.637  51.588  1.00 29.03           C  
ANISOU  735  CG  GLN A 119     1544   3447   6037    584    655   -677       C  
ATOM    736  CD  GLN A 119      97.442  17.764  50.530  1.00 30.86           C  
ANISOU  736  CD  GLN A 119     1799   3423   6500    619    510   -936       C  
ATOM    737  OE1 GLN A 119      96.776  17.041  49.793  1.00 31.12           O  
ANISOU  737  OE1 GLN A 119     2064   3362   6398    905    382  -1179       O  
ATOM    738  NE2 GLN A 119      98.766  17.860  50.427  1.00 31.39           N  
ANISOU  738  NE2 GLN A 119     1733   3739   6454   1079    671  -1095       N  
ATOM    739  N   ALA A 120      95.632  21.619  52.344  1.00 28.46           N  
ANISOU  739  N   ALA A 120     1679   3104   6030    417    550   -640       N  
ATOM    740  CA  ALA A 120      95.881  22.852  51.600  1.00 29.59           C  
ANISOU  740  CA  ALA A 120     1916   3210   6117    398    605   -722       C  
ATOM    741  C   ALA A 120      96.678  22.486  50.351  1.00 30.26           C  
ANISOU  741  C   ALA A 120     2050   3253   6194    404    649   -772       C  
ATOM    742  O   ALA A 120      97.846  22.852  50.202  1.00 30.54           O  
ANISOU  742  O   ALA A 120     2185   3228   6188    357    652   -792       O  
ATOM    743  CB  ALA A 120      96.634  23.888  52.457  1.00 29.36           C  
ANISOU  743  CB  ALA A 120     1912   3136   6108    417    590   -712       C  
ATOM    744  N   LYS A 121      96.029  21.738  49.466  1.00 31.25           N  
ANISOU  744  N   LYS A 121     2241   3370   6260    373    674   -827       N  
ATOM    745  CA  LYS A 121      96.675  21.152  48.300  1.00 31.87           C  
ANISOU  745  CA  LYS A 121     2364   3422   6324    360    752   -862       C  
ATOM    746  C   LYS A 121      96.840  22.222  47.229  1.00 31.77           C  
ANISOU  746  C   LYS A 121     2319   3427   6325    392    788   -837       C  
ATOM    747  O   LYS A 121      95.851  22.746  46.703  1.00 31.21           O  
ANISOU  747  O   LYS A 121     2237   3331   6289    422    827   -815       O  
ATOM    748  CB  LYS A 121      95.847  19.984  47.762  1.00 32.43           C  
ANISOU  748  CB  LYS A 121     2471   3442   6408    317    741   -871       C  
ATOM    749  CG  LYS A 121      96.472  19.376  46.526  1.00 35.71           C  
ANISOU  749  CG  LYS A 121     3255   3706   6607    199    743  -1049       C  
ATOM    750  CD  LYS A 121      95.658  18.244  45.943  1.00 40.49           C  
ANISOU  750  CD  LYS A 121     4064   4130   7189     89    576  -1323       C  
ATOM    751  CE  LYS A 121      96.597  17.351  45.138  1.00 43.43           C  
ANISOU  751  CE  LYS A 121     4605   4440   7456    223    663  -1530       C  
ATOM    752  NZ  LYS A 121      95.822  16.398  44.300  1.00 45.75           N  
ANISOU  752  NZ  LYS A 121     4900   4736   7746    267    374  -1639       N  
ATOM    753  N   ASP A 122      98.094  22.554  46.937  1.00 31.57           N  
ANISOU  753  N   ASP A 122     2284   3417   6294    484    880   -864       N  
ATOM    754  CA  ASP A 122      98.421  23.613  45.984  1.00 32.29           C  
ANISOU  754  CA  ASP A 122     2369   3574   6324    496    913   -809       C  
ATOM    755  C   ASP A 122      97.763  24.950  46.352  1.00 31.23           C  
ANISOU  755  C   ASP A 122     2178   3491   6195    486    928   -764       C  
ATOM    756  O   ASP A 122      97.456  25.757  45.471  1.00 31.89           O  
ANISOU  756  O   ASP A 122     2350   3555   6208    502    952   -732       O  
ATOM    757  CB  ASP A 122      98.011  23.207  44.564  1.00 33.57           C  
ANISOU  757  CB  ASP A 122     2626   3737   6390    487    903   -822       C  
ATOM    758  CG  ASP A 122      98.796  22.013  44.041  1.00 37.81           C  
ANISOU  758  CG  ASP A 122     3229   4384   6751    505    961   -931       C  
ATOM    759  OD1 ASP A 122     100.026  21.956  44.259  1.00 42.09           O  
ANISOU  759  OD1 ASP A 122     3641   5292   7057    641    916   -880       O  
ATOM    760  OD2 ASP A 122      98.179  21.124  43.409  1.00 43.66           O  
ANISOU  760  OD2 ASP A 122     4559   4962   7065    333    727  -1116       O  
ATOM    761  N   GLN A 123      97.509  25.182  47.637  1.00 29.27           N  
ANISOU  761  N   GLN A 123     1759   3342   6020    426    882   -704       N  
ATOM    762  CA  GLN A 123      96.946  26.464  48.051  1.00 27.15           C  
ANISOU  762  CA  GLN A 123     1283   3208   5824    428    883   -680       C  
ATOM    763  C   GLN A 123      97.787  27.092  49.144  1.00 26.77           C  
ANISOU  763  C   GLN A 123     1208   3116   5845    462    845   -622       C  
ATOM    764  O   GLN A 123      98.262  26.402  50.046  1.00 27.20           O  
ANISOU  764  O   GLN A 123     1302   3038   5994    488    794   -641       O  
ATOM    765  CB  GLN A 123      95.504  26.331  48.565  1.00 27.03           C  
ANISOU  765  CB  GLN A 123     1231   3290   5749    315    793   -657       C  
ATOM    766  CG  GLN A 123      94.499  26.032  47.477  1.00 25.93           C  
ANISOU  766  CG  GLN A 123     1139   3169   5541    333    792   -616       C  
ATOM    767  CD  GLN A 123      93.098  26.100  48.016  1.00 24.91           C  
ANISOU  767  CD  GLN A 123     1222   3247   4993    182    554   -735       C  
ATOM    768  OE1 GLN A 123      92.577  25.107  48.533  1.00 24.63           O  
ANISOU  768  OE1 GLN A 123     1324   3315   4718    -39    819   -793       O  
ATOM    769  NE2 GLN A 123      92.497  27.286  47.950  1.00 24.33           N  
ANISOU  769  NE2 GLN A 123     1532   3118   4592    347    331   -573       N  
ATOM    770  N   ALA A 124      97.943  28.408  49.074  1.00 25.94           N  
ANISOU  770  N   ALA A 124     1096   2985   5773    486    767   -558       N  
ATOM    771  CA  ALA A 124      98.583  29.150  50.151  1.00 25.61           C  
ANISOU  771  CA  ALA A 124     1169   2935   5626    555    744   -522       C  
ATOM    772  C   ALA A 124      98.103  30.588  50.050  1.00 25.72           C  
ANISOU  772  C   ALA A 124     1335   2923   5513    577    728   -526       C  
ATOM    773  O   ALA A 124      97.939  31.123  48.947  1.00 26.94           O  
ANISOU  773  O   ALA A 124     1745   2863   5627    662    608   -570       O  
ATOM    774  CB  ALA A 124     100.135  29.077  50.046  1.00 25.32           C  
ANISOU  774  CB  ALA A 124      946   3011   5661    628    720   -491       C  
ATOM    775  N   GLY A 125      97.909  31.222  51.198  1.00 24.41           N  
ANISOU  775  N   GLY A 125     1160   2868   5244    508    867   -457       N  
ATOM    776  CA  GLY A 125      97.437  32.601  51.218  1.00 22.76           C  
ANISOU  776  CA  GLY A 125      882   2775   4991    502    805   -392       C  
ATOM    777  C   GLY A 125      96.554  32.838  52.426  1.00 22.32           C  
ANISOU  777  C   GLY A 125      911   2736   4832    414    697   -351       C  
ATOM    778  O   GLY A 125      96.671  32.147  53.440  1.00 22.81           O  
ANISOU  778  O   GLY A 125      948   2783   4934    455    683   -337       O  
ATOM    779  N   THR A 126      95.670  33.823  52.304  1.00 20.45           N  
ANISOU  779  N   THR A 126      668   2577   4524    315    585   -382       N  
ATOM    780  CA  THR A 126      94.862  34.276  53.427  1.00 19.45           C  
ANISOU  780  CA  THR A 126      649   2413   4328    235    503   -300       C  
ATOM    781  C   THR A 126      93.429  33.766  53.297  1.00 19.38           C  
ANISOU  781  C   THR A 126      744   2431   4186    179    447   -245       C  
ATOM    782  O   THR A 126      92.772  33.979  52.268  1.00 19.21           O  
ANISOU  782  O   THR A 126      903   2446   3947    285    464   -296       O  
ATOM    783  CB  THR A 126      94.897  35.821  53.548  1.00 19.33           C  
ANISOU  783  CB  THR A 126      656   2373   4313    160    538   -286       C  
ATOM    784  OG1 THR A 126      96.253  36.289  53.444  1.00 19.44           O  
ANISOU  784  OG1 THR A 126      818   2296   4272    201    310    -61       O  
ATOM    785  CG2 THR A 126      94.293  36.257  54.873  1.00 17.75           C  
ANISOU  785  CG2 THR A 126      467   1889   4388    210    443   -593       C  
ATOM    786  N   PHE A 127      92.955  33.108  54.356  1.00 18.46           N  
ANISOU  786  N   PHE A 127      702   2354   3957    177    435   -203       N  
ATOM    787  CA  PHE A 127      91.642  32.465  54.342  1.00 18.78           C  
ANISOU  787  CA  PHE A 127      892   2282   3960    152    468   -139       C  
ATOM    788  C   PHE A 127      90.916  32.872  55.613  1.00 18.54           C  
ANISOU  788  C   PHE A 127      813   2249   3980    126    394   -124       C  
ATOM    789  O   PHE A 127      91.414  33.693  56.399  1.00 18.67           O  
ANISOU  789  O   PHE A 127      925   2192   3974    213    436    -30       O  
ATOM    790  CB  PHE A 127      91.795  30.932  54.301  1.00 19.16           C  
ANISOU  790  CB  PHE A 127      983   2400   3896    163    413   -273       C  
ATOM    791  CG  PHE A 127      92.558  30.415  53.111  1.00 20.86           C  
ANISOU  791  CG  PHE A 127     1436   2367   4121    292    432   -239       C  
ATOM    792  CD1 PHE A 127      93.942  30.296  53.148  1.00 20.38           C  
ANISOU  792  CD1 PHE A 127     1401   2312   4029    346    530   -233       C  
ATOM    793  CD2 PHE A 127      91.882  30.031  51.955  1.00 22.35           C  
ANISOU  793  CD2 PHE A 127     1620   2671   4198    297    390   -426       C  
ATOM    794  CE1 PHE A 127      94.649  29.793  52.061  1.00 21.78           C  
ANISOU  794  CE1 PHE A 127     1703   2582   3990    171    471    -53       C  
ATOM    795  CE2 PHE A 127      92.586  29.544  50.850  1.00 22.96           C  
ANISOU  795  CE2 PHE A 127     1607   2585   4532    208    660   -425       C  
ATOM    796  CZ  PHE A 127      93.977  29.410  50.915  1.00 22.08           C  
ANISOU  796  CZ  PHE A 127     1568   2615   4204    348    273   -343       C  
ATOM    797  N   TRP A 128      89.735  32.293  55.827  1.00 18.27           N  
ANISOU  797  N   TRP A 128      824   2200   3917    119    414    -65       N  
ATOM    798  CA  TRP A 128      89.092  32.419  57.127  1.00 17.21           C  
ANISOU  798  CA  TRP A 128      734   2027   3775    108    309   -113       C  
ATOM    799  C   TRP A 128      88.150  31.255  57.384  1.00 17.23           C  
ANISOU  799  C   TRP A 128      816   2080   3649     42    228    -66       C  
ATOM    800  O   TRP A 128      87.916  30.443  56.495  1.00 18.38           O  
ANISOU  800  O   TRP A 128     1139   2107   3737     25    166    -35       O  
ATOM    801  CB  TRP A 128      88.377  33.767  57.276  1.00 16.24           C  
ANISOU  801  CB  TRP A 128      479   1967   3725    174    252    -65       C  
ATOM    802  CG  TRP A 128      87.223  34.056  56.370  1.00 17.18           C  
ANISOU  802  CG  TRP A 128      680   1995   3850    211    231   -239       C  
ATOM    803  CD1 TRP A 128      87.236  34.139  55.008  1.00 15.75           C  
ANISOU  803  CD1 TRP A 128      314   2023   3648    172    203   -227       C  
ATOM    804  CD2 TRP A 128      85.895  34.417  56.783  1.00 16.27           C  
ANISOU  804  CD2 TRP A 128      330   2015   3837    213     97   -316       C  
ATOM    805  NE1 TRP A 128      85.991  34.512  54.543  1.00 16.95           N  
ANISOU  805  NE1 TRP A 128      393   1941   4104    306    307   -206       N  
ATOM    806  CE2 TRP A 128      85.149  34.679  55.614  1.00 17.22           C  
ANISOU  806  CE2 TRP A 128      575   2023   3942    229    145   -259       C  
ATOM    807  CE3 TRP A 128      85.257  34.518  58.028  1.00 16.62           C  
ANISOU  807  CE3 TRP A 128      410   1937   3967     95    -70   -489       C  
ATOM    808  CZ2 TRP A 128      83.804  35.057  55.655  1.00 16.35           C  
ANISOU  808  CZ2 TRP A 128      356   1951   3903    -28    350   -344       C  
ATOM    809  CZ3 TRP A 128      83.928  34.933  58.069  1.00 17.13           C  
ANISOU  809  CZ3 TRP A 128      523   1999   3985   -110     32   -362       C  
ATOM    810  CH2 TRP A 128      83.212  35.175  56.887  1.00 17.41           C  
ANISOU  810  CH2 TRP A 128      614   2028   3971    -91     54   -365       C  
ATOM    811  N   TYR A 129      87.628  31.161  58.602  1.00 16.43           N  
ANISOU  811  N   TYR A 129      649   2104   3489     48    125    -81       N  
ATOM    812  CA  TYR A 129      86.688  30.106  58.907  1.00 15.62           C  
ANISOU  812  CA  TYR A 129      462   2117   3353     66     96    -33       C  
ATOM    813  C   TYR A 129      85.503  30.711  59.640  1.00 15.83           C  
ANISOU  813  C   TYR A 129      491   2176   3345     19    141   -105       C  
ATOM    814  O   TYR A 129      85.642  31.692  60.392  1.00 15.47           O  
ANISOU  814  O   TYR A 129      303   2283   3290    -20    234    -86       O  
ATOM    815  CB  TYR A 129      87.332  28.997  59.747  1.00 15.67           C  
ANISOU  815  CB  TYR A 129      646   2090   3218     83    -18   -102       C  
ATOM    816  CG  TYR A 129      87.822  29.447  61.103  1.00 16.14           C  
ANISOU  816  CG  TYR A 129      681   2286   3165    102   -265    222       C  
ATOM    817  CD1 TYR A 129      89.038  30.099  61.240  1.00 14.83           C  
ANISOU  817  CD1 TYR A 129      605   2107   2922    -63   -246    136       C  
ATOM    818  CD2 TYR A 129      87.051  29.238  62.250  1.00 15.81           C  
ANISOU  818  CD2 TYR A 129      721   2498   2788     48   -362    176       C  
ATOM    819  CE1 TYR A 129      89.500  30.496  62.491  1.00 15.63           C  
ANISOU  819  CE1 TYR A 129      699   2103   3136     61   -327     19       C  
ATOM    820  CE2 TYR A 129      87.507  29.631  63.505  1.00 17.02           C  
ANISOU  820  CE2 TYR A 129      665   2432   3367   -117   -667    -51       C  
ATOM    821  CZ  TYR A 129      88.727  30.278  63.604  1.00 16.71           C  
ANISOU  821  CZ  TYR A 129      758   2383   3208    -57   -524      0       C  
ATOM    822  OH  TYR A 129      89.203  30.661  64.833  1.00 16.92           O  
ANISOU  822  OH  TYR A 129      643   2564   3218    -87   -280   -411       O  
ATOM    823  N   HIS A 130      84.347  30.084  59.455  1.00 14.81           N  
ANISOU  823  N   HIS A 130      292   2192   3140     35     51    -37       N  
ATOM    824  CA  HIS A 130      83.132  30.627  60.067  1.00 14.78           C  
ANISOU  824  CA  HIS A 130      463   2073   3078     13    174   -147       C  
ATOM    825  C   HIS A 130      82.070  29.546  60.174  1.00 15.22           C  
ANISOU  825  C   HIS A 130      458   2047   3278    -12    195   -177       C  
ATOM    826  O   HIS A 130      82.063  28.613  59.367  1.00 14.95           O  
ANISOU  826  O   HIS A 130      348   1901   3429     47    191   -294       O  
ATOM    827  CB  HIS A 130      82.572  31.859  59.320  1.00 13.43           C  
ANISOU  827  CB  HIS A 130      401   2017   2682    152     -4   -243       C  
ATOM    828  CG  HIS A 130      82.335  31.665  57.846  1.00 15.15           C  
ANISOU  828  CG  HIS A 130      935   2393   2429    253    435   -399       C  
ATOM    829  ND1 HIS A 130      81.129  31.240  57.329  1.00 14.33           N  
ANISOU  829  ND1 HIS A 130     1531   2477   1434    248    442   -455       N  
ATOM    830  CD2 HIS A 130      83.121  31.934  56.776  1.00 15.31           C  
ANISOU  830  CD2 HIS A 130     1179   2330   2305    290    589   -897       C  
ATOM    831  CE1 HIS A 130      81.203  31.208  56.005  1.00 16.19           C  
ANISOU  831  CE1 HIS A 130     1555   2794   1800    407    853   -811       C  
ATOM    832  NE2 HIS A 130      82.398  31.646  55.643  1.00 14.76           N  
ANISOU  832  NE2 HIS A 130     1004   2548   2053    667    578   -732       N  
ATOM    833  N   SER A 131      81.157  29.700  61.133  1.00 15.33           N  
ANISOU  833  N   SER A 131      597   1945   3280   -111    300    -76       N  
ATOM    834  CA  SER A 131      79.963  28.857  61.128  1.00 15.29           C  
ANISOU  834  CA  SER A 131      443   2000   3367   -140    198   -200       C  
ATOM    835  C   SER A 131      79.246  29.012  59.797  1.00 16.07           C  
ANISOU  835  C   SER A 131      599   2064   3442    -61    214   -138       C  
ATOM    836  O   SER A 131      79.144  30.134  59.282  1.00 16.18           O  
ANISOU  836  O   SER A 131      484   2103   3561   -105    250   -154       O  
ATOM    837  CB  SER A 131      78.972  29.258  62.209  1.00 14.33           C  
ANISOU  837  CB  SER A 131      329   1867   3247   -199    242   -125       C  
ATOM    838  OG  SER A 131      77.832  28.410  62.074  1.00 16.35           O  
ANISOU  838  OG  SER A 131      868   1928   3416    -95    172   -520       O  
ATOM    839  N   HIS A 132      78.758  27.902  59.248  1.00 16.24           N  
ANISOU  839  N   HIS A 132      565   2087   3517   -125    149   -118       N  
ATOM    840  CA  HIS A 132      77.935  27.955  58.040  1.00 17.11           C  
ANISOU  840  CA  HIS A 132      830   2153   3517    -92    246   -108       C  
ATOM    841  C   HIS A 132      76.578  27.345  58.364  1.00 17.84           C  
ANISOU  841  C   HIS A 132      928   2268   3582   -123    127   -153       C  
ATOM    842  O   HIS A 132      75.999  26.660  57.533  1.00 19.61           O  
ANISOU  842  O   HIS A 132     1098   2566   3785   -335    112   -136       O  
ATOM    843  CB  HIS A 132      78.607  27.226  56.869  1.00 17.52           C  
ANISOU  843  CB  HIS A 132     1061   2072   3523     -8    204   -148       C  
ATOM    844  CG  HIS A 132      78.315  27.819  55.524  1.00 19.77           C  
ANISOU  844  CG  HIS A 132     1412   2394   3706    253    200   -151       C  
ATOM    845  ND1 HIS A 132      77.042  27.878  54.996  1.00 19.76           N  
ANISOU  845  ND1 HIS A 132     1606   2192   3707    452    183   -386       N  
ATOM    846  CD2 HIS A 132      79.139  28.343  54.580  1.00 20.15           C  
ANISOU  846  CD2 HIS A 132     1416   2483   3754    435    425    -51       C  
ATOM    847  CE1 HIS A 132      77.096  28.437  53.797  1.00 22.67           C  
ANISOU  847  CE1 HIS A 132     2011   2758   3842    536    318   -232       C  
ATOM    848  NE2 HIS A 132      78.356  28.726  53.515  1.00 21.98           N  
ANISOU  848  NE2 HIS A 132     1721   2812   3816    352    353    -73       N  
ATOM    849  N   LEU A 133      76.102  27.556  59.586  1.00 16.65           N  
ANISOU  849  N   LEU A 133      731   2113   3479     21    282   -115       N  
ATOM    850  CA  LEU A 133      74.752  27.153  59.976  1.00 17.29           C  
ANISOU  850  CA  LEU A 133      919   2086   3562     57    168    -91       C  
ATOM    851  C   LEU A 133      73.946  28.426  60.222  1.00 17.87           C  
ANISOU  851  C   LEU A 133      926   2195   3669     81    168   -127       C  
ATOM    852  O   LEU A 133      74.271  29.193  61.131  1.00 18.30           O  
ANISOU  852  O   LEU A 133      968   2242   3740     94    -15   -158       O  
ATOM    853  CB  LEU A 133      74.820  26.322  61.261  1.00 17.43           C  
ANISOU  853  CB  LEU A 133     1015   2190   3416     24    205   -131       C  
ATOM    854  CG  LEU A 133      73.509  25.873  61.912  1.00 17.20           C  
ANISOU  854  CG  LEU A 133     1036   2309   3188    -36    103   -128       C  
ATOM    855  CD1 LEU A 133      72.722  24.950  61.008  1.00 18.49           C  
ANISOU  855  CD1 LEU A 133     1246   2518   3259   -164   -168   -277       C  
ATOM    856  CD2 LEU A 133      73.769  25.191  63.248  1.00 17.71           C  
ANISOU  856  CD2 LEU A 133     1171   2438   3120    237   -102     15       C  
ATOM    857  N   SER A 134      72.919  28.658  59.407  1.00 17.87           N  
ANISOU  857  N   SER A 134     1036   2131   3622    125    102    -24       N  
ATOM    858  CA  SER A 134      72.071  29.848  59.518  1.00 17.68           C  
ANISOU  858  CA  SER A 134     1015   2058   3644    151    231    -82       C  
ATOM    859  C   SER A 134      72.937  31.108  59.688  1.00 18.36           C  
ANISOU  859  C   SER A 134     1141   2121   3713    135    172    -66       C  
ATOM    860  O   SER A 134      73.941  31.264  58.982  1.00 18.13           O  
ANISOU  860  O   SER A 134     1066   2108   3715    102    158     47       O  
ATOM    861  CB  SER A 134      71.041  29.673  60.644  1.00 17.66           C  
ANISOU  861  CB  SER A 134     1092   2056   3559    255    225    -85       C  
ATOM    862  OG  SER A 134      70.098  30.743  60.686  1.00 17.09           O  
ANISOU  862  OG  SER A 134      929   2153   3411    293     63   -213       O  
ATOM    863  N   THR A 135      72.586  31.987  60.625  1.00 18.22           N  
ANISOU  863  N   THR A 135     1119   1966   3837    226    159    -54       N  
ATOM    864  CA  THR A 135      73.348  33.235  60.826  1.00 17.98           C  
ANISOU  864  CA  THR A 135      998   2026   3805    290     13      5       C  
ATOM    865  C   THR A 135      74.275  33.172  62.036  1.00 17.82           C  
ANISOU  865  C   THR A 135      923   1958   3891    268    114    -20       C  
ATOM    866  O   THR A 135      74.649  34.189  62.625  1.00 17.40           O  
ANISOU  866  O   THR A 135      658   2038   3914    213    -27    -41       O  
ATOM    867  CB  THR A 135      72.402  34.447  60.948  1.00 18.68           C  
ANISOU  867  CB  THR A 135     1183   2067   3847    331     52      6       C  
ATOM    868  OG1 THR A 135      71.363  34.165  61.899  1.00 17.31           O  
ANISOU  868  OG1 THR A 135      890   2100   3584    136   -134    -44       O  
ATOM    869  CG2 THR A 135      71.764  34.768  59.577  1.00 18.40           C  
ANISOU  869  CG2 THR A 135     1141   2104   3745    421   -176    227       C  
ATOM    870  N   GLN A 136      74.682  31.962  62.392  1.00 16.99           N  
ANISOU  870  N   GLN A 136      868   1847   3738    295     89    168       N  
ATOM    871  CA  GLN A 136      75.455  31.787  63.603  1.00 16.66           C  
ANISOU  871  CA  GLN A 136      797   1820   3711    174    108    138       C  
ATOM    872  C   GLN A 136      76.825  32.453  63.521  1.00 15.93           C  
ANISOU  872  C   GLN A 136      670   1830   3552    176    180    174       C  
ATOM    873  O   GLN A 136      77.362  32.848  64.552  1.00 16.60           O  
ANISOU  873  O   GLN A 136      910   1733   3662    123    308    105       O  
ATOM    874  CB  GLN A 136      75.604  30.299  63.925  1.00 16.63           C  
ANISOU  874  CB  GLN A 136      836   1806   3676    251     90    233       C  
ATOM    875  CG  GLN A 136      76.279  29.987  65.249  1.00 16.26           C  
ANISOU  875  CG  GLN A 136      868   1642   3665    188    197    295       C  
ATOM    876  CD  GLN A 136      76.441  28.484  65.424  1.00 18.47           C  
ANISOU  876  CD  GLN A 136     1136   1797   4082     99    141    391       C  
ATOM    877  OE1 GLN A 136      77.117  27.813  64.631  1.00 18.76           O  
ANISOU  877  OE1 GLN A 136     1186   1829   4113   -101    -84     43       O  
ATOM    878  NE2 GLN A 136      75.815  27.949  66.463  1.00 16.52           N  
ANISOU  878  NE2 GLN A 136      682   1737   3858   -130    -51    549       N  
ATOM    879  N   TYR A 137      77.424  32.603  62.344  1.00 15.20           N  
ANISOU  879  N   TYR A 137      533   1799   3442    136    138    147       N  
ATOM    880  CA  TYR A 137      78.721  33.279  62.371  1.00 15.27           C  
ANISOU  880  CA  TYR A 137      498   1886   3416     98    129     88       C  
ATOM    881  C   TYR A 137      78.638  34.742  62.822  1.00 15.88           C  
ANISOU  881  C   TYR A 137      558   1968   3507     80     90    141       C  
ATOM    882  O   TYR A 137      79.606  35.284  63.381  1.00 15.68           O  
ANISOU  882  O   TYR A 137      560   1778   3618     99   -112    109       O  
ATOM    883  CB  TYR A 137      79.553  33.029  61.102  1.00 14.54           C  
ANISOU  883  CB  TYR A 137      303   2005   3216    -62    211    143       C  
ATOM    884  CG  TYR A 137      79.465  33.984  59.926  1.00 15.85           C  
ANISOU  884  CG  TYR A 137      690   1820   3509    181   -134    122       C  
ATOM    885  CD1 TYR A 137      80.076  35.238  59.957  1.00 16.74           C  
ANISOU  885  CD1 TYR A 137     1228   1848   3282    169   -118     86       C  
ATOM    886  CD2 TYR A 137      78.939  33.548  58.716  1.00 17.04           C  
ANISOU  886  CD2 TYR A 137     1093   1806   3572     71   -174     40       C  
ATOM    887  CE1 TYR A 137      80.050  36.091  58.854  1.00 15.29           C  
ANISOU  887  CE1 TYR A 137      657   1906   3246    238   -327    108       C  
ATOM    888  CE2 TYR A 137      78.928  34.367  57.586  1.00 18.15           C  
ANISOU  888  CE2 TYR A 137     1095   1835   3965    307    -63    254       C  
ATOM    889  CZ  TYR A 137      79.497  35.636  57.664  1.00 17.06           C  
ANISOU  889  CZ  TYR A 137     1062   1940   3477     87   -168     41       C  
ATOM    890  OH  TYR A 137      79.477  36.464  56.564  1.00 17.41           O  
ANISOU  890  OH  TYR A 137      995   2198   3419     65     77    -99       O  
ATOM    891  N   CYS A 138      77.462  35.345  62.665  1.00 15.94           N  
ANISOU  891  N   CYS A 138      624   2002   3430    149     56    180       N  
ATOM    892  CA  CYS A 138      77.282  36.730  63.096  1.00 17.70           C  
ANISOU  892  CA  CYS A 138      849   2220   3656    211     60     51       C  
ATOM    893  C   CYS A 138      77.360  36.814  64.622  1.00 16.71           C  
ANISOU  893  C   CYS A 138      619   2152   3578     84     79      5       C  
ATOM    894  O   CYS A 138      77.791  37.829  65.162  1.00 17.65           O  
ANISOU  894  O   CYS A 138      876   2171   3658   -111    233     12       O  
ATOM    895  CB  CYS A 138      75.947  37.304  62.595  1.00 18.68           C  
ANISOU  895  CB  CYS A 138      786   2504   3805    192     58    139       C  
ATOM    896  SG  CYS A 138      75.683  37.057  60.816  1.00 23.12           S  
ANISOU  896  SG  CYS A 138     1596   2799   4390     88    132    200       S  
ATOM    897  N   ASP A 139      76.971  35.748  65.313  1.00 15.70           N  
ANISOU  897  N   ASP A 139      374   2041   3548     52     58    -39       N  
ATOM    898  CA  ASP A 139      77.031  35.698  66.773  1.00 15.81           C  
ANISOU  898  CA  ASP A 139      315   2099   3593     13     54    -28       C  
ATOM    899  C   ASP A 139      78.426  35.410  67.344  1.00 16.04           C  
ANISOU  899  C   ASP A 139      405   2003   3683     55    -18     12       C  
ATOM    900  O   ASP A 139      78.603  35.356  68.568  1.00 16.85           O  
ANISOU  900  O   ASP A 139      482   2079   3841     -9    -87     -3       O  
ATOM    901  CB  ASP A 139      76.020  34.682  67.321  1.00 15.33           C  
ANISOU  901  CB  ASP A 139      330   2059   3436   -158     93    -85       C  
ATOM    902  CG  ASP A 139      74.580  35.206  67.287  1.00 15.97           C  
ANISOU  902  CG  ASP A 139      486   2135   3445    -55    -96    -46       C  
ATOM    903  OD1 ASP A 139      74.362  36.431  67.478  1.00 16.33           O  
ANISOU  903  OD1 ASP A 139      571   2440   3193    143    -10    243       O  
ATOM    904  OD2 ASP A 139      73.650  34.394  67.065  1.00 15.78           O  
ANISOU  904  OD2 ASP A 139      716   2427   2850   -331   -392      3       O  
ATOM    905  N   GLY A 140      79.416  35.247  66.468  1.00 16.12           N  
ANISOU  905  N   GLY A 140      319   1972   3833    215    -65     -1       N  
ATOM    906  CA  GLY A 140      80.813  35.255  66.914  1.00 16.68           C  
ANISOU  906  CA  GLY A 140      439   2051   3844    231   -101    -78       C  
ATOM    907  C   GLY A 140      81.698  34.160  66.357  1.00 17.11           C  
ANISOU  907  C   GLY A 140      511   2099   3888    227    -88   -135       C  
ATOM    908  O   GLY A 140      82.927  34.230  66.515  1.00 17.54           O  
ANISOU  908  O   GLY A 140      474   2280   3908    270    -79   -220       O  
ATOM    909  N   LEU A 141      81.109  33.152  65.708  1.00 16.64           N  
ANISOU  909  N   LEU A 141      551   1899   3869    218    -81   -128       N  
ATOM    910  CA  LEU A 141      81.923  31.993  65.291  1.00 16.85           C  
ANISOU  910  CA  LEU A 141      641   1907   3854     93    -11   -171       C  
ATOM    911  C   LEU A 141      82.598  32.290  63.955  1.00 16.73           C  
ANISOU  911  C   LEU A 141      500   2006   3848    104     -2    -94       C  
ATOM    912  O   LEU A 141      82.068  31.920  62.908  1.00 17.04           O  
ANISOU  912  O   LEU A 141      622   2034   3819    101    -37   -148       O  
ATOM    913  CB  LEU A 141      81.073  30.710  65.167  1.00 16.95           C  
ANISOU  913  CB  LEU A 141      854   1721   3862    149     17    -91       C  
ATOM    914  CG  LEU A 141      81.891  29.440  65.477  1.00 16.98           C  
ANISOU  914  CG  LEU A 141      910   1531   4009     92     53   -204       C  
ATOM    915  CD1 LEU A 141      81.009  28.199  65.423  1.00 17.54           C  
ANISOU  915  CD1 LEU A 141     1275   1673   3714   -174   -263   -121       C  
ATOM    916  CD2 LEU A 141      83.059  29.285  64.517  1.00 17.85           C  
ANISOU  916  CD2 LEU A 141     1020   1680   4080    334     24   -213       C  
ATOM    917  N   ARG A 142      83.746  32.961  63.993  1.00 17.26           N  
ANISOU  917  N   ARG A 142      441   2222   3894     81    -27    -14       N  
ATOM    918  CA  ARG A 142      84.469  33.387  62.792  1.00 17.08           C  
ANISOU  918  CA  ARG A 142      419   2189   3879    138     20     -6       C  
ATOM    919  C   ARG A 142      85.883  33.801  63.203  1.00 17.29           C  
ANISOU  919  C   ARG A 142      327   2274   3969     39     84    -28       C  
ATOM    920  O   ARG A 142      86.084  34.376  64.278  1.00 18.49           O  
ANISOU  920  O   ARG A 142      313   2572   4139    -73     14    -14       O  
ATOM    921  CB  ARG A 142      83.765  34.561  62.089  1.00 17.35           C  
ANISOU  921  CB  ARG A 142      432   2261   3898    238     57    -41       C  
ATOM    922  CG  ARG A 142      83.237  35.670  63.029  1.00 19.15           C  
ANISOU  922  CG  ARG A 142     1385   2073   3815    409     53    193       C  
ATOM    923  CD  ARG A 142      82.579  36.844  62.306  1.00 18.54           C  
ANISOU  923  CD  ARG A 142      687   2558   3800    914    362    234       C  
ATOM    924  NE  ARG A 142      81.790  37.630  63.243  1.00 22.47           N  
ANISOU  924  NE  ARG A 142     2738   2451   3348   1025    455    624       N  
ATOM    925  CZ  ARG A 142      81.092  38.721  62.956  1.00 19.86           C  
ANISOU  925  CZ  ARG A 142     1909   2618   3018   1339    740    675       C  
ATOM    926  NH1 ARG A 142      81.094  39.232  61.742  1.00 18.62           N  
ANISOU  926  NH1 ARG A 142     1825   2746   2504   1189     19    616       N  
ATOM    927  NH2 ARG A 142      80.414  39.318  63.918  1.00 27.04           N  
ANISOU  927  NH2 ARG A 142     3861   3131   3279   1176    964    255       N  
ATOM    928  N   GLY A 143      86.865  33.518  62.361  1.00 17.06           N  
ANISOU  928  N   GLY A 143      335   2169   3977     72     62    -62       N  
ATOM    929  CA  GLY A 143      88.250  33.877  62.677  1.00 17.33           C  
ANISOU  929  CA  GLY A 143      302   2298   3984    -64    233   -120       C  
ATOM    930  C   GLY A 143      89.084  33.722  61.420  1.00 17.68           C  
ANISOU  930  C   GLY A 143      331   2278   4109     30    256   -157       C  
ATOM    931  O   GLY A 143      88.583  33.192  60.432  1.00 17.71           O  
ANISOU  931  O   GLY A 143      334   2273   4121    148    215   -283       O  
ATOM    932  N   PRO A 144      90.340  34.193  61.449  1.00 17.66           N  
ANISOU  932  N   PRO A 144      318   2285   4105     -5    347    -86       N  
ATOM    933  CA  PRO A 144      91.238  34.194  60.299  1.00 18.08           C  
ANISOU  933  CA  PRO A 144      325   2272   4271     53    384   -116       C  
ATOM    934  C   PRO A 144      91.986  32.869  60.175  1.00 18.42           C  
ANISOU  934  C   PRO A 144      405   2273   4321    109    435   -124       C  
ATOM    935  O   PRO A 144      92.105  32.128  61.148  1.00 18.96           O  
ANISOU  935  O   PRO A 144      421   2355   4426     96    447    -58       O  
ATOM    936  CB  PRO A 144      92.195  35.343  60.625  1.00 18.08           C  
ANISOU  936  CB  PRO A 144      331   2368   4169    -97    396   -148       C  
ATOM    937  CG  PRO A 144      92.296  35.313  62.144  1.00 18.39           C  
ANISOU  937  CG  PRO A 144      332   2417   4236    -93    394     45       C  
ATOM    938  CD  PRO A 144      90.941  34.847  62.628  1.00 18.16           C  
ANISOU  938  CD  PRO A 144      311   2399   4187    -93    282    -58       C  
ATOM    939  N   PHE A 145      92.504  32.574  58.990  1.00 18.93           N  
ANISOU  939  N   PHE A 145      585   2239   4366    208    487   -122       N  
ATOM    940  CA  PHE A 145      93.162  31.287  58.757  1.00 18.80           C  
ANISOU  940  CA  PHE A 145      526   2186   4431    291    472   -150       C  
ATOM    941  C   PHE A 145      94.233  31.581  57.718  1.00 19.46           C  
ANISOU  941  C   PHE A 145      475   2365   4552    287    492   -118       C  
ATOM    942  O   PHE A 145      93.894  32.022  56.607  1.00 20.68           O  
ANISOU  942  O   PHE A 145      576   2628   4651    246    477    -83       O  
ATOM    943  CB  PHE A 145      92.081  30.331  58.221  1.00 18.06           C  
ANISOU  943  CB  PHE A 145      374   2080   4404    246    445   -146       C  
ATOM    944  CG  PHE A 145      92.491  28.875  58.110  1.00 19.00           C  
ANISOU  944  CG  PHE A 145      472   2102   4643    343    440   -242       C  
ATOM    945  CD1 PHE A 145      93.765  28.476  57.707  1.00 20.20           C  
ANISOU  945  CD1 PHE A 145      788   1851   5033    557    408   -245       C  
ATOM    946  CD2 PHE A 145      91.528  27.887  58.315  1.00 19.71           C  
ANISOU  946  CD2 PHE A 145      965   1777   4744    391    543   -117       C  
ATOM    947  CE1 PHE A 145      94.079  27.107  57.591  1.00 20.57           C  
ANISOU  947  CE1 PHE A 145      655   2085   5073    616    420     58       C  
ATOM    948  CE2 PHE A 145      91.823  26.533  58.196  1.00 19.51           C  
ANISOU  948  CE2 PHE A 145      766   1990   4654    861    290   -116       C  
ATOM    949  CZ  PHE A 145      93.106  26.130  57.836  1.00 19.66           C  
ANISOU  949  CZ  PHE A 145      474   2209   4788    498    451   -161       C  
ATOM    950  N   VAL A 146      95.512  31.380  58.056  1.00 19.42           N  
ANISOU  950  N   VAL A 146      525   2284   4567    321    622   -204       N  
ATOM    951  CA  VAL A 146      96.583  31.694  57.110  1.00 19.62           C  
ANISOU  951  CA  VAL A 146      608   2219   4626    381    717   -284       C  
ATOM    952  C   VAL A 146      97.362  30.433  56.768  1.00 20.62           C  
ANISOU  952  C   VAL A 146      692   2402   4738    428    743   -237       C  
ATOM    953  O   VAL A 146      97.795  29.697  57.658  1.00 20.80           O  
ANISOU  953  O   VAL A 146      755   2456   4690    478    682   -201       O  
ATOM    954  CB  VAL A 146      97.548  32.789  57.629  1.00 19.22           C  
ANISOU  954  CB  VAL A 146      570   2196   4537    376    848   -281       C  
ATOM    955  CG1 VAL A 146      98.785  32.963  56.711  1.00 18.87           C  
ANISOU  955  CG1 VAL A 146      603   1952   4614    188    817   -228       C  
ATOM    956  CG2 VAL A 146      96.786  34.119  57.784  1.00 20.27           C  
ANISOU  956  CG2 VAL A 146      884   2009   4807    243    582   -291       C  
ATOM    957  N   VAL A 147      97.531  30.191  55.472  1.00 21.51           N  
ANISOU  957  N   VAL A 147      844   2526   4803    439    728   -306       N  
ATOM    958  CA  VAL A 147      98.444  29.139  55.024  1.00 21.82           C  
ANISOU  958  CA  VAL A 147      751   2633   4907    449    729   -250       C  
ATOM    959  C   VAL A 147      99.700  29.792  54.446  1.00 22.63           C  
ANISOU  959  C   VAL A 147      795   2728   5073    395    627   -234       C  
ATOM    960  O   VAL A 147      99.660  30.421  53.383  1.00 22.57           O  
ANISOU  960  O   VAL A 147      778   2779   5018    216    452   -238       O  
ATOM    961  CB  VAL A 147      97.782  28.200  53.987  1.00 21.81           C  
ANISOU  961  CB  VAL A 147      803   2640   4842    455    835   -277       C  
ATOM    962  CG1 VAL A 147      98.791  27.135  53.518  1.00 21.77           C  
ANISOU  962  CG1 VAL A 147      804   2661   4805    590    872   -274       C  
ATOM    963  CG2 VAL A 147      96.502  27.554  54.532  1.00 22.95           C  
ANISOU  963  CG2 VAL A 147      997   2715   5006    386    685   -269       C  
ATOM    964  N   TYR A 148     100.819  29.647  55.154  1.00 23.42           N  
ANISOU  964  N   TYR A 148      751   2845   5300    429    645   -181       N  
ATOM    965  CA  TYR A 148     102.086  30.251  54.740  1.00 24.00           C  
ANISOU  965  CA  TYR A 148      782   2825   5510    453    728   -185       C  
ATOM    966  C   TYR A 148     102.705  29.491  53.576  1.00 25.19           C  
ANISOU  966  C   TYR A 148      940   2907   5724    536    727   -187       C  
ATOM    967  O   TYR A 148     102.524  28.275  53.441  1.00 25.92           O  
ANISOU  967  O   TYR A 148     1247   2849   5751    628    855   -273       O  
ATOM    968  CB  TYR A 148     103.047  30.340  55.934  1.00 24.15           C  
ANISOU  968  CB  TYR A 148      834   2791   5548    483    770   -143       C  
ATOM    969  CG  TYR A 148     102.500  31.265  57.008  1.00 23.85           C  
ANISOU  969  CG  TYR A 148      497   3003   5560    398    843   -215       C  
ATOM    970  CD1 TYR A 148     102.573  32.652  56.862  1.00 24.75           C  
ANISOU  970  CD1 TYR A 148      577   3191   5634    652    846    -39       C  
ATOM    971  CD2 TYR A 148     101.867  30.759  58.139  1.00 24.34           C  
ANISOU  971  CD2 TYR A 148      563   3168   5516    674    753    -41       C  
ATOM    972  CE1 TYR A 148     102.080  33.509  57.827  1.00 25.19           C  
ANISOU  972  CE1 TYR A 148      556   3322   5693    598    840   -190       C  
ATOM    973  CE2 TYR A 148     101.354  31.611  59.108  1.00 24.95           C  
ANISOU  973  CE2 TYR A 148      555   3129   5793    598    608   -139       C  
ATOM    974  CZ  TYR A 148     101.461  32.977  58.952  1.00 26.14           C  
ANISOU  974  CZ  TYR A 148      897   3338   5695    613    700     37       C  
ATOM    975  OH  TYR A 148     100.921  33.804  59.923  1.00 25.30           O  
ANISOU  975  OH  TYR A 148      551   3232   5827    720    684     56       O  
ATOM    976  N   ASP A 149     103.413  30.222  52.721  1.00 26.04           N  
ANISOU  976  N   ASP A 149      974   2956   5964    580    762   -190       N  
ATOM    977  CA  ASP A 149     104.173  29.597  51.652  1.00 27.95           C  
ANISOU  977  CA  ASP A 149     1231   3164   6225    572    790   -162       C  
ATOM    978  C   ASP A 149     105.663  29.764  51.956  1.00 28.80           C  
ANISOU  978  C   ASP A 149     1276   3207   6457    615    734   -138       C  
ATOM    979  O   ASP A 149     106.189  30.881  51.909  1.00 28.83           O  
ANISOU  979  O   ASP A 149     1287   3178   6488    469    671    -89       O  
ATOM    980  CB  ASP A 149     103.779  30.221  50.309  1.00 28.24           C  
ANISOU  980  CB  ASP A 149     1253   3270   6207    625    799   -150       C  
ATOM    981  CG  ASP A 149     104.444  29.538  49.116  1.00 29.81           C  
ANISOU  981  CG  ASP A 149     1631   3396   6298    838    811   -220       C  
ATOM    982  OD1 ASP A 149     105.331  28.660  49.285  1.00 29.73           O  
ANISOU  982  OD1 ASP A 149     1419   3663   6213   1036   1222   -215       O  
ATOM    983  OD2 ASP A 149     104.063  29.902  47.981  1.00 31.14           O  
ANISOU  983  OD2 ASP A 149     1889   3700   6241   1010    776   -267       O  
ATOM    984  N   PRO A 150     106.356  28.658  52.278  1.00 29.80           N  
ANISOU  984  N   PRO A 150     1363   3283   6675    647    743   -109       N  
ATOM    985  CA  PRO A 150     107.787  28.762  52.585  1.00 30.41           C  
ANISOU  985  CA  PRO A 150     1342   3371   6839    631    784   -114       C  
ATOM    986  C   PRO A 150     108.591  29.283  51.403  1.00 31.32           C  
ANISOU  986  C   PRO A 150     1496   3474   6929    662    838   -138       C  
ATOM    987  O   PRO A 150     109.730  29.737  51.582  1.00 32.14           O  
ANISOU  987  O   PRO A 150     1585   3675   6950    533    797   -137       O  
ATOM    988  CB  PRO A 150     108.206  27.317  52.854  1.00 30.71           C  
ANISOU  988  CB  PRO A 150     1425   3392   6850    673    731    -19       C  
ATOM    989  CG  PRO A 150     106.954  26.617  53.222  1.00 30.68           C  
ANISOU  989  CG  PRO A 150     1439   3359   6857    628    677     35       C  
ATOM    990  CD  PRO A 150     105.855  27.284  52.442  1.00 29.75           C  
ANISOU  990  CD  PRO A 150     1266   3276   6758    662    760    -94       C  
ATOM    991  N   LYS A 151     108.017  29.175  50.209  1.00 31.28           N  
ANISOU  991  N   LYS A 151     1500   3419   6965    743    866   -201       N  
ATOM    992  CA  LYS A 151     108.630  29.715  49.004  1.00 32.28           C  
ANISOU  992  CA  LYS A 151     1736   3519   7008    837    979   -246       C  
ATOM    993  C   LYS A 151     107.809  30.850  48.386  1.00 31.95           C  
ANISOU  993  C   LYS A 151     1691   3530   6917    779    994   -241       C  
ATOM    994  O   LYS A 151     107.780  31.020  47.168  1.00 31.97           O  
ANISOU  994  O   LYS A 151     1705   3560   6880    728   1083   -240       O  
ATOM    995  CB  LYS A 151     108.943  28.596  48.002  1.00 33.10           C  
ANISOU  995  CB  LYS A 151     1962   3511   7103    830    941   -270       C  
ATOM    996  CG  LYS A 151     109.925  27.566  48.566  1.00 35.68           C  
ANISOU  996  CG  LYS A 151     2391   3750   7416   1170   1065   -349       C  
ATOM    997  CD  LYS A 151     110.419  26.574  47.520  1.00 42.05           C  
ANISOU  997  CD  LYS A 151     3809   4256   7910   1023   1166   -624       C  
ATOM    998  CE  LYS A 151     109.454  25.402  47.374  1.00 45.11           C  
ANISOU  998  CE  LYS A 151     4378   4456   8302    834   1164   -585       C  
ATOM    999  NZ  LYS A 151     110.116  24.235  46.726  1.00 47.71           N  
ANISOU  999  NZ  LYS A 151     4762   4724   8641   1110   1304   -690       N  
ATOM   1000  N   ASP A 152     107.165  31.644  49.239  1.00 31.22           N  
ANISOU 1000  N   ASP A 152     1548   3457   6858    762   1027   -206       N  
ATOM   1001  CA  ASP A 152     106.319  32.741  48.775  1.00 31.33           C  
ANISOU 1001  CA  ASP A 152     1689   3486   6728    684   1031   -182       C  
ATOM   1002  C   ASP A 152     107.081  33.588  47.758  1.00 31.21           C  
ANISOU 1002  C   ASP A 152     1589   3526   6740    646   1031   -159       C  
ATOM   1003  O   ASP A 152     108.148  34.116  48.074  1.00 31.00           O  
ANISOU 1003  O   ASP A 152     1598   3428   6752    623   1018   -128       O  
ATOM   1004  CB  ASP A 152     105.875  33.617  49.948  1.00 30.99           C  
ANISOU 1004  CB  ASP A 152     1607   3419   6746    743   1024   -196       C  
ATOM   1005  CG  ASP A 152     104.591  34.356  49.656  1.00 30.66           C  
ANISOU 1005  CG  ASP A 152     1757   3390   6502    631    858   -225       C  
ATOM   1006  OD1 ASP A 152     104.565  35.092  48.646  1.00 31.32           O  
ANISOU 1006  OD1 ASP A 152     2162   3455   6279    395    898   -246       O  
ATOM   1007  OD2 ASP A 152     103.615  34.183  50.421  1.00 28.68           O  
ANISOU 1007  OD2 ASP A 152     1288   3593   6017    712    603   -293       O  
ATOM   1008  N   PRO A 153     106.547  33.701  46.530  1.00 31.03           N  
ANISOU 1008  N   PRO A 153     1546   3556   6685    613   1067   -165       N  
ATOM   1009  CA  PRO A 153     107.230  34.493  45.512  1.00 31.04           C  
ANISOU 1009  CA  PRO A 153     1500   3628   6664    622   1059   -184       C  
ATOM   1010  C   PRO A 153     107.285  35.978  45.880  1.00 30.94           C  
ANISOU 1010  C   PRO A 153     1449   3694   6612    556   1062   -210       C  
ATOM   1011  O   PRO A 153     108.077  36.712  45.300  1.00 31.57           O  
ANISOU 1011  O   PRO A 153     1606   3720   6668    442   1043   -240       O  
ATOM   1012  CB  PRO A 153     106.387  34.254  44.254  1.00 31.05           C  
ANISOU 1012  CB  PRO A 153     1478   3655   6664    582   1083   -232       C  
ATOM   1013  CG  PRO A 153     105.035  33.869  44.774  1.00 30.87           C  
ANISOU 1013  CG  PRO A 153     1556   3564   6608    607   1183   -156       C  
ATOM   1014  CD  PRO A 153     105.315  33.078  46.014  1.00 30.80           C  
ANISOU 1014  CD  PRO A 153     1458   3554   6687    691   1023   -187       C  
ATOM   1015  N   HIS A 154     106.464  36.417  46.831  1.00 30.50           N  
ANISOU 1015  N   HIS A 154     1351   3666   6570    652   1068   -221       N  
ATOM   1016  CA  HIS A 154     106.482  37.798  47.289  1.00 30.18           C  
ANISOU 1016  CA  HIS A 154     1206   3710   6548    661   1052   -261       C  
ATOM   1017  C   HIS A 154     107.369  38.035  48.507  1.00 30.52           C  
ANISOU 1017  C   HIS A 154     1246   3744   6606    637   1085   -232       C  
ATOM   1018  O   HIS A 154     107.451  39.158  48.996  1.00 29.81           O  
ANISOU 1018  O   HIS A 154     1061   3677   6586    701   1078   -240       O  
ATOM   1019  CB  HIS A 154     105.054  38.264  47.617  1.00 30.21           C  
ANISOU 1019  CB  HIS A 154     1208   3697   6571    737   1029   -256       C  
ATOM   1020  CG  HIS A 154     104.209  38.541  46.413  1.00 29.98           C  
ANISOU 1020  CG  HIS A 154     1376   3593   6420    648    994   -406       C  
ATOM   1021  ND1 HIS A 154     104.675  39.250  45.326  1.00 28.58           N  
ANISOU 1021  ND1 HIS A 154     1383   3223   6252    433   1051   -542       N  
ATOM   1022  CD2 HIS A 154     102.906  38.262  46.155  1.00 29.55           C  
ANISOU 1022  CD2 HIS A 154     1563   3394   6268    408    911   -567       C  
ATOM   1023  CE1 HIS A 154     103.702  39.379  44.440  1.00 29.93           C  
ANISOU 1023  CE1 HIS A 154     1567   3549   6253    268    898   -501       C  
ATOM   1024  NE2 HIS A 154     102.617  38.792  44.919  1.00 30.24           N  
ANISOU 1024  NE2 HIS A 154     1536   3660   6293    351    799   -594       N  
ATOM   1025  N   LYS A 155     108.063  37.010  48.994  1.00 30.89           N  
ANISOU 1025  N   LYS A 155     1367   3750   6617    577   1072   -227       N  
ATOM   1026  CA  LYS A 155     108.737  37.149  50.281  1.00 32.03           C  
ANISOU 1026  CA  LYS A 155     1554   3917   6696    468   1043   -198       C  
ATOM   1027  C   LYS A 155     109.809  38.245  50.342  1.00 31.78           C  
ANISOU 1027  C   LYS A 155     1552   3847   6676    420   1062   -179       C  
ATOM   1028  O   LYS A 155     110.004  38.847  51.400  1.00 31.62           O  
ANISOU 1028  O   LYS A 155     1501   3827   6686    237   1075    -78       O  
ATOM   1029  CB  LYS A 155     109.235  35.789  50.789  1.00 33.41           C  
ANISOU 1029  CB  LYS A 155     1945   3985   6761    475    934   -244       C  
ATOM   1030  CG  LYS A 155     110.151  35.833  52.014  1.00 37.78           C  
ANISOU 1030  CG  LYS A 155     2611   4698   7043    479    818   -279       C  
ATOM   1031  CD  LYS A 155     109.407  36.377  53.246  1.00 41.70           C  
ANISOU 1031  CD  LYS A 155     3024   5489   7330    618    931   -468       C  
ATOM   1032  CE  LYS A 155     110.315  37.260  54.103  1.00 44.15           C  
ANISOU 1032  CE  LYS A 155     3688   5595   7490    556    710   -628       C  
ATOM   1033  NZ  LYS A 155     109.627  37.736  55.333  1.00 45.70           N  
ANISOU 1033  NZ  LYS A 155     3917   5888   7557    558    565   -632       N  
ATOM   1034  N   LYS A 156     110.458  38.557  49.223  1.00 31.21           N  
ANISOU 1034  N   LYS A 156     1411   3797   6648    381   1084   -155       N  
ATOM   1035  CA  LYS A 156     111.466  39.622  49.227  1.00 31.84           C  
ANISOU 1035  CA  LYS A 156     1463   3956   6677    434   1093   -150       C  
ATOM   1036  C   LYS A 156     110.915  41.026  49.485  1.00 30.55           C  
ANISOU 1036  C   LYS A 156     1306   3826   6475    308    973   -152       C  
ATOM   1037  O   LYS A 156     111.690  41.946  49.785  1.00 30.98           O  
ANISOU 1037  O   LYS A 156     1255   4011   6505    249    946   -124       O  
ATOM   1038  CB  LYS A 156     112.341  39.594  47.966  1.00 32.98           C  
ANISOU 1038  CB  LYS A 156     1667   4081   6781    471   1192   -102       C  
ATOM   1039  CG  LYS A 156     113.159  38.316  47.846  1.00 36.53           C  
ANISOU 1039  CG  LYS A 156     2029   4545   7306    648   1192   -126       C  
ATOM   1040  CD  LYS A 156     114.431  38.527  47.027  1.00 42.03           C  
ANISOU 1040  CD  LYS A 156     2790   5527   7649    757   1510    -41       C  
ATOM   1041  CE  LYS A 156     115.277  37.265  47.012  1.00 46.58           C  
ANISOU 1041  CE  LYS A 156     3582   5995   8118   1050   1036    181       C  
ATOM   1042  NZ  LYS A 156     115.770  36.908  48.379  1.00 51.44           N  
ANISOU 1042  NZ  LYS A 156     4579   6754   8209    861    904    336       N  
ATOM   1043  N   LEU A 157     109.591  41.168  49.395  1.00 29.08           N  
ANISOU 1043  N   LEU A 157     1184   3695   6168    284    883   -192       N  
ATOM   1044  CA  LEU A 157     108.935  42.455  49.562  1.00 27.81           C  
ANISOU 1044  CA  LEU A 157     1026   3536   6003    254    703   -191       C  
ATOM   1045  C   LEU A 157     108.662  42.841  51.013  1.00 27.32           C  
ANISOU 1045  C   LEU A 157      979   3464   5936    216    655   -185       C  
ATOM   1046  O   LEU A 157     108.233  43.973  51.277  1.00 27.26           O  
ANISOU 1046  O   LEU A 157     1086   3410   5862    289    591   -201       O  
ATOM   1047  CB  LEU A 157     107.621  42.511  48.770  1.00 27.92           C  
ANISOU 1047  CB  LEU A 157     1095   3504   6008    169    697   -228       C  
ATOM   1048  CG  LEU A 157     107.722  42.292  47.255  1.00 29.38           C  
ANISOU 1048  CG  LEU A 157     1437   3679   6045     86    492   -229       C  
ATOM   1049  CD1 LEU A 157     106.340  42.426  46.637  1.00 30.46           C  
ANISOU 1049  CD1 LEU A 157     1756   3508   6308    467    189   -360       C  
ATOM   1050  CD2 LEU A 157     108.704  43.237  46.581  1.00 30.62           C  
ANISOU 1050  CD2 LEU A 157     1566   4003   6062     67    336   -213       C  
ATOM   1051  N   TYR A 158     108.859  41.923  51.955  1.00 25.82           N  
ANISOU 1051  N   TYR A 158      721   3276   5811    189    669   -205       N  
ATOM   1052  CA  TYR A 158     108.536  42.260  53.344  1.00 25.15           C  
ANISOU 1052  CA  TYR A 158      693   3153   5707     66    592   -210       C  
ATOM   1053  C   TYR A 158     109.422  41.563  54.348  1.00 25.11           C  
ANISOU 1053  C   TYR A 158      681   3111   5748     37    567   -236       C  
ATOM   1054  O   TYR A 158     110.062  40.569  54.034  1.00 26.25           O  
ANISOU 1054  O   TYR A 158     1046   3068   5857     36    477   -381       O  
ATOM   1055  CB  TYR A 158     107.067  41.957  53.667  1.00 24.59           C  
ANISOU 1055  CB  TYR A 158      624   3130   5587      0    565   -218       C  
ATOM   1056  CG  TYR A 158     106.676  40.527  53.369  1.00 24.33           C  
ANISOU 1056  CG  TYR A 158      685   3217   5341    -58    533   -241       C  
ATOM   1057  CD1 TYR A 158     106.846  39.515  54.317  1.00 22.81           C  
ANISOU 1057  CD1 TYR A 158      727   3060   4878    -43    198   -401       C  
ATOM   1058  CD2 TYR A 158     106.127  40.193  52.131  1.00 23.77           C  
ANISOU 1058  CD2 TYR A 158      559   3379   5091    -40    544   -312       C  
ATOM   1059  CE1 TYR A 158     106.466  38.194  54.031  1.00 23.27           C  
ANISOU 1059  CE1 TYR A 158      816   3055   4968     92    479   -318       C  
ATOM   1060  CE2 TYR A 158     105.744  38.893  51.837  1.00 23.46           C  
ANISOU 1060  CE2 TYR A 158      683   3132   5097    147    748   -213       C  
ATOM   1061  CZ  TYR A 158     105.907  37.902  52.791  1.00 23.68           C  
ANISOU 1061  CZ  TYR A 158      822   3232   4943    232    446   -280       C  
ATOM   1062  OH  TYR A 158     105.516  36.622  52.473  1.00 24.77           O  
ANISOU 1062  OH  TYR A 158     1057   3471   4880    163    260    -46       O  
ATOM   1063  N   ASP A 159     109.454  42.118  55.550  1.00 25.34           N  
ANISOU 1063  N   ASP A 159      769   3133   5723     30    615   -165       N  
ATOM   1064  CA  ASP A 159     110.261  41.617  56.653  1.00 24.95           C  
ANISOU 1064  CA  ASP A 159      557   3116   5805     -1    540   -153       C  
ATOM   1065  C   ASP A 159     109.431  40.858  57.688  1.00 25.31           C  
ANISOU 1065  C   ASP A 159      753   3080   5783     33    481   -105       C  
ATOM   1066  O   ASP A 159     109.942  39.941  58.332  1.00 25.78           O  
ANISOU 1066  O   ASP A 159      826   3122   5848     20    541      1       O  
ATOM   1067  CB  ASP A 159     110.911  42.812  57.337  1.00 25.55           C  
ANISOU 1067  CB  ASP A 159      642   3159   5906    -11    463   -126       C  
ATOM   1068  CG  ASP A 159     111.746  43.637  56.377  1.00 26.54           C  
ANISOU 1068  CG  ASP A 159      843   3214   6027    -38    362   -131       C  
ATOM   1069  OD1 ASP A 159     112.671  43.079  55.745  1.00 27.28           O  
ANISOU 1069  OD1 ASP A 159     1080   2899   6386    116    304   -420       O  
ATOM   1070  OD2 ASP A 159     111.475  44.849  56.273  1.00 28.51           O  
ANISOU 1070  OD2 ASP A 159     1202   3216   6412   -107    -85    -95       O  
ATOM   1071  N   VAL A 160     108.168  41.254  57.857  1.00 24.06           N  
ANISOU 1071  N   VAL A 160      492   2998   5650    -71    490   -163       N  
ATOM   1072  CA  VAL A 160     107.361  40.730  58.948  1.00 23.38           C  
ANISOU 1072  CA  VAL A 160      530   2803   5550    -52    393   -164       C  
ATOM   1073  C   VAL A 160     106.031  40.208  58.415  1.00 23.65           C  
ANISOU 1073  C   VAL A 160      603   2830   5549     -7    350   -154       C  
ATOM   1074  O   VAL A 160     105.299  40.935  57.743  1.00 23.43           O  
ANISOU 1074  O   VAL A 160      669   2721   5511     52    368   -184       O  
ATOM   1075  CB  VAL A 160     107.098  41.807  60.021  1.00 23.79           C  
ANISOU 1075  CB  VAL A 160      549   2939   5549    -93    350   -172       C  
ATOM   1076  CG1 VAL A 160     106.288  41.221  61.179  1.00 23.39           C  
ANISOU 1076  CG1 VAL A 160      738   2640   5507   -204    464   -267       C  
ATOM   1077  CG2 VAL A 160     108.410  42.428  60.527  1.00 23.50           C  
ANISOU 1077  CG2 VAL A 160      464   2960   5504   -117    476   -303       C  
ATOM   1078  N   ASP A 161     105.727  38.950  58.726  1.00 23.31           N  
ANISOU 1078  N   ASP A 161      567   2731   5557    -25    274   -133       N  
ATOM   1079  CA  ASP A 161     104.470  38.314  58.333  1.00 23.82           C  
ANISOU 1079  CA  ASP A 161      599   2825   5625     21    221    -66       C  
ATOM   1080  C   ASP A 161     104.154  37.263  59.387  1.00 23.75           C  
ANISOU 1080  C   ASP A 161      563   2831   5628    -15    191    -67       C  
ATOM   1081  O   ASP A 161     104.739  36.169  59.399  1.00 24.54           O  
ANISOU 1081  O   ASP A 161      546   3005   5774    161    233     14       O  
ATOM   1082  CB  ASP A 161     104.605  37.671  56.950  1.00 23.74           C  
ANISOU 1082  CB  ASP A 161      607   2790   5623     35    279   -114       C  
ATOM   1083  CG  ASP A 161     103.364  36.895  56.539  1.00 24.33           C  
ANISOU 1083  CG  ASP A 161      639   2883   5721    156    246    -17       C  
ATOM   1084  OD1 ASP A 161     102.269  37.207  57.048  1.00 25.27           O  
ANISOU 1084  OD1 ASP A 161      890   2941   5769     87    600     52       O  
ATOM   1085  OD2 ASP A 161     103.464  35.987  55.690  1.00 25.01           O  
ANISOU 1085  OD2 ASP A 161      855   2769   5875    201    307     55       O  
ATOM   1086  N   ASN A 162     103.273  37.612  60.312  1.00 23.39           N  
ANISOU 1086  N   ASN A 162      429   2862   5595    -57     93     13       N  
ATOM   1087  CA  ASN A 162     102.997  36.697  61.418  1.00 23.72           C  
ANISOU 1087  CA  ASN A 162      479   2953   5579    -96     32     33       C  
ATOM   1088  C   ASN A 162     101.626  36.977  62.030  1.00 22.88           C  
ANISOU 1088  C   ASN A 162      402   2831   5459    -91     70     82       C  
ATOM   1089  O   ASN A 162     100.794  37.679  61.433  1.00 23.00           O  
ANISOU 1089  O   ASN A 162      341   2871   5524   -249     99    106       O  
ATOM   1090  CB  ASN A 162     104.149  36.732  62.452  1.00 23.60           C  
ANISOU 1090  CB  ASN A 162      480   2926   5560    -40    -22    -51       C  
ATOM   1091  CG  ASN A 162     104.308  38.094  63.129  1.00 24.52           C  
ANISOU 1091  CG  ASN A 162      503   3012   5800   -189    -24    -61       C  
ATOM   1092  OD1 ASN A 162     103.369  38.891  63.184  1.00 24.32           O  
ANISOU 1092  OD1 ASN A 162      561   2613   6063   -223   -111   -523       O  
ATOM   1093  ND2 ASN A 162     105.501  38.352  63.673  1.00 24.57           N  
ANISOU 1093  ND2 ASN A 162      440   3340   5554    -56    227   -125       N  
ATOM   1094  N   GLU A 163     101.392  36.454  63.227  1.00 22.61           N  
ANISOU 1094  N   GLU A 163      474   2722   5395    -45    -12    137       N  
ATOM   1095  CA  GLU A 163     100.097  36.637  63.898  1.00 23.58           C  
ANISOU 1095  CA  GLU A 163      773   2904   5278    -37     29    204       C  
ATOM   1096  C   GLU A 163      99.727  38.100  64.176  1.00 23.04           C  
ANISOU 1096  C   GLU A 163      687   2877   5189    -41   -100    235       C  
ATOM   1097  O   GLU A 163      98.539  38.481  64.188  1.00 23.73           O  
ANISOU 1097  O   GLU A 163      913   2890   5211     10    -19    266       O  
ATOM   1098  CB  GLU A 163     100.123  35.843  65.202  1.00 24.23           C  
ANISOU 1098  CB  GLU A 163      832   3005   5367    -46     76    256       C  
ATOM   1099  CG  GLU A 163      98.777  35.686  65.879  1.00 25.17           C  
ANISOU 1099  CG  GLU A 163     1036   3142   5385   -122     24    219       C  
ATOM   1100  CD  GLU A 163      98.863  34.657  67.001  1.00 27.74           C  
ANISOU 1100  CD  GLU A 163     1522   3565   5451   -176    -97    369       C  
ATOM   1101  OE1 GLU A 163      99.906  34.596  67.702  1.00 29.57           O  
ANISOU 1101  OE1 GLU A 163     1595   4156   5485    318      0    208       O  
ATOM   1102  OE2 GLU A 163      97.878  33.916  67.165  1.00 28.02           O  
ANISOU 1102  OE2 GLU A 163     1522   3665   5456   -336   -239    262       O  
ATOM   1103  N   SER A 164     100.741  38.932  64.380  1.00 22.79           N  
ANISOU 1103  N   SER A 164      832   2774   5053     -8   -314    117       N  
ATOM   1104  CA  SER A 164     100.515  40.346  64.632  1.00 22.90           C  
ANISOU 1104  CA  SER A 164      850   2787   5064   -123   -436     12       C  
ATOM   1105  C   SER A 164     100.306  41.164  63.352  1.00 22.26           C  
ANISOU 1105  C   SER A 164      763   2677   5014    -94   -372     30       C  
ATOM   1106  O   SER A 164     100.051  42.367  63.457  1.00 23.83           O  
ANISOU 1106  O   SER A 164     1220   2813   5019    -76   -422     14       O  
ATOM   1107  CB  SER A 164     101.669  40.924  65.462  1.00 22.84           C  
ANISOU 1107  CB  SER A 164      553   2837   5285   -148   -406    -86       C  
ATOM   1108  OG  SER A 164     102.731  41.262  64.589  1.00 27.88           O  
ANISOU 1108  OG  SER A 164     1466   3525   5599   -250   -463   -204       O  
ATOM   1109  N   THR A 165     100.369  40.543  62.172  1.00 20.52           N  
ANISOU 1109  N   THR A 165      422   2558   4815   -101   -279     84       N  
ATOM   1110  CA  THR A 165     100.084  41.240  60.907  1.00 20.38           C  
ANISOU 1110  CA  THR A 165      372   2596   4773    -76   -227     90       C  
ATOM   1111  C   THR A 165      98.787  40.810  60.227  1.00 20.00           C  
ANISOU 1111  C   THR A 165      437   2487   4673    -72   -176     96       C  
ATOM   1112  O   THR A 165      98.482  41.248  59.114  1.00 19.87           O  
ANISOU 1112  O   THR A 165      416   2527   4605    -95    -38    164       O  
ATOM   1113  CB  THR A 165     101.252  41.188  59.894  1.00 20.69           C  
ANISOU 1113  CB  THR A 165      494   2649   4717    -81   -291     76       C  
ATOM   1114  OG1 THR A 165     101.398  39.853  59.371  1.00 21.79           O  
ANISOU 1114  OG1 THR A 165      606   2755   4917    200   -134    171       O  
ATOM   1115  CG2 THR A 165     102.568  41.687  60.551  1.00 21.93           C  
ANISOU 1115  CG2 THR A 165      506   2868   4959   -213   -195    102       C  
ATOM   1116  N   VAL A 166      98.014  39.965  60.905  1.00 19.30           N  
ANISOU 1116  N   VAL A 166      289   2443   4600    -53   -123     69       N  
ATOM   1117  CA  VAL A 166      96.658  39.661  60.456  1.00 18.64           C  
ANISOU 1117  CA  VAL A 166      287   2241   4551     30   -114     60       C  
ATOM   1118  C   VAL A 166      95.740  40.763  60.948  1.00 18.86           C  
ANISOU 1118  C   VAL A 166      336   2302   4528     24   -100    109       C  
ATOM   1119  O   VAL A 166      95.787  41.137  62.126  1.00 19.42           O  
ANISOU 1119  O   VAL A 166      540   2357   4480    228    -55     79       O  
ATOM   1120  CB  VAL A 166      96.193  38.292  60.967  1.00 18.81           C  
ANISOU 1120  CB  VAL A 166      288   2243   4616      8   -126     65       C  
ATOM   1121  CG1 VAL A 166      94.760  38.000  60.469  1.00 18.61           C  
ANISOU 1121  CG1 VAL A 166      332   2206   4530    -64   -339    105       C  
ATOM   1122  CG2 VAL A 166      97.197  37.228  60.482  1.00 19.72           C  
ANISOU 1122  CG2 VAL A 166      455   2251   4786    161   -209    129       C  
ATOM   1123  N   ILE A 167      94.939  41.310  60.040  1.00 18.04           N  
ANISOU 1123  N   ILE A 167      288   2230   4334     40   -116    130       N  
ATOM   1124  CA  ILE A 167      93.971  42.345  60.419  1.00 17.91           C  
ANISOU 1124  CA  ILE A 167      314   2233   4256     37     12     14       C  
ATOM   1125  C   ILE A 167      92.579  41.845  60.084  1.00 17.53           C  
ANISOU 1125  C   ILE A 167      298   2245   4116    149     74     16       C  
ATOM   1126  O   ILE A 167      92.274  41.642  58.915  1.00 18.38           O  
ANISOU 1126  O   ILE A 167      465   2549   3968    201     86    -17       O  
ATOM   1127  CB  ILE A 167      94.199  43.683  59.667  1.00 18.05           C  
ANISOU 1127  CB  ILE A 167      284   2273   4297      0    -29     53       C  
ATOM   1128  CG1 ILE A 167      95.653  44.173  59.830  1.00 18.43           C  
ANISOU 1128  CG1 ILE A 167      319   2289   4392   -257      5    -25       C  
ATOM   1129  CG2 ILE A 167      93.199  44.744  60.161  1.00 17.05           C  
ANISOU 1129  CG2 ILE A 167      289   2124   4063    -60     65     45       C  
ATOM   1130  CD1 ILE A 167      95.929  45.436  59.020  1.00 19.17           C  
ANISOU 1130  CD1 ILE A 167      327   2453   4503   -229    261    -33       C  
ATOM   1131  N   THR A 168      91.744  41.625  61.096  1.00 17.22           N  
ANISOU 1131  N   THR A 168      424   2138   3979    222    176    -43       N  
ATOM   1132  CA  THR A 168      90.371  41.192  60.847  1.00 17.09           C  
ANISOU 1132  CA  THR A 168      430   2146   3917    281    127      0       C  
ATOM   1133  C   THR A 168      89.415  42.369  60.988  1.00 17.25           C  
ANISOU 1133  C   THR A 168      434   2190   3929    286    118     11       C  
ATOM   1134  O   THR A 168      89.609  43.231  61.851  1.00 17.13           O  
ANISOU 1134  O   THR A 168      491   2204   3812    325    171    141       O  
ATOM   1135  CB  THR A 168      89.906  40.073  61.802  1.00 16.74           C  
ANISOU 1135  CB  THR A 168      333   2109   3917    227    115    -66       C  
ATOM   1136  OG1 THR A 168      89.972  40.540  63.153  1.00 16.31           O  
ANISOU 1136  OG1 THR A 168      486   2044   3664    200    268     31       O  
ATOM   1137  CG2 THR A 168      90.767  38.839  61.666  1.00 17.70           C  
ANISOU 1137  CG2 THR A 168      630   1954   4140    234      5    -96       C  
ATOM   1138  N   LEU A 169      88.393  42.384  60.133  1.00 16.94           N  
ANISOU 1138  N   LEU A 169      417   2183   3836    254    124    126       N  
ATOM   1139  CA  LEU A 169      87.290  43.346  60.203  1.00 16.96           C  
ANISOU 1139  CA  LEU A 169      387   2268   3786    205    290     75       C  
ATOM   1140  C   LEU A 169      85.983  42.612  60.473  1.00 17.10           C  
ANISOU 1140  C   LEU A 169      326   2351   3817    201    260     68       C  
ATOM   1141  O   LEU A 169      85.682  41.614  59.809  1.00 16.95           O  
ANISOU 1141  O   LEU A 169      352   2396   3690    196    378   -137       O  
ATOM   1142  CB  LEU A 169      87.143  44.073  58.866  1.00 16.54           C  
ANISOU 1142  CB  LEU A 169      353   2243   3689    179    198    118       C  
ATOM   1143  CG  LEU A 169      88.407  44.767  58.337  1.00 16.78           C  
ANISOU 1143  CG  LEU A 169      728   2161   3487     46    223      0       C  
ATOM   1144  CD1 LEU A 169      88.070  45.529  57.066  1.00 17.64           C  
ANISOU 1144  CD1 LEU A 169     1384   2130   3187    -68    194     66       C  
ATOM   1145  CD2 LEU A 169      89.004  45.731  59.373  1.00 17.10           C  
ANISOU 1145  CD2 LEU A 169      666   2291   3538   -199    238   -126       C  
ATOM   1146  N   GLU A 170      85.201  43.125  61.420  1.00 17.87           N  
ANISOU 1146  N   GLU A 170      514   2460   3816    103    356     46       N  
ATOM   1147  CA  GLU A 170      83.911  42.519  61.755  1.00 18.44           C  
ANISOU 1147  CA  GLU A 170      470   2597   3938     91    253     81       C  
ATOM   1148  C   GLU A 170      82.873  43.573  62.013  1.00 18.24           C  
ANISOU 1148  C   GLU A 170      471   2500   3957      2    274     49       C  
ATOM   1149  O   GLU A 170      83.182  44.609  62.604  1.00 18.19           O  
ANISOU 1149  O   GLU A 170      341   2644   3924     44    334    -24       O  
ATOM   1150  CB  GLU A 170      83.986  41.780  63.091  1.00 19.87           C  
ANISOU 1150  CB  GLU A 170      745   2740   4062    145    370     59       C  
ATOM   1151  CG  GLU A 170      84.922  40.609  63.122  1.00 24.32           C  
ANISOU 1151  CG  GLU A 170     1593   3177   4468    142    -11    168       C  
ATOM   1152  CD  GLU A 170      85.032  40.092  64.526  1.00 28.12           C  
ANISOU 1152  CD  GLU A 170     2265   3745   4674   -322   -161    225       C  
ATOM   1153  OE1 GLU A 170      84.162  39.288  64.932  1.00 30.53           O  
ANISOU 1153  OE1 GLU A 170     2624   3979   4997   -972   -180    134       O  
ATOM   1154  OE2 GLU A 170      85.972  40.551  65.207  1.00 29.05           O  
ANISOU 1154  OE2 GLU A 170     2175   3741   5120   -136   -487    213       O  
ATOM   1155  N   ASP A 171      81.637  43.261  61.628  1.00 17.38           N  
ANISOU 1155  N   ASP A 171      334   2382   3885     -1    209    101       N  
ATOM   1156  CA  ASP A 171      80.475  44.021  62.066  1.00 16.74           C  
ANISOU 1156  CA  ASP A 171      493   2169   3696    -16    256    173       C  
ATOM   1157  C   ASP A 171      79.993  43.375  63.356  1.00 16.92           C  
ANISOU 1157  C   ASP A 171      638   2144   3645    -76    313    137       C  
ATOM   1158  O   ASP A 171      79.910  42.147  63.427  1.00 17.38           O  
ANISOU 1158  O   ASP A 171      970   1953   3680   -110    393    291       O  
ATOM   1159  CB  ASP A 171      79.360  44.008  61.008  1.00 16.46           C  
ANISOU 1159  CB  ASP A 171      381   2243   3628     45     69     66       C  
ATOM   1160  CG  ASP A 171      79.045  42.627  60.429  1.00 17.19           C  
ANISOU 1160  CG  ASP A 171      450   2502   3579    182      5     93       C  
ATOM   1161  OD1 ASP A 171      79.885  41.702  60.430  1.00 15.49           O  
ANISOU 1161  OD1 ASP A 171      765   2658   2460    278    -53   -314       O  
ATOM   1162  OD2 ASP A 171      77.916  42.472  59.887  1.00 17.17           O  
ANISOU 1162  OD2 ASP A 171      504   2473   3547    253   -238   -300       O  
ATOM   1163  N   TRP A 172      79.680  44.182  64.365  1.00 15.81           N  
ANISOU 1163  N   TRP A 172      371   2023   3613    -51    374    217       N  
ATOM   1164  CA  TRP A 172      79.271  43.635  65.648  1.00 15.52           C  
ANISOU 1164  CA  TRP A 172      424   2077   3395    -36    394    220       C  
ATOM   1165  C   TRP A 172      77.921  44.225  66.068  1.00 15.84           C  
ANISOU 1165  C   TRP A 172      474   2096   3447   -108    465    251       C  
ATOM   1166  O   TRP A 172      77.711  45.436  65.954  1.00 16.31           O  
ANISOU 1166  O   TRP A 172      498   2058   3639   -103    621    282       O  
ATOM   1167  CB  TRP A 172      80.374  43.861  66.692  1.00 15.17           C  
ANISOU 1167  CB  TRP A 172      462   1937   3365   -110    313    362       C  
ATOM   1168  CG  TRP A 172      80.107  43.128  67.972  1.00 16.70           C  
ANISOU 1168  CG  TRP A 172      707   2451   3186   -128    321    317       C  
ATOM   1169  CD1 TRP A 172      79.752  43.674  69.169  1.00 16.44           C  
ANISOU 1169  CD1 TRP A 172      574   2680   2991   -264    181    607       C  
ATOM   1170  CD2 TRP A 172      80.163  41.706  68.178  1.00 16.19           C  
ANISOU 1170  CD2 TRP A 172      635   2644   2871      1     94    736       C  
ATOM   1171  NE1 TRP A 172      79.586  42.689  70.102  1.00 17.76           N  
ANISOU 1171  NE1 TRP A 172     1016   2919   2812   -314    153    685       N  
ATOM   1172  CE2 TRP A 172      79.821  41.468  69.525  1.00 17.99           C  
ANISOU 1172  CE2 TRP A 172      931   2976   2927     74    278    695       C  
ATOM   1173  CE3 TRP A 172      80.457  40.616  67.353  1.00 17.84           C  
ANISOU 1173  CE3 TRP A 172      652   2920   3204    263    206    622       C  
ATOM   1174  CZ2 TRP A 172      79.760  40.176  70.077  1.00 18.79           C  
ANISOU 1174  CZ2 TRP A 172      876   3084   3179    170      1    670       C  
ATOM   1175  CZ3 TRP A 172      80.389  39.325  67.894  1.00 18.31           C  
ANISOU 1175  CZ3 TRP A 172     1102   3136   2719    210    278    849       C  
ATOM   1176  CH2 TRP A 172      80.057  39.120  69.250  1.00 20.10           C  
ANISOU 1176  CH2 TRP A 172     1336   3318   2981    172    441    755       C  
ATOM   1177  N   TYR A 173      77.027  43.368  66.553  1.00 15.52           N  
ANISOU 1177  N   TYR A 173      417   2162   3317   -237    479    221       N  
ATOM   1178  CA  TYR A 173      75.641  43.736  66.889  1.00 15.41           C  
ANISOU 1178  CA  TYR A 173      585   2145   3123   -250    534     85       C  
ATOM   1179  C   TYR A 173      75.407  43.558  68.379  1.00 16.50           C  
ANISOU 1179  C   TYR A 173      740   2233   3294   -311    458     25       C  
ATOM   1180  O   TYR A 173      75.865  42.579  68.964  1.00 17.26           O  
ANISOU 1180  O   TYR A 173     1200   2118   3238   -289    362      7       O  
ATOM   1181  CB  TYR A 173      74.670  42.831  66.122  1.00 15.35           C  
ANISOU 1181  CB  TYR A 173      493   2250   3088   -326    576    186       C  
ATOM   1182  CG  TYR A 173      74.897  42.962  64.633  1.00 15.74           C  
ANISOU 1182  CG  TYR A 173      654   2312   3014   -259    655      1       C  
ATOM   1183  CD1 TYR A 173      75.896  42.225  63.987  1.00 16.17           C  
ANISOU 1183  CD1 TYR A 173      718   2398   3029   -173    625    106       C  
ATOM   1184  CD2 TYR A 173      74.179  43.897  63.890  1.00 16.03           C  
ANISOU 1184  CD2 TYR A 173      883   2220   2986   -449    337    -22       C  
ATOM   1185  CE1 TYR A 173      76.122  42.394  62.621  1.00 16.60           C  
ANISOU 1185  CE1 TYR A 173      742   2585   2980     14    451     57       C  
ATOM   1186  CE2 TYR A 173      74.406  44.068  62.523  1.00 16.36           C  
ANISOU 1186  CE2 TYR A 173      802   2374   3039   -319    486   -237       C  
ATOM   1187  CZ  TYR A 173      75.378  43.320  61.896  1.00 16.32           C  
ANISOU 1187  CZ  TYR A 173      869   2362   2970    -30    207   -235       C  
ATOM   1188  OH  TYR A 173      75.613  43.496  60.535  1.00 16.50           O  
ANISOU 1188  OH  TYR A 173      862   2332   3073    105    212    219       O  
ATOM   1189  N   HIS A 174      74.711  44.498  69.006  1.00 16.60           N  
ANISOU 1189  N   HIS A 174      764   2215   3327   -442    493   -130       N  
ATOM   1190  CA  HIS A 174      74.365  44.288  70.412  1.00 17.58           C  
ANISOU 1190  CA  HIS A 174      942   2210   3525   -545    478    -84       C  
ATOM   1191  C   HIS A 174      73.184  43.357  70.645  1.00 18.02           C  
ANISOU 1191  C   HIS A 174     1023   2172   3650   -475    488   -106       C  
ATOM   1192  O   HIS A 174      73.100  42.756  71.719  1.00 19.41           O  
ANISOU 1192  O   HIS A 174     1351   2354   3670   -591    557    -39       O  
ATOM   1193  CB  HIS A 174      74.152  45.629  71.107  1.00 17.36           C  
ANISOU 1193  CB  HIS A 174      951   2074   3571   -692    494   -136       C  
ATOM   1194  CG  HIS A 174      75.423  46.406  71.234  1.00 17.80           C  
ANISOU 1194  CG  HIS A 174      777   2225   3761   -688    312     19       C  
ATOM   1195  ND1 HIS A 174      75.492  47.627  71.868  1.00 19.85           N  
ANISOU 1195  ND1 HIS A 174      991   2291   4258   -860    220   -165       N  
ATOM   1196  CD2 HIS A 174      76.676  46.126  70.808  1.00 18.94           C  
ANISOU 1196  CD2 HIS A 174      871   2494   3829   -753    484    152       C  
ATOM   1197  CE1 HIS A 174      76.735  48.077  71.807  1.00 19.49           C  
ANISOU 1197  CE1 HIS A 174      840   2450   4113   -747    614    117       C  
ATOM   1198  NE2 HIS A 174      77.476  47.181  71.178  1.00 19.09           N  
ANISOU 1198  NE2 HIS A 174     1048   2299   3904   -695    313     -1       N  
ATOM   1199  N   THR A 175      72.319  43.212  69.642  1.00 17.49           N  
ANISOU 1199  N   THR A 175      820   2057   3766   -261    344   -142       N  
ATOM   1200  CA  THR A 175      71.229  42.238  69.676  1.00 17.83           C  
ANISOU 1200  CA  THR A 175      722   2189   3863   -201    351   -129       C  
ATOM   1201  C   THR A 175      71.604  41.020  68.824  1.00 17.50           C  
ANISOU 1201  C   THR A 175      797   2144   3709   -118    306   -137       C  
ATOM   1202  O   THR A 175      72.052  41.181  67.677  1.00 16.82           O  
ANISOU 1202  O   THR A 175      648   2187   3554    -32    218    -62       O  
ATOM   1203  CB  THR A 175      69.925  42.837  69.112  1.00 17.91           C  
ANISOU 1203  CB  THR A 175      683   2186   3934   -245    369   -150       C  
ATOM   1204  OG1 THR A 175      69.581  43.986  69.889  1.00 21.57           O  
ANISOU 1204  OG1 THR A 175     1106   2449   4641   -176    350   -199       O  
ATOM   1205  CG2 THR A 175      68.767  41.804  69.188  1.00 16.67           C  
ANISOU 1205  CG2 THR A 175      369   2216   3749   -323    250    -45       C  
ATOM   1206  N   ALA A 176      71.428  39.824  69.389  1.00 16.90           N  
ANISOU 1206  N   ALA A 176      801   2082   3535    -71    275   -131       N  
ATOM   1207  CA  ALA A 176      71.829  38.585  68.725  1.00 16.75           C  
ANISOU 1207  CA  ALA A 176      905   2052   3405     -9    235    -85       C  
ATOM   1208  C   ALA A 176      71.132  38.374  67.377  1.00 16.46           C  
ANISOU 1208  C   ALA A 176      807   2079   3369    -27    230   -129       C  
ATOM   1209  O   ALA A 176      70.032  38.876  67.135  1.00 16.86           O  
ANISOU 1209  O   ALA A 176      965   2025   3414    -23    316   -235       O  
ATOM   1210  CB  ALA A 176      71.574  37.384  69.618  1.00 17.02           C  
ANISOU 1210  CB  ALA A 176     1087   2036   3343      3    263    -39       C  
ATOM   1211  N   ALA A 177      71.789  37.624  66.503  1.00 16.26           N  
ANISOU 1211  N   ALA A 177      701   2101   3375    -48    251    -68       N  
ATOM   1212  CA  ALA A 177      71.308  37.445  65.139  1.00 16.08           C  
ANISOU 1212  CA  ALA A 177      562   2202   3344     11    211    -67       C  
ATOM   1213  C   ALA A 177      69.867  36.939  65.045  1.00 16.64           C  
ANISOU 1213  C   ALA A 177      589   2218   3515     85    150    -16       C  
ATOM   1214  O   ALA A 177      69.106  37.396  64.171  1.00 17.06           O  
ANISOU 1214  O   ALA A 177      625   2372   3484     14    -22     93       O  
ATOM   1215  CB  ALA A 177      72.251  36.495  64.396  1.00 16.02           C  
ANISOU 1215  CB  ALA A 177      377   2243   3467    202    206    -44       C  
ATOM   1216  N   ARG A 178      69.488  36.017  65.933  1.00 16.29           N  
ANISOU 1216  N   ARG A 178      548   2170   3471     62    269      6       N  
ATOM   1217  CA  ARG A 178      68.132  35.419  65.882  1.00 17.72           C  
ANISOU 1217  CA  ARG A 178      798   2173   3761    119    171      7       C  
ATOM   1218  C   ARG A 178      67.090  36.205  66.677  1.00 18.23           C  
ANISOU 1218  C   ARG A 178      815   2331   3777     90    201     68       C  
ATOM   1219  O   ARG A 178      65.904  35.852  66.683  1.00 18.78           O  
ANISOU 1219  O   ARG A 178      756   2340   4037    161     62     20       O  
ATOM   1220  CB  ARG A 178      68.140  33.952  66.339  1.00 18.28           C  
ANISOU 1220  CB  ARG A 178      894   2195   3854    105    265     49       C  
ATOM   1221  CG  ARG A 178      69.114  33.066  65.549  1.00 18.78           C  
ANISOU 1221  CG  ARG A 178     1147   2066   3920    251    235   -153       C  
ATOM   1222  CD  ARG A 178      68.967  31.576  65.892  1.00 19.03           C  
ANISOU 1222  CD  ARG A 178     1544   1944   3741     59     25   -234       C  
ATOM   1223  NE  ARG A 178      67.771  30.986  65.291  1.00 20.33           N  
ANISOU 1223  NE  ARG A 178     1168   2252   4302    200    118   -479       N  
ATOM   1224  CZ  ARG A 178      67.700  30.598  64.018  1.00 22.00           C  
ANISOU 1224  CZ  ARG A 178     1273   2657   4427   -180    -21   -381       C  
ATOM   1225  NH1 ARG A 178      68.757  30.749  63.233  1.00 22.53           N  
ANISOU 1225  NH1 ARG A 178     1401   2520   4638    347    207   -168       N  
ATOM   1226  NH2 ARG A 178      66.573  30.089  63.516  1.00 21.77           N  
ANISOU 1226  NH2 ARG A 178      869   2815   4588   -273    100   -463       N  
ATOM   1227  N   LEU A 179      67.536  37.281  67.321  1.00 18.25           N  
ANISOU 1227  N   LEU A 179      940   2394   3599    128    129    -73       N  
ATOM   1228  CA  LEU A 179      66.658  38.163  68.096  1.00 18.74           C  
ANISOU 1228  CA  LEU A 179     1053   2558   3506    102    217    -41       C  
ATOM   1229  C   LEU A 179      66.426  39.523  67.455  1.00 19.29           C  
ANISOU 1229  C   LEU A 179     1155   2641   3530    124    263    -94       C  
ATOM   1230  O   LEU A 179      65.493  40.223  67.842  1.00 20.50           O  
ANISOU 1230  O   LEU A 179     1219   2879   3689    111    414    -70       O  
ATOM   1231  CB  LEU A 179      67.216  38.375  69.503  1.00 18.07           C  
ANISOU 1231  CB  LEU A 179      989   2413   3463     19    156   -114       C  
ATOM   1232  CG  LEU A 179      67.246  37.152  70.424  1.00 18.83           C  
ANISOU 1232  CG  LEU A 179     1075   2615   3461   -133     37   -101       C  
ATOM   1233  CD1 LEU A 179      67.808  37.573  71.764  1.00 19.72           C  
ANISOU 1233  CD1 LEU A 179     1085   2808   3599   -161   -353   -114       C  
ATOM   1234  CD2 LEU A 179      65.864  36.502  70.603  1.00 21.06           C  
ANISOU 1234  CD2 LEU A 179      955   3150   3896   -198     41   -355       C  
ATOM   1235  N   GLY A 180      67.262  39.901  66.492  1.00 19.18           N  
ANISOU 1235  N   GLY A 180     1174   2726   3385    188    293    -69       N  
ATOM   1236  CA  GLY A 180      67.150  41.193  65.817  1.00 19.82           C  
ANISOU 1236  CA  GLY A 180     1356   2958   3215     46    190    -51       C  
ATOM   1237  C   GLY A 180      66.347  41.106  64.529  1.00 20.25           C  
ANISOU 1237  C   GLY A 180     1507   3030   3154     64     83    -34       C  
ATOM   1238  O   GLY A 180      65.695  40.094  64.270  1.00 19.83           O  
ANISOU 1238  O   GLY A 180     1503   3078   2953     26     72    -32       O  
ATOM   1239  N   PRO A 181      66.368  42.173  63.718  1.00 21.64           N  
ANISOU 1239  N   PRO A 181     1730   3231   3261      6     27    -64       N  
ATOM   1240  CA  PRO A 181      65.640  42.170  62.442  1.00 22.23           C  
ANISOU 1240  CA  PRO A 181     1863   3196   3386     33    -58     -9       C  
ATOM   1241  C   PRO A 181      66.170  41.083  61.506  1.00 22.54           C  
ANISOU 1241  C   PRO A 181     1788   3233   3540     43    -11    -92       C  
ATOM   1242  O   PRO A 181      67.336  40.695  61.612  1.00 22.39           O  
ANISOU 1242  O   PRO A 181     1860   3051   3594    190     39     -8       O  
ATOM   1243  CB  PRO A 181      65.942  43.545  61.844  1.00 22.30           C  
ANISOU 1243  CB  PRO A 181     1798   3325   3348     -1    -88    -26       C  
ATOM   1244  CG  PRO A 181      66.888  44.213  62.717  1.00 24.25           C  
ANISOU 1244  CG  PRO A 181     2261   3418   3533    -90   -104     35       C  
ATOM   1245  CD  PRO A 181      66.963  43.486  64.026  1.00 21.58           C  
ANISOU 1245  CD  PRO A 181     1790   3193   3216    -47     -4     44       C  
ATOM   1246  N   ARG A 182      65.324  40.607  60.599  1.00 22.67           N  
ANISOU 1246  N   ARG A 182     1761   3116   3735    -60     -4   -113       N  
ATOM   1247  CA  ARG A 182      65.717  39.687  59.527  1.00 23.18           C  
ANISOU 1247  CA  ARG A 182     1721   3118   3967    -44     45   -243       C  
ATOM   1248  C   ARG A 182      66.819  40.312  58.677  1.00 22.96           C  
ANISOU 1248  C   ARG A 182     1649   3004   4069    -19      0   -276       C  
ATOM   1249  O   ARG A 182      67.750  39.617  58.250  1.00 22.35           O  
ANISOU 1249  O   ARG A 182     1581   2950   3959    -74     74   -345       O  
ATOM   1250  CB  ARG A 182      64.498  39.396  58.634  1.00 23.81           C  
ANISOU 1250  CB  ARG A 182     1805   3250   3992   -132    -16   -293       C  
ATOM   1251  CG  ARG A 182      64.679  38.364  57.515  1.00 25.09           C  
ANISOU 1251  CG  ARG A 182     1819   3361   4354    -44    -54   -339       C  
ATOM   1252  CD  ARG A 182      63.302  37.836  57.044  1.00 28.30           C  
ANISOU 1252  CD  ARG A 182     2226   3749   4778    -61   -522   -340       C  
ATOM   1253  NE  ARG A 182      63.343  36.854  55.954  1.00 28.56           N  
ANISOU 1253  NE  ARG A 182     2176   3912   4760    265   -569   -368       N  
ATOM   1254  CZ  ARG A 182      63.707  35.577  56.078  1.00 30.80           C  
ANISOU 1254  CZ  ARG A 182     2702   4138   4863     73   -537   -412       C  
ATOM   1255  NH1 ARG A 182      64.126  35.079  57.244  1.00 33.42           N  
ANISOU 1255  NH1 ARG A 182     3195   4370   5132    392   -627   -167       N  
ATOM   1256  NH2 ARG A 182      63.696  34.787  55.013  1.00 27.56           N  
ANISOU 1256  NH2 ARG A 182     1658   4245   4568    -72   -163   -432       N  
ATOM   1257  N   PHE A 183      66.699  41.619  58.440  1.00 22.36           N  
ANISOU 1257  N   PHE A 183     1568   2822   4104     21      5   -359       N  
ATOM   1258  CA  PHE A 183      67.636  42.331  57.576  1.00 22.46           C  
ANISOU 1258  CA  PHE A 183     1728   2683   4121     58   -179   -370       C  
ATOM   1259  C   PHE A 183      68.157  43.588  58.271  1.00 22.66           C  
ANISOU 1259  C   PHE A 183     1744   2784   4080     66   -258   -418       C  
ATOM   1260  O   PHE A 183      67.705  44.702  57.993  1.00 22.00           O  
ANISOU 1260  O   PHE A 183     1569   2763   4026    136   -358   -569       O  
ATOM   1261  CB  PHE A 183      66.988  42.674  56.231  1.00 22.56           C  
ANISOU 1261  CB  PHE A 183     1773   2705   4092     -8   -152   -427       C  
ATOM   1262  CG  PHE A 183      66.457  41.482  55.480  1.00 21.98           C  
ANISOU 1262  CG  PHE A 183     1736   2345   4270     86    -94   -348       C  
ATOM   1263  CD1 PHE A 183      67.305  40.462  55.041  1.00 21.00           C  
ANISOU 1263  CD1 PHE A 183     1666   2241   4072    109     11   -364       C  
ATOM   1264  CD2 PHE A 183      65.107  41.388  55.193  1.00 21.67           C  
ANISOU 1264  CD2 PHE A 183     1656   2245   4332    198   -237   -302       C  
ATOM   1265  CE1 PHE A 183      66.791  39.374  54.337  1.00 22.23           C  
ANISOU 1265  CE1 PHE A 183     1634   2498   4314      9   -125   -174       C  
ATOM   1266  CE2 PHE A 183      64.585  40.297  54.496  1.00 22.28           C  
ANISOU 1266  CE2 PHE A 183     1807   2197   4460     63   -161   -271       C  
ATOM   1267  CZ  PHE A 183      65.422  39.298  54.058  1.00 21.76           C  
ANISOU 1267  CZ  PHE A 183     1476   2220   4572     52   -147   -407       C  
ATOM   1268  N   PRO A 184      69.134  43.418  59.176  1.00 23.45           N  
ANISOU 1268  N   PRO A 184     1897   2880   4130     84   -295   -387       N  
ATOM   1269  CA  PRO A 184      69.692  44.585  59.858  1.00 24.14           C  
ANISOU 1269  CA  PRO A 184     2118   2868   4184    100   -229   -390       C  
ATOM   1270  C   PRO A 184      70.212  45.623  58.863  1.00 25.88           C  
ANISOU 1270  C   PRO A 184     2479   3058   4296     90   -175   -306       C  
ATOM   1271  O   PRO A 184      70.670  45.297  57.768  1.00 25.85           O  
ANISOU 1271  O   PRO A 184     2469   3084   4269     56      0   -276       O  
ATOM   1272  CB  PRO A 184      70.852  44.006  60.673  1.00 23.95           C  
ANISOU 1272  CB  PRO A 184     2035   2909   4155    -45   -343   -359       C  
ATOM   1273  CG  PRO A 184      70.511  42.548  60.866  1.00 23.96           C  
ANISOU 1273  CG  PRO A 184     2111   2859   4131    134   -387   -471       C  
ATOM   1274  CD  PRO A 184      69.749  42.152  59.614  1.00 22.97           C  
ANISOU 1274  CD  PRO A 184     1860   2773   4093     98   -357   -441       C  
ATOM   1275  N   LEU A 185      70.116  46.890  59.239  1.00 28.11           N  
ANISOU 1275  N   LEU A 185     2890   3281   4507     81   -154   -191       N  
ATOM   1276  CA  LEU A 185      70.632  47.949  58.385  1.00 29.39           C  
ANISOU 1276  CA  LEU A 185     2922   3557   4688     89   -122    -81       C  
ATOM   1277  C   LEU A 185      71.832  48.666  58.994  1.00 28.83           C  
ANISOU 1277  C   LEU A 185     2744   3431   4776    149    -65   -115       C  
ATOM   1278  O   LEU A 185      71.846  49.885  59.087  1.00 29.51           O  
ANISOU 1278  O   LEU A 185     2941   3452   4818    206     58   -177       O  
ATOM   1279  CB  LEU A 185      69.494  48.924  58.094  1.00 30.74           C  
ANISOU 1279  CB  LEU A 185     3116   3776   4786    198   -225     -1       C  
ATOM   1280  CG  LEU A 185      68.762  48.887  56.750  1.00 34.94           C  
ANISOU 1280  CG  LEU A 185     3683   4572   5019    -80   -269    127       C  
ATOM   1281  CD1 LEU A 185      67.238  48.761  56.965  1.00 36.55           C  
ANISOU 1281  CD1 LEU A 185     3613   5066   5208   -140   -511    273       C  
ATOM   1282  CD2 LEU A 185      69.145  50.186  55.992  1.00 37.42           C  
ANISOU 1282  CD2 LEU A 185     4478   4644   5093    122   -222    393       C  
ATOM   1283  N   GLY A 186      72.884  47.921  59.327  1.00 28.32           N  
ANISOU 1283  N   GLY A 186     2534   3423   4800    -26   -139    -84       N  
ATOM   1284  CA  GLY A 186      74.040  48.491  60.008  1.00 26.00           C  
ANISOU 1284  CA  GLY A 186     2051   3252   4577     39     70   -116       C  
ATOM   1285  C   GLY A 186      74.221  47.860  61.373  1.00 24.20           C  
ANISOU 1285  C   GLY A 186     1646   3160   4388    -48    146   -132       C  
ATOM   1286  O   GLY A 186      73.267  47.371  61.984  1.00 22.87           O  
ANISOU 1286  O   GLY A 186     1244   3203   4241     89    157   -152       O  
ATOM   1287  N   SER A 187      75.461  47.888  61.844  1.00 22.57           N  
ANISOU 1287  N   SER A 187     1264   2999   4312    -50    371   -171       N  
ATOM   1288  CA  SER A 187      75.846  47.265  63.103  1.00 21.08           C  
ANISOU 1288  CA  SER A 187     1110   2673   4226   -111    468   -223       C  
ATOM   1289  C   SER A 187      76.091  48.299  64.206  1.00 20.35           C  
ANISOU 1289  C   SER A 187      929   2671   4129   -140    506   -169       C  
ATOM   1290  O   SER A 187      76.056  49.513  63.967  1.00 19.90           O  
ANISOU 1290  O   SER A 187     1134   2489   3938   -201    471   -211       O  
ATOM   1291  CB  SER A 187      77.070  46.363  62.868  1.00 20.74           C  
ANISOU 1291  CB  SER A 187      825   2788   4265   -202    608   -230       C  
ATOM   1292  OG  SER A 187      78.211  47.157  62.610  1.00 21.41           O  
ANISOU 1292  OG  SER A 187     1451   2521   4161   -390    703   -571       O  
ATOM   1293  N   ASP A 188      76.281  47.819  65.429  1.00 18.73           N  
ANISOU 1293  N   ASP A 188      619   2490   4005   -132    435   -143       N  
ATOM   1294  CA  ASP A 188      76.538  48.689  66.562  1.00 18.25           C  
ANISOU 1294  CA  ASP A 188      516   2406   4010   -199    463   -203       C  
ATOM   1295  C   ASP A 188      77.997  49.131  66.661  1.00 18.15           C  
ANISOU 1295  C   ASP A 188      514   2422   3957   -256    385   -234       C  
ATOM   1296  O   ASP A 188      78.298  50.183  67.241  1.00 18.66           O  
ANISOU 1296  O   ASP A 188      566   2467   4054   -185    546   -171       O  
ATOM   1297  CB  ASP A 188      76.102  47.997  67.847  1.00 18.68           C  
ANISOU 1297  CB  ASP A 188      591   2492   4013   -245    476   -236       C  
ATOM   1298  CG  ASP A 188      74.600  47.844  67.906  1.00 19.35           C  
ANISOU 1298  CG  ASP A 188      723   2539   4087    -43    262   -200       C  
ATOM   1299  OD1 ASP A 188      73.937  48.856  68.205  1.00 22.38           O  
ANISOU 1299  OD1 ASP A 188      920   2697   4885    -76    490   -479       O  
ATOM   1300  OD2 ASP A 188      74.077  46.741  67.632  1.00 19.29           O  
ANISOU 1300  OD2 ASP A 188     1194   2506   3627    -20     -7   -279       O  
ATOM   1301  N   SER A 189      78.895  48.336  66.089  1.00 16.98           N  
ANISOU 1301  N   SER A 189      417   2257   3774   -322    286   -243       N  
ATOM   1302  CA  SER A 189      80.302  48.724  66.027  1.00 17.45           C  
ANISOU 1302  CA  SER A 189      587   2325   3715   -229     94   -191       C  
ATOM   1303  C   SER A 189      81.005  47.983  64.898  1.00 17.05           C  
ANISOU 1303  C   SER A 189      539   2359   3579   -230     51   -161       C  
ATOM   1304  O   SER A 189      80.510  46.967  64.408  1.00 17.40           O  
ANISOU 1304  O   SER A 189      672   2221   3718   -168    184    -99       O  
ATOM   1305  CB  SER A 189      81.006  48.442  67.364  1.00 17.89           C  
ANISOU 1305  CB  SER A 189      738   2316   3743   -366    -20   -240       C  
ATOM   1306  OG  SER A 189      80.858  47.085  67.795  1.00 19.70           O  
ANISOU 1306  OG  SER A 189     1348   2349   3787   -255   -224   -151       O  
ATOM   1307  N   THR A 190      82.155  48.511  64.498  1.00 16.16           N  
ANISOU 1307  N   THR A 190      452   2192   3494   -202    -39    -66       N  
ATOM   1308  CA  THR A 190      83.085  47.820  63.622  1.00 16.74           C  
ANISOU 1308  CA  THR A 190      446   2284   3630   -113    -62     17       C  
ATOM   1309  C   THR A 190      84.239  47.411  64.516  1.00 16.79           C  
ANISOU 1309  C   THR A 190      556   2228   3593   -112    -62     66       C  
ATOM   1310  O   THR A 190      84.768  48.248  65.251  1.00 17.47           O  
ANISOU 1310  O   THR A 190      702   2210   3723   -117   -104    118       O  
ATOM   1311  CB  THR A 190      83.623  48.791  62.555  1.00 17.19           C  
ANISOU 1311  CB  THR A 190      498   2380   3650    -86    -42     49       C  
ATOM   1312  OG1 THR A 190      82.540  49.199  61.716  1.00 16.94           O  
ANISOU 1312  OG1 THR A 190      379   2165   3892    -41   -134   -108       O  
ATOM   1313  CG2 THR A 190      84.668  48.117  61.686  1.00 18.01           C  
ANISOU 1313  CG2 THR A 190      499   2447   3896    -35     25   -173       C  
ATOM   1314  N   LEU A 191      84.616  46.135  64.454  1.00 15.90           N  
ANISOU 1314  N   LEU A 191      489   2096   3455    -67    -66    223       N  
ATOM   1315  CA  LEU A 191      85.735  45.630  65.234  1.00 15.92           C  
ANISOU 1315  CA  LEU A 191      381   2126   3543   -165     14    170       C  
ATOM   1316  C   LEU A 191      86.916  45.421  64.295  1.00 16.20           C  
ANISOU 1316  C   LEU A 191      422   2111   3620   -168     26    195       C  
ATOM   1317  O   LEU A 191      86.782  44.803  63.231  1.00 16.62           O  
ANISOU 1317  O   LEU A 191      394   2152   3766   -185    -11    169       O  
ATOM   1318  CB  LEU A 191      85.347  44.313  65.922  1.00 15.32           C  
ANISOU 1318  CB  LEU A 191      468   1998   3351    -56    -72    227       C  
ATOM   1319  CG  LEU A 191      84.068  44.309  66.762  1.00 15.58           C  
ANISOU 1319  CG  LEU A 191      703   1907   3309   -305     57     86       C  
ATOM   1320  CD1 LEU A 191      83.800  42.901  67.349  1.00 16.27           C  
ANISOU 1320  CD1 LEU A 191     1062   1969   3148   -284   -115    185       C  
ATOM   1321  CD2 LEU A 191      84.169  45.338  67.889  1.00 16.72           C  
ANISOU 1321  CD2 LEU A 191     1268   2074   3009      8    230    116       C  
ATOM   1322  N   ILE A 192      88.066  45.958  64.683  1.00 16.49           N  
ANISOU 1322  N   ILE A 192      325   2153   3786   -241     61    140       N  
ATOM   1323  CA  ILE A 192      89.307  45.705  63.946  1.00 17.02           C  
ANISOU 1323  CA  ILE A 192      380   2141   3944    -91     15    207       C  
ATOM   1324  C   ILE A 192      90.172  44.892  64.898  1.00 17.76           C  
ANISOU 1324  C   ILE A 192      486   2224   4038    -91     48    170       C  
ATOM   1325  O   ILE A 192      90.450  45.346  66.006  1.00 18.53           O  
ANISOU 1325  O   ILE A 192      670   2205   4164     36    -35     68       O  
ATOM   1326  CB  ILE A 192      90.002  47.047  63.556  1.00 17.21           C  
ANISOU 1326  CB  ILE A 192      307   2225   4005    -57      1    243       C  
ATOM   1327  CG1 ILE A 192      89.089  47.839  62.597  1.00 17.57           C  
ANISOU 1327  CG1 ILE A 192      922   2015   3739     30   -242    336       C  
ATOM   1328  CG2 ILE A 192      91.347  46.775  62.892  1.00 17.85           C  
ANISOU 1328  CG2 ILE A 192      290   2421   4070      7     56    188       C  
ATOM   1329  CD1 ILE A 192      89.490  49.294  62.371  1.00 17.12           C  
ANISOU 1329  CD1 ILE A 192      951   2169   3382   -114   -549    409       C  
ATOM   1330  N   ASN A 193      90.583  43.692  64.491  1.00 17.51           N  
ANISOU 1330  N   ASN A 193      389   2209   4053     29    106    159       N  
ATOM   1331  CA  ASN A 193      91.283  42.799  65.413  1.00 18.54           C  
ANISOU 1331  CA  ASN A 193      537   2445   4059      0     61    105       C  
ATOM   1332  C   ASN A 193      90.522  42.643  66.721  1.00 19.04           C  
ANISOU 1332  C   ASN A 193      622   2523   4086    -25    -29    109       C  
ATOM   1333  O   ASN A 193      91.108  42.686  67.800  1.00 20.10           O  
ANISOU 1333  O   ASN A 193      775   2733   4126     38   -183    213       O  
ATOM   1334  CB  ASN A 193      92.721  43.266  65.652  1.00 19.14           C  
ANISOU 1334  CB  ASN A 193      621   2479   4173    -34     93     90       C  
ATOM   1335  CG  ASN A 193      93.584  43.059  64.426  1.00 19.87           C  
ANISOU 1335  CG  ASN A 193      644   2658   4247     60    155     80       C  
ATOM   1336  OD1 ASN A 193      93.177  42.356  63.506  1.00 20.78           O  
ANISOU 1336  OD1 ASN A 193      537   3110   4248    135    140   -108       O  
ATOM   1337  ND2 ASN A 193      94.769  43.655  64.403  1.00 21.37           N  
ANISOU 1337  ND2 ASN A 193      755   2757   4605    112    -22    149       N  
ATOM   1338  N   GLY A 194      89.202  42.530  66.610  1.00 18.80           N  
ANISOU 1338  N   GLY A 194      635   2410   4097    -43     -9     49       N  
ATOM   1339  CA  GLY A 194      88.400  42.162  67.757  1.00 18.80           C  
ANISOU 1339  CA  GLY A 194      561   2420   4162     -5    -50     30       C  
ATOM   1340  C   GLY A 194      88.011  43.302  68.671  1.00 18.90           C  
ANISOU 1340  C   GLY A 194      594   2432   4154     -7   -129     56       C  
ATOM   1341  O   GLY A 194      87.259  43.064  69.608  1.00 19.69           O  
ANISOU 1341  O   GLY A 194      784   2458   4239    -16     17    141       O  
ATOM   1342  N   LEU A 195      88.480  44.523  68.412  1.00 18.61           N  
ANISOU 1342  N   LEU A 195      543   2397   4127      7   -244    107       N  
ATOM   1343  CA  LEU A 195      88.167  45.669  69.272  1.00 18.64           C  
ANISOU 1343  CA  LEU A 195      500   2485   4096     48   -397    115       C  
ATOM   1344  C   LEU A 195      87.664  46.863  68.460  1.00 18.25           C  
ANISOU 1344  C   LEU A 195      541   2322   4068    122   -335     39       C  
ATOM   1345  O   LEU A 195      88.032  47.053  67.296  1.00 18.35           O  
ANISOU 1345  O   LEU A 195      624   2265   4082    174   -403    113       O  
ATOM   1346  CB  LEU A 195      89.421  46.111  70.050  1.00 18.64           C  
ANISOU 1346  CB  LEU A 195      494   2586   4002    -13   -523     85       C  
ATOM   1347  CG  LEU A 195      90.100  45.123  71.011  1.00 19.89           C  
ANISOU 1347  CG  LEU A 195      368   2978   4210    -84   -504    387       C  
ATOM   1348  CD1 LEU A 195      91.453  45.684  71.477  1.00 21.42           C  
ANISOU 1348  CD1 LEU A 195      639   3388   4110   -142   -768    107       C  
ATOM   1349  CD2 LEU A 195      89.206  44.838  72.216  1.00 21.25           C  
ANISOU 1349  CD2 LEU A 195      839   3262   3971    343   -598    688       C  
ATOM   1350  N   GLY A 196      86.813  47.671  69.081  1.00 17.78           N  
ANISOU 1350  N   GLY A 196      531   2241   3983     46   -396    -30       N  
ATOM   1351  CA  GLY A 196      86.459  48.954  68.484  1.00 16.94           C  
ANISOU 1351  CA  GLY A 196      496   2155   3786    131   -318    -95       C  
ATOM   1352  C   GLY A 196      85.475  49.706  69.345  1.00 17.58           C  
ANISOU 1352  C   GLY A 196      571   2266   3840     80   -277   -165       C  
ATOM   1353  O   GLY A 196      85.016  49.190  70.372  1.00 18.16           O  
ANISOU 1353  O   GLY A 196      652   2394   3850    191   -169   -149       O  
ATOM   1354  N   ARG A 197      85.167  50.927  68.926  1.00 17.07           N  
ANISOU 1354  N   ARG A 197      449   2229   3805    142   -250   -193       N  
ATOM   1355  CA  ARG A 197      84.239  51.781  69.663  1.00 17.82           C  
ANISOU 1355  CA  ARG A 197      598   2284   3888    129   -332   -312       C  
ATOM   1356  C   ARG A 197      82.805  51.632  69.168  1.00 17.55           C  
ANISOU 1356  C   ARG A 197      515   2240   3912     69   -221   -313       C  
ATOM   1357  O   ARG A 197      82.565  51.490  67.972  1.00 17.41           O  
ANISOU 1357  O   ARG A 197      545   2284   3786    176   -361   -407       O  
ATOM   1358  CB  ARG A 197      84.687  53.249  69.576  1.00 16.91           C  
ANISOU 1358  CB  ARG A 197      341   2227   3856    -57   -346   -279       C  
ATOM   1359  CG  ARG A 197      86.030  53.439  70.254  1.00 20.39           C  
ANISOU 1359  CG  ARG A 197      970   2893   3882    206   -813   -315       C  
ATOM   1360  CD  ARG A 197      86.047  54.652  71.132  1.00 21.55           C  
ANISOU 1360  CD  ARG A 197     1278   3125   3783    134   -839   -356       C  
ATOM   1361  NE  ARG A 197      87.241  54.663  71.975  1.00 20.54           N  
ANISOU 1361  NE  ARG A 197     1273   3238   3294    145   -899      5       N  
ATOM   1362  CZ  ARG A 197      88.227  55.551  71.865  1.00 23.66           C  
ANISOU 1362  CZ  ARG A 197     1869   3391   3728    -12   -779     61       C  
ATOM   1363  NH1 ARG A 197      88.155  56.503  70.944  1.00 25.34           N  
ANISOU 1363  NH1 ARG A 197     2393   3083   4150   -112   -674    130       N  
ATOM   1364  NH2 ARG A 197      89.276  55.498  72.679  1.00 22.82           N  
ANISOU 1364  NH2 ARG A 197     1629   3349   3691     38   -713    -57       N  
ATOM   1365  N   SER A 198      81.853  51.695  70.087  1.00 18.71           N  
ANISOU 1365  N   SER A 198      645   2403   4058     91    -92   -305       N  
ATOM   1366  CA  SER A 198      80.437  51.646  69.716  1.00 19.21           C  
ANISOU 1366  CA  SER A 198      750   2378   4171     60   -104   -274       C  
ATOM   1367  C   SER A 198      79.781  53.003  69.950  1.00 20.17           C  
ANISOU 1367  C   SER A 198      878   2518   4265     99      3   -316       C  
ATOM   1368  O   SER A 198      79.824  53.531  71.064  1.00 20.79           O  
ANISOU 1368  O   SER A 198     1110   2549   4237    142    -13   -312       O  
ATOM   1369  CB  SER A 198      79.691  50.595  70.531  1.00 19.44           C  
ANISOU 1369  CB  SER A 198      602   2522   4260     -1    -29   -358       C  
ATOM   1370  OG  SER A 198      78.309  50.675  70.215  1.00 21.39           O  
ANISOU 1370  OG  SER A 198      605   2751   4768     15    -16    -99       O  
ATOM   1371  N   ALA A 199      79.177  53.566  68.905  1.00 20.43           N  
ANISOU 1371  N   ALA A 199      968   2442   4351     27     23   -215       N  
ATOM   1372  CA  ALA A 199      78.427  54.813  69.050  1.00 21.48           C  
ANISOU 1372  CA  ALA A 199     1117   2557   4485     55    162   -226       C  
ATOM   1373  C   ALA A 199      77.142  54.567  69.832  1.00 22.94           C  
ANISOU 1373  C   ALA A 199     1358   2739   4619     -6    248   -252       C  
ATOM   1374  O   ALA A 199      76.626  55.482  70.471  1.00 24.14           O  
ANISOU 1374  O   ALA A 199     1502   2792   4875    182    197   -202       O  
ATOM   1375  CB  ALA A 199      78.098  55.401  67.676  1.00 21.50           C  
ANISOU 1375  CB  ALA A 199     1187   2501   4480     47     67   -215       C  
ATOM   1376  N   THR A 200      76.641  53.334  69.814  1.00 23.76           N  
ANISOU 1376  N   THR A 200     1380   2955   4690   -178    315   -248       N  
ATOM   1377  CA  THR A 200      75.382  52.996  70.507  1.00 24.66           C  
ANISOU 1377  CA  THR A 200     1522   3133   4712   -236    452   -312       C  
ATOM   1378  C   THR A 200      75.515  53.180  72.009  1.00 24.91           C  
ANISOU 1378  C   THR A 200     1586   3116   4761   -221    513   -348       C  
ATOM   1379  O   THR A 200      74.595  53.675  72.660  1.00 25.31           O  
ANISOU 1379  O   THR A 200     1653   3238   4725   -202    586   -404       O  
ATOM   1380  CB  THR A 200      75.002  51.522  70.260  1.00 24.69           C  
ANISOU 1380  CB  THR A 200     1425   3164   4790   -262    430   -288       C  
ATOM   1381  OG1 THR A 200      75.023  51.262  68.852  1.00 24.81           O  
ANISOU 1381  OG1 THR A 200     1413   3202   4811   -350    369   -177       O  
ATOM   1382  CG2 THR A 200      73.624  51.149  70.857  1.00 25.79           C  
ANISOU 1382  CG2 THR A 200     1611   3395   4793   -276    581   -387       C  
ATOM   1383  N   THR A 201      76.663  52.781  72.550  1.00 25.05           N  
ANISOU 1383  N   THR A 201     1708   3109   4699   -235    474   -390       N  
ATOM   1384  CA  THR A 201      76.830  52.709  73.997  1.00 25.64           C  
ANISOU 1384  CA  THR A 201     1783   3142   4816   -230    431   -460       C  
ATOM   1385  C   THR A 201      77.892  53.674  74.501  1.00 25.93           C  
ANISOU 1385  C   THR A 201     1853   3160   4839   -149    358   -528       C  
ATOM   1386  O   THR A 201      78.056  53.822  75.715  1.00 26.40           O  
ANISOU 1386  O   THR A 201     1813   3330   4887    -63    448   -493       O  
ATOM   1387  CB  THR A 201      77.176  51.274  74.467  1.00 25.26           C  
ANISOU 1387  CB  THR A 201     1722   3074   4801   -261    517   -448       C  
ATOM   1388  OG1 THR A 201      78.172  50.719  73.605  1.00 23.70           O  
ANISOU 1388  OG1 THR A 201     1595   2785   4623   -249    522   -439       O  
ATOM   1389  CG2 THR A 201      75.935  50.384  74.450  1.00 25.40           C  
ANISOU 1389  CG2 THR A 201     1644   3184   4823   -440    392   -653       C  
ATOM   1390  N   ALA A 202      78.592  54.324  73.572  1.00 25.77           N  
ANISOU 1390  N   ALA A 202     1939   3097   4755   -112    328   -533       N  
ATOM   1391  CA  ALA A 202      79.698  55.226  73.904  1.00 25.56           C  
ANISOU 1391  CA  ALA A 202     1978   2955   4775     -8    160   -657       C  
ATOM   1392  C   ALA A 202      80.752  54.473  74.716  1.00 25.80           C  
ANISOU 1392  C   ALA A 202     2109   2942   4748    -31    128   -654       C  
ATOM   1393  O   ALA A 202      81.232  54.964  75.742  1.00 26.15           O  
ANISOU 1393  O   ALA A 202     2258   2813   4863    -82     -2   -726       O  
ATOM   1394  CB  ALA A 202      79.183  56.464  74.662  1.00 27.28           C  
ANISOU 1394  CB  ALA A 202     2385   3150   4827    -42    129   -643       C  
ATOM   1395  N   THR A 203      81.113  53.277  74.251  1.00 24.03           N  
ANISOU 1395  N   THR A 203     1771   2732   4626     29    133   -628       N  
ATOM   1396  CA  THR A 203      82.075  52.426  74.949  1.00 23.58           C  
ANISOU 1396  CA  THR A 203     1601   2810   4549     60    240   -588       C  
ATOM   1397  C   THR A 203      83.078  51.853  73.944  1.00 22.48           C  
ANISOU 1397  C   THR A 203     1360   2725   4455     71    209   -592       C  
ATOM   1398  O   THR A 203      82.899  52.001  72.733  1.00 21.14           O  
ANISOU 1398  O   THR A 203     1127   2542   4359    168    373   -566       O  
ATOM   1399  CB  THR A 203      81.387  51.245  75.690  1.00 23.35           C  
ANISOU 1399  CB  THR A 203     1584   2754   4533     48    228   -580       C  
ATOM   1400  OG1 THR A 203      80.598  50.484  74.764  1.00 22.92           O  
ANISOU 1400  OG1 THR A 203     1515   2658   4535    -97    313   -527       O  
ATOM   1401  CG2 THR A 203      80.471  51.739  76.808  1.00 25.18           C  
ANISOU 1401  CG2 THR A 203     1923   3145   4496    130    270   -540       C  
ATOM   1402  N   GLY A 204      84.121  51.199  74.452  1.00 22.19           N  
ANISOU 1402  N   GLY A 204     1322   2706   4400     10     76   -566       N  
ATOM   1403  CA  GLY A 204      85.043  50.466  73.587  1.00 21.73           C  
ANISOU 1403  CA  GLY A 204     1077   2897   4281    -35     11   -456       C  
ATOM   1404  C   GLY A 204      86.448  51.033  73.561  1.00 22.99           C  
ANISOU 1404  C   GLY A 204     1380   3009   4345   -130    -54   -397       C  
ATOM   1405  O   GLY A 204      86.648  52.227  73.819  1.00 22.79           O  
ANISOU 1405  O   GLY A 204     1286   3015   4355   -141   -145   -407       O  
ATOM   1406  N   ASP A 205      87.400  50.160  73.230  1.00 22.30           N  
ANISOU 1406  N   ASP A 205     1220   3007   4246   -128    -74   -317       N  
ATOM   1407  CA  ASP A 205      88.807  50.527  73.133  1.00 23.19           C  
ANISOU 1407  CA  ASP A 205     1450   3191   4171   -148    -83   -258       C  
ATOM   1408  C   ASP A 205      89.231  50.390  71.673  1.00 22.36           C  
ANISOU 1408  C   ASP A 205     1299   3086   4112   -165   -102   -351       C  
ATOM   1409  O   ASP A 205      88.545  49.775  70.855  1.00 23.76           O  
ANISOU 1409  O   ASP A 205     1603   3346   4077   -243    -44   -283       O  
ATOM   1410  CB  ASP A 205      89.661  49.633  74.034  1.00 24.22           C  
ANISOU 1410  CB  ASP A 205     1528   3362   4312   -191   -123   -244       C  
ATOM   1411  CG  ASP A 205      89.358  49.827  75.513  1.00 28.41           C  
ANISOU 1411  CG  ASP A 205     2529   3660   4604    -53   -150   -213       C  
ATOM   1412  OD1 ASP A 205      89.063  50.964  75.939  1.00 31.90           O  
ANISOU 1412  OD1 ASP A 205     3135   3936   5046      0   -238   -479       O  
ATOM   1413  OD2 ASP A 205      89.420  48.836  76.272  1.00 35.26           O  
ANISOU 1413  OD2 ASP A 205     3896   4241   5258   -371     -1    219       O  
ATOM   1414  N   LEU A 206      90.359  50.995  71.339  1.00 21.99           N  
ANISOU 1414  N   LEU A 206     1329   2974   4052   -217   -146   -339       N  
ATOM   1415  CA  LEU A 206      90.903  50.900  69.994  1.00 20.41           C  
ANISOU 1415  CA  LEU A 206     1047   2788   3917   -178   -280   -415       C  
ATOM   1416  C   LEU A 206      91.977  49.831  69.947  1.00 19.94           C  
ANISOU 1416  C   LEU A 206      860   2768   3947   -179   -391   -342       C  
ATOM   1417  O   LEU A 206      92.881  49.798  70.802  1.00 19.98           O  
ANISOU 1417  O   LEU A 206      815   2964   3810   -103   -426   -382       O  
ATOM   1418  CB  LEU A 206      91.524  52.250  69.591  1.00 20.24           C  
ANISOU 1418  CB  LEU A 206      991   2668   4030   -138   -309   -390       C  
ATOM   1419  CG  LEU A 206      90.520  53.406  69.508  1.00 19.85           C  
ANISOU 1419  CG  LEU A 206     1027   2564   3951   -137   -474   -532       C  
ATOM   1420  CD1 LEU A 206      91.272  54.755  69.471  1.00 21.66           C  
ANISOU 1420  CD1 LEU A 206      998   2707   4523   -314   -503   -434       C  
ATOM   1421  CD2 LEU A 206      89.614  53.233  68.296  1.00 21.97           C  
ANISOU 1421  CD2 LEU A 206      790   3066   4492    141   -787   -337       C  
ATOM   1422  N   ALA A 207      91.907  48.983  68.924  1.00 19.13           N  
ANISOU 1422  N   ALA A 207      550   2753   3964   -138   -405   -383       N  
ATOM   1423  CA  ALA A 207      93.005  48.053  68.648  1.00 19.02           C  
ANISOU 1423  CA  ALA A 207      433   2717   4075   -133   -480   -310       C  
ATOM   1424  C   ALA A 207      94.274  48.830  68.301  1.00 19.53           C  
ANISOU 1424  C   ALA A 207      481   2785   4154   -124   -545   -270       C  
ATOM   1425  O   ALA A 207      94.213  49.912  67.697  1.00 19.64           O  
ANISOU 1425  O   ALA A 207      533   2776   4154    -80   -669   -218       O  
ATOM   1426  CB  ALA A 207      92.632  47.135  67.494  1.00 19.12           C  
ANISOU 1426  CB  ALA A 207      365   2768   4131   -157   -444   -305       C  
ATOM   1427  N   VAL A 208      95.428  48.275  68.660  1.00 19.34           N  
ANISOU 1427  N   VAL A 208      389   2771   4187   -129   -556   -133       N  
ATOM   1428  CA  VAL A 208      96.701  48.909  68.305  1.00 19.75           C  
ANISOU 1428  CA  VAL A 208      406   2836   4261   -122   -615   -195       C  
ATOM   1429  C   VAL A 208      97.449  47.904  67.440  1.00 20.38           C  
ANISOU 1429  C   VAL A 208      468   2888   4387    -76   -517   -143       C  
ATOM   1430  O   VAL A 208      97.612  46.751  67.838  1.00 20.56           O  
ANISOU 1430  O   VAL A 208      653   2749   4409      9   -565   -172       O  
ATOM   1431  CB  VAL A 208      97.505  49.293  69.558  1.00 19.80           C  
ANISOU 1431  CB  VAL A 208      401   2880   4243   -156   -578   -207       C  
ATOM   1432  CG1 VAL A 208      98.908  49.815  69.189  1.00 20.15           C  
ANISOU 1432  CG1 VAL A 208      480   2936   4240   -367   -659   -262       C  
ATOM   1433  CG2 VAL A 208      96.738  50.326  70.365  1.00 21.25           C  
ANISOU 1433  CG2 VAL A 208      730   2961   4380    -74   -752   -165       C  
ATOM   1434  N   ILE A 209      97.814  48.324  66.232  1.00 20.62           N  
ANISOU 1434  N   ILE A 209      451   2928   4453   -157   -480   -138       N  
ATOM   1435  CA  ILE A 209      98.656  47.530  65.346  1.00 21.01           C  
ANISOU 1435  CA  ILE A 209      354   3049   4577    -89   -491    -62       C  
ATOM   1436  C   ILE A 209     100.062  48.148  65.401  1.00 22.05           C  
ANISOU 1436  C   ILE A 209      472   3089   4818   -138   -444     -7       C  
ATOM   1437  O   ILE A 209     100.245  49.334  65.077  1.00 21.44           O  
ANISOU 1437  O   ILE A 209      340   2937   4868    -56   -455    -13       O  
ATOM   1438  CB  ILE A 209      98.073  47.541  63.913  1.00 21.46           C  
ANISOU 1438  CB  ILE A 209      395   3220   4536   -217   -414   -152       C  
ATOM   1439  CG1 ILE A 209      96.674  46.913  63.899  1.00 20.99           C  
ANISOU 1439  CG1 ILE A 209      526   3116   4333   -424   -729      4       C  
ATOM   1440  CG2 ILE A 209      99.010  46.822  62.931  1.00 22.55           C  
ANISOU 1440  CG2 ILE A 209      582   3294   4691     52   -239    -36       C  
ATOM   1441  CD1 ILE A 209      95.893  47.174  62.629  1.00 21.91           C  
ANISOU 1441  CD1 ILE A 209      722   3291   4311   -876   -777    -98       C  
ATOM   1442  N   LYS A 210     101.047  47.363  65.842  1.00 22.24           N  
ANISOU 1442  N   LYS A 210      351   3065   5033   -104   -503     10       N  
ATOM   1443  CA  LYS A 210     102.391  47.896  66.115  1.00 23.19           C  
ANISOU 1443  CA  LYS A 210      484   3091   5236   -226   -389     78       C  
ATOM   1444  C   LYS A 210     103.318  47.700  64.928  1.00 23.59           C  
ANISOU 1444  C   LYS A 210      439   3041   5481   -261   -306     53       C  
ATOM   1445  O   LYS A 210     103.346  46.628  64.320  1.00 24.64           O  
ANISOU 1445  O   LYS A 210      613   3087   5659   -312    -91     91       O  
ATOM   1446  CB  LYS A 210     103.013  47.247  67.357  1.00 23.41           C  
ANISOU 1446  CB  LYS A 210      507   3198   5187   -233   -524     60       C  
ATOM   1447  CG  LYS A 210     102.223  47.471  68.662  1.00 24.07           C  
ANISOU 1447  CG  LYS A 210      673   3440   5030   -222   -541    210       C  
ATOM   1448  CD  LYS A 210     102.966  46.981  69.921  1.00 29.38           C  
ANISOU 1448  CD  LYS A 210     2240   3999   4923   -143   -875    469       C  
ATOM   1449  CE  LYS A 210     102.727  45.485  70.217  1.00 31.82           C  
ANISOU 1449  CE  LYS A 210     2965   4294   4831    173   -832    666       C  
ATOM   1450  NZ  LYS A 210     103.270  44.950  71.520  1.00 33.48           N  
ANISOU 1450  NZ  LYS A 210     3013   4734   4970    480   -843    844       N  
ATOM   1451  N   VAL A 211     104.059  48.745  64.581  1.00 23.83           N  
ANISOU 1451  N   VAL A 211      462   2951   5640   -223   -360     65       N  
ATOM   1452  CA  VAL A 211     105.103  48.635  63.566  1.00 23.87           C  
ANISOU 1452  CA  VAL A 211      330   2927   5810   -187   -392    103       C  
ATOM   1453  C   VAL A 211     106.411  49.239  64.094  1.00 24.38           C  
ANISOU 1453  C   VAL A 211      381   2899   5983   -191   -415     85       C  
ATOM   1454  O   VAL A 211     106.395  50.076  65.002  1.00 24.30           O  
ANISOU 1454  O   VAL A 211      325   3007   5898    -79   -415     75       O  
ATOM   1455  CB  VAL A 211     104.683  49.281  62.219  1.00 24.02           C  
ANISOU 1455  CB  VAL A 211      450   2878   5798   -231   -402     91       C  
ATOM   1456  CG1 VAL A 211     103.499  48.528  61.601  1.00 23.43           C  
ANISOU 1456  CG1 VAL A 211      392   2739   5769   -157   -715    167       C  
ATOM   1457  CG2 VAL A 211     104.340  50.783  62.359  1.00 24.07           C  
ANISOU 1457  CG2 VAL A 211      361   2925   5860    -91   -267    100       C  
ATOM   1458  N   THR A 212     107.533  48.802  63.535  1.00 24.29           N  
ANISOU 1458  N   THR A 212      314   2778   6134   -168   -287    112       N  
ATOM   1459  CA  THR A 212     108.839  49.396  63.862  1.00 25.14           C  
ANISOU 1459  CA  THR A 212      324   2888   6338   -154   -381     91       C  
ATOM   1460  C   THR A 212     109.343  50.138  62.637  1.00 25.41           C  
ANISOU 1460  C   THR A 212      316   2867   6469   -177   -307     93       C  
ATOM   1461  O   THR A 212     109.375  49.572  61.545  1.00 25.79           O  
ANISOU 1461  O   THR A 212      355   2914   6531   -160   -132    109       O  
ATOM   1462  CB  THR A 212     109.863  48.286  64.172  1.00 25.17           C  
ANISOU 1462  CB  THR A 212      320   2908   6335    -99   -401    138       C  
ATOM   1463  OG1 THR A 212     109.364  47.482  65.245  1.00 25.08           O  
ANISOU 1463  OG1 THR A 212      373   2981   6173    -11   -685    208       O  
ATOM   1464  CG2 THR A 212     111.264  48.851  64.502  1.00 27.17           C  
ANISOU 1464  CG2 THR A 212      539   3173   6611   -123   -343    110       C  
ATOM   1465  N   ARG A 213     109.747  51.392  62.817  1.00 26.40           N  
ANISOU 1465  N   ARG A 213      470   2953   6608   -202   -224     96       N  
ATOM   1466  CA  ARG A 213     110.264  52.178  61.712  1.00 27.60           C  
ANISOU 1466  CA  ARG A 213      741   2955   6788   -250   -135     85       C  
ATOM   1467  C   ARG A 213     111.382  51.432  60.982  1.00 27.79           C  
ANISOU 1467  C   ARG A 213      779   2995   6783   -204    -55     60       C  
ATOM   1468  O   ARG A 213     112.297  50.881  61.609  1.00 27.72           O  
ANISOU 1468  O   ARG A 213      836   2801   6894   -178    -88    105       O  
ATOM   1469  CB  ARG A 213     110.781  53.525  62.208  1.00 28.28           C  
ANISOU 1469  CB  ARG A 213      935   2955   6855   -249   -133     55       C  
ATOM   1470  CG  ARG A 213     110.869  54.554  61.101  1.00 31.41           C  
ANISOU 1470  CG  ARG A 213     1552   3065   7316   -544   -173    123       C  
ATOM   1471  CD  ARG A 213     111.431  55.852  61.636  1.00 37.09           C  
ANISOU 1471  CD  ARG A 213     2882   3122   8088   -632   -325     -6       C  
ATOM   1472  NE  ARG A 213     111.164  56.977  60.744  1.00 41.60           N  
ANISOU 1472  NE  ARG A 213     3515   3622   8669   -640   -349    199       N  
ATOM   1473  CZ  ARG A 213     111.566  58.220  60.988  1.00 42.75           C  
ANISOU 1473  CZ  ARG A 213     3842   3491   8910   -709   -354    206       C  
ATOM   1474  NH1 ARG A 213     112.262  58.485  62.087  1.00 43.22           N  
ANISOU 1474  NH1 ARG A 213     4056   3466   8897   -742   -385     56       N  
ATOM   1475  NH2 ARG A 213     111.284  59.194  60.134  1.00 45.59           N  
ANISOU 1475  NH2 ARG A 213     4300   4109   8911   -691   -314    467       N  
ATOM   1476  N   GLY A 214     111.322  51.444  59.654  1.00 27.73           N  
ANISOU 1476  N   GLY A 214      798   2998   6739   -257     33     28       N  
ATOM   1477  CA  GLY A 214     112.338  50.772  58.846  1.00 27.59           C  
ANISOU 1477  CA  GLY A 214      755   3088   6640   -306    256     70       C  
ATOM   1478  C   GLY A 214     111.974  49.360  58.406  1.00 28.42           C  
ANISOU 1478  C   GLY A 214     1039   3181   6576   -241    324    138       C  
ATOM   1479  O   GLY A 214     112.652  48.801  57.544  1.00 29.40           O  
ANISOU 1479  O   GLY A 214     1296   3263   6609   -319    560    140       O  
ATOM   1480  N   LYS A 215     110.940  48.756  58.996  1.00 27.44           N  
ANISOU 1480  N   LYS A 215      796   3256   6371   -256    208    185       N  
ATOM   1481  CA  LYS A 215     110.512  47.412  58.597  1.00 27.40           C  
ANISOU 1481  CA  LYS A 215      984   3256   6171   -149     71    233       C  
ATOM   1482  C   LYS A 215     109.361  47.460  57.585  1.00 26.82           C  
ANISOU 1482  C   LYS A 215      805   3268   6116   -122    102    182       C  
ATOM   1483  O   LYS A 215     108.587  48.425  57.555  1.00 27.28           O  
ANISOU 1483  O   LYS A 215      954   3262   6149    -24     10    149       O  
ATOM   1484  CB  LYS A 215     110.100  46.556  59.809  1.00 27.29           C  
ANISOU 1484  CB  LYS A 215      952   3302   6113    -96    -24    295       C  
ATOM   1485  CG  LYS A 215     111.245  46.217  60.770  1.00 29.05           C  
ANISOU 1485  CG  LYS A 215     1489   3483   6063     38   -262    443       C  
ATOM   1486  CD  LYS A 215     110.682  45.398  61.938  1.00 30.78           C  
ANISOU 1486  CD  LYS A 215     2016   3901   5776    300   -816    800       C  
ATOM   1487  CE  LYS A 215     111.704  45.189  63.045  1.00 32.15           C  
ANISOU 1487  CE  LYS A 215     2285   3979   5950    530  -1008    748       C  
ATOM   1488  NZ  LYS A 215     112.093  43.760  63.132  1.00 33.04           N  
ANISOU 1488  NZ  LYS A 215     2531   4107   5913    572  -1313    880       N  
ATOM   1489  N   ARG A 216     109.255  46.419  56.759  1.00 25.58           N  
ANISOU 1489  N   ARG A 216      619   3141   5958   -161     95    161       N  
ATOM   1490  CA  ARG A 216     108.159  46.286  55.801  1.00 24.92           C  
ANISOU 1490  CA  ARG A 216      474   3198   5794   -181    180    150       C  
ATOM   1491  C   ARG A 216     107.265  45.141  56.265  1.00 24.28           C  
ANISOU 1491  C   ARG A 216      385   3204   5634   -135    190    110       C  
ATOM   1492  O   ARG A 216     107.777  44.093  56.675  1.00 24.01           O  
ANISOU 1492  O   ARG A 216      356   3274   5492   -231    227    111       O  
ATOM   1493  CB  ARG A 216     108.696  46.020  54.391  1.00 24.82           C  
ANISOU 1493  CB  ARG A 216      467   3170   5789   -184    237    131       C  
ATOM   1494  CG  ARG A 216     109.739  47.041  53.926  1.00 25.76           C  
ANISOU 1494  CG  ARG A 216      387   3461   5936   -171    255    150       C  
ATOM   1495  CD  ARG A 216     110.707  46.478  52.863  1.00 28.29           C  
ANISOU 1495  CD  ARG A 216     1075   3483   6189     86    397   -139       C  
ATOM   1496  NE  ARG A 216     111.405  45.259  53.284  1.00 29.81           N  
ANISOU 1496  NE  ARG A 216      924   4028   6375    424    341   -191       N  
ATOM   1497  CZ  ARG A 216     111.783  44.284  52.461  1.00 31.23           C  
ANISOU 1497  CZ  ARG A 216     1173   4162   6528    588    224   -174       C  
ATOM   1498  NH1 ARG A 216     111.574  44.388  51.151  1.00 32.51           N  
ANISOU 1498  NH1 ARG A 216     1394   4570   6388    208    377   -119       N  
ATOM   1499  NH2 ARG A 216     112.371  43.197  52.948  1.00 30.91           N  
ANISOU 1499  NH2 ARG A 216     1145   4037   6563    856    251   -253       N  
ATOM   1500  N   TYR A 217     105.946  45.353  56.216  1.00 23.41           N  
ANISOU 1500  N   TYR A 217      312   3167   5414   -138    150     57       N  
ATOM   1501  CA  TYR A 217     104.986  44.434  56.811  1.00 22.73           C  
ANISOU 1501  CA  TYR A 217      374   3008   5252   -106    103    -11       C  
ATOM   1502  C   TYR A 217     104.099  43.829  55.736  1.00 22.83           C  
ANISOU 1502  C   TYR A 217      539   2937   5197    -61    151    -79       C  
ATOM   1503  O   TYR A 217     103.565  44.548  54.883  1.00 23.44           O  
ANISOU 1503  O   TYR A 217      925   2815   5165    -97     52    -18       O  
ATOM   1504  CB  TYR A 217     104.114  45.174  57.847  1.00 22.73           C  
ANISOU 1504  CB  TYR A 217      326   3134   5176   -145     99    -10       C  
ATOM   1505  CG  TYR A 217     104.926  45.517  59.071  1.00 23.53           C  
ANISOU 1505  CG  TYR A 217      466   3237   5236   -208    -33    -12       C  
ATOM   1506  CD1 TYR A 217     105.810  46.598  59.049  1.00 22.47           C  
ANISOU 1506  CD1 TYR A 217      323   3201   5012   -320    108     19       C  
ATOM   1507  CD2 TYR A 217     104.870  44.723  60.221  1.00 23.71           C  
ANISOU 1507  CD2 TYR A 217      437   3197   5372   -232   -143    -12       C  
ATOM   1508  CE1 TYR A 217     106.622  46.893  60.143  1.00 22.97           C  
ANISOU 1508  CE1 TYR A 217      360   3273   5095   -468     13   -151       C  
ATOM   1509  CE2 TYR A 217     105.679  45.013  61.326  1.00 23.38           C  
ANISOU 1509  CE2 TYR A 217      619   3055   5206   -167   -346    -45       C  
ATOM   1510  CZ  TYR A 217     106.556  46.095  61.265  1.00 23.65           C  
ANISOU 1510  CZ  TYR A 217      433   3399   5154   -238   -427   -188       C  
ATOM   1511  OH  TYR A 217     107.363  46.403  62.332  1.00 24.23           O  
ANISOU 1511  OH  TYR A 217      337   3527   5342    -64   -478   -375       O  
ATOM   1512  N   ARG A 218     103.911  42.516  55.788  1.00 22.05           N  
ANISOU 1512  N   ARG A 218      452   2822   5101    -26    223   -153       N  
ATOM   1513  CA  ARG A 218     102.816  41.929  55.024  1.00 21.40           C  
ANISOU 1513  CA  ARG A 218      423   2788   4919     90    257   -225       C  
ATOM   1514  C   ARG A 218     101.562  41.878  55.891  1.00 21.14           C  
ANISOU 1514  C   ARG A 218      378   2764   4888    156    311   -152       C  
ATOM   1515  O   ARG A 218     101.410  40.960  56.687  1.00 21.26           O  
ANISOU 1515  O   ARG A 218      389   2837   4851    359    461   -117       O  
ATOM   1516  CB  ARG A 218     103.160  40.506  54.549  1.00 21.40           C  
ANISOU 1516  CB  ARG A 218      420   2713   4997     18    220   -218       C  
ATOM   1517  CG  ARG A 218     102.042  39.945  53.660  1.00 21.47           C  
ANISOU 1517  CG  ARG A 218      933   2569   4655    -69     26   -274       C  
ATOM   1518  CD  ARG A 218     102.069  38.442  53.600  1.00 20.42           C  
ANISOU 1518  CD  ARG A 218      938   2486   4335   -259    -64   -283       C  
ATOM   1519  NE  ARG A 218     101.096  37.912  52.641  1.00 19.66           N  
ANISOU 1519  NE  ARG A 218      948   2489   4032    257    -66   -246       N  
ATOM   1520  CZ  ARG A 218     101.412  37.118  51.623  1.00 22.46           C  
ANISOU 1520  CZ  ARG A 218     1160   3283   4088    264    107   -265       C  
ATOM   1521  NH1 ARG A 218     102.687  36.770  51.425  1.00 23.81           N  
ANISOU 1521  NH1 ARG A 218      934   3593   4519     -6    155   -333       N  
ATOM   1522  NH2 ARG A 218     100.451  36.643  50.834  1.00 22.34           N  
ANISOU 1522  NH2 ARG A 218     1179   3239   4068    202    239   -462       N  
ATOM   1523  N   PHE A 219     100.655  42.840  55.725  1.00 20.56           N  
ANISOU 1523  N   PHE A 219      349   2736   4725    184    447   -205       N  
ATOM   1524  CA  PHE A 219      99.381  42.778  56.438  1.00 20.26           C  
ANISOU 1524  CA  PHE A 219      321   2674   4703     44    301   -150       C  
ATOM   1525  C   PHE A 219      98.406  41.927  55.645  1.00 20.32           C  
ANISOU 1525  C   PHE A 219      376   2588   4756    109    360   -166       C  
ATOM   1526  O   PHE A 219      98.307  42.056  54.417  1.00 20.54           O  
ANISOU 1526  O   PHE A 219      395   2657   4750     52    313   -220       O  
ATOM   1527  CB  PHE A 219      98.832  44.175  56.726  1.00 20.26           C  
ANISOU 1527  CB  PHE A 219      356   2740   4598     -1    430   -250       C  
ATOM   1528  CG  PHE A 219      99.592  44.897  57.816  1.00 20.82           C  
ANISOU 1528  CG  PHE A 219      543   2838   4530    -79    126    -90       C  
ATOM   1529  CD1 PHE A 219      99.489  44.473  59.142  1.00 19.99           C  
ANISOU 1529  CD1 PHE A 219      575   2689   4329    154      9   -108       C  
ATOM   1530  CD2 PHE A 219     100.387  46.000  57.523  1.00 21.06           C  
ANISOU 1530  CD2 PHE A 219      756   2863   4383    -49    302    -83       C  
ATOM   1531  CE1 PHE A 219     100.191  45.129  60.165  1.00 19.88           C  
ANISOU 1531  CE1 PHE A 219      649   2677   4226   -135    -16     53       C  
ATOM   1532  CE2 PHE A 219     101.099  46.664  58.529  1.00 19.99           C  
ANISOU 1532  CE2 PHE A 219      650   2652   4290   -290    156    216       C  
ATOM   1533  CZ  PHE A 219     100.990  46.233  59.860  1.00 20.50           C  
ANISOU 1533  CZ  PHE A 219      762   2790   4236   -177    -26    151       C  
ATOM   1534  N   ARG A 220      97.727  41.043  56.368  1.00 19.62           N  
ANISOU 1534  N   ARG A 220      327   2397   4728     79    414   -121       N  
ATOM   1535  CA  ARG A 220      96.738  40.147  55.778  1.00 19.28           C  
ANISOU 1535  CA  ARG A 220      334   2337   4653    246    290   -105       C  
ATOM   1536  C   ARG A 220      95.365  40.578  56.275  1.00 19.33           C  
ANISOU 1536  C   ARG A 220      399   2337   4608    218    315    -23       C  
ATOM   1537  O   ARG A 220      94.987  40.334  57.428  1.00 19.25           O  
ANISOU 1537  O   ARG A 220      368   2310   4635    260    327    184       O  
ATOM   1538  CB  ARG A 220      97.054  38.683  56.134  1.00 19.64           C  
ANISOU 1538  CB  ARG A 220      371   2321   4767    280    280   -160       C  
ATOM   1539  CG  ARG A 220      98.434  38.235  55.647  1.00 19.46           C  
ANISOU 1539  CG  ARG A 220      402   2223   4768    401    345   -159       C  
ATOM   1540  CD  ARG A 220      98.722  36.808  56.136  1.00 19.79           C  
ANISOU 1540  CD  ARG A 220      475   2095   4949    509    313   -417       C  
ATOM   1541  NE  ARG A 220      99.972  36.251  55.617  1.00 20.72           N  
ANISOU 1541  NE  ARG A 220      556   2092   5224    514    493   -265       N  
ATOM   1542  CZ  ARG A 220     100.080  35.480  54.539  1.00 20.05           C  
ANISOU 1542  CZ  ARG A 220      442   1990   5186    382    456   -252       C  
ATOM   1543  NH1 ARG A 220      99.022  35.150  53.819  1.00 21.49           N  
ANISOU 1543  NH1 ARG A 220      591   2274   5301    334    388   -201       N  
ATOM   1544  NH2 ARG A 220     101.264  35.012  54.187  1.00 19.69           N  
ANISOU 1544  NH2 ARG A 220      709   1516   5255    523    421    -86       N  
ATOM   1545  N   LEU A 221      94.658  41.293  55.404  1.00 18.64           N  
ANISOU 1545  N   LEU A 221      331   2300   4450    248    267     -6       N  
ATOM   1546  CA  LEU A 221      93.396  41.925  55.765  1.00 18.21           C  
ANISOU 1546  CA  LEU A 221      432   2184   4300    273    329    -37       C  
ATOM   1547  C   LEU A 221      92.257  40.972  55.443  1.00 18.50           C  
ANISOU 1547  C   LEU A 221      506   2194   4327    150    367     31       C  
ATOM   1548  O   LEU A 221      92.101  40.566  54.287  1.00 18.84           O  
ANISOU 1548  O   LEU A 221      725   2236   4197    117    289    133       O  
ATOM   1549  CB  LEU A 221      93.217  43.195  54.939  1.00 18.02           C  
ANISOU 1549  CB  LEU A 221      460   2141   4244    323    446    -36       C  
ATOM   1550  CG  LEU A 221      91.902  43.947  55.176  1.00 18.32           C  
ANISOU 1550  CG  LEU A 221      624   2243   4094    463    334   -157       C  
ATOM   1551  CD1 LEU A 221      91.913  44.537  56.580  1.00 18.94           C  
ANISOU 1551  CD1 LEU A 221      862   2362   3971    -28    475   -229       C  
ATOM   1552  CD2 LEU A 221      91.775  45.050  54.146  1.00 20.33           C  
ANISOU 1552  CD2 LEU A 221     1084   2528   4110    426    459    139       C  
ATOM   1553  N   VAL A 222      91.448  40.628  56.441  1.00 17.68           N  
ANISOU 1553  N   VAL A 222      458   2037   4221    103    387     59       N  
ATOM   1554  CA  VAL A 222      90.379  39.655  56.201  1.00 18.30           C  
ANISOU 1554  CA  VAL A 222      434   2212   4304     46    353     89       C  
ATOM   1555  C   VAL A 222      89.030  40.225  56.631  1.00 17.61           C  
ANISOU 1555  C   VAL A 222      303   2271   4117     94    250     82       C  
ATOM   1556  O   VAL A 222      88.859  40.664  57.770  1.00 17.81           O  
ANISOU 1556  O   VAL A 222      297   2422   4046     27    225    170       O  
ATOM   1557  CB  VAL A 222      90.630  38.342  57.004  1.00 18.46           C  
ANISOU 1557  CB  VAL A 222      394   2060   4557     14    408     94       C  
ATOM   1558  CG1 VAL A 222      89.503  37.304  56.770  1.00 20.15           C  
ANISOU 1558  CG1 VAL A 222     1301   1866   4489    -72    534    -46       C  
ATOM   1559  CG2 VAL A 222      92.025  37.799  56.746  1.00 21.59           C  
ANISOU 1559  CG2 VAL A 222     1108   2258   4837     50    337    106       C  
ATOM   1560  N   SER A 223      88.051  40.204  55.736  1.00 17.07           N  
ANISOU 1560  N   SER A 223      311   2281   3892    137    276    196       N  
ATOM   1561  CA  SER A 223      86.707  40.590  56.163  1.00 17.01           C  
ANISOU 1561  CA  SER A 223      373   2284   3803    136    273    143       C  
ATOM   1562  C   SER A 223      85.932  39.381  56.687  1.00 16.93           C  
ANISOU 1562  C   SER A 223      454   2301   3677     41    264    100       C  
ATOM   1563  O   SER A 223      85.641  38.439  55.931  1.00 17.81           O  
ANISOU 1563  O   SER A 223      943   2194   3627    -71    274     68       O  
ATOM   1564  CB  SER A 223      85.905  41.225  55.033  1.00 16.53           C  
ANISOU 1564  CB  SER A 223      331   2284   3662    248    270    218       C  
ATOM   1565  OG  SER A 223      84.545  41.338  55.451  1.00 18.94           O  
ANISOU 1565  OG  SER A 223      462   2432   4300    117    400    226       O  
ATOM   1566  N   LEU A 224      85.588  39.438  57.970  1.00 15.90           N  
ANISOU 1566  N   LEU A 224      311   2215   3512    146    127    -11       N  
ATOM   1567  CA  LEU A 224      84.709  38.463  58.607  1.00 15.91           C  
ANISOU 1567  CA  LEU A 224      312   2253   3479    224     98     22       C  
ATOM   1568  C   LEU A 224      83.273  39.008  58.665  1.00 16.41           C  
ANISOU 1568  C   LEU A 224      361   2280   3591    244    110    114       C  
ATOM   1569  O   LEU A 224      82.468  38.525  59.459  1.00 16.85           O  
ANISOU 1569  O   LEU A 224      298   2371   3730    158    102    152       O  
ATOM   1570  CB  LEU A 224      85.190  38.157  60.031  1.00 15.58           C  
ANISOU 1570  CB  LEU A 224      313   2152   3453    230    -36    112       C  
ATOM   1571  CG  LEU A 224      86.681  37.908  60.301  1.00 16.07           C  
ANISOU 1571  CG  LEU A 224      428   2390   3286    299   -141   -237       C  
ATOM   1572  CD1 LEU A 224      86.921  37.785  61.803  1.00 18.23           C  
ANISOU 1572  CD1 LEU A 224      472   3118   3336    279   -487     37       C  
ATOM   1573  CD2 LEU A 224      87.179  36.661  59.620  1.00 19.29           C  
ANISOU 1573  CD2 LEU A 224      807   2252   4268    270   -127   -394       C  
ATOM   1574  N   SER A 225      82.949  39.995  57.828  1.00 16.01           N  
ANISOU 1574  N   SER A 225      385   2127   3571    328    139    145       N  
ATOM   1575  CA  SER A 225      81.646  40.669  57.850  1.00 16.03           C  
ANISOU 1575  CA  SER A 225      409   2095   3586    221    164    195       C  
ATOM   1576  C   SER A 225      80.462  39.752  57.577  1.00 16.29           C  
ANISOU 1576  C   SER A 225      501   2109   3579    210    154    187       C  
ATOM   1577  O   SER A 225      80.515  38.917  56.686  1.00 17.34           O  
ANISOU 1577  O   SER A 225      721   2219   3647     45     73    218       O  
ATOM   1578  CB  SER A 225      81.621  41.794  56.805  1.00 15.07           C  
ANISOU 1578  CB  SER A 225      374   1943   3407    378    133    171       C  
ATOM   1579  OG  SER A 225      80.437  42.560  56.945  1.00 16.14           O  
ANISOU 1579  OG  SER A 225      488   1998   3645    247    268    264       O  
ATOM   1580  N   CYS A 226      79.406  39.909  58.364  1.00 16.93           N  
ANISOU 1580  N   CYS A 226      580   2229   3623      4    249    173       N  
ATOM   1581  CA  CYS A 226      78.091  39.357  58.036  1.00 18.48           C  
ANISOU 1581  CA  CYS A 226      727   2521   3772     72    240    204       C  
ATOM   1582  C   CYS A 226      77.311  40.163  57.009  1.00 18.45           C  
ANISOU 1582  C   CYS A 226      750   2543   3718     27    192    157       C  
ATOM   1583  O   CYS A 226      76.296  39.664  56.496  1.00 18.53           O  
ANISOU 1583  O   CYS A 226      797   2484   3759    -70     64     91       O  
ATOM   1584  CB  CYS A 226      77.244  39.215  59.308  1.00 19.48           C  
ANISOU 1584  CB  CYS A 226      830   2556   4015      8    456    192       C  
ATOM   1585  SG  CYS A 226      77.455  37.538  59.969  1.00 26.17           S  
ANISOU 1585  SG  CYS A 226     1855   3450   4638    287    528    368       S  
ATOM   1586  N   ASP A 227      77.714  41.407  56.757  1.00 17.40           N  
ANISOU 1586  N   ASP A 227      569   2490   3549     34    220    174       N  
ATOM   1587  CA  ASP A 227      76.897  42.285  55.910  1.00 18.56           C  
ANISOU 1587  CA  ASP A 227      945   2635   3472    -33     72    225       C  
ATOM   1588  C   ASP A 227      77.637  43.448  55.230  1.00 17.74           C  
ANISOU 1588  C   ASP A 227      830   2637   3274      3     39    196       C  
ATOM   1589  O   ASP A 227      77.877  43.379  54.030  1.00 18.79           O  
ANISOU 1589  O   ASP A 227     1110   2755   3274      1    -69    322       O  
ATOM   1590  CB  ASP A 227      75.666  42.755  56.697  1.00 19.01           C  
ANISOU 1590  CB  ASP A 227      885   2764   3571     42     78    208       C  
ATOM   1591  CG  ASP A 227      74.595  43.389  55.828  1.00 23.35           C  
ANISOU 1591  CG  ASP A 227     1635   3279   3957    145     51    361       C  
ATOM   1592  OD1 ASP A 227      74.867  43.689  54.642  1.00 24.58           O  
ANISOU 1592  OD1 ASP A 227     1959   3378   4000    123     51    291       O  
ATOM   1593  OD2 ASP A 227      73.462  43.584  56.341  1.00 29.75           O  
ANISOU 1593  OD2 ASP A 227     2655   4045   4603    547    418    255       O  
ATOM   1594  N   PRO A 228      77.995  44.518  55.965  1.00 17.05           N  
ANISOU 1594  N   PRO A 228      878   2449   3152     -4     54    168       N  
ATOM   1595  CA  PRO A 228      78.593  45.672  55.291  1.00 16.01           C  
ANISOU 1595  CA  PRO A 228      804   2329   2949     -7     51    163       C  
ATOM   1596  C   PRO A 228      79.917  45.368  54.604  1.00 15.71           C  
ANISOU 1596  C   PRO A 228      847   2231   2889     14     66    165       C  
ATOM   1597  O   PRO A 228      80.659  44.467  55.024  1.00 14.83           O  
ANISOU 1597  O   PRO A 228      705   2384   2544    114      3    221       O  
ATOM   1598  CB  PRO A 228      78.852  46.664  56.431  1.00 16.36           C  
ANISOU 1598  CB  PRO A 228      985   2191   3040     22     59    204       C  
ATOM   1599  CG  PRO A 228      78.904  45.850  57.658  1.00 16.58           C  
ANISOU 1599  CG  PRO A 228      787   2424   3086   -224     38    269       C  
ATOM   1600  CD  PRO A 228      77.857  44.757  57.413  1.00 16.65           C  
ANISOU 1600  CD  PRO A 228      804   2487   3033   -130    -30    179       C  
ATOM   1601  N   PHE A 229      80.189  46.112  53.535  1.00 16.42           N  
ANISOU 1601  N   PHE A 229      999   2299   2939     82    112     82       N  
ATOM   1602  CA  PHE A 229      81.547  46.218  53.022  1.00 15.42           C  
ANISOU 1602  CA  PHE A 229      709   2172   2979    123    116     -4       C  
ATOM   1603  C   PHE A 229      82.237  47.371  53.717  1.00 15.98           C  
ANISOU 1603  C   PHE A 229      807   2172   3091    147    136     38       C  
ATOM   1604  O   PHE A 229      81.558  48.287  54.197  1.00 15.05           O  
ANISOU 1604  O   PHE A 229      434   2288   2995    159    291   -172       O  
ATOM   1605  CB  PHE A 229      81.591  46.329  51.489  1.00 15.67           C  
ANISOU 1605  CB  PHE A 229      844   2124   2985    126    128    168       C  
ATOM   1606  CG  PHE A 229      81.156  47.656  50.896  1.00 18.34           C  
ANISOU 1606  CG  PHE A 229     1195   2508   3263    132     46    111       C  
ATOM   1607  CD1 PHE A 229      82.049  48.724  50.804  1.00 18.76           C  
ANISOU 1607  CD1 PHE A 229     1031   2610   3486     32    196    401       C  
ATOM   1608  CD2 PHE A 229      79.907  47.791  50.298  1.00 17.15           C  
ANISOU 1608  CD2 PHE A 229     1198   2446   2869    370    112    121       C  
ATOM   1609  CE1 PHE A 229      81.686  49.923  50.191  1.00 20.82           C  
ANISOU 1609  CE1 PHE A 229     1330   2906   3671    266    254    297       C  
ATOM   1610  CE2 PHE A 229      79.533  48.992  49.671  1.00 19.91           C  
ANISOU 1610  CE2 PHE A 229     1775   2783   3007    295     -1    149       C  
ATOM   1611  CZ  PHE A 229      80.423  50.057  49.614  1.00 20.06           C  
ANISOU 1611  CZ  PHE A 229     1710   3077   2833    173   -105    307       C  
ATOM   1612  N   TYR A 230      83.567  47.301  53.783  1.00 16.01           N  
ANISOU 1612  N   TYR A 230      752   2119   3212      7    166    -11       N  
ATOM   1613  CA  TYR A 230      84.377  48.328  54.401  1.00 16.42           C  
ANISOU 1613  CA  TYR A 230      899   2163   3175   -112     68     58       C  
ATOM   1614  C   TYR A 230      85.278  49.039  53.409  1.00 16.93           C  
ANISOU 1614  C   TYR A 230      916   2217   3297   -105    119     39       C  
ATOM   1615  O   TYR A 230      85.846  48.432  52.498  1.00 17.08           O  
ANISOU 1615  O   TYR A 230      934   2182   3372   -181    166    -66       O  
ATOM   1616  CB  TYR A 230      85.221  47.773  55.552  1.00 16.19           C  
ANISOU 1616  CB  TYR A 230      835   2251   3066   -112    134    132       C  
ATOM   1617  CG  TYR A 230      84.343  47.259  56.654  1.00 15.18           C  
ANISOU 1617  CG  TYR A 230      811   2344   2612   -230    211      7       C  
ATOM   1618  CD1 TYR A 230      83.837  48.120  57.623  1.00 14.25           C  
ANISOU 1618  CD1 TYR A 230     1043   1912   2459   -305    263    142       C  
ATOM   1619  CD2 TYR A 230      83.980  45.917  56.694  1.00 13.57           C  
ANISOU 1619  CD2 TYR A 230      899   2191   2065   -313    434     70       C  
ATOM   1620  CE1 TYR A 230      82.980  47.646  58.616  1.00 14.25           C  
ANISOU 1620  CE1 TYR A 230      600   2594   2219   -428     87     86       C  
ATOM   1621  CE2 TYR A 230      83.135  45.423  57.692  1.00 16.52           C  
ANISOU 1621  CE2 TYR A 230     1079   2798   2400   -295    606     29       C  
ATOM   1622  CZ  TYR A 230      82.643  46.296  58.639  1.00 14.60           C  
ANISOU 1622  CZ  TYR A 230      918   2559   2067   -282    387    212       C  
ATOM   1623  OH  TYR A 230      81.796  45.808  59.605  1.00 14.95           O  
ANISOU 1623  OH  TYR A 230      843   2519   2317   -210    353    466       O  
ATOM   1624  N   THR A 231      85.371  50.352  53.600  1.00 17.69           N  
ANISOU 1624  N   THR A 231     1028   2243   3448   -198     19    110       N  
ATOM   1625  CA  THR A 231      86.376  51.157  52.922  1.00 17.23           C  
ANISOU 1625  CA  THR A 231      775   2290   3481   -124     48    145       C  
ATOM   1626  C   THR A 231      87.531  51.262  53.914  1.00 17.31           C  
ANISOU 1626  C   THR A 231      740   2279   3559    -59     -1    155       C  
ATOM   1627  O   THR A 231      87.383  51.868  54.978  1.00 17.31           O  
ANISOU 1627  O   THR A 231      692   2425   3458    110    -87    280       O  
ATOM   1628  CB  THR A 231      85.806  52.539  52.536  1.00 17.62           C  
ANISOU 1628  CB  THR A 231      779   2333   3583   -180     61    149       C  
ATOM   1629  OG1 THR A 231      84.682  52.346  51.668  1.00 19.02           O  
ANISOU 1629  OG1 THR A 231     1129   2588   3509     29   -141    -13       O  
ATOM   1630  CG2 THR A 231      86.852  53.417  51.826  1.00 19.01           C  
ANISOU 1630  CG2 THR A 231     1283   2240   3697   -180    233    255       C  
ATOM   1631  N   PHE A 232      88.650  50.629  53.568  1.00 17.07           N  
ANISOU 1631  N   PHE A 232      554   2294   3634    -57     22    156       N  
ATOM   1632  CA  PHE A 232      89.803  50.474  54.459  1.00 16.78           C  
ANISOU 1632  CA  PHE A 232      508   2302   3564   -156     12     57       C  
ATOM   1633  C   PHE A 232      90.955  51.357  53.989  1.00 17.36           C  
ANISOU 1633  C   PHE A 232      628   2336   3630   -191     20     81       C  
ATOM   1634  O   PHE A 232      91.273  51.394  52.791  1.00 17.66           O  
ANISOU 1634  O   PHE A 232      804   2398   3508   -123    -88    282       O  
ATOM   1635  CB  PHE A 232      90.255  49.000  54.483  1.00 16.31           C  
ANISOU 1635  CB  PHE A 232      384   2239   3573   -179     19    109       C  
ATOM   1636  CG  PHE A 232      91.379  48.713  55.438  1.00 17.79           C  
ANISOU 1636  CG  PHE A 232      586   2265   3905    101    131    -15       C  
ATOM   1637  CD1 PHE A 232      91.114  48.432  56.774  1.00 18.68           C  
ANISOU 1637  CD1 PHE A 232      965   2185   3944    207    -73   -207       C  
ATOM   1638  CD2 PHE A 232      92.707  48.760  55.010  1.00 18.23           C  
ANISOU 1638  CD2 PHE A 232      477   2177   4273    343     64   -298       C  
ATOM   1639  CE1 PHE A 232      92.158  48.192  57.665  1.00 18.18           C  
ANISOU 1639  CE1 PHE A 232      772   2003   4129    400    -31   -508       C  
ATOM   1640  CE2 PHE A 232      93.762  48.511  55.895  1.00 18.39           C  
ANISOU 1640  CE2 PHE A 232      545   2289   4152    408    228   -289       C  
ATOM   1641  CZ  PHE A 232      93.492  48.227  57.225  1.00 18.84           C  
ANISOU 1641  CZ  PHE A 232      981   2074   4101    240    219   -472       C  
ATOM   1642  N   SER A 233      91.628  52.008  54.937  1.00 17.34           N  
ANISOU 1642  N   SER A 233      533   2314   3739   -231     60     25       N  
ATOM   1643  CA  SER A 233      92.825  52.792  54.619  1.00 17.84           C  
ANISOU 1643  CA  SER A 233      467   2339   3970   -271    -71    -32       C  
ATOM   1644  C   SER A 233      93.614  53.032  55.884  1.00 18.14           C  
ANISOU 1644  C   SER A 233      458   2312   4120   -222    -78    -17       C  
ATOM   1645  O   SER A 233      93.087  52.892  56.987  1.00 18.33           O  
ANISOU 1645  O   SER A 233      359   2464   4141   -363   -203     30       O  
ATOM   1646  CB  SER A 233      92.449  54.154  54.027  1.00 18.84           C  
ANISOU 1646  CB  SER A 233      749   2311   4098   -267     67   -117       C  
ATOM   1647  OG  SER A 233      91.742  54.934  54.982  1.00 21.09           O  
ANISOU 1647  OG  SER A 233     1023   2919   4069   -127     86    -64       O  
ATOM   1648  N   ILE A 234      94.870  53.431  55.702  1.00 18.08           N  
ANISOU 1648  N   ILE A 234      313   2247   4309   -175   -200    -82       N  
ATOM   1649  CA  ILE A 234      95.736  53.758  56.825  1.00 19.03           C  
ANISOU 1649  CA  ILE A 234      498   2274   4456   -123   -142    -35       C  
ATOM   1650  C   ILE A 234      96.309  55.152  56.576  1.00 19.77           C  
ANISOU 1650  C   ILE A 234      561   2377   4572   -170    -31    -58       C  
ATOM   1651  O   ILE A 234      97.015  55.367  55.585  1.00 20.25           O  
ANISOU 1651  O   ILE A 234      672   2409   4613   -236    105    -37       O  
ATOM   1652  CB  ILE A 234      96.840  52.695  56.953  1.00 19.37           C  
ANISOU 1652  CB  ILE A 234      588   2250   4520   -168   -273     -3       C  
ATOM   1653  CG1 ILE A 234      96.198  51.310  57.187  1.00 19.33           C  
ANISOU 1653  CG1 ILE A 234      577   2013   4754    118   -118     90       C  
ATOM   1654  CG2 ILE A 234      97.836  53.091  58.044  1.00 20.04           C  
ANISOU 1654  CG2 ILE A 234      580   2383   4650    -83   -544     26       C  
ATOM   1655  CD1 ILE A 234      97.234  50.147  57.179  1.00 19.77           C  
ANISOU 1655  CD1 ILE A 234      743   1883   4883    372   -206    201       C  
ATOM   1656  N   ASP A 235      95.991  56.103  57.450  1.00 20.14           N  
ANISOU 1656  N   ASP A 235      615   2396   4641   -159     71    -86       N  
ATOM   1657  CA  ASP A 235      96.499  57.472  57.289  1.00 20.80           C  
ANISOU 1657  CA  ASP A 235      553   2520   4829   -185    256   -129       C  
ATOM   1658  C   ASP A 235      98.022  57.467  57.080  1.00 21.27           C  
ANISOU 1658  C   ASP A 235      527   2653   4901   -186    170   -112       C  
ATOM   1659  O   ASP A 235      98.768  56.758  57.776  1.00 21.06           O  
ANISOU 1659  O   ASP A 235      577   2473   4949   -147    194   -170       O  
ATOM   1660  CB  ASP A 235      96.165  58.334  58.510  1.00 20.93           C  
ANISOU 1660  CB  ASP A 235      664   2516   4770   -100    252    -80       C  
ATOM   1661  CG  ASP A 235      94.702  58.741  58.572  1.00 21.61           C  
ANISOU 1661  CG  ASP A 235      707   2605   4897    -50    275    -41       C  
ATOM   1662  OD1 ASP A 235      93.860  58.200  57.818  1.00 22.56           O  
ANISOU 1662  OD1 ASP A 235      663   3197   4709    426    185    128       O  
ATOM   1663  OD2 ASP A 235      94.386  59.613  59.412  1.00 23.17           O  
ANISOU 1663  OD2 ASP A 235      669   2833   5298    -24    292   -236       O  
ATOM   1664  N   GLY A 236      98.469  58.213  56.077  1.00 20.54           N  
ANISOU 1664  N   GLY A 236      330   2611   4863   -200    325    -80       N  
ATOM   1665  CA  GLY A 236      99.910  58.461  55.908  1.00 22.34           C  
ANISOU 1665  CA  GLY A 236      679   2909   4897   -159    412    -91       C  
ATOM   1666  C   GLY A 236     100.681  57.337  55.245  1.00 21.97           C  
ANISOU 1666  C   GLY A 236      678   2877   4791    -84    444     -6       C  
ATOM   1667  O   GLY A 236     101.902  57.435  55.084  1.00 22.51           O  
ANISOU 1667  O   GLY A 236      883   2885   4782   -175    641     23       O  
ATOM   1668  N   HIS A 237      99.985  56.259  54.897  1.00 22.54           N  
ANISOU 1668  N   HIS A 237      875   2906   4781   -125    528     51       N  
ATOM   1669  CA  HIS A 237     100.644  55.077  54.339  1.00 23.62           C  
ANISOU 1669  CA  HIS A 237     1152   3071   4752   -205    471     78       C  
ATOM   1670  C   HIS A 237      99.862  54.525  53.154  1.00 23.97           C  
ANISOU 1670  C   HIS A 237     1245   3144   4717   -212    499    131       C  
ATOM   1671  O   HIS A 237      98.631  54.402  53.194  1.00 24.85           O  
ANISOU 1671  O   HIS A 237     1349   3328   4762   -184    617    163       O  
ATOM   1672  CB  HIS A 237     100.760  53.973  55.386  1.00 22.65           C  
ANISOU 1672  CB  HIS A 237      966   2921   4720   -252    339     86       C  
ATOM   1673  CG  HIS A 237     101.618  54.330  56.560  1.00 23.18           C  
ANISOU 1673  CG  HIS A 237     1025   3124   4656   -172    386     71       C  
ATOM   1674  ND1 HIS A 237     101.190  55.162  57.575  1.00 22.12           N  
ANISOU 1674  ND1 HIS A 237      621   3235   4546    -88    459    238       N  
ATOM   1675  CD2 HIS A 237     102.885  53.968  56.875  1.00 22.15           C  
ANISOU 1675  CD2 HIS A 237      629   3131   4655   -464    364     54       C  
ATOM   1676  CE1 HIS A 237     102.161  55.303  58.461  1.00 22.39           C  
ANISOU 1676  CE1 HIS A 237      694   3294   4516   -401    532    260       C  
ATOM   1677  NE2 HIS A 237     103.190  54.568  58.072  1.00 21.69           N  
ANISOU 1677  NE2 HIS A 237      506   3107   4628   -489    345    281       N  
ATOM   1678  N   ASN A 238     100.582  54.178  52.098  1.00 23.58           N  
ANISOU 1678  N   ASN A 238     1286   3040   4633   -182    639    156       N  
ATOM   1679  CA  ASN A 238      99.976  53.424  51.013  1.00 24.46           C  
ANISOU 1679  CA  ASN A 238     1479   3100   4714   -149    598    149       C  
ATOM   1680  C   ASN A 238     100.050  51.923  51.277  1.00 23.76           C  
ANISOU 1680  C   ASN A 238     1356   3078   4592   -126    731    157       C  
ATOM   1681  O   ASN A 238     100.795  51.457  52.145  1.00 24.17           O  
ANISOU 1681  O   ASN A 238     1220   3147   4815     -7    675    130       O  
ATOM   1682  CB  ASN A 238     100.671  53.737  49.698  1.00 25.50           C  
ANISOU 1682  CB  ASN A 238     1938   3103   4646   -258    502    155       C  
ATOM   1683  CG  ASN A 238     100.405  55.147  49.220  1.00 30.64           C  
ANISOU 1683  CG  ASN A 238     2885   3499   5256   -178    177    306       C  
ATOM   1684  OD1 ASN A 238      99.318  55.705  49.429  1.00 29.41           O  
ANISOU 1684  OD1 ASN A 238     2810   3355   5008   -150     73    431       O  
ATOM   1685  ND2 ASN A 238     101.411  55.736  48.575  1.00 35.98           N  
ANISOU 1685  ND2 ASN A 238     3706   4164   5801   -747     62    530       N  
ATOM   1686  N   MET A 239      99.292  51.166  50.498  1.00 22.75           N  
ANISOU 1686  N   MET A 239     1103   2975   4564   -120    790     97       N  
ATOM   1687  CA  MET A 239      99.199  49.719  50.670  1.00 22.47           C  
ANISOU 1687  CA  MET A 239     1145   2875   4518     41    851    113       C  
ATOM   1688  C   MET A 239      99.476  49.072  49.321  1.00 23.09           C  
ANISOU 1688  C   MET A 239     1158   2862   4752     17    826     40       C  
ATOM   1689  O   MET A 239      98.789  49.366  48.332  1.00 22.57           O  
ANISOU 1689  O   MET A 239     1205   2753   4615    116    789     34       O  
ATOM   1690  CB  MET A 239      97.781  49.341  51.120  1.00 22.47           C  
ANISOU 1690  CB  MET A 239     1036   2961   4539     61    788    123       C  
ATOM   1691  CG  MET A 239      97.313  50.052  52.384  1.00 21.39           C  
ANISOU 1691  CG  MET A 239     1049   2812   4265    380    827    275       C  
ATOM   1692  SD  MET A 239      95.619  49.612  52.882  1.00 22.29           S  
ANISOU 1692  SD  MET A 239     1170   3334   3964    304    643    737       S  
ATOM   1693  CE  MET A 239      94.628  50.480  51.661  1.00 19.60           C  
ANISOU 1693  CE  MET A 239      733   3042   3669    -98    575    671       C  
ATOM   1694  N   THR A 240     100.479  48.201  49.280  1.00 22.91           N  
ANISOU 1694  N   THR A 240     1084   2722   4897      5    843     12       N  
ATOM   1695  CA  THR A 240     100.801  47.513  48.041  1.00 23.63           C  
ANISOU 1695  CA  THR A 240     1118   2854   5004    -29    901     -4       C  
ATOM   1696  C   THR A 240     100.191  46.118  48.056  1.00 23.31           C  
ANISOU 1696  C   THR A 240      949   2865   5039    -38    829    -52       C  
ATOM   1697  O   THR A 240     100.682  45.206  48.736  1.00 22.79           O  
ANISOU 1697  O   THR A 240      810   2838   5011    -23    841   -108       O  
ATOM   1698  CB  THR A 240     102.323  47.440  47.829  1.00 23.90           C  
ANISOU 1698  CB  THR A 240     1126   2875   5078    -95    893    -16       C  
ATOM   1699  OG1 THR A 240     102.835  48.777  47.728  1.00 25.29           O  
ANISOU 1699  OG1 THR A 240     1454   2953   5200   -255    901    -86       O  
ATOM   1700  CG2 THR A 240     102.641  46.676  46.546  1.00 24.96           C  
ANISOU 1700  CG2 THR A 240     1614   2791   5076    -34    969    -89       C  
ATOM   1701  N   ILE A 241      99.098  45.973  47.313  1.00 23.66           N  
ANISOU 1701  N   ILE A 241     1060   2910   5018     64    800    -18       N  
ATOM   1702  CA  ILE A 241      98.348  44.719  47.288  1.00 22.89           C  
ANISOU 1702  CA  ILE A 241      934   2790   4971    124    830    -13       C  
ATOM   1703  C   ILE A 241      99.167  43.669  46.551  1.00 23.00           C  
ANISOU 1703  C   ILE A 241      868   2835   5035    176    845     66       C  
ATOM   1704  O   ILE A 241      99.657  43.941  45.450  1.00 22.84           O  
ANISOU 1704  O   ILE A 241      884   2835   4957     96    990      6       O  
ATOM   1705  CB  ILE A 241      96.979  44.899  46.596  1.00 23.04           C  
ANISOU 1705  CB  ILE A 241      976   2824   4953    144    827     -3       C  
ATOM   1706  CG1 ILE A 241      96.077  45.816  47.447  1.00 22.62           C  
ANISOU 1706  CG1 ILE A 241      594   2863   5137    379    668    -68       C  
ATOM   1707  CG2 ILE A 241      96.302  43.554  46.372  1.00 23.43           C  
ANISOU 1707  CG2 ILE A 241     1283   2866   4750     84    711    -53       C  
ATOM   1708  CD1 ILE A 241      94.765  46.086  46.818  1.00 26.22           C  
ANISOU 1708  CD1 ILE A 241     1636   3286   5039    440    453    361       C  
ATOM   1709  N   ILE A 242      99.306  42.493  47.163  1.00 22.41           N  
ANISOU 1709  N   ILE A 242      770   2691   5055    143    821     75       N  
ATOM   1710  CA  ILE A 242     100.075  41.377  46.594  1.00 22.90           C  
ANISOU 1710  CA  ILE A 242      861   2744   5095    198    737    141       C  
ATOM   1711  C   ILE A 242      99.285  40.064  46.558  1.00 22.54           C  
ANISOU 1711  C   ILE A 242      831   2732   4998    160    780    112       C  
ATOM   1712  O   ILE A 242      99.747  39.070  45.988  1.00 23.06           O  
ANISOU 1712  O   ILE A 242      919   2823   5018    200    895    240       O  
ATOM   1713  CB  ILE A 242     101.400  41.136  47.357  1.00 22.74           C  
ANISOU 1713  CB  ILE A 242      776   2659   5205    125    694    119       C  
ATOM   1714  CG1 ILE A 242     101.122  40.814  48.834  1.00 22.69           C  
ANISOU 1714  CG1 ILE A 242      837   2597   5187    426    437     59       C  
ATOM   1715  CG2 ILE A 242     102.366  42.308  47.142  1.00 24.30           C  
ANISOU 1715  CG2 ILE A 242     1034   2864   5332      8    657    144       C  
ATOM   1716  CD1 ILE A 242     102.303  40.110  49.554  1.00 24.58           C  
ANISOU 1716  CD1 ILE A 242      853   2626   5858    649    381    -42       C  
ATOM   1717  N   GLU A 243      98.101  40.045  47.164  1.00 22.10           N  
ANISOU 1717  N   GLU A 243      756   2793   4847    224    763    110       N  
ATOM   1718  CA  GLU A 243      97.257  38.844  47.197  1.00 21.91           C  
ANISOU 1718  CA  GLU A 243      831   2722   4772    183    720     98       C  
ATOM   1719  C   GLU A 243      95.799  39.280  47.277  1.00 22.17           C  
ANISOU 1719  C   GLU A 243      946   2753   4724    183    684     36       C  
ATOM   1720  O   GLU A 243      95.487  40.218  48.006  1.00 21.48           O  
ANISOU 1720  O   GLU A 243      833   2639   4689    174    606   -101       O  
ATOM   1721  CB  GLU A 243      97.596  37.979  48.425  1.00 22.27           C  
ANISOU 1721  CB  GLU A 243      833   2887   4740    206    663    139       C  
ATOM   1722  CG  GLU A 243      96.742  36.721  48.640  1.00 22.58           C  
ANISOU 1722  CG  GLU A 243      978   3010   4590     74    689    413       C  
ATOM   1723  CD  GLU A 243      96.471  36.376  50.108  1.00 24.26           C  
ANISOU 1723  CD  GLU A 243      952   3462   4802      1    567    528       C  
ATOM   1724  OE1 GLU A 243      97.281  36.721  50.987  1.00 23.92           O  
ANISOU 1724  OE1 GLU A 243     1027   3406   4652     26    513    722       O  
ATOM   1725  OE2 GLU A 243      95.435  35.738  50.415  1.00 24.71           O  
ANISOU 1725  OE2 GLU A 243     1112   3524   4750    220    872    661       O  
ATOM   1726  N   ALA A 244      94.918  38.624  46.522  1.00 21.94           N  
ANISOU 1726  N   ALA A 244     1015   2651   4668     99    722    -18       N  
ATOM   1727  CA  ALA A 244      93.485  38.786  46.687  1.00 22.27           C  
ANISOU 1727  CA  ALA A 244     1183   2638   4637    281    673     -2       C  
ATOM   1728  C   ALA A 244      92.843  37.405  46.848  1.00 22.31           C  
ANISOU 1728  C   ALA A 244     1182   2662   4631    308    719    -68       C  
ATOM   1729  O   ALA A 244      93.070  36.523  46.014  1.00 22.51           O  
ANISOU 1729  O   ALA A 244     1256   2732   4563    440    729   -124       O  
ATOM   1730  CB  ALA A 244      92.899  39.503  45.470  1.00 23.04           C  
ANISOU 1730  CB  ALA A 244     1491   2636   4625    185    589    -30       C  
ATOM   1731  N   ASP A 245      92.028  37.216  47.888  1.00 22.14           N  
ANISOU 1731  N   ASP A 245     1303   2634   4474    291    779    -40       N  
ATOM   1732  CA  ASP A 245      91.350  35.937  48.128  1.00 22.06           C  
ANISOU 1732  CA  ASP A 245     1165   2655   4562    365    789    -10       C  
ATOM   1733  C   ASP A 245      92.309  34.753  47.915  1.00 23.30           C  
ANISOU 1733  C   ASP A 245     1391   2779   4683    359    786    -17       C  
ATOM   1734  O   ASP A 245      91.989  33.815  47.191  1.00 23.07           O  
ANISOU 1734  O   ASP A 245     1495   2529   4739    360    735     39       O  
ATOM   1735  CB  ASP A 245      90.111  35.781  47.231  1.00 21.46           C  
ANISOU 1735  CB  ASP A 245     1045   2578   4531    356    838    -29       C  
ATOM   1736  CG  ASP A 245      89.053  36.864  47.464  1.00 21.32           C  
ANISOU 1736  CG  ASP A 245      895   2698   4507    297    679      0       C  
ATOM   1737  OD1 ASP A 245      89.254  37.784  48.294  1.00 19.96           O  
ANISOU 1737  OD1 ASP A 245      615   2573   4394     89    540    111       O  
ATOM   1738  OD2 ASP A 245      87.991  36.796  46.803  1.00 20.15           O  
ANISOU 1738  OD2 ASP A 245      585   2786   4284    466    628   -437       O  
ATOM   1739  N   ALA A 246      93.498  34.814  48.515  1.00 23.80           N  
ANISOU 1739  N   ALA A 246     1378   2909   4756    351    911     50       N  
ATOM   1740  CA  ALA A 246      94.444  33.701  48.493  1.00 24.70           C  
ANISOU 1740  CA  ALA A 246     1501   3020   4863    344    932     45       C  
ATOM   1741  C   ALA A 246      95.068  33.398  47.140  1.00 25.24           C  
ANISOU 1741  C   ALA A 246     1565   3139   4883    346   1011     50       C  
ATOM   1742  O   ALA A 246      95.638  32.317  46.955  1.00 26.67           O  
ANISOU 1742  O   ALA A 246     1772   3369   4991    490   1043     51       O  
ATOM   1743  CB  ALA A 246      93.821  32.435  49.098  1.00 24.66           C  
ANISOU 1743  CB  ALA A 246     1584   2916   4867    284    911     41       C  
ATOM   1744  N   VAL A 247      94.971  34.320  46.189  1.00 25.73           N  
ANISOU 1744  N   VAL A 247     1563   3237   4975    318   1051     31       N  
ATOM   1745  CA  VAL A 247      95.690  34.139  44.919  1.00 26.05           C  
ANISOU 1745  CA  VAL A 247     1593   3341   4962    259   1132     81       C  
ATOM   1746  C   VAL A 247      96.645  35.311  44.744  1.00 26.05           C  
ANISOU 1746  C   VAL A 247     1583   3295   5019    331   1126     44       C  
ATOM   1747  O   VAL A 247      96.238  36.466  44.858  1.00 25.26           O  
ANISOU 1747  O   VAL A 247     1473   3199   4923    412   1276    -29       O  
ATOM   1748  CB  VAL A 247      94.740  34.017  43.690  1.00 26.72           C  
ANISOU 1748  CB  VAL A 247     1721   3445   4984    177   1085     97       C  
ATOM   1749  CG1 VAL A 247      95.530  33.849  42.392  1.00 27.17           C  
ANISOU 1749  CG1 VAL A 247     1934   3435   4953    309   1146     69       C  
ATOM   1750  CG2 VAL A 247      93.772  32.846  43.856  1.00 28.56           C  
ANISOU 1750  CG2 VAL A 247     2063   3632   5157     97   1082    192       C  
ATOM   1751  N   ASN A 248      97.911  35.003  44.466  1.00 25.53           N  
ANISOU 1751  N   ASN A 248     1479   3247   4973    321   1217     49       N  
ATOM   1752  CA  ASN A 248      98.947  36.019  44.380  1.00 25.89           C  
ANISOU 1752  CA  ASN A 248     1575   3176   5085    281   1090     46       C  
ATOM   1753  C   ASN A 248      98.674  36.959  43.220  1.00 26.36           C  
ANISOU 1753  C   ASN A 248     1678   3205   5131    237   1128     50       C  
ATOM   1754  O   ASN A 248      98.326  36.512  42.123  1.00 27.02           O  
ANISOU 1754  O   ASN A 248     1952   3191   5123    165   1117     71       O  
ATOM   1755  CB  ASN A 248     100.312  35.355  44.182  1.00 26.47           C  
ANISOU 1755  CB  ASN A 248     1676   3243   5135    330   1057      0       C  
ATOM   1756  CG  ASN A 248     100.770  34.594  45.416  1.00 25.93           C  
ANISOU 1756  CG  ASN A 248     1626   3077   5148    370    936    -55       C  
ATOM   1757  OD1 ASN A 248     100.401  34.938  46.538  1.00 25.31           O  
ANISOU 1757  OD1 ASN A 248     1416   3172   5029    368   1007    -77       O  
ATOM   1758  ND2 ASN A 248     101.576  33.561  45.212  1.00 25.51           N  
ANISOU 1758  ND2 ASN A 248     1289   3092   5309    522    623   -189       N  
ATOM   1759  N   THR A 249      98.815  38.256  43.466  1.00 25.78           N  
ANISOU 1759  N   THR A 249     1522   3145   5126    236   1162     41       N  
ATOM   1760  CA  THR A 249      98.682  39.227  42.381  1.00 25.84           C  
ANISOU 1760  CA  THR A 249     1521   3171   5126    283   1255    -11       C  
ATOM   1761  C   THR A 249     100.026  39.895  42.088  1.00 26.36           C  
ANISOU 1761  C   THR A 249     1670   3351   4993    255   1323     -9       C  
ATOM   1762  O   THR A 249     100.968  39.820  42.896  1.00 25.24           O  
ANISOU 1762  O   THR A 249     1498   3217   4873    273   1367      6       O  
ATOM   1763  CB  THR A 249      97.638  40.319  42.727  1.00 25.38           C  
ANISOU 1763  CB  THR A 249     1392   3135   5113    261   1401    -26       C  
ATOM   1764  OG1 THR A 249      98.180  41.160  43.753  1.00 26.08           O  
ANISOU 1764  OG1 THR A 249     1378   3088   5441    410   1347    -58       O  
ATOM   1765  CG2 THR A 249      96.301  39.712  43.211  1.00 23.57           C  
ANISOU 1765  CG2 THR A 249     1031   2840   5082    473   1364   -162       C  
ATOM   1766  N   LYS A 250     100.112  40.544  40.927  1.00 27.04           N  
ANISOU 1766  N   LYS A 250     1864   3491   4916    218   1243    -50       N  
ATOM   1767  CA  LYS A 250     101.173  41.519  40.672  1.00 27.91           C  
ANISOU 1767  CA  LYS A 250     2029   3740   4835    214   1218   -127       C  
ATOM   1768  C   LYS A 250     101.022  42.649  41.685  1.00 26.89           C  
ANISOU 1768  C   LYS A 250     1828   3599   4787    271   1241   -161       C  
ATOM   1769  O   LYS A 250      99.897  43.035  42.006  1.00 26.90           O  
ANISOU 1769  O   LYS A 250     1811   3563   4845    298   1148   -216       O  
ATOM   1770  CB  LYS A 250     101.079  42.074  39.250  1.00 27.86           C  
ANISOU 1770  CB  LYS A 250     2054   3796   4732    210   1279   -102       C  
ATOM   1771  CG  LYS A 250     101.526  41.030  38.234  1.00 32.03           C  
ANISOU 1771  CG  LYS A 250     3171   4264   4732    187   1057   -271       C  
ATOM   1772  CD  LYS A 250     101.283  41.492  36.817  1.00 37.68           C  
ANISOU 1772  CD  LYS A 250     4371   5175   4768    274    715   -375       C  
ATOM   1773  CE  LYS A 250     101.694  40.401  35.841  1.00 40.44           C  
ANISOU 1773  CE  LYS A 250     5092   5475   4796    200    572   -510       C  
ATOM   1774  NZ  LYS A 250     101.188  40.761  34.486  1.00 43.44           N  
ANISOU 1774  NZ  LYS A 250     5414   6030   5062    155    102   -596       N  
ATOM   1775  N   PRO A 251     102.144  43.165  42.211  1.00 26.75           N  
ANISOU 1775  N   PRO A 251     1759   3635   4769    317   1226   -141       N  
ATOM   1776  CA  PRO A 251     102.011  44.211  43.229  1.00 27.25           C  
ANISOU 1776  CA  PRO A 251     1822   3696   4836    280   1197    -78       C  
ATOM   1777  C   PRO A 251     101.271  45.415  42.654  1.00 27.46           C  
ANISOU 1777  C   PRO A 251     1870   3753   4808    240   1247    -13       C  
ATOM   1778  O   PRO A 251     101.537  45.812  41.516  1.00 28.43           O  
ANISOU 1778  O   PRO A 251     2092   3830   4880    214   1302     91       O  
ATOM   1779  CB  PRO A 251     103.467  44.574  43.566  1.00 27.01           C  
ANISOU 1779  CB  PRO A 251     1702   3780   4781    313   1227   -145       C  
ATOM   1780  CG  PRO A 251     104.265  43.375  43.134  1.00 28.02           C  
ANISOU 1780  CG  PRO A 251     1850   3778   5017    429   1009   -130       C  
ATOM   1781  CD  PRO A 251     103.555  42.823  41.931  1.00 26.80           C  
ANISOU 1781  CD  PRO A 251     1707   3610   4863    325   1155   -157       C  
ATOM   1782  N   HIS A 252     100.327  45.963  43.412  1.00 26.86           N  
ANISOU 1782  N   HIS A 252     1823   3664   4717    185   1296     45       N  
ATOM   1783  CA  HIS A 252      99.581  47.139  42.975  1.00 26.75           C  
ANISOU 1783  CA  HIS A 252     1806   3709   4648    177   1245    106       C  
ATOM   1784  C   HIS A 252      99.298  48.057  44.160  1.00 26.30           C  
ANISOU 1784  C   HIS A 252     1766   3566   4657    186   1205    126       C  
ATOM   1785  O   HIS A 252      98.626  47.667  45.113  1.00 25.87           O  
ANISOU 1785  O   HIS A 252     1836   3536   4457    207   1379    161       O  
ATOM   1786  CB  HIS A 252      98.277  46.741  42.277  1.00 27.34           C  
ANISOU 1786  CB  HIS A 252     1833   3848   4704    108   1231    105       C  
ATOM   1787  CG  HIS A 252      97.426  47.909  41.889  1.00 27.38           C  
ANISOU 1787  CG  HIS A 252     1864   3925   4611    105   1272    243       C  
ATOM   1788  ND1 HIS A 252      97.803  48.821  40.926  1.00 30.12           N  
ANISOU 1788  ND1 HIS A 252     2175   4566   4701    141   1266    269       N  
ATOM   1789  CD2 HIS A 252      96.212  48.313  42.332  1.00 27.62           C  
ANISOU 1789  CD2 HIS A 252     2029   4051   4412    100   1244    149       C  
ATOM   1790  CE1 HIS A 252      96.865  49.742  40.801  1.00 29.11           C  
ANISOU 1790  CE1 HIS A 252     2200   4281   4576    156   1359    222       C  
ATOM   1791  NE2 HIS A 252      95.887  49.456  41.644  1.00 28.85           N  
ANISOU 1791  NE2 HIS A 252     2195   4233   4531    -13   1332    288       N  
ATOM   1792  N   THR A 253      99.821  49.278  44.095  1.00 25.93           N  
ANISOU 1792  N   THR A 253     1772   3456   4621    234   1122    135       N  
ATOM   1793  CA  THR A 253      99.795  50.169  45.244  1.00 25.10           C  
ANISOU 1793  CA  THR A 253     1572   3352   4611    274    998    123       C  
ATOM   1794  C   THR A 253      98.567  51.072  45.201  1.00 24.81           C  
ANISOU 1794  C   THR A 253     1614   3251   4560    302    892    129       C  
ATOM   1795  O   THR A 253      98.260  51.664  44.166  1.00 25.29           O  
ANISOU 1795  O   THR A 253     1771   3311   4526    390    865    209       O  
ATOM   1796  CB  THR A 253     101.095  50.985  45.300  1.00 25.30           C  
ANISOU 1796  CB  THR A 253     1587   3399   4626    297    959     93       C  
ATOM   1797  OG1 THR A 253     102.186  50.057  45.382  1.00 24.80           O  
ANISOU 1797  OG1 THR A 253     1254   3556   4611    233   1143     28       O  
ATOM   1798  CG2 THR A 253     101.101  51.917  46.511  1.00 26.83           C  
ANISOU 1798  CG2 THR A 253     1831   3553   4809    241    851     63       C  
ATOM   1799  N   VAL A 254      97.871  51.169  46.329  1.00 23.67           N  
ANISOU 1799  N   VAL A 254     1403   3108   4482    266    839    131       N  
ATOM   1800  CA  VAL A 254      96.675  52.005  46.434  1.00 23.38           C  
ANISOU 1800  CA  VAL A 254     1421   3007   4454    212    700     28       C  
ATOM   1801  C   VAL A 254      96.700  52.709  47.787  1.00 23.14           C  
ANISOU 1801  C   VAL A 254     1361   2910   4519    182    635     71       C  
ATOM   1802  O   VAL A 254      97.480  52.347  48.669  1.00 23.53           O  
ANISOU 1802  O   VAL A 254     1469   3002   4467    215    484     56       O  
ATOM   1803  CB  VAL A 254      95.373  51.157  46.356  1.00 23.52           C  
ANISOU 1803  CB  VAL A 254     1469   2980   4484    188    696      9       C  
ATOM   1804  CG1 VAL A 254      95.285  50.412  45.029  1.00 24.71           C  
ANISOU 1804  CG1 VAL A 254     1849   3124   4412    169    600    -76       C  
ATOM   1805  CG2 VAL A 254      95.267  50.177  47.530  1.00 22.57           C  
ANISOU 1805  CG2 VAL A 254     1362   3035   4178    184    638     -2       C  
ATOM   1806  N   ASP A 255      95.819  53.682  47.983  1.00 21.79           N  
ANISOU 1806  N   ASP A 255     1173   2686   4417    153    630    110       N  
ATOM   1807  CA  ASP A 255      95.767  54.345  49.274  1.00 21.14           C  
ANISOU 1807  CA  ASP A 255     1124   2625   4280     85    629    155       C  
ATOM   1808  C   ASP A 255      94.449  54.095  50.011  1.00 21.08           C  
ANISOU 1808  C   ASP A 255     1157   2599   4252     37    616    148       C  
ATOM   1809  O   ASP A 255      94.244  54.574  51.129  1.00 21.24           O  
ANISOU 1809  O   ASP A 255     1138   2709   4223     55    703     56       O  
ATOM   1810  CB  ASP A 255      96.112  55.836  49.147  1.00 21.74           C  
ANISOU 1810  CB  ASP A 255     1290   2583   4385     75    671    163       C  
ATOM   1811  CG  ASP A 255      95.080  56.642  48.365  1.00 22.82           C  
ANISOU 1811  CG  ASP A 255     1714   2564   4393     -9    603    242       C  
ATOM   1812  OD1 ASP A 255      94.132  56.075  47.781  1.00 20.89           O  
ANISOU 1812  OD1 ASP A 255     1765   2473   3699    -47    895    151       O  
ATOM   1813  OD2 ASP A 255      95.235  57.891  48.336  1.00 27.19           O  
ANISOU 1813  OD2 ASP A 255     2754   2688   4888   -216    821    209       O  
ATOM   1814  N   SER A 256      93.578  53.305  49.395  1.00 20.14           N  
ANISOU 1814  N   SER A 256     1017   2470   4165      7    499    189       N  
ATOM   1815  CA  SER A 256      92.365  52.833  50.070  1.00 20.39           C  
ANISOU 1815  CA  SER A 256     1046   2436   4264     70    488    166       C  
ATOM   1816  C   SER A 256      91.756  51.701  49.244  1.00 20.24           C  
ANISOU 1816  C   SER A 256      990   2429   4270    -15    544    211       C  
ATOM   1817  O   SER A 256      92.103  51.528  48.072  1.00 20.01           O  
ANISOU 1817  O   SER A 256      984   2412   4206   -136    557    199       O  
ATOM   1818  CB  SER A 256      91.370  53.978  50.242  1.00 21.47           C  
ANISOU 1818  CB  SER A 256     1399   2435   4324     48    421    142       C  
ATOM   1819  OG  SER A 256      90.693  54.221  49.021  1.00 24.07           O  
ANISOU 1819  OG  SER A 256     1949   2544   4652    439    151     62       O  
ATOM   1820  N   LEU A 257      90.867  50.917  49.852  1.00 19.20           N  
ANISOU 1820  N   LEU A 257      716   2387   4193     44    568    203       N  
ATOM   1821  CA  LEU A 257      90.240  49.800  49.149  1.00 19.28           C  
ANISOU 1821  CA  LEU A 257      741   2385   4198    105    511    251       C  
ATOM   1822  C   LEU A 257      88.855  49.537  49.742  1.00 19.40           C  
ANISOU 1822  C   LEU A 257      779   2403   4188     47    459    206       C  
ATOM   1823  O   LEU A 257      88.614  49.851  50.911  1.00 19.87           O  
ANISOU 1823  O   LEU A 257      756   2469   4323    -15    532    133       O  
ATOM   1824  CB  LEU A 257      91.122  48.539  49.202  1.00 18.91           C  
ANISOU 1824  CB  LEU A 257      658   2442   4082    215    492    259       C  
ATOM   1825  CG  LEU A 257      91.455  47.928  50.572  1.00 18.64           C  
ANISOU 1825  CG  LEU A 257      496   2379   4204    132    513    354       C  
ATOM   1826  CD1 LEU A 257      90.357  46.986  51.086  1.00 18.64           C  
ANISOU 1826  CD1 LEU A 257      806   2424   3850    165    536    216       C  
ATOM   1827  CD2 LEU A 257      92.799  47.213  50.516  1.00 20.36           C  
ANISOU 1827  CD2 LEU A 257      936   2454   4345    515     11    162       C  
ATOM   1828  N   GLU A 258      87.950  48.980  48.939  1.00 18.66           N  
ANISOU 1828  N   GLU A 258      751   2271   4065     96    273    165       N  
ATOM   1829  CA  GLU A 258      86.709  48.422  49.469  1.00 18.79           C  
ANISOU 1829  CA  GLU A 258      996   2288   3854    154    317    227       C  
ATOM   1830  C   GLU A 258      86.896  46.916  49.593  1.00 18.78           C  
ANISOU 1830  C   GLU A 258     1064   2304   3765     95    316    101       C  
ATOM   1831  O   GLU A 258      87.488  46.285  48.711  1.00 20.13           O  
ANISOU 1831  O   GLU A 258     1386   2418   3844    216    295     23       O  
ATOM   1832  CB  GLU A 258      85.520  48.719  48.543  1.00 19.05           C  
ANISOU 1832  CB  GLU A 258      982   2338   3918     29    182    228       C  
ATOM   1833  CG  GLU A 258      85.196  50.210  48.451  1.00 22.03           C  
ANISOU 1833  CG  GLU A 258     1602   2628   4140    289    151    335       C  
ATOM   1834  CD  GLU A 258      84.027  50.555  47.526  1.00 26.31           C  
ANISOU 1834  CD  GLU A 258     2266   3246   4485    310   -223    300       C  
ATOM   1835  OE1 GLU A 258      83.439  49.658  46.878  1.00 28.01           O  
ANISOU 1835  OE1 GLU A 258     2507   3576   4558    219    -89     55       O  
ATOM   1836  OE2 GLU A 258      83.678  51.756  47.456  1.00 27.32           O  
ANISOU 1836  OE2 GLU A 258     2616   3548   4217    655    -60    349       O  
ATOM   1837  N   ILE A 259      86.456  46.354  50.713  1.00 17.36           N  
ANISOU 1837  N   ILE A 259      886   2160   3548      2    302     42       N  
ATOM   1838  CA  ILE A 259      86.546  44.913  50.943  1.00 16.84           C  
ANISOU 1838  CA  ILE A 259      779   2206   3411     24    216     30       C  
ATOM   1839  C   ILE A 259      85.156  44.404  51.344  1.00 16.79           C  
ANISOU 1839  C   ILE A 259      718   2214   3444    -42    179    -50       C  
ATOM   1840  O   ILE A 259      84.537  44.873  52.308  1.00 16.48           O  
ANISOU 1840  O   ILE A 259      580   2327   3355   -138    119    -94       O  
ATOM   1841  CB  ILE A 259      87.657  44.554  51.965  1.00 16.60           C  
ANISOU 1841  CB  ILE A 259      773   2124   3408    126    295     63       C  
ATOM   1842  CG1 ILE A 259      87.801  43.034  52.126  1.00 16.48           C  
ANISOU 1842  CG1 ILE A 259      657   2206   3396    155    123     70       C  
ATOM   1843  CG2 ILE A 259      87.434  45.258  53.310  1.00 18.10           C  
ANISOU 1843  CG2 ILE A 259     1365   2120   3390    110     84     99       C  
ATOM   1844  CD1 ILE A 259      89.019  42.635  52.943  1.00 15.89           C  
ANISOU 1844  CD1 ILE A 259      517   2230   3288    163    129    170       C  
ATOM   1845  N   PHE A 260      84.662  43.466  50.546  1.00 16.82           N  
ANISOU 1845  N   PHE A 260      730   2302   3358    -45    109    -73       N  
ATOM   1846  CA  PHE A 260      83.327  42.902  50.733  1.00 16.99           C  
ANISOU 1846  CA  PHE A 260      830   2247   3378    -11     66   -106       C  
ATOM   1847  C   PHE A 260      83.381  41.678  51.643  1.00 16.80           C  
ANISOU 1847  C   PHE A 260      830   2305   3244    -35    116   -122       C  
ATOM   1848  O   PHE A 260      84.471  41.140  51.892  1.00 17.21           O  
ANISOU 1848  O   PHE A 260      842   2218   3479     23    309   -160       O  
ATOM   1849  CB  PHE A 260      82.739  42.595  49.354  1.00 16.58           C  
ANISOU 1849  CB  PHE A 260      900   2255   3143     29     -2    -58       C  
ATOM   1850  CG  PHE A 260      82.582  43.824  48.506  1.00 17.99           C  
ANISOU 1850  CG  PHE A 260     1164   2351   3319    171    164    -30       C  
ATOM   1851  CD1 PHE A 260      83.645  44.301  47.745  1.00 16.93           C  
ANISOU 1851  CD1 PHE A 260     1424   2042   2963     -2   -146    114       C  
ATOM   1852  CD2 PHE A 260      81.369  44.514  48.485  1.00 18.44           C  
ANISOU 1852  CD2 PHE A 260     1239   2504   3262    286      4    115       C  
ATOM   1853  CE1 PHE A 260      83.508  45.461  46.984  1.00 18.90           C  
ANISOU 1853  CE1 PHE A 260     1763   2558   2857    171    -42    217       C  
ATOM   1854  CE2 PHE A 260      81.221  45.674  47.734  1.00 18.30           C  
ANISOU 1854  CE2 PHE A 260     1502   2430   3020     83    490     66       C  
ATOM   1855  CZ  PHE A 260      82.297  46.151  46.983  1.00 18.02           C  
ANISOU 1855  CZ  PHE A 260     1410   2386   3050    -38    213     -6       C  
ATOM   1856  N   ALA A 261      82.220  41.273  52.156  1.00 16.24           N  
ANISOU 1856  N   ALA A 261      699   2265   3204     52    236   -174       N  
ATOM   1857  CA  ALA A 261      82.098  40.182  53.118  1.00 15.94           C  
ANISOU 1857  CA  ALA A 261      771   2184   3101     85    212   -115       C  
ATOM   1858  C   ALA A 261      82.821  38.936  52.633  1.00 16.66           C  
ANISOU 1858  C   ALA A 261      902   2238   3187     92    234    -98       C  
ATOM   1859  O   ALA A 261      82.523  38.406  51.562  1.00 16.74           O  
ANISOU 1859  O   ALA A 261     1045   2243   3071    154    176   -137       O  
ATOM   1860  CB  ALA A 261      80.624  39.851  53.386  1.00 17.11           C  
ANISOU 1860  CB  ALA A 261      914   2335   3250     -4    270    -79       C  
ATOM   1861  N   GLY A 262      83.797  38.501  53.420  1.00 16.42           N  
ANISOU 1861  N   GLY A 262     1079   2030   3128     76    244     15       N  
ATOM   1862  CA  GLY A 262      84.554  37.288  53.102  1.00 15.89           C  
ANISOU 1862  CA  GLY A 262      863   2128   3044    121    430    -16       C  
ATOM   1863  C   GLY A 262      85.730  37.402  52.151  1.00 15.86           C  
ANISOU 1863  C   GLY A 262      874   2166   2984     86    319     -8       C  
ATOM   1864  O   GLY A 262      86.411  36.401  51.929  1.00 16.01           O  
ANISOU 1864  O   GLY A 262     1025   2091   2965     35    342    -94       O  
ATOM   1865  N   GLN A 263      85.986  38.586  51.593  1.00 15.80           N  
ANISOU 1865  N   GLN A 263      831   2142   3028     49    379     34       N  
ATOM   1866  CA  GLN A 263      87.212  38.820  50.812  1.00 15.79           C  
ANISOU 1866  CA  GLN A 263      631   2280   3085    100    322     81       C  
ATOM   1867  C   GLN A 263      88.451  38.991  51.688  1.00 16.67           C  
ANISOU 1867  C   GLN A 263      755   2312   3264     79    339     70       C  
ATOM   1868  O   GLN A 263      88.322  39.280  52.880  1.00 15.57           O  
ANISOU 1868  O   GLN A 263      577   2138   3199    184    551     66       O  
ATOM   1869  CB  GLN A 263      87.042  40.060  49.941  1.00 16.35           C  
ANISOU 1869  CB  GLN A 263      730   2392   3088    -61    412     24       C  
ATOM   1870  CG  GLN A 263      86.103  39.866  48.763  1.00 16.54           C  
ANISOU 1870  CG  GLN A 263      603   2704   2977    154    151   -104       C  
ATOM   1871  CD  GLN A 263      85.954  41.118  47.935  1.00 18.11           C  
ANISOU 1871  CD  GLN A 263     1058   3071   2750    394    194   -238       C  
ATOM   1872  OE1 GLN A 263      86.247  42.222  48.409  1.00 18.87           O  
ANISOU 1872  OE1 GLN A 263     1187   3398   2584    200    -95   -405       O  
ATOM   1873  NE2 GLN A 263      85.527  40.956  46.681  1.00 17.77           N  
ANISOU 1873  NE2 GLN A 263      741   3353   2655    560   -123   -135       N  
ATOM   1874  N   ARG A 264      89.628  38.770  51.091  1.00 17.01           N  
ANISOU 1874  N   ARG A 264      621   2399   3440     82    229    102       N  
ATOM   1875  CA  ARG A 264      90.938  38.930  51.733  1.00 18.42           C  
ANISOU 1875  CA  ARG A 264      800   2501   3694     88    215    188       C  
ATOM   1876  C   ARG A 264      91.887  39.668  50.786  1.00 19.37           C  
ANISOU 1876  C   ARG A 264      899   2689   3772     22    200    172       C  
ATOM   1877  O   ARG A 264      91.828  39.466  49.573  1.00 19.97           O  
ANISOU 1877  O   ARG A 264     1076   2837   3675     -8    335    226       O  
ATOM   1878  CB  ARG A 264      91.563  37.563  52.076  1.00 18.36           C  
ANISOU 1878  CB  ARG A 264      811   2460   3704     14     96    143       C  
ATOM   1879  CG  ARG A 264      90.819  36.789  53.176  1.00 19.32           C  
ANISOU 1879  CG  ARG A 264      952   2516   3870    -59    174    119       C  
ATOM   1880  CD  ARG A 264      89.675  35.955  52.605  1.00 17.90           C  
ANISOU 1880  CD  ARG A 264      583   2077   4141    190    115   -114       C  
ATOM   1881  NE  ARG A 264      90.193  34.859  51.787  1.00 19.21           N  
ANISOU 1881  NE  ARG A 264      980   2281   4035    413    -21    -60       N  
ATOM   1882  CZ  ARG A 264      89.561  34.319  50.750  1.00 20.16           C  
ANISOU 1882  CZ  ARG A 264     1022   2138   4497     76    240   -201       C  
ATOM   1883  NH1 ARG A 264      88.380  34.785  50.375  1.00 20.52           N  
ANISOU 1883  NH1 ARG A 264     1153   2230   4412    105    142     45       N  
ATOM   1884  NH2 ARG A 264      90.122  33.324  50.075  1.00 20.96           N  
ANISOU 1884  NH2 ARG A 264     1061   2493   4410     57    576   -338       N  
ATOM   1885  N   TYR A 265      92.750  40.510  51.349  1.00 19.70           N  
ANISOU 1885  N   TYR A 265      946   2696   3841     40    205    154       N  
ATOM   1886  CA  TYR A 265      93.876  41.098  50.633  1.00 19.28           C  
ANISOU 1886  CA  TYR A 265      752   2671   3901    116    170    134       C  
ATOM   1887  C   TYR A 265      95.097  41.026  51.530  1.00 20.00           C  
ANISOU 1887  C   TYR A 265      713   2801   4084    122    236    105       C  
ATOM   1888  O   TYR A 265      94.992  41.248  52.742  1.00 20.61           O  
ANISOU 1888  O   TYR A 265      617   2979   4234    124    257     93       O  
ATOM   1889  CB  TYR A 265      93.607  42.577  50.323  1.00 19.46           C  
ANISOU 1889  CB  TYR A 265      899   2696   3797    132    156    112       C  
ATOM   1890  CG  TYR A 265      92.529  42.827  49.291  1.00 18.57           C  
ANISOU 1890  CG  TYR A 265      773   2609   3673    253     74     64       C  
ATOM   1891  CD1 TYR A 265      92.758  42.539  47.949  1.00 18.95           C  
ANISOU 1891  CD1 TYR A 265      773   2809   3617    264     32    124       C  
ATOM   1892  CD2 TYR A 265      91.302  43.395  49.652  1.00 18.49           C  
ANISOU 1892  CD2 TYR A 265      839   2662   3525    146      9    199       C  
ATOM   1893  CE1 TYR A 265      91.779  42.756  46.988  1.00 17.98           C  
ANISOU 1893  CE1 TYR A 265      905   2649   3275    265    138    433       C  
ATOM   1894  CE2 TYR A 265      90.304  43.629  48.693  1.00 18.15           C  
ANISOU 1894  CE2 TYR A 265     1395   2642   2859    127     82    167       C  
ATOM   1895  CZ  TYR A 265      90.576  43.318  47.369  1.00 16.62           C  
ANISOU 1895  CZ  TYR A 265     1083   2357   2874    200    132     91       C  
ATOM   1896  OH  TYR A 265      89.617  43.542  46.420  1.00 17.48           O  
ANISOU 1896  OH  TYR A 265     1315   2742   2582    231    299    108       O  
ATOM   1897  N   SER A 266      96.249  40.702  50.951  1.00 20.11           N  
ANISOU 1897  N   SER A 266      701   2705   4234    203    255    116       N  
ATOM   1898  CA  SER A 266      97.506  40.988  51.636  1.00 20.53           C  
ANISOU 1898  CA  SER A 266      718   2687   4395    167    352     95       C  
ATOM   1899  C   SER A 266      98.026  42.260  51.004  1.00 20.74           C  
ANISOU 1899  C   SER A 266      730   2664   4486    131    329     91       C  
ATOM   1900  O   SER A 266      97.987  42.395  49.782  1.00 21.05           O  
ANISOU 1900  O   SER A 266      777   2712   4509    110    301    165       O  
ATOM   1901  CB  SER A 266      98.551  39.892  51.416  1.00 20.50           C  
ANISOU 1901  CB  SER A 266      749   2642   4397    267    407    121       C  
ATOM   1902  OG  SER A 266      98.320  38.768  52.249  1.00 22.02           O  
ANISOU 1902  OG  SER A 266     1108   2862   4393    371    583      4       O  
ATOM   1903  N   PHE A 267      98.566  43.159  51.821  1.00 20.87           N  
ANISOU 1903  N   PHE A 267      771   2578   4581    168    462     17       N  
ATOM   1904  CA  PHE A 267      99.228  44.334  51.274  1.00 21.06           C  
ANISOU 1904  CA  PHE A 267      698   2540   4760    136    372    -12       C  
ATOM   1905  C   PHE A 267     100.518  44.595  52.027  1.00 21.61           C  
ANISOU 1905  C   PHE A 267      594   2696   4920    139    399     -8       C  
ATOM   1906  O   PHE A 267     100.609  44.284  53.224  1.00 21.44           O  
ANISOU 1906  O   PHE A 267      503   2714   4929     -6    459      5       O  
ATOM   1907  CB  PHE A 267      98.309  45.560  51.312  1.00 20.46           C  
ANISOU 1907  CB  PHE A 267      666   2411   4695    258    411    -37       C  
ATOM   1908  CG  PHE A 267      97.892  45.994  52.696  1.00 20.74           C  
ANISOU 1908  CG  PHE A 267      905   2301   4673    128    395     38       C  
ATOM   1909  CD1 PHE A 267      98.687  46.872  53.441  1.00 21.38           C  
ANISOU 1909  CD1 PHE A 267     1252   2337   4535    324    261     36       C  
ATOM   1910  CD2 PHE A 267      96.677  45.582  53.225  1.00 19.98           C  
ANISOU 1910  CD2 PHE A 267      790   2048   4753    284    363    -49       C  
ATOM   1911  CE1 PHE A 267      98.288  47.306  54.717  1.00 20.10           C  
ANISOU 1911  CE1 PHE A 267     1165   2184   4284    242    261    316       C  
ATOM   1912  CE2 PHE A 267      96.260  45.996  54.501  1.00 21.03           C  
ANISOU 1912  CE2 PHE A 267     1107   2323   4560    -38    326    224       C  
ATOM   1913  CZ  PHE A 267      97.054  46.873  55.247  1.00 20.34           C  
ANISOU 1913  CZ  PHE A 267     1075   2250   4402    199    118    345       C  
ATOM   1914  N   ILE A 268     101.501  45.167  51.335  1.00 22.14           N  
ANISOU 1914  N   ILE A 268      553   2892   4964    115    434     19       N  
ATOM   1915  CA  ILE A 268     102.746  45.562  51.994  1.00 23.50           C  
ANISOU 1915  CA  ILE A 268      638   3121   5167     76    401    -30       C  
ATOM   1916  C   ILE A 268     102.563  46.963  52.545  1.00 23.25           C  
ANISOU 1916  C   ILE A 268      584   3062   5187    101    395      8       C  
ATOM   1917  O   ILE A 268     102.080  47.845  51.837  1.00 23.46           O  
ANISOU 1917  O   ILE A 268      689   3183   5042    217    421      9       O  
ATOM   1918  CB  ILE A 268     103.950  45.587  51.020  1.00 24.14           C  
ANISOU 1918  CB  ILE A 268      674   3218   5278     52    380    -59       C  
ATOM   1919  CG1 ILE A 268     104.054  44.271  50.236  1.00 27.00           C  
ANISOU 1919  CG1 ILE A 268     1429   3259   5569     98    262    -61       C  
ATOM   1920  CG2 ILE A 268     105.262  45.896  51.768  1.00 24.34           C  
ANISOU 1920  CG2 ILE A 268      415   3570   5264     19    492     53       C  
ATOM   1921  CD1 ILE A 268     104.157  43.037  51.106  1.00 31.31           C  
ANISOU 1921  CD1 ILE A 268     2494   3524   5877    299     -5     63       C  
ATOM   1922  N   LEU A 269     102.911  47.155  53.813  1.00 22.98           N  
ANISOU 1922  N   LEU A 269      536   2947   5245    103    248     -8       N  
ATOM   1923  CA  LEU A 269     103.055  48.495  54.363  1.00 23.31           C  
ANISOU 1923  CA  LEU A 269      450   2979   5426     -1    266      0       C  
ATOM   1924  C   LEU A 269     104.527  48.669  54.719  1.00 24.02           C  
ANISOU 1924  C   LEU A 269      554   2998   5574    -86    254     28       C  
ATOM   1925  O   LEU A 269     105.115  47.840  55.418  1.00 22.79           O  
ANISOU 1925  O   LEU A 269      299   2889   5469     23    277    -39       O  
ATOM   1926  CB  LEU A 269     102.162  48.705  55.587  1.00 23.34           C  
ANISOU 1926  CB  LEU A 269      487   2978   5400    -47    234   -104       C  
ATOM   1927  CG  LEU A 269     102.243  50.090  56.245  1.00 23.64           C  
ANISOU 1927  CG  LEU A 269      508   3040   5434    302    190   -128       C  
ATOM   1928  CD1 LEU A 269     100.879  50.554  56.744  1.00 23.90           C  
ANISOU 1928  CD1 LEU A 269      500   3371   5209    236    442     -2       C  
ATOM   1929  CD2 LEU A 269     103.275  50.084  57.377  1.00 22.07           C  
ANISOU 1929  CD2 LEU A 269      423   2594   5365    144     77   -217       C  
ATOM   1930  N   ASN A 270     105.112  49.737  54.192  1.00 24.77           N  
ANISOU 1930  N   ASN A 270      613   2929   5867   -231    294    120       N  
ATOM   1931  CA  ASN A 270     106.473  50.137  54.511  1.00 26.41           C  
ANISOU 1931  CA  ASN A 270      776   3049   6208   -282    364    142       C  
ATOM   1932  C   ASN A 270     106.428  51.139  55.661  1.00 26.72           C  
ANISOU 1932  C   ASN A 270      844   2915   6392   -305    334    135       C  
ATOM   1933  O   ASN A 270     105.878  52.233  55.513  1.00 26.61           O  
ANISOU 1933  O   ASN A 270      824   2813   6471   -214    245    115       O  
ATOM   1934  CB  ASN A 270     107.120  50.753  53.270  1.00 27.41           C  
ANISOU 1934  CB  ASN A 270      993   3225   6196   -266    433    153       C  
ATOM   1935  CG  ASN A 270     108.611  50.994  53.445  1.00 30.06           C  
ANISOU 1935  CG  ASN A 270     1300   3778   6341   -594    743    205       C  
ATOM   1936  OD1 ASN A 270     109.156  50.860  54.545  1.00 32.31           O  
ANISOU 1936  OD1 ASN A 270     2086   3974   6214   -721    856    176       O  
ATOM   1937  ND2 ASN A 270     109.290  51.330  52.351  1.00 35.43           N  
ANISOU 1937  ND2 ASN A 270     2659   4580   6221   -680   1100    274       N  
ATOM   1938  N   ALA A 271     106.957  50.771  56.823  1.00 26.53           N  
ANISOU 1938  N   ALA A 271      781   2786   6514   -367    317    148       N  
ATOM   1939  CA  ALA A 271     106.865  51.683  57.962  1.00 27.43           C  
ANISOU 1939  CA  ALA A 271      933   2765   6721   -490    425    166       C  
ATOM   1940  C   ALA A 271     108.027  52.685  57.929  1.00 28.44           C  
ANISOU 1940  C   ALA A 271     1111   2837   6856   -533    474    168       C  
ATOM   1941  O   ALA A 271     108.967  52.614  58.730  1.00 29.31           O  
ANISOU 1941  O   ALA A 271     1336   2844   6956   -616    482    179       O  
ATOM   1942  CB  ALA A 271     106.791  50.921  59.285  1.00 26.19           C  
ANISOU 1942  CB  ALA A 271      551   2717   6683   -401    419    184       C  
ATOM   1943  N   ASN A 272     107.951  53.611  56.976  1.00 28.78           N  
ANISOU 1943  N   ASN A 272     1335   2709   6891   -625    559    183       N  
ATOM   1944  CA  ASN A 272     109.022  54.581  56.751  1.00 30.59           C  
ANISOU 1944  CA  ASN A 272     1719   2907   6993   -635    572    174       C  
ATOM   1945  C   ASN A 272     108.605  56.024  57.063  1.00 30.51           C  
ANISOU 1945  C   ASN A 272     1721   2833   7036   -729    514    137       C  
ATOM   1946  O   ASN A 272     109.302  56.970  56.706  1.00 30.56           O  
ANISOU 1946  O   ASN A 272     1953   2594   7061   -820    636    140       O  
ATOM   1947  CB  ASN A 272     109.522  54.456  55.307  1.00 31.76           C  
ANISOU 1947  CB  ASN A 272     1920   3096   7049   -585    616    180       C  
ATOM   1948  CG  ASN A 272     108.460  54.833  54.274  1.00 33.66           C  
ANISOU 1948  CG  ASN A 272     2385   3424   6980   -476    688    287       C  
ATOM   1949  OD1 ASN A 272     107.288  55.035  54.585  1.00 34.33           O  
ANISOU 1949  OD1 ASN A 272     2632   3191   7220   -620    643    168       O  
ATOM   1950  ND2 ASN A 272     108.888  54.952  53.025  1.00 39.00           N  
ANISOU 1950  ND2 ASN A 272     3603   4205   7008    -44    958    210       N  
ATOM   1951  N   GLN A 273     107.475  56.191  57.741  1.00 29.84           N  
ANISOU 1951  N   GLN A 273     1566   2781   6988   -652    431    106       N  
ATOM   1952  CA  GLN A 273     106.951  57.513  58.064  1.00 30.50           C  
ANISOU 1952  CA  GLN A 273     1613   2948   7025   -616    310     93       C  
ATOM   1953  C   GLN A 273     107.497  57.917  59.428  1.00 30.23           C  
ANISOU 1953  C   GLN A 273     1483   2991   7013   -577    276     83       C  
ATOM   1954  O   GLN A 273     108.123  57.095  60.104  1.00 30.47           O  
ANISOU 1954  O   GLN A 273     1436   3112   7030   -500    285     72       O  
ATOM   1955  CB  GLN A 273     105.419  57.482  58.062  1.00 30.69           C  
ANISOU 1955  CB  GLN A 273     1670   2912   7078   -535    324    131       C  
ATOM   1956  CG  GLN A 273     104.824  57.258  56.675  1.00 32.16           C  
ANISOU 1956  CG  GLN A 273     2011   3043   7165   -587    255    115       C  
ATOM   1957  CD  GLN A 273     105.401  58.234  55.667  1.00 35.89           C  
ANISOU 1957  CD  GLN A 273     2993   3305   7337   -394    375    279       C  
ATOM   1958  OE1 GLN A 273     105.152  59.435  55.743  1.00 36.38           O  
ANISOU 1958  OE1 GLN A 273     3256   3125   7439   -610    282    621       O  
ATOM   1959  NE2 GLN A 273     106.218  57.731  54.749  1.00 38.35           N  
ANISOU 1959  NE2 GLN A 273     3459   3712   7399   -407    474     55       N  
ATOM   1960  N   PRO A 274     107.275  59.173  59.842  1.00 29.81           N  
ANISOU 1960  N   PRO A 274     1386   2967   6971   -553    196     86       N  
ATOM   1961  CA  PRO A 274     107.711  59.549  61.184  1.00 29.59           C  
ANISOU 1961  CA  PRO A 274     1362   2988   6890   -480    144     39       C  
ATOM   1962  C   PRO A 274     107.072  58.709  62.292  1.00 29.02           C  
ANISOU 1962  C   PRO A 274     1215   3008   6800   -431     56    -13       C  
ATOM   1963  O   PRO A 274     105.914  58.296  62.178  1.00 28.81           O  
ANISOU 1963  O   PRO A 274     1158   2990   6797   -411     75    -37       O  
ATOM   1964  CB  PRO A 274     107.271  61.011  61.301  1.00 30.36           C  
ANISOU 1964  CB  PRO A 274     1558   3077   6898   -472    102     86       C  
ATOM   1965  CG  PRO A 274     107.273  61.511  59.884  1.00 31.53           C  
ANISOU 1965  CG  PRO A 274     1845   3167   6968   -561    188     69       C  
ATOM   1966  CD  PRO A 274     106.792  60.332  59.068  1.00 30.36           C  
ANISOU 1966  CD  PRO A 274     1528   3002   7002   -608    143     82       C  
ATOM   1967  N   VAL A 275     107.840  58.444  63.346  1.00 28.32           N  
ANISOU 1967  N   VAL A 275     1045   3007   6706   -364     33    -65       N  
ATOM   1968  CA  VAL A 275     107.326  57.749  64.525  1.00 27.30           C  
ANISOU 1968  CA  VAL A 275      801   2985   6585   -293    -51    -86       C  
ATOM   1969  C   VAL A 275     106.118  58.501  65.080  1.00 26.50           C  
ANISOU 1969  C   VAL A 275      748   2890   6427   -362    -90   -121       C  
ATOM   1970  O   VAL A 275     106.228  59.632  65.552  1.00 26.39           O  
ANISOU 1970  O   VAL A 275      662   2920   6442   -320   -105   -128       O  
ATOM   1971  CB  VAL A 275     108.409  57.634  65.617  1.00 27.09           C  
ANISOU 1971  CB  VAL A 275      765   2961   6567   -342    -67   -158       C  
ATOM   1972  CG1 VAL A 275     107.856  56.997  66.875  1.00 27.63           C  
ANISOU 1972  CG1 VAL A 275      800   3106   6591   -240    -38   -136       C  
ATOM   1973  CG2 VAL A 275     109.575  56.819  65.095  1.00 27.38           C  
ANISOU 1973  CG2 VAL A 275      571   3136   6693   -152    -75   -134       C  
ATOM   1974  N   ASP A 276     104.951  57.878  64.994  1.00 25.68           N  
ANISOU 1974  N   ASP A 276      692   2842   6220   -335   -209   -118       N  
ATOM   1975  CA  ASP A 276     103.737  58.503  65.493  1.00 24.90           C  
ANISOU 1975  CA  ASP A 276      748   2698   6016   -364   -216   -128       C  
ATOM   1976  C   ASP A 276     102.647  57.435  65.601  1.00 23.74           C  
ANISOU 1976  C   ASP A 276      629   2693   5696   -369   -284   -135       C  
ATOM   1977  O   ASP A 276     102.858  56.242  65.336  1.00 22.76           O  
ANISOU 1977  O   ASP A 276      384   2621   5640   -368   -379    -62       O  
ATOM   1978  CB  ASP A 276     103.277  59.587  64.507  1.00 25.64           C  
ANISOU 1978  CB  ASP A 276      997   2627   6118   -376   -233   -126       C  
ATOM   1979  CG  ASP A 276     102.511  60.732  65.165  1.00 28.19           C  
ANISOU 1979  CG  ASP A 276     1374   2725   6609   -263   -161    -28       C  
ATOM   1980  OD1 ASP A 276     101.933  60.587  66.268  1.00 28.70           O  
ANISOU 1980  OD1 ASP A 276     1793   2615   6495   -314   -360   -168       O  
ATOM   1981  OD2 ASP A 276     102.494  61.820  64.548  1.00 31.50           O  
ANISOU 1981  OD2 ASP A 276     2063   2802   7101    109    -51     94       O  
ATOM   1982  N   ASN A 277     101.483  57.903  66.026  1.00 22.37           N  
ANISOU 1982  N   ASN A 277      561   2614   5323   -275   -314   -123       N  
ATOM   1983  CA  ASN A 277     100.244  57.153  65.953  1.00 21.27           C  
ANISOU 1983  CA  ASN A 277      588   2535   4959   -310   -310    -75       C  
ATOM   1984  C   ASN A 277      99.439  57.612  64.736  1.00 21.03           C  
ANISOU 1984  C   ASN A 277      690   2504   4795   -269   -247    -55       C  
ATOM   1985  O   ASN A 277      99.220  58.817  64.586  1.00 21.38           O  
ANISOU 1985  O   ASN A 277      872   2536   4713   -194   -280   -112       O  
ATOM   1986  CB  ASN A 277      99.468  57.451  67.230  1.00 20.84           C  
ANISOU 1986  CB  ASN A 277      643   2497   4776   -263   -339    -49       C  
ATOM   1987  CG  ASN A 277     100.125  56.836  68.448  1.00 22.52           C  
ANISOU 1987  CG  ASN A 277     1005   2716   4835   -302   -474   -117       C  
ATOM   1988  OD1 ASN A 277     100.201  55.605  68.566  1.00 22.21           O  
ANISOU 1988  OD1 ASN A 277     1234   2555   4648     27   -525    -21       O  
ATOM   1989  ND2 ASN A 277     100.608  57.691  69.357  1.00 21.56           N  
ANISOU 1989  ND2 ASN A 277      891   2926   4374   -423   -801    100       N  
ATOM   1990  N   TYR A 278      99.006  56.667  63.894  1.00 20.31           N  
ANISOU 1990  N   TYR A 278      516   2525   4675   -217   -157    -36       N  
ATOM   1991  CA  TYR A 278      98.245  56.929  62.671  1.00 19.46           C  
ANISOU 1991  CA  TYR A 278      413   2392   4586   -132   -127    -41       C  
ATOM   1992  C   TYR A 278      96.884  56.218  62.710  1.00 19.25           C  
ANISOU 1992  C   TYR A 278      399   2390   4524    -71   -141    -40       C  
ATOM   1993  O   TYR A 278      96.799  55.053  63.113  1.00 18.50           O  
ANISOU 1993  O   TYR A 278      389   2286   4352    -31   -128     61       O  
ATOM   1994  CB  TYR A 278      99.012  56.435  61.437  1.00 19.31           C  
ANISOU 1994  CB  TYR A 278      374   2356   4607   -153    -61    -43       C  
ATOM   1995  CG  TYR A 278     100.336  57.139  61.237  1.00 19.75           C  
ANISOU 1995  CG  TYR A 278      500   2334   4668   -262     -6   -153       C  
ATOM   1996  CD1 TYR A 278     101.468  56.732  61.931  1.00 19.93           C  
ANISOU 1996  CD1 TYR A 278      363   2546   4663   -332   -255   -282       C  
ATOM   1997  CD2 TYR A 278     100.450  58.231  60.378  1.00 20.39           C  
ANISOU 1997  CD2 TYR A 278      768   2193   4784   -563    133   -205       C  
ATOM   1998  CE1 TYR A 278     102.700  57.400  61.770  1.00 20.24           C  
ANISOU 1998  CE1 TYR A 278      755   1964   4971   -663    132   -247       C  
ATOM   1999  CE2 TYR A 278     101.679  58.882  60.197  1.00 19.89           C  
ANISOU 1999  CE2 TYR A 278      488   2210   4860   -455     19   -195       C  
ATOM   2000  CZ  TYR A 278     102.794  58.467  60.898  1.00 20.12           C  
ANISOU 2000  CZ  TYR A 278      611   2178   4854   -352    196   -256       C  
ATOM   2001  OH  TYR A 278     103.994  59.143  60.748  1.00 21.94           O  
ANISOU 2001  OH  TYR A 278     1029   2084   5220   -363      9   -175       O  
ATOM   2002  N   TRP A 279      95.825  56.886  62.258  1.00 18.76           N  
ANISOU 2002  N   TRP A 279      353   2341   4432     92   -148    -33       N  
ATOM   2003  CA  TRP A 279      94.514  56.227  62.208  1.00 18.51           C  
ANISOU 2003  CA  TRP A 279      394   2234   4403     89   -226   -138       C  
ATOM   2004  C   TRP A 279      94.454  55.115  61.168  1.00 18.92           C  
ANISOU 2004  C   TRP A 279      487   2271   4430     75   -161   -132       C  
ATOM   2005  O   TRP A 279      94.876  55.320  60.018  1.00 20.20           O  
ANISOU 2005  O   TRP A 279      901   2356   4415     23   -163   -121       O  
ATOM   2006  CB  TRP A 279      93.383  57.213  61.892  1.00 18.79           C  
ANISOU 2006  CB  TRP A 279      470   2328   4339    127   -306   -134       C  
ATOM   2007  CG  TRP A 279      92.998  58.136  63.000  1.00 19.56           C  
ANISOU 2007  CG  TRP A 279      333   2690   4407    266   -194   -207       C  
ATOM   2008  CD1 TRP A 279      93.069  59.504  62.986  1.00 20.12           C  
ANISOU 2008  CD1 TRP A 279      398   2913   4333    -94   -208   -369       C  
ATOM   2009  CD2 TRP A 279      92.482  57.770  64.284  1.00 20.95           C  
ANISOU 2009  CD2 TRP A 279      589   3031   4338    -62   -259   -254       C  
ATOM   2010  NE1 TRP A 279      92.603  60.014  64.179  1.00 22.44           N  
ANISOU 2010  NE1 TRP A 279      996   3122   4406    136   -165   -334       N  
ATOM   2011  CE2 TRP A 279      92.227  58.972  64.989  1.00 22.98           C  
ANISOU 2011  CE2 TRP A 279     1162   3192   4375   -154   -194   -281       C  
ATOM   2012  CE3 TRP A 279      92.185  56.545  64.901  1.00 22.29           C  
ANISOU 2012  CE3 TRP A 279      935   3163   4371   -173   -236   -369       C  
ATOM   2013  CZ2 TRP A 279      91.700  58.985  66.288  1.00 23.09           C  
ANISOU 2013  CZ2 TRP A 279      965   3352   4454      9   -204   -223       C  
ATOM   2014  CZ3 TRP A 279      91.651  56.560  66.194  1.00 23.58           C  
ANISOU 2014  CZ3 TRP A 279     1250   3370   4336   -440   -250   -284       C  
ATOM   2015  CH2 TRP A 279      91.417  57.773  66.870  1.00 23.44           C  
ANISOU 2015  CH2 TRP A 279     1027   3428   4449   -386     54   -304       C  
ATOM   2016  N   VAL A 280      93.959  53.949  61.594  1.00 17.81           N  
ANISOU 2016  N   VAL A 280      295   2103   4366     37   -121   -160       N  
ATOM   2017  CA  VAL A 280      93.545  52.875  60.691  1.00 17.64           C  
ANISOU 2017  CA  VAL A 280      294   1987   4419     61   -101   -184       C  
ATOM   2018  C   VAL A 280      92.032  52.951  60.557  1.00 17.78           C  
ANISOU 2018  C   VAL A 280      378   1988   4390     42    -54   -128       C  
ATOM   2019  O   VAL A 280      91.337  53.026  61.575  1.00 19.03           O  
ANISOU 2019  O   VAL A 280      415   2333   4479     53    -15   -157       O  
ATOM   2020  CB  VAL A 280      93.984  51.487  61.215  1.00 18.01           C  
ANISOU 2020  CB  VAL A 280      296   2014   4533    -56   -139   -172       C  
ATOM   2021  CG1 VAL A 280      93.444  50.378  60.314  1.00 18.97           C  
ANISOU 2021  CG1 VAL A 280      563   2002   4639     87    -65   -235       C  
ATOM   2022  CG2 VAL A 280      95.539  51.408  61.281  1.00 17.29           C  
ANISOU 2022  CG2 VAL A 280      327   1968   4271    220   -209   -328       C  
ATOM   2023  N   ARG A 281      91.515  52.935  59.329  1.00 16.97           N  
ANISOU 2023  N   ARG A 281      295   1850   4301     20   -105   -168       N  
ATOM   2024  CA  ARG A 281      90.104  53.240  59.103  1.00 17.40           C  
ANISOU 2024  CA  ARG A 281      430   1814   4363    -95    -19    -59       C  
ATOM   2025  C   ARG A 281      89.415  52.073  58.403  1.00 17.52           C  
ANISOU 2025  C   ARG A 281      462   1883   4311    -61    -11    -17       C  
ATOM   2026  O   ARG A 281      89.937  51.537  57.425  1.00 18.46           O  
ANISOU 2026  O   ARG A 281      627   2076   4310   -149    178     52       O  
ATOM   2027  CB  ARG A 281      89.969  54.508  58.256  1.00 17.27           C  
ANISOU 2027  CB  ARG A 281      380   1762   4418    -81   -113    -89       C  
ATOM   2028  CG  ARG A 281      90.539  55.758  58.920  1.00 17.69           C  
ANISOU 2028  CG  ARG A 281      653   1518   4549   -125      9     -4       C  
ATOM   2029  CD  ARG A 281      90.462  56.965  57.991  1.00 18.11           C  
ANISOU 2029  CD  ARG A 281      705   1945   4229    -51    -61    148       C  
ATOM   2030  NE  ARG A 281      91.203  58.102  58.545  1.00 19.06           N  
ANISOU 2030  NE  ARG A 281      743   1913   4586    -53    259     81       N  
ATOM   2031  CZ  ARG A 281      90.709  58.962  59.434  1.00 19.59           C  
ANISOU 2031  CZ  ARG A 281      769   1949   4722   -118    237     57       C  
ATOM   2032  NH1 ARG A 281      89.450  58.859  59.866  1.00 19.97           N  
ANISOU 2032  NH1 ARG A 281      743   2365   4478   -118    164    377       N  
ATOM   2033  NH2 ARG A 281      91.484  59.934  59.889  1.00 19.32           N  
ANISOU 2033  NH2 ARG A 281      916   1904   4518      7     55    205       N  
ATOM   2034  N   ALA A 282      88.278  51.643  58.947  1.00 16.70           N  
ANISOU 2034  N   ALA A 282      307   1825   4211    -66     25     73       N  
ATOM   2035  CA  ALA A 282      87.449  50.623  58.303  1.00 16.71           C  
ANISOU 2035  CA  ALA A 282      360   1828   4160     55    -18     69       C  
ATOM   2036  C   ALA A 282      86.007  51.094  58.394  1.00 16.70           C  
ANISOU 2036  C   ALA A 282      416   1894   4033     85     14     68       C  
ATOM   2037  O   ALA A 282      85.314  50.851  59.382  1.00 16.61           O  
ANISOU 2037  O   ALA A 282      293   1981   4038     95     45    140       O  
ATOM   2038  CB  ALA A 282      87.623  49.263  58.990  1.00 17.38           C  
ANISOU 2038  CB  ALA A 282      558   1889   4154    -29   -103    115       C  
ATOM   2039  N   ASN A 283      85.562  51.774  57.343  1.00 16.46           N  
ANISOU 2039  N   ASN A 283      401   1904   3946    209     22     68       N  
ATOM   2040  CA  ASN A 283      84.288  52.494  57.392  1.00 16.10           C  
ANISOU 2040  CA  ASN A 283      384   1983   3751    169    249     13       C  
ATOM   2041  C   ASN A 283      83.223  51.662  56.686  1.00 15.70           C  
ANISOU 2041  C   ASN A 283      414   1989   3561    115    267    -81       C  
ATOM   2042  O   ASN A 283      83.359  51.381  55.494  1.00 15.89           O  
ANISOU 2042  O   ASN A 283      641   2023   3374    175    342     15       O  
ATOM   2043  CB  ASN A 283      84.467  53.826  56.669  1.00 16.75           C  
ANISOU 2043  CB  ASN A 283      645   1909   3810    278    155    -17       C  
ATOM   2044  CG  ASN A 283      83.488  54.887  57.131  1.00 17.22           C  
ANISOU 2044  CG  ASN A 283      610   2011   3921    253    326    168       C  
ATOM   2045  OD1 ASN A 283      82.792  54.739  58.146  1.00 18.46           O  
ANISOU 2045  OD1 ASN A 283      936   2128   3948    -90    252   -291       O  
ATOM   2046  ND2 ASN A 283      83.483  56.008  56.415  1.00 18.69           N  
ANISOU 2046  ND2 ASN A 283     1044   2311   3743    150    114    503       N  
ATOM   2047  N   PRO A 284      82.160  51.259  57.407  1.00 15.56           N  
ANISOU 2047  N   PRO A 284      325   2049   3538     16    339   -166       N  
ATOM   2048  CA  PRO A 284      81.133  50.438  56.758  1.00 15.50           C  
ANISOU 2048  CA  PRO A 284      366   2032   3488     13    263   -165       C  
ATOM   2049  C   PRO A 284      80.319  51.261  55.770  1.00 16.05           C  
ANISOU 2049  C   PRO A 284      469   2043   3584    111    220   -144       C  
ATOM   2050  O   PRO A 284      80.366  52.492  55.812  1.00 16.73           O  
ANISOU 2050  O   PRO A 284      650   2111   3595    187    148   -163       O  
ATOM   2051  CB  PRO A 284      80.225  50.014  57.921  1.00 15.41           C  
ANISOU 2051  CB  PRO A 284      336   2028   3489     81    362   -147       C  
ATOM   2052  CG  PRO A 284      80.297  51.168  58.859  1.00 15.22           C  
ANISOU 2052  CG  PRO A 284      342   1944   3496   -154    365   -264       C  
ATOM   2053  CD  PRO A 284      81.780  51.610  58.788  1.00 15.75           C  
ANISOU 2053  CD  PRO A 284      329   2126   3527    -17    353   -163       C  
ATOM   2054  N   ASN A 285      79.603  50.595  54.871  1.00 16.36           N  
ANISOU 2054  N   ASN A 285      482   2132   3598    133     76   -110       N  
ATOM   2055  CA  ASN A 285      78.830  51.324  53.860  1.00 17.35           C  
ANISOU 2055  CA  ASN A 285      745   2138   3709    132    -40    -23       C  
ATOM   2056  C   ASN A 285      77.489  51.822  54.391  1.00 17.75           C  
ANISOU 2056  C   ASN A 285      878   2180   3686    165    -23      7       C  
ATOM   2057  O   ASN A 285      76.854  52.681  53.771  1.00 18.51           O  
ANISOU 2057  O   ASN A 285      941   2175   3914    171    -28    141       O  
ATOM   2058  CB  ASN A 285      78.641  50.516  52.567  1.00 17.97           C  
ANISOU 2058  CB  ASN A 285      849   2210   3769    154    -19    -88       C  
ATOM   2059  CG  ASN A 285      77.978  49.163  52.793  1.00 18.99           C  
ANISOU 2059  CG  ASN A 285     1039   2372   3804     90   -105   -110       C  
ATOM   2060  OD1 ASN A 285      78.341  48.423  53.701  1.00 20.12           O  
ANISOU 2060  OD1 ASN A 285     1428   2117   4098      3     44    135       O  
ATOM   2061  ND2 ASN A 285      77.001  48.833  51.952  1.00 21.97           N  
ANISOU 2061  ND2 ASN A 285     1600   2621   4124   -287   -518   -281       N  
ATOM   2062  N   PHE A 286      77.047  51.283  55.525  1.00 17.25           N  
ANISOU 2062  N   PHE A 286      879   2093   3583     43   -100     35       N  
ATOM   2063  CA  PHE A 286      75.836  51.813  56.175  1.00 17.21           C  
ANISOU 2063  CA  PHE A 286      904   2131   3504    -17   -295     49       C  
ATOM   2064  C   PHE A 286      75.978  51.514  57.667  1.00 16.82           C  
ANISOU 2064  C   PHE A 286      779   2152   3460     22   -374    107       C  
ATOM   2065  O   PHE A 286      76.899  50.773  58.072  1.00 17.82           O  
ANISOU 2065  O   PHE A 286      805   2237   3726     83   -425    117       O  
ATOM   2066  CB  PHE A 286      74.550  51.199  55.594  1.00 17.45           C  
ANISOU 2066  CB  PHE A 286     1036   2197   3395     21   -354    128       C  
ATOM   2067  CG  PHE A 286      74.613  49.707  55.472  1.00 19.63           C  
ANISOU 2067  CG  PHE A 286     1942   2187   3327   -388   -383    159       C  
ATOM   2068  CD1 PHE A 286      74.490  48.910  56.588  1.00 24.01           C  
ANISOU 2068  CD1 PHE A 286     3356   2331   3433   -502   -615    446       C  
ATOM   2069  CD2 PHE A 286      74.860  49.094  54.258  1.00 25.60           C  
ANISOU 2069  CD2 PHE A 286     3410   2503   3814   -365   -388     89       C  
ATOM   2070  CE1 PHE A 286      74.588  47.520  56.499  1.00 25.43           C  
ANISOU 2070  CE1 PHE A 286     3840   2495   3328   -199   -751    252       C  
ATOM   2071  CE2 PHE A 286      74.950  47.703  54.167  1.00 27.26           C  
ANISOU 2071  CE2 PHE A 286     3880   2611   3865   -210   -363    354       C  
ATOM   2072  CZ  PHE A 286      74.824  46.917  55.296  1.00 24.89           C  
ANISOU 2072  CZ  PHE A 286     3435   2491   3530   -249   -336    279       C  
ATOM   2073  N   GLY A 287      75.091  52.082  58.479  1.00 15.76           N  
ANISOU 2073  N   GLY A 287      613   2025   3351     32   -510     74       N  
ATOM   2074  CA  GLY A 287      75.231  52.038  59.934  1.00 16.05           C  
ANISOU 2074  CA  GLY A 287      584   2274   3240     -4   -461     75       C  
ATOM   2075  C   GLY A 287      75.778  53.361  60.450  1.00 17.03           C  
ANISOU 2075  C   GLY A 287      791   2467   3210    141   -538     31       C  
ATOM   2076  O   GLY A 287      75.338  54.439  60.050  1.00 16.92           O  
ANISOU 2076  O   GLY A 287      843   2464   3121    144   -613    -46       O  
ATOM   2077  N   ASN A 288      76.776  53.304  61.326  1.00 17.26           N  
ANISOU 2077  N   ASN A 288      816   2599   3140    104   -500     83       N  
ATOM   2078  CA  ASN A 288      77.436  54.527  61.745  1.00 17.04           C  
ANISOU 2078  CA  ASN A 288      772   2571   3130    102   -261    163       C  
ATOM   2079  C   ASN A 288      78.604  54.681  60.797  1.00 16.94           C  
ANISOU 2079  C   ASN A 288      664   2610   3162    139   -218    126       C  
ATOM   2080  O   ASN A 288      79.528  53.861  60.850  1.00 17.63           O  
ANISOU 2080  O   ASN A 288      747   2642   3310    127   -231    133       O  
ATOM   2081  CB  ASN A 288      77.892  54.409  63.201  1.00 16.91           C  
ANISOU 2081  CB  ASN A 288      739   2700   2982    106   -238    160       C  
ATOM   2082  CG  ASN A 288      76.715  54.184  64.135  1.00 20.52           C  
ANISOU 2082  CG  ASN A 288     1334   3196   3264     70    -56    310       C  
ATOM   2083  OD1 ASN A 288      76.629  53.183  64.847  1.00 26.39           O  
ANISOU 2083  OD1 ASN A 288     2207   4196   3622     82     51    705       O  
ATOM   2084  ND2 ASN A 288      75.772  55.099  64.092  1.00 21.88           N  
ANISOU 2084  ND2 ASN A 288     1422   3597   3295     69    226    252       N  
ATOM   2085  N   VAL A 289      78.495  55.649  59.884  1.00 16.66           N  
ANISOU 2085  N   VAL A 289      616   2392   3319     51    -45     71       N  
ATOM   2086  CA  VAL A 289      79.490  55.868  58.836  1.00 16.02           C  
ANISOU 2086  CA  VAL A 289      461   2339   3285    -66   -155     18       C  
ATOM   2087  C   VAL A 289      80.248  57.145  59.202  1.00 17.07           C  
ANISOU 2087  C   VAL A 289      531   2421   3532     -7   -139    -57       C  
ATOM   2088  O   VAL A 289      79.640  58.196  59.476  1.00 16.50           O  
ANISOU 2088  O   VAL A 289      342   2305   3622     59    -84    -96       O  
ATOM   2089  CB  VAL A 289      78.815  55.985  57.445  1.00 16.20           C  
ANISOU 2089  CB  VAL A 289      525   2355   3272    -46   -137     38       C  
ATOM   2090  CG1 VAL A 289      79.833  56.375  56.373  1.00 17.05           C  
ANISOU 2090  CG1 VAL A 289      477   2611   3389    -81   -257    122       C  
ATOM   2091  CG2 VAL A 289      78.109  54.670  57.084  1.00 14.83           C  
ANISOU 2091  CG2 VAL A 289      309   2416   2911      4   -219    -54       C  
ATOM   2092  N   GLY A 290      81.573  57.029  59.252  1.00 16.36           N  
ANISOU 2092  N   GLY A 290      295   2374   3544    -14   -112   -108       N  
ATOM   2093  CA  GLY A 290      82.400  58.127  59.729  1.00 17.26           C  
ANISOU 2093  CA  GLY A 290      501   2290   3765   -100   -207   -104       C  
ATOM   2094  C   GLY A 290      83.227  57.739  60.946  1.00 18.38           C  
ANISOU 2094  C   GLY A 290      661   2380   3941    -46   -179   -146       C  
ATOM   2095  O   GLY A 290      83.344  56.559  61.296  1.00 18.35           O  
ANISOU 2095  O   GLY A 290      578   2397   3997     13   -128   -120       O  
ATOM   2096  N   PHE A 291      83.780  58.742  61.625  1.00 18.87           N  
ANISOU 2096  N   PHE A 291      676   2462   4030   -150   -174   -128       N  
ATOM   2097  CA  PHE A 291      84.773  58.475  62.662  1.00 18.33           C  
ANISOU 2097  CA  PHE A 291      654   2365   3945     16   -138   -186       C  
ATOM   2098  C   PHE A 291      84.573  59.226  63.977  1.00 18.90           C  
ANISOU 2098  C   PHE A 291      808   2370   4001     50   -149   -164       C  
ATOM   2099  O   PHE A 291      85.504  59.372  64.763  1.00 18.77           O  
ANISOU 2099  O   PHE A 291      860   2375   3895    -19   -238   -374       O  
ATOM   2100  CB  PHE A 291      86.165  58.685  62.060  1.00 18.86           C  
ANISOU 2100  CB  PHE A 291      715   2451   4000     58    -86   -213       C  
ATOM   2101  CG  PHE A 291      86.350  57.934  60.771  1.00 16.93           C  
ANISOU 2101  CG  PHE A 291      411   2148   3871      3    -31   -298       C  
ATOM   2102  CD1 PHE A 291      86.685  56.587  60.790  1.00 17.12           C  
ANISOU 2102  CD1 PHE A 291      519   2047   3938   -101     91   -448       C  
ATOM   2103  CD2 PHE A 291      86.147  58.563  59.544  1.00 16.74           C  
ANISOU 2103  CD2 PHE A 291      311   2021   4029    -62     19   -411       C  
ATOM   2104  CE1 PHE A 291      86.869  55.883  59.606  1.00 17.65           C  
ANISOU 2104  CE1 PHE A 291      773   2017   3915   -222    -33   -453       C  
ATOM   2105  CE2 PHE A 291      86.291  57.863  58.348  1.00 16.66           C  
ANISOU 2105  CE2 PHE A 291      361   2093   3873    242    298   -361       C  
ATOM   2106  CZ  PHE A 291      86.646  56.513  58.382  1.00 17.59           C  
ANISOU 2106  CZ  PHE A 291      770   1900   4010     55    410   -261       C  
ATOM   2107  N   THR A 292      83.352  59.688  64.231  1.00 18.63           N  
ANISOU 2107  N   THR A 292      772   2339   3965    118   -104   -120       N  
ATOM   2108  CA  THR A 292      83.073  60.374  65.483  1.00 19.44           C  
ANISOU 2108  CA  THR A 292     1032   2375   3980    188    -93   -132       C  
ATOM   2109  C   THR A 292      83.516  59.539  66.678  1.00 19.65           C  
ANISOU 2109  C   THR A 292      945   2438   4080    199   -160   -178       C  
ATOM   2110  O   THR A 292      83.182  58.351  66.793  1.00 19.90           O  
ANISOU 2110  O   THR A 292     1004   2452   4104    324   -178     17       O  
ATOM   2111  CB  THR A 292      81.576  60.698  65.631  1.00 19.83           C  
ANISOU 2111  CB  THR A 292     1112   2490   3930    335   -115   -110       C  
ATOM   2112  OG1 THR A 292      81.210  61.618  64.599  1.00 22.07           O  
ANISOU 2112  OG1 THR A 292     1896   2572   3917    537   -155    -49       O  
ATOM   2113  CG2 THR A 292      81.294  61.354  66.975  1.00 20.89           C  
ANISOU 2113  CG2 THR A 292     1347   2644   3944    160    -59   -207       C  
ATOM   2114  N   ASN A 293      84.268  60.168  67.571  1.00 20.29           N  
ANISOU 2114  N   ASN A 293     1029   2478   4202     35   -110   -234       N  
ATOM   2115  CA  ASN A 293      84.773  59.481  68.761  1.00 21.37           C  
ANISOU 2115  CA  ASN A 293     1301   2535   4282     36   -122   -299       C  
ATOM   2116  C   ASN A 293      85.631  58.243  68.515  1.00 20.85           C  
ANISOU 2116  C   ASN A 293     1134   2537   4250      5   -117   -288       C  
ATOM   2117  O   ASN A 293      85.766  57.397  69.404  1.00 21.43           O  
ANISOU 2117  O   ASN A 293     1341   2562   4237     23   -155   -312       O  
ATOM   2118  CB  ASN A 293      83.601  59.155  69.692  1.00 21.75           C  
ANISOU 2118  CB  ASN A 293     1186   2642   4432     36   -133   -326       C  
ATOM   2119  CG  ASN A 293      82.953  60.412  70.248  1.00 24.21           C  
ANISOU 2119  CG  ASN A 293     1584   2963   4648     46     15   -506       C  
ATOM   2120  OD1 ASN A 293      83.617  61.448  70.377  1.00 26.92           O  
ANISOU 2120  OD1 ASN A 293     2006   3172   5050   -140     59   -880       O  
ATOM   2121  ND2 ASN A 293      81.653  60.343  70.550  1.00 25.42           N  
ANISOU 2121  ND2 ASN A 293     1550   3394   4714     86    270   -496       N  
ATOM   2122  N   GLY A 294      86.194  58.129  67.314  1.00 20.24           N  
ANISOU 2122  N   GLY A 294     1088   2422   4177   -124   -130   -277       N  
ATOM   2123  CA  GLY A 294      87.087  57.018  66.994  1.00 19.24           C  
ANISOU 2123  CA  GLY A 294      871   2357   4081   -114    -73   -224       C  
ATOM   2124  C   GLY A 294      86.393  55.696  66.665  1.00 18.50           C  
ANISOU 2124  C   GLY A 294      752   2331   3945    -56     -7   -155       C  
ATOM   2125  O   GLY A 294      87.007  54.629  66.733  1.00 18.69           O  
ANISOU 2125  O   GLY A 294      789   2275   4034    -71     10   -159       O  
ATOM   2126  N   ILE A 295      85.121  55.749  66.284  1.00 17.07           N  
ANISOU 2126  N   ILE A 295      447   2250   3788    -42     40   -109       N  
ATOM   2127  CA  ILE A 295      84.451  54.546  65.791  1.00 15.95           C  
ANISOU 2127  CA  ILE A 295      300   2126   3632     87     38    -91       C  
ATOM   2128  C   ILE A 295      85.068  54.202  64.440  1.00 15.57           C  
ANISOU 2128  C   ILE A 295      299   2073   3541     91     33    -38       C  
ATOM   2129  O   ILE A 295      85.710  55.048  63.799  1.00 15.56           O  
ANISOU 2129  O   ILE A 295      370   2005   3533     58     73    -45       O  
ATOM   2130  CB  ILE A 295      82.908  54.701  65.626  1.00 16.53           C  
ANISOU 2130  CB  ILE A 295      368   2263   3647    192     68    -85       C  
ATOM   2131  CG1 ILE A 295      82.563  55.838  64.656  1.00 16.46           C  
ANISOU 2131  CG1 ILE A 295      338   2308   3605    255   -184    -86       C  
ATOM   2132  CG2 ILE A 295      82.231  54.902  66.988  1.00 15.68           C  
ANISOU 2132  CG2 ILE A 295      329   2091   3538     36    307     85       C  
ATOM   2133  CD1 ILE A 295      81.094  55.793  64.227  1.00 18.30           C  
ANISOU 2133  CD1 ILE A 295      441   2767   3746    593   -161   -407       C  
ATOM   2134  N   ASN A 296      84.900  52.944  64.045  1.00 14.98           N  
ANISOU 2134  N   ASN A 296      293   1979   3417    -18    -10    -39       N  
ATOM   2135  CA  ASN A 296      85.370  52.448  62.753  1.00 14.52           C  
ANISOU 2135  CA  ASN A 296      293   2027   3197    -14    -59     36       C  
ATOM   2136  C   ASN A 296      86.871  52.649  62.587  1.00 14.73           C  
ANISOU 2136  C   ASN A 296      298   1972   3327    -52   -115     24       C  
ATOM   2137  O   ASN A 296      87.368  52.825  61.473  1.00 14.45           O  
ANISOU 2137  O   ASN A 296      295   2073   3121    -43    -98    122       O  
ATOM   2138  CB  ASN A 296      84.594  53.145  61.630  1.00 14.75           C  
ANISOU 2138  CB  ASN A 296      299   2024   3280     57   -129     90       C  
ATOM   2139  CG  ASN A 296      83.086  52.889  61.730  1.00 14.39           C  
ANISOU 2139  CG  ASN A 296      380   2028   3059     72    -12     26       C  
ATOM   2140  OD1 ASN A 296      82.654  51.805  62.138  1.00 14.10           O  
ANISOU 2140  OD1 ASN A 296      784   2143   2431    192    -56    198       O  
ATOM   2141  ND2 ASN A 296      82.288  53.888  61.371  1.00 14.65           N  
ANISOU 2141  ND2 ASN A 296      355   2185   3026    290   -202     61       N  
ATOM   2142  N   SER A 297      87.595  52.593  63.700  1.00 14.84           N  
ANISOU 2142  N   SER A 297      306   1922   3407    -80   -169     82       N  
ATOM   2143  CA  SER A 297      89.017  52.955  63.690  1.00 16.07           C  
ANISOU 2143  CA  SER A 297      368   2011   3726    -37   -228     78       C  
ATOM   2144  C   SER A 297      89.855  52.025  64.547  1.00 16.44           C  
ANISOU 2144  C   SER A 297      365   2020   3861    -34   -202    120       C  
ATOM   2145  O   SER A 297      89.346  51.401  65.481  1.00 17.12           O  
ANISOU 2145  O   SER A 297      316   2127   4060   -129    -44    200       O  
ATOM   2146  CB  SER A 297      89.224  54.389  64.216  1.00 15.76           C  
ANISOU 2146  CB  SER A 297      364   1889   3733    -54   -266    176       C  
ATOM   2147  OG  SER A 297      88.409  55.297  63.500  1.00 16.46           O  
ANISOU 2147  OG  SER A 297      491   2077   3683     48   -375     48       O  
ATOM   2148  N   ALA A 298      91.150  52.019  64.249  1.00 16.81           N  
ANISOU 2148  N   ALA A 298      428   2058   3899    -64   -171    -62       N  
ATOM   2149  CA  ALA A 298      92.176  51.395  65.075  1.00 17.24           C  
ANISOU 2149  CA  ALA A 298      316   2099   4134   -113   -234    -65       C  
ATOM   2150  C   ALA A 298      93.412  52.297  64.962  1.00 18.28           C  
ANISOU 2150  C   ALA A 298      460   2307   4178   -185   -101    -15       C  
ATOM   2151  O   ALA A 298      93.374  53.314  64.254  1.00 18.70           O  
ANISOU 2151  O   ALA A 298      565   2304   4236   -134    -83    -13       O  
ATOM   2152  CB  ALA A 298      92.479  49.985  64.581  1.00 17.39           C  
ANISOU 2152  CB  ALA A 298      340   2057   4209   -144   -353   -138       C  
ATOM   2153  N   ILE A 299      94.484  51.950  65.670  1.00 17.93           N  
ANISOU 2153  N   ILE A 299      327   2363   4123   -233   -137    -57       N  
ATOM   2154  CA  ILE A 299      95.682  52.803  65.714  1.00 18.29           C  
ANISOU 2154  CA  ILE A 299      338   2528   4081   -243    -36   -116       C  
ATOM   2155  C   ILE A 299      96.869  52.023  65.167  1.00 18.84           C  
ANISOU 2155  C   ILE A 299      324   2579   4252   -163    -36    -62       C  
ATOM   2156  O   ILE A 299      97.135  50.902  65.616  1.00 19.81           O  
ANISOU 2156  O   ILE A 299      338   2779   4410    -71    -19     58       O  
ATOM   2157  CB  ILE A 299      96.031  53.289  67.156  1.00 17.99           C  
ANISOU 2157  CB  ILE A 299      344   2459   4031   -306    -96   -110       C  
ATOM   2158  CG1 ILE A 299      94.830  53.984  67.806  1.00 16.91           C  
ANISOU 2158  CG1 ILE A 299      397   2748   3278   -183   -111   -265       C  
ATOM   2159  CG2 ILE A 299      97.326  54.175  67.161  1.00 18.18           C  
ANISOU 2159  CG2 ILE A 299      412   2476   4018   -429   -262   -289       C  
ATOM   2160  CD1 ILE A 299      95.011  54.219  69.329  1.00 17.77           C  
ANISOU 2160  CD1 ILE A 299      600   2979   3172    236   -132   -413       C  
ATOM   2161  N   LEU A 300      97.538  52.597  64.170  1.00 18.99           N  
ANISOU 2161  N   LEU A 300      360   2659   4197    -57     43   -124       N  
ATOM   2162  CA  LEU A 300      98.834  52.087  63.743  1.00 19.33           C  
ANISOU 2162  CA  LEU A 300      497   2655   4191    -98    -10   -146       C  
ATOM   2163  C   LEU A 300      99.874  52.829  64.579  1.00 19.45           C  
ANISOU 2163  C   LEU A 300      563   2583   4244   -196    -93   -157       C  
ATOM   2164  O   LEU A 300     100.006  54.054  64.462  1.00 19.17           O  
ANISOU 2164  O   LEU A 300      578   2546   4160   -259   -119    -83       O  
ATOM   2165  CB  LEU A 300      99.070  52.361  62.252  1.00 19.45           C  
ANISOU 2165  CB  LEU A 300      689   2617   4083     74    149   -154       C  
ATOM   2166  CG  LEU A 300     100.390  51.768  61.740  1.00 20.06           C  
ANISOU 2166  CG  LEU A 300      571   2704   4344    -60    111    -85       C  
ATOM   2167  CD1 LEU A 300     100.216  50.251  61.525  1.00 21.32           C  
ANISOU 2167  CD1 LEU A 300      746   2711   4644    516     20   -341       C  
ATOM   2168  CD2 LEU A 300     100.856  52.463  60.462  1.00 21.00           C  
ANISOU 2168  CD2 LEU A 300      918   3197   3864   -114    271   -402       C  
ATOM   2169  N   ARG A 301     100.577  52.099  65.440  1.00 18.79           N  
ANISOU 2169  N   ARG A 301      375   2446   4316   -179   -169   -218       N  
ATOM   2170  CA  ARG A 301     101.480  52.753  66.376  1.00 20.19           C  
ANISOU 2170  CA  ARG A 301      624   2548   4498   -188   -242   -212       C  
ATOM   2171  C   ARG A 301     102.920  52.354  66.106  1.00 21.16           C  
ANISOU 2171  C   ARG A 301      655   2612   4771   -207   -281   -261       C  
ATOM   2172  O   ARG A 301     103.274  51.172  66.204  1.00 22.22           O  
ANISOU 2172  O   ARG A 301      815   2717   4910   -161   -226   -269       O  
ATOM   2173  CB  ARG A 301     101.071  52.480  67.830  1.00 20.57           C  
ANISOU 2173  CB  ARG A 301      757   2619   4439   -145   -285   -233       C  
ATOM   2174  CG  ARG A 301     102.130  52.905  68.864  1.00 20.08           C  
ANISOU 2174  CG  ARG A 301      707   2679   4243     18   -280   -225       C  
ATOM   2175  CD  ARG A 301     101.560  52.900  70.281  1.00 20.58           C  
ANISOU 2175  CD  ARG A 301     1010   2742   4066     17   -284   -181       C  
ATOM   2176  NE  ARG A 301     100.307  53.655  70.400  1.00 20.80           N  
ANISOU 2176  NE  ARG A 301     1014   3414   3474     70   -355   -157       N  
ATOM   2177  CZ  ARG A 301      99.348  53.366  71.275  1.00 21.13           C  
ANISOU 2177  CZ  ARG A 301     1386   3456   3187    182   -413   -202       C  
ATOM   2178  NH1 ARG A 301      99.499  52.331  72.097  1.00 21.14           N  
ANISOU 2178  NH1 ARG A 301     1907   3428   2694   -127   -506   -256       N  
ATOM   2179  NH2 ARG A 301      98.238  54.094  71.329  1.00 21.01           N  
ANISOU 2179  NH2 ARG A 301     1115   3729   3135    191   -595   -195       N  
ATOM   2180  N   TYR A 302     103.750  53.338  65.765  1.00 21.68           N  
ANISOU 2180  N   TYR A 302      599   2702   4936   -305   -322   -317       N  
ATOM   2181  CA  TYR A 302     105.187  53.079  65.644  1.00 22.67           C  
ANISOU 2181  CA  TYR A 302      689   2789   5133   -244   -457   -306       C  
ATOM   2182  C   TYR A 302     105.811  52.907  67.024  1.00 23.60           C  
ANISOU 2182  C   TYR A 302      719   2909   5338   -274   -547   -309       C  
ATOM   2183  O   TYR A 302     105.497  53.668  67.945  1.00 23.92           O  
ANISOU 2183  O   TYR A 302      690   2956   5442   -264   -637   -331       O  
ATOM   2184  CB  TYR A 302     105.895  54.235  64.941  1.00 22.41           C  
ANISOU 2184  CB  TYR A 302      653   2789   5070   -394   -461   -352       C  
ATOM   2185  CG  TYR A 302     105.777  54.251  63.429  1.00 23.17           C  
ANISOU 2185  CG  TYR A 302      859   2809   5136   -362   -234   -319       C  
ATOM   2186  CD1 TYR A 302     104.539  54.401  62.794  1.00 21.82           C  
ANISOU 2186  CD1 TYR A 302      864   2412   5013   -147    -81   -324       C  
ATOM   2187  CD2 TYR A 302     106.923  54.155  62.639  1.00 21.28           C  
ANISOU 2187  CD2 TYR A 302      476   2410   5197   -424   -257   -235       C  
ATOM   2188  CE1 TYR A 302     104.447  54.413  61.403  1.00 21.74           C  
ANISOU 2188  CE1 TYR A 302      868   2336   5056   -205     88   -154       C  
ATOM   2189  CE2 TYR A 302     106.846  54.173  61.258  1.00 22.75           C  
ANISOU 2189  CE2 TYR A 302      967   2382   5296   -493   -124    -95       C  
ATOM   2190  CZ  TYR A 302     105.611  54.303  60.648  1.00 22.52           C  
ANISOU 2190  CZ  TYR A 302      697   2648   5212   -256     80   -239       C  
ATOM   2191  OH  TYR A 302     105.551  54.330  59.272  1.00 22.58           O  
ANISOU 2191  OH  TYR A 302      559   2841   5179   -137    401    -54       O  
ATOM   2192  N   ASP A 303     106.672  51.902  67.164  1.00 24.77           N  
ANISOU 2192  N   ASP A 303      894   2950   5565   -220   -617   -244       N  
ATOM   2193  CA  ASP A 303     107.523  51.782  68.347  1.00 26.37           C  
ANISOU 2193  CA  ASP A 303     1018   3118   5883   -203   -744   -271       C  
ATOM   2194  C   ASP A 303     108.124  53.135  68.727  1.00 26.86           C  
ANISOU 2194  C   ASP A 303     1133   3118   5951   -152   -825   -258       C  
ATOM   2195  O   ASP A 303     108.768  53.790  67.901  1.00 25.37           O  
ANISOU 2195  O   ASP A 303      729   2954   5956   -222   -825   -240       O  
ATOM   2196  CB  ASP A 303     108.680  50.815  68.099  1.00 27.99           C  
ANISOU 2196  CB  ASP A 303     1365   3202   6067    -95   -713   -274       C  
ATOM   2197  CG  ASP A 303     108.252  49.364  67.959  1.00 30.71           C  
ANISOU 2197  CG  ASP A 303     1581   3453   6631    -86   -581   -318       C  
ATOM   2198  OD1 ASP A 303     107.046  48.999  68.020  1.00 34.30           O  
ANISOU 2198  OD1 ASP A 303     1953   3899   7178    -66   -252   -310       O  
ATOM   2199  OD2 ASP A 303     109.200  48.568  67.787  1.00 34.38           O  
ANISOU 2199  OD2 ASP A 303     2133   3775   7154    235   -139   -150       O  
ATOM   2200  N   GLY A 304     107.948  53.530  69.986  1.00 27.64           N  
ANISOU 2200  N   GLY A 304     1240   3210   6050   -139   -917   -277       N  
ATOM   2201  CA  GLY A 304     108.461  54.819  70.444  1.00 28.02           C  
ANISOU 2201  CA  GLY A 304     1206   3410   6029   -148  -1073   -320       C  
ATOM   2202  C   GLY A 304     107.415  55.921  70.438  1.00 29.17           C  
ANISOU 2202  C   GLY A 304     1522   3470   6088   -148  -1094   -297       C  
ATOM   2203  O   GLY A 304     107.635  56.962  71.057  1.00 29.52           O  
ANISOU 2203  O   GLY A 304     1531   3508   6177   -216  -1142   -292       O  
ATOM   2204  N   ALA A 305     106.284  55.716  69.759  1.00 29.30           N  
ANISOU 2204  N   ALA A 305     1452   3549   6131   -201  -1066   -243       N  
ATOM   2205  CA  ALA A 305     105.222  56.726  69.792  1.00 29.35           C  
ANISOU 2205  CA  ALA A 305     1495   3599   6056   -168  -1015   -286       C  
ATOM   2206  C   ALA A 305     104.550  56.678  71.160  1.00 30.04           C  
ANISOU 2206  C   ALA A 305     1694   3667   6049   -174  -1005   -265       C  
ATOM   2207  O   ALA A 305     104.582  55.648  71.834  1.00 30.36           O  
ANISOU 2207  O   ALA A 305     1669   3769   6096   -134  -1010   -238       O  
ATOM   2208  CB  ALA A 305     104.190  56.505  68.678  1.00 29.43           C  
ANISOU 2208  CB  ALA A 305     1630   3526   6025   -107  -1005   -276       C  
ATOM   2209  N   ALA A 306     103.934  57.785  71.565  1.00 30.49           N  
ANISOU 2209  N   ALA A 306     1887   3707   5988   -204   -878   -312       N  
ATOM   2210  CA  ALA A 306     103.212  57.831  72.834  1.00 30.80           C  
ANISOU 2210  CA  ALA A 306     2003   3770   5929   -237   -860   -265       C  
ATOM   2211  C   ALA A 306     102.037  56.860  72.838  1.00 30.26           C  
ANISOU 2211  C   ALA A 306     1910   3768   5819   -309   -892   -279       C  
ATOM   2212  O   ALA A 306     101.464  56.540  71.790  1.00 29.61           O  
ANISOU 2212  O   ALA A 306     1746   3768   5737   -332   -856   -304       O  
ATOM   2213  CB  ALA A 306     102.719  59.251  73.133  1.00 31.37           C  
ANISOU 2213  CB  ALA A 306     2227   3769   5921   -281   -807   -320       C  
ATOM   2214  N   VAL A 307     101.675  56.402  74.032  1.00 30.50           N  
ANISOU 2214  N   VAL A 307     1946   3853   5790   -321   -969   -242       N  
ATOM   2215  CA  VAL A 307     100.452  55.619  74.194  1.00 30.56           C  
ANISOU 2215  CA  VAL A 307     1950   3908   5751   -341   -992   -198       C  
ATOM   2216  C   VAL A 307      99.315  56.638  74.215  1.00 30.40           C  
ANISOU 2216  C   VAL A 307     1941   3934   5673   -323   -934   -229       C  
ATOM   2217  O   VAL A 307      98.970  57.193  75.264  1.00 31.03           O  
ANISOU 2217  O   VAL A 307     2112   4040   5636   -384   -921   -254       O  
ATOM   2218  CB  VAL A 307     100.471  54.711  75.449  1.00 30.98           C  
ANISOU 2218  CB  VAL A 307     1931   4032   5807   -318  -1016   -198       C  
ATOM   2219  CG1 VAL A 307      99.158  53.933  75.589  1.00 31.14           C  
ANISOU 2219  CG1 VAL A 307     2193   3828   5809   -535  -1090   -200       C  
ATOM   2220  CG2 VAL A 307     101.654  53.745  75.383  1.00 31.41           C  
ANISOU 2220  CG2 VAL A 307     2192   3978   5763   -115  -1082   -240       C  
ATOM   2221  N   ALA A 308      98.785  56.902  73.022  1.00 29.10           N  
ANISOU 2221  N   ALA A 308     1755   3778   5522   -344   -934   -226       N  
ATOM   2222  CA  ALA A 308      97.808  57.953  72.778  1.00 27.89           C  
ANISOU 2222  CA  ALA A 308     1498   3673   5425   -295   -880   -233       C  
ATOM   2223  C   ALA A 308      97.129  57.690  71.443  1.00 27.25           C  
ANISOU 2223  C   ALA A 308     1446   3568   5337   -250   -761   -200       C  
ATOM   2224  O   ALA A 308      97.640  56.933  70.613  1.00 26.62           O  
ANISOU 2224  O   ALA A 308     1303   3517   5293   -181   -862   -192       O  
ATOM   2225  CB  ALA A 308      98.470  59.334  72.742  1.00 28.34           C  
ANISOU 2225  CB  ALA A 308     1647   3662   5456   -293   -882   -205       C  
ATOM   2226  N   GLU A 309      95.990  58.346  71.237  1.00 26.48           N  
ANISOU 2226  N   GLU A 309     1252   3485   5320   -252   -564   -188       N  
ATOM   2227  CA  GLU A 309      95.303  58.303  69.954  1.00 25.76           C  
ANISOU 2227  CA  GLU A 309     1196   3379   5212   -248   -408   -188       C  
ATOM   2228  C   GLU A 309      96.025  59.213  68.969  1.00 25.30           C  
ANISOU 2228  C   GLU A 309     1143   3180   5289   -255   -400   -189       C  
ATOM   2229  O   GLU A 309      96.657  60.186  69.387  1.00 25.55           O  
ANISOU 2229  O   GLU A 309     1310   3082   5314   -220   -337   -186       O  
ATOM   2230  CB  GLU A 309      93.858  58.793  70.090  1.00 25.69           C  
ANISOU 2230  CB  GLU A 309     1164   3344   5250   -261   -291   -214       C  
ATOM   2231  CG  GLU A 309      93.022  57.947  71.032  1.00 26.85           C  
ANISOU 2231  CG  GLU A 309     1434   3561   5207   -271     85   -234       C  
ATOM   2232  CD  GLU A 309      91.570  58.365  71.057  1.00 29.09           C  
ANISOU 2232  CD  GLU A 309     1537   4234   5282   -428    263    -99       C  
ATOM   2233  OE1 GLU A 309      91.183  59.258  70.267  1.00 29.96           O  
ANISOU 2233  OE1 GLU A 309     1627   4412   5342   -164    456     -7       O  
ATOM   2234  OE2 GLU A 309      90.816  57.795  71.875  1.00 30.15           O  
ANISOU 2234  OE2 GLU A 309     1719   4503   5233   -576    697   -362       O  
ATOM   2235  N   PRO A 310      95.940  58.888  67.667  1.00 25.11           N  
ANISOU 2235  N   PRO A 310     1202   3074   5262   -243   -328   -195       N  
ATOM   2236  CA  PRO A 310      96.286  59.856  66.633  1.00 25.43           C  
ANISOU 2236  CA  PRO A 310     1288   3058   5313   -249   -288   -184       C  
ATOM   2237  C   PRO A 310      95.413  61.102  66.801  1.00 26.56           C  
ANISOU 2237  C   PRO A 310     1503   3140   5447   -214   -272   -176       C  
ATOM   2238  O   PRO A 310      94.309  61.029  67.378  1.00 25.14           O  
ANISOU 2238  O   PRO A 310     1318   2867   5364   -217   -317   -164       O  
ATOM   2239  CB  PRO A 310      95.934  59.141  65.324  1.00 25.21           C  
ANISOU 2239  CB  PRO A 310     1284   3019   5273   -285   -210   -211       C  
ATOM   2240  CG  PRO A 310      95.814  57.695  65.666  1.00 25.02           C  
ANISOU 2240  CG  PRO A 310     1274   3031   5199   -242   -208   -187       C  
ATOM   2241  CD  PRO A 310      95.417  57.626  67.111  1.00 25.06           C  
ANISOU 2241  CD  PRO A 310     1233   3050   5235   -321   -341   -230       C  
ATOM   2242  N   ALA A 311      95.934  62.229  66.317  1.00 27.63           N  
ANISOU 2242  N   ALA A 311     1722   3205   5570   -213   -194   -121       N  
ATOM   2243  CA  ALA A 311      95.257  63.518  66.375  1.00 29.73           C  
ANISOU 2243  CA  ALA A 311     2078   3474   5741   -144   -210   -124       C  
ATOM   2244  C   ALA A 311      93.918  63.439  65.651  1.00 31.23           C  
ANISOU 2244  C   ALA A 311     2330   3710   5826    -55   -182   -107       C  
ATOM   2245  O   ALA A 311      93.789  62.787  64.613  1.00 31.56           O  
ANISOU 2245  O   ALA A 311     2426   3729   5835     46   -120   -178       O  
ATOM   2246  CB  ALA A 311      96.142  64.595  65.749  1.00 30.27           C  
ANISOU 2246  CB  ALA A 311     2304   3403   5793   -120   -207   -103       C  
ATOM   2247  N   THR A 312      92.902  64.080  66.214  1.00 32.50           N  
ANISOU 2247  N   THR A 312     2528   3922   5897     -2   -152   -114       N  
ATOM   2248  CA  THR A 312      91.621  64.169  65.519  1.00 34.07           C  
ANISOU 2248  CA  THR A 312     2736   4232   5976     -5   -157    -43       C  
ATOM   2249  C   THR A 312      91.857  64.888  64.177  1.00 33.48           C  
ANISOU 2249  C   THR A 312     2786   4033   5898    -43   -181     -6       C  
ATOM   2250  O   THR A 312      92.714  65.779  64.067  1.00 34.58           O  
ANISOU 2250  O   THR A 312     3076   4150   5910    -67   -138     59       O  
ATOM   2251  CB  THR A 312      90.539  64.794  66.434  1.00 34.88           C  
ANISOU 2251  CB  THR A 312     2754   4391   6106     31   -163    -64       C  
ATOM   2252  OG1 THR A 312      89.257  64.761  65.787  1.00 38.00           O  
ANISOU 2252  OG1 THR A 312     3004   5189   6245    -59   -120    -32       O  
ATOM   2253  CG2 THR A 312      90.888  66.219  66.797  1.00 37.02           C  
ANISOU 2253  CG2 THR A 312     3040   4626   6401    -56   -265   -274       C  
ATOM   2254  N   ALA A 313      91.176  64.444  63.128  1.00 31.98           N  
ANISOU 2254  N   ALA A 313     2707   3751   5693    -13   -146     43       N  
ATOM   2255  CA  ALA A 313      91.503  64.907  61.785  1.00 30.97           C  
ANISOU 2255  CA  ALA A 313     2591   3597   5579     -2   -108     65       C  
ATOM   2256  C   ALA A 313      90.282  64.796  60.881  1.00 29.91           C  
ANISOU 2256  C   ALA A 313     2493   3438   5432     -4    -61    110       C  
ATOM   2257  O   ALA A 313      89.440  63.913  61.084  1.00 29.82           O  
ANISOU 2257  O   ALA A 313     2575   3333   5419    -30    -66     79       O  
ATOM   2258  CB  ALA A 313      92.646  64.071  61.213  1.00 31.63           C  
ANISOU 2258  CB  ALA A 313     2602   3743   5672     24   -141    142       C  
ATOM   2259  N   ILE A 314      90.173  65.697  59.905  1.00 28.56           N  
ANISOU 2259  N   ILE A 314     2307   3262   5282    -78     16    150       N  
ATOM   2260  CA  ILE A 314      89.250  65.470  58.793  1.00 27.09           C  
ANISOU 2260  CA  ILE A 314     2204   3026   5061      0     53    217       C  
ATOM   2261  C   ILE A 314      89.764  64.239  58.050  1.00 26.67           C  
ANISOU 2261  C   ILE A 314     2181   2970   4981    -11    125    262       C  
ATOM   2262  O   ILE A 314      90.933  64.211  57.640  1.00 26.54           O  
ANISOU 2262  O   ILE A 314     2139   3073   4873    -41     23    285       O  
ATOM   2263  CB  ILE A 314      89.181  66.666  57.821  1.00 27.10           C  
ANISOU 2263  CB  ILE A 314     2245   2965   5085     -4     44    197       C  
ATOM   2264  CG1 ILE A 314      88.724  67.929  58.563  1.00 27.36           C  
ANISOU 2264  CG1 ILE A 314     2374   2949   5072     12    102    228       C  
ATOM   2265  CG2 ILE A 314      88.251  66.342  56.639  1.00 25.32           C  
ANISOU 2265  CG2 ILE A 314     1770   2772   5077    -62    -25    141       C  
ATOM   2266  CD1 ILE A 314      88.569  69.154  57.686  1.00 27.62           C  
ANISOU 2266  CD1 ILE A 314     2642   2565   5286   -223    450    219       C  
ATOM   2267  N   PRO A 315      88.910  63.216  57.877  1.00 25.87           N  
ANISOU 2267  N   PRO A 315     2117   2786   4925     50    264    350       N  
ATOM   2268  CA  PRO A 315      89.405  62.013  57.213  1.00 25.92           C  
ANISOU 2268  CA  PRO A 315     2211   2754   4881     39    330    339       C  
ATOM   2269  C   PRO A 315      90.013  62.347  55.848  1.00 25.82           C  
ANISOU 2269  C   PRO A 315     2300   2695   4814    139    392    366       C  
ATOM   2270  O   PRO A 315      89.411  63.090  55.077  1.00 25.66           O  
ANISOU 2270  O   PRO A 315     2358   2588   4803    262    427    384       O  
ATOM   2271  CB  PRO A 315      88.156  61.137  57.074  1.00 25.74           C  
ANISOU 2271  CB  PRO A 315     2109   2730   4938     18    348    389       C  
ATOM   2272  CG  PRO A 315      87.227  61.634  58.137  1.00 25.62           C  
ANISOU 2272  CG  PRO A 315     2217   2578   4937     -6    321    325       C  
ATOM   2273  CD  PRO A 315      87.481  63.109  58.230  1.00 26.17           C  
ANISOU 2273  CD  PRO A 315     2204   2762   4975    -96    329    389       C  
ATOM   2274  N   PRO A 316      91.204  61.803  55.557  1.00 25.76           N  
ANISOU 2274  N   PRO A 316     2301   2728   4756    160    497    394       N  
ATOM   2275  CA  PRO A 316      91.864  62.092  54.287  1.00 25.80           C  
ANISOU 2275  CA  PRO A 316     2376   2659   4767    117    539    411       C  
ATOM   2276  C   PRO A 316      91.151  61.527  53.063  1.00 25.54           C  
ANISOU 2276  C   PRO A 316     2487   2570   4646     64    599    393       C  
ATOM   2277  O   PRO A 316      90.448  60.521  53.150  1.00 25.52           O  
ANISOU 2277  O   PRO A 316     2544   2571   4580    -63    656    425       O  
ATOM   2278  CB  PRO A 316      93.268  61.494  54.446  1.00 26.45           C  
ANISOU 2278  CB  PRO A 316     2407   2777   4863    208    579    409       C  
ATOM   2279  CG  PRO A 316      93.251  60.633  55.659  1.00 26.97           C  
ANISOU 2279  CG  PRO A 316     2451   2954   4839    132    625    424       C  
ATOM   2280  CD  PRO A 316      91.941  60.836  56.394  1.00 25.96           C  
ANISOU 2280  CD  PRO A 316     2287   2781   4792    217    506    398       C  
ATOM   2281  N   ALA A 317      91.330  62.194  51.929  1.00 25.51           N  
ANISOU 2281  N   ALA A 317     2534   2556   4600     80    582    371       N  
ATOM   2282  CA  ALA A 317      90.703  61.808  50.668  1.00 25.39           C  
ANISOU 2282  CA  ALA A 317     2520   2543   4582    146    622    365       C  
ATOM   2283  C   ALA A 317      91.616  60.823  49.948  1.00 25.31           C  
ANISOU 2283  C   ALA A 317     2484   2601   4530    109    669    350       C  
ATOM   2284  O   ALA A 317      92.826  61.037  49.843  1.00 25.44           O  
ANISOU 2284  O   ALA A 317     2465   2737   4465    102    670    282       O  
ATOM   2285  CB  ALA A 317      90.467  63.048  49.801  1.00 24.84           C  
ANISOU 2285  CB  ALA A 317     2365   2632   4441    152    633    496       C  
ATOM   2286  N   SER A 318      91.023  59.750  49.442  1.00 24.91           N  
ANISOU 2286  N   SER A 318     2487   2438   4536    146    706    315       N  
ATOM   2287  CA  SER A 318      91.755  58.734  48.701  1.00 24.78           C  
ANISOU 2287  CA  SER A 318     2356   2417   4640    174    732    265       C  
ATOM   2288  C   SER A 318      92.044  59.263  47.299  1.00 25.49           C  
ANISOU 2288  C   SER A 318     2511   2483   4689    220    783    243       C  
ATOM   2289  O   SER A 318      91.145  59.797  46.649  1.00 25.82           O  
ANISOU 2289  O   SER A 318     2468   2604   4735    314    765    263       O  
ATOM   2290  CB  SER A 318      90.915  57.459  48.626  1.00 23.85           C  
ANISOU 2290  CB  SER A 318     2176   2266   4618    176    654    242       C  
ATOM   2291  OG  SER A 318      91.473  56.549  47.688  1.00 23.52           O  
ANISOU 2291  OG  SER A 318     1789   2454   4692    150    577    113       O  
ATOM   2292  N   VAL A 319      93.290  59.127  46.848  1.00 26.00           N  
ANISOU 2292  N   VAL A 319     2625   2415   4838    106    841    203       N  
ATOM   2293  CA  VAL A 319      93.678  59.551  45.507  1.00 26.85           C  
ANISOU 2293  CA  VAL A 319     2709   2603   4886    154    940    128       C  
ATOM   2294  C   VAL A 319      93.767  58.367  44.541  1.00 27.04           C  
ANISOU 2294  C   VAL A 319     2659   2723   4890    164    873    202       C  
ATOM   2295  O   VAL A 319      93.546  58.521  43.341  1.00 27.04           O  
ANISOU 2295  O   VAL A 319     2770   2706   4796    272    947    280       O  
ATOM   2296  CB  VAL A 319      95.015  60.310  45.571  1.00 27.62           C  
ANISOU 2296  CB  VAL A 319     2953   2633   4907     41    933    140       C  
ATOM   2297  CG1 VAL A 319      95.610  60.553  44.192  1.00 29.93           C  
ANISOU 2297  CG1 VAL A 319     3099   3170   5102    102   1089    -56       C  
ATOM   2298  CG2 VAL A 319      94.803  61.629  46.278  1.00 28.60           C  
ANISOU 2298  CG2 VAL A 319     3053   2686   5128    157   1028     -4       C  
ATOM   2299  N   THR A 320      94.081  57.186  45.067  1.00 26.49           N  
ANISOU 2299  N   THR A 320     2427   2726   4911    199    837    246       N  
ATOM   2300  CA  THR A 320      94.222  55.996  44.232  1.00 26.47           C  
ANISOU 2300  CA  THR A 320     2313   2883   4860    236    886    266       C  
ATOM   2301  C   THR A 320      93.478  54.825  44.880  1.00 25.58           C  
ANISOU 2301  C   THR A 320     2294   2818   4608    246    880    262       C  
ATOM   2302  O   THR A 320      94.109  53.893  45.398  1.00 25.15           O  
ANISOU 2302  O   THR A 320     2182   2808   4565    306    924    162       O  
ATOM   2303  CB  THR A 320      95.707  55.630  44.067  1.00 27.35           C  
ANISOU 2303  CB  THR A 320     2386   3024   4981    205    823    392       C  
ATOM   2304  OG1 THR A 320      96.284  55.599  45.376  1.00 30.76           O  
ANISOU 2304  OG1 THR A 320     2680   3705   5302    255    656    176       O  
ATOM   2305  CG2 THR A 320      96.451  56.689  43.270  1.00 27.87           C  
ANISOU 2305  CG2 THR A 320     2255   3214   5120    170   1123    372       C  
ATOM   2306  N   PRO A 321      92.134  54.860  44.864  1.00 24.94           N  
ANISOU 2306  N   PRO A 321     2275   2767   4434    201    856    253       N  
ATOM   2307  CA  PRO A 321      91.377  53.748  45.435  1.00 24.77           C  
ANISOU 2307  CA  PRO A 321     2314   2752   4344    130    851    252       C  
ATOM   2308  C   PRO A 321      91.589  52.489  44.599  1.00 25.20           C  
ANISOU 2308  C   PRO A 321     2407   2840   4326     87    813    234       C  
ATOM   2309  O   PRO A 321      91.828  52.598  43.391  1.00 25.83           O  
ANISOU 2309  O   PRO A 321     2600   2862   4349     44    844    146       O  
ATOM   2310  CB  PRO A 321      89.922  54.217  45.344  1.00 24.98           C  
ANISOU 2310  CB  PRO A 321     2348   2779   4361    104    803    332       C  
ATOM   2311  CG  PRO A 321      89.900  55.212  44.223  1.00 25.15           C  
ANISOU 2311  CG  PRO A 321     2314   2810   4430    106    798    298       C  
ATOM   2312  CD  PRO A 321      91.259  55.873  44.240  1.00 24.77           C  
ANISOU 2312  CD  PRO A 321     2209   2769   4431    202    904    325       C  
ATOM   2313  N   LEU A 322      91.537  51.320  45.234  1.00 24.58           N  
ANISOU 2313  N   LEU A 322     2307   2798   4232     95    727    216       N  
ATOM   2314  CA  LEU A 322      91.606  50.061  44.501  1.00 24.29           C  
ANISOU 2314  CA  LEU A 322     2193   2870   4162    119    716    198       C  
ATOM   2315  C   LEU A 322      90.432  49.877  43.539  1.00 24.46           C  
ANISOU 2315  C   LEU A 322     2217   2987   4087     86    657    173       C  
ATOM   2316  O   LEU A 322      89.255  50.005  43.923  1.00 24.04           O  
ANISOU 2316  O   LEU A 322     2055   2985   4094     47    610    191       O  
ATOM   2317  CB  LEU A 322      91.657  48.860  45.457  1.00 24.47           C  
ANISOU 2317  CB  LEU A 322     2251   2853   4193    116    679    164       C  
ATOM   2318  CG  LEU A 322      91.598  47.481  44.782  1.00 22.97           C  
ANISOU 2318  CG  LEU A 322     1986   2780   3959    140    848     63       C  
ATOM   2319  CD1 LEU A 322      92.849  47.204  43.931  1.00 23.87           C  
ANISOU 2319  CD1 LEU A 322     1877   3279   3913    -27    779    -55       C  
ATOM   2320  CD2 LEU A 322      91.427  46.403  45.832  1.00 25.11           C  
ANISOU 2320  CD2 LEU A 322     2545   2743   4251    148    604     -4       C  
ATOM   2321  N   LEU A 323      90.768  49.585  42.287  1.00 24.55           N  
ANISOU 2321  N   LEU A 323     2213   3015   4100     78    671    155       N  
ATOM   2322  CA  LEU A 323      89.809  49.009  41.346  1.00 24.85           C  
ANISOU 2322  CA  LEU A 323     2373   3118   3949     65    634    187       C  
ATOM   2323  C   LEU A 323      90.147  47.544  41.092  1.00 24.90           C  
ANISOU 2323  C   LEU A 323     2361   3167   3929    -36    626    191       C  
ATOM   2324  O   LEU A 323      91.306  47.186  40.877  1.00 25.05           O  
ANISOU 2324  O   LEU A 323     2325   3118   4074    103    661    129       O  
ATOM   2325  CB  LEU A 323      89.843  49.776  40.029  1.00 25.73           C  
ANISOU 2325  CB  LEU A 323     2549   3210   4017     34    622    279       C  
ATOM   2326  CG  LEU A 323      89.528  51.274  40.123  1.00 25.91           C  
ANISOU 2326  CG  LEU A 323     2803   3249   3791    -51    691    322       C  
ATOM   2327  CD1 LEU A 323      89.798  51.900  38.768  1.00 27.89           C  
ANISOU 2327  CD1 LEU A 323     3319   3693   3585   -395    500    358       C  
ATOM   2328  CD2 LEU A 323      88.090  51.534  40.562  1.00 26.00           C  
ANISOU 2328  CD2 LEU A 323     2832   3517   3526   -283    977    351       C  
ATOM   2329  N   GLU A 324      89.138  46.682  41.124  1.00 24.70           N  
ANISOU 2329  N   GLU A 324     2359   3167   3855   -107    582    112       N  
ATOM   2330  CA  GLU A 324      89.362  45.258  40.888  1.00 24.59           C  
ANISOU 2330  CA  GLU A 324     2351   3197   3793    -96    670     61       C  
ATOM   2331  C   GLU A 324      89.955  44.977  39.501  1.00 24.65           C  
ANISOU 2331  C   GLU A 324     2340   3275   3750    -98    659     13       C  
ATOM   2332  O   GLU A 324      90.696  44.011  39.319  1.00 24.36           O  
ANISOU 2332  O   GLU A 324     2194   3370   3689    -36    598    -57       O  
ATOM   2333  CB  GLU A 324      88.039  44.511  41.067  1.00 24.14           C  
ANISOU 2333  CB  GLU A 324     2366   3028   3779   -207    713    104       C  
ATOM   2334  CG  GLU A 324      88.147  42.989  41.071  1.00 24.13           C  
ANISOU 2334  CG  GLU A 324     2337   3006   3822   -162    745     81       C  
ATOM   2335  CD  GLU A 324      86.825  42.366  41.477  1.00 25.25           C  
ANISOU 2335  CD  GLU A 324     2595   2981   4016   -306    793    111       C  
ATOM   2336  OE1 GLU A 324      85.884  42.354  40.654  1.00 24.97           O  
ANISOU 2336  OE1 GLU A 324     2743   2807   3937   -173    750   -117       O  
ATOM   2337  OE2 GLU A 324      86.721  41.914  42.634  1.00 25.55           O  
ANISOU 2337  OE2 GLU A 324     2553   3157   3995   -357    889    128       O  
ATOM   2338  N   THR A 325      89.632  45.824  38.529  1.00 24.66           N  
ANISOU 2338  N   THR A 325     2302   3405   3662    -38    667     16       N  
ATOM   2339  CA  THR A 325      90.169  45.704  37.174  1.00 25.35           C  
ANISOU 2339  CA  THR A 325     2440   3504   3686    -10    705      4       C  
ATOM   2340  C   THR A 325      91.667  46.038  37.103  1.00 25.80           C  
ANISOU 2340  C   THR A 325     2556   3545   3700    -24    835     18       C  
ATOM   2341  O   THR A 325      92.337  45.772  36.094  1.00 26.22           O  
ANISOU 2341  O   THR A 325     2599   3699   3663      0    842    -64       O  
ATOM   2342  CB  THR A 325      89.390  46.621  36.217  1.00 25.43           C  
ANISOU 2342  CB  THR A 325     2483   3466   3712    -31    662     15       C  
ATOM   2343  OG1 THR A 325      89.354  47.933  36.781  1.00 25.74           O  
ANISOU 2343  OG1 THR A 325     2298   3464   4017    199    513     40       O  
ATOM   2344  CG2 THR A 325      87.950  46.143  36.061  1.00 24.42           C  
ANISOU 2344  CG2 THR A 325     2383   3484   3412    -62    666     16       C  
ATOM   2345  N   ASP A 326      92.201  46.629  38.169  1.00 25.84           N  
ANISOU 2345  N   ASP A 326     2660   3485   3671    -19    944      0       N  
ATOM   2346  CA  ASP A 326      93.641  46.879  38.247  1.00 26.68           C  
ANISOU 2346  CA  ASP A 326     2844   3476   3816    -23    971     36       C  
ATOM   2347  C   ASP A 326      94.447  45.720  38.817  1.00 26.91           C  
ANISOU 2347  C   ASP A 326     2869   3470   3883     78   1050    -20       C  
ATOM   2348  O   ASP A 326      95.678  45.790  38.865  1.00 27.09           O  
ANISOU 2348  O   ASP A 326     2912   3493   3884    -66   1070    -38       O  
ATOM   2349  CB  ASP A 326      93.923  48.134  39.069  1.00 27.10           C  
ANISOU 2349  CB  ASP A 326     2918   3478   3899    -51    942     13       C  
ATOM   2350  CG  ASP A 326      93.572  49.407  38.328  1.00 29.31           C  
ANISOU 2350  CG  ASP A 326     3250   3618   4267    -30    907     88       C  
ATOM   2351  OD1 ASP A 326      93.569  49.400  37.078  1.00 31.24           O  
ANISOU 2351  OD1 ASP A 326     3897   3486   4485   -311   1024    363       O  
ATOM   2352  OD2 ASP A 326      93.309  50.424  39.007  1.00 31.73           O  
ANISOU 2352  OD2 ASP A 326     3161   3839   5055     70    762    -73       O  
ATOM   2353  N   LEU A 327      93.763  44.681  39.291  1.00 26.64           N  
ANISOU 2353  N   LEU A 327     2905   3363   3852    167   1085    -11       N  
ATOM   2354  CA  LEU A 327      94.461  43.512  39.833  1.00 26.71           C  
ANISOU 2354  CA  LEU A 327     2856   3395   3897    317   1140    -39       C  
ATOM   2355  C   LEU A 327      94.664  42.464  38.746  1.00 27.36           C  
ANISOU 2355  C   LEU A 327     2922   3416   4057    388   1159    -57       C  
ATOM   2356  O   LEU A 327      93.743  42.206  37.974  1.00 26.67           O  
ANISOU 2356  O   LEU A 327     2776   3312   4043    466   1110   -122       O  
ATOM   2357  CB  LEU A 327      93.679  42.909  41.002  1.00 26.79           C  
ANISOU 2357  CB  LEU A 327     3009   3345   3824    365   1026     24       C  
ATOM   2358  CG  LEU A 327      93.524  43.825  42.214  1.00 26.62           C  
ANISOU 2358  CG  LEU A 327     3015   3398   3702    450   1127     52       C  
ATOM   2359  CD1 LEU A 327      92.623  43.195  43.272  1.00 26.93           C  
ANISOU 2359  CD1 LEU A 327     3352   3542   3338    568   1270     83       C  
ATOM   2360  CD2 LEU A 327      94.879  44.220  42.796  1.00 26.28           C  
ANISOU 2360  CD2 LEU A 327     3011   3172   3801    617   1066    -76       C  
ATOM   2361  N   HIS A 328      95.861  41.872  38.690  1.00 27.47           N  
ANISOU 2361  N   HIS A 328     2831   3517   4087    409   1359    -67       N  
ATOM   2362  CA  HIS A 328      96.178  40.816  37.734  1.00 28.82           C  
ANISOU 2362  CA  HIS A 328     3045   3604   4299    426   1398    -81       C  
ATOM   2363  C   HIS A 328      96.958  39.687  38.418  1.00 29.16           C  
ANISOU 2363  C   HIS A 328     2986   3700   4392    454   1474   -161       C  
ATOM   2364  O   HIS A 328      97.716  39.936  39.357  1.00 28.73           O  
ANISOU 2364  O   HIS A 328     2955   3566   4394    604   1488   -191       O  
ATOM   2365  CB  HIS A 328      96.951  41.410  36.543  1.00 29.22           C  
ANISOU 2365  CB  HIS A 328     3166   3643   4294    445   1398    -74       C  
ATOM   2366  CG  HIS A 328      96.227  42.545  35.883  1.00 31.77           C  
ANISOU 2366  CG  HIS A 328     3679   3802   4587    458   1249     53       C  
ATOM   2367  ND1 HIS A 328      95.140  42.354  35.057  1.00 33.01           N  
ANISOU 2367  ND1 HIS A 328     3983   3855   4704    442   1038     61       N  
ATOM   2368  CD2 HIS A 328      96.391  43.887  35.983  1.00 33.73           C  
ANISOU 2368  CD2 HIS A 328     4170   3884   4760    406   1092    127       C  
ATOM   2369  CE1 HIS A 328      94.675  43.527  34.663  1.00 33.74           C  
ANISOU 2369  CE1 HIS A 328     4178   4012   4628    448   1101     62       C  
ATOM   2370  NE2 HIS A 328      95.417  44.474  35.209  1.00 33.86           N  
ANISOU 2370  NE2 HIS A 328     4093   3993   4778    410   1164    118       N  
ATOM   2371  N   PRO A 329      96.762  38.435  37.971  1.00 29.74           N  
ANISOU 2371  N   PRO A 329     2996   3781   4522    412   1550   -212       N  
ATOM   2372  CA  PRO A 329      97.489  37.323  38.576  1.00 30.47           C  
ANISOU 2372  CA  PRO A 329     2971   3961   4642    408   1519   -247       C  
ATOM   2373  C   PRO A 329      98.999  37.518  38.456  1.00 31.77           C  
ANISOU 2373  C   PRO A 329     3128   4136   4804    361   1593   -287       C  
ATOM   2374  O   PRO A 329      99.465  37.977  37.409  1.00 31.05           O  
ANISOU 2374  O   PRO A 329     2993   4110   4694    172   1724   -273       O  
ATOM   2375  CB  PRO A 329      97.071  36.122  37.718  1.00 31.28           C  
ANISOU 2375  CB  PRO A 329     3130   3980   4775    459   1441   -251       C  
ATOM   2376  CG  PRO A 329      95.749  36.507  37.127  1.00 30.65           C  
ANISOU 2376  CG  PRO A 329     3044   3912   4689    441   1401   -241       C  
ATOM   2377  CD  PRO A 329      95.881  37.988  36.877  1.00 29.67           C  
ANISOU 2377  CD  PRO A 329     2967   3802   4502    426   1472   -172       C  
ATOM   2378  N   LEU A 330      99.722  37.170  39.518  1.00 32.50           N  
ANISOU 2378  N   LEU A 330     3142   4320   4886    398   1514   -404       N  
ATOM   2379  CA  LEU A 330     101.181  37.234  39.534  1.00 34.75           C  
ANISOU 2379  CA  LEU A 330     3447   4602   5154    434   1465   -404       C  
ATOM   2380  C   LEU A 330     101.766  36.373  38.427  1.00 36.68           C  
ANISOU 2380  C   LEU A 330     3753   4871   5312    531   1446   -467       C  
ATOM   2381  O   LEU A 330     102.688  36.809  37.733  1.00 37.10           O  
ANISOU 2381  O   LEU A 330     3813   4961   5320    510   1469   -466       O  
ATOM   2382  CB  LEU A 330     101.749  36.794  40.887  1.00 34.28           C  
ANISOU 2382  CB  LEU A 330     3276   4540   5206    353   1400   -380       C  
ATOM   2383  CG  LEU A 330     103.278  36.741  41.027  1.00 33.84           C  
ANISOU 2383  CG  LEU A 330     3226   4414   5217    474   1445   -314       C  
ATOM   2384  CD1 LEU A 330     103.899  38.103  40.740  1.00 33.46           C  
ANISOU 2384  CD1 LEU A 330     2643   4845   5224    142   1576   -162       C  
ATOM   2385  CD2 LEU A 330     103.635  36.295  42.436  1.00 33.54           C  
ANISOU 2385  CD2 LEU A 330     2914   4382   5446    532   1291   -187       C  
ATOM   2386  N   VAL A 331     101.246  35.157  38.283  1.00 38.82           N  
ANISOU 2386  N   VAL A 331     4112   5126   5511    562   1373   -562       N  
ATOM   2387  CA  VAL A 331     101.732  34.236  37.249  1.00 41.40           C  
ANISOU 2387  CA  VAL A 331     4541   5476   5712    636   1392   -650       C  
ATOM   2388  C   VAL A 331     100.727  34.208  36.105  1.00 42.43           C  
ANISOU 2388  C   VAL A 331     4665   5675   5781    602   1387   -711       C  
ATOM   2389  O   VAL A 331      99.518  34.228  36.345  1.00 42.52           O  
ANISOU 2389  O   VAL A 331     4731   5646   5779    670   1390   -771       O  
ATOM   2390  CB  VAL A 331     101.992  32.788  37.761  1.00 41.56           C  
ANISOU 2390  CB  VAL A 331     4558   5482   5752    649   1379   -650       C  
ATOM   2391  CG1 VAL A 331     103.072  32.762  38.843  1.00 43.23           C  
ANISOU 2391  CG1 VAL A 331     4853   5598   5974    729   1197   -556       C  
ATOM   2392  CG2 VAL A 331     100.723  32.117  38.255  1.00 42.22           C  
ANISOU 2392  CG2 VAL A 331     4696   5479   5866    652   1300   -646       C  
ATOM   2393  N   SER A 332     101.222  34.178  34.870  1.00 44.08           N  
ANISOU 2393  N   SER A 332     4892   5946   5907    587   1429   -724       N  
ATOM   2394  CA  SER A 332     100.342  34.051  33.715  1.00 45.53           C  
ANISOU 2394  CA  SER A 332     5057   6204   6036    572   1387   -762       C  
ATOM   2395  C   SER A 332      99.463  32.836  33.939  1.00 45.93           C  
ANISOU 2395  C   SER A 332     5127   6207   6116    551   1369   -790       C  
ATOM   2396  O   SER A 332      99.946  31.722  34.117  1.00 45.91           O  
ANISOU 2396  O   SER A 332     5017   6252   6174    646   1404   -795       O  
ATOM   2397  CB  SER A 332     101.115  33.897  32.406  1.00 46.30           C  
ANISOU 2397  CB  SER A 332     5250   6311   6027    543   1381   -737       C  
ATOM   2398  OG  SER A 332     100.516  32.879  31.612  1.00 48.33           O  
ANISOU 2398  OG  SER A 332     5556   6698   6109    472   1250   -629       O  
ATOM   2399  N   THR A 333      98.160  33.080  33.972  1.00 46.60           N  
ANISOU 2399  N   THR A 333     5219   6273   6215    519   1313   -825       N  
ATOM   2400  CA  THR A 333      97.180  32.030  34.204  1.00 47.10           C  
ANISOU 2400  CA  THR A 333     5389   6240   6266    424   1233   -837       C  
ATOM   2401  C   THR A 333      96.197  32.113  33.039  1.00 46.94           C  
ANISOU 2401  C   THR A 333     5380   6181   6273    399   1221   -889       C  
ATOM   2402  O   THR A 333      95.668  33.190  32.756  1.00 47.76           O  
ANISOU 2402  O   THR A 333     5462   6226   6459    357   1079   -823       O  
ATOM   2403  CB  THR A 333      96.458  32.257  35.552  1.00 47.35           C  
ANISOU 2403  CB  THR A 333     5437   6286   6265    397   1221   -829       C  
ATOM   2404  OG1 THR A 333      97.430  32.484  36.584  1.00 47.99           O  
ANISOU 2404  OG1 THR A 333     5661   6297   6273    400   1131   -818       O  
ATOM   2405  CG2 THR A 333      95.588  31.063  35.929  1.00 47.95           C  
ANISOU 2405  CG2 THR A 333     5604   6341   6274    354   1140   -797       C  
ATOM   2406  N   PRO A 334      95.960  30.992  32.341  1.00 46.34           N  
ANISOU 2406  N   PRO A 334     5334   6110   6161    400   1273   -936       N  
ATOM   2407  CA  PRO A 334      94.993  31.093  31.248  1.00 45.59           C  
ANISOU 2407  CA  PRO A 334     5267   6038   6016    405   1321   -960       C  
ATOM   2408  C   PRO A 334      93.556  31.234  31.760  1.00 44.46           C  
ANISOU 2408  C   PRO A 334     5193   5920   5780    390   1334   -958       C  
ATOM   2409  O   PRO A 334      93.213  30.702  32.821  1.00 44.45           O  
ANISOU 2409  O   PRO A 334     5086   5981   5820    440   1356   -939       O  
ATOM   2410  CB  PRO A 334      95.189  29.789  30.469  1.00 46.25           C  
ANISOU 2410  CB  PRO A 334     5388   6106   6076    381   1280   -971       C  
ATOM   2411  CG  PRO A 334      95.799  28.830  31.446  1.00 46.57           C  
ANISOU 2411  CG  PRO A 334     5409   6099   6185    418   1259   -947       C  
ATOM   2412  CD  PRO A 334      96.526  29.638  32.493  1.00 46.44           C  
ANISOU 2412  CD  PRO A 334     5330   6106   6209    385   1267   -934       C  
ATOM   2413  N   VAL A 335      92.745  31.992  31.031  1.00 42.76           N  
ANISOU 2413  N   VAL A 335     5104   5714   5426    339   1361  -1013       N  
ATOM   2414  CA  VAL A 335      91.323  32.128  31.335  1.00 41.45           C  
ANISOU 2414  CA  VAL A 335     5111   5474   5162    349   1302  -1087       C  
ATOM   2415  C   VAL A 335      90.611  30.953  30.675  1.00 40.62           C  
ANISOU 2415  C   VAL A 335     5066   5416   4950    308   1343  -1087       C  
ATOM   2416  O   VAL A 335      90.821  30.713  29.489  1.00 39.43           O  
ANISOU 2416  O   VAL A 335     4939   5257   4782    304   1411  -1146       O  
ATOM   2417  CB  VAL A 335      90.764  33.458  30.781  1.00 41.74           C  
ANISOU 2417  CB  VAL A 335     5162   5490   5206    314   1267  -1094       C  
ATOM   2418  CG1 VAL A 335      89.246  33.512  30.897  1.00 40.44           C  
ANISOU 2418  CG1 VAL A 335     4970   5373   5021    450   1239  -1070       C  
ATOM   2419  CG2 VAL A 335      91.392  34.635  31.512  1.00 41.81           C  
ANISOU 2419  CG2 VAL A 335     5247   5385   5250    296   1130  -1015       C  
ATOM   2420  N   PRO A 336      89.790  30.204  31.434  1.00 40.10           N  
ANISOU 2420  N   PRO A 336     5085   5382   4767    296   1374  -1120       N  
ATOM   2421  CA  PRO A 336      89.061  29.097  30.817  1.00 39.94           C  
ANISOU 2421  CA  PRO A 336     5168   5333   4674    259   1376  -1140       C  
ATOM   2422  C   PRO A 336      88.263  29.551  29.596  1.00 39.83           C  
ANISOU 2422  C   PRO A 336     5198   5323   4610    218   1340  -1150       C  
ATOM   2423  O   PRO A 336      87.684  30.640  29.601  1.00 39.31           O  
ANISOU 2423  O   PRO A 336     5182   5271   4484    150   1367  -1164       O  
ATOM   2424  CB  PRO A 336      88.094  28.638  31.915  1.00 40.00           C  
ANISOU 2424  CB  PRO A 336     5184   5333   4680    214   1351  -1119       C  
ATOM   2425  CG  PRO A 336      88.664  29.151  33.195  1.00 40.39           C  
ANISOU 2425  CG  PRO A 336     5164   5427   4753    274   1413  -1126       C  
ATOM   2426  CD  PRO A 336      89.444  30.386  32.857  1.00 40.32           C  
ANISOU 2426  CD  PRO A 336     5150   5389   4779    253   1341  -1113       C  
ATOM   2427  N   GLY A 337      88.239  28.717  28.562  1.00 39.96           N  
ANISOU 2427  N   GLY A 337     5280   5343   4559    258   1320  -1146       N  
ATOM   2428  CA  GLY A 337      87.414  28.968  27.386  1.00 40.37           C  
ANISOU 2428  CA  GLY A 337     5431   5370   4538    263   1237  -1140       C  
ATOM   2429  C   GLY A 337      88.042  29.898  26.370  1.00 40.69           C  
ANISOU 2429  C   GLY A 337     5564   5416   4480    276   1164  -1109       C  
ATOM   2430  O   GLY A 337      89.262  30.093  26.362  1.00 40.85           O  
ANISOU 2430  O   GLY A 337     5564   5448   4509    306   1160  -1088       O  
ATOM   2431  N   SER A 338      87.209  30.460  25.500  1.00 40.73           N  
ANISOU 2431  N   SER A 338     5614   5458   4402    296   1099  -1095       N  
ATOM   2432  CA  SER A 338      87.693  31.379  24.469  1.00 41.12           C  
ANISOU 2432  CA  SER A 338     5742   5504   4376    261   1023  -1058       C  
ATOM   2433  C   SER A 338      87.241  32.820  24.726  1.00 40.65           C  
ANISOU 2433  C   SER A 338     5748   5470   4226    252   1012  -1044       C  
ATOM   2434  O   SER A 338      86.240  33.040  25.420  1.00 39.69           O  
ANISOU 2434  O   SER A 338     5669   5288   4123    269    967  -1109       O  
ATOM   2435  CB  SER A 338      87.308  30.893  23.063  1.00 41.49           C  
ANISOU 2435  CB  SER A 338     5753   5623   4386    216    968   -986       C  
ATOM   2436  OG  SER A 338      85.921  31.053  22.842  1.00 44.09           O  
ANISOU 2436  OG  SER A 338     6004   5860   4888    269    780   -893       O  
ATOM   2437  N   PRO A 339      87.991  33.801  24.189  1.00 40.43           N  
ANISOU 2437  N   PRO A 339     5773   5457   4129    253   1036  -1030       N  
ATOM   2438  CA  PRO A 339      87.755  35.194  24.554  1.00 40.48           C  
ANISOU 2438  CA  PRO A 339     5779   5508   4090    255   1030  -1014       C  
ATOM   2439  C   PRO A 339      86.563  35.834  23.827  1.00 40.61           C  
ANISOU 2439  C   PRO A 339     5823   5553   4054    252    965   -995       C  
ATOM   2440  O   PRO A 339      86.727  36.828  23.120  1.00 40.19           O  
ANISOU 2440  O   PRO A 339     5752   5553   3964    311    971   -944       O  
ATOM   2441  CB  PRO A 339      89.083  35.877  24.202  1.00 40.44           C  
ANISOU 2441  CB  PRO A 339     5748   5480   4134    247   1026  -1082       C  
ATOM   2442  CG  PRO A 339      89.633  35.065  23.068  1.00 40.59           C  
ANISOU 2442  CG  PRO A 339     5767   5552   4102    176   1075  -1043       C  
ATOM   2443  CD  PRO A 339      89.123  33.660  23.249  1.00 40.36           C  
ANISOU 2443  CD  PRO A 339     5806   5422   4106    253   1046  -1024       C  
ATOM   2444  N   VAL A 340      85.378  35.263  24.031  1.00 40.51           N  
ANISOU 2444  N   VAL A 340     5771   5609   4009    266    933  -1014       N  
ATOM   2445  CA  VAL A 340      84.113  35.781  23.518  1.00 40.69           C  
ANISOU 2445  CA  VAL A 340     5805   5642   4012    257    864   -963       C  
ATOM   2446  C   VAL A 340      83.026  35.445  24.545  1.00 40.38           C  
ANISOU 2446  C   VAL A 340     5752   5614   3977    259    850   -971       C  
ATOM   2447  O   VAL A 340      83.143  34.448  25.266  1.00 39.70           O  
ANISOU 2447  O   VAL A 340     5595   5588   3897    279    878   -933       O  
ATOM   2448  CB  VAL A 340      83.779  35.196  22.119  1.00 41.22           C  
ANISOU 2448  CB  VAL A 340     5865   5651   4147    239    791   -960       C  
ATOM   2449  CG1 VAL A 340      83.461  33.706  22.184  1.00 41.39           C  
ANISOU 2449  CG1 VAL A 340     5871   5696   4157    207    782   -926       C  
ATOM   2450  CG2 VAL A 340      82.649  35.972  21.447  1.00 42.11           C  
ANISOU 2450  CG2 VAL A 340     5856   5735   4408    193    682   -923       C  
ATOM   2451  N   ALA A 341      81.991  36.279  24.632  1.00 39.91           N  
ANISOU 2451  N   ALA A 341     5756   5547   3859    277    838   -997       N  
ATOM   2452  CA  ALA A 341      80.856  36.003  25.519  1.00 39.80           C  
ANISOU 2452  CA  ALA A 341     5781   5523   3816    310    791  -1031       C  
ATOM   2453  C   ALA A 341      80.303  34.618  25.199  1.00 39.55           C  
ANISOU 2453  C   ALA A 341     5771   5512   3743    313    733  -1027       C  
ATOM   2454  O   ALA A 341      80.134  34.272  24.028  1.00 39.53           O  
ANISOU 2454  O   ALA A 341     5862   5500   3657    355    697  -1111       O  
ATOM   2455  CB  ALA A 341      79.766  37.061  25.359  1.00 39.75           C  
ANISOU 2455  CB  ALA A 341     5753   5539   3811    310    829  -1010       C  
ATOM   2456  N   GLY A 342      80.049  33.823  26.233  1.00 38.93           N  
ANISOU 2456  N   GLY A 342     5710   5412   3668    339    679  -1026       N  
ATOM   2457  CA  GLY A 342      79.569  32.458  26.053  1.00 38.88           C  
ANISOU 2457  CA  GLY A 342     5751   5365   3655    282    644   -981       C  
ATOM   2458  C   GLY A 342      80.554  31.497  25.411  1.00 38.65           C  
ANISOU 2458  C   GLY A 342     5780   5259   3644    255    605   -971       C  
ATOM   2459  O   GLY A 342      80.167  30.402  24.999  1.00 38.42           O  
ANISOU 2459  O   GLY A 342     5761   5241   3593    174    631   -896       O  
ATOM   2460  N   GLY A 343      81.823  31.892  25.311  1.00 38.25           N  
ANISOU 2460  N   GLY A 343     5748   5122   3664    224    565   -986       N  
ATOM   2461  CA  GLY A 343      82.845  31.030  24.711  1.00 38.18           C  
ANISOU 2461  CA  GLY A 343     5746   5034   3727    216    508   -921       C  
ATOM   2462  C   GLY A 343      83.333  29.968  25.678  1.00 37.88           C  
ANISOU 2462  C   GLY A 343     5724   4869   3799    210    483   -938       C  
ATOM   2463  O   GLY A 343      84.528  29.893  25.981  1.00 38.05           O  
ANISOU 2463  O   GLY A 343     5777   4870   3809    203    513   -864       O  
ATOM   2464  N   VAL A 344      82.396  29.169  26.180  1.00 37.22           N  
ANISOU 2464  N   VAL A 344     5639   4679   3824    195    419  -1011       N  
ATOM   2465  CA  VAL A 344      82.660  28.145  27.192  1.00 36.63           C  
ANISOU 2465  CA  VAL A 344     5587   4556   3772    150    382  -1091       C  
ATOM   2466  C   VAL A 344      81.786  26.920  26.919  1.00 36.60           C  
ANISOU 2466  C   VAL A 344     5559   4549   3796    124    372  -1155       C  
ATOM   2467  O   VAL A 344      80.844  26.996  26.130  1.00 36.24           O  
ANISOU 2467  O   VAL A 344     5533   4527   3708    138    279  -1178       O  
ATOM   2468  CB  VAL A 344      82.398  28.634  28.638  1.00 36.38           C  
ANISOU 2468  CB  VAL A 344     5586   4481   3754    152    361  -1092       C  
ATOM   2469  CG1 VAL A 344      83.464  29.627  29.101  1.00 35.22           C  
ANISOU 2469  CG1 VAL A 344     5467   4402   3513    196    355  -1064       C  
ATOM   2470  CG2 VAL A 344      80.991  29.203  28.777  1.00 35.86           C  
ANISOU 2470  CG2 VAL A 344     5503   4483   3638    113    367  -1029       C  
ATOM   2471  N   ASP A 345      82.084  25.803  27.578  1.00 36.01           N  
ANISOU 2471  N   ASP A 345     5466   4381   3834    171    371  -1234       N  
ATOM   2472  CA  ASP A 345      81.232  24.618  27.461  1.00 36.55           C  
ANISOU 2472  CA  ASP A 345     5501   4448   3935    149    312  -1277       C  
ATOM   2473  C   ASP A 345      79.810  24.866  27.979  1.00 36.24           C  
ANISOU 2473  C   ASP A 345     5421   4386   3961    113    253  -1283       C  
ATOM   2474  O   ASP A 345      78.834  24.447  27.354  1.00 35.73           O  
ANISOU 2474  O   ASP A 345     5420   4335   3821     49    223  -1395       O  
ATOM   2475  CB  ASP A 345      81.851  23.414  28.182  1.00 36.78           C  
ANISOU 2475  CB  ASP A 345     5526   4414   4033    174    296  -1268       C  
ATOM   2476  CG  ASP A 345      83.206  23.022  27.624  1.00 38.32           C  
ANISOU 2476  CG  ASP A 345     5724   4641   4193    287    331  -1306       C  
ATOM   2477  OD1 ASP A 345      83.347  22.953  26.384  1.00 39.59           O  
ANISOU 2477  OD1 ASP A 345     5761   4924   4356    555    521  -1186       O  
ATOM   2478  OD2 ASP A 345      84.132  22.764  28.427  1.00 39.39           O  
ANISOU 2478  OD2 ASP A 345     5660   4828   4477    306    254  -1403       O  
ATOM   2479  N   LYS A 346      79.704  25.552  29.115  1.00 35.21           N  
ANISOU 2479  N   LYS A 346     5280   4246   3853    117    262  -1272       N  
ATOM   2480  CA  LYS A 346      78.424  25.806  29.766  1.00 35.46           C  
ANISOU 2480  CA  LYS A 346     5174   4270   4028     74    178  -1167       C  
ATOM   2481  C   LYS A 346      78.363  27.241  30.310  1.00 34.21           C  
ANISOU 2481  C   LYS A 346     4952   4173   3872    110    148  -1102       C  
ATOM   2482  O   LYS A 346      79.179  27.641  31.140  1.00 34.19           O  
ANISOU 2482  O   LYS A 346     4821   4196   3971    139    204  -1092       O  
ATOM   2483  CB  LYS A 346      78.207  24.780  30.887  1.00 36.06           C  
ANISOU 2483  CB  LYS A 346     5316   4305   4078     45    160  -1168       C  
ATOM   2484  CG  LYS A 346      76.965  24.979  31.753  1.00 37.80           C  
ANISOU 2484  CG  LYS A 346     5357   4622   4383    -96     73  -1194       C  
ATOM   2485  CD  LYS A 346      75.864  23.987  31.409  1.00 43.75           C  
ANISOU 2485  CD  LYS A 346     5914   5525   5182   -498   -430  -1309       C  
ATOM   2486  CE  LYS A 346      75.054  24.454  30.209  1.00 45.95           C  
ANISOU 2486  CE  LYS A 346     6303   5754   5401   -653   -674  -1271       C  
ATOM   2487  NZ  LYS A 346      74.187  23.365  29.648  1.00 48.48           N  
ANISOU 2487  NZ  LYS A 346     6586   5815   6017   -853   -602  -1503       N  
ATOM   2488  N   ALA A 347      77.409  28.022  29.807  1.00 33.15           N  
ANISOU 2488  N   ALA A 347     4687   4095   3815     94     70  -1047       N  
ATOM   2489  CA  ALA A 347      77.223  29.405  30.239  1.00 31.60           C  
ANISOU 2489  CA  ALA A 347     4423   3978   3603    101    -88   -965       C  
ATOM   2490  C   ALA A 347      75.854  29.524  30.904  1.00 30.96           C  
ANISOU 2490  C   ALA A 347     4350   3895   3516    107   -211   -886       C  
ATOM   2491  O   ALA A 347      74.854  29.039  30.369  1.00 31.01           O  
ANISOU 2491  O   ALA A 347     4218   3960   3605    132   -338   -901       O  
ATOM   2492  CB  ALA A 347      77.349  30.364  29.064  1.00 31.46           C  
ANISOU 2492  CB  ALA A 347     4369   3919   3662     97    -52   -994       C  
ATOM   2493  N   LEU A 348      75.829  30.122  32.091  1.00 29.26           N  
ANISOU 2493  N   LEU A 348     4177   3650   3290     98   -321   -815       N  
ATOM   2494  CA  LEU A 348      74.599  30.245  32.863  1.00 28.55           C  
ANISOU 2494  CA  LEU A 348     4094   3599   3154     89   -423   -697       C  
ATOM   2495  C   LEU A 348      74.431  31.686  33.315  1.00 27.86           C  
ANISOU 2495  C   LEU A 348     3948   3583   3052    126   -432   -621       C  
ATOM   2496  O   LEU A 348      75.387  32.303  33.788  1.00 26.70           O  
ANISOU 2496  O   LEU A 348     3752   3414   2977    108   -510   -623       O  
ATOM   2497  CB  LEU A 348      74.633  29.340  34.098  1.00 28.92           C  
ANISOU 2497  CB  LEU A 348     4164   3561   3263     35   -414   -698       C  
ATOM   2498  CG  LEU A 348      74.626  27.827  33.881  1.00 30.72           C  
ANISOU 2498  CG  LEU A 348     4633   3619   3418     22   -532   -618       C  
ATOM   2499  CD1 LEU A 348      74.570  27.166  35.241  1.00 32.13           C  
ANISOU 2499  CD1 LEU A 348     5171   3657   3376     45   -296   -691       C  
ATOM   2500  CD2 LEU A 348      73.417  27.426  33.060  1.00 32.08           C  
ANISOU 2500  CD2 LEU A 348     4945   3807   3434    -94   -695   -728       C  
ATOM   2501  N   ASN A 349      73.214  32.201  33.159  1.00 27.37           N  
ANISOU 2501  N   ASN A 349     3796   3659   2944    139   -442   -535       N  
ATOM   2502  CA  ASN A 349      72.858  33.535  33.636  1.00 27.12           C  
ANISOU 2502  CA  ASN A 349     3652   3722   2927    165   -477   -523       C  
ATOM   2503  C   ASN A 349      71.910  33.436  34.828  1.00 27.16           C  
ANISOU 2503  C   ASN A 349     3596   3790   2931    107   -493   -478       C  
ATOM   2504  O   ASN A 349      70.960  32.648  34.796  1.00 28.10           O  
ANISOU 2504  O   ASN A 349     3741   4037   2897    -78   -504   -508       O  
ATOM   2505  CB  ASN A 349      72.164  34.315  32.520  1.00 26.83           C  
ANISOU 2505  CB  ASN A 349     3625   3682   2884    294   -499   -548       C  
ATOM   2506  CG  ASN A 349      71.995  35.785  32.858  1.00 27.78           C  
ANISOU 2506  CG  ASN A 349     3574   3795   3186    317   -738   -510       C  
ATOM   2507  OD1 ASN A 349      72.962  36.464  33.210  1.00 25.97           O  
ANISOU 2507  OD1 ASN A 349     3527   3926   2412    469  -1051   -330       O  
ATOM   2508  ND2 ASN A 349      70.764  36.284  32.748  1.00 27.41           N  
ANISOU 2508  ND2 ASN A 349     3337   3755   3322    651   -812   -502       N  
ATOM   2509  N   PHE A 350      72.140  34.241  35.861  1.00 26.43           N  
ANISOU 2509  N   PHE A 350     3356   3698   2987    124   -521   -457       N  
ATOM   2510  CA  PHE A 350      71.307  34.182  37.057  1.00 25.94           C  
ANISOU 2510  CA  PHE A 350     3140   3592   3122    190   -477   -320       C  
ATOM   2511  C   PHE A 350      70.462  35.428  37.241  1.00 25.99           C  
ANISOU 2511  C   PHE A 350     3068   3641   3164    207   -527   -294       C  
ATOM   2512  O   PHE A 350      70.982  36.541  37.371  1.00 25.91           O  
ANISOU 2512  O   PHE A 350     2893   3645   3304    187   -553   -316       O  
ATOM   2513  CB  PHE A 350      72.135  33.895  38.311  1.00 25.23           C  
ANISOU 2513  CB  PHE A 350     3095   3464   3027    174   -423   -328       C  
ATOM   2514  CG  PHE A 350      72.823  32.559  38.261  1.00 28.08           C  
ANISOU 2514  CG  PHE A 350     3410   3554   3705    238   -339   -139       C  
ATOM   2515  CD1 PHE A 350      72.113  31.390  38.493  1.00 28.17           C  
ANISOU 2515  CD1 PHE A 350     3714   3311   3675    268   -307   -163       C  
ATOM   2516  CD2 PHE A 350      74.164  32.470  37.924  1.00 30.67           C  
ANISOU 2516  CD2 PHE A 350     3611   3505   4535    352   -197   -231       C  
ATOM   2517  CE1 PHE A 350      72.731  30.147  38.432  1.00 27.71           C  
ANISOU 2517  CE1 PHE A 350     3578   3412   3538    479   -452    -44       C  
ATOM   2518  CE2 PHE A 350      74.799  31.232  37.867  1.00 32.78           C  
ANISOU 2518  CE2 PHE A 350     3985   3559   4910    297   -319     -1       C  
ATOM   2519  CZ  PHE A 350      74.079  30.066  38.126  1.00 30.68           C  
ANISOU 2519  CZ  PHE A 350     3799   3496   4361    123   -282     -4       C  
ATOM   2520  N   VAL A 351      69.152  35.194  37.234  1.00 25.50           N  
ANISOU 2520  N   VAL A 351     2891   3627   3167    255   -521   -249       N  
ATOM   2521  CA  VAL A 351      68.134  36.214  37.415  1.00 25.10           C  
ANISOU 2521  CA  VAL A 351     2807   3611   3118    347   -579   -243       C  
ATOM   2522  C   VAL A 351      67.706  36.253  38.881  1.00 24.93           C  
ANISOU 2522  C   VAL A 351     2573   3609   3287    320   -580   -185       C  
ATOM   2523  O   VAL A 351      67.152  35.291  39.419  1.00 24.87           O  
ANISOU 2523  O   VAL A 351     2416   3651   3382    229   -569   -101       O  
ATOM   2524  CB  VAL A 351      66.942  35.941  36.486  1.00 25.49           C  
ANISOU 2524  CB  VAL A 351     2868   3656   3158    382   -542   -200       C  
ATOM   2525  CG1 VAL A 351      65.858  37.018  36.635  1.00 25.61           C  
ANISOU 2525  CG1 VAL A 351     2953   3837   2939    505   -511   -243       C  
ATOM   2526  CG2 VAL A 351      67.458  35.850  35.054  1.00 25.85           C  
ANISOU 2526  CG2 VAL A 351     3165   3568   3088    359   -587   -299       C  
ATOM   2527  N   PHE A 352      67.987  37.383  39.521  1.00 23.45           N  
ANISOU 2527  N   PHE A 352     2242   3484   3184    274   -670   -304       N  
ATOM   2528  CA  PHE A 352      67.734  37.540  40.944  1.00 23.20           C  
ANISOU 2528  CA  PHE A 352     2108   3476   3229    249   -633   -268       C  
ATOM   2529  C   PHE A 352      66.342  38.133  41.149  1.00 23.53           C  
ANISOU 2529  C   PHE A 352     2133   3485   3320    250   -658   -345       C  
ATOM   2530  O   PHE A 352      65.855  38.899  40.313  1.00 23.72           O  
ANISOU 2530  O   PHE A 352     2218   3547   3245    317   -693   -418       O  
ATOM   2531  CB  PHE A 352      68.772  38.477  41.565  1.00 22.48           C  
ANISOU 2531  CB  PHE A 352     2025   3463   3051    234   -726   -252       C  
ATOM   2532  CG  PHE A 352      70.200  38.021  41.411  1.00 22.37           C  
ANISOU 2532  CG  PHE A 352     2011   3669   2818    192   -737     27       C  
ATOM   2533  CD1 PHE A 352      70.536  36.675  41.436  1.00 22.58           C  
ANISOU 2533  CD1 PHE A 352     1910   3780   2887    222   -543   -182       C  
ATOM   2534  CD2 PHE A 352      71.221  38.961  41.317  1.00 23.76           C  
ANISOU 2534  CD2 PHE A 352     1941   3967   3120    194   -666    279       C  
ATOM   2535  CE1 PHE A 352      71.867  36.261  41.337  1.00 23.58           C  
ANISOU 2535  CE1 PHE A 352     1954   4065   2937    205   -599      3       C  
ATOM   2536  CE2 PHE A 352      72.556  38.564  41.213  1.00 25.11           C  
ANISOU 2536  CE2 PHE A 352     2207   4117   3216    241   -601    179       C  
ATOM   2537  CZ  PHE A 352      72.880  37.210  41.221  1.00 24.84           C  
ANISOU 2537  CZ  PHE A 352     2149   4058   3231    271   -568    160       C  
ATOM   2538  N   ASN A 353      65.720  37.789  42.274  1.00 22.85           N  
ANISOU 2538  N   ASN A 353     1947   3374   3358    199   -587   -444       N  
ATOM   2539  CA  ASN A 353      64.451  38.379  42.655  1.00 23.03           C  
ANISOU 2539  CA  ASN A 353     1897   3312   3541    212   -585   -515       C  
ATOM   2540  C   ASN A 353      64.280  38.263  44.163  1.00 22.85           C  
ANISOU 2540  C   ASN A 353     1809   3216   3654    186   -530   -470       C  
ATOM   2541  O   ASN A 353      65.124  37.655  44.845  1.00 21.85           O  
ANISOU 2541  O   ASN A 353     1571   3101   3630    205   -443   -498       O  
ATOM   2542  CB  ASN A 353      63.292  37.718  41.902  1.00 23.50           C  
ANISOU 2542  CB  ASN A 353     1963   3431   3535    255   -609   -516       C  
ATOM   2543  CG  ASN A 353      62.154  38.679  41.626  1.00 25.22           C  
ANISOU 2543  CG  ASN A 353     2119   3690   3773    250   -729   -687       C  
ATOM   2544  OD1 ASN A 353      61.937  39.648  42.350  1.00 25.48           O  
ANISOU 2544  OD1 ASN A 353     2266   3401   4012    125   -491   -724       O  
ATOM   2545  ND2 ASN A 353      61.424  38.419  40.557  1.00 29.50           N  
ANISOU 2545  ND2 ASN A 353     2797   4485   3927    570  -1129   -676       N  
ATOM   2546  N   PHE A 354      63.209  38.876  44.669  1.00 23.05           N  
ANISOU 2546  N   PHE A 354     1715   3159   3882    124   -480   -463       N  
ATOM   2547  CA  PHE A 354      62.999  39.049  46.102  1.00 23.92           C  
ANISOU 2547  CA  PHE A 354     1745   3264   4076    180   -441   -404       C  
ATOM   2548  C   PHE A 354      61.530  39.388  46.303  1.00 25.24           C  
ANISOU 2548  C   PHE A 354     1799   3392   4397    244   -433   -336       C  
ATOM   2549  O   PHE A 354      60.960  40.143  45.521  1.00 25.94           O  
ANISOU 2549  O   PHE A 354     2143   3437   4275    320   -487   -209       O  
ATOM   2550  CB  PHE A 354      63.852  40.205  46.628  1.00 23.44           C  
ANISOU 2550  CB  PHE A 354     1676   3169   4060    134   -466   -438       C  
ATOM   2551  CG  PHE A 354      63.686  40.489  48.112  1.00 24.13           C  
ANISOU 2551  CG  PHE A 354     1802   3256   4107    111   -487   -467       C  
ATOM   2552  CD1 PHE A 354      64.083  39.560  49.069  1.00 22.77           C  
ANISOU 2552  CD1 PHE A 354     1447   2900   4304      4   -424   -380       C  
ATOM   2553  CD2 PHE A 354      63.201  41.716  48.546  1.00 24.32           C  
ANISOU 2553  CD2 PHE A 354     1823   3237   4180    216   -431   -427       C  
ATOM   2554  CE1 PHE A 354      63.970  39.840  50.443  1.00 23.48           C  
ANISOU 2554  CE1 PHE A 354     1479   3039   4401    223   -562   -435       C  
ATOM   2555  CE2 PHE A 354      63.080  42.012  49.914  1.00 24.55           C  
ANISOU 2555  CE2 PHE A 354     1997   3043   4285    458   -372   -588       C  
ATOM   2556  CZ  PHE A 354      63.454  41.070  50.869  1.00 23.27           C  
ANISOU 2556  CZ  PHE A 354     1540   3123   4176    186   -463   -598       C  
ATOM   2557  N   ASP A 355      60.910  38.847  47.346  1.00 26.03           N  
ANISOU 2557  N   ASP A 355     1771   3463   4653    212   -297   -297       N  
ATOM   2558  CA  ASP A 355      59.481  39.089  47.538  1.00 27.57           C  
ANISOU 2558  CA  ASP A 355     1844   3539   5091    254   -198   -346       C  
ATOM   2559  C   ASP A 355      59.126  39.772  48.862  1.00 28.35           C  
ANISOU 2559  C   ASP A 355     1910   3609   5251    275   -107   -342       C  
ATOM   2560  O   ASP A 355      57.963  39.789  49.257  1.00 29.46           O  
ANISOU 2560  O   ASP A 355     1896   3769   5529    347   -127   -288       O  
ATOM   2561  CB  ASP A 355      58.706  37.784  47.357  1.00 27.73           C  
ANISOU 2561  CB  ASP A 355     1674   3704   5157    188   -136   -336       C  
ATOM   2562  CG  ASP A 355      58.973  36.781  48.477  1.00 27.45           C  
ANISOU 2562  CG  ASP A 355     1517   3592   5317    265   -181   -430       C  
ATOM   2563  OD1 ASP A 355      59.656  37.113  49.478  1.00 27.75           O  
ANISOU 2563  OD1 ASP A 355     1474   3988   5081     43     68   -753       O  
ATOM   2564  OD2 ASP A 355      58.480  35.644  48.354  1.00 28.36           O  
ANISOU 2564  OD2 ASP A 355     1561   3663   5551    -49   -317   -620       O  
ATOM   2565  N   GLY A 356      60.120  40.329  49.547  1.00 28.12           N  
ANISOU 2565  N   GLY A 356     1991   3442   5251    256    -70   -443       N  
ATOM   2566  CA  GLY A 356      59.891  40.974  50.838  1.00 28.45           C  
ANISOU 2566  CA  GLY A 356     2126   3434   5249    252    -61   -460       C  
ATOM   2567  C   GLY A 356      60.340  40.115  52.001  1.00 28.22           C  
ANISOU 2567  C   GLY A 356     2125   3421   5175    261    -65   -542       C  
ATOM   2568  O   GLY A 356      60.612  40.624  53.092  1.00 28.77           O  
ANISOU 2568  O   GLY A 356     2368   3322   5239    315     10   -647       O  
ATOM   2569  N   THR A 357      60.426  38.810  51.757  1.00 26.91           N  
ANISOU 2569  N   THR A 357     1878   3318   5026    355     -9   -576       N  
ATOM   2570  CA  THR A 357      60.801  37.839  52.772  1.00 26.90           C  
ANISOU 2570  CA  THR A 357     1876   3365   4978    304     26   -563       C  
ATOM   2571  C   THR A 357      61.987  36.997  52.290  1.00 25.52           C  
ANISOU 2571  C   THR A 357     1704   3274   4718    216    -14   -558       C  
ATOM   2572  O   THR A 357      63.003  36.872  52.977  1.00 25.97           O  
ANISOU 2572  O   THR A 357     1799   3332   4734    145     67   -615       O  
ATOM   2573  CB  THR A 357      59.609  36.926  53.094  1.00 26.96           C  
ANISOU 2573  CB  THR A 357     1726   3447   5068    371     26   -484       C  
ATOM   2574  OG1 THR A 357      58.492  37.739  53.491  1.00 28.29           O  
ANISOU 2574  OG1 THR A 357     2218   3444   5084    410    121   -647       O  
ATOM   2575  CG2 THR A 357      59.949  35.968  54.230  1.00 29.36           C  
ANISOU 2575  CG2 THR A 357     2217   3581   5358    444     -5   -503       C  
ATOM   2576  N   ASN A 358      61.847  36.432  51.095  1.00 24.64           N  
ANISOU 2576  N   ASN A 358     1693   3169   4500     72    -88   -530       N  
ATOM   2577  CA  ASN A 358      62.860  35.554  50.526  1.00 22.97           C  
ANISOU 2577  CA  ASN A 358     1433   3076   4215    -54   -183   -472       C  
ATOM   2578  C   ASN A 358      63.470  36.062  49.225  1.00 22.34           C  
ANISOU 2578  C   ASN A 358     1395   2998   4095    -76   -296   -510       C  
ATOM   2579  O   ASN A 358      62.782  36.695  48.418  1.00 21.77           O  
ANISOU 2579  O   ASN A 358     1166   3083   4020   -112   -424   -533       O  
ATOM   2580  CB  ASN A 358      62.256  34.163  50.302  1.00 24.16           C  
ANISOU 2580  CB  ASN A 358     1678   3111   4389    -52   -113   -426       C  
ATOM   2581  CG  ASN A 358      61.763  33.536  51.592  1.00 26.88           C  
ANISOU 2581  CG  ASN A 358     2042   3451   4721   -277    -75   -282       C  
ATOM   2582  OD1 ASN A 358      60.596  33.162  51.707  1.00 31.86           O  
ANISOU 2582  OD1 ASN A 358     2479   4159   5468   -303     33   -120       O  
ATOM   2583  ND2 ASN A 358      62.650  33.420  52.574  1.00 29.64           N  
ANISOU 2583  ND2 ASN A 358     2825   3736   4700   -229    -19     33       N  
ATOM   2584  N   PHE A 359      64.762  35.782  49.045  1.00 20.01           N  
ANISOU 2584  N   PHE A 359     1028   2896   3677   -104   -337   -564       N  
ATOM   2585  CA  PHE A 359      65.435  35.968  47.763  1.00 20.03           C  
ANISOU 2585  CA  PHE A 359     1258   2823   3528   -174   -362   -557       C  
ATOM   2586  C   PHE A 359      65.306  34.751  46.855  1.00 21.11           C  
ANISOU 2586  C   PHE A 359     1555   2939   3525   -111   -304   -532       C  
ATOM   2587  O   PHE A 359      65.175  33.617  47.329  1.00 20.98           O  
ANISOU 2587  O   PHE A 359     1678   2793   3498   -156   -207   -576       O  
ATOM   2588  CB  PHE A 359      66.927  36.241  47.995  1.00 19.61           C  
ANISOU 2588  CB  PHE A 359     1242   2821   3386   -124   -392   -608       C  
ATOM   2589  CG  PHE A 359      67.219  37.625  48.496  1.00 18.64           C  
ANISOU 2589  CG  PHE A 359     1135   2881   3067   -166   -536   -664       C  
ATOM   2590  CD1 PHE A 359      67.407  38.676  47.608  1.00 17.02           C  
ANISOU 2590  CD1 PHE A 359      701   2827   2936     69   -722   -724       C  
ATOM   2591  CD2 PHE A 359      67.321  37.872  49.860  1.00 17.98           C  
ANISOU 2591  CD2 PHE A 359     1067   2918   2847     83   -804   -693       C  
ATOM   2592  CE1 PHE A 359      67.689  39.961  48.073  1.00 17.97           C  
ANISOU 2592  CE1 PHE A 359     1191   3008   2626   -215   -716   -782       C  
ATOM   2593  CE2 PHE A 359      67.602  39.144  50.329  1.00 18.67           C  
ANISOU 2593  CE2 PHE A 359     1140   3056   2897      7   -637   -714       C  
ATOM   2594  CZ  PHE A 359      67.789  40.196  49.445  1.00 16.06           C  
ANISOU 2594  CZ  PHE A 359      819   2897   2384     13   -297   -833       C  
ATOM   2595  N   PHE A 360      65.368  34.995  45.547  1.00 21.75           N  
ANISOU 2595  N   PHE A 360     1717   2991   3553   -129   -335   -499       N  
ATOM   2596  CA  PHE A 360      65.201  33.968  44.533  1.00 21.96           C  
ANISOU 2596  CA  PHE A 360     1715   3045   3583    -97   -370   -616       C  
ATOM   2597  C   PHE A 360      66.330  34.063  43.520  1.00 22.19           C  
ANISOU 2597  C   PHE A 360     1806   3063   3561   -172   -406   -556       C  
ATOM   2598  O   PHE A 360      66.805  35.158  43.219  1.00 22.75           O  
ANISOU 2598  O   PHE A 360     1930   3077   3638    -44   -272   -663       O  
ATOM   2599  CB  PHE A 360      63.865  34.134  43.802  1.00 22.54           C  
ANISOU 2599  CB  PHE A 360     1815   3167   3579   -206   -447   -641       C  
ATOM   2600  CG  PHE A 360      62.675  33.916  44.679  1.00 24.78           C  
ANISOU 2600  CG  PHE A 360     2059   3452   3904   -187   -348   -822       C  
ATOM   2601  CD1 PHE A 360      62.247  34.905  45.556  1.00 25.01           C  
ANISOU 2601  CD1 PHE A 360     2228   3346   3926    -42   -500   -879       C  
ATOM   2602  CD2 PHE A 360      62.010  32.693  44.659  1.00 25.79           C  
ANISOU 2602  CD2 PHE A 360     2362   3458   3978   -407   -439  -1038       C  
ATOM   2603  CE1 PHE A 360      61.149  34.681  46.383  1.00 26.66           C  
ANISOU 2603  CE1 PHE A 360     2239   3781   4110   -317   -465  -1035       C  
ATOM   2604  CE2 PHE A 360      60.914  32.460  45.478  1.00 26.85           C  
ANISOU 2604  CE2 PHE A 360     2532   3650   4020   -146   -251  -1050       C  
ATOM   2605  CZ  PHE A 360      60.482  33.455  46.343  1.00 27.93           C  
ANISOU 2605  CZ  PHE A 360     2809   3539   4264   -175   -195  -1137       C  
ATOM   2606  N   ILE A 361      66.764  32.910  43.020  1.00 21.81           N  
ANISOU 2606  N   ILE A 361     1707   3018   3562   -139   -493   -580       N  
ATOM   2607  CA  ILE A 361      67.707  32.844  41.919  1.00 22.51           C  
ANISOU 2607  CA  ILE A 361     1883   3085   3583   -190   -522   -599       C  
ATOM   2608  C   ILE A 361      67.051  31.939  40.884  1.00 24.30           C  
ANISOU 2608  C   ILE A 361     2053   3264   3915   -207   -591   -564       C  
ATOM   2609  O   ILE A 361      66.757  30.770  41.168  1.00 24.76           O  
ANISOU 2609  O   ILE A 361     2119   3291   3996   -397   -624   -572       O  
ATOM   2610  CB  ILE A 361      69.073  32.265  42.363  1.00 22.65           C  
ANISOU 2610  CB  ILE A 361     1862   3132   3611   -209   -427   -652       C  
ATOM   2611  CG1 ILE A 361      69.738  33.164  43.421  1.00 21.31           C  
ANISOU 2611  CG1 ILE A 361     1548   3216   3330   -255   -597   -635       C  
ATOM   2612  CG2 ILE A 361      69.974  32.073  41.151  1.00 22.82           C  
ANISOU 2612  CG2 ILE A 361     2173   2971   3525    -56   -313   -557       C  
ATOM   2613  CD1 ILE A 361      71.110  32.661  43.950  1.00 23.19           C  
ANISOU 2613  CD1 ILE A 361     2079   3138   3594    -78   -783   -815       C  
ATOM   2614  N   ASN A 362      66.843  32.481  39.685  1.00 25.61           N  
ANISOU 2614  N   ASN A 362     2272   3419   4039   -162   -627   -556       N  
ATOM   2615  CA  ASN A 362      66.079  31.799  38.641  1.00 26.77           C  
ANISOU 2615  CA  ASN A 362     2536   3445   4189   -111   -656   -607       C  
ATOM   2616  C   ASN A 362      64.811  31.169  39.222  1.00 27.49           C  
ANISOU 2616  C   ASN A 362     2623   3523   4296    -74   -736   -575       C  
ATOM   2617  O   ASN A 362      64.526  29.988  39.012  1.00 27.36           O  
ANISOU 2617  O   ASN A 362     2743   3365   4286    -54   -820   -598       O  
ATOM   2618  CB  ASN A 362      66.948  30.756  37.928  1.00 27.21           C  
ANISOU 2618  CB  ASN A 362     2630   3519   4190    -65   -562   -579       C  
ATOM   2619  CG  ASN A 362      68.098  31.375  37.162  1.00 27.97           C  
ANISOU 2619  CG  ASN A 362     2791   3490   4344    -79   -445   -638       C  
ATOM   2620  OD1 ASN A 362      68.026  32.527  36.729  1.00 29.48           O  
ANISOU 2620  OD1 ASN A 362     3215   3605   4381     10    -74   -625       O  
ATOM   2621  ND2 ASN A 362      69.162  30.601  36.964  1.00 27.54           N  
ANISOU 2621  ND2 ASN A 362     2734   3464   4262   -158   -121   -565       N  
ATOM   2622  N   ASP A 363      64.079  31.985  39.977  1.00 27.74           N  
ANISOU 2622  N   ASP A 363     2670   3603   4266     57   -832   -556       N  
ATOM   2623  CA  ASP A 363      62.763  31.666  40.548  1.00 28.00           C  
ANISOU 2623  CA  ASP A 363     2590   3634   4416    -34   -898   -500       C  
ATOM   2624  C   ASP A 363      62.702  30.602  41.639  1.00 27.64           C  
ANISOU 2624  C   ASP A 363     2462   3596   4443    -29   -865   -543       C  
ATOM   2625  O   ASP A 363      61.611  30.095  41.952  1.00 27.69           O  
ANISOU 2625  O   ASP A 363     2381   3551   4585   -129   -794   -513       O  
ATOM   2626  CB  ASP A 363      61.735  31.382  39.448  1.00 28.99           C  
ANISOU 2626  CB  ASP A 363     2806   3836   4372     55   -971   -494       C  
ATOM   2627  CG  ASP A 363      61.449  32.614  38.606  1.00 32.93           C  
ANISOU 2627  CG  ASP A 363     3568   4267   4675     96  -1055   -374       C  
ATOM   2628  OD1 ASP A 363      61.025  33.655  39.165  1.00 34.01           O  
ANISOU 2628  OD1 ASP A 363     3909   4244   4766     24  -1722   -482       O  
ATOM   2629  OD2 ASP A 363      61.645  32.531  37.374  1.00 38.70           O  
ANISOU 2629  OD2 ASP A 363     4625   5221   4857    248   -873   -177       O  
ATOM   2630  N   ALA A 364      63.861  30.301  42.227  1.00 25.92           N  
ANISOU 2630  N   ALA A 364     2234   3267   4345     33   -842   -624       N  
ATOM   2631  CA  ALA A 364      63.955  29.327  43.302  1.00 25.24           C  
ANISOU 2631  CA  ALA A 364     2161   3106   4321      8   -808   -673       C  
ATOM   2632  C   ALA A 364      64.622  29.978  44.509  1.00 25.21           C  
ANISOU 2632  C   ALA A 364     2145   3073   4358     10   -731   -661       C  
ATOM   2633  O   ALA A 364      65.647  30.654  44.376  1.00 24.81           O  
ANISOU 2633  O   ALA A 364     2101   3024   4299   -128   -755   -680       O  
ATOM   2634  CB  ALA A 364      64.777  28.099  42.850  1.00 24.68           C  
ANISOU 2634  CB  ALA A 364     2144   2991   4239     34   -768   -706       C  
ATOM   2635  N   THR A 365      64.047  29.758  45.686  1.00 25.35           N  
ANISOU 2635  N   THR A 365     2107   3078   4447     13   -674   -586       N  
ATOM   2636  CA  THR A 365      64.666  30.234  46.916  1.00 24.98           C  
ANISOU 2636  CA  THR A 365     2049   2984   4455     49   -607   -553       C  
ATOM   2637  C   THR A 365      65.276  29.038  47.654  1.00 24.98           C  
ANISOU 2637  C   THR A 365     1985   2961   4544     15   -533   -528       C  
ATOM   2638  O   THR A 365      64.678  27.966  47.716  1.00 25.34           O  
ANISOU 2638  O   THR A 365     2035   3024   4567     17   -479   -579       O  
ATOM   2639  CB  THR A 365      63.674  31.069  47.786  1.00 25.19           C  
ANISOU 2639  CB  THR A 365     2064   3009   4498     -6   -631   -552       C  
ATOM   2640  OG1 THR A 365      64.364  31.589  48.932  1.00 24.74           O  
ANISOU 2640  OG1 THR A 365     1993   2847   4559    -23   -700   -402       O  
ATOM   2641  CG2 THR A 365      62.455  30.248  48.226  1.00 25.66           C  
ANISOU 2641  CG2 THR A 365     2035   3281   4432    157   -566   -584       C  
ATOM   2642  N   PHE A 366      66.481  29.195  48.192  1.00 24.65           N  
ANISOU 2642  N   PHE A 366     1830   2876   4660     54   -478   -415       N  
ATOM   2643  CA  PHE A 366      67.106  28.088  48.890  1.00 25.49           C  
ANISOU 2643  CA  PHE A 366     1915   2965   4804      4   -381   -279       C  
ATOM   2644  C   PHE A 366      66.528  27.886  50.288  1.00 26.80           C  
ANISOU 2644  C   PHE A 366     2115   3068   5000      7   -286   -237       C  
ATOM   2645  O   PHE A 366      66.594  28.787  51.123  1.00 27.93           O  
ANISOU 2645  O   PHE A 366     2444   3032   5134     -9   -113   -191       O  
ATOM   2646  CB  PHE A 366      68.628  28.275  48.989  1.00 23.86           C  
ANISOU 2646  CB  PHE A 366     1602   2870   4594     58   -452   -232       C  
ATOM   2647  CG  PHE A 366      69.329  27.063  49.524  1.00 25.21           C  
ANISOU 2647  CG  PHE A 366     1699   3018   4862     -9   -316   -163       C  
ATOM   2648  CD1 PHE A 366      69.594  25.979  48.700  1.00 25.73           C  
ANISOU 2648  CD1 PHE A 366     1943   2831   5000    107   -402    -35       C  
ATOM   2649  CD2 PHE A 366      69.693  26.994  50.862  1.00 26.29           C  
ANISOU 2649  CD2 PHE A 366     2005   3149   4835    321   -130    -49       C  
ATOM   2650  CE1 PHE A 366      70.238  24.849  49.199  1.00 25.97           C  
ANISOU 2650  CE1 PHE A 366     1634   2964   5270    108   -449    -27       C  
ATOM   2651  CE2 PHE A 366      70.338  25.874  51.373  1.00 27.04           C  
ANISOU 2651  CE2 PHE A 366     2257   3045   4968    143     77    178       C  
ATOM   2652  CZ  PHE A 366      70.598  24.794  50.543  1.00 25.61           C  
ANISOU 2652  CZ  PHE A 366     1805   2883   5041    277    -18    122       C  
ATOM   2653  N   THR A 367      65.997  26.700  50.559  1.00 27.89           N  
ANISOU 2653  N   THR A 367     2310   3066   5221     38   -269   -165       N  
ATOM   2654  CA  THR A 367      65.670  26.320  51.931  1.00 29.67           C  
ANISOU 2654  CA  THR A 367     2576   3271   5426     40   -243    -57       C  
ATOM   2655  C   THR A 367      66.460  25.051  52.241  1.00 29.59           C  
ANISOU 2655  C   THR A 367     2643   3161   5436     18   -246    -91       C  
ATOM   2656  O   THR A 367      66.458  24.117  51.436  1.00 30.96           O  
ANISOU 2656  O   THR A 367     2941   3329   5493    152   -315    -65       O  
ATOM   2657  CB  THR A 367      64.157  26.061  52.148  1.00 30.44           C  
ANISOU 2657  CB  THR A 367     2687   3335   5543     22   -235    -87       C  
ATOM   2658  OG1 THR A 367      63.737  24.958  51.338  1.00 33.91           O  
ANISOU 2658  OG1 THR A 367     3278   3780   5825   -254   -190     16       O  
ATOM   2659  CG2 THR A 367      63.336  27.283  51.762  1.00 30.70           C  
ANISOU 2659  CG2 THR A 367     2423   3645   5596    159   -259    189       C  
ATOM   2660  N   PRO A 368      67.128  24.995  53.403  1.00 28.70           N  
ANISOU 2660  N   PRO A 368     2488   3003   5412    -67   -247   -100       N  
ATOM   2661  CA  PRO A 368      67.987  23.837  53.606  1.00 28.40           C  
ANISOU 2661  CA  PRO A 368     2468   2899   5424    -86   -226   -111       C  
ATOM   2662  C   PRO A 368      67.166  22.543  53.614  1.00 27.72           C  
ANISOU 2662  C   PRO A 368     2294   2808   5427    -90   -175   -127       C  
ATOM   2663  O   PRO A 368      66.096  22.503  54.225  1.00 27.66           O  
ANISOU 2663  O   PRO A 368     2305   2693   5510   -126   -148    -70       O  
ATOM   2664  CB  PRO A 368      68.608  24.079  54.984  1.00 28.88           C  
ANISOU 2664  CB  PRO A 368     2502   2989   5479    -10   -280    -96       C  
ATOM   2665  CG  PRO A 368      67.742  25.099  55.641  1.00 30.57           C  
ANISOU 2665  CG  PRO A 368     2862   3226   5525    146   -240   -127       C  
ATOM   2666  CD  PRO A 368      67.182  25.944  54.529  1.00 29.80           C  
ANISOU 2666  CD  PRO A 368     2745   3155   5419     64   -238    -86       C  
ATOM   2667  N   PRO A 369      67.655  21.499  52.930  1.00 26.82           N  
ANISOU 2667  N   PRO A 369     2142   2690   5356   -115   -144   -129       N  
ATOM   2668  CA  PRO A 369      66.921  20.238  52.943  1.00 26.79           C  
ANISOU 2668  CA  PRO A 369     2096   2758   5322   -117   -114   -118       C  
ATOM   2669  C   PRO A 369      67.234  19.451  54.223  1.00 26.92           C  
ANISOU 2669  C   PRO A 369     2147   2791   5290   -134    -72   -121       C  
ATOM   2670  O   PRO A 369      68.307  19.613  54.807  1.00 26.64           O  
ANISOU 2670  O   PRO A 369     2193   2810   5117   -223   -145   -150       O  
ATOM   2671  CB  PRO A 369      67.466  19.525  51.708  1.00 25.92           C  
ANISOU 2671  CB  PRO A 369     1965   2608   5276   -107   -123   -210       C  
ATOM   2672  CG  PRO A 369      68.943  19.999  51.634  1.00 24.98           C  
ANISOU 2672  CG  PRO A 369     1869   2331   5290   -167    -39    -54       C  
ATOM   2673  CD  PRO A 369      68.910  21.424  52.149  1.00 26.35           C  
ANISOU 2673  CD  PRO A 369     2033   2692   5284   -143   -133   -171       C  
ATOM   2674  N   SER A 370      66.318  18.599  54.662  1.00 26.71           N  
ANISOU 2674  N   SER A 370     2026   2852   5269   -152    -16   -168       N  
ATOM   2675  CA  SER A 370      66.598  17.798  55.850  1.00 27.75           C  
ANISOU 2675  CA  SER A 370     2170   3015   5357   -208     29   -191       C  
ATOM   2676  C   SER A 370      67.704  16.760  55.604  1.00 27.32           C  
ANISOU 2676  C   SER A 370     2154   2936   5287   -144     16   -189       C  
ATOM   2677  O   SER A 370      68.426  16.412  56.535  1.00 26.98           O  
ANISOU 2677  O   SER A 370     1889   3109   5251    -77     64   -220       O  
ATOM   2678  CB  SER A 370      65.320  17.129  56.344  1.00 28.93           C  
ANISOU 2678  CB  SER A 370     2502   3097   5391   -422    -70   -193       C  
ATOM   2679  OG  SER A 370      64.923  16.245  55.332  1.00 32.14           O  
ANISOU 2679  OG  SER A 370     2856   3525   5828   -728   -274   -299       O  
ATOM   2680  N   VAL A 371      67.840  16.274  54.369  1.00 25.96           N  
ANISOU 2680  N   VAL A 371     1946   2706   5211   -148     41   -242       N  
ATOM   2681  CA  VAL A 371      68.949  15.381  54.017  1.00 25.74           C  
ANISOU 2681  CA  VAL A 371     2086   2608   5086   -206     21   -267       C  
ATOM   2682  C   VAL A 371      69.986  16.206  53.258  1.00 25.22           C  
ANISOU 2682  C   VAL A 371     1963   2602   5017   -190    -75   -304       C  
ATOM   2683  O   VAL A 371      69.665  16.776  52.212  1.00 25.98           O  
ANISOU 2683  O   VAL A 371     2191   2628   5051   -181    -57   -298       O  
ATOM   2684  CB  VAL A 371      68.474  14.204  53.132  1.00 25.87           C  
ANISOU 2684  CB  VAL A 371     2122   2601   5104   -171     67   -227       C  
ATOM   2685  CG1 VAL A 371      69.658  13.298  52.779  1.00 24.37           C  
ANISOU 2685  CG1 VAL A 371     1808   2548   4900    -98     57   -248       C  
ATOM   2686  CG2 VAL A 371      67.367  13.416  53.826  1.00 26.56           C  
ANISOU 2686  CG2 VAL A 371     2181   2692   5217   -260    -40   -168       C  
ATOM   2687  N   PRO A 372      71.224  16.297  53.778  1.00 24.80           N  
ANISOU 2687  N   PRO A 372     2031   2516   4876   -222   -174   -341       N  
ATOM   2688  CA  PRO A 372      72.196  17.150  53.102  1.00 23.82           C  
ANISOU 2688  CA  PRO A 372     1844   2496   4710   -212   -189   -359       C  
ATOM   2689  C   PRO A 372      72.345  16.769  51.635  1.00 23.49           C  
ANISOU 2689  C   PRO A 372     1908   2396   4622   -170   -220   -364       C  
ATOM   2690  O   PRO A 372      72.264  15.593  51.307  1.00 23.69           O  
ANISOU 2690  O   PRO A 372     2021   2352   4628    -91   -179   -345       O  
ATOM   2691  CB  PRO A 372      73.497  16.857  53.857  1.00 24.47           C  
ANISOU 2691  CB  PRO A 372     1928   2599   4769   -208   -247   -336       C  
ATOM   2692  CG  PRO A 372      73.049  16.471  55.219  1.00 24.12           C  
ANISOU 2692  CG  PRO A 372     1942   2462   4758   -275   -258   -382       C  
ATOM   2693  CD  PRO A 372      71.776  15.694  55.005  1.00 24.39           C  
ANISOU 2693  CD  PRO A 372     1834   2534   4896   -255   -209   -332       C  
ATOM   2694  N   VAL A 373      72.566  17.741  50.759  1.00 23.25           N  
ANISOU 2694  N   VAL A 373     2006   2400   4427    -88   -196   -401       N  
ATOM   2695  CA  VAL A 373      72.678  17.469  49.326  1.00 23.40           C  
ANISOU 2695  CA  VAL A 373     2211   2352   4326    -79   -189   -404       C  
ATOM   2696  C   VAL A 373      73.741  16.399  49.042  1.00 23.65           C  
ANISOU 2696  C   VAL A 373     2219   2394   4371   -137   -188   -405       C  
ATOM   2697  O   VAL A 373      73.510  15.509  48.215  1.00 24.40           O  
ANISOU 2697  O   VAL A 373     2397   2462   4410   -135   -116   -428       O  
ATOM   2698  CB  VAL A 373      73.001  18.755  48.525  1.00 23.13           C  
ANISOU 2698  CB  VAL A 373     2179   2362   4245    -46   -263   -397       C  
ATOM   2699  CG1 VAL A 373      73.092  18.448  47.044  1.00 24.00           C  
ANISOU 2699  CG1 VAL A 373     2590   2443   4086    -21   -186   -251       C  
ATOM   2700  CG2 VAL A 373      71.977  19.862  48.801  1.00 22.72           C  
ANISOU 2700  CG2 VAL A 373     2150   2353   4128     -5   -177   -516       C  
ATOM   2701  N   LEU A 374      74.886  16.458  49.721  1.00 22.93           N  
ANISOU 2701  N   LEU A 374     2068   2312   4331   -175   -228   -384       N  
ATOM   2702  CA  LEU A 374      75.917  15.444  49.504  1.00 23.01           C  
ANISOU 2702  CA  LEU A 374     2058   2253   4431   -164   -259   -379       C  
ATOM   2703  C   LEU A 374      75.380  14.047  49.804  1.00 23.98           C  
ANISOU 2703  C   LEU A 374     2190   2326   4594   -143   -274   -399       C  
ATOM   2704  O   LEU A 374      75.652  13.103  49.059  1.00 24.26           O  
ANISOU 2704  O   LEU A 374     2087   2399   4728    -31   -236   -332       O  
ATOM   2705  CB  LEU A 374      77.186  15.691  50.329  1.00 22.27           C  
ANISOU 2705  CB  LEU A 374     1891   2153   4418   -178   -249   -467       C  
ATOM   2706  CG  LEU A 374      78.323  14.662  50.160  1.00 21.80           C  
ANISOU 2706  CG  LEU A 374     1892   1981   4411   -164   -501   -408       C  
ATOM   2707  CD1 LEU A 374      78.759  14.507  48.700  1.00 21.54           C  
ANISOU 2707  CD1 LEU A 374     1780   1922   4480    135   -373   -620       C  
ATOM   2708  CD2 LEU A 374      79.541  15.034  51.018  1.00 22.26           C  
ANISOU 2708  CD2 LEU A 374     1753   2049   4654   -265   -448   -202       C  
ATOM   2709  N   LEU A 375      74.604  13.924  50.878  1.00 24.42           N  
ANISOU 2709  N   LEU A 375     2187   2375   4716   -149   -271   -317       N  
ATOM   2710  CA  LEU A 375      74.081  12.624  51.267  1.00 25.24           C  
ANISOU 2710  CA  LEU A 375     2357   2357   4874   -171   -308   -383       C  
ATOM   2711  C   LEU A 375      72.997  12.147  50.302  1.00 26.19           C  
ANISOU 2711  C   LEU A 375     2486   2417   5046   -158   -342   -437       C  
ATOM   2712  O   LEU A 375      72.896  10.950  50.014  1.00 26.72           O  
ANISOU 2712  O   LEU A 375     2543   2445   5162   -226   -412   -445       O  
ATOM   2713  CB  LEU A 375      73.575  12.648  52.708  1.00 25.42           C  
ANISOU 2713  CB  LEU A 375     2397   2423   4837   -193   -219   -330       C  
ATOM   2714  CG  LEU A 375      72.986  11.328  53.220  1.00 26.83           C  
ANISOU 2714  CG  LEU A 375     2757   2571   4867    -82    -86   -186       C  
ATOM   2715  CD1 LEU A 375      74.002  10.201  53.134  1.00 26.69           C  
ANISOU 2715  CD1 LEU A 375     2744   2574   4823   -210     54   -178       C  
ATOM   2716  CD2 LEU A 375      72.502  11.530  54.657  1.00 28.66           C  
ANISOU 2716  CD2 LEU A 375     2912   3099   4876     75     98     60       C  
ATOM   2717  N   GLN A 376      72.210  13.083  49.780  1.00 26.16           N  
ANISOU 2717  N   GLN A 376     2434   2381   5123    -75   -389   -525       N  
ATOM   2718  CA  GLN A 376      71.265  12.755  48.711  1.00 27.31           C  
ANISOU 2718  CA  GLN A 376     2704   2431   5239    -53   -386   -665       C  
ATOM   2719  C   GLN A 376      71.976  12.143  47.500  1.00 27.73           C  
ANISOU 2719  C   GLN A 376     2759   2450   5325    -81   -368   -695       C  
ATOM   2720  O   GLN A 376      71.507  11.160  46.928  1.00 27.45           O  
ANISOU 2720  O   GLN A 376     2798   2444   5188   -166   -391   -720       O  
ATOM   2721  CB  GLN A 376      70.507  14.004  48.262  1.00 27.02           C  
ANISOU 2721  CB  GLN A 376     2633   2439   5194     99   -461   -677       C  
ATOM   2722  CG  GLN A 376      69.606  14.645  49.310  1.00 27.12           C  
ANISOU 2722  CG  GLN A 376     2522   2488   5292    123   -349   -707       C  
ATOM   2723  CD  GLN A 376      68.987  15.924  48.776  1.00 27.83           C  
ANISOU 2723  CD  GLN A 376     2429   2673   5472    143   -297   -850       C  
ATOM   2724  OE1 GLN A 376      69.092  17.003  49.380  1.00 28.01           O  
ANISOU 2724  OE1 GLN A 376     2288   2537   5817    -28   -164   -966       O  
ATOM   2725  NE2 GLN A 376      68.358  15.810  47.612  1.00 26.21           N  
ANISOU 2725  NE2 GLN A 376     1903   2729   5325     22   -332   -823       N  
ATOM   2726  N   ILE A 377      73.118  12.720  47.128  1.00 28.48           N  
ANISOU 2726  N   ILE A 377     2891   2469   5459   -130   -310   -702       N  
ATOM   2727  CA  ILE A 377      73.912  12.208  46.011  1.00 29.07           C  
ANISOU 2727  CA  ILE A 377     3004   2446   5594   -174   -321   -809       C  
ATOM   2728  C   ILE A 377      74.521  10.849  46.335  1.00 30.14           C  
ANISOU 2728  C   ILE A 377     3208   2453   5789   -280   -312   -837       C  
ATOM   2729  O   ILE A 377      74.438   9.919  45.525  1.00 30.52           O  
ANISOU 2729  O   ILE A 377     3334   2509   5752   -275   -338   -875       O  
ATOM   2730  CB  ILE A 377      75.026  13.197  45.591  1.00 28.88           C  
ANISOU 2730  CB  ILE A 377     3030   2345   5597   -144   -232   -761       C  
ATOM   2731  CG1 ILE A 377      74.404  14.503  45.079  1.00 28.21           C  
ANISOU 2731  CG1 ILE A 377     2899   2326   5491   -127   -360   -810       C  
ATOM   2732  CG2 ILE A 377      75.993  12.537  44.569  1.00 27.71           C  
ANISOU 2732  CG2 ILE A 377     2786   2136   5607    -23   -260   -809       C  
ATOM   2733  CD1 ILE A 377      75.330  15.709  45.123  1.00 25.43           C  
ANISOU 2733  CD1 ILE A 377     2454   1779   5430     82   -373   -516       C  
ATOM   2734  N   LEU A 378      75.121  10.725  47.516  1.00 31.16           N  
ANISOU 2734  N   LEU A 378     3342   2563   5931   -391   -382   -897       N  
ATOM   2735  CA  LEU A 378      75.737   9.456  47.895  1.00 33.54           C  
ANISOU 2735  CA  LEU A 378     3678   2822   6243   -350   -473   -952       C  
ATOM   2736  C   LEU A 378      74.720   8.315  48.009  1.00 35.87           C  
ANISOU 2736  C   LEU A 378     4051   3056   6521   -438   -454   -956       C  
ATOM   2737  O   LEU A 378      75.048   7.144  47.788  1.00 35.12           O  
ANISOU 2737  O   LEU A 378     3900   2906   6534   -427   -475  -1019       O  
ATOM   2738  CB  LEU A 378      76.573   9.620  49.166  1.00 33.11           C  
ANISOU 2738  CB  LEU A 378     3688   2722   6168   -344   -478   -976       C  
ATOM   2739  CG  LEU A 378      77.717  10.638  49.062  1.00 33.44           C  
ANISOU 2739  CG  LEU A 378     3535   3056   6114   -222   -592  -1037       C  
ATOM   2740  CD1 LEU A 378      78.526  10.704  50.354  1.00 33.00           C  
ANISOU 2740  CD1 LEU A 378     3482   2927   6129   -312   -731  -1541       C  
ATOM   2741  CD2 LEU A 378      78.633  10.403  47.861  1.00 34.67           C  
ANISOU 2741  CD2 LEU A 378     3593   3438   6141   -221   -593  -1107       C  
ATOM   2742  N   SER A 379      73.475   8.670  48.314  1.00 39.03           N  
ANISOU 2742  N   SER A 379     4454   3484   6889   -460   -448   -979       N  
ATOM   2743  CA  SER A 379      72.396   7.699  48.466  1.00 42.00           C  
ANISOU 2743  CA  SER A 379     4905   3803   7249   -664   -445  -1012       C  
ATOM   2744  C   SER A 379      71.797   7.257  47.136  1.00 44.66           C  
ANISOU 2744  C   SER A 379     5297   4164   7506   -691   -486  -1023       C  
ATOM   2745  O   SER A 379      70.941   6.373  47.103  1.00 44.61           O  
ANISOU 2745  O   SER A 379     5336   4110   7501   -831   -504  -1045       O  
ATOM   2746  CB  SER A 379      71.297   8.246  49.379  1.00 41.94           C  
ANISOU 2746  CB  SER A 379     4876   3804   7255   -629   -468  -1005       C  
ATOM   2747  OG  SER A 379      71.757   8.337  50.716  1.00 42.45           O  
ANISOU 2747  OG  SER A 379     4978   3865   7286   -666   -322  -1003       O  
ATOM   2748  N   GLY A 380      72.234   7.876  46.045  1.00 47.33           N  
ANISOU 2748  N   GLY A 380     5707   4497   7779   -742   -458   -979       N  
ATOM   2749  CA  GLY A 380      71.866   7.426  44.708  1.00 50.66           C  
ANISOU 2749  CA  GLY A 380     6215   4971   8061   -720   -518  -1041       C  
ATOM   2750  C   GLY A 380      70.860   8.289  43.970  1.00 52.98           C  
ANISOU 2750  C   GLY A 380     6508   5307   8315   -646   -538  -1021       C  
ATOM   2751  O   GLY A 380      70.022   7.759  43.243  1.00 53.04           O  
ANISOU 2751  O   GLY A 380     6624   5220   8308   -685   -552  -1082       O  
ATOM   2752  N   ALA A 381      70.926   9.608  44.141  1.00 55.15           N  
ANISOU 2752  N   ALA A 381     6841   5597   8513   -622   -515  -1063       N  
ATOM   2753  CA  ALA A 381      70.129  10.499  43.299  1.00 57.39           C  
ANISOU 2753  CA  ALA A 381     7118   5971   8714   -539   -525  -1029       C  
ATOM   2754  C   ALA A 381      70.866  10.756  41.983  1.00 58.98           C  
ANISOU 2754  C   ALA A 381     7316   6248   8845   -521   -503  -1021       C  
ATOM   2755  O   ALA A 381      72.023  11.193  41.984  1.00 59.54           O  
ANISOU 2755  O   ALA A 381     7337   6388   8897   -480   -512   -992       O  
ATOM   2756  CB  ALA A 381      69.795  11.796  44.015  1.00 57.23           C  
ANISOU 2756  CB  ALA A 381     7119   5931   8696   -568   -500  -1044       C  
ATOM   2757  N   GLN A 382      70.184  10.474  40.873  1.00 60.66           N  
ANISOU 2757  N   GLN A 382     7524   6539   8985   -472   -537  -1032       N  
ATOM   2758  CA  GLN A 382      70.797  10.410  39.541  1.00 62.12           C  
ANISOU 2758  CA  GLN A 382     7695   6808   9100   -414   -526  -1039       C  
ATOM   2759  C   GLN A 382      70.872  11.768  38.838  1.00 62.25           C  
ANISOU 2759  C   GLN A 382     7658   6884   9109   -417   -558  -1052       C  
ATOM   2760  O   GLN A 382      71.914  12.131  38.288  1.00 62.61           O  
ANISOU 2760  O   GLN A 382     7686   6959   9143   -412   -536  -1051       O  
ATOM   2761  CB  GLN A 382      70.068   9.395  38.648  1.00 62.60           C  
ANISOU 2761  CB  GLN A 382     7776   6860   9148   -391   -530  -1050       C  
ATOM   2762  CG  GLN A 382      69.912   7.986  39.231  1.00 64.74           C  
ANISOU 2762  CG  GLN A 382     8135   7139   9322   -269   -445   -945       C  
ATOM   2763  CD  GLN A 382      71.237   7.284  39.504  1.00 67.21           C  
ANISOU 2763  CD  GLN A 382     8438   7590   9506    -23   -408   -833       C  
ATOM   2764  OE1 GLN A 382      72.086   7.149  38.619  1.00 68.29           O  
ANISOU 2764  OE1 GLN A 382     8599   7783   9562     56   -304   -856       O  
ATOM   2765  NE2 GLN A 382      71.413   6.821  40.739  1.00 68.30           N  
ANISOU 2765  NE2 GLN A 382     8685   7797   9469      1   -379   -789       N  
ATOM   2766  N   ALA A 383      69.766  12.506  38.857  1.00 62.36           N  
ANISOU 2766  N   ALA A 383     7620   6968   9103   -406   -604  -1086       N  
ATOM   2767  CA  ALA A 383      69.696  13.831  38.245  1.00 62.03           C  
ANISOU 2767  CA  ALA A 383     7531   6990   9045   -430   -650  -1137       C  
ATOM   2768  C   ALA A 383      69.669  14.921  39.311  1.00 61.76           C  
ANISOU 2768  C   ALA A 383     7449   7009   9009   -443   -680  -1163       C  
ATOM   2769  O   ALA A 383      69.187  14.698  40.424  1.00 61.73           O  
ANISOU 2769  O   ALA A 383     7453   7000   9001   -450   -691  -1188       O  
ATOM   2770  CB  ALA A 383      68.467  13.937  37.346  1.00 62.19           C  
ANISOU 2770  CB  ALA A 383     7545   7024   9059   -437   -643  -1126       C  
ATOM   2771  N   ALA A 384      70.188  16.096  38.962  1.00 61.41           N  
ANISOU 2771  N   ALA A 384     7355   7050   8924   -437   -711  -1177       N  
ATOM   2772  CA  ALA A 384      70.112  17.271  39.833  1.00 60.81           C  
ANISOU 2772  CA  ALA A 384     7202   7071   8830   -451   -757  -1171       C  
ATOM   2773  C   ALA A 384      68.673  17.775  39.908  1.00 60.23           C  
ANISOU 2773  C   ALA A 384     7088   7067   8727   -464   -787  -1188       C  
ATOM   2774  O   ALA A 384      68.322  18.579  40.775  1.00 60.33           O  
ANISOU 2774  O   ALA A 384     7116   7074   8730   -444   -771  -1189       O  
ATOM   2775  CB  ALA A 384      71.041  18.366  39.345  1.00 60.90           C  
ANISOU 2775  CB  ALA A 384     7202   7086   8848   -456   -792  -1179       C  
ATOM   2776  N   GLN A 385      67.868  17.288  38.967  1.00 59.46           N  
ANISOU 2776  N   GLN A 385     6905   7058   8628   -505   -801  -1188       N  
ATOM   2777  CA  GLN A 385      66.415  17.435  38.946  1.00 58.52           C  
ANISOU 2777  CA  GLN A 385     6787   7004   8445   -544   -821  -1200       C  
ATOM   2778  C   GLN A 385      65.769  16.809  40.181  1.00 56.65           C  
ANISOU 2778  C   GLN A 385     6537   6732   8255   -520   -835  -1239       C  
ATOM   2779  O   GLN A 385      64.798  17.339  40.726  1.00 56.49           O  
ANISOU 2779  O   GLN A 385     6477   6760   8225   -516   -833  -1234       O  
ATOM   2780  CB  GLN A 385      65.873  16.751  37.686  1.00 59.11           C  
ANISOU 2780  CB  GLN A 385     6866   7107   8485   -589   -852  -1225       C  
ATOM   2781  CG  GLN A 385      64.364  16.818  37.509  1.00 61.42           C  
ANISOU 2781  CG  GLN A 385     7075   7597   8663   -671   -879  -1163       C  
ATOM   2782  CD  GLN A 385      63.962  16.791  36.047  1.00 64.37           C  
ANISOU 2782  CD  GLN A 385     7554   8166   8738   -827   -865  -1113       C  
ATOM   2783  OE1 GLN A 385      64.695  17.284  35.185  1.00 66.20           O  
ANISOU 2783  OE1 GLN A 385     7781   8500   8872   -840   -696  -1051       O  
ATOM   2784  NE2 GLN A 385      62.792  16.223  35.759  1.00 65.13           N  
ANISOU 2784  NE2 GLN A 385     7567   8272   8906   -901   -838  -1116       N  
ATOM   2785  N   ASP A 386      66.326  15.677  40.604  1.00 54.39           N  
ANISOU 2785  N   ASP A 386     6257   6410   7997   -587   -822  -1294       N  
ATOM   2786  CA  ASP A 386      65.806  14.899  41.724  1.00 51.81           C  
ANISOU 2786  CA  ASP A 386     5895   6054   7735   -586   -866  -1387       C  
ATOM   2787  C   ASP A 386      66.300  15.403  43.083  1.00 48.93           C  
ANISOU 2787  C   ASP A 386     5461   5611   7516   -596   -812  -1362       C  
ATOM   2788  O   ASP A 386      65.764  15.007  44.122  1.00 48.40           O  
ANISOU 2788  O   ASP A 386     5407   5528   7453   -633   -852  -1423       O  
ATOM   2789  CB  ASP A 386      66.167  13.420  41.535  1.00 52.45           C  
ANISOU 2789  CB  ASP A 386     5998   6130   7798   -604   -885  -1436       C  
ATOM   2790  CG  ASP A 386      65.566  12.822  40.264  1.00 54.39           C  
ANISOU 2790  CG  ASP A 386     6209   6538   7919   -614   -941  -1519       C  
ATOM   2791  OD1 ASP A 386      64.338  12.970  40.055  1.00 56.24           O  
ANISOU 2791  OD1 ASP A 386     6318   6985   8065   -603  -1148  -1556       O  
ATOM   2792  OD2 ASP A 386      66.319  12.192  39.484  1.00 55.39           O  
ANISOU 2792  OD2 ASP A 386     6323   6760   7961   -646   -878  -1688       O  
ATOM   2793  N   LEU A 387      67.304  16.280  43.072  1.00 45.43           N  
ANISOU 2793  N   LEU A 387     4914   5189   7156   -483   -762  -1309       N  
ATOM   2794  CA  LEU A 387      67.887  16.798  44.306  1.00 41.80           C  
ANISOU 2794  CA  LEU A 387     4357   4635   6891   -441   -672  -1261       C  
ATOM   2795  C   LEU A 387      67.064  17.929  44.935  1.00 40.14           C  
ANISOU 2795  C   LEU A 387     4084   4468   6698   -455   -700  -1190       C  
ATOM   2796  O   LEU A 387      66.467  18.749  44.233  1.00 39.74           O  
ANISOU 2796  O   LEU A 387     4010   4363   6725   -344   -647  -1209       O  
ATOM   2797  CB  LEU A 387      69.349  17.217  44.083  1.00 41.59           C  
ANISOU 2797  CB  LEU A 387     4316   4643   6842   -390   -648  -1257       C  
ATOM   2798  CG  LEU A 387      70.328  16.120  43.645  1.00 40.26           C  
ANISOU 2798  CG  LEU A 387     4151   4448   6695   -369   -584  -1233       C  
ATOM   2799  CD1 LEU A 387      71.653  16.689  43.165  1.00 37.90           C  
ANISOU 2799  CD1 LEU A 387     4094   4068   6237    -39   -383  -1330       C  
ATOM   2800  CD2 LEU A 387      70.576  15.143  44.780  1.00 39.52           C  
ANISOU 2800  CD2 LEU A 387     3797   4470   6745   -248   -446  -1186       C  
ATOM   2801  N   LEU A 388      67.042  17.949  46.265  1.00 37.19           N  
ANISOU 2801  N   LEU A 388     3659   4047   6423   -485   -708  -1181       N  
ATOM   2802  CA  LEU A 388      66.290  18.926  47.044  1.00 35.86           C  
ANISOU 2802  CA  LEU A 388     3477   3905   6242   -523   -781  -1077       C  
ATOM   2803  C   LEU A 388      67.251  19.919  47.702  1.00 34.63           C  
ANISOU 2803  C   LEU A 388     3355   3767   6036   -496   -751  -1090       C  
ATOM   2804  O   LEU A 388      68.332  19.517  48.118  1.00 33.41           O  
ANISOU 2804  O   LEU A 388     3175   3549   5969   -546   -772  -1070       O  
ATOM   2805  CB  LEU A 388      65.450  18.212  48.106  1.00 35.62           C  
ANISOU 2805  CB  LEU A 388     3406   3865   6262   -460   -749  -1073       C  
ATOM   2806  CG  LEU A 388      64.475  17.130  47.624  1.00 36.34           C  
ANISOU 2806  CG  LEU A 388     3471   3948   6386   -617   -822   -933       C  
ATOM   2807  CD1 LEU A 388      63.851  16.406  48.812  1.00 36.72           C  
ANISOU 2807  CD1 LEU A 388     3624   3797   6529   -562   -830   -768       C  
ATOM   2808  CD2 LEU A 388      63.396  17.732  46.729  1.00 38.45           C  
ANISOU 2808  CD2 LEU A 388     3794   4227   6588   -535   -910   -706       C  
ATOM   2809  N   PRO A 389      66.860  21.203  47.820  1.00 33.99           N  
ANISOU 2809  N   PRO A 389     3286   3734   5891   -504   -787  -1021       N  
ATOM   2810  CA  PRO A 389      65.558  21.761  47.436  1.00 33.69           C  
ANISOU 2810  CA  PRO A 389     3280   3746   5772   -472   -793  -1033       C  
ATOM   2811  C   PRO A 389      65.359  21.881  45.925  1.00 33.33           C  
ANISOU 2811  C   PRO A 389     3203   3741   5717   -506   -864  -1047       C  
ATOM   2812  O   PRO A 389      66.269  22.289  45.199  1.00 32.92           O  
ANISOU 2812  O   PRO A 389     3141   3733   5632   -489   -856  -1039       O  
ATOM   2813  CB  PRO A 389      65.571  23.150  48.082  1.00 33.44           C  
ANISOU 2813  CB  PRO A 389     3285   3697   5721   -507   -781  -1078       C  
ATOM   2814  CG  PRO A 389      67.009  23.504  48.188  1.00 33.40           C  
ANISOU 2814  CG  PRO A 389     3231   3724   5734   -432   -750  -1063       C  
ATOM   2815  CD  PRO A 389      67.703  22.209  48.492  1.00 33.85           C  
ANISOU 2815  CD  PRO A 389     3356   3680   5824   -462   -770  -1055       C  
ATOM   2816  N   SER A 390      64.158  21.538  45.473  1.00 32.92           N  
ANISOU 2816  N   SER A 390     3086   3796   5625   -529   -911  -1004       N  
ATOM   2817  CA  SER A 390      63.857  21.495  44.053  1.00 33.38           C  
ANISOU 2817  CA  SER A 390     3124   3908   5647   -517   -955   -954       C  
ATOM   2818  C   SER A 390      64.001  22.866  43.399  1.00 32.56           C  
ANISOU 2818  C   SER A 390     3013   3850   5507   -510   -958   -998       C  
ATOM   2819  O   SER A 390      63.449  23.848  43.899  1.00 33.01           O  
ANISOU 2819  O   SER A 390     3045   3900   5598   -368   -860   -942       O  
ATOM   2820  CB  SER A 390      62.433  20.976  43.856  1.00 33.85           C  
ANISOU 2820  CB  SER A 390     3190   4021   5650   -578  -1039  -1020       C  
ATOM   2821  OG  SER A 390      62.214  20.779  42.477  1.00 38.02           O  
ANISOU 2821  OG  SER A 390     3942   4567   5934   -450  -1056   -911       O  
ATOM   2822  N   GLY A 391      64.732  22.928  42.287  1.00 31.31           N  
ANISOU 2822  N   GLY A 391     2850   3735   5310   -516   -983   -991       N  
ATOM   2823  CA  GLY A 391      64.968  24.195  41.594  1.00 30.58           C  
ANISOU 2823  CA  GLY A 391     2784   3737   5097   -380   -993   -940       C  
ATOM   2824  C   GLY A 391      66.232  24.932  42.016  1.00 30.07           C  
ANISOU 2824  C   GLY A 391     2854   3581   4990   -364   -945   -939       C  
ATOM   2825  O   GLY A 391      66.688  25.829  41.301  1.00 30.09           O  
ANISOU 2825  O   GLY A 391     2861   3611   4958   -269  -1053   -895       O  
ATOM   2826  N   SER A 392      66.804  24.563  43.161  1.00 28.80           N  
ANISOU 2826  N   SER A 392     2697   3427   4817   -198   -934   -907       N  
ATOM   2827  CA  SER A 392      67.981  25.244  43.716  1.00 28.16           C  
ANISOU 2827  CA  SER A 392     2721   3272   4703   -109   -777   -952       C  
ATOM   2828  C   SER A 392      69.297  24.493  43.484  1.00 27.91           C  
ANISOU 2828  C   SER A 392     2785   3179   4638    -41   -761   -924       C  
ATOM   2829  O   SER A 392      70.381  25.032  43.732  1.00 28.17           O  
ANISOU 2829  O   SER A 392     2902   3093   4707     37   -730   -875       O  
ATOM   2830  CB  SER A 392      67.809  25.466  45.224  1.00 28.22           C  
ANISOU 2830  CB  SER A 392     2701   3273   4745    -74   -782   -981       C  
ATOM   2831  OG  SER A 392      66.790  26.409  45.506  1.00 26.42           O  
ANISOU 2831  OG  SER A 392     2170   3224   4643   -140   -737   -916       O  
ATOM   2832  N   VAL A 393      69.199  23.244  43.036  1.00 27.72           N  
ANISOU 2832  N   VAL A 393     2881   3154   4494     42   -643   -921       N  
ATOM   2833  CA  VAL A 393      70.379  22.419  42.783  1.00 27.59           C  
ANISOU 2833  CA  VAL A 393     3009   3087   4387     52   -533   -958       C  
ATOM   2834  C   VAL A 393      70.585  22.263  41.277  1.00 28.42           C  
ANISOU 2834  C   VAL A 393     3199   3231   4367     24   -516  -1008       C  
ATOM   2835  O   VAL A 393      69.726  21.732  40.574  1.00 28.61           O  
ANISOU 2835  O   VAL A 393     3252   3374   4244    -31   -559  -1074       O  
ATOM   2836  CB  VAL A 393      70.303  21.055  43.512  1.00 27.53           C  
ANISOU 2836  CB  VAL A 393     2967   3059   4435    117   -478   -909       C  
ATOM   2837  CG1 VAL A 393      71.644  20.326  43.412  1.00 27.34           C  
ANISOU 2837  CG1 VAL A 393     2839   2904   4644    135   -409   -824       C  
ATOM   2838  CG2 VAL A 393      69.973  21.273  44.986  1.00 27.51           C  
ANISOU 2838  CG2 VAL A 393     3072   2971   4409    -22   -406   -799       C  
ATOM   2839  N   ILE A 394      71.731  22.736  40.795  1.00 28.41           N  
ANISOU 2839  N   ILE A 394     3313   3218   4261     29   -434  -1058       N  
ATOM   2840  CA  ILE A 394      71.987  22.873  39.366  1.00 28.89           C  
ANISOU 2840  CA  ILE A 394     3521   3277   4180     61   -425  -1085       C  
ATOM   2841  C   ILE A 394      73.176  21.990  39.008  1.00 29.55           C  
ANISOU 2841  C   ILE A 394     3684   3335   4207     98   -351  -1175       C  
ATOM   2842  O   ILE A 394      74.255  22.127  39.602  1.00 28.93           O  
ANISOU 2842  O   ILE A 394     3623   3304   4063     99   -393  -1214       O  
ATOM   2843  CB  ILE A 394      72.323  24.353  39.021  1.00 28.81           C  
ANISOU 2843  CB  ILE A 394     3574   3280   4090     81   -460  -1121       C  
ATOM   2844  CG1 ILE A 394      71.201  25.283  39.487  1.00 28.55           C  
ANISOU 2844  CG1 ILE A 394     3687   3191   3967     46   -565  -1139       C  
ATOM   2845  CG2 ILE A 394      72.602  24.544  37.527  1.00 28.99           C  
ANISOU 2845  CG2 ILE A 394     3594   3313   4107     20   -419  -1030       C  
ATOM   2846  CD1 ILE A 394      71.545  26.761  39.397  1.00 28.12           C  
ANISOU 2846  CD1 ILE A 394     3691   3389   3603    -60   -806  -1217       C  
ATOM   2847  N   PRO A 395      72.998  21.089  38.030  1.00 30.51           N  
ANISOU 2847  N   PRO A 395     3812   3480   4299     84   -340  -1213       N  
ATOM   2848  CA  PRO A 395      74.084  20.217  37.583  1.00 30.92           C  
ANISOU 2848  CA  PRO A 395     3937   3457   4353    153   -255  -1260       C  
ATOM   2849  C   PRO A 395      75.115  20.972  36.750  1.00 31.52           C  
ANISOU 2849  C   PRO A 395     4066   3470   4438    195   -176  -1278       C  
ATOM   2850  O   PRO A 395      74.748  21.877  35.996  1.00 32.39           O  
ANISOU 2850  O   PRO A 395     4158   3674   4474    180   -172  -1179       O  
ATOM   2851  CB  PRO A 395      73.364  19.203  36.686  1.00 31.75           C  
ANISOU 2851  CB  PRO A 395     4021   3594   4445    164   -269  -1243       C  
ATOM   2852  CG  PRO A 395      72.201  19.975  36.126  1.00 31.64           C  
ANISOU 2852  CG  PRO A 395     3906   3747   4369    196   -231  -1224       C  
ATOM   2853  CD  PRO A 395      71.768  20.894  37.241  1.00 30.99           C  
ANISOU 2853  CD  PRO A 395     3895   3507   4372    141   -373  -1228       C  
ATOM   2854  N   LEU A 396      76.389  20.625  36.909  1.00 30.92           N  
ANISOU 2854  N   LEU A 396     4055   3298   4395    274    -26  -1365       N  
ATOM   2855  CA  LEU A 396      77.433  21.108  36.015  1.00 31.88           C  
ANISOU 2855  CA  LEU A 396     4165   3367   4580    336     57  -1347       C  
ATOM   2856  C   LEU A 396      78.141  19.895  35.422  1.00 32.97           C  
ANISOU 2856  C   LEU A 396     4237   3555   4732    395    144  -1346       C  
ATOM   2857  O   LEU A 396      78.426  18.943  36.149  1.00 33.25           O  
ANISOU 2857  O   LEU A 396     4306   3514   4813    369    206  -1364       O  
ATOM   2858  CB  LEU A 396      78.435  22.008  36.748  1.00 30.91           C  
ANISOU 2858  CB  LEU A 396     4061   3202   4480    334    142  -1372       C  
ATOM   2859  CG  LEU A 396      77.939  23.350  37.302  1.00 30.28           C  
ANISOU 2859  CG  LEU A 396     4022   2978   4504    356     69  -1266       C  
ATOM   2860  CD1 LEU A 396      79.053  24.104  38.016  1.00 29.65           C  
ANISOU 2860  CD1 LEU A 396     4307   2458   4498    285    133  -1249       C  
ATOM   2861  CD2 LEU A 396      77.417  24.186  36.176  1.00 31.89           C  
ANISOU 2861  CD2 LEU A 396     4385   3044   4685    460    118  -1075       C  
ATOM   2862  N   PRO A 397      78.426  19.919  34.109  1.00 34.16           N  
ANISOU 2862  N   PRO A 397     4404   3744   4831    434    171  -1276       N  
ATOM   2863  CA  PRO A 397      79.193  18.838  33.499  1.00 34.91           C  
ANISOU 2863  CA  PRO A 397     4509   3838   4913    529    229  -1293       C  
ATOM   2864  C   PRO A 397      80.634  18.773  34.009  1.00 35.46           C  
ANISOU 2864  C   PRO A 397     4646   3840   4987    593    240  -1264       C  
ATOM   2865  O   PRO A 397      81.212  19.807  34.357  1.00 35.55           O  
ANISOU 2865  O   PRO A 397     4558   3904   5043    687    253  -1230       O  
ATOM   2866  CB  PRO A 397      79.195  19.201  32.010  1.00 35.39           C  
ANISOU 2866  CB  PRO A 397     4554   3902   4991    471    185  -1184       C  
ATOM   2867  CG  PRO A 397      79.038  20.680  31.980  1.00 34.77           C  
ANISOU 2867  CG  PRO A 397     4476   3857   4875    517    284  -1408       C  
ATOM   2868  CD  PRO A 397      78.193  21.037  33.176  1.00 34.85           C  
ANISOU 2868  CD  PRO A 397     4457   3903   4879    474    208  -1273       C  
ATOM   2869  N   ALA A 398      81.207  17.570  34.027  1.00 35.84           N  
ANISOU 2869  N   ALA A 398     4733   3810   5074    671    340  -1266       N  
ATOM   2870  CA  ALA A 398      82.574  17.366  34.503  1.00 35.97           C  
ANISOU 2870  CA  ALA A 398     4864   3762   5038    710    448  -1272       C  
ATOM   2871  C   ALA A 398      83.550  17.932  33.486  1.00 36.24           C  
ANISOU 2871  C   ALA A 398     4919   3766   5084    711    502  -1259       C  
ATOM   2872  O   ALA A 398      83.231  17.996  32.294  1.00 36.04           O  
ANISOU 2872  O   ALA A 398     4979   3702   5011    706    532  -1293       O  
ATOM   2873  CB  ALA A 398      82.851  15.882  34.726  1.00 36.11           C  
ANISOU 2873  CB  ALA A 398     4809   3838   5074    735    442  -1190       C  
ATOM   2874  N   LEU A 399      84.718  18.337  33.983  1.00 36.77           N  
ANISOU 2874  N   LEU A 399     5085   3826   5060    714    538  -1271       N  
ATOM   2875  CA  LEU A 399      85.860  18.785  33.180  1.00 37.32           C  
ANISOU 2875  CA  LEU A 399     5090   3929   5159    685    559  -1174       C  
ATOM   2876  C   LEU A 399      85.478  19.725  32.034  1.00 36.89           C  
ANISOU 2876  C   LEU A 399     5029   3944   5043    624    596  -1179       C  
ATOM   2877  O   LEU A 399      85.864  19.520  30.878  1.00 36.68           O  
ANISOU 2877  O   LEU A 399     5054   3885   4997    705    635  -1262       O  
ATOM   2878  CB  LEU A 399      86.679  17.590  32.667  1.00 37.97           C  
ANISOU 2878  CB  LEU A 399     5167   4048   5211    726    583  -1165       C  
ATOM   2879  CG  LEU A 399      87.514  16.779  33.669  1.00 40.80           C  
ANISOU 2879  CG  LEU A 399     5482   4397   5621    720    477   -949       C  
ATOM   2880  CD1 LEU A 399      88.179  17.654  34.724  1.00 42.89           C  
ANISOU 2880  CD1 LEU A 399     5766   4876   5651    647    378   -949       C  
ATOM   2881  CD2 LEU A 399      86.682  15.688  34.334  1.00 43.91           C  
ANISOU 2881  CD2 LEU A 399     5709   4953   6018    554    486   -650       C  
ATOM   2882  N   SER A 400      84.727  20.765  32.386  1.00 35.56           N  
ANISOU 2882  N   SER A 400     4820   3815   4876    565    624  -1138       N  
ATOM   2883  CA  SER A 400      84.179  21.698  31.412  1.00 34.79           C  
ANISOU 2883  CA  SER A 400     4740   3841   4636    403    634  -1040       C  
ATOM   2884  C   SER A 400      84.493  23.132  31.818  1.00 33.49           C  
ANISOU 2884  C   SER A 400     4506   3714   4503    380    691   -981       C  
ATOM   2885  O   SER A 400      84.728  23.430  32.991  1.00 32.78           O  
ANISOU 2885  O   SER A 400     4376   3594   4482    341    630   -917       O  
ATOM   2886  CB  SER A 400      82.661  21.525  31.302  1.00 34.92           C  
ANISOU 2886  CB  SER A 400     4764   3888   4613    407    600  -1059       C  
ATOM   2887  OG  SER A 400      82.340  20.193  30.939  1.00 35.91           O  
ANISOU 2887  OG  SER A 400     5177   3965   4501    269    474   -983       O  
ATOM   2888  N   THR A 401      84.472  24.026  30.839  1.00 32.54           N  
ANISOU 2888  N   THR A 401     4299   3742   4321    305    739   -971       N  
ATOM   2889  CA  THR A 401      84.631  25.449  31.118  1.00 31.27           C  
ANISOU 2889  CA  THR A 401     4177   3646   4057    284    786   -953       C  
ATOM   2890  C   THR A 401      83.248  26.045  31.363  1.00 31.09           C  
ANISOU 2890  C   THR A 401     4166   3644   4001    237    765   -944       C  
ATOM   2891  O   THR A 401      82.294  25.759  30.631  1.00 30.56           O  
ANISOU 2891  O   THR A 401     4138   3575   3899    176    863   -911       O  
ATOM   2892  CB  THR A 401      85.406  26.167  29.990  1.00 31.52           C  
ANISOU 2892  CB  THR A 401     4150   3693   4130    244    733   -922       C  
ATOM   2893  OG1 THR A 401      84.716  25.991  28.749  1.00 31.22           O  
ANISOU 2893  OG1 THR A 401     4214   3687   3959    238    672   -808       O  
ATOM   2894  CG2 THR A 401      86.794  25.543  29.841  1.00 30.19           C  
ANISOU 2894  CG2 THR A 401     3950   3556   3963    258    911   -936       C  
ATOM   2895  N   ILE A 402      83.152  26.837  32.428  1.00 30.84           N  
ANISOU 2895  N   ILE A 402     4104   3632   3980    226    726   -959       N  
ATOM   2896  CA  ILE A 402      81.892  27.429  32.879  1.00 30.17           C  
ANISOU 2896  CA  ILE A 402     4007   3582   3873    178    633   -919       C  
ATOM   2897  C   ILE A 402      81.991  28.952  32.896  1.00 30.18           C  
ANISOU 2897  C   ILE A 402     3985   3676   3805    181    561   -856       C  
ATOM   2898  O   ILE A 402      83.007  29.514  33.322  1.00 29.70           O  
ANISOU 2898  O   ILE A 402     3886   3607   3790    149    605   -826       O  
ATOM   2899  CB  ILE A 402      81.525  26.963  34.312  1.00 30.22           C  
ANISOU 2899  CB  ILE A 402     4035   3562   3885    193    632   -973       C  
ATOM   2900  CG1 ILE A 402      81.696  25.442  34.483  1.00 30.67           C  
ANISOU 2900  CG1 ILE A 402     4175   3490   3986    166    624   -927       C  
ATOM   2901  CG2 ILE A 402      80.131  27.448  34.708  1.00 28.36           C  
ANISOU 2901  CG2 ILE A 402     3824   3353   3598    113    555  -1081       C  
ATOM   2902  CD1 ILE A 402      80.796  24.577  33.612  1.00 30.89           C  
ANISOU 2902  CD1 ILE A 402     4511   3606   3618    190    718  -1089       C  
ATOM   2903  N   GLU A 403      80.929  29.616  32.446  1.00 29.48           N  
ANISOU 2903  N   GLU A 403     3902   3705   3593    144    433   -742       N  
ATOM   2904  CA  GLU A 403      80.819  31.061  32.591  1.00 28.36           C  
ANISOU 2904  CA  GLU A 403     3814   3627   3332     91    331   -761       C  
ATOM   2905  C   GLU A 403      79.509  31.397  33.296  1.00 27.44           C  
ANISOU 2905  C   GLU A 403     3705   3587   3133     77    244   -697       C  
ATOM   2906  O   GLU A 403      78.446  30.978  32.840  1.00 27.83           O  
ANISOU 2906  O   GLU A 403     3744   3645   3185    -16    144   -770       O  
ATOM   2907  CB  GLU A 403      80.892  31.757  31.229  1.00 28.68           C  
ANISOU 2907  CB  GLU A 403     3904   3687   3302     90    323   -713       C  
ATOM   2908  CG  GLU A 403      80.818  33.294  31.300  1.00 29.28           C  
ANISOU 2908  CG  GLU A 403     4096   3809   3218     34    358   -825       C  
ATOM   2909  CD  GLU A 403      81.152  33.957  29.969  1.00 31.03           C  
ANISOU 2909  CD  GLU A 403     4280   4176   3335   -100    216   -800       C  
ATOM   2910  OE1 GLU A 403      80.359  33.839  29.011  1.00 32.57           O  
ANISOU 2910  OE1 GLU A 403     4020   4506   3845    -39    -53  -1021       O  
ATOM   2911  OE2 GLU A 403      82.221  34.594  29.863  1.00 30.97           O  
ANISOU 2911  OE2 GLU A 403     4211   4343   3213    -19    604   -905       O  
ATOM   2912  N   LEU A 404      79.588  32.127  34.406  1.00 25.71           N  
ANISOU 2912  N   LEU A 404     3462   3334   2972    117    140   -693       N  
ATOM   2913  CA  LEU A 404      78.397  32.533  35.147  1.00 24.88           C  
ANISOU 2913  CA  LEU A 404     3354   3352   2747     88    144   -630       C  
ATOM   2914  C   LEU A 404      78.249  34.046  35.091  1.00 24.78           C  
ANISOU 2914  C   LEU A 404     3294   3380   2741    159    154   -614       C  
ATOM   2915  O   LEU A 404      79.229  34.769  35.308  1.00 24.82           O  
ANISOU 2915  O   LEU A 404     3151   3433   2847    177    143   -603       O  
ATOM   2916  CB  LEU A 404      78.481  32.126  36.624  1.00 23.95           C  
ANISOU 2916  CB  LEU A 404     3178   3287   2632     52     34   -615       C  
ATOM   2917  CG  LEU A 404      78.810  30.657  36.906  1.00 23.86           C  
ANISOU 2917  CG  LEU A 404     3252   3201   2610   -124     42   -664       C  
ATOM   2918  CD1 LEU A 404      78.801  30.401  38.406  1.00 24.75           C  
ANISOU 2918  CD1 LEU A 404     3098   3446   2860     -5    459   -534       C  
ATOM   2919  CD2 LEU A 404      77.833  29.729  36.165  1.00 24.20           C  
ANISOU 2919  CD2 LEU A 404     3030   3022   3140    -90     94   -602       C  
ATOM   2920  N   SER A 405      77.028  34.520  34.861  1.00 24.16           N  
ANISOU 2920  N   SER A 405     3244   3398   2535    232     82   -570       N  
ATOM   2921  CA  SER A 405      76.757  35.951  34.970  1.00 24.52           C  
ANISOU 2921  CA  SER A 405     3212   3376   2727    241     66   -507       C  
ATOM   2922  C   SER A 405      75.705  36.262  36.044  1.00 24.68           C  
ANISOU 2922  C   SER A 405     3158   3330   2887    309     33   -510       C  
ATOM   2923  O   SER A 405      74.734  35.509  36.224  1.00 25.09           O  
ANISOU 2923  O   SER A 405     3225   3296   3012    385    -73   -523       O  
ATOM   2924  CB  SER A 405      76.347  36.523  33.613  1.00 24.75           C  
ANISOU 2924  CB  SER A 405     3280   3426   2698    187      3   -510       C  
ATOM   2925  OG  SER A 405      75.477  35.631  32.942  1.00 24.62           O  
ANISOU 2925  OG  SER A 405     3049   3574   2728     56     33   -536       O  
ATOM   2926  N   PHE A 406      75.915  37.370  36.752  1.00 24.27           N  
ANISOU 2926  N   PHE A 406     3004   3171   3045    327    -25   -446       N  
ATOM   2927  CA  PHE A 406      75.087  37.753  37.899  1.00 24.29           C  
ANISOU 2927  CA  PHE A 406     2917   3064   3247    347    -65   -412       C  
ATOM   2928  C   PHE A 406      74.569  39.183  37.724  1.00 23.94           C  
ANISOU 2928  C   PHE A 406     2881   3030   3184    300    -72   -447       C  
ATOM   2929  O   PHE A 406      74.939  40.068  38.486  1.00 23.85           O  
ANISOU 2929  O   PHE A 406     2892   2908   3260    356    -17   -510       O  
ATOM   2930  CB  PHE A 406      75.916  37.689  39.185  1.00 24.57           C  
ANISOU 2930  CB  PHE A 406     3017   3024   3292    276    -34   -363       C  
ATOM   2931  CG  PHE A 406      76.599  36.376  39.417  1.00 26.90           C  
ANISOU 2931  CG  PHE A 406     2800   3197   4225    278    -74   -144       C  
ATOM   2932  CD1 PHE A 406      75.882  35.273  39.865  1.00 30.37           C  
ANISOU 2932  CD1 PHE A 406     3225   3243   5071    352     89    228       C  
ATOM   2933  CD2 PHE A 406      77.964  36.246  39.220  1.00 28.73           C  
ANISOU 2933  CD2 PHE A 406     2904   3130   4881    154    223    -10       C  
ATOM   2934  CE1 PHE A 406      76.516  34.057  40.091  1.00 31.68           C  
ANISOU 2934  CE1 PHE A 406     3142   3428   5464    386    137     53       C  
ATOM   2935  CE2 PHE A 406      78.598  35.040  39.457  1.00 31.10           C  
ANISOU 2935  CE2 PHE A 406     3060   3446   5310    255    281    -52       C  
ATOM   2936  CZ  PHE A 406      77.880  33.941  39.882  1.00 30.72           C  
ANISOU 2936  CZ  PHE A 406     3077   3414   5181    277    352    122       C  
ATOM   2937  N   PRO A 407      73.731  39.425  36.705  1.00 23.71           N  
ANISOU 2937  N   PRO A 407     2781   2968   3257    333   -146   -389       N  
ATOM   2938  CA  PRO A 407      73.365  40.806  36.390  1.00 24.07           C  
ANISOU 2938  CA  PRO A 407     2837   2954   3352    306   -199   -471       C  
ATOM   2939  C   PRO A 407      72.647  41.491  37.553  1.00 24.13           C  
ANISOU 2939  C   PRO A 407     2774   2929   3465    282   -224   -488       C  
ATOM   2940  O   PRO A 407      71.681  40.945  38.087  1.00 23.96           O  
ANISOU 2940  O   PRO A 407     2688   2894   3520    215   -203   -481       O  
ATOM   2941  CB  PRO A 407      72.432  40.663  35.184  1.00 24.15           C  
ANISOU 2941  CB  PRO A 407     2910   3007   3258    288   -284   -374       C  
ATOM   2942  CG  PRO A 407      72.028  39.209  35.148  1.00 23.30           C  
ANISOU 2942  CG  PRO A 407     2722   2928   3202    380   -263   -399       C  
ATOM   2943  CD  PRO A 407      73.185  38.463  35.731  1.00 24.00           C  
ANISOU 2943  CD  PRO A 407     2874   3040   3203    264   -156   -373       C  
ATOM   2944  N   ALA A 408      73.146  42.657  37.962  1.00 23.69           N  
ANISOU 2944  N   ALA A 408     2669   2831   3498    278   -333   -566       N  
ATOM   2945  CA  ALA A 408      72.558  43.393  39.083  1.00 23.41           C  
ANISOU 2945  CA  ALA A 408     2436   2828   3628    368   -420   -535       C  
ATOM   2946  C   ALA A 408      71.147  43.823  38.700  1.00 23.70           C  
ANISOU 2946  C   ALA A 408     2402   2893   3710    331   -512   -442       C  
ATOM   2947  O   ALA A 408      70.899  44.166  37.542  1.00 24.05           O  
ANISOU 2947  O   ALA A 408     2448   3027   3661    269   -677   -458       O  
ATOM   2948  CB  ALA A 408      73.412  44.606  39.432  1.00 22.45           C  
ANISOU 2948  CB  ALA A 408     2325   2692   3513    350   -369   -658       C  
ATOM   2949  N   THR A 409      70.231  43.800  39.662  1.00 23.89           N  
ANISOU 2949  N   THR A 409     2383   2865   3826    366   -539   -341       N  
ATOM   2950  CA  THR A 409      68.813  44.061  39.381  1.00 23.52           C  
ANISOU 2950  CA  THR A 409     2242   2784   3910    412   -668   -304       C  
ATOM   2951  C   THR A 409      68.147  44.668  40.602  1.00 23.79           C  
ANISOU 2951  C   THR A 409     2226   2825   3988    418   -605   -253       C  
ATOM   2952  O   THR A 409      68.425  44.271  41.732  1.00 22.59           O  
ANISOU 2952  O   THR A 409     1989   2867   3725    413   -533   -386       O  
ATOM   2953  CB  THR A 409      68.004  42.815  38.901  1.00 24.16           C  
ANISOU 2953  CB  THR A 409     2311   2815   4050    446   -659   -205       C  
ATOM   2954  OG1 THR A 409      66.615  43.158  38.780  1.00 25.02           O  
ANISOU 2954  OG1 THR A 409     2409   2938   4158    247   -863   -270       O  
ATOM   2955  CG2 THR A 409      68.125  41.617  39.860  1.00 24.06           C  
ANISOU 2955  CG2 THR A 409     2268   2721   4150    306   -710   -227       C  
ATOM   2956  N   ALA A 410      67.262  45.629  40.363  1.00 24.11           N  
ANISOU 2956  N   ALA A 410     2403   2693   4063    432   -593   -289       N  
ATOM   2957  CA  ALA A 410      66.495  46.230  41.447  1.00 24.59           C  
ANISOU 2957  CA  ALA A 410     2505   2729   4107    478   -526   -251       C  
ATOM   2958  C   ALA A 410      65.498  45.229  42.033  1.00 24.49           C  
ANISOU 2958  C   ALA A 410     2524   2647   4134    409   -572   -258       C  
ATOM   2959  O   ALA A 410      64.940  45.435  43.117  1.00 24.81           O  
ANISOU 2959  O   ALA A 410     2673   2599   4155    318   -515   -297       O  
ATOM   2960  CB  ALA A 410      65.799  47.513  40.971  1.00 25.03           C  
ANISOU 2960  CB  ALA A 410     2619   2793   4097    559   -644   -194       C  
ATOM   2961  N   ASN A 411      65.273  44.131  41.319  1.00 23.94           N  
ANISOU 2961  N   ASN A 411     2437   2600   4056    439   -618   -187       N  
ATOM   2962  CA  ASN A 411      64.438  43.075  41.867  1.00 24.52           C  
ANISOU 2962  CA  ASN A 411     2399   2726   4189    327   -653   -266       C  
ATOM   2963  C   ASN A 411      65.071  42.363  43.063  1.00 23.97           C  
ANISOU 2963  C   ASN A 411     2319   2692   4095    316   -583   -240       C  
ATOM   2964  O   ASN A 411      64.391  41.635  43.788  1.00 23.74           O  
ANISOU 2964  O   ASN A 411     2236   2709   4073    215   -559   -364       O  
ATOM   2965  CB  ASN A 411      64.048  42.093  40.762  1.00 25.41           C  
ANISOU 2965  CB  ASN A 411     2580   2850   4224    356   -603   -285       C  
ATOM   2966  CG  ASN A 411      63.068  42.705  39.794  1.00 27.45           C  
ANISOU 2966  CG  ASN A 411     2811   3058   4558    344   -719   -275       C  
ATOM   2967  OD1 ASN A 411      62.358  43.652  40.141  1.00 29.93           O  
ANISOU 2967  OD1 ASN A 411     2936   3386   5050    533   -597   -320       O  
ATOM   2968  ND2 ASN A 411      63.035  42.189  38.570  1.00 30.10           N  
ANISOU 2968  ND2 ASN A 411     3349   3358   4729    206   -678   -400       N  
ATOM   2969  N   ALA A 412      66.368  42.586  43.270  1.00 23.40           N  
ANISOU 2969  N   ALA A 412     2208   2629   4054    331   -578   -206       N  
ATOM   2970  CA  ALA A 412      67.041  42.048  44.438  1.00 23.83           C  
ANISOU 2970  CA  ALA A 412     2079   2764   4210    371   -555   -125       C  
ATOM   2971  C   ALA A 412      67.723  43.187  45.191  1.00 24.31           C  
ANISOU 2971  C   ALA A 412     2044   2899   4294    368   -497   -100       C  
ATOM   2972  O   ALA A 412      68.929  43.418  45.020  1.00 24.81           O  
ANISOU 2972  O   ALA A 412     1990   2997   4440    354   -517     42       O  
ATOM   2973  CB  ALA A 412      68.043  40.972  44.027  1.00 24.35           C  
ANISOU 2973  CB  ALA A 412     2289   2780   4181    343   -465   -149       C  
ATOM   2974  N   PRO A 413      66.959  43.909  46.030  1.00 23.81           N  
ANISOU 2974  N   PRO A 413     1820   2889   4338    414   -502   -131       N  
ATOM   2975  CA  PRO A 413      67.569  45.024  46.757  1.00 23.41           C  
ANISOU 2975  CA  PRO A 413     1753   2878   4261    443   -483   -152       C  
ATOM   2976  C   PRO A 413      68.575  44.536  47.788  1.00 22.34           C  
ANISOU 2976  C   PRO A 413     1576   2793   4118    393   -457   -177       C  
ATOM   2977  O   PRO A 413      68.675  43.338  48.054  1.00 21.60           O  
ANISOU 2977  O   PRO A 413     1445   2772   3988    427   -560   -201       O  
ATOM   2978  CB  PRO A 413      66.382  45.706  47.447  1.00 24.14           C  
ANISOU 2978  CB  PRO A 413     1836   2942   4393    441   -418   -164       C  
ATOM   2979  CG  PRO A 413      65.298  44.679  47.491  1.00 24.86           C  
ANISOU 2979  CG  PRO A 413     1882   2990   4572    351   -395   -203       C  
ATOM   2980  CD  PRO A 413      65.526  43.738  46.343  1.00 24.77           C  
ANISOU 2980  CD  PRO A 413     2012   3028   4370    324   -361   -150       C  
ATOM   2981  N   GLY A 414      69.326  45.466  48.356  1.00 21.39           N  
ANISOU 2981  N   GLY A 414     1398   2682   4046    321   -471   -148       N  
ATOM   2982  CA  GLY A 414      70.428  45.086  49.225  1.00 20.97           C  
ANISOU 2982  CA  GLY A 414     1355   2644   3967    409   -364    -25       C  
ATOM   2983  C   GLY A 414      71.757  45.087  48.494  1.00 20.61           C  
ANISOU 2983  C   GLY A 414     1377   2647   3806    291   -274     12       C  
ATOM   2984  O   GLY A 414      72.749  44.541  48.998  1.00 20.11           O  
ANISOU 2984  O   GLY A 414     1268   2432   3938    329   -201    125       O  
ATOM   2985  N   VAL A 415      71.792  45.730  47.329  1.00 21.01           N  
ANISOU 2985  N   VAL A 415     1422   2786   3775    328   -221    -30       N  
ATOM   2986  CA  VAL A 415      73.016  45.825  46.523  1.00 21.15           C  
ANISOU 2986  CA  VAL A 415     1583   2823   3627    200   -216    -76       C  
ATOM   2987  C   VAL A 415      74.075  46.660  47.246  1.00 20.63           C  
ANISOU 2987  C   VAL A 415     1536   2813   3489    177   -146    -76       C  
ATOM   2988  O   VAL A 415      73.725  47.509  48.081  1.00 21.64           O  
ANISOU 2988  O   VAL A 415     1747   2788   3684    126   -100    -42       O  
ATOM   2989  CB  VAL A 415      72.729  46.427  45.119  1.00 20.76           C  
ANISOU 2989  CB  VAL A 415     1590   2729   3568    230   -179   -116       C  
ATOM   2990  CG1 VAL A 415      71.666  45.602  44.389  1.00 20.80           C  
ANISOU 2990  CG1 VAL A 415     1289   2805   3807    261   -333   -149       C  
ATOM   2991  CG2 VAL A 415      72.294  47.889  45.219  1.00 22.87           C  
ANISOU 2991  CG2 VAL A 415     2102   2828   3759    269   -338   -116       C  
ATOM   2992  N   PRO A 416      75.364  46.438  46.935  1.00 20.30           N  
ANISOU 2992  N   PRO A 416     1578   2809   3326    154   -183   -139       N  
ATOM   2993  CA  PRO A 416      75.893  45.411  46.030  1.00 19.70           C  
ANISOU 2993  CA  PRO A 416     1456   2751   3276    201   -146   -142       C  
ATOM   2994  C   PRO A 416      75.948  44.050  46.730  1.00 19.75           C  
ANISOU 2994  C   PRO A 416     1542   2735   3224    162   -154   -171       C  
ATOM   2995  O   PRO A 416      76.398  43.986  47.878  1.00 19.79           O  
ANISOU 2995  O   PRO A 416     1730   2740   3047    198   -184    -42       O  
ATOM   2996  CB  PRO A 416      77.301  45.930  45.715  1.00 19.88           C  
ANISOU 2996  CB  PRO A 416     1540   2780   3232    114   -122   -179       C  
ATOM   2997  CG  PRO A 416      77.705  46.654  46.966  1.00 20.01           C  
ANISOU 2997  CG  PRO A 416     1357   2820   3425    159   -137   -257       C  
ATOM   2998  CD  PRO A 416      76.436  47.278  47.507  1.00 20.44           C  
ANISOU 2998  CD  PRO A 416     1455   2842   3468     86    -88   -153       C  
ATOM   2999  N   HIS A 417      75.501  42.983  46.068  1.00 19.18           N  
ANISOU 2999  N   HIS A 417     1503   2614   3170    169   -152   -225       N  
ATOM   3000  CA  HIS A 417      75.584  41.629  46.638  1.00 19.17           C  
ANISOU 3000  CA  HIS A 417     1427   2642   3214    179   -193   -229       C  
ATOM   3001  C   HIS A 417      76.913  40.953  46.314  1.00 18.13           C  
ANISOU 3001  C   HIS A 417     1331   2461   3094    149   -103   -325       C  
ATOM   3002  O   HIS A 417      77.221  40.764  45.136  1.00 19.55           O  
ANISOU 3002  O   HIS A 417     1562   2578   3285    156   -146   -302       O  
ATOM   3003  CB  HIS A 417      74.468  40.733  46.090  1.00 18.45           C  
ANISOU 3003  CB  HIS A 417     1319   2615   3075    180   -317   -248       C  
ATOM   3004  CG  HIS A 417      73.091  41.238  46.397  1.00 19.33           C  
ANISOU 3004  CG  HIS A 417     1233   3099   3010    155   -441   -132       C  
ATOM   3005  ND1 HIS A 417      72.504  41.092  47.635  1.00 20.13           N  
ANISOU 3005  ND1 HIS A 417     1415   3397   2835    100   -601    -35       N  
ATOM   3006  CD2 HIS A 417      72.203  41.915  45.630  1.00 19.13           C  
ANISOU 3006  CD2 HIS A 417     1330   3088   2849     76   -468    -74       C  
ATOM   3007  CE1 HIS A 417      71.313  41.665  47.618  1.00 18.92           C  
ANISOU 3007  CE1 HIS A 417     1473   3168   2545     -3   -643   -143       C  
ATOM   3008  NE2 HIS A 417      71.094  42.151  46.406  1.00 19.43           N  
ANISOU 3008  NE2 HIS A 417     1364   3223   2792     60   -437     41       N  
ATOM   3009  N   PRO A 418      77.701  40.592  47.338  1.00 17.87           N  
ANISOU 3009  N   PRO A 418     1423   2336   3031    212      0   -302       N  
ATOM   3010  CA  PRO A 418      78.966  39.907  47.059  1.00 17.87           C  
ANISOU 3010  CA  PRO A 418     1448   2300   3041    211     33   -354       C  
ATOM   3011  C   PRO A 418      78.766  38.388  46.974  1.00 19.72           C  
ANISOU 3011  C   PRO A 418     1753   2510   3228    151     40   -312       C  
ATOM   3012  O   PRO A 418      78.490  37.724  47.980  1.00 20.11           O  
ANISOU 3012  O   PRO A 418     1934   2507   3197    -15    202   -317       O  
ATOM   3013  CB  PRO A 418      79.851  40.289  48.244  1.00 17.84           C  
ANISOU 3013  CB  PRO A 418     1426   2274   3077    234    121   -266       C  
ATOM   3014  CG  PRO A 418      78.877  40.443  49.387  1.00 17.28           C  
ANISOU 3014  CG  PRO A 418     1271   2283   3009    518    159   -319       C  
ATOM   3015  CD  PRO A 418      77.564  40.935  48.767  1.00 16.26           C  
ANISOU 3015  CD  PRO A 418     1089   2328   2761    222    -70   -342       C  
ATOM   3016  N   PHE A 419      78.876  37.849  45.767  1.00 18.88           N  
ANISOU 3016  N   PHE A 419     1543   2451   3178    175     52   -500       N  
ATOM   3017  CA  PHE A 419      78.671  36.417  45.585  1.00 19.81           C  
ANISOU 3017  CA  PHE A 419     1643   2585   3297    264    -27   -365       C  
ATOM   3018  C   PHE A 419      79.930  35.590  45.791  1.00 19.82           C  
ANISOU 3018  C   PHE A 419     1681   2554   3295    236     10   -463       C  
ATOM   3019  O   PHE A 419      81.041  35.986  45.431  1.00 19.17           O  
ANISOU 3019  O   PHE A 419     1533   2522   3228    320     59   -341       O  
ATOM   3020  CB  PHE A 419      78.021  36.113  44.237  1.00 19.66           C  
ANISOU 3020  CB  PHE A 419     1561   2589   3319    134    -53   -390       C  
ATOM   3021  CG  PHE A 419      76.529  36.033  44.327  1.00 20.25           C  
ANISOU 3021  CG  PHE A 419     1491   2893   3308    301     -1   -327       C  
ATOM   3022  CD1 PHE A 419      75.779  37.185  44.542  1.00 21.19           C  
ANISOU 3022  CD1 PHE A 419     1552   3156   3340    299     64   -293       C  
ATOM   3023  CD2 PHE A 419      75.885  34.808  44.250  1.00 20.32           C  
ANISOU 3023  CD2 PHE A 419     1151   3138   3430    -10   -207   -312       C  
ATOM   3024  CE1 PHE A 419      74.399  37.121  44.667  1.00 21.99           C  
ANISOU 3024  CE1 PHE A 419     1568   3384   3404    260    -64   -455       C  
ATOM   3025  CE2 PHE A 419      74.486  34.731  44.347  1.00 21.21           C  
ANISOU 3025  CE2 PHE A 419     1062   3356   3641    500   -396   -297       C  
ATOM   3026  CZ  PHE A 419      73.744  35.893  44.566  1.00 21.46           C  
ANISOU 3026  CZ  PHE A 419     1719   3169   3265    306    -37   -479       C  
ATOM   3027  N   HIS A 420      79.710  34.423  46.380  1.00 19.89           N  
ANISOU 3027  N   HIS A 420     1779   2558   3220    285    -14   -393       N  
ATOM   3028  CA  HIS A 420      80.798  33.522  46.695  1.00 19.87           C  
ANISOU 3028  CA  HIS A 420     1720   2645   3185    163     59   -516       C  
ATOM   3029  C   HIS A 420      80.494  32.103  46.213  1.00 20.16           C  
ANISOU 3029  C   HIS A 420     1815   2631   3214    160    133   -522       C  
ATOM   3030  O   HIS A 420      79.387  31.591  46.410  1.00 19.35           O  
ANISOU 3030  O   HIS A 420     1650   2649   3053     45    212   -635       O  
ATOM   3031  CB  HIS A 420      80.972  33.537  48.207  1.00 19.44           C  
ANISOU 3031  CB  HIS A 420     1571   2757   3058    145    -46   -411       C  
ATOM   3032  CG  HIS A 420      81.897  32.474  48.687  1.00 20.78           C  
ANISOU 3032  CG  HIS A 420     1832   2913   3147    267    172   -352       C  
ATOM   3033  ND1 HIS A 420      83.167  32.323  48.167  1.00 21.77           N  
ANISOU 3033  ND1 HIS A 420     2095   3596   2579    494    559   -292       N  
ATOM   3034  CD2 HIS A 420      81.740  31.507  49.617  1.00 18.51           C  
ANISOU 3034  CD2 HIS A 420     1903   3404   1725    287     39   -474       C  
ATOM   3035  CE1 HIS A 420      83.760  31.301  48.756  1.00 21.32           C  
ANISOU 3035  CE1 HIS A 420     2075   3684   2340    396    228   -425       C  
ATOM   3036  NE2 HIS A 420      82.906  30.781  49.618  1.00 23.62           N  
ANISOU 3036  NE2 HIS A 420     1988   3920   3064    309    259   -259       N  
ATOM   3037  N   LEU A 421      81.484  31.491  45.572  1.00 19.56           N  
ANISOU 3037  N   LEU A 421     1779   2534   3116    161    154   -555       N  
ATOM   3038  CA  LEU A 421      81.388  30.118  45.093  1.00 20.42           C  
ANISOU 3038  CA  LEU A 421     2027   2514   3218    106    218   -522       C  
ATOM   3039  C   LEU A 421      82.331  29.213  45.871  1.00 20.58           C  
ANISOU 3039  C   LEU A 421     1947   2467   3405     82    197   -539       C  
ATOM   3040  O   LEU A 421      83.544  29.445  45.869  1.00 21.53           O  
ANISOU 3040  O   LEU A 421     2053   2492   3635    -13    298   -423       O  
ATOM   3041  CB  LEU A 421      81.775  30.081  43.612  1.00 20.00           C  
ANISOU 3041  CB  LEU A 421     2080   2532   2984    128    200   -601       C  
ATOM   3042  CG  LEU A 421      81.938  28.716  42.942  1.00 20.32           C  
ANISOU 3042  CG  LEU A 421     2473   2559   2688     -5    400   -354       C  
ATOM   3043  CD1 LEU A 421      80.599  27.975  42.954  1.00 19.30           C  
ANISOU 3043  CD1 LEU A 421     2209   2686   2437    103    169   -359       C  
ATOM   3044  CD2 LEU A 421      82.427  28.941  41.511  1.00 20.97           C  
ANISOU 3044  CD2 LEU A 421     2857   2630   2479    260    484   -425       C  
ATOM   3045  N   HIS A 422      81.780  28.194  46.529  1.00 20.70           N  
ANISOU 3045  N   HIS A 422     1904   2425   3533     84    223   -574       N  
ATOM   3046  CA  HIS A 422      82.584  27.165  47.183  1.00 21.35           C  
ANISOU 3046  CA  HIS A 422     2016   2432   3664    101    274   -524       C  
ATOM   3047  C   HIS A 422      83.329  26.276  46.187  1.00 21.83           C  
ANISOU 3047  C   HIS A 422     2140   2438   3713     70    343   -505       C  
ATOM   3048  O   HIS A 422      82.929  26.157  45.029  1.00 22.14           O  
ANISOU 3048  O   HIS A 422     2282   2468   3661     50    440   -531       O  
ATOM   3049  CB  HIS A 422      81.732  26.271  48.078  1.00 21.40           C  
ANISOU 3049  CB  HIS A 422     2038   2406   3684    111    244   -570       C  
ATOM   3050  CG  HIS A 422      81.126  26.970  49.256  1.00 21.35           C  
ANISOU 3050  CG  HIS A 422     2077   2347   3686     79    280   -643       C  
ATOM   3051  ND1 HIS A 422      81.045  26.380  50.498  1.00 20.96           N  
ANISOU 3051  ND1 HIS A 422     2106   2278   3580    -59   -131   -733       N  
ATOM   3052  CD2 HIS A 422      80.542  28.187  49.377  1.00 21.86           C  
ANISOU 3052  CD2 HIS A 422     1992   2384   3929    154    265   -619       C  
ATOM   3053  CE1 HIS A 422      80.420  27.198  51.331  1.00 21.72           C  
ANISOU 3053  CE1 HIS A 422     2041   2213   3996    -52    109   -529       C  
ATOM   3054  NE2 HIS A 422      80.117  28.306  50.679  1.00 21.51           N  
ANISOU 3054  NE2 HIS A 422     1827   2535   3811    403    -82   -512       N  
ATOM   3055  N   GLY A 423      84.415  25.668  46.659  1.00 22.06           N  
ANISOU 3055  N   GLY A 423     2123   2438   3820    149    460   -399       N  
ATOM   3056  CA  GLY A 423      85.160  24.657  45.909  1.00 22.93           C  
ANISOU 3056  CA  GLY A 423     2294   2505   3912    143    454   -417       C  
ATOM   3057  C   GLY A 423      86.025  25.174  44.774  1.00 23.80           C  
ANISOU 3057  C   GLY A 423     2388   2637   4017    173    495   -450       C  
ATOM   3058  O   GLY A 423      86.631  24.376  44.053  1.00 24.14           O  
ANISOU 3058  O   GLY A 423     2408   2646   4115    241    487   -364       O  
ATOM   3059  N   HIS A 424      86.090  26.492  44.593  1.00 23.67           N  
ANISOU 3059  N   HIS A 424     2418   2578   3994    156    493   -479       N  
ATOM   3060  CA  HIS A 424      86.724  27.052  43.394  1.00 24.14           C  
ANISOU 3060  CA  HIS A 424     2502   2734   3934    123    440   -551       C  
ATOM   3061  C   HIS A 424      87.203  28.479  43.588  1.00 23.99           C  
ANISOU 3061  C   HIS A 424     2476   2807   3832    137    422   -521       C  
ATOM   3062  O   HIS A 424      86.603  29.221  44.345  1.00 24.65           O  
ANISOU 3062  O   HIS A 424     2685   2875   3804     39    588   -648       O  
ATOM   3063  CB  HIS A 424      85.702  27.129  42.262  1.00 23.62           C  
ANISOU 3063  CB  HIS A 424     2379   2689   3906    123    423   -563       C  
ATOM   3064  CG  HIS A 424      85.280  25.799  41.729  1.00 24.65           C  
ANISOU 3064  CG  HIS A 424     2518   2753   4094    188    553   -704       C  
ATOM   3065  ND1 HIS A 424      86.019  25.104  40.795  1.00 25.37           N  
ANISOU 3065  ND1 HIS A 424     2354   3030   4253    117    773   -709       N  
ATOM   3066  CD2 HIS A 424      84.166  25.066  41.953  1.00 24.87           C  
ANISOU 3066  CD2 HIS A 424     2483   2779   4185    262    868   -762       C  
ATOM   3067  CE1 HIS A 424      85.392  23.982  40.490  1.00 25.98           C  
ANISOU 3067  CE1 HIS A 424     2614   3028   4228     97    909   -866       C  
ATOM   3068  NE2 HIS A 424      84.260  23.940  41.171  1.00 25.73           N  
ANISOU 3068  NE2 HIS A 424     2801   2772   4204    240   1008   -777       N  
ATOM   3069  N   THR A 425      88.240  28.883  42.866  1.00 24.28           N  
ANISOU 3069  N   THR A 425     2513   3027   3685    181    407   -507       N  
ATOM   3070  CA  THR A 425      88.465  30.309  42.618  1.00 24.65           C  
ANISOU 3070  CA  THR A 425     2581   3133   3650    164    344   -483       C  
ATOM   3071  C   THR A 425      87.992  30.502  41.187  1.00 24.82           C  
ANISOU 3071  C   THR A 425     2687   3132   3609    181    342   -513       C  
ATOM   3072  O   THR A 425      87.907  29.532  40.428  1.00 25.94           O  
ANISOU 3072  O   THR A 425     2915   3170   3771    213    311   -550       O  
ATOM   3073  CB  THR A 425      89.941  30.745  42.717  1.00 24.62           C  
ANISOU 3073  CB  THR A 425     2624   3275   3455    290    310   -562       C  
ATOM   3074  OG1 THR A 425      90.726  29.913  41.854  1.00 28.23           O  
ANISOU 3074  OG1 THR A 425     2770   3834   4121    223    648   -449       O  
ATOM   3075  CG2 THR A 425      90.443  30.588  44.141  1.00 26.08           C  
ANISOU 3075  CG2 THR A 425     2483   3680   3745     63    -14   -258       C  
ATOM   3076  N   PHE A 426      87.695  31.738  40.809  1.00 24.00           N  
ANISOU 3076  N   PHE A 426     2544   2995   3578    185    401   -494       N  
ATOM   3077  CA  PHE A 426      87.198  31.995  39.467  1.00 23.58           C  
ANISOU 3077  CA  PHE A 426     2624   3053   3281    184    529   -524       C  
ATOM   3078  C   PHE A 426      87.829  33.247  38.879  1.00 24.00           C  
ANISOU 3078  C   PHE A 426     2774   3114   3231    239    535   -464       C  
ATOM   3079  O   PHE A 426      88.259  34.136  39.607  1.00 24.19           O  
ANISOU 3079  O   PHE A 426     2827   3072   3289    225    595   -326       O  
ATOM   3080  CB  PHE A 426      85.674  32.143  39.481  1.00 23.84           C  
ANISOU 3080  CB  PHE A 426     2655   3064   3335    218    501   -571       C  
ATOM   3081  CG  PHE A 426      85.148  32.993  40.615  1.00 23.24           C  
ANISOU 3081  CG  PHE A 426     2561   3125   3143     25    380   -687       C  
ATOM   3082  CD1 PHE A 426      85.185  34.383  40.540  1.00 21.23           C  
ANISOU 3082  CD1 PHE A 426     2173   3044   2850    -35    175   -674       C  
ATOM   3083  CD2 PHE A 426      84.587  32.396  41.745  1.00 21.19           C  
ANISOU 3083  CD2 PHE A 426     2191   3062   2797   -160    281   -802       C  
ATOM   3084  CE1 PHE A 426      84.697  35.169  41.581  1.00 22.70           C  
ANISOU 3084  CE1 PHE A 426     2338   3197   3089    -38    282   -663       C  
ATOM   3085  CE2 PHE A 426      84.075  33.180  42.779  1.00 22.31           C  
ANISOU 3085  CE2 PHE A 426     2143   3269   3064   -162    117   -762       C  
ATOM   3086  CZ  PHE A 426      84.122  34.573  42.692  1.00 21.02           C  
ANISOU 3086  CZ  PHE A 426     2177   3132   2677     33    132   -737       C  
ATOM   3087  N   ALA A 427      87.897  33.301  37.554  1.00 23.95           N  
ANISOU 3087  N   ALA A 427     2847   3150   3103    263    607   -388       N  
ATOM   3088  CA  ALA A 427      88.349  34.505  36.871  1.00 24.09           C  
ANISOU 3088  CA  ALA A 427     2939   3150   3064    332    579   -424       C  
ATOM   3089  C   ALA A 427      87.237  35.551  36.822  1.00 24.35           C  
ANISOU 3089  C   ALA A 427     3004   3172   3074    344    580   -428       C  
ATOM   3090  O   ALA A 427      86.144  35.270  36.321  1.00 24.43           O  
ANISOU 3090  O   ALA A 427     2998   3249   3033    230    507   -559       O  
ATOM   3091  CB  ALA A 427      88.790  34.147  35.459  1.00 23.72           C  
ANISOU 3091  CB  ALA A 427     2857   3151   3004    388    676   -392       C  
ATOM   3092  N   VAL A 428      87.508  36.760  37.311  1.00 23.34           N  
ANISOU 3092  N   VAL A 428     2971   3026   2868    383    543   -418       N  
ATOM   3093  CA  VAL A 428      86.503  37.824  37.201  1.00 23.89           C  
ANISOU 3093  CA  VAL A 428     3164   3019   2894    399    562   -320       C  
ATOM   3094  C   VAL A 428      86.617  38.533  35.858  1.00 24.61           C  
ANISOU 3094  C   VAL A 428     3324   3066   2959    441    438   -336       C  
ATOM   3095  O   VAL A 428      87.304  39.545  35.720  1.00 24.88           O  
ANISOU 3095  O   VAL A 428     3329   3114   3010    305    478   -209       O  
ATOM   3096  CB  VAL A 428      86.584  38.816  38.373  1.00 23.23           C  
ANISOU 3096  CB  VAL A 428     3040   2947   2840    428    533   -329       C  
ATOM   3097  CG1 VAL A 428      85.464  39.857  38.289  1.00 23.00           C  
ANISOU 3097  CG1 VAL A 428     2989   2861   2886    435    624   -243       C  
ATOM   3098  CG2 VAL A 428      86.515  38.039  39.685  1.00 21.38           C  
ANISOU 3098  CG2 VAL A 428     2776   2813   2532    380    528   -179       C  
ATOM   3099  N   VAL A 429      85.944  37.979  34.861  1.00 25.58           N  
ANISOU 3099  N   VAL A 429     3510   3189   3020    498    394   -339       N  
ATOM   3100  CA  VAL A 429      86.052  38.481  33.503  1.00 26.22           C  
ANISOU 3100  CA  VAL A 429     3687   3302   2973    506    389   -344       C  
ATOM   3101  C   VAL A 429      85.443  39.879  33.376  1.00 26.05           C  
ANISOU 3101  C   VAL A 429     3532   3372   2991    475    442   -289       C  
ATOM   3102  O   VAL A 429      85.933  40.723  32.610  1.00 26.17           O  
ANISOU 3102  O   VAL A 429     3623   3459   2860    492    506   -250       O  
ATOM   3103  CB  VAL A 429      85.431  37.462  32.520  1.00 26.65           C  
ANISOU 3103  CB  VAL A 429     3843   3283   2997    501    315   -335       C  
ATOM   3104  CG1 VAL A 429      85.081  38.115  31.200  1.00 29.43           C  
ANISOU 3104  CG1 VAL A 429     4269   3699   3213    559    199   -316       C  
ATOM   3105  CG2 VAL A 429      86.408  36.305  32.303  1.00 26.78           C  
ANISOU 3105  CG2 VAL A 429     3788   3412   2973    514    314   -608       C  
ATOM   3106  N   ARG A 430      84.385  40.136  34.139  1.00 25.28           N  
ANISOU 3106  N   ARG A 430     3392   3370   2841    381    442   -281       N  
ATOM   3107  CA  ARG A 430      83.834  41.481  34.177  1.00 24.57           C  
ANISOU 3107  CA  ARG A 430     3117   3320   2897    392    445   -243       C  
ATOM   3108  C   ARG A 430      83.551  41.834  35.625  1.00 24.80           C  
ANISOU 3108  C   ARG A 430     3120   3310   2993    289    466   -270       C  
ATOM   3109  O   ARG A 430      82.865  41.084  36.322  1.00 24.74           O  
ANISOU 3109  O   ARG A 430     3062   3182   3154    300    434   -269       O  
ATOM   3110  CB  ARG A 430      82.577  41.619  33.309  1.00 24.38           C  
ANISOU 3110  CB  ARG A 430     3169   3310   2783    350    385   -245       C  
ATOM   3111  CG  ARG A 430      81.922  42.990  33.445  1.00 23.14           C  
ANISOU 3111  CG  ARG A 430     2836   3348   2609    434    312      9       C  
ATOM   3112  CD  ARG A 430      80.885  43.268  32.373  1.00 24.69           C  
ANISOU 3112  CD  ARG A 430     2575   3667   3135    593    253    131       C  
ATOM   3113  NE  ARG A 430      80.278  44.573  32.611  1.00 25.09           N  
ANISOU 3113  NE  ARG A 430     2828   3603   3102    403    181    404       N  
ATOM   3114  CZ  ARG A 430      79.096  44.970  32.144  1.00 25.88           C  
ANISOU 3114  CZ  ARG A 430     2643   3791   3398    532    464    352       C  
ATOM   3115  NH1 ARG A 430      78.350  44.181  31.378  1.00 25.64           N  
ANISOU 3115  NH1 ARG A 430     2419   3901   3421    317    402    419       N  
ATOM   3116  NH2 ARG A 430      78.668  46.185  32.444  1.00 27.28           N  
ANISOU 3116  NH2 ARG A 430     2986   3736   3641    629    312    396       N  
ATOM   3117  N   SER A 431      84.089  42.970  36.067  1.00 24.89           N  
ANISOU 3117  N   SER A 431     3051   3253   3150    178    557   -230       N  
ATOM   3118  CA  SER A 431      83.915  43.426  37.444  1.00 24.40           C  
ANISOU 3118  CA  SER A 431     2881   3238   3150    163    554   -272       C  
ATOM   3119  C   SER A 431      82.761  44.429  37.570  1.00 24.06           C  
ANISOU 3119  C   SER A 431     2715   3241   3184    117    564   -209       C  
ATOM   3120  O   SER A 431      82.352  45.050  36.584  1.00 24.97           O  
ANISOU 3120  O   SER A 431     2777   3341   3369    149    567   -220       O  
ATOM   3121  CB  SER A 431      85.201  44.098  37.948  1.00 24.39           C  
ANISOU 3121  CB  SER A 431     2726   3315   3224    179    550   -233       C  
ATOM   3122  OG  SER A 431      86.242  43.160  38.192  1.00 25.17           O  
ANISOU 3122  OG  SER A 431     2637   3510   3415    108    410   -309       O  
ATOM   3123  N   ALA A 432      82.275  44.622  38.791  1.00 23.60           N  
ANISOU 3123  N   ALA A 432     2744   3057   3164      8    621   -202       N  
ATOM   3124  CA  ALA A 432      81.322  45.704  39.083  1.00 23.52           C  
ANISOU 3124  CA  ALA A 432     2817   2961   3156     31    592   -101       C  
ATOM   3125  C   ALA A 432      81.947  47.064  38.782  1.00 24.57           C  
ANISOU 3125  C   ALA A 432     3059   3090   3185     16    608    -91       C  
ATOM   3126  O   ALA A 432      83.134  47.281  39.060  1.00 24.52           O  
ANISOU 3126  O   ALA A 432     2975   2992   3349    -82    490    -78       O  
ATOM   3127  CB  ALA A 432      80.918  45.665  40.542  1.00 23.57           C  
ANISOU 3127  CB  ALA A 432     2838   2921   3196     59    657   -111       C  
ATOM   3128  N   GLY A 433      81.151  47.975  38.234  1.00 24.84           N  
ANISOU 3128  N   GLY A 433     3236   3189   3012     46    536      7       N  
ATOM   3129  CA  GLY A 433      81.603  49.353  37.982  1.00 26.11           C  
ANISOU 3129  CA  GLY A 433     3505   3426   2988   -100    667     95       C  
ATOM   3130  C   GLY A 433      82.425  49.455  36.712  1.00 27.72           C  
ANISOU 3130  C   GLY A 433     3795   3675   3063    -70    706    141       C  
ATOM   3131  O   GLY A 433      83.022  50.493  36.398  1.00 28.87           O  
ANISOU 3131  O   GLY A 433     3905   3835   3229   -168    738    160       O  
ATOM   3132  N   SER A 434      82.446  48.364  35.963  1.00 28.32           N  
ANISOU 3132  N   SER A 434     3946   3792   3019    -12    768    130       N  
ATOM   3133  CA  SER A 434      83.196  48.293  34.719  1.00 28.77           C  
ANISOU 3133  CA  SER A 434     4086   4013   2831     18    885    149       C  
ATOM   3134  C   SER A 434      82.354  47.655  33.625  1.00 29.44           C  
ANISOU 3134  C   SER A 434     4114   4184   2887     73    820    178       C  
ATOM   3135  O   SER A 434      81.651  46.677  33.875  1.00 29.16           O  
ANISOU 3135  O   SER A 434     4174   4208   2697    124    869    276       O  
ATOM   3136  CB  SER A 434      84.480  47.486  34.930  1.00 28.70           C  
ANISOU 3136  CB  SER A 434     4032   4055   2815    -26    860    113       C  
ATOM   3137  OG  SER A 434      85.138  47.214  33.698  1.00 30.40           O  
ANISOU 3137  OG  SER A 434     4295   4317   2937    -35    938    -60       O  
ATOM   3138  N   THR A 435      82.458  48.179  32.407  1.00 30.57           N  
ANISOU 3138  N   THR A 435     4367   4398   2850    118    874    130       N  
ATOM   3139  CA  THR A 435      81.743  47.597  31.267  1.00 32.28           C  
ANISOU 3139  CA  THR A 435     4578   4588   3097    192    806     77       C  
ATOM   3140  C   THR A 435      82.639  46.680  30.435  1.00 32.27           C  
ANISOU 3140  C   THR A 435     4586   4629   3044    161    788     43       C  
ATOM   3141  O   THR A 435      82.168  46.046  29.496  1.00 32.70           O  
ANISOU 3141  O   THR A 435     4705   4718   3000    170    686     60       O  
ATOM   3142  CB  THR A 435      81.192  48.673  30.293  1.00 32.78           C  
ANISOU 3142  CB  THR A 435     4628   4639   3189    209    846    113       C  
ATOM   3143  OG1 THR A 435      82.275  49.465  29.797  1.00 32.99           O  
ANISOU 3143  OG1 THR A 435     4658   4540   3336    277   1081     63       O  
ATOM   3144  CG2 THR A 435      80.174  49.580  30.977  1.00 33.49           C  
ANISOU 3144  CG2 THR A 435     4698   4680   3345    438    825    -35       C  
ATOM   3145  N   ALA A 436      83.924  46.609  30.770  1.00 32.40           N  
ANISOU 3145  N   ALA A 436     4609   4652   3048    108    771     40       N  
ATOM   3146  CA  ALA A 436      84.889  45.816  30.006  1.00 32.21           C  
ANISOU 3146  CA  ALA A 436     4538   4704   2994     99    773     31       C  
ATOM   3147  C   ALA A 436      84.878  44.329  30.375  1.00 32.16           C  
ANISOU 3147  C   ALA A 436     4514   4717   2988    126    725      8       C  
ATOM   3148  O   ALA A 436      84.633  43.956  31.528  1.00 31.30           O  
ANISOU 3148  O   ALA A 436     4381   4600   2912     96    756     54       O  
ATOM   3149  CB  ALA A 436      86.285  46.385  30.185  1.00 32.61           C  
ANISOU 3149  CB  ALA A 436     4609   4755   3027     75    862     66       C  
ATOM   3150  N   TYR A 437      85.152  43.492  29.379  1.00 32.34           N  
ANISOU 3150  N   TYR A 437     4460   4784   3044    135    648    -32       N  
ATOM   3151  CA  TYR A 437      85.387  42.063  29.586  1.00 32.33           C  
ANISOU 3151  CA  TYR A 437     4451   4845   2989    168    570   -104       C  
ATOM   3152  C   TYR A 437      86.880  41.764  29.432  1.00 32.22           C  
ANISOU 3152  C   TYR A 437     4430   4909   2903    161    540   -119       C  
ATOM   3153  O   TYR A 437      87.451  42.000  28.371  1.00 31.82           O  
ANISOU 3153  O   TYR A 437     4489   4985   2614    240    583    -31       O  
ATOM   3154  CB  TYR A 437      84.562  41.248  28.578  1.00 32.11           C  
ANISOU 3154  CB  TYR A 437     4409   4840   2952    125    493    -79       C  
ATOM   3155  CG  TYR A 437      83.086  41.292  28.897  1.00 32.97           C  
ANISOU 3155  CG  TYR A 437     4376   4805   3344    146    279    -75       C  
ATOM   3156  CD1 TYR A 437      82.277  42.327  28.428  1.00 33.08           C  
ANISOU 3156  CD1 TYR A 437     4348   4928   3290     68    -87    -21       C  
ATOM   3157  CD2 TYR A 437      82.507  40.323  29.720  1.00 31.98           C  
ANISOU 3157  CD2 TYR A 437     4400   4711   3040    155     71   -175       C  
ATOM   3158  CE1 TYR A 437      80.923  42.382  28.756  1.00 31.40           C  
ANISOU 3158  CE1 TYR A 437     4082   4628   3217    141   -235    -88       C  
ATOM   3159  CE2 TYR A 437      81.154  40.359  30.034  1.00 30.88           C  
ANISOU 3159  CE2 TYR A 437     4002   4401   3331      7   -193   -314       C  
ATOM   3160  CZ  TYR A 437      80.365  41.396  29.550  1.00 31.55           C  
ANISOU 3160  CZ  TYR A 437     4037   4612   3338    -20   -452   -208       C  
ATOM   3161  OH  TYR A 437      79.021  41.457  29.891  1.00 32.00           O  
ANISOU 3161  OH  TYR A 437     4033   4343   3781    146   -414   -189       O  
ATOM   3162  N   ASN A 438      87.520  41.259  30.480  1.00 31.56           N  
ANISOU 3162  N   ASN A 438     4354   4898   2738    185    511   -253       N  
ATOM   3163  CA  ASN A 438      88.926  40.875  30.397  1.00 31.85           C  
ANISOU 3163  CA  ASN A 438     4303   4902   2894    133    427   -380       C  
ATOM   3164  C   ASN A 438      89.095  39.353  30.317  1.00 32.02           C  
ANISOU 3164  C   ASN A 438     4263   4980   2921    131    419   -465       C  
ATOM   3165  O   ASN A 438      88.984  38.636  31.315  1.00 30.82           O  
ANISOU 3165  O   ASN A 438     4103   4838   2769     91    306   -516       O  
ATOM   3166  CB  ASN A 438      89.712  41.465  31.572  1.00 31.48           C  
ANISOU 3166  CB  ASN A 438     4226   4837   2898    151    412   -419       C  
ATOM   3167  CG  ASN A 438      91.213  41.222  31.472  1.00 31.50           C  
ANISOU 3167  CG  ASN A 438     4231   4709   3026    -14    417   -357       C  
ATOM   3168  OD1 ASN A 438      91.698  40.459  30.629  1.00 30.52           O  
ANISOU 3168  OD1 ASN A 438     3881   4555   3160    -61    520   -322       O  
ATOM   3169  ND2 ASN A 438      91.961  41.874  32.358  1.00 30.97           N  
ANISOU 3169  ND2 ASN A 438     3922   4541   3300     66    196   -386       N  
ATOM   3170  N   TYR A 439      89.358  38.873  29.106  1.00 32.55           N  
ANISOU 3170  N   TYR A 439     4238   5127   3000    134    412   -546       N  
ATOM   3171  CA  TYR A 439      89.593  37.457  28.859  1.00 33.46           C  
ANISOU 3171  CA  TYR A 439     4222   5276   3214    203    428   -545       C  
ATOM   3172  C   TYR A 439      91.078  37.106  28.865  1.00 34.59           C  
ANISOU 3172  C   TYR A 439     4236   5380   3525    237    528   -537       C  
ATOM   3173  O   TYR A 439      91.425  35.961  28.574  1.00 34.92           O  
ANISOU 3173  O   TYR A 439     4231   5426   3611    370    495   -547       O  
ATOM   3174  CB  TYR A 439      89.001  37.043  27.505  1.00 33.36           C  
ANISOU 3174  CB  TYR A 439     4293   5302   3078    144    367   -573       C  
ATOM   3175  CG  TYR A 439      87.518  37.317  27.378  1.00 33.93           C  
ANISOU 3175  CG  TYR A 439     4436   5446   3007    150    175   -584       C  
ATOM   3176  CD1 TYR A 439      86.598  36.644  28.183  1.00 34.34           C  
ANISOU 3176  CD1 TYR A 439     4470   5508   3069     -8      1   -646       C  
ATOM   3177  CD2 TYR A 439      87.033  38.236  26.444  1.00 35.09           C  
ANISOU 3177  CD2 TYR A 439     4646   5676   3011    137     28   -525       C  
ATOM   3178  CE1 TYR A 439      85.232  36.892  28.068  1.00 35.42           C  
ANISOU 3178  CE1 TYR A 439     4598   5709   3148   -109    -92   -521       C  
ATOM   3179  CE2 TYR A 439      85.673  38.491  26.327  1.00 34.40           C  
ANISOU 3179  CE2 TYR A 439     4601   5686   2781   -178    -83   -450       C  
ATOM   3180  CZ  TYR A 439      84.778  37.818  27.142  1.00 34.98           C  
ANISOU 3180  CZ  TYR A 439     4715   5827   2747   -196   -148   -460       C  
ATOM   3181  OH  TYR A 439      83.425  38.068  27.036  1.00 32.09           O  
ANISOU 3181  OH  TYR A 439     4627   5583   1979   -455   -212   -410       O  
ATOM   3182  N   GLU A 440      91.943  38.074  29.158  1.00 35.13           N  
ANISOU 3182  N   GLU A 440     4132   5463   3753    214    680   -515       N  
ATOM   3183  CA  GLU A 440      93.382  37.820  29.096  1.00 36.39           C  
ANISOU 3183  CA  GLU A 440     4177   5562   4087    142    790   -463       C  
ATOM   3184  C   GLU A 440      94.054  37.688  30.463  1.00 35.21           C  
ANISOU 3184  C   GLU A 440     3930   5393   4055     42    884   -419       C  
ATOM   3185  O   GLU A 440      94.695  36.662  30.721  1.00 34.97           O  
ANISOU 3185  O   GLU A 440     3819   5406   4060     50    883   -499       O  
ATOM   3186  CB  GLU A 440      94.108  38.824  28.191  1.00 37.28           C  
ANISOU 3186  CB  GLU A 440     4304   5673   4186    135    857   -454       C  
ATOM   3187  CG  GLU A 440      95.591  38.502  27.930  1.00 41.20           C  
ANISOU 3187  CG  GLU A 440     4746   6072   4835    547    752   -657       C  
ATOM   3188  CD  GLU A 440      95.838  37.127  27.299  1.00 45.77           C  
ANISOU 3188  CD  GLU A 440     5455   6564   5371    788    661   -919       C  
ATOM   3189  OE1 GLU A 440      95.167  36.771  26.302  1.00 46.59           O  
ANISOU 3189  OE1 GLU A 440     5631   6863   5207    913    603   -983       O  
ATOM   3190  OE2 GLU A 440      96.719  36.392  27.807  1.00 48.24           O  
ANISOU 3190  OE2 GLU A 440     5868   6633   5827    995    595   -875       O  
ATOM   3191  N   ASP A 441      93.901  38.691  31.327  1.00 33.56           N  
ANISOU 3191  N   ASP A 441     3581   5124   4044    -70   1018   -357       N  
ATOM   3192  CA  ASP A 441      94.541  38.657  32.644  1.00 32.45           C  
ANISOU 3192  CA  ASP A 441     3415   4889   4024   -108   1116   -270       C  
ATOM   3193  C   ASP A 441      93.679  39.172  33.799  1.00 31.35           C  
ANISOU 3193  C   ASP A 441     3312   4673   3925   -118   1126   -297       C  
ATOM   3194  O   ASP A 441      94.117  40.001  34.606  1.00 30.79           O  
ANISOU 3194  O   ASP A 441     3254   4637   3807   -174   1145   -236       O  
ATOM   3195  CB  ASP A 441      95.912  39.347  32.606  1.00 33.15           C  
ANISOU 3195  CB  ASP A 441     3433   4981   4180   -139   1044   -227       C  
ATOM   3196  CG  ASP A 441      95.845  40.804  32.156  1.00 34.66           C  
ANISOU 3196  CG  ASP A 441     3437   5166   4566   -201   1070      3       C  
ATOM   3197  OD1 ASP A 441      94.743  41.355  31.945  1.00 35.34           O  
ANISOU 3197  OD1 ASP A 441     3462   5195   4767     -7   1108    226       O  
ATOM   3198  OD2 ASP A 441      96.925  41.416  32.034  1.00 36.93           O  
ANISOU 3198  OD2 ASP A 441     3543   5561   4926   -401   1231    176       O  
ATOM   3199  N   PRO A 442      92.440  38.670  33.891  1.00 29.76           N  
ANISOU 3199  N   PRO A 442     3104   4417   3787   -112   1243   -348       N  
ATOM   3200  CA  PRO A 442      91.567  39.134  34.968  1.00 29.38           C  
ANISOU 3200  CA  PRO A 442     3141   4309   3710    -84   1190   -399       C  
ATOM   3201  C   PRO A 442      92.027  38.498  36.268  1.00 29.21           C  
ANISOU 3201  C   PRO A 442     3119   4193   3786    -58   1122   -412       C  
ATOM   3202  O   PRO A 442      92.679  37.456  36.242  1.00 29.47           O  
ANISOU 3202  O   PRO A 442     3312   4116   3769     34    996   -379       O  
ATOM   3203  CB  PRO A 442      90.199  38.573  34.575  1.00 29.03           C  
ANISOU 3203  CB  PRO A 442     3034   4282   3710   -107   1261   -431       C  
ATOM   3204  CG  PRO A 442      90.535  37.314  33.826  1.00 28.82           C  
ANISOU 3204  CG  PRO A 442     2966   4296   3685   -160   1334   -365       C  
ATOM   3205  CD  PRO A 442      91.752  37.714  33.007  1.00 29.58           C  
ANISOU 3205  CD  PRO A 442     3074   4419   3745   -127   1287   -387       C  
ATOM   3206  N   VAL A 443      91.703  39.150  37.378  1.00 29.10           N  
ANISOU 3206  N   VAL A 443     3132   4115   3809    -60   1047   -442       N  
ATOM   3207  CA  VAL A 443      91.999  38.639  38.706  1.00 28.80           C  
ANISOU 3207  CA  VAL A 443     3070   3984   3886     -1    972   -448       C  
ATOM   3208  C   VAL A 443      91.234  37.338  38.961  1.00 28.85           C  
ANISOU 3208  C   VAL A 443     3096   3889   3974    100    985   -531       C  
ATOM   3209  O   VAL A 443      90.125  37.141  38.446  1.00 28.36           O  
ANISOU 3209  O   VAL A 443     3036   3809   3928    144    877   -573       O  
ATOM   3210  CB  VAL A 443      91.661  39.712  39.776  1.00 28.89           C  
ANISOU 3210  CB  VAL A 443     3076   4061   3839     -3    995   -454       C  
ATOM   3211  CG1 VAL A 443      90.169  40.046  39.815  1.00 28.95           C  
ANISOU 3211  CG1 VAL A 443     3040   4102   3857    -91    892   -417       C  
ATOM   3212  CG2 VAL A 443      92.188  39.324  41.156  1.00 29.60           C  
ANISOU 3212  CG2 VAL A 443     3127   4087   4031     18    858   -342       C  
ATOM   3213  N   TRP A 444      91.852  36.451  39.738  1.00 28.38           N  
ANISOU 3213  N   TRP A 444     3039   3758   3983    175    991   -536       N  
ATOM   3214  CA  TRP A 444      91.200  35.238  40.214  1.00 28.63           C  
ANISOU 3214  CA  TRP A 444     3021   3751   4104    166   1067   -557       C  
ATOM   3215  C   TRP A 444      90.816  35.509  41.658  1.00 26.99           C  
ANISOU 3215  C   TRP A 444     2793   3474   3986    167    985   -510       C  
ATOM   3216  O   TRP A 444      91.620  36.044  42.416  1.00 26.68           O  
ANISOU 3216  O   TRP A 444     2635   3583   3919     40   1026   -506       O  
ATOM   3217  CB  TRP A 444      92.141  34.033  40.117  1.00 30.68           C  
ANISOU 3217  CB  TRP A 444     3373   3831   4453    196    992   -577       C  
ATOM   3218  CG  TRP A 444      92.260  33.574  38.694  1.00 36.16           C  
ANISOU 3218  CG  TRP A 444     4101   4596   5041    192   1247   -731       C  
ATOM   3219  CD1 TRP A 444      92.929  34.203  37.680  1.00 41.16           C  
ANISOU 3219  CD1 TRP A 444     4934   4917   5786     83   1357   -650       C  
ATOM   3220  CD2 TRP A 444      91.635  32.427  38.110  1.00 41.47           C  
ANISOU 3220  CD2 TRP A 444     4728   5084   5945    -17   1119   -816       C  
ATOM   3221  NE1 TRP A 444      92.767  33.512  36.502  1.00 43.54           N  
ANISOU 3221  NE1 TRP A 444     5099   5277   6164    -68   1046   -878       N  
ATOM   3222  CE2 TRP A 444      91.978  32.416  36.740  1.00 43.56           C  
ANISOU 3222  CE2 TRP A 444     5006   5381   6160     -2   1128   -746       C  
ATOM   3223  CE3 TRP A 444      90.816  31.406  38.612  1.00 43.27           C  
ANISOU 3223  CE3 TRP A 444     5033   5220   6186     -3   1170   -577       C  
ATOM   3224  CZ2 TRP A 444      91.542  31.413  35.868  1.00 44.94           C  
ANISOU 3224  CZ2 TRP A 444     5198   5486   6390     17    920   -842       C  
ATOM   3225  CZ3 TRP A 444      90.377  30.410  37.740  1.00 44.72           C  
ANISOU 3225  CZ3 TRP A 444     5192   5485   6315     81   1136   -705       C  
ATOM   3226  CH2 TRP A 444      90.744  30.422  36.386  1.00 45.96           C  
ANISOU 3226  CH2 TRP A 444     5436   5736   6291     35   1026   -626       C  
ATOM   3227  N   ARG A 445      89.581  35.193  42.031  1.00 24.93           N  
ANISOU 3227  N   ARG A 445     2479   3122   3871    217    938   -444       N  
ATOM   3228  CA  ARG A 445      89.217  35.319  43.434  1.00 23.86           C  
ANISOU 3228  CA  ARG A 445     2297   2992   3776    271    830   -359       C  
ATOM   3229  C   ARG A 445      88.076  34.372  43.808  1.00 23.35           C  
ANISOU 3229  C   ARG A 445     2183   2911   3774    279    733   -305       C  
ATOM   3230  O   ARG A 445      87.715  33.516  43.002  1.00 23.35           O  
ANISOU 3230  O   ARG A 445     2191   2849   3830    278    748   -284       O  
ATOM   3231  CB  ARG A 445      88.929  36.781  43.800  1.00 24.53           C  
ANISOU 3231  CB  ARG A 445     2428   3041   3850    209    731   -306       C  
ATOM   3232  CG  ARG A 445      87.653  37.419  43.275  1.00 24.10           C  
ANISOU 3232  CG  ARG A 445     2357   2995   3804    458    537   -331       C  
ATOM   3233  CD  ARG A 445      87.632  38.931  43.634  1.00 22.19           C  
ANISOU 3233  CD  ARG A 445     2317   2726   3388    -73    402   -209       C  
ATOM   3234  NE  ARG A 445      88.079  39.155  45.016  1.00 20.18           N  
ANISOU 3234  NE  ARG A 445     1525   2619   3523    211    270   -297       N  
ATOM   3235  CZ  ARG A 445      88.579  40.287  45.506  1.00 20.15           C  
ANISOU 3235  CZ  ARG A 445     1557   2778   3319    352    494   -246       C  
ATOM   3236  NH1 ARG A 445      88.689  41.387  44.760  1.00 22.40           N  
ANISOU 3236  NH1 ARG A 445     1797   2710   4001     80    226    -78       N  
ATOM   3237  NH2 ARG A 445      88.997  40.318  46.763  1.00 17.78           N  
ANISOU 3237  NH2 ARG A 445      643   2763   3347    400    442   -398       N  
ATOM   3238  N   ASP A 446      87.555  34.472  45.030  1.00 21.49           N  
ANISOU 3238  N   ASP A 446     1892   2681   3590    401    712   -270       N  
ATOM   3239  CA  ASP A 446      86.432  33.596  45.397  1.00 21.37           C  
ANISOU 3239  CA  ASP A 446     1801   2707   3609    408    551   -299       C  
ATOM   3240  C   ASP A 446      85.177  34.291  45.918  1.00 20.77           C  
ANISOU 3240  C   ASP A 446     1805   2614   3472    403    474   -374       C  
ATOM   3241  O   ASP A 446      84.163  33.623  46.139  1.00 20.80           O  
ANISOU 3241  O   ASP A 446     1809   2739   3352    382    555   -345       O  
ATOM   3242  CB  ASP A 446      86.842  32.431  46.319  1.00 20.95           C  
ANISOU 3242  CB  ASP A 446     1764   2540   3653    399    554   -249       C  
ATOM   3243  CG  ASP A 446      87.410  32.893  47.657  1.00 22.61           C  
ANISOU 3243  CG  ASP A 446     1898   2898   3791    617    556   -113       C  
ATOM   3244  OD1 ASP A 446      86.828  33.796  48.297  1.00 23.62           O  
ANISOU 3244  OD1 ASP A 446     1825   2918   4230    888    199    -50       O  
ATOM   3245  OD2 ASP A 446      88.455  32.349  48.087  1.00 26.26           O  
ANISOU 3245  OD2 ASP A 446     2150   3280   4546    892    600     75       O  
ATOM   3246  N   VAL A 447      85.241  35.611  46.105  1.00 19.85           N  
ANISOU 3246  N   VAL A 447     1718   2543   3281    437    293   -399       N  
ATOM   3247  CA  VAL A 447      84.073  36.423  46.479  1.00 19.06           C  
ANISOU 3247  CA  VAL A 447     1688   2414   3137    413    204   -425       C  
ATOM   3248  C   VAL A 447      84.161  37.662  45.603  1.00 19.32           C  
ANISOU 3248  C   VAL A 447     1721   2409   3209    379    159   -351       C  
ATOM   3249  O   VAL A 447      85.227  38.292  45.545  1.00 19.27           O  
ANISOU 3249  O   VAL A 447     1510   2503   3308    451    124   -189       O  
ATOM   3250  CB  VAL A 447      84.118  36.891  47.953  1.00 18.63           C  
ANISOU 3250  CB  VAL A 447     1635   2337   3104    404    185   -503       C  
ATOM   3251  CG1 VAL A 447      82.965  37.853  48.263  1.00 18.53           C  
ANISOU 3251  CG1 VAL A 447     1599   2139   3301    225     80   -621       C  
ATOM   3252  CG2 VAL A 447      84.079  35.713  48.906  1.00 19.52           C  
ANISOU 3252  CG2 VAL A 447     1903   2427   3084    508    226   -487       C  
ATOM   3253  N   VAL A 448      83.061  38.012  44.938  1.00 18.94           N  
ANISOU 3253  N   VAL A 448     1698   2421   3073    307    146   -301       N  
ATOM   3254  CA  VAL A 448      83.044  39.151  44.019  1.00 18.51           C  
ANISOU 3254  CA  VAL A 448     1738   2352   2942    190    227   -258       C  
ATOM   3255  C   VAL A 448      81.768  39.976  44.184  1.00 18.88           C  
ANISOU 3255  C   VAL A 448     1798   2325   3050    191    211   -250       C  
ATOM   3256  O   VAL A 448      80.656  39.423  44.224  1.00 18.75           O  
ANISOU 3256  O   VAL A 448     1789   2247   3086    133    318   -126       O  
ATOM   3257  CB  VAL A 448      83.211  38.675  42.548  1.00 19.11           C  
ANISOU 3257  CB  VAL A 448     1897   2404   2960     84    187   -166       C  
ATOM   3258  CG1 VAL A 448      82.046  37.762  42.130  1.00 18.16           C  
ANISOU 3258  CG1 VAL A 448     1708   2581   2610     67    199   -320       C  
ATOM   3259  CG2 VAL A 448      83.423  39.867  41.576  1.00 18.85           C  
ANISOU 3259  CG2 VAL A 448     2012   2429   2719    132    330    -99       C  
ATOM   3260  N   SER A 449      81.918  41.298  44.285  1.00 18.45           N  
ANISOU 3260  N   SER A 449     1726   2312   2970    217    272   -234       N  
ATOM   3261  CA  SER A 449      80.748  42.172  44.311  1.00 18.96           C  
ANISOU 3261  CA  SER A 449     1755   2323   3123    306      5   -291       C  
ATOM   3262  C   SER A 449      80.054  42.087  42.961  1.00 19.33           C  
ANISOU 3262  C   SER A 449     1795   2372   3176    257     -1   -348       C  
ATOM   3263  O   SER A 449      80.711  42.181  41.928  1.00 19.69           O  
ANISOU 3263  O   SER A 449     1877   2438   3163    257   -109   -450       O  
ATOM   3264  CB  SER A 449      81.126  43.631  44.578  1.00 19.07           C  
ANISOU 3264  CB  SER A 449     1753   2331   3161    376     31   -259       C  
ATOM   3265  OG  SER A 449      79.994  44.467  44.380  1.00 19.56           O  
ANISOU 3265  OG  SER A 449     1640   2403   3388    376    -39   -487       O  
ATOM   3266  N   THR A 450      78.741  41.886  42.983  1.00 19.39           N  
ANISOU 3266  N   THR A 450     1703   2369   3295    343    -77   -384       N  
ATOM   3267  CA  THR A 450      77.936  41.923  41.764  1.00 20.32           C  
ANISOU 3267  CA  THR A 450     1786   2522   3413    266    -74   -322       C  
ATOM   3268  C   THR A 450      77.403  43.318  41.428  1.00 21.18           C  
ANISOU 3268  C   THR A 450     1798   2734   3516    261    -42   -272       C  
ATOM   3269  O   THR A 450      76.645  43.474  40.465  1.00 22.24           O  
ANISOU 3269  O   THR A 450     1799   2932   3717    318   -165   -244       O  
ATOM   3270  CB  THR A 450      76.817  40.853  41.806  1.00 20.08           C  
ANISOU 3270  CB  THR A 450     1725   2488   3415    333    -42   -370       C  
ATOM   3271  OG1 THR A 450      75.925  41.120  42.893  1.00 20.39           O  
ANISOU 3271  OG1 THR A 450     1645   2591   3511    143   -137   -391       O  
ATOM   3272  CG2 THR A 450      77.437  39.456  41.985  1.00 20.26           C  
ANISOU 3272  CG2 THR A 450     1955   2412   3331    268   -201   -172       C  
ATOM   3273  N   GLY A 451      77.820  44.336  42.182  1.00 21.68           N  
ANISOU 3273  N   GLY A 451     1845   2798   3593    222    -23   -201       N  
ATOM   3274  CA  GLY A 451      77.491  45.722  41.832  1.00 22.15           C  
ANISOU 3274  CA  GLY A 451     1920   2845   3650    205   -117   -187       C  
ATOM   3275  C   GLY A 451      76.021  46.119  41.858  1.00 22.19           C  
ANISOU 3275  C   GLY A 451     1997   2872   3561    183   -219   -128       C  
ATOM   3276  O   GLY A 451      75.254  45.617  42.676  1.00 21.97           O  
ANISOU 3276  O   GLY A 451     1830   2825   3691     37   -204   -153       O  
ATOM   3277  N   THR A 452      75.636  47.033  40.969  1.00 23.26           N  
ANISOU 3277  N   THR A 452     2268   2978   3590    164   -269   -162       N  
ATOM   3278  CA  THR A 452      74.331  47.690  41.034  1.00 23.28           C  
ANISOU 3278  CA  THR A 452     2310   2922   3611     82   -517    -26       C  
ATOM   3279  C   THR A 452      73.704  47.829  39.660  1.00 23.71           C  
ANISOU 3279  C   THR A 452     2337   2948   3725    118   -558     64       C  
ATOM   3280  O   THR A 452      74.417  47.960  38.661  1.00 22.82           O  
ANISOU 3280  O   THR A 452     2182   2838   3650    154   -567     54       O  
ATOM   3281  CB  THR A 452      74.435  49.121  41.620  1.00 24.49           C  
ANISOU 3281  CB  THR A 452     2689   3048   3567    -42   -426    -42       C  
ATOM   3282  OG1 THR A 452      75.255  49.939  40.771  1.00 27.76           O  
ANISOU 3282  OG1 THR A 452     3165   3222   4158   -196   -338   -129       O  
ATOM   3283  CG2 THR A 452      75.104  49.073  42.982  1.00 24.64           C  
ANISOU 3283  CG2 THR A 452     2477   3155   3728   -134   -670   -200       C  
ATOM   3284  N   PRO A 453      72.361  47.834  39.612  1.00 23.87           N  
ANISOU 3284  N   PRO A 453     2213   3050   3804    209   -680    246       N  
ATOM   3285  CA  PRO A 453      71.723  48.039  38.318  1.00 25.03           C  
ANISOU 3285  CA  PRO A 453     2381   3196   3931    274   -706    392       C  
ATOM   3286  C   PRO A 453      71.856  49.488  37.848  1.00 26.21           C  
ANISOU 3286  C   PRO A 453     2549   3339   4071    341   -678    522       C  
ATOM   3287  O   PRO A 453      71.688  49.751  36.654  1.00 27.58           O  
ANISOU 3287  O   PRO A 453     2851   3471   4155    428   -766    668       O  
ATOM   3288  CB  PRO A 453      70.257  47.678  38.586  1.00 24.31           C  
ANISOU 3288  CB  PRO A 453     2164   3174   3896    286   -719    340       C  
ATOM   3289  CG  PRO A 453      70.061  47.949  40.047  1.00 23.92           C  
ANISOU 3289  CG  PRO A 453     2056   3178   3855    247   -793    378       C  
ATOM   3290  CD  PRO A 453      71.385  47.630  40.701  1.00 24.20           C  
ANISOU 3290  CD  PRO A 453     2192   3087   3912    203   -710    223       C  
ATOM   3291  N   ALA A 454      72.135  50.411  38.767  1.00 26.81           N  
ANISOU 3291  N   ALA A 454     2611   3332   4241    382   -665    593       N  
ATOM   3292  CA  ALA A 454      72.419  51.801  38.406  1.00 28.30           C  
ANISOU 3292  CA  ALA A 454     2823   3529   4397    339   -545    641       C  
ATOM   3293  C   ALA A 454      73.565  51.873  37.399  1.00 29.11           C  
ANISOU 3293  C   ALA A 454     3027   3611   4421    334   -503    710       C  
ATOM   3294  O   ALA A 454      73.577  52.757  36.542  1.00 30.22           O  
ANISOU 3294  O   ALA A 454     3234   3681   4567    356   -555    817       O  
ATOM   3295  CB  ALA A 454      72.750  52.627  39.649  1.00 28.39           C  
ANISOU 3295  CB  ALA A 454     2949   3417   4420    363   -511    625       C  
ATOM   3296  N   ALA A 455      74.527  50.960  37.521  1.00 28.68           N  
ANISOU 3296  N   ALA A 455     2940   3544   4410    345   -367    616       N  
ATOM   3297  CA  ALA A 455      75.703  50.953  36.657  1.00 28.70           C  
ANISOU 3297  CA  ALA A 455     3039   3612   4252    321   -327    513       C  
ATOM   3298  C   ALA A 455      75.534  50.022  35.461  1.00 28.96           C  
ANISOU 3298  C   ALA A 455     3072   3745   4185    306   -288    449       C  
ATOM   3299  O   ALA A 455      76.454  49.884  34.654  1.00 29.41           O  
ANISOU 3299  O   ALA A 455     3175   3843   4156    194   -201    478       O  
ATOM   3300  CB  ALA A 455      76.950  50.575  37.465  1.00 28.23           C  
ANISOU 3300  CB  ALA A 455     2861   3547   4318    316   -257    613       C  
ATOM   3301  N   GLY A 456      74.384  49.358  35.360  1.00 28.53           N  
ANISOU 3301  N   GLY A 456     3057   3755   4026    313   -285    286       N  
ATOM   3302  CA  GLY A 456      74.172  48.338  34.328  1.00 28.23           C  
ANISOU 3302  CA  GLY A 456     3098   3844   3782    392   -270    180       C  
ATOM   3303  C   GLY A 456      75.175  47.206  34.491  1.00 27.50           C  
ANISOU 3303  C   GLY A 456     3102   3794   3553    383   -287    112       C  
ATOM   3304  O   GLY A 456      75.691  46.653  33.513  1.00 28.36           O  
ANISOU 3304  O   GLY A 456     3207   3945   3623    404   -277     92       O  
ATOM   3305  N   ASP A 457      75.478  46.865  35.736  1.00 26.18           N  
ANISOU 3305  N   ASP A 457     2989   3701   3257    391   -250     87       N  
ATOM   3306  CA  ASP A 457      76.524  45.880  36.012  1.00 25.26           C  
ANISOU 3306  CA  ASP A 457     2983   3571   3042    381   -223    -14       C  
ATOM   3307  C   ASP A 457      76.099  44.486  35.572  1.00 25.32           C  
ANISOU 3307  C   ASP A 457     3023   3605   2992    394   -264    -24       C  
ATOM   3308  O   ASP A 457      74.919  44.134  35.636  1.00 25.31           O  
ANISOU 3308  O   ASP A 457     2927   3508   3178    436   -219    -26       O  
ATOM   3309  CB  ASP A 457      76.870  45.855  37.503  1.00 23.87           C  
ANISOU 3309  CB  ASP A 457     2678   3595   2796    315   -248    -28       C  
ATOM   3310  CG  ASP A 457      77.852  46.944  37.904  1.00 23.45           C  
ANISOU 3310  CG  ASP A 457     2920   3240   2746    354     85    -61       C  
ATOM   3311  OD1 ASP A 457      78.778  47.281  37.123  1.00 22.94           O  
ANISOU 3311  OD1 ASP A 457     2552   3320   2844    112     -7    -29       O  
ATOM   3312  OD2 ASP A 457      77.727  47.430  39.050  1.00 22.13           O  
ANISOU 3312  OD2 ASP A 457     2390   3385   2633     25    106   -262       O  
ATOM   3313  N   ASN A 458      77.065  43.688  35.129  1.00 24.32           N  
ANISOU 3313  N   ASN A 458     2952   3519   2769    411   -311   -134       N  
ATOM   3314  CA  ASN A 458      76.776  42.298  34.798  1.00 24.73           C  
ANISOU 3314  CA  ASN A 458     3084   3589   2723    357   -314   -164       C  
ATOM   3315  C   ASN A 458      78.041  41.492  35.031  1.00 24.95           C  
ANISOU 3315  C   ASN A 458     3165   3521   2793    307   -224   -207       C  
ATOM   3316  O   ASN A 458      78.730  41.087  34.091  1.00 24.93           O  
ANISOU 3316  O   ASN A 458     3109   3554   2807    353   -167   -199       O  
ATOM   3317  CB  ASN A 458      76.284  42.174  33.352  1.00 25.30           C  
ANISOU 3317  CB  ASN A 458     3189   3665   2756    228   -432   -287       C  
ATOM   3318  CG  ASN A 458      75.630  40.835  33.079  1.00 26.27           C  
ANISOU 3318  CG  ASN A 458     3559   3712   2709    269   -514   -252       C  
ATOM   3319  OD1 ASN A 458      75.638  39.940  33.926  1.00 25.59           O  
ANISOU 3319  OD1 ASN A 458     3619   3624   2478    590   -852   -255       O  
ATOM   3320  ND2 ASN A 458      75.040  40.702  31.903  1.00 26.62           N  
ANISOU 3320  ND2 ASN A 458     3574   3943   2597    189   -766   -394       N  
ATOM   3321  N   VAL A 459      78.346  41.316  36.314  1.00 23.80           N  
ANISOU 3321  N   VAL A 459     2955   3382   2704    307   -172   -108       N  
ATOM   3322  CA  VAL A 459      79.579  40.678  36.733  1.00 23.61           C  
ANISOU 3322  CA  VAL A 459     2958   3333   2679    305    -17   -203       C  
ATOM   3323  C   VAL A 459      79.556  39.243  36.233  1.00 24.37           C  
ANISOU 3323  C   VAL A 459     3003   3395   2859    381     90   -194       C  
ATOM   3324  O   VAL A 459      78.537  38.557  36.364  1.00 24.21           O  
ANISOU 3324  O   VAL A 459     2706   3411   3079    416     84   -246       O  
ATOM   3325  CB  VAL A 459      79.700  40.782  38.262  1.00 23.02           C  
ANISOU 3325  CB  VAL A 459     2921   3276   2549    262    -54   -217       C  
ATOM   3326  CG1 VAL A 459      80.779  39.838  38.786  1.00 22.03           C  
ANISOU 3326  CG1 VAL A 459     2731   3158   2478    172    -42   -166       C  
ATOM   3327  CG2 VAL A 459      79.957  42.249  38.641  1.00 21.76           C  
ANISOU 3327  CG2 VAL A 459     2824   3186   2258    380    143   -300       C  
ATOM   3328  N   THR A 460      80.675  38.823  35.645  1.00 24.59           N  
ANISOU 3328  N   THR A 460     2971   3437   2935    436    240   -275       N  
ATOM   3329  CA  THR A 460      80.766  37.581  34.893  1.00 25.47           C  
ANISOU 3329  CA  THR A 460     3180   3437   3060    465    286   -295       C  
ATOM   3330  C   THR A 460      82.070  36.891  35.274  1.00 25.04           C  
ANISOU 3330  C   THR A 460     3096   3474   2941    472    435   -346       C  
ATOM   3331  O   THR A 460      83.130  37.528  35.330  1.00 24.52           O  
ANISOU 3331  O   THR A 460     3039   3423   2854    508    441   -285       O  
ATOM   3332  CB  THR A 460      80.696  37.855  33.373  1.00 25.97           C  
ANISOU 3332  CB  THR A 460     3275   3472   3120    479    317   -386       C  
ATOM   3333  OG1 THR A 460      79.470  38.535  33.085  1.00 27.03           O  
ANISOU 3333  OG1 THR A 460     3444   3336   3491    518    161   -588       O  
ATOM   3334  CG2 THR A 460      80.739  36.570  32.556  1.00 26.51           C  
ANISOU 3334  CG2 THR A 460     3429   3300   3341    320    224   -282       C  
ATOM   3335  N   ILE A 461      81.965  35.601  35.591  1.00 24.04           N  
ANISOU 3335  N   ILE A 461     2951   3441   2742    469    517   -318       N  
ATOM   3336  CA  ILE A 461      83.117  34.839  36.067  1.00 23.90           C  
ANISOU 3336  CA  ILE A 461     3020   3438   2621    392    554   -325       C  
ATOM   3337  C   ILE A 461      83.273  33.516  35.325  1.00 24.78           C  
ANISOU 3337  C   ILE A 461     3089   3507   2820    364    625   -366       C  
ATOM   3338  O   ILE A 461      82.283  32.966  34.830  1.00 24.64           O  
ANISOU 3338  O   ILE A 461     2960   3430   2970    286    560   -322       O  
ATOM   3339  CB  ILE A 461      83.012  34.564  37.575  1.00 22.91           C  
ANISOU 3339  CB  ILE A 461     2863   3423   2416    411    567   -341       C  
ATOM   3340  CG1 ILE A 461      81.908  33.542  37.848  1.00 21.52           C  
ANISOU 3340  CG1 ILE A 461     2933   3576   1667    291    493   -261       C  
ATOM   3341  CG2 ILE A 461      82.808  35.877  38.337  1.00 22.80           C  
ANISOU 3341  CG2 ILE A 461     2865   3231   2564    305    544   -330       C  
ATOM   3342  CD1 ILE A 461      81.756  33.182  39.320  1.00 18.95           C  
ANISOU 3342  CD1 ILE A 461     2081   3626   1491    319    396   -207       C  
ATOM   3343  N   ARG A 462      84.512  33.023  35.258  1.00 25.19           N  
ANISOU 3343  N   ARG A 462     3080   3548   2941    373    705   -432       N  
ATOM   3344  CA  ARG A 462      84.792  31.722  34.655  1.00 25.82           C  
ANISOU 3344  CA  ARG A 462     3203   3589   3016    332    877   -488       C  
ATOM   3345  C   ARG A 462      85.601  30.794  35.552  1.00 26.54           C  
ANISOU 3345  C   ARG A 462     3226   3526   3330    337    817   -578       C  
ATOM   3346  O   ARG A 462      86.467  31.244  36.307  1.00 27.07           O  
ANISOU 3346  O   ARG A 462     3270   3594   3419    365    810   -612       O  
ATOM   3347  CB  ARG A 462      85.522  31.891  33.322  1.00 25.97           C  
ANISOU 3347  CB  ARG A 462     3228   3671   2966    248    931   -481       C  
ATOM   3348  CG  ARG A 462      84.606  32.362  32.205  1.00 25.76           C  
ANISOU 3348  CG  ARG A 462     3300   3957   2529    265   1183   -290       C  
ATOM   3349  CD  ARG A 462      85.404  32.498  30.902  1.00 27.61           C  
ANISOU 3349  CD  ARG A 462     3131   4531   2828     92   1434   -241       C  
ATOM   3350  NE  ARG A 462      84.582  33.044  29.822  1.00 28.62           N  
ANISOU 3350  NE  ARG A 462     3290   4659   2923   -244   1284   -282       N  
ATOM   3351  CZ  ARG A 462      84.917  33.023  28.536  1.00 30.53           C  
ANISOU 3351  CZ  ARG A 462     3578   5001   3021   -244   1021   -211       C  
ATOM   3352  NH1 ARG A 462      86.063  32.468  28.148  1.00 31.67           N  
ANISOU 3352  NH1 ARG A 462     3585   5180   3268   -247   1204   -399       N  
ATOM   3353  NH2 ARG A 462      84.092  33.548  27.642  1.00 32.59           N  
ANISOU 3353  NH2 ARG A 462     3723   5061   3596   -126    692    -13       N  
ATOM   3354  N   PHE A 463      85.306  29.499  35.461  1.00 27.24           N  
ANISOU 3354  N   PHE A 463     3299   3439   3610    339    762   -645       N  
ATOM   3355  CA  PHE A 463      86.107  28.457  36.107  1.00 27.90           C  
ANISOU 3355  CA  PHE A 463     3436   3319   3846    303    707   -688       C  
ATOM   3356  C   PHE A 463      85.976  27.139  35.356  1.00 28.76           C  
ANISOU 3356  C   PHE A 463     3558   3296   4073    362    741   -704       C  
ATOM   3357  O   PHE A 463      85.220  27.041  34.381  1.00 28.03           O  
ANISOU 3357  O   PHE A 463     3544   3133   3973    339    675   -674       O  
ATOM   3358  CB  PHE A 463      85.715  28.280  37.576  1.00 27.43           C  
ANISOU 3358  CB  PHE A 463     3352   3270   3800    219    724   -649       C  
ATOM   3359  CG  PHE A 463      84.281  27.872  37.779  1.00 27.28           C  
ANISOU 3359  CG  PHE A 463     3238   3364   3762    291    622   -689       C  
ATOM   3360  CD1 PHE A 463      83.254  28.805  37.678  1.00 26.66           C  
ANISOU 3360  CD1 PHE A 463     3010   3587   3530    288    488   -447       C  
ATOM   3361  CD2 PHE A 463      83.963  26.553  38.073  1.00 26.63           C  
ANISOU 3361  CD2 PHE A 463     3170   3406   3542    218    647   -527       C  
ATOM   3362  CE1 PHE A 463      81.935  28.422  37.857  1.00 25.98           C  
ANISOU 3362  CE1 PHE A 463     2931   3639   3301    162    295   -568       C  
ATOM   3363  CE2 PHE A 463      82.636  26.159  38.246  1.00 26.01           C  
ANISOU 3363  CE2 PHE A 463     3054   3338   3488    287    462   -673       C  
ATOM   3364  CZ  PHE A 463      81.627  27.096  38.144  1.00 26.12           C  
ANISOU 3364  CZ  PHE A 463     2924   3504   3494    384    274   -499       C  
ATOM   3365  N   VAL A 464      86.727  26.141  35.819  1.00 29.69           N  
ANISOU 3365  N   VAL A 464     3654   3308   4317    393    726   -696       N  
ATOM   3366  CA  VAL A 464      86.684  24.805  35.235  1.00 31.32           C  
ANISOU 3366  CA  VAL A 464     3870   3394   4633    489    728   -765       C  
ATOM   3367  C   VAL A 464      86.187  23.817  36.288  1.00 31.83           C  
ANISOU 3367  C   VAL A 464     3900   3454   4739    465    696   -739       C  
ATOM   3368  O   VAL A 464      86.551  23.928  37.463  1.00 32.10           O  
ANISOU 3368  O   VAL A 464     3860   3486   4850    479    654   -797       O  
ATOM   3369  CB  VAL A 464      88.068  24.362  34.693  1.00 31.56           C  
ANISOU 3369  CB  VAL A 464     3854   3421   4717    474    779   -722       C  
ATOM   3370  CG1 VAL A 464      88.005  22.925  34.184  1.00 31.59           C  
ANISOU 3370  CG1 VAL A 464     3860   3393   4748    560    639   -856       C  
ATOM   3371  CG2 VAL A 464      88.521  25.263  33.557  1.00 32.40           C  
ANISOU 3371  CG2 VAL A 464     4295   3287   4728    451    658   -710       C  
ATOM   3372  N   THR A 465      85.350  22.869  35.869  1.00 32.35           N  
ANISOU 3372  N   THR A 465     3928   3513   4849    481    645   -764       N  
ATOM   3373  CA  THR A 465      84.762  21.892  36.785  1.00 32.54           C  
ANISOU 3373  CA  THR A 465     3946   3536   4881    502    628   -756       C  
ATOM   3374  C   THR A 465      85.688  20.697  37.025  1.00 33.05           C  
ANISOU 3374  C   THR A 465     3964   3592   5001    516    609   -746       C  
ATOM   3375  O   THR A 465      85.454  19.588  36.537  1.00 33.71           O  
ANISOU 3375  O   THR A 465     4168   3689   4951    623    641   -785       O  
ATOM   3376  CB  THR A 465      83.379  21.411  36.303  1.00 32.32           C  
ANISOU 3376  CB  THR A 465     3930   3501   4846    456    636   -788       C  
ATOM   3377  OG1 THR A 465      83.446  21.127  34.903  1.00 33.74           O  
ANISOU 3377  OG1 THR A 465     4366   3626   4827    312    609   -697       O  
ATOM   3378  CG2 THR A 465      82.331  22.480  36.541  1.00 31.73           C  
ANISOU 3378  CG2 THR A 465     3968   3341   4744    502    578   -825       C  
ATOM   3379  N   ASP A 466      86.735  20.950  37.803  1.00 32.71           N  
ANISOU 3379  N   ASP A 466     3739   3627   5059    563    640   -690       N  
ATOM   3380  CA  ASP A 466      87.767  19.971  38.129  1.00 32.61           C  
ANISOU 3380  CA  ASP A 466     3573   3647   5166    529    668   -693       C  
ATOM   3381  C   ASP A 466      87.562  19.404  39.536  1.00 31.48           C  
ANISOU 3381  C   ASP A 466     3386   3436   5137    544    697   -689       C  
ATOM   3382  O   ASP A 466      88.504  18.896  40.146  1.00 31.28           O  
ANISOU 3382  O   ASP A 466     3241   3421   5222    609    746   -708       O  
ATOM   3383  CB  ASP A 466      89.137  20.663  38.051  1.00 33.56           C  
ANISOU 3383  CB  ASP A 466     3583   3824   5341    505    659   -627       C  
ATOM   3384  CG  ASP A 466      89.248  21.873  38.982  1.00 35.53           C  
ANISOU 3384  CG  ASP A 466     3665   4242   5592    324    598   -633       C  
ATOM   3385  OD1 ASP A 466      88.321  22.181  39.760  1.00 35.12           O  
ANISOU 3385  OD1 ASP A 466     3216   4416   5710    399    466   -478       O  
ATOM   3386  OD2 ASP A 466      90.292  22.559  38.950  1.00 41.92           O  
ANISOU 3386  OD2 ASP A 466     4121   5282   6525    -26    582   -515       O  
ATOM   3387  N   ASN A 467      86.353  19.529  40.078  1.00 29.57           N  
ANISOU 3387  N   ASN A 467     3198   3140   4895    452    719   -779       N  
ATOM   3388  CA  ASN A 467      86.152  19.277  41.501  1.00 28.37           C  
ANISOU 3388  CA  ASN A 467     3089   2869   4821    434    657   -806       C  
ATOM   3389  C   ASN A 467      84.775  18.679  41.798  1.00 27.84           C  
ANISOU 3389  C   ASN A 467     3093   2691   4791    385    739   -838       C  
ATOM   3390  O   ASN A 467      83.856  19.420  42.150  1.00 27.65           O  
ANISOU 3390  O   ASN A 467     3109   2620   4776    420    725   -939       O  
ATOM   3391  CB  ASN A 467      86.348  20.598  42.266  1.00 27.30           C  
ANISOU 3391  CB  ASN A 467     3000   2815   4557    407    610   -767       C  
ATOM   3392  CG  ASN A 467      86.595  20.386  43.741  1.00 27.18           C  
ANISOU 3392  CG  ASN A 467     2804   2879   4643    348    439   -714       C  
ATOM   3393  OD1 ASN A 467      86.735  19.247  44.195  1.00 26.66           O  
ANISOU 3393  OD1 ASN A 467     2849   3058   4223    205    124   -510       O  
ATOM   3394  ND2 ASN A 467      86.651  21.476  44.499  1.00 23.68           N  
ANISOU 3394  ND2 ASN A 467     2247   2738   4011    274    321   -420       N  
ATOM   3395  N   PRO A 468      84.611  17.349  41.641  1.00 27.56           N  
ANISOU 3395  N   PRO A 468     3053   2598   4821    414    770   -888       N  
ATOM   3396  CA  PRO A 468      83.287  16.734  41.788  1.00 27.23           C  
ANISOU 3396  CA  PRO A 468     3056   2521   4769    321    812   -876       C  
ATOM   3397  C   PRO A 468      82.658  16.895  43.174  1.00 26.98           C  
ANISOU 3397  C   PRO A 468     2948   2545   4756    309    776   -856       C  
ATOM   3398  O   PRO A 468      83.321  16.677  44.187  1.00 27.39           O  
ANISOU 3398  O   PRO A 468     2944   2661   4800    213    776   -843       O  
ATOM   3399  CB  PRO A 468      83.554  15.257  41.468  1.00 27.22           C  
ANISOU 3399  CB  PRO A 468     3038   2505   4797    336    854   -881       C  
ATOM   3400  CG  PRO A 468      84.745  15.290  40.555  1.00 27.00           C  
ANISOU 3400  CG  PRO A 468     3068   2375   4815    315    843   -862       C  
ATOM   3401  CD  PRO A 468      85.609  16.352  41.202  1.00 28.12           C  
ANISOU 3401  CD  PRO A 468     3212   2605   4866    345    840   -904       C  
ATOM   3402  N   GLY A 469      81.394  17.306  43.216  1.00 26.90           N  
ANISOU 3402  N   GLY A 469     2975   2553   4693    208    743   -869       N  
ATOM   3403  CA  GLY A 469      80.650  17.399  44.474  1.00 25.42           C  
ANISOU 3403  CA  GLY A 469     2760   2383   4514    277    652   -899       C  
ATOM   3404  C   GLY A 469      79.686  18.574  44.451  1.00 24.90           C  
ANISOU 3404  C   GLY A 469     2674   2376   4409    147    547   -852       C  
ATOM   3405  O   GLY A 469      79.695  19.353  43.503  1.00 25.56           O  
ANISOU 3405  O   GLY A 469     2919   2304   4489    281    514   -861       O  
ATOM   3406  N   PRO A 470      78.829  18.690  45.476  1.00 23.64           N  
ANISOU 3406  N   PRO A 470     2505   2289   4186     66    479   -893       N  
ATOM   3407  CA  PRO A 470      77.892  19.803  45.585  1.00 23.07           C  
ANISOU 3407  CA  PRO A 470     2366   2307   4093      0    445   -808       C  
ATOM   3408  C   PRO A 470      78.555  21.017  46.240  1.00 22.60           C  
ANISOU 3408  C   PRO A 470     2246   2268   4070    -67    449   -720       C  
ATOM   3409  O   PRO A 470      79.047  20.898  47.368  1.00 21.76           O  
ANISOU 3409  O   PRO A 470     2087   2145   4033   -182    388   -722       O  
ATOM   3410  CB  PRO A 470      76.798  19.253  46.509  1.00 23.56           C  
ANISOU 3410  CB  PRO A 470     2379   2362   4211    -21    478   -736       C  
ATOM   3411  CG  PRO A 470      77.485  18.179  47.328  1.00 22.78           C  
ANISOU 3411  CG  PRO A 470     2302   2295   4057    123    475   -883       C  
ATOM   3412  CD  PRO A 470      78.551  17.608  46.437  1.00 24.41           C  
ANISOU 3412  CD  PRO A 470     2595   2453   4225     91    490   -802       C  
ATOM   3413  N   TRP A 471      78.544  22.159  45.550  1.00 22.22           N  
ANISOU 3413  N   TRP A 471     2208   2295   3938    -43    433   -663       N  
ATOM   3414  CA  TRP A 471      79.178  23.385  46.036  1.00 21.41           C  
ANISOU 3414  CA  TRP A 471     2067   2355   3713    -38    374   -646       C  
ATOM   3415  C   TRP A 471      78.176  24.535  46.114  1.00 21.32           C  
ANISOU 3415  C   TRP A 471     2146   2323   3629    -29    364   -603       C  
ATOM   3416  O   TRP A 471      77.481  24.817  45.136  1.00 22.37           O  
ANISOU 3416  O   TRP A 471     2348   2391   3761     57    265   -564       O  
ATOM   3417  CB  TRP A 471      80.348  23.779  45.119  1.00 21.48           C  
ANISOU 3417  CB  TRP A 471     2013   2465   3682    -48    403   -688       C  
ATOM   3418  CG  TRP A 471      81.363  22.670  44.927  1.00 20.51           C  
ANISOU 3418  CG  TRP A 471     2057   2278   3459     -2    305   -911       C  
ATOM   3419  CD1 TRP A 471      81.580  21.943  43.790  1.00 22.43           C  
ANISOU 3419  CD1 TRP A 471     2179   2594   3747     19    123  -1023       C  
ATOM   3420  CD2 TRP A 471      82.269  22.153  45.909  1.00 20.55           C  
ANISOU 3420  CD2 TRP A 471     2122   2417   3269   -120    200  -1003       C  
ATOM   3421  NE1 TRP A 471      82.576  21.008  44.002  1.00 22.85           N  
ANISOU 3421  NE1 TRP A 471     2425   2696   3560    144    115  -1012       N  
ATOM   3422  CE2 TRP A 471      83.022  21.129  45.292  1.00 21.41           C  
ANISOU 3422  CE2 TRP A 471     2190   2487   3456   -104     99   -892       C  
ATOM   3423  CE3 TRP A 471      82.547  22.486  47.244  1.00 21.40           C  
ANISOU 3423  CE3 TRP A 471     2410   2529   3189   -102    287   -834       C  
ATOM   3424  CZ2 TRP A 471      84.012  20.410  45.969  1.00 21.05           C  
ANISOU 3424  CZ2 TRP A 471     2295   2449   3250     38    128   -884       C  
ATOM   3425  CZ3 TRP A 471      83.553  21.787  47.912  1.00 19.39           C  
ANISOU 3425  CZ3 TRP A 471     2048   2191   3127   -183    375   -890       C  
ATOM   3426  CH2 TRP A 471      84.253  20.744  47.279  1.00 22.15           C  
ANISOU 3426  CH2 TRP A 471     2494   2564   3356      1    305  -1147       C  
ATOM   3427  N   PHE A 472      78.070  25.165  47.280  1.00 20.62           N  
ANISOU 3427  N   PHE A 472     2017   2330   3488    -46    356   -518       N  
ATOM   3428  CA  PHE A 472      77.259  26.378  47.450  1.00 20.43           C  
ANISOU 3428  CA  PHE A 472     2150   2355   3255    -33    370   -439       C  
ATOM   3429  C   PHE A 472      77.739  27.517  46.534  1.00 20.13           C  
ANISOU 3429  C   PHE A 472     2117   2344   3185     18    301   -373       C  
ATOM   3430  O   PHE A 472      78.949  27.718  46.335  1.00 19.20           O  
ANISOU 3430  O   PHE A 472     2056   2241   2995    149    399   -342       O  
ATOM   3431  CB  PHE A 472      77.396  26.857  48.900  1.00 20.22           C  
ANISOU 3431  CB  PHE A 472     2106   2423   3153      4    442   -467       C  
ATOM   3432  CG  PHE A 472      76.168  26.694  49.763  1.00 20.66           C  
ANISOU 3432  CG  PHE A 472     2026   2706   3115    -36    301   -351       C  
ATOM   3433  CD1 PHE A 472      74.887  27.019  49.308  1.00 19.67           C  
ANISOU 3433  CD1 PHE A 472     1962   2515   2995   -148    347   -346       C  
ATOM   3434  CD2 PHE A 472      76.322  26.303  51.091  1.00 18.94           C  
ANISOU 3434  CD2 PHE A 472     1587   2845   2763     26    355   -506       C  
ATOM   3435  CE1 PHE A 472      73.787  26.915  50.156  1.00 18.83           C  
ANISOU 3435  CE1 PHE A 472     2226   2333   2593   -137    209   -446       C  
ATOM   3436  CE2 PHE A 472      75.228  26.174  51.937  1.00 19.73           C  
ANISOU 3436  CE2 PHE A 472     1763   2929   2805   -278    221   -716       C  
ATOM   3437  CZ  PHE A 472      73.958  26.491  51.477  1.00 19.01           C  
ANISOU 3437  CZ  PHE A 472     1991   2726   2507    137    -96   -640       C  
ATOM   3438  N   LEU A 473      76.789  28.278  45.999  1.00 19.59           N  
ANISOU 3438  N   LEU A 473     1999   2355   3087    -15    223   -298       N  
ATOM   3439  CA  LEU A 473      77.060  29.575  45.388  1.00 19.71           C  
ANISOU 3439  CA  LEU A 473     2016   2305   3166      3     65   -306       C  
ATOM   3440  C   LEU A 473      75.992  30.489  45.977  1.00 20.11           C  
ANISOU 3440  C   LEU A 473     1952   2354   3335     57     25   -284       C  
ATOM   3441  O   LEU A 473      74.795  30.197  45.842  1.00 20.23           O  
ANISOU 3441  O   LEU A 473     1969   2334   3381    -16   -183   -292       O  
ATOM   3442  CB  LEU A 473      76.862  29.537  43.868  1.00 20.19           C  
ANISOU 3442  CB  LEU A 473     2187   2352   3130   -166     44   -259       C  
ATOM   3443  CG  LEU A 473      76.826  30.912  43.178  1.00 21.00           C  
ANISOU 3443  CG  LEU A 473     2067   2643   3268   -320   -218   -102       C  
ATOM   3444  CD1 LEU A 473      78.209  31.583  43.126  1.00 20.88           C  
ANISOU 3444  CD1 LEU A 473     1766   2519   3647   -376    141      8       C  
ATOM   3445  CD2 LEU A 473      76.240  30.791  41.780  1.00 24.21           C  
ANISOU 3445  CD2 LEU A 473     2956   3130   3110   -269   -194    220       C  
ATOM   3446  N   HIS A 474      76.415  31.561  46.647  1.00 18.45           N  
ANISOU 3446  N   HIS A 474     1688   2082   3238    130      3   -326       N  
ATOM   3447  CA  HIS A 474      75.460  32.405  47.360  1.00 18.33           C  
ANISOU 3447  CA  HIS A 474     1453   2164   3346    245     34   -279       C  
ATOM   3448  C   HIS A 474      75.986  33.807  47.644  1.00 18.47           C  
ANISOU 3448  C   HIS A 474     1405   2224   3388    357     48   -333       C  
ATOM   3449  O   HIS A 474      77.199  34.070  47.587  1.00 17.89           O  
ANISOU 3449  O   HIS A 474     1423   2028   3345    238    246   -424       O  
ATOM   3450  CB  HIS A 474      75.056  31.735  48.682  1.00 18.65           C  
ANISOU 3450  CB  HIS A 474     1480   2219   3386    295     22   -212       C  
ATOM   3451  CG  HIS A 474      76.195  31.562  49.639  1.00 19.41           C  
ANISOU 3451  CG  HIS A 474     1538   2258   3579     33     42    -50       C  
ATOM   3452  ND1 HIS A 474      76.604  32.562  50.495  1.00 21.53           N  
ANISOU 3452  ND1 HIS A 474     1968   2407   3802    -79   -223     18       N  
ATOM   3453  CD2 HIS A 474      77.003  30.504  49.882  1.00 21.30           C  
ANISOU 3453  CD2 HIS A 474     1704   2379   4008    116    -45    -66       C  
ATOM   3454  CE1 HIS A 474      77.643  32.142  51.198  1.00 21.28           C  
ANISOU 3454  CE1 HIS A 474     2048   2308   3728    122    -35    191       C  
ATOM   3455  NE2 HIS A 474      77.891  30.890  50.858  1.00 23.11           N  
ANISOU 3455  NE2 HIS A 474     2076   2739   3963    398   -123    -69       N  
ATOM   3456  N   CYS A 475      75.062  34.699  48.005  1.00 18.68           N  
ANISOU 3456  N   CYS A 475     1445   2264   3389    390     34   -345       N  
ATOM   3457  CA  CYS A 475      75.467  36.001  48.492  1.00 18.83           C  
ANISOU 3457  CA  CYS A 475     1370   2379   3406    413     27   -344       C  
ATOM   3458  C   CYS A 475      76.073  35.811  49.879  1.00 19.02           C  
ANISOU 3458  C   CYS A 475     1153   2572   3498    415    -68   -239       C  
ATOM   3459  O   CYS A 475      75.474  35.120  50.698  1.00 18.92           O  
ANISOU 3459  O   CYS A 475     1229   2638   3320    263    -96   -231       O  
ATOM   3460  CB  CYS A 475      74.230  36.895  48.604  1.00 19.32           C  
ANISOU 3460  CB  CYS A 475     1411   2415   3514    356     -3   -370       C  
ATOM   3461  SG  CYS A 475      74.785  38.534  49.104  1.00 21.22           S  
ANISOU 3461  SG  CYS A 475     1755   2261   4043    306    158   -354       S  
ATOM   3462  N   HIS A 476      77.204  36.453  50.168  1.00 19.44           N  
ANISOU 3462  N   HIS A 476     1180   2724   3479    354   -100   -256       N  
ATOM   3463  CA  HIS A 476      77.890  36.280  51.450  1.00 19.42           C  
ANISOU 3463  CA  HIS A 476     1023   2848   3506    520   -135   -140       C  
ATOM   3464  C   HIS A 476      77.399  37.292  52.487  1.00 19.25           C  
ANISOU 3464  C   HIS A 476     1032   2759   3521    518   -165   -122       C  
ATOM   3465  O   HIS A 476      77.918  37.360  53.604  1.00 20.53           O  
ANISOU 3465  O   HIS A 476     1321   2920   3557    541   -112   -171       O  
ATOM   3466  CB  HIS A 476      79.442  36.298  51.304  1.00 19.28           C  
ANISOU 3466  CB  HIS A 476      819   2926   3581    370   -178   -151       C  
ATOM   3467  CG  HIS A 476      80.161  35.345  52.219  1.00 20.03           C  
ANISOU 3467  CG  HIS A 476     1015   3178   3415    445   -173   -107       C  
ATOM   3468  ND1 HIS A 476      80.126  35.471  53.593  1.00 20.41           N  
ANISOU 3468  ND1 HIS A 476     1105   3427   3221    580   -262   -435       N  
ATOM   3469  CD2 HIS A 476      80.972  34.282  51.968  1.00 19.79           C  
ANISOU 3469  CD2 HIS A 476      839   3208   3471    577    -34   -124       C  
ATOM   3470  CE1 HIS A 476      80.847  34.503  54.138  1.00 22.05           C  
ANISOU 3470  CE1 HIS A 476     1448   3587   3340    598   -499   -292       C  
ATOM   3471  NE2 HIS A 476      81.396  33.775  53.180  1.00 20.69           N  
ANISOU 3471  NE2 HIS A 476     1026   3498   3336    661    -18   -201       N  
ATOM   3472  N   ILE A 477      76.381  38.074  52.138  1.00 18.64           N  
ANISOU 3472  N   ILE A 477     1051   2543   3486    477   -102   -125       N  
ATOM   3473  CA  ILE A 477      75.660  38.797  53.173  1.00 17.90           C  
ANISOU 3473  CA  ILE A 477      942   2374   3483    418    -95    -74       C  
ATOM   3474  C   ILE A 477      74.806  37.731  53.856  1.00 18.01           C  
ANISOU 3474  C   ILE A 477      978   2367   3495    384   -212    -52       C  
ATOM   3475  O   ILE A 477      73.881  37.199  53.253  1.00 18.30           O  
ANISOU 3475  O   ILE A 477      931   2444   3576    235   -250    -25       O  
ATOM   3476  CB  ILE A 477      74.832  39.970  52.633  1.00 17.29           C  
ANISOU 3476  CB  ILE A 477      921   2215   3431    440    -42   -103       C  
ATOM   3477  CG1 ILE A 477      75.771  41.053  52.080  1.00 18.34           C  
ANISOU 3477  CG1 ILE A 477     1033   2202   3731    526    -84     50       C  
ATOM   3478  CG2 ILE A 477      73.888  40.486  53.753  1.00 17.24           C  
ANISOU 3478  CG2 ILE A 477      913   1936   3699    289    109   -240       C  
ATOM   3479  CD1 ILE A 477      75.063  42.164  51.275  1.00 21.10           C  
ANISOU 3479  CD1 ILE A 477     1139   2609   4269    562     84    423       C  
ATOM   3480  N   ASP A 478      75.165  37.388  55.094  1.00 17.86           N  
ANISOU 3480  N   ASP A 478     1006   2411   3366    289   -194     18       N  
ATOM   3481  CA  ASP A 478      74.666  36.185  55.751  1.00 18.38           C  
ANISOU 3481  CA  ASP A 478     1162   2480   3339    231   -259      8       C  
ATOM   3482  C   ASP A 478      73.152  36.256  55.955  1.00 17.87           C  
ANISOU 3482  C   ASP A 478     1134   2429   3224    154   -188   -111       C  
ATOM   3483  O   ASP A 478      72.463  35.229  55.911  1.00 18.00           O  
ANISOU 3483  O   ASP A 478     1379   2226   3235    102   -132   -132       O  
ATOM   3484  CB  ASP A 478      75.409  35.970  57.082  1.00 18.43           C  
ANISOU 3484  CB  ASP A 478     1184   2566   3249    207   -316    168       C  
ATOM   3485  CG  ASP A 478      75.577  34.492  57.440  1.00 21.24           C  
ANISOU 3485  CG  ASP A 478     1821   2848   3398     36   -354    154       C  
ATOM   3486  OD1 ASP A 478      75.686  33.643  56.532  1.00 23.57           O  
ANISOU 3486  OD1 ASP A 478     2075   3232   3648    -99   -291     50       O  
ATOM   3487  OD2 ASP A 478      75.637  34.167  58.653  1.00 24.30           O  
ANISOU 3487  OD2 ASP A 478     2546   3138   3548   -284   -273    794       O  
ATOM   3488  N   PHE A 479      72.621  37.471  56.109  1.00 16.57           N  
ANISOU 3488  N   PHE A 479      835   2337   3123    214   -230   -246       N  
ATOM   3489  CA  PHE A 479      71.173  37.638  56.281  1.00 17.88           C  
ANISOU 3489  CA  PHE A 479     1037   2476   3281    112   -158   -376       C  
ATOM   3490  C   PHE A 479      70.429  37.337  54.989  1.00 18.05           C  
ANISOU 3490  C   PHE A 479     1050   2487   3319     61   -181   -322       C  
ATOM   3491  O   PHE A 479      69.260  36.917  55.012  1.00 18.66           O  
ANISOU 3491  O   PHE A 479     1104   2504   3479    -48    -56   -300       O  
ATOM   3492  CB  PHE A 479      70.879  39.061  56.765  1.00 16.90           C  
ANISOU 3492  CB  PHE A 479      787   2464   3170    189   -239   -483       C  
ATOM   3493  CG  PHE A 479      71.598  39.384  58.037  1.00 18.37           C  
ANISOU 3493  CG  PHE A 479     1225   2578   3175    115   -224   -712       C  
ATOM   3494  CD1 PHE A 479      71.188  38.809  59.233  1.00 20.57           C  
ANISOU 3494  CD1 PHE A 479     1989   2719   3106    211   -559   -491       C  
ATOM   3495  CD2 PHE A 479      72.706  40.219  58.028  1.00 17.44           C  
ANISOU 3495  CD2 PHE A 479      848   2611   3167     69   -439   -979       C  
ATOM   3496  CE1 PHE A 479      71.878  39.071  60.424  1.00 20.18           C  
ANISOU 3496  CE1 PHE A 479     1737   2714   3213     83   -501   -879       C  
ATOM   3497  CE2 PHE A 479      73.389  40.498  59.213  1.00 20.04           C  
ANISOU 3497  CE2 PHE A 479     1361   3243   3008    160   -353   -770       C  
ATOM   3498  CZ  PHE A 479      72.977  39.918  60.408  1.00 21.29           C  
ANISOU 3498  CZ  PHE A 479     1602   3178   3307    230   -369   -681       C  
ATOM   3499  N   HIS A 480      71.108  37.547  53.859  1.00 18.42           N  
ANISOU 3499  N   HIS A 480     1207   2333   3456     27    -80   -330       N  
ATOM   3500  CA  HIS A 480      70.485  37.251  52.565  1.00 18.48           C  
ANISOU 3500  CA  HIS A 480     1210   2335   3475     56   -213   -289       C  
ATOM   3501  C   HIS A 480      70.562  35.751  52.273  1.00 18.32           C  
ANISOU 3501  C   HIS A 480     1179   2221   3560     78   -227   -262       C  
ATOM   3502  O   HIS A 480      69.629  35.163  51.721  1.00 18.20           O  
ANISOU 3502  O   HIS A 480     1135   2204   3575     20   -245   -331       O  
ATOM   3503  CB  HIS A 480      71.160  38.020  51.422  1.00 18.49           C  
ANISOU 3503  CB  HIS A 480     1183   2301   3538    -52   -202   -245       C  
ATOM   3504  CG  HIS A 480      71.052  39.509  51.536  1.00 18.57           C  
ANISOU 3504  CG  HIS A 480     1059   2382   3612    126   -131   -360       C  
ATOM   3505  ND1 HIS A 480      71.768  40.364  50.722  1.00 20.49           N  
ANISOU 3505  ND1 HIS A 480     1594   2477   3713      3    111   -346       N  
ATOM   3506  CD2 HIS A 480      70.341  40.294  52.384  1.00 19.66           C  
ANISOU 3506  CD2 HIS A 480     1104   2684   3679    -78   -192   -264       C  
ATOM   3507  CE1 HIS A 480      71.485  41.612  51.056  1.00 20.60           C  
ANISOU 3507  CE1 HIS A 480     1109   2734   3984    100    144   -342       C  
ATOM   3508  NE2 HIS A 480      70.630  41.601  52.067  1.00 18.58           N  
ANISOU 3508  NE2 HIS A 480     1021   2528   3511    -46   -151   -465       N  
ATOM   3509  N   LEU A 481      71.692  35.136  52.602  1.00 18.51           N  
ANISOU 3509  N   LEU A 481     1228   2237   3565    178   -168   -192       N  
ATOM   3510  CA  LEU A 481      71.819  33.674  52.510  1.00 18.77           C  
ANISOU 3510  CA  LEU A 481     1234   2283   3614    226   -219   -124       C  
ATOM   3511  C   LEU A 481      70.692  33.006  53.299  1.00 19.41           C  
ANISOU 3511  C   LEU A 481     1300   2400   3673    184   -197    -83       C  
ATOM   3512  O   LEU A 481      70.004  32.111  52.788  1.00 19.12           O  
ANISOU 3512  O   LEU A 481     1285   2410   3569    125   -225     28       O  
ATOM   3513  CB  LEU A 481      73.188  33.214  53.050  1.00 18.89           C  
ANISOU 3513  CB  LEU A 481     1250   2276   3649    353   -267   -118       C  
ATOM   3514  CG  LEU A 481      73.403  31.700  53.176  1.00 18.09           C  
ANISOU 3514  CG  LEU A 481     1291   2196   3386    491   -421   -226       C  
ATOM   3515  CD1 LEU A 481      73.139  30.981  51.851  1.00 20.68           C  
ANISOU 3515  CD1 LEU A 481     1850   2663   3344    383   -196   -257       C  
ATOM   3516  CD2 LEU A 481      74.819  31.367  53.700  1.00 22.05           C  
ANISOU 3516  CD2 LEU A 481     1828   2583   3967    871   -603   -115       C  
ATOM   3517  N   GLU A 482      70.497  33.467  54.536  1.00 19.43           N  
ANISOU 3517  N   GLU A 482     1276   2476   3628    124   -133     -5       N  
ATOM   3518  CA  GLU A 482      69.435  32.956  55.410  1.00 20.27           C  
ANISOU 3518  CA  GLU A 482     1275   2659   3765    112   -136     -3       C  
ATOM   3519  C   GLU A 482      68.057  33.102  54.757  1.00 20.34           C  
ANISOU 3519  C   GLU A 482     1387   2550   3791     73   -200     -3       C  
ATOM   3520  O   GLU A 482      67.201  32.212  54.877  1.00 19.60           O  
ANISOU 3520  O   GLU A 482     1282   2307   3858    -11   -260    123       O  
ATOM   3521  CB  GLU A 482      69.501  33.706  56.747  1.00 21.13           C  
ANISOU 3521  CB  GLU A 482     1437   2784   3805     57     39    -32       C  
ATOM   3522  CG  GLU A 482      68.353  33.452  57.733  1.00 22.59           C  
ANISOU 3522  CG  GLU A 482     1247   3037   4297    178    244    112       C  
ATOM   3523  CD  GLU A 482      68.305  32.037  58.289  1.00 25.30           C  
ANISOU 3523  CD  GLU A 482     1525   3415   4670    166    391    289       C  
ATOM   3524  OE1 GLU A 482      69.287  31.269  58.175  1.00 26.63           O  
ANISOU 3524  OE1 GLU A 482     1786   3548   4783    340    293    179       O  
ATOM   3525  OE2 GLU A 482      67.254  31.687  58.867  1.00 28.02           O  
ANISOU 3525  OE2 GLU A 482     1742   3621   5283    109    661    545       O  
ATOM   3526  N   ALA A 483      67.864  34.206  54.039  1.00 19.56           N  
ANISOU 3526  N   ALA A 483     1431   2312   3689     84   -307    -95       N  
ATOM   3527  CA  ALA A 483      66.617  34.450  53.301  1.00 19.91           C  
ANISOU 3527  CA  ALA A 483     1595   2338   3631    127   -359   -167       C  
ATOM   3528  C   ALA A 483      66.582  33.745  51.936  1.00 20.35           C  
ANISOU 3528  C   ALA A 483     1704   2399   3626    101   -331   -163       C  
ATOM   3529  O   ALA A 483      65.681  34.008  51.135  1.00 21.27           O  
ANISOU 3529  O   ALA A 483     2022   2541   3516     91   -373   -141       O  
ATOM   3530  CB  ALA A 483      66.376  35.961  53.150  1.00 19.69           C  
ANISOU 3530  CB  ALA A 483     1492   2340   3647    140   -348   -182       C  
ATOM   3531  N   GLY A 484      67.514  32.823  51.689  1.00 20.29           N  
ANISOU 3531  N   GLY A 484     1768   2355   3584     61   -259   -258       N  
ATOM   3532  CA  GLY A 484      67.421  31.898  50.552  1.00 20.76           C  
ANISOU 3532  CA  GLY A 484     1878   2218   3790     59   -136   -269       C  
ATOM   3533  C   GLY A 484      68.229  32.266  49.313  1.00 20.67           C  
ANISOU 3533  C   GLY A 484     1827   2192   3833     42   -139   -319       C  
ATOM   3534  O   GLY A 484      68.068  31.625  48.272  1.00 20.65           O  
ANISOU 3534  O   GLY A 484     1820   2064   3962    -16   -243   -419       O  
ATOM   3535  N   PHE A 485      69.114  33.261  49.419  1.00 19.48           N  
ANISOU 3535  N   PHE A 485     1734   1850   3815     57   -188   -332       N  
ATOM   3536  CA  PHE A 485      69.819  33.806  48.249  1.00 19.03           C  
ANISOU 3536  CA  PHE A 485     1556   1953   3719     -4   -110   -333       C  
ATOM   3537  C   PHE A 485      71.027  32.949  47.880  1.00 20.03           C  
ANISOU 3537  C   PHE A 485     1735   2069   3807     15   -134   -311       C  
ATOM   3538  O   PHE A 485      72.189  33.365  48.039  1.00 20.20           O  
ANISOU 3538  O   PHE A 485     1593   2311   3771     69    -77   -273       O  
ATOM   3539  CB  PHE A 485      70.219  35.275  48.497  1.00 19.05           C  
ANISOU 3539  CB  PHE A 485     1541   2038   3657    -11   -191   -269       C  
ATOM   3540  CG  PHE A 485      70.348  36.113  47.243  1.00 18.60           C  
ANISOU 3540  CG  PHE A 485     1536   2100   3429      9   -293   -318       C  
ATOM   3541  CD1 PHE A 485      69.775  35.703  46.040  1.00 20.85           C  
ANISOU 3541  CD1 PHE A 485     1875   2518   3527     20   -202   -377       C  
ATOM   3542  CD2 PHE A 485      70.950  37.367  47.295  1.00 18.80           C  
ANISOU 3542  CD2 PHE A 485     1683   2337   3123     35   -308   -284       C  
ATOM   3543  CE1 PHE A 485      69.858  36.502  44.903  1.00 20.88           C  
ANISOU 3543  CE1 PHE A 485     1853   2493   3585   -283   -205   -400       C  
ATOM   3544  CE2 PHE A 485      71.043  38.179  46.166  1.00 19.99           C  
ANISOU 3544  CE2 PHE A 485     1897   2419   3276    -78   -223   -426       C  
ATOM   3545  CZ  PHE A 485      70.486  37.748  44.966  1.00 21.15           C  
ANISOU 3545  CZ  PHE A 485     2050   2507   3478   -264   -228   -578       C  
ATOM   3546  N   ALA A 486      70.726  31.745  47.399  1.00 19.99           N  
ANISOU 3546  N   ALA A 486     1799   2061   3734     77   -105   -406       N  
ATOM   3547  CA  ALA A 486      71.716  30.698  47.148  1.00 20.26           C  
ANISOU 3547  CA  ALA A 486     1792   2133   3771    134    -68   -415       C  
ATOM   3548  C   ALA A 486      71.228  29.654  46.157  1.00 20.55           C  
ANISOU 3548  C   ALA A 486     1892   2130   3785    212    -50   -423       C  
ATOM   3549  O   ALA A 486      70.031  29.366  46.081  1.00 20.42           O  
ANISOU 3549  O   ALA A 486     1947   2114   3696    247      3   -374       O  
ATOM   3550  CB  ALA A 486      72.056  29.981  48.433  1.00 19.87           C  
ANISOU 3550  CB  ALA A 486     1765   2104   3681    142    -76   -447       C  
ATOM   3551  N   VAL A 487      72.188  29.051  45.458  1.00 21.53           N  
ANISOU 3551  N   VAL A 487     2043   2280   3857    171     29   -462       N  
ATOM   3552  CA  VAL A 487      71.984  27.786  44.760  1.00 21.87           C  
ANISOU 3552  CA  VAL A 487     2021   2364   3923    246    -14   -483       C  
ATOM   3553  C   VAL A 487      73.106  26.824  45.153  1.00 21.77           C  
ANISOU 3553  C   VAL A 487     2062   2301   3907    290     -3   -459       C  
ATOM   3554  O   VAL A 487      74.101  27.222  45.769  1.00 21.82           O  
ANISOU 3554  O   VAL A 487     2030   2261   3996    269     58   -533       O  
ATOM   3555  CB  VAL A 487      71.959  27.947  43.213  1.00 21.81           C  
ANISOU 3555  CB  VAL A 487     2001   2387   3897    239      1   -433       C  
ATOM   3556  CG1 VAL A 487      70.770  28.781  42.772  1.00 22.73           C  
ANISOU 3556  CG1 VAL A 487     2024   2418   4191    372   -210   -480       C  
ATOM   3557  CG2 VAL A 487      73.276  28.510  42.692  1.00 21.26           C  
ANISOU 3557  CG2 VAL A 487     1846   2422   3808    -60   -198   -431       C  
ATOM   3558  N   VAL A 488      72.944  25.558  44.793  1.00 21.63           N  
ANISOU 3558  N   VAL A 488     2071   2243   3902    296     28   -476       N  
ATOM   3559  CA  VAL A 488      74.020  24.576  44.938  1.00 22.35           C  
ANISOU 3559  CA  VAL A 488     2272   2277   3940    323     65   -538       C  
ATOM   3560  C   VAL A 488      74.319  24.001  43.563  1.00 23.13           C  
ANISOU 3560  C   VAL A 488     2402   2380   4005    258     65   -585       C  
ATOM   3561  O   VAL A 488      73.394  23.603  42.851  1.00 23.30           O  
ANISOU 3561  O   VAL A 488     2524   2294   4033    200     38   -663       O  
ATOM   3562  CB  VAL A 488      73.616  23.444  45.907  1.00 22.22           C  
ANISOU 3562  CB  VAL A 488     2304   2271   3867    426     83   -507       C  
ATOM   3563  CG1 VAL A 488      74.657  22.320  45.921  1.00 22.25           C  
ANISOU 3563  CG1 VAL A 488     2521   2104   3827    347     78   -382       C  
ATOM   3564  CG2 VAL A 488      73.406  24.022  47.311  1.00 22.61           C  
ANISOU 3564  CG2 VAL A 488     2467   2321   3799    332    145   -485       C  
ATOM   3565  N   PHE A 489      75.597  23.973  43.188  1.00 23.32           N  
ANISOU 3565  N   PHE A 489     2432   2328   4099    177     76   -639       N  
ATOM   3566  CA  PHE A 489      75.993  23.288  41.964  1.00 24.35           C  
ANISOU 3566  CA  PHE A 489     2648   2470   4133    104     92   -637       C  
ATOM   3567  C   PHE A 489      76.294  21.824  42.265  1.00 24.61           C  
ANISOU 3567  C   PHE A 489     2723   2468   4158     72    142   -715       C  
ATOM   3568  O   PHE A 489      77.142  21.544  43.110  1.00 24.26           O  
ANISOU 3568  O   PHE A 489     2665   2462   4088    157    110   -702       O  
ATOM   3569  CB  PHE A 489      77.248  23.917  41.346  1.00 24.09           C  
ANISOU 3569  CB  PHE A 489     2589   2391   4173     36     35   -597       C  
ATOM   3570  CG  PHE A 489      77.005  25.238  40.681  1.00 25.44           C  
ANISOU 3570  CG  PHE A 489     2786   2626   4251     15    -61   -461       C  
ATOM   3571  CD1 PHE A 489      76.010  25.379  39.720  1.00 25.97           C  
ANISOU 3571  CD1 PHE A 489     2794   2740   4334     62   -203   -364       C  
ATOM   3572  CD2 PHE A 489      77.790  26.335  41.002  1.00 25.53           C  
ANISOU 3572  CD2 PHE A 489     2736   2606   4358   -181    -92   -288       C  
ATOM   3573  CE1 PHE A 489      75.792  26.601  39.096  1.00 27.03           C  
ANISOU 3573  CE1 PHE A 489     3085   2658   4524     11   -269   -310       C  
ATOM   3574  CE2 PHE A 489      77.578  27.574  40.395  1.00 26.60           C  
ANISOU 3574  CE2 PHE A 489     2814   2769   4524    -41   -418     -4       C  
ATOM   3575  CZ  PHE A 489      76.572  27.708  39.436  1.00 27.09           C  
ANISOU 3575  CZ  PHE A 489     2788   2927   4579   -236   -543   -108       C  
ATOM   3576  N   ALA A 490      75.612  20.903  41.587  1.00 24.97           N  
ANISOU 3576  N   ALA A 490     2861   2437   4189     -3    127   -844       N  
ATOM   3577  CA  ALA A 490      76.005  19.495  41.625  1.00 25.71           C  
ANISOU 3577  CA  ALA A 490     2995   2501   4271    -48    126   -945       C  
ATOM   3578  C   ALA A 490      77.067  19.280  40.551  1.00 26.40           C  
ANISOU 3578  C   ALA A 490     3087   2539   4404    -56    138   -998       C  
ATOM   3579  O   ALA A 490      76.744  18.942  39.410  1.00 26.31           O  
ANISOU 3579  O   ALA A 490     3264   2507   4226    -62    188  -1052       O  
ATOM   3580  CB  ALA A 490      74.794  18.583  41.385  1.00 25.42           C  
ANISOU 3580  CB  ALA A 490     2856   2460   4341    -41    127   -907       C  
ATOM   3581  N   GLU A 491      78.328  19.526  40.899  1.00 27.53           N  
ANISOU 3581  N   GLU A 491     3237   2624   4599     37    121  -1023       N  
ATOM   3582  CA  GLU A 491      79.412  19.444  39.922  1.00 28.15           C  
ANISOU 3582  CA  GLU A 491     3318   2652   4724     19    147  -1077       C  
ATOM   3583  C   GLU A 491      79.824  17.983  39.719  1.00 29.50           C  
ANISOU 3583  C   GLU A 491     3455   2787   4964    104    146  -1123       C  
ATOM   3584  O   GLU A 491      80.135  17.289  40.685  1.00 29.40           O  
ANISOU 3584  O   GLU A 491     3502   2636   5030     65    186  -1122       O  
ATOM   3585  CB  GLU A 491      80.587  20.300  40.395  1.00 27.59           C  
ANISOU 3585  CB  GLU A 491     3223   2642   4616     62    139  -1056       C  
ATOM   3586  CG  GLU A 491      81.786  20.305  39.470  1.00 28.28           C  
ANISOU 3586  CG  GLU A 491     3326   2827   4592     -5    128  -1053       C  
ATOM   3587  CD  GLU A 491      82.852  21.295  39.918  1.00 29.16           C  
ANISOU 3587  CD  GLU A 491     3427   3047   4602     -9    206   -985       C  
ATOM   3588  OE1 GLU A 491      82.545  22.251  40.676  1.00 28.35           O  
ANISOU 3588  OE1 GLU A 491     3289   3240   4241     92    314   -884       O  
ATOM   3589  OE2 GLU A 491      84.016  21.114  39.511  1.00 29.68           O  
ANISOU 3589  OE2 GLU A 491     3761   3196   4320    113    246   -933       O  
ATOM   3590  N   ASP A 492      79.807  17.520  38.471  1.00 31.42           N  
ANISOU 3590  N   ASP A 492     3740   2957   5240     59    106  -1175       N  
ATOM   3591  CA  ASP A 492      80.164  16.140  38.123  1.00 33.33           C  
ANISOU 3591  CA  ASP A 492     3972   3161   5528    196     97  -1204       C  
ATOM   3592  C   ASP A 492      79.462  15.130  39.042  1.00 34.20           C  
ANISOU 3592  C   ASP A 492     4103   3161   5731    121     49  -1230       C  
ATOM   3593  O   ASP A 492      80.097  14.387  39.799  1.00 33.87           O  
ANISOU 3593  O   ASP A 492     3939   3162   5768    104     32  -1218       O  
ATOM   3594  CB  ASP A 492      81.686  15.941  38.126  1.00 33.77           C  
ANISOU 3594  CB  ASP A 492     4020   3278   5533    131    105  -1186       C  
ATOM   3595  CG  ASP A 492      82.108  14.539  37.674  1.00 35.64           C  
ANISOU 3595  CG  ASP A 492     4253   3607   5681    350    186  -1268       C  
ATOM   3596  OD1 ASP A 492      81.257  13.719  37.250  1.00 35.82           O  
ANISOU 3596  OD1 ASP A 492     4386   3663   5561    396    254  -1384       O  
ATOM   3597  OD2 ASP A 492      83.322  14.245  37.743  1.00 38.92           O  
ANISOU 3597  OD2 ASP A 492     4499   4282   6006    510    169  -1206       O  
ATOM   3598  N   LEU A 493      78.134  15.137  38.985  1.00 35.32           N  
ANISOU 3598  N   LEU A 493     4246   3252   5922    184      2  -1288       N  
ATOM   3599  CA  LEU A 493      77.306  14.199  39.731  1.00 36.56           C  
ANISOU 3599  CA  LEU A 493     4481   3329   6080    207    -13  -1257       C  
ATOM   3600  C   LEU A 493      77.775  12.741  39.607  1.00 37.19           C  
ANISOU 3600  C   LEU A 493     4649   3319   6161    176    -59  -1280       C  
ATOM   3601  O   LEU A 493      78.007  12.088  40.630  1.00 36.85           O  
ANISOU 3601  O   LEU A 493     4617   3168   6216    154   -145  -1254       O  
ATOM   3602  CB  LEU A 493      75.849  14.365  39.285  1.00 37.35           C  
ANISOU 3602  CB  LEU A 493     4525   3517   6150    223    -19  -1262       C  
ATOM   3603  CG  LEU A 493      74.689  14.050  40.227  1.00 39.47           C  
ANISOU 3603  CG  LEU A 493     4678   3993   6324    334    -18  -1122       C  
ATOM   3604  CD1 LEU A 493      75.031  14.466  41.637  1.00 39.77           C  
ANISOU 3604  CD1 LEU A 493     4873   3920   6316    341    -99  -1237       C  
ATOM   3605  CD2 LEU A 493      73.436  14.787  39.769  1.00 40.83           C  
ANISOU 3605  CD2 LEU A 493     4751   4180   6582    537    -89  -1058       C  
ATOM   3606  N   PRO A 494      77.956  12.231  38.373  1.00 37.33           N  
ANISOU 3606  N   PRO A 494     4743   3250   6190    211    -73  -1321       N  
ATOM   3607  CA  PRO A 494      78.318  10.817  38.289  1.00 37.77           C  
ANISOU 3607  CA  PRO A 494     4773   3337   6239    269    -68  -1334       C  
ATOM   3608  C   PRO A 494      79.660  10.503  38.955  1.00 37.48           C  
ANISOU 3608  C   PRO A 494     4732   3249   6257    283    -45  -1290       C  
ATOM   3609  O   PRO A 494      79.831   9.412  39.501  1.00 37.83           O  
ANISOU 3609  O   PRO A 494     4779   3293   6299    279    -72  -1333       O  
ATOM   3610  CB  PRO A 494      78.373  10.549  36.779  1.00 38.19           C  
ANISOU 3610  CB  PRO A 494     4868   3396   6246    270    -70  -1336       C  
ATOM   3611  CG  PRO A 494      77.572  11.641  36.154  1.00 37.73           C  
ANISOU 3611  CG  PRO A 494     4872   3292   6168    249   -109  -1361       C  
ATOM   3612  CD  PRO A 494      77.829  12.832  37.032  1.00 37.63           C  
ANISOU 3612  CD  PRO A 494     4797   3312   6187    176    -57  -1357       C  
ATOM   3613  N   GLY A 495      80.588  11.453  38.935  1.00 36.84           N  
ANISOU 3613  N   GLY A 495     4590   3160   6246    312    -12  -1248       N  
ATOM   3614  CA  GLY A 495      81.888  11.250  39.556  1.00 36.54           C  
ANISOU 3614  CA  GLY A 495     4519   3091   6272    297    122  -1165       C  
ATOM   3615  C   GLY A 495      81.978  11.572  41.038  1.00 35.75           C  
ANISOU 3615  C   GLY A 495     4366   3006   6211    359    227  -1134       C  
ATOM   3616  O   GLY A 495      83.032  11.374  41.646  1.00 36.25           O  
ANISOU 3616  O   GLY A 495     4406   3124   6243    308    259  -1200       O  
ATOM   3617  N   THR A 496      80.894  12.063  41.632  1.00 35.16           N  
ANISOU 3617  N   THR A 496     4206   2928   6223    351    282  -1022       N  
ATOM   3618  CA  THR A 496      80.915  12.505  43.035  1.00 34.09           C  
ANISOU 3618  CA  THR A 496     3972   2787   6193    377    319   -969       C  
ATOM   3619  C   THR A 496      81.196  11.423  44.088  1.00 34.24           C  
ANISOU 3619  C   THR A 496     4042   2758   6210    245    316   -933       C  
ATOM   3620  O   THR A 496      82.085  11.600  44.928  1.00 33.74           O  
ANISOU 3620  O   THR A 496     3979   2638   6202     46    325   -890       O  
ATOM   3621  CB  THR A 496      79.658  13.349  43.398  1.00 33.89           C  
ANISOU 3621  CB  THR A 496     3955   2733   6188    435    359   -973       C  
ATOM   3622  OG1 THR A 496      79.704  14.584  42.675  1.00 32.85           O  
ANISOU 3622  OG1 THR A 496     3533   2905   6043    750    325   -912       O  
ATOM   3623  CG2 THR A 496      79.620  13.668  44.888  1.00 32.80           C  
ANISOU 3623  CG2 THR A 496     3610   2777   6072    564    392   -880       C  
ATOM   3624  N   PRO A 497      80.470  10.288  44.046  1.00 34.59           N  
ANISOU 3624  N   PRO A 497     4085   2778   6277    173    308   -888       N  
ATOM   3625  CA  PRO A 497      80.750   9.243  45.040  1.00 34.61           C  
ANISOU 3625  CA  PRO A 497     4094   2790   6264    231    315   -892       C  
ATOM   3626  C   PRO A 497      82.194   8.736  45.057  1.00 34.75           C  
ANISOU 3626  C   PRO A 497     4138   2831   6234    285    375   -896       C  
ATOM   3627  O   PRO A 497      82.773   8.589  46.138  1.00 34.50           O  
ANISOU 3627  O   PRO A 497     4133   2790   6185    297    386   -971       O  
ATOM   3628  CB  PRO A 497      79.782   8.116  44.652  1.00 34.77           C  
ANISOU 3628  CB  PRO A 497     4159   2775   6277    183    305   -875       C  
ATOM   3629  CG  PRO A 497      78.662   8.824  43.955  1.00 34.42           C  
ANISOU 3629  CG  PRO A 497     3982   2750   6344    136    254   -887       C  
ATOM   3630  CD  PRO A 497      79.346   9.910  43.168  1.00 34.08           C  
ANISOU 3630  CD  PRO A 497     3939   2755   6255    229    289   -890       C  
ATOM   3631  N   ALA A 498      82.762   8.464  43.883  1.00 34.50           N  
ANISOU 3631  N   ALA A 498     4113   2830   6164    370    427   -871       N  
ATOM   3632  CA  ALA A 498      84.148   7.998  43.781  1.00 34.32           C  
ANISOU 3632  CA  ALA A 498     4103   2819   6117    422    444   -856       C  
ATOM   3633  C   ALA A 498      85.159   9.031  44.254  1.00 33.82           C  
ANISOU 3633  C   ALA A 498     4023   2764   6062    446    450   -827       C  
ATOM   3634  O   ALA A 498      86.169   8.691  44.878  1.00 34.10           O  
ANISOU 3634  O   ALA A 498     4120   2726   6110    438    438   -826       O  
ATOM   3635  CB  ALA A 498      84.470   7.591  42.353  1.00 34.99           C  
ANISOU 3635  CB  ALA A 498     4142   2998   6152    486    466   -866       C  
ATOM   3636  N   ALA A 499      84.894  10.294  43.941  1.00 33.12           N  
ANISOU 3636  N   ALA A 499     3908   2708   5965    397    463   -817       N  
ATOM   3637  CA  ALA A 499      85.814  11.367  44.298  1.00 32.62           C  
ANISOU 3637  CA  ALA A 499     3867   2639   5886    392    438   -759       C  
ATOM   3638  C   ALA A 499      85.838  11.662  45.795  1.00 32.08           C  
ANISOU 3638  C   ALA A 499     3725   2627   5834    402    435   -708       C  
ATOM   3639  O   ALA A 499      86.883  12.054  46.319  1.00 32.33           O  
ANISOU 3639  O   ALA A 499     3788   2668   5828    334    426   -684       O  
ATOM   3640  CB  ALA A 499      85.491  12.622  43.514  1.00 32.56           C  
ANISOU 3640  CB  ALA A 499     3874   2574   5923    429    423   -802       C  
ATOM   3641  N   ASN A 500      84.712  11.436  46.470  1.00 30.58           N  
ANISOU 3641  N   ASN A 500     3415   2576   5629    426    416   -646       N  
ATOM   3642  CA  ASN A 500      84.524  11.864  47.859  1.00 29.87           C  
ANISOU 3642  CA  ASN A 500     3246   2633   5469    451    390   -511       C  
ATOM   3643  C   ASN A 500      84.152  10.732  48.820  1.00 30.52           C  
ANISOU 3643  C   ASN A 500     3195   2640   5758    448    442   -487       C  
ATOM   3644  O   ASN A 500      83.008  10.669  49.287  1.00 31.08           O  
ANISOU 3644  O   ASN A 500     3265   2718   5823    570    499   -479       O  
ATOM   3645  CB  ASN A 500      83.434  12.940  47.941  1.00 28.62           C  
ANISOU 3645  CB  ASN A 500     3103   2638   5132    397    370   -501       C  
ATOM   3646  CG  ASN A 500      83.798  14.211  47.204  1.00 26.29           C  
ANISOU 3646  CG  ASN A 500     2851   2826   4311    396    136   -491       C  
ATOM   3647  OD1 ASN A 500      84.570  15.039  47.695  1.00 25.75           O  
ANISOU 3647  OD1 ASN A 500     2601   2866   4314    371    234   -515       O  
ATOM   3648  ND2 ASN A 500      83.212  14.394  46.030  1.00 25.16           N  
ANISOU 3648  ND2 ASN A 500     2882   2898   3779    391    180   -357       N  
ATOM   3649  N   PRO A 501      85.103   9.832  49.119  1.00 30.48           N  
ANISOU 3649  N   PRO A 501     3109   2534   5938    473    461   -462       N  
ATOM   3650  CA  PRO A 501      84.837   8.849  50.167  1.00 30.54           C  
ANISOU 3650  CA  PRO A 501     3022   2524   6055    378    475   -452       C  
ATOM   3651  C   PRO A 501      84.593   9.565  51.492  1.00 29.89           C  
ANISOU 3651  C   PRO A 501     2893   2374   6090    340    478   -449       C  
ATOM   3652  O   PRO A 501      85.273  10.550  51.790  1.00 30.99           O  
ANISOU 3652  O   PRO A 501     2995   2661   6115    336    458   -567       O  
ATOM   3653  CB  PRO A 501      86.129   8.022  50.231  1.00 30.87           C  
ANISOU 3653  CB  PRO A 501     3098   2534   6097    405    464   -446       C  
ATOM   3654  CG  PRO A 501      87.186   8.859  49.565  1.00 31.14           C  
ANISOU 3654  CG  PRO A 501     3128   2631   6070    429    486   -343       C  
ATOM   3655  CD  PRO A 501      86.434   9.648  48.515  1.00 30.70           C  
ANISOU 3655  CD  PRO A 501     3091   2576   5996    485    488   -401       C  
ATOM   3656  N   VAL A 502      83.620   9.101  52.266  1.00 29.17           N  
ANISOU 3656  N   VAL A 502     2760   2220   6103    253    399   -352       N  
ATOM   3657  CA  VAL A 502      83.240   9.790  53.502  1.00 28.05           C  
ANISOU 3657  CA  VAL A 502     2503   2099   6054    228    387   -219       C  
ATOM   3658  C   VAL A 502      83.555   8.983  54.757  1.00 27.50           C  
ANISOU 3658  C   VAL A 502     2368   2049   6032    172    369   -136       C  
ATOM   3659  O   VAL A 502      83.391   7.756  54.753  1.00 27.68           O  
ANISOU 3659  O   VAL A 502     2376   2071   6070    121    409     -7       O  
ATOM   3660  CB  VAL A 502      81.754  10.235  53.491  1.00 28.19           C  
ANISOU 3660  CB  VAL A 502     2515   2074   6123    206    292   -232       C  
ATOM   3661  CG1 VAL A 502      81.561  11.293  52.423  1.00 28.42           C  
ANISOU 3661  CG1 VAL A 502     2564   2207   6024    131    254   -235       C  
ATOM   3662  CG2 VAL A 502      80.790   9.054  53.288  1.00 28.20           C  
ANISOU 3662  CG2 VAL A 502     2452   2206   6057    255    354   -227       C  
ATOM   3663  N   PRO A 503      84.016   9.656  55.827  1.00 26.63           N  
ANISOU 3663  N   PRO A 503     2192   1918   6005    122    346    -38       N  
ATOM   3664  CA  PRO A 503      84.290   8.919  57.062  1.00 26.77           C  
ANISOU 3664  CA  PRO A 503     2234   2001   5936     98    291    -14       C  
ATOM   3665  C   PRO A 503      83.007   8.556  57.806  1.00 26.28           C  
ANISOU 3665  C   PRO A 503     2169   1974   5843     43    232     46       C  
ATOM   3666  O   PRO A 503      81.979   9.230  57.648  1.00 26.51           O  
ANISOU 3666  O   PRO A 503     2251   1929   5892    170    283     43       O  
ATOM   3667  CB  PRO A 503      85.104   9.908  57.892  1.00 26.38           C  
ANISOU 3667  CB  PRO A 503     2171   1889   5960    135    246    -21       C  
ATOM   3668  CG  PRO A 503      84.604  11.259  57.431  1.00 26.90           C  
ANISOU 3668  CG  PRO A 503     2304   1881   6035     69    328    -10       C  
ATOM   3669  CD  PRO A 503      84.298  11.098  55.967  1.00 26.85           C  
ANISOU 3669  CD  PRO A 503     2281   1934   5984    108    277      1       C  
ATOM   3670  N   GLN A 504      83.084   7.520  58.635  1.00 25.71           N  
ANISOU 3670  N   GLN A 504     2100   1902   5765     27    203     81       N  
ATOM   3671  CA  GLN A 504      81.910   7.083  59.402  1.00 25.53           C  
ANISOU 3671  CA  GLN A 504     2109   1924   5666    -54    132    200       C  
ATOM   3672  C   GLN A 504      81.396   8.211  60.293  1.00 25.03           C  
ANISOU 3672  C   GLN A 504     2062   1958   5490     -9    118    247       C  
ATOM   3673  O   GLN A 504      80.188   8.382  60.448  1.00 24.71           O  
ANISOU 3673  O   GLN A 504     2163   1824   5399     67     14    292       O  
ATOM   3674  CB  GLN A 504      82.224   5.846  60.249  1.00 25.22           C  
ANISOU 3674  CB  GLN A 504     1927   1932   5724    -12    157    226       C  
ATOM   3675  CG  GLN A 504      80.971   5.268  60.925  1.00 25.95           C  
ANISOU 3675  CG  GLN A 504     1995   2040   5824   -135     85    233       C  
ATOM   3676  CD  GLN A 504      79.941   4.836  59.904  1.00 25.59           C  
ANISOU 3676  CD  GLN A 504     1673   2137   5913    182    142    171       C  
ATOM   3677  OE1 GLN A 504      80.217   3.978  59.070  1.00 27.93           O  
ANISOU 3677  OE1 GLN A 504     2070   2533   6006    323    -29    -45       O  
ATOM   3678  NE2 GLN A 504      78.749   5.408  59.968  1.00 24.47           N  
ANISOU 3678  NE2 GLN A 504     1616   1797   5884    379    208    274       N  
ATOM   3679  N   SER A 505      82.318   8.987  60.860  1.00 24.52           N  
ANISOU 3679  N   SER A 505     2027   1924   5365    -18     52    248       N  
ATOM   3680  CA  SER A 505      81.958  10.120  61.718  1.00 24.83           C  
ANISOU 3680  CA  SER A 505     2045   1996   5393    -48      8    228       C  
ATOM   3681  C   SER A 505      81.052  11.125  61.005  1.00 24.60           C  
ANISOU 3681  C   SER A 505     2024   2040   5283      5    -10    142       C  
ATOM   3682  O   SER A 505      80.171  11.701  61.633  1.00 23.85           O  
ANISOU 3682  O   SER A 505     1715   2151   5194    -73     -5    158       O  
ATOM   3683  CB  SER A 505      83.204  10.840  62.229  1.00 25.59           C  
ANISOU 3683  CB  SER A 505     2148   2138   5434    -98     23    197       C  
ATOM   3684  OG  SER A 505      83.974  11.265  61.122  1.00 26.47           O  
ANISOU 3684  OG  SER A 505     2104   2099   5853   -139     18    205       O  
ATOM   3685  N   TRP A 506      81.294  11.357  59.716  1.00 24.00           N  
ANISOU 3685  N   TRP A 506     2001   1924   5191    -49    -46    142       N  
ATOM   3686  CA  TRP A 506      80.423  12.209  58.916  1.00 23.62           C  
ANISOU 3686  CA  TRP A 506     1888   1980   5106     -9    -70     44       C  
ATOM   3687  C   TRP A 506      79.039  11.593  58.722  1.00 23.78           C  
ANISOU 3687  C   TRP A 506     1970   1951   5114    -48   -109     42       C  
ATOM   3688  O   TRP A 506      78.025  12.294  58.850  1.00 23.46           O  
ANISOU 3688  O   TRP A 506     1872   1908   5134     15   -113     21       O  
ATOM   3689  CB  TRP A 506      81.055  12.510  57.559  1.00 23.63           C  
ANISOU 3689  CB  TRP A 506     1898   1975   5106    -78   -123      8       C  
ATOM   3690  CG  TRP A 506      80.198  13.330  56.638  1.00 22.93           C  
ANISOU 3690  CG  TRP A 506     1862   1973   4875     44    -56   -152       C  
ATOM   3691  CD1 TRP A 506      80.170  14.692  56.534  1.00 22.69           C  
ANISOU 3691  CD1 TRP A 506     1996   2004   4618    162     80   -252       C  
ATOM   3692  CD2 TRP A 506      79.261  12.831  55.672  1.00 23.43           C  
ANISOU 3692  CD2 TRP A 506     1936   2189   4775     14    105   -281       C  
ATOM   3693  NE1 TRP A 506      79.261  15.072  55.568  1.00 22.23           N  
ANISOU 3693  NE1 TRP A 506     1515   2249   4683    159    356   -340       N  
ATOM   3694  CE2 TRP A 506      78.698  13.949  55.020  1.00 22.26           C  
ANISOU 3694  CE2 TRP A 506     1525   2339   4592    141    183   -373       C  
ATOM   3695  CE3 TRP A 506      78.862  11.547  55.281  1.00 24.32           C  
ANISOU 3695  CE3 TRP A 506     1994   2520   4725   -264     41   -226       C  
ATOM   3696  CZ2 TRP A 506      77.766  13.823  53.997  1.00 21.52           C  
ANISOU 3696  CZ2 TRP A 506     1131   2379   4668    165    178   -408       C  
ATOM   3697  CZ3 TRP A 506      77.908  11.424  54.274  1.00 24.05           C  
ANISOU 3697  CZ3 TRP A 506     1853   2476   4809    -48      4   -291       C  
ATOM   3698  CH2 TRP A 506      77.381  12.558  53.642  1.00 23.41           C  
ANISOU 3698  CH2 TRP A 506     1610   2350   4933    293     61   -365       C  
ATOM   3699  N   SER A 507      78.995  10.296  58.425  1.00 24.28           N  
ANISOU 3699  N   SER A 507     2061   2019   5144    106    -83     23       N  
ATOM   3700  CA  SER A 507      77.714   9.602  58.231  1.00 24.52           C  
ANISOU 3700  CA  SER A 507     2169   2011   5133     12    -31     28       C  
ATOM   3701  C   SER A 507      76.859   9.609  59.498  1.00 25.07           C  
ANISOU 3701  C   SER A 507     2226   2116   5182     28    -72     74       C  
ATOM   3702  O   SER A 507      75.630   9.614  59.421  1.00 25.19           O  
ANISOU 3702  O   SER A 507     2220   2255   5095     44     56    117       O  
ATOM   3703  CB  SER A 507      77.911   8.160  57.749  1.00 25.24           C  
ANISOU 3703  CB  SER A 507     2321   2104   5163     87    -14     16       C  
ATOM   3704  OG  SER A 507      78.631   8.112  56.528  1.00 24.62           O  
ANISOU 3704  OG  SER A 507     2342   1965   5047     97    -95   -201       O  
ATOM   3705  N   ASP A 508      77.517   9.619  60.656  1.00 24.73           N  
ANISOU 3705  N   ASP A 508     2263   1954   5177     48    -95    189       N  
ATOM   3706  CA  ASP A 508      76.809   9.678  61.937  1.00 23.81           C  
ANISOU 3706  CA  ASP A 508     1974   1840   5230     70   -112    195       C  
ATOM   3707  C   ASP A 508      76.185  11.031  62.290  1.00 23.11           C  
ANISOU 3707  C   ASP A 508     1807   1713   5260     14   -133    201       C  
ATOM   3708  O   ASP A 508      75.299  11.092  63.150  1.00 22.57           O  
ANISOU 3708  O   ASP A 508     1694   1538   5341     17   -116    184       O  
ATOM   3709  CB  ASP A 508      77.752   9.269  63.073  1.00 23.28           C  
ANISOU 3709  CB  ASP A 508     1879   1824   5140    120   -131    261       C  
ATOM   3710  CG  ASP A 508      78.191   7.816  62.997  1.00 24.26           C  
ANISOU 3710  CG  ASP A 508     1981   2010   5225    216   -212    305       C  
ATOM   3711  OD1 ASP A 508      77.643   7.020  62.193  1.00 24.60           O  
ANISOU 3711  OD1 ASP A 508     2029   2133   5184    244   -354    595       O  
ATOM   3712  OD2 ASP A 508      79.111   7.471  63.775  1.00 23.46           O  
ANISOU 3712  OD2 ASP A 508     1896   1891   5125    419   -275    256       O  
ATOM   3713  N   LEU A 509      76.644  12.117  61.667  1.00 22.67           N  
ANISOU 3713  N   LEU A 509     1655   1680   5275    -57   -159    110       N  
ATOM   3714  CA  LEU A 509      76.122  13.449  62.014  1.00 22.14           C  
ANISOU 3714  CA  LEU A 509     1527   1660   5223    -92   -120    125       C  
ATOM   3715  C   LEU A 509      74.608  13.579  61.849  1.00 22.94           C  
ANISOU 3715  C   LEU A 509     1646   1775   5293   -124    -77    137       C  
ATOM   3716  O   LEU A 509      73.934  14.172  62.697  1.00 22.45           O  
ANISOU 3716  O   LEU A 509     1511   1846   5173   -106    -91     67       O  
ATOM   3717  CB  LEU A 509      76.821  14.550  61.212  1.00 21.77           C  
ANISOU 3717  CB  LEU A 509     1548   1540   5181    -65   -150     62       C  
ATOM   3718  CG  LEU A 509      78.321  14.742  61.433  1.00 21.30           C  
ANISOU 3718  CG  LEU A 509     1482   1618   4991   -235     76    -16       C  
ATOM   3719  CD1 LEU A 509      78.880  15.755  60.438  1.00 21.45           C  
ANISOU 3719  CD1 LEU A 509     1678   1394   5079      6    106    247       C  
ATOM   3720  CD2 LEU A 509      78.588  15.228  62.855  1.00 23.78           C  
ANISOU 3720  CD2 LEU A 509     1725   2287   5024   -465   -202    -83       C  
ATOM   3721  N   CYS A 510      74.066  13.055  60.752  1.00 23.74           N  
ANISOU 3721  N   CYS A 510     1777   1820   5421   -194    -57    124       N  
ATOM   3722  CA  CYS A 510      72.633  13.240  60.518  1.00 25.37           C  
ANISOU 3722  CA  CYS A 510     1915   2163   5560   -117    -55    140       C  
ATOM   3723  C   CYS A 510      71.749  12.471  61.499  1.00 25.20           C  
ANISOU 3723  C   CYS A 510     1941   2021   5611   -116    -58    107       C  
ATOM   3724  O   CYS A 510      70.817  13.062  62.058  1.00 24.82           O  
ANISOU 3724  O   CYS A 510     1618   2173   5639   -141     -3    118       O  
ATOM   3725  CB  CYS A 510      72.245  12.958  59.067  1.00 26.12           C  
ANISOU 3725  CB  CYS A 510     2228   2051   5646   -158    -84     89       C  
ATOM   3726  SG  CYS A 510      72.861  14.228  57.940  1.00 31.74           S  
ANISOU 3726  SG  CYS A 510     2874   3318   5867   -116    146    232       S  
ATOM   3727  N   PRO A 511      72.035  11.177  61.737  1.00 25.22           N  
ANISOU 3727  N   PRO A 511     1903   2054   5624    -38    -69     94       N  
ATOM   3728  CA  PRO A 511      71.219  10.493  62.747  1.00 24.94           C  
ANISOU 3728  CA  PRO A 511     1933   1950   5594    -36    -74    139       C  
ATOM   3729  C   PRO A 511      71.285  11.182  64.111  1.00 24.48           C  
ANISOU 3729  C   PRO A 511     1812   1954   5534    -23    -98    202       C  
ATOM   3730  O   PRO A 511      70.257  11.339  64.757  1.00 24.42           O  
ANISOU 3730  O   PRO A 511     1875   1904   5497    -62    -88    299       O  
ATOM   3731  CB  PRO A 511      71.829   9.086  62.810  1.00 25.95           C  
ANISOU 3731  CB  PRO A 511     2187   2026   5647   -103    -82    109       C  
ATOM   3732  CG  PRO A 511      72.419   8.881  61.461  1.00 25.53           C  
ANISOU 3732  CG  PRO A 511     1973   2022   5703    -30    102     22       C  
ATOM   3733  CD  PRO A 511      72.874  10.230  60.976  1.00 25.25           C  
ANISOU 3733  CD  PRO A 511     2030   1946   5616    -37    -61     37       C  
ATOM   3734  N   ILE A 512      72.473  11.607  64.537  1.00 23.53           N  
ANISOU 3734  N   ILE A 512     1739   1750   5451    -34   -139    254       N  
ATOM   3735  CA  ILE A 512      72.619  12.302  65.819  1.00 22.97           C  
ANISOU 3735  CA  ILE A 512     1604   1808   5314     40   -136    314       C  
ATOM   3736  C   ILE A 512      71.841  13.619  65.855  1.00 22.87           C  
ANISOU 3736  C   ILE A 512     1518   1932   5237      3   -116    304       C  
ATOM   3737  O   ILE A 512      71.121  13.902  66.818  1.00 22.89           O  
ANISOU 3737  O   ILE A 512     1577   1908   5211     22    -61    289       O  
ATOM   3738  CB  ILE A 512      74.115  12.515  66.172  1.00 22.82           C  
ANISOU 3738  CB  ILE A 512     1622   1752   5295     68   -151    285       C  
ATOM   3739  CG1 ILE A 512      74.772  11.148  66.437  1.00 22.86           C  
ANISOU 3739  CG1 ILE A 512     1349   1963   5370    256   -130    302       C  
ATOM   3740  CG2 ILE A 512      74.275  13.479  67.348  1.00 23.40           C  
ANISOU 3740  CG2 ILE A 512     1578   1754   5557    -95   -159    221       C  
ATOM   3741  CD1 ILE A 512      76.294  11.185  66.449  1.00 22.83           C  
ANISOU 3741  CD1 ILE A 512     1168   2014   5492    124    -14    308       C  
ATOM   3742  N   TYR A 513      71.992  14.427  64.809  1.00 21.96           N  
ANISOU 3742  N   TYR A 513     1383   1874   5084    -15   -128    381       N  
ATOM   3743  CA  TYR A 513      71.293  15.708  64.743  1.00 22.42           C  
ANISOU 3743  CA  TYR A 513     1435   2051   5031     24    -40    394       C  
ATOM   3744  C   TYR A 513      69.771  15.525  64.695  1.00 22.71           C  
ANISOU 3744  C   TYR A 513     1480   2174   4974    -29   -133    389       C  
ATOM   3745  O   TYR A 513      69.012  16.265  65.332  1.00 22.84           O  
ANISOU 3745  O   TYR A 513     1455   2412   4810    -82   -109    514       O  
ATOM   3746  CB  TYR A 513      71.773  16.517  63.538  1.00 21.92           C  
ANISOU 3746  CB  TYR A 513     1450   1880   4996    115    -74    416       C  
ATOM   3747  CG  TYR A 513      71.071  17.852  63.405  1.00 21.68           C  
ANISOU 3747  CG  TYR A 513     1443   1953   4841    157     80    336       C  
ATOM   3748  CD1 TYR A 513      71.480  18.940  64.171  1.00 20.43           C  
ANISOU 3748  CD1 TYR A 513     1202   1776   4783    206     75    360       C  
ATOM   3749  CD2 TYR A 513      70.009  18.020  62.523  1.00 20.71           C  
ANISOU 3749  CD2 TYR A 513     1279   1864   4723    247    226    417       C  
ATOM   3750  CE1 TYR A 513      70.864  20.168  64.060  1.00 20.55           C  
ANISOU 3750  CE1 TYR A 513     1306   1969   4533    188    117    370       C  
ATOM   3751  CE2 TYR A 513      69.367  19.250  62.412  1.00 22.29           C  
ANISOU 3751  CE2 TYR A 513     1475   2068   4924    489     58    233       C  
ATOM   3752  CZ  TYR A 513      69.807  20.317  63.188  1.00 21.19           C  
ANISOU 3752  CZ  TYR A 513     1231   2015   4803    323    164    374       C  
ATOM   3753  OH  TYR A 513      69.202  21.544  63.103  1.00 23.42           O  
ANISOU 3753  OH  TYR A 513     1656   2110   5132    403   -284    241       O  
ATOM   3754  N   ASP A 514      69.324  14.541  63.924  1.00 23.49           N  
ANISOU 3754  N   ASP A 514     1592   2346   4984    -74    -58    354       N  
ATOM   3755  CA  ASP A 514      67.894  14.371  63.666  1.00 23.23           C  
ANISOU 3755  CA  ASP A 514     1575   2371   4877   -140    -39    305       C  
ATOM   3756  C   ASP A 514      67.173  13.842  64.898  1.00 23.71           C  
ANISOU 3756  C   ASP A 514     1459   2406   5143   -125     35    375       C  
ATOM   3757  O   ASP A 514      65.953  13.918  64.980  1.00 23.77           O  
ANISOU 3757  O   ASP A 514     1272   2466   5291   -220    -69    467       O  
ATOM   3758  CB  ASP A 514      67.673  13.424  62.490  1.00 23.45           C  
ANISOU 3758  CB  ASP A 514     1751   2535   4623   -165    -10    255       C  
ATOM   3759  CG  ASP A 514      67.949  14.078  61.161  1.00 24.05           C  
ANISOU 3759  CG  ASP A 514     2334   2617   4184    -53   -145    -40       C  
ATOM   3760  OD1 ASP A 514      67.917  15.324  61.102  1.00 26.44           O  
ANISOU 3760  OD1 ASP A 514     2734   3011   4301   -317   -238     -7       O  
ATOM   3761  OD2 ASP A 514      68.206  13.360  60.168  1.00 26.14           O  
ANISOU 3761  OD2 ASP A 514     2623   3360   3948    -94    -18   -203       O  
ATOM   3762  N   ALA A 515      67.933  13.322  65.859  1.00 23.90           N  
ANISOU 3762  N   ALA A 515     1510   2280   5289   -146     87    416       N  
ATOM   3763  CA  ALA A 515      67.373  12.863  67.120  1.00 24.48           C  
ANISOU 3763  CA  ALA A 515     1544   2343   5413   -139    226    407       C  
ATOM   3764  C   ALA A 515      67.090  14.007  68.101  1.00 25.50           C  
ANISOU 3764  C   ALA A 515     1774   2401   5514   -218    269    395       C  
ATOM   3765  O   ALA A 515      66.309  13.835  69.033  1.00 26.41           O  
ANISOU 3765  O   ALA A 515     1947   2492   5593   -238    326    328       O  
ATOM   3766  CB  ALA A 515      68.247  11.778  67.754  1.00 23.47           C  
ANISOU 3766  CB  ALA A 515     1417   2196   5302   -176    305    505       C  
ATOM   3767  N   LEU A 516      67.666  15.181  67.865  1.00 25.43           N  
ANISOU 3767  N   LEU A 516     1677   2410   5572   -243    228    307       N  
ATOM   3768  CA  LEU A 516      67.461  16.342  68.731  1.00 25.87           C  
ANISOU 3768  CA  LEU A 516     1716   2460   5654   -177    309    338       C  
ATOM   3769  C   LEU A 516      66.054  16.933  68.715  1.00 26.34           C  
ANISOU 3769  C   LEU A 516     1745   2506   5756   -197    343    338       C  
ATOM   3770  O   LEU A 516      65.443  17.099  67.658  1.00 26.70           O  
ANISOU 3770  O   LEU A 516     1781   2517   5843   -184    325    303       O  
ATOM   3771  CB  LEU A 516      68.431  17.457  68.332  1.00 25.00           C  
ANISOU 3771  CB  LEU A 516     1537   2421   5539   -188    333    260       C  
ATOM   3772  CG  LEU A 516      69.929  17.163  68.354  1.00 25.13           C  
ANISOU 3772  CG  LEU A 516     1658   2426   5464   -106    314    407       C  
ATOM   3773  CD1 LEU A 516      70.637  18.393  67.804  1.00 22.76           C  
ANISOU 3773  CD1 LEU A 516     1075   2297   5272   -315    523    157       C  
ATOM   3774  CD2 LEU A 516      70.387  16.886  69.766  1.00 24.98           C  
ANISOU 3774  CD2 LEU A 516     1697   2472   5319    409    322    401       C  
ATOM   3775  N   ALA A 517      65.551  17.286  69.892  1.00 26.66           N  
ANISOU 3775  N   ALA A 517     1768   2520   5838   -160    396    367       N  
ATOM   3776  CA  ALA A 517      64.389  18.167  69.971  1.00 27.65           C  
ANISOU 3776  CA  ALA A 517     1784   2776   5945   -108    436    451       C  
ATOM   3777  C   ALA A 517      64.777  19.547  69.429  1.00 28.00           C  
ANISOU 3777  C   ALA A 517     1821   2769   6048    -62    378    426       C  
ATOM   3778  O   ALA A 517      65.953  19.926  69.453  1.00 27.45           O  
ANISOU 3778  O   ALA A 517     1672   2747   6008    -94    402    439       O  
ATOM   3779  CB  ALA A 517      63.916  18.278  71.409  1.00 28.30           C  
ANISOU 3779  CB  ALA A 517     1890   2875   5986    -46    425    388       C  
ATOM   3780  N   GLU A 518      63.795  20.283  68.921  1.00 28.20           N  
ANISOU 3780  N   GLU A 518     1675   2984   6055    -15    320    461       N  
ATOM   3781  CA  GLU A 518      64.019  21.622  68.384  1.00 29.41           C  
ANISOU 3781  CA  GLU A 518     1913   3140   6121     82    325    510       C  
ATOM   3782  C   GLU A 518      64.792  22.525  69.346  1.00 29.55           C  
ANISOU 3782  C   GLU A 518     1997   3177   6052    121    337    519       C  
ATOM   3783  O   GLU A 518      65.709  23.219  68.907  1.00 28.28           O  
ANISOU 3783  O   GLU A 518     1765   3020   5959    145    315    524       O  
ATOM   3784  CB  GLU A 518      62.703  22.291  67.967  1.00 30.74           C  
ANISOU 3784  CB  GLU A 518     2100   3341   6236    107    214    591       C  
ATOM   3785  CG  GLU A 518      62.885  23.747  67.539  1.00 33.69           C  
ANISOU 3785  CG  GLU A 518     2287   3743   6768     95    236    849       C  
ATOM   3786  CD  GLU A 518      61.702  24.316  66.777  1.00 39.34           C  
ANISOU 3786  CD  GLU A 518     3114   4595   7236     22      8   1276       C  
ATOM   3787  OE1 GLU A 518      60.568  23.802  66.916  1.00 41.36           O  
ANISOU 3787  OE1 GLU A 518     2961   5286   7466     -1     87   1292       O  
ATOM   3788  OE2 GLU A 518      61.917  25.301  66.039  1.00 42.70           O  
ANISOU 3788  OE2 GLU A 518     3927   4768   7527     -6     96   1446       O  
ATOM   3789  N   ASP A 519      64.436  22.520  70.632  1.00 29.64           N  
ANISOU 3789  N   ASP A 519     2136   3235   5888    122    429    442       N  
ATOM   3790  CA  ASP A 519      65.106  23.388  71.611  1.00 30.63           C  
ANISOU 3790  CA  ASP A 519     2366   3377   5892     90    478    426       C  
ATOM   3791  C   ASP A 519      66.572  23.019  71.850  1.00 29.16           C  
ANISOU 3791  C   ASP A 519     2188   3220   5670    -49    551    402       C  
ATOM   3792  O   ASP A 519      67.314  23.784  72.470  1.00 28.97           O  
ANISOU 3792  O   ASP A 519     2183   3073   5749     31    638    357       O  
ATOM   3793  CB  ASP A 519      64.355  23.415  72.955  1.00 32.65           C  
ANISOU 3793  CB  ASP A 519     2679   3689   6035     81    523    425       C  
ATOM   3794  CG  ASP A 519      64.918  24.459  73.936  1.00 37.93           C  
ANISOU 3794  CG  ASP A 519     3707   4259   6445    152    394    379       C  
ATOM   3795  OD1 ASP A 519      64.955  25.673  73.606  1.00 43.07           O  
ANISOU 3795  OD1 ASP A 519     4921   4533   6909    349    499    475       O  
ATOM   3796  OD2 ASP A 519      65.338  24.069  75.053  1.00 42.96           O  
ANISOU 3796  OD2 ASP A 519     4329   5191   6800    563    361    648       O  
ATOM   3797  N   ASP A 520      66.975  21.847  71.369  1.00 26.88           N  
ANISOU 3797  N   ASP A 520     1986   2848   5379   -107    520    433       N  
ATOM   3798  CA  ASP A 520      68.352  21.379  71.522  1.00 26.52           C  
ANISOU 3798  CA  ASP A 520     2048   2838   5189   -327    518    425       C  
ATOM   3799  C   ASP A 520      69.181  21.539  70.246  1.00 25.41           C  
ANISOU 3799  C   ASP A 520     1856   2756   5042   -387    435    334       C  
ATOM   3800  O   ASP A 520      70.371  21.213  70.230  1.00 25.39           O  
ANISOU 3800  O   ASP A 520     1876   2843   4926   -358    439    288       O  
ATOM   3801  CB  ASP A 520      68.335  19.931  72.043  1.00 27.37           C  
ANISOU 3801  CB  ASP A 520     2185   2936   5277   -228    533    437       C  
ATOM   3802  CG  ASP A 520      67.956  19.857  73.524  1.00 29.56           C  
ANISOU 3802  CG  ASP A 520     2620   3185   5426   -415    523    458       C  
ATOM   3803  OD1 ASP A 520      68.398  20.748  74.292  1.00 32.21           O  
ANISOU 3803  OD1 ASP A 520     3211   3463   5562   -446    403    177       O  
ATOM   3804  OD2 ASP A 520      67.227  18.924  73.928  1.00 30.04           O  
ANISOU 3804  OD2 ASP A 520     2653   3272   5486   -487    607    607       O  
ATOM   3805  N   GLN A 521      68.565  22.078  69.192  1.00 24.05           N  
ANISOU 3805  N   GLN A 521     1683   2603   4850   -520    446    342       N  
ATOM   3806  CA  GLN A 521      69.276  22.304  67.930  1.00 23.53           C  
ANISOU 3806  CA  GLN A 521     1568   2623   4750   -533    317    301       C  
ATOM   3807  C   GLN A 521      70.153  23.560  67.976  1.00 23.16           C  
ANISOU 3807  C   GLN A 521     1497   2618   4682   -546    364    350       C  
ATOM   3808  O   GLN A 521      70.034  24.384  68.898  1.00 22.16           O  
ANISOU 3808  O   GLN A 521     1313   2604   4501   -571    361    306       O  
ATOM   3809  CB  GLN A 521      68.300  22.400  66.763  1.00 23.52           C  
ANISOU 3809  CB  GLN A 521     1594   2591   4750   -544    355    301       C  
ATOM   3810  CG  GLN A 521      67.532  21.133  66.464  1.00 24.43           C  
ANISOU 3810  CG  GLN A 521     1679   2720   4883   -489     86     72       C  
ATOM   3811  CD  GLN A 521      66.481  21.366  65.399  1.00 26.10           C  
ANISOU 3811  CD  GLN A 521     1701   2818   5397   -388   -236     39       C  
ATOM   3812  OE1 GLN A 521      66.024  22.495  65.177  1.00 28.84           O  
ANISOU 3812  OE1 GLN A 521     1980   3167   5810   -381   -610    106       O  
ATOM   3813  NE2 GLN A 521      66.083  20.297  64.736  1.00 25.28           N  
ANISOU 3813  NE2 GLN A 521     1683   2736   5185    125   -420   -139       N  
ATOM   3814  OXT GLN A 521      70.977  23.777  67.073  1.00 21.96           O  
ANISOU 3814  OXT GLN A 521     1242   2565   4534   -474    402    287       O  
TER    3815      GLN A 521                                                      
ATOM   3816  N   SER B  22      52.957  80.557  55.096  1.00 33.65           N  
ANISOU 3816  N   SER B  22     1473   2532   8781    415   -911   -295       N  
ATOM   3817  CA  SER B  22      54.096  81.324  54.504  1.00 34.30           C  
ANISOU 3817  CA  SER B  22     1559   2742   8728    424  -1049   -367       C  
ATOM   3818  C   SER B  22      53.964  82.810  54.812  1.00 34.10           C  
ANISOU 3818  C   SER B  22     1570   2657   8728    479  -1008   -308       C  
ATOM   3819  O   SER B  22      52.912  83.287  55.253  1.00 34.05           O  
ANISOU 3819  O   SER B  22     1570   2667   8700    410   -949   -327       O  
ATOM   3820  CB  SER B  22      54.118  81.173  52.981  1.00 34.48           C  
ANISOU 3820  CB  SER B  22     1571   2748   8781    487   -979   -362       C  
ATOM   3821  OG  SER B  22      52.879  81.615  52.440  1.00 36.57           O  
ANISOU 3821  OG  SER B  22     2050   3097   8747    665  -1359   -587       O  
ATOM   3822  N   VAL B  23      55.036  83.537  54.520  1.00 34.25           N  
ANISOU 3822  N   VAL B  23     1585   2740   8685    515  -1038   -306       N  
ATOM   3823  CA  VAL B  23      55.057  84.994  54.608  1.00 34.48           C  
ANISOU 3823  CA  VAL B  23     1753   2688   8660    596  -1060   -265       C  
ATOM   3824  C   VAL B  23      55.641  85.572  53.320  1.00 35.43           C  
ANISOU 3824  C   VAL B  23     1986   2823   8652    616  -1090   -207       C  
ATOM   3825  O   VAL B  23      56.271  84.844  52.544  1.00 35.76           O  
ANISOU 3825  O   VAL B  23     2149   2795   8640    588  -1096   -173       O  
ATOM   3826  CB  VAL B  23      55.901  85.471  55.817  1.00 34.03           C  
ANISOU 3826  CB  VAL B  23     1581   2720   8628    651  -1083   -286       C  
ATOM   3827  CG1 VAL B  23      55.281  84.975  57.114  1.00 34.35           C  
ANISOU 3827  CG1 VAL B  23     1812   2586   8654    599  -1088   -360       C  
ATOM   3828  CG2 VAL B  23      57.372  85.007  55.713  1.00 33.52           C  
ANISOU 3828  CG2 VAL B  23     1621   2481   8631    734   -987   -327       C  
ATOM   3829  N   GLY B  24      55.459  86.875  53.109  1.00 35.89           N  
ANISOU 3829  N   GLY B  24     2156   2895   8583    663  -1140   -115       N  
ATOM   3830  CA  GLY B  24      56.152  87.586  52.034  1.00 35.97           C  
ANISOU 3830  CA  GLY B  24     2143   3001   8522    632  -1166    -58       C  
ATOM   3831  C   GLY B  24      55.213  87.907  50.881  1.00 36.32           C  
ANISOU 3831  C   GLY B  24     2189   3109   8499    631  -1166    -20       C  
ATOM   3832  O   GLY B  24      54.088  87.408  50.846  1.00 36.45           O  
ANISOU 3832  O   GLY B  24     2050   3345   8452    585  -1259    -19       O  
ATOM   3833  N   PRO B  25      55.672  88.703  49.899  1.00 36.28           N  
ANISOU 3833  N   PRO B  25     2242   3095   8447    666  -1169      9       N  
ATOM   3834  CA  PRO B  25      57.007  89.277  49.743  1.00 36.04           C  
ANISOU 3834  CA  PRO B  25     2272   3067   8353    643  -1168      8       C  
ATOM   3835  C   PRO B  25      57.346  90.414  50.710  1.00 35.82           C  
ANISOU 3835  C   PRO B  25     2239   3110   8261    682  -1146      8       C  
ATOM   3836  O   PRO B  25      58.512  90.780  50.821  1.00 35.43           O  
ANISOU 3836  O   PRO B  25     2223   3027   8210    620  -1138     28       O  
ATOM   3837  CB  PRO B  25      56.989  89.796  48.302  1.00 36.58           C  
ANISOU 3837  CB  PRO B  25     2379   3145   8375    659  -1167     23       C  
ATOM   3838  CG  PRO B  25      55.549  90.097  48.033  1.00 36.42           C  
ANISOU 3838  CG  PRO B  25     2291   3171   8373    578  -1160     16       C  
ATOM   3839  CD  PRO B  25      54.823  88.972  48.723  1.00 36.48           C  
ANISOU 3839  CD  PRO B  25     2317   3108   8436    605  -1180      4       C  
ATOM   3840  N   VAL B  26      56.348  90.961  51.400  1.00 34.84           N  
ANISOU 3840  N   VAL B  26     2094   2991   8151    764  -1155     12       N  
ATOM   3841  CA  VAL B  26      56.587  91.951  52.448  1.00 34.87           C  
ANISOU 3841  CA  VAL B  26     2111   3019   8116    722  -1095      0       C  
ATOM   3842  C   VAL B  26      56.299  91.275  53.791  1.00 34.61           C  
ANISOU 3842  C   VAL B  26     1997   3100   8052    611  -1062    -58       C  
ATOM   3843  O   VAL B  26      55.177  90.822  54.030  1.00 35.36           O  
ANISOU 3843  O   VAL B  26     1979   3303   8153    510  -1033     -8       O  
ATOM   3844  CB  VAL B  26      55.691  93.201  52.251  1.00 35.16           C  
ANISOU 3844  CB  VAL B  26     2209   2992   8157    751  -1115    -48       C  
ATOM   3845  CG1 VAL B  26      55.945  94.224  53.350  1.00 36.16           C  
ANISOU 3845  CG1 VAL B  26     2442   3152   8143    777  -1099    -57       C  
ATOM   3846  CG2 VAL B  26      55.957  93.833  50.881  1.00 35.01           C  
ANISOU 3846  CG2 VAL B  26     2282   2895   8122    923  -1162     42       C  
ATOM   3847  N   ALA B  27      57.292  91.221  54.675  1.00 33.04           N  
ANISOU 3847  N   ALA B  27     1732   2962   7857    528   -991   -133       N  
ATOM   3848  CA  ALA B  27      57.189  90.399  55.878  1.00 32.48           C  
ANISOU 3848  CA  ALA B  27     1800   2861   7681    482   -989   -219       C  
ATOM   3849  C   ALA B  27      58.145  90.834  56.977  1.00 31.69           C  
ANISOU 3849  C   ALA B  27     1719   2782   7539    464   -902   -237       C  
ATOM   3850  O   ALA B  27      59.222  91.367  56.698  1.00 32.07           O  
ANISOU 3850  O   ALA B  27     1835   2791   7559    427   -964   -294       O  
ATOM   3851  CB  ALA B  27      57.455  88.919  55.540  1.00 32.06           C  
ANISOU 3851  CB  ALA B  27     1681   2862   7637    442  -1039   -229       C  
ATOM   3852  N   ASN B  28      57.743  90.588  58.220  1.00 31.19           N  
ANISOU 3852  N   ASN B  28     1717   2729   7405    445   -807   -309       N  
ATOM   3853  CA  ASN B  28      58.673  90.595  59.350  1.00 30.33           C  
ANISOU 3853  CA  ASN B  28     1653   2659   7211    433   -616   -358       C  
ATOM   3854  C   ASN B  28      59.180  89.186  59.632  1.00 29.67           C  
ANISOU 3854  C   ASN B  28     1628   2608   7037    375   -530   -328       C  
ATOM   3855  O   ASN B  28      58.412  88.218  59.624  1.00 29.86           O  
ANISOU 3855  O   ASN B  28     1691   2545   7107    355   -549   -369       O  
ATOM   3856  CB  ASN B  28      58.011  91.168  60.606  1.00 30.71           C  
ANISOU 3856  CB  ASN B  28     1694   2734   7239    394   -592   -365       C  
ATOM   3857  CG  ASN B  28      57.611  92.620  60.439  1.00 31.38           C  
ANISOU 3857  CG  ASN B  28     1705   2912   7304    523   -518   -426       C  
ATOM   3858  OD1 ASN B  28      58.271  93.385  59.734  1.00 32.29           O  
ANISOU 3858  OD1 ASN B  28     2199   2788   7281    342   -477   -382       O  
ATOM   3859  ND2 ASN B  28      56.520  93.009  61.090  1.00 35.25           N  
ANISOU 3859  ND2 ASN B  28     2305   3551   7536    751   -203   -506       N  
ATOM   3860  N   LEU B  29      60.485  89.089  59.860  1.00 28.48           N  
ANISOU 3860  N   LEU B  29     1533   2502   6786    417   -337   -322       N  
ATOM   3861  CA  LEU B  29      61.139  87.846  60.240  1.00 27.71           C  
ANISOU 3861  CA  LEU B  29     1546   2465   6516    359   -220   -323       C  
ATOM   3862  C   LEU B  29      61.809  88.076  61.590  1.00 27.34           C  
ANISOU 3862  C   LEU B  29     1508   2514   6363    361   -122   -326       C  
ATOM   3863  O   LEU B  29      62.877  88.688  61.668  1.00 26.84           O  
ANISOU 3863  O   LEU B  29     1463   2528   6208    342   -171   -303       O  
ATOM   3864  CB  LEU B  29      62.173  87.436  59.185  1.00 27.37           C  
ANISOU 3864  CB  LEU B  29     1480   2433   6483    328   -192   -339       C  
ATOM   3865  CG  LEU B  29      61.644  87.235  57.758  1.00 27.59           C  
ANISOU 3865  CG  LEU B  29     1549   2432   6498    195   -143   -331       C  
ATOM   3866  CD1 LEU B  29      62.790  87.084  56.755  1.00 26.44           C  
ANISOU 3866  CD1 LEU B  29     1311   2276   6457   -123    -39   -350       C  
ATOM   3867  CD2 LEU B  29      60.704  86.040  57.687  1.00 29.01           C  
ANISOU 3867  CD2 LEU B  29     1658   2721   6641     29    -63   -173       C  
ATOM   3868  N   LYS B  30      61.159  87.588  62.642  1.00 26.93           N  
ANISOU 3868  N   LYS B  30     1450   2558   6224    409     48   -408       N  
ATOM   3869  CA  LYS B  30      61.666  87.718  64.003  1.00 26.25           C  
ANISOU 3869  CA  LYS B  30     1288   2561   6125    377     96   -420       C  
ATOM   3870  C   LYS B  30      62.645  86.596  64.277  1.00 25.41           C  
ANISOU 3870  C   LYS B  30     1375   2366   5912    301     83   -442       C  
ATOM   3871  O   LYS B  30      62.299  85.416  64.222  1.00 25.20           O  
ANISOU 3871  O   LYS B  30     1305   2346   5923    178     74   -313       O  
ATOM   3872  CB  LYS B  30      60.540  87.708  65.040  1.00 27.42           C  
ANISOU 3872  CB  LYS B  30     1568   2640   6208    429    199   -451       C  
ATOM   3873  CG  LYS B  30      59.732  88.989  65.021  1.00 29.65           C  
ANISOU 3873  CG  LYS B  30     1492   3147   6624    603    447   -419       C  
ATOM   3874  CD  LYS B  30      58.583  88.961  66.012  1.00 34.67           C  
ANISOU 3874  CD  LYS B  30     2132   4042   6996    892   1033   -620       C  
ATOM   3875  CE  LYS B  30      57.797  90.256  65.922  1.00 37.17           C  
ANISOU 3875  CE  LYS B  30     2506   4250   7364    912   1195   -631       C  
ATOM   3876  NZ  LYS B  30      56.663  90.264  66.888  1.00 40.85           N  
ANISOU 3876  NZ  LYS B  30     2891   4941   7687   1129   1504   -664       N  
ATOM   3877  N   ILE B  31      63.882  86.986  64.555  1.00 23.70           N  
ANISOU 3877  N   ILE B  31     1161   2182   5660    238    111   -435       N  
ATOM   3878  CA  ILE B  31      64.942  86.022  64.837  1.00 22.57           C  
ANISOU 3878  CA  ILE B  31     1219   2035   5321    235    107   -451       C  
ATOM   3879  C   ILE B  31      65.141  85.946  66.347  1.00 22.88           C  
ANISOU 3879  C   ILE B  31     1356   2113   5221    177    168   -450       C  
ATOM   3880  O   ILE B  31      65.406  86.956  67.006  1.00 23.89           O  
ANISOU 3880  O   ILE B  31     1752   2161   5163    153    154   -354       O  
ATOM   3881  CB  ILE B  31      66.269  86.431  64.180  1.00 22.01           C  
ANISOU 3881  CB  ILE B  31     1099   1936   5325    193     20   -474       C  
ATOM   3882  CG1 ILE B  31      66.091  86.816  62.701  1.00 22.44           C  
ANISOU 3882  CG1 ILE B  31     1249   1986   5289    -29     22   -597       C  
ATOM   3883  CG2 ILE B  31      67.309  85.332  64.390  1.00 20.33           C  
ANISOU 3883  CG2 ILE B  31      802   1628   5294    200     68   -490       C  
ATOM   3884  CD1 ILE B  31      65.504  85.723  61.790  1.00 23.77           C  
ANISOU 3884  CD1 ILE B  31     1747   2158   5127    238   -267   -773       C  
ATOM   3885  N   GLY B  32      65.001  84.751  66.904  1.00 22.49           N  
ANISOU 3885  N   GLY B  32     1409   2134   5002    228    241   -459       N  
ATOM   3886  CA  GLY B  32      65.039  84.610  68.348  1.00 22.75           C  
ANISOU 3886  CA  GLY B  32     1508   2233   4900     94    370   -471       C  
ATOM   3887  C   GLY B  32      65.598  83.266  68.754  1.00 22.57           C  
ANISOU 3887  C   GLY B  32     1436   2358   4780    125    450   -504       C  
ATOM   3888  O   GLY B  32      65.892  82.425  67.906  1.00 22.15           O  
ANISOU 3888  O   GLY B  32     1280   2419   4714    104    541   -501       O  
ATOM   3889  N   ASN B  33      65.709  83.062  70.063  1.00 22.71           N  
ANISOU 3889  N   ASN B  33     1522   2441   4664     50    482   -506       N  
ATOM   3890  CA  ASN B  33      66.148  81.788  70.614  1.00 22.45           C  
ANISOU 3890  CA  ASN B  33     1469   2475   4586     -1    599   -502       C  
ATOM   3891  C   ASN B  33      64.940  81.071  71.198  1.00 22.83           C  
ANISOU 3891  C   ASN B  33     1518   2517   4637      0    663   -451       C  
ATOM   3892  O   ASN B  33      64.072  81.709  71.802  1.00 21.82           O  
ANISOU 3892  O   ASN B  33     1292   2561   4435     33    863   -385       O  
ATOM   3893  CB  ASN B  33      67.205  82.010  71.691  1.00 22.24           C  
ANISOU 3893  CB  ASN B  33     1415   2538   4494     33    641   -481       C  
ATOM   3894  CG  ASN B  33      68.491  82.562  71.125  1.00 22.61           C  
ANISOU 3894  CG  ASN B  33     1364   2655   4572    -82    462   -682       C  
ATOM   3895  OD1 ASN B  33      69.162  81.932  70.296  1.00 24.96           O  
ANISOU 3895  OD1 ASN B  33     1593   3243   4646   -180    575   -760       O  
ATOM   3896  ND2 ASN B  33      68.831  83.759  71.549  1.00 20.88           N  
ANISOU 3896  ND2 ASN B  33     1269   2708   3954   -146    523   -811       N  
ATOM   3897  N   ALA B  34      64.877  79.757  70.993  1.00 23.00           N  
ANISOU 3897  N   ALA B  34     1525   2510   4703   -116    637   -423       N  
ATOM   3898  CA  ALA B  34      63.832  78.953  71.615  1.00 23.44           C  
ANISOU 3898  CA  ALA B  34     1701   2439   4766   -180    642   -365       C  
ATOM   3899  C   ALA B  34      64.329  77.526  71.823  1.00 23.09           C  
ANISOU 3899  C   ALA B  34     1722   2341   4707   -159    682   -375       C  
ATOM   3900  O   ALA B  34      65.243  77.079  71.137  1.00 23.61           O  
ANISOU 3900  O   ALA B  34     1980   2314   4676   -223    785   -315       O  
ATOM   3901  CB  ALA B  34      62.567  78.963  70.756  1.00 23.12           C  
ANISOU 3901  CB  ALA B  34     1613   2433   4739    -68    596   -448       C  
ATOM   3902  N   ALA B  35      63.742  76.822  72.786  1.00 23.17           N  
ANISOU 3902  N   ALA B  35     1791   2297   4715   -241    723   -382       N  
ATOM   3903  CA  ALA B  35      63.984  75.390  72.925  1.00 22.84           C  
ANISOU 3903  CA  ALA B  35     1779   2225   4672   -245    774   -456       C  
ATOM   3904  C   ALA B  35      63.068  74.711  71.910  1.00 23.22           C  
ANISOU 3904  C   ALA B  35     1814   2257   4752   -257    760   -493       C  
ATOM   3905  O   ALA B  35      61.863  75.015  71.846  1.00 22.59           O  
ANISOU 3905  O   ALA B  35     1647   2147   4787    -79    787   -532       O  
ATOM   3906  CB  ALA B  35      63.678  74.912  74.355  1.00 23.72           C  
ANISOU 3906  CB  ALA B  35     2008   2306   4696   -254    755   -367       C  
ATOM   3907  N   VAL B  36      63.653  73.825  71.106  1.00 21.89           N  
ANISOU 3907  N   VAL B  36     1651   1987   4679   -262    747   -524       N  
ATOM   3908  CA  VAL B  36      62.925  73.097  70.057  1.00 22.15           C  
ANISOU 3908  CA  VAL B  36     1794   2020   4600   -308    675   -453       C  
ATOM   3909  C   VAL B  36      63.227  71.600  70.146  1.00 22.07           C  
ANISOU 3909  C   VAL B  36     1749   2070   4565   -320    712   -428       C  
ATOM   3910  O   VAL B  36      64.245  71.205  70.717  1.00 21.23           O  
ANISOU 3910  O   VAL B  36     1741   2039   4285   -414    600   -372       O  
ATOM   3911  CB  VAL B  36      63.293  73.602  68.647  1.00 22.24           C  
ANISOU 3911  CB  VAL B  36     1860   1957   4633   -266    676   -499       C  
ATOM   3912  CG1 VAL B  36      62.860  75.078  68.458  1.00 23.12           C  
ANISOU 3912  CG1 VAL B  36     2156   1988   4638   -163    661   -531       C  
ATOM   3913  CG2 VAL B  36      64.790  73.429  68.367  1.00 22.37           C  
ANISOU 3913  CG2 VAL B  36     1854   2102   4542   -330    586   -496       C  
ATOM   3914  N   SER B  37      62.354  70.756  69.595  1.00 22.06           N  
ANISOU 3914  N   SER B  37     1637   2217   4525   -292    639   -384       N  
ATOM   3915  CA  SER B  37      62.658  69.325  69.522  1.00 23.27           C  
ANISOU 3915  CA  SER B  37     1888   2332   4621   -221    694   -242       C  
ATOM   3916  C   SER B  37      62.215  68.669  68.216  1.00 22.04           C  
ANISOU 3916  C   SER B  37     1606   2224   4544   -252    636   -314       C  
ATOM   3917  O   SER B  37      61.303  67.833  68.207  1.00 21.24           O  
ANISOU 3917  O   SER B  37     1296   2223   4550   -262    701   -314       O  
ATOM   3918  CB  SER B  37      62.147  68.542  70.743  1.00 24.36           C  
ANISOU 3918  CB  SER B  37     1866   2676   4711   -182    804   -138       C  
ATOM   3919  OG  SER B  37      60.930  69.057  71.192  1.00 28.89           O  
ANISOU 3919  OG  SER B  37     3145   2645   5185    394   1041     64       O  
ATOM   3920  N   PRO B  38      62.882  69.050  67.116  1.00 21.43           N  
ANISOU 3920  N   PRO B  38     1578   2110   4453   -219    512   -353       N  
ATOM   3921  CA  PRO B  38      62.492  68.592  65.799  1.00 21.89           C  
ANISOU 3921  CA  PRO B  38     1560   2190   4567   -184    435   -309       C  
ATOM   3922  C   PRO B  38      62.655  67.080  65.654  1.00 21.61           C  
ANISOU 3922  C   PRO B  38     1487   2102   4619   -215    389   -304       C  
ATOM   3923  O   PRO B  38      61.980  66.481  64.818  1.00 21.64           O  
ANISOU 3923  O   PRO B  38     1397   2191   4631   -157    342   -281       O  
ATOM   3924  CB  PRO B  38      63.448  69.342  64.871  1.00 21.45           C  
ANISOU 3924  CB  PRO B  38     1454   2142   4553   -307    379   -243       C  
ATOM   3925  CG  PRO B  38      64.677  69.644  65.737  1.00 22.65           C  
ANISOU 3925  CG  PRO B  38     1815   2326   4463   -223    356   -337       C  
ATOM   3926  CD  PRO B  38      64.023  69.982  67.056  1.00 21.29           C  
ANISOU 3926  CD  PRO B  38     1469   2235   4384   -265    603   -302       C  
ATOM   3927  N   ASP B  39      63.536  66.488  66.460  1.00 21.18           N  
ANISOU 3927  N   ASP B  39     1237   2121   4688   -195    357   -324       N  
ATOM   3928  CA  ASP B  39      63.798  65.048  66.396  1.00 21.48           C  
ANISOU 3928  CA  ASP B  39     1159   2276   4723   -185    396   -303       C  
ATOM   3929  C   ASP B  39      63.524  64.397  67.748  1.00 21.64           C  
ANISOU 3929  C   ASP B  39     1105   2350   4768   -271    344   -338       C  
ATOM   3930  O   ASP B  39      64.042  63.331  68.065  1.00 21.53           O  
ANISOU 3930  O   ASP B  39      988   2366   4823   -311    378   -357       O  
ATOM   3931  CB  ASP B  39      65.233  64.779  65.899  1.00 20.70           C  
ANISOU 3931  CB  ASP B  39      934   2221   4707   -229    356   -268       C  
ATOM   3932  CG  ASP B  39      66.290  65.287  66.853  1.00 21.26           C  
ANISOU 3932  CG  ASP B  39     1118   2275   4682   -111    359   -176       C  
ATOM   3933  OD1 ASP B  39      65.914  65.886  67.879  1.00 21.41           O  
ANISOU 3933  OD1 ASP B  39     1232   2503   4399   -170    247     -3       O  
ATOM   3934  OD2 ASP B  39      67.500  65.114  66.566  1.00 20.70           O  
ANISOU 3934  OD2 ASP B  39      729   2230   4904    -54     68   -257       O  
ATOM   3935  N   GLY B  40      62.671  65.037  68.544  1.00 22.74           N  
ANISOU 3935  N   GLY B  40     1400   2517   4722   -321    354   -379       N  
ATOM   3936  CA  GLY B  40      62.288  64.479  69.827  1.00 23.51           C  
ANISOU 3936  CA  GLY B  40     1526   2573   4834   -413    343   -276       C  
ATOM   3937  C   GLY B  40      63.236  64.741  70.972  1.00 23.66           C  
ANISOU 3937  C   GLY B  40     1534   2648   4807   -374    318   -258       C  
ATOM   3938  O   GLY B  40      62.950  64.329  72.093  1.00 24.67           O  
ANISOU 3938  O   GLY B  40     1514   2924   4933   -404    418   -191       O  
ATOM   3939  N   TYR B  41      64.370  65.383  70.698  1.00 23.79           N  
ANISOU 3939  N   TYR B  41     1694   2507   4837   -435    249   -323       N  
ATOM   3940  CA  TYR B  41      65.334  65.773  71.727  1.00 23.82           C  
ANISOU 3940  CA  TYR B  41     1823   2509   4716   -366    193   -387       C  
ATOM   3941  C   TYR B  41      65.293  67.302  71.840  1.00 23.58           C  
ANISOU 3941  C   TYR B  41     1807   2474   4678   -381    290   -389       C  
ATOM   3942  O   TYR B  41      65.375  67.998  70.822  1.00 24.35           O  
ANISOU 3942  O   TYR B  41     2126   2350   4774   -305    267   -343       O  
ATOM   3943  CB  TYR B  41      66.741  65.318  71.310  1.00 23.90           C  
ANISOU 3943  CB  TYR B  41     1837   2503   4740   -352    113   -446       C  
ATOM   3944  CG  TYR B  41      67.860  65.796  72.220  1.00 25.23           C  
ANISOU 3944  CG  TYR B  41     2040   2722   4823   -310    -15   -412       C  
ATOM   3945  CD1 TYR B  41      68.086  65.182  73.453  1.00 26.53           C  
ANISOU 3945  CD1 TYR B  41     2294   2824   4959   -166   -197   -445       C  
ATOM   3946  CD2 TYR B  41      68.673  66.875  71.859  1.00 24.35           C  
ANISOU 3946  CD2 TYR B  41     1920   2624   4707   -289   -212   -524       C  
ATOM   3947  CE1 TYR B  41      69.093  65.632  74.306  1.00 27.69           C  
ANISOU 3947  CE1 TYR B  41     2446   2973   5101   -456   -190   -284       C  
ATOM   3948  CE2 TYR B  41      69.690  67.333  72.704  1.00 25.97           C  
ANISOU 3948  CE2 TYR B  41     2203   2692   4970   -566   -196   -459       C  
ATOM   3949  CZ  TYR B  41      69.889  66.697  73.920  1.00 26.66           C  
ANISOU 3949  CZ  TYR B  41     2363   2790   4974   -502   -289   -500       C  
ATOM   3950  OH  TYR B  41      70.871  67.122  74.773  1.00 29.04           O  
ANISOU 3950  OH  TYR B  41     2774   3151   5107   -758   -340   -240       O  
ATOM   3951  N   THR B  42      65.172  67.830  73.055  1.00 23.05           N  
ANISOU 3951  N   THR B  42     1820   2379   4558   -425    365   -411       N  
ATOM   3952  CA  THR B  42      65.047  69.277  73.249  1.00 22.95           C  
ANISOU 3952  CA  THR B  42     1871   2344   4502   -441    567   -393       C  
ATOM   3953  C   THR B  42      66.403  69.988  73.346  1.00 22.70           C  
ANISOU 3953  C   THR B  42     1955   2288   4380   -408    481   -449       C  
ATOM   3954  O   THR B  42      67.284  69.587  74.127  1.00 22.63           O  
ANISOU 3954  O   THR B  42     2034   2296   4266   -479    470   -439       O  
ATOM   3955  CB  THR B  42      64.161  69.599  74.474  1.00 23.68           C  
ANISOU 3955  CB  THR B  42     2029   2406   4560   -486    555   -453       C  
ATOM   3956  OG1 THR B  42      62.867  69.012  74.275  1.00 24.98           O  
ANISOU 3956  OG1 THR B  42     1981   2779   4729   -438    916   -340       O  
ATOM   3957  CG2 THR B  42      63.985  71.107  74.660  1.00 24.26           C  
ANISOU 3957  CG2 THR B  42     2233   2481   4503   -351    623   -283       C  
ATOM   3958  N   ARG B  43      66.592  71.006  72.507  1.00 21.33           N  
ANISOU 3958  N   ARG B  43     1768   2073   4261   -386    578   -408       N  
ATOM   3959  CA  ARG B  43      67.773  71.868  72.621  1.00 21.29           C  
ANISOU 3959  CA  ARG B  43     1766   2164   4157   -277    474   -420       C  
ATOM   3960  C   ARG B  43      67.453  73.304  72.221  1.00 21.67           C  
ANISOU 3960  C   ARG B  43     1829   2195   4208   -262    389   -403       C  
ATOM   3961  O   ARG B  43      66.460  73.583  71.536  1.00 22.07           O  
ANISOU 3961  O   ARG B  43     1831   2211   4342   -178    287   -312       O  
ATOM   3962  CB  ARG B  43      68.971  71.355  71.789  1.00 20.56           C  
ANISOU 3962  CB  ARG B  43     1707   2063   4041   -231    581   -425       C  
ATOM   3963  CG  ARG B  43      68.671  71.240  70.281  1.00 19.23           C  
ANISOU 3963  CG  ARG B  43     1558   2113   3634   -191    782   -428       C  
ATOM   3964  CD  ARG B  43      69.921  71.391  69.377  1.00 17.02           C  
ANISOU 3964  CD  ARG B  43     1259   1743   3465   -549    634   -314       C  
ATOM   3965  NE  ARG B  43      70.434  72.759  69.304  1.00 16.03           N  
ANISOU 3965  NE  ARG B  43     1190   1751   3150   -397    286   -431       N  
ATOM   3966  CZ  ARG B  43      71.431  73.181  68.525  1.00 17.10           C  
ANISOU 3966  CZ  ARG B  43     1580   1709   3206   -311    358   -497       C  
ATOM   3967  NH1 ARG B  43      72.101  72.346  67.723  1.00 15.75           N  
ANISOU 3967  NH1 ARG B  43     1610   1610   2763   -129    125   -389       N  
ATOM   3968  NH2 ARG B  43      71.785  74.465  68.575  1.00 15.79           N  
ANISOU 3968  NH2 ARG B  43     1286   1472   3238    -43     23   -337       N  
ATOM   3969  N   ASP B  44      68.307  74.216  72.663  1.00 21.95           N  
ANISOU 3969  N   ASP B  44     1842   2261   4234   -286    264   -368       N  
ATOM   3970  CA  ASP B  44      68.166  75.637  72.353  1.00 22.80           C  
ANISOU 3970  CA  ASP B  44     2046   2406   4208   -256    200   -363       C  
ATOM   3971  C   ASP B  44      68.626  75.869  70.925  1.00 22.16           C  
ANISOU 3971  C   ASP B  44     1949   2287   4181   -287    133   -320       C  
ATOM   3972  O   ASP B  44      69.618  75.280  70.497  1.00 22.06           O  
ANISOU 3972  O   ASP B  44     1940   2365   4076   -271    181   -317       O  
ATOM   3973  CB  ASP B  44      69.035  76.427  73.330  1.00 23.01           C  
ANISOU 3973  CB  ASP B  44     2143   2510   4089   -189    220   -412       C  
ATOM   3974  CG  ASP B  44      68.542  76.275  74.747  1.00 26.11           C  
ANISOU 3974  CG  ASP B  44     2632   3173   4114     28    136   -323       C  
ATOM   3975  OD1 ASP B  44      67.331  76.507  74.974  1.00 26.24           O  
ANISOU 3975  OD1 ASP B  44     2933   3557   3480    294    472   -487       O  
ATOM   3976  OD2 ASP B  44      69.347  75.868  75.610  1.00 30.78           O  
ANISOU 3976  OD2 ASP B  44     3316   4137   4240     94   -153   -516       O  
ATOM   3977  N   ALA B  45      67.892  76.692  70.186  1.00 22.03           N  
ANISOU 3977  N   ALA B  45     1831   2187   4350   -306     43   -317       N  
ATOM   3978  CA  ALA B  45      68.220  76.941  68.785  1.00 21.63           C  
ANISOU 3978  CA  ALA B  45     1713   2110   4393   -250     42   -300       C  
ATOM   3979  C   ALA B  45      68.017  78.413  68.417  1.00 22.17           C  
ANISOU 3979  C   ALA B  45     1713   2156   4556   -229     16   -291       C  
ATOM   3980  O   ALA B  45      67.599  79.231  69.244  1.00 21.96           O  
ANISOU 3980  O   ALA B  45     1691   2048   4603   -357    -45   -411       O  
ATOM   3981  CB  ALA B  45      67.374  76.047  67.881  1.00 21.75           C  
ANISOU 3981  CB  ALA B  45     1814   2018   4430   -227    104   -312       C  
ATOM   3982  N   VAL B  46      68.334  78.739  67.167  1.00 22.02           N  
ANISOU 3982  N   VAL B  46     1614   2112   4638   -160   -101   -182       N  
ATOM   3983  CA  VAL B  46      67.977  80.024  66.580  1.00 21.69           C  
ANISOU 3983  CA  VAL B  46     1404   2125   4712    -11   -133   -134       C  
ATOM   3984  C   VAL B  46      66.756  79.757  65.697  1.00 21.75           C  
ANISOU 3984  C   VAL B  46     1377   2185   4702     33   -175   -129       C  
ATOM   3985  O   VAL B  46      66.798  78.874  64.835  1.00 21.80           O  
ANISOU 3985  O   VAL B  46     1260   2365   4657    146   -214   -184       O  
ATOM   3986  CB  VAL B  46      69.141  80.593  65.753  1.00 22.31           C  
ANISOU 3986  CB  VAL B  46     1614   2152   4710     31   -162    -18       C  
ATOM   3987  CG1 VAL B  46      68.726  81.928  65.098  1.00 22.83           C  
ANISOU 3987  CG1 VAL B  46     1922   1830   4921    282     38      7       C  
ATOM   3988  CG2 VAL B  46      70.373  80.770  66.627  1.00 20.57           C  
ANISOU 3988  CG2 VAL B  46     1114   2009   4690    134    -94   -347       C  
ATOM   3989  N   VAL B  47      65.660  80.467  65.958  1.00 21.28           N  
ANISOU 3989  N   VAL B  47     1212   2115   4758     18   -134    -99       N  
ATOM   3990  CA  VAL B  47      64.412  80.250  65.228  1.00 21.83           C  
ANISOU 3990  CA  VAL B  47     1203   2168   4923     -1    -67    -89       C  
ATOM   3991  C   VAL B  47      63.948  81.516  64.504  1.00 22.08           C  
ANISOU 3991  C   VAL B  47     1182   2236   4971    -28    -51    -68       C  
ATOM   3992  O   VAL B  47      64.369  82.627  64.844  1.00 22.32           O  
ANISOU 3992  O   VAL B  47     1252   2241   4985    -56    -19    -17       O  
ATOM   3993  CB  VAL B  47      63.286  79.738  66.177  1.00 22.40           C  
ANISOU 3993  CB  VAL B  47     1336   2200   4972     41    -95    -91       C  
ATOM   3994  CG1 VAL B  47      63.629  78.347  66.763  1.00 23.04           C  
ANISOU 3994  CG1 VAL B  47     1714   1940   5097    -79     78   -172       C  
ATOM   3995  CG2 VAL B  47      62.997  80.755  67.290  1.00 22.81           C  
ANISOU 3995  CG2 VAL B  47     1280   2307   5077     33    -10   -209       C  
ATOM   3996  N   VAL B  48      63.074  81.330  63.515  1.00 21.73           N  
ANISOU 3996  N   VAL B  48     1000   2217   5038     36    -65    -45       N  
ATOM   3997  CA  VAL B  48      62.514  82.394  62.683  1.00 22.09           C  
ANISOU 3997  CA  VAL B  48      971   2269   5152     90    -64    -98       C  
ATOM   3998  C   VAL B  48      60.988  82.366  62.874  1.00 22.69           C  
ANISOU 3998  C   VAL B  48      984   2265   5368    102   -151    -75       C  
ATOM   3999  O   VAL B  48      60.333  81.336  62.631  1.00 21.83           O  
ANISOU 3999  O   VAL B  48      855   2193   5245    135   -311    -81       O  
ATOM   4000  CB  VAL B  48      62.912  82.184  61.195  1.00 21.81           C  
ANISOU 4000  CB  VAL B  48      839   2332   5114    121   -106    -53       C  
ATOM   4001  CG1 VAL B  48      62.385  83.325  60.326  1.00 21.37           C  
ANISOU 4001  CG1 VAL B  48      929   2033   5155    -38   -136   -143       C  
ATOM   4002  CG2 VAL B  48      64.440  82.086  61.049  1.00 20.58           C  
ANISOU 4002  CG2 VAL B  48      809   2187   4822     83    -62   -309       C  
ATOM   4003  N   ASN B  49      60.426  83.482  63.340  1.00 23.55           N  
ANISOU 4003  N   ASN B  49     1067   2371   5510     39     -4   -134       N  
ATOM   4004  CA  ASN B  49      59.005  83.552  63.696  1.00 25.10           C  
ANISOU 4004  CA  ASN B  49     1228   2444   5862     25     14   -140       C  
ATOM   4005  C   ASN B  49      58.614  82.327  64.529  1.00 26.12           C  
ANISOU 4005  C   ASN B  49     1402   2594   5928    -23    122   -158       C  
ATOM   4006  O   ASN B  49      57.575  81.690  64.297  1.00 26.68           O  
ANISOU 4006  O   ASN B  49     1257   2774   6104    -62    171    -71       O  
ATOM   4007  CB  ASN B  49      58.121  83.675  62.447  1.00 25.10           C  
ANISOU 4007  CB  ASN B  49     1231   2392   5912    100    -50    -92       C  
ATOM   4008  CG  ASN B  49      58.266  85.023  61.755  1.00 26.24           C  
ANISOU 4008  CG  ASN B  49     1354   2365   6250    123   -124   -193       C  
ATOM   4009  OD1 ASN B  49      58.896  85.921  62.290  1.00 27.51           O  
ANISOU 4009  OD1 ASN B  49     1288   2329   6833    187   -224   -201       O  
ATOM   4010  ND2 ASN B  49      57.664  85.179  60.580  1.00 27.64           N  
ANISOU 4010  ND2 ASN B  49     1757   2430   6311    336   -259   -159       N  
ATOM   4011  N   GLY B  50      59.489  81.984  65.469  1.00 26.18           N  
ANISOU 4011  N   GLY B  50     1478   2497   5969     53    154   -158       N  
ATOM   4012  CA  GLY B  50      59.224  80.937  66.446  1.00 26.94           C  
ANISOU 4012  CA  GLY B  50     1720   2487   6028    -77    269   -212       C  
ATOM   4013  C   GLY B  50      59.600  79.520  66.044  1.00 26.73           C  
ANISOU 4013  C   GLY B  50     1696   2509   5950    -11    309   -266       C  
ATOM   4014  O   GLY B  50      59.487  78.602  66.865  1.00 27.18           O  
ANISOU 4014  O   GLY B  50     1884   2502   5940   -128    427   -241       O  
ATOM   4015  N   ALA B  51      60.023  79.316  64.797  1.00 26.06           N  
ANISOU 4015  N   ALA B  51     1477   2526   5898    -90    336   -261       N  
ATOM   4016  CA  ALA B  51      60.227  77.951  64.298  1.00 25.16           C  
ANISOU 4016  CA  ALA B  51     1298   2448   5812    -36    238   -258       C  
ATOM   4017  C   ALA B  51      61.567  77.732  63.614  1.00 24.98           C  
ANISOU 4017  C   ALA B  51     1301   2446   5741    -90    140   -270       C  
ATOM   4018  O   ALA B  51      62.119  78.654  63.016  1.00 24.69           O  
ANISOU 4018  O   ALA B  51     1234   2431   5714   -152    245   -189       O  
ATOM   4019  CB  ALA B  51      59.138  77.567  63.335  1.00 26.08           C  
ANISOU 4019  CB  ALA B  51     1370   2621   5916    -23    190   -330       C  
ATOM   4020  N   THR B  52      62.056  76.499  63.695  1.00 23.70           N  
ANISOU 4020  N   THR B  52     1067   2329   5608    -45    -41   -271       N  
ATOM   4021  CA  THR B  52      63.142  76.051  62.833  1.00 23.70           C  
ANISOU 4021  CA  THR B  52     1254   2283   5468   -119    -79   -280       C  
ATOM   4022  C   THR B  52      62.763  74.689  62.261  1.00 23.36           C  
ANISOU 4022  C   THR B  52     1221   2206   5445   -151   -169   -312       C  
ATOM   4023  O   THR B  52      62.248  73.846  62.985  1.00 23.52           O  
ANISOU 4023  O   THR B  52     1501   2077   5357   -166   -190   -406       O  
ATOM   4024  CB  THR B  52      64.539  76.035  63.541  1.00 23.63           C  
ANISOU 4024  CB  THR B  52     1166   2362   5449    -61   -114   -232       C  
ATOM   4025  OG1 THR B  52      65.554  75.650  62.607  1.00 22.85           O  
ANISOU 4025  OG1 THR B  52      915   2408   5357    -53   -184    -23       O  
ATOM   4026  CG2 THR B  52      64.584  75.058  64.710  1.00 24.82           C  
ANISOU 4026  CG2 THR B  52     1691   2261   5476    -39    -96   -147       C  
ATOM   4027  N   PRO B  53      62.932  74.496  60.945  1.00 23.43           N  
ANISOU 4027  N   PRO B  53     1338   2119   5443   -160   -194   -353       N  
ATOM   4028  CA  PRO B  53      63.324  75.507  59.965  1.00 23.94           C  
ANISOU 4028  CA  PRO B  53     1417   2159   5519   -128   -212   -366       C  
ATOM   4029  C   PRO B  53      62.316  76.663  59.911  1.00 23.84           C  
ANISOU 4029  C   PRO B  53     1359   2141   5558    -92   -309   -328       C  
ATOM   4030  O   PRO B  53      61.175  76.526  60.354  1.00 23.29           O  
ANISOU 4030  O   PRO B  53     1303   2004   5540    -88   -293   -404       O  
ATOM   4031  CB  PRO B  53      63.324  74.724  58.648  1.00 24.26           C  
ANISOU 4031  CB  PRO B  53     1401   2331   5484   -286   -126   -408       C  
ATOM   4032  CG  PRO B  53      62.365  73.571  58.890  1.00 24.94           C  
ANISOU 4032  CG  PRO B  53     1782   2135   5559   -182   -227   -377       C  
ATOM   4033  CD  PRO B  53      62.600  73.204  60.317  1.00 23.80           C  
ANISOU 4033  CD  PRO B  53     1451   2173   5419   -206   -190   -345       C  
ATOM   4034  N   GLY B  54      62.745  77.799  59.375  1.00 23.80           N  
ANISOU 4034  N   GLY B  54     1385   2072   5584     27   -393   -285       N  
ATOM   4035  CA  GLY B  54      61.922  78.999  59.325  1.00 24.03           C  
ANISOU 4035  CA  GLY B  54     1289   2126   5715    163   -591   -170       C  
ATOM   4036  C   GLY B  54      60.784  78.847  58.324  1.00 24.35           C  
ANISOU 4036  C   GLY B  54     1395   2039   5816     51   -666   -158       C  
ATOM   4037  O   GLY B  54      60.778  77.909  57.517  1.00 24.70           O  
ANISOU 4037  O   GLY B  54     1420   2173   5792     94   -654    -83       O  
ATOM   4038  N   PRO B  55      59.835  79.795  58.342  1.00 24.08           N  
ANISOU 4038  N   PRO B  55     1305   1996   5848    118   -800   -152       N  
ATOM   4039  CA  PRO B  55      58.672  79.766  57.458  1.00 25.18           C  
ANISOU 4039  CA  PRO B  55     1530   2074   5961    199   -829   -112       C  
ATOM   4040  C   PRO B  55      59.079  79.882  55.992  1.00 25.41           C  
ANISOU 4040  C   PRO B  55     1564   2122   5968    207   -898   -109       C  
ATOM   4041  O   PRO B  55      60.125  80.464  55.675  1.00 25.63           O  
ANISOU 4041  O   PRO B  55     1713   2106   5917    180   -809    -51       O  
ATOM   4042  CB  PRO B  55      57.873  81.003  57.885  1.00 25.28           C  
ANISOU 4042  CB  PRO B  55     1577   2044   5984    152   -869   -217       C  
ATOM   4043  CG  PRO B  55      58.929  81.947  58.434  1.00 24.99           C  
ANISOU 4043  CG  PRO B  55     1286   2148   6060    229   -926   -133       C  
ATOM   4044  CD  PRO B  55      59.874  81.021  59.158  1.00 24.99           C  
ANISOU 4044  CD  PRO B  55     1543   2021   5928    239   -797   -116       C  
ATOM   4045  N   LEU B  56      58.250  79.311  55.126  1.00 25.69           N  
ANISOU 4045  N   LEU B  56     1615   2116   6030    152   -982   -120       N  
ATOM   4046  CA  LEU B  56      58.360  79.511  53.683  1.00 25.78           C  
ANISOU 4046  CA  LEU B  56     1499   2183   6110    162  -1084   -133       C  
ATOM   4047  C   LEU B  56      58.189  81.002  53.368  1.00 26.25           C  
ANISOU 4047  C   LEU B  56     1607   2199   6165    195  -1147   -144       C  
ATOM   4048  O   LEU B  56      57.181  81.607  53.735  1.00 26.47           O  
ANISOU 4048  O   LEU B  56     1604   2288   6165    181  -1165   -249       O  
ATOM   4049  CB  LEU B  56      57.304  78.675  52.942  1.00 24.97           C  
ANISOU 4049  CB  LEU B  56     1379   2053   6053    233  -1078   -150       C  
ATOM   4050  CG  LEU B  56      57.295  78.846  51.416  1.00 23.92           C  
ANISOU 4050  CG  LEU B  56      969   2091   6028    138  -1243   -177       C  
ATOM   4051  CD1 LEU B  56      58.633  78.424  50.796  1.00 22.84           C  
ANISOU 4051  CD1 LEU B  56      879   1863   5934    131  -1043    103       C  
ATOM   4052  CD2 LEU B  56      56.135  78.130  50.734  1.00 24.45           C  
ANISOU 4052  CD2 LEU B  56      818   2305   6165    -85  -1366     17       C  
ATOM   4053  N   ILE B  57      59.171  81.610  52.707  1.00 26.55           N  
ANISOU 4053  N   ILE B  57     1684   2127   6274    131  -1222   -123       N  
ATOM   4054  CA  ILE B  57      58.964  82.965  52.175  1.00 27.09           C  
ANISOU 4054  CA  ILE B  57     1634   2231   6427    285  -1295     12       C  
ATOM   4055  C   ILE B  57      58.500  82.823  50.731  1.00 27.83           C  
ANISOU 4055  C   ILE B  57     1652   2290   6631    316  -1373    107       C  
ATOM   4056  O   ILE B  57      59.045  81.994  50.000  1.00 28.16           O  
ANISOU 4056  O   ILE B  57     1479   2494   6725    272  -1305    212       O  
ATOM   4057  CB  ILE B  57      60.251  83.827  52.269  1.00 26.67           C  
ANISOU 4057  CB  ILE B  57     1706   2127   6298    220  -1278    -16       C  
ATOM   4058  CG1 ILE B  57      60.712  83.933  53.728  1.00 25.84           C  
ANISOU 4058  CG1 ILE B  57     1266   2270   6281    286  -1363      0       C  
ATOM   4059  CG2 ILE B  57      59.998  85.218  51.667  1.00 27.70           C  
ANISOU 4059  CG2 ILE B  57     1948   2247   6328    241  -1238    -22       C  
ATOM   4060  CD1 ILE B  57      62.053  84.645  53.955  1.00 25.11           C  
ANISOU 4060  CD1 ILE B  57     1277   2371   5892    409  -1453   -123       C  
ATOM   4061  N   VAL B  58      57.458  83.559  50.335  1.00 29.23           N  
ANISOU 4061  N   VAL B  58     1890   2361   6855    381  -1479    218       N  
ATOM   4062  CA  VAL B  58      56.961  83.500  48.962  1.00 30.48           C  
ANISOU 4062  CA  VAL B  58     2086   2446   7046    386  -1623    236       C  
ATOM   4063  C   VAL B  58      56.899  84.840  48.224  1.00 31.44           C  
ANISOU 4063  C   VAL B  58     2318   2478   7148    389  -1712    287       C  
ATOM   4064  O   VAL B  58      56.788  85.910  48.836  1.00 31.42           O  
ANISOU 4064  O   VAL B  58     2264   2478   7196    346  -1688    267       O  
ATOM   4065  CB  VAL B  58      55.564  82.817  48.863  1.00 30.64           C  
ANISOU 4065  CB  VAL B  58     2172   2378   7089    342  -1540    227       C  
ATOM   4066  CG1 VAL B  58      55.663  81.366  49.323  1.00 31.68           C  
ANISOU 4066  CG1 VAL B  58     2446   2448   7140    447  -1662    349       C  
ATOM   4067  CG2 VAL B  58      54.518  83.586  49.663  1.00 30.58           C  
ANISOU 4067  CG2 VAL B  58     1874   2559   7185    434  -1680    316       C  
ATOM   4068  N   GLY B  59      56.949  84.765  46.897  1.00 32.27           N  
ANISOU 4068  N   GLY B  59     2578   2516   7167    449  -1835    357       N  
ATOM   4069  CA  GLY B  59      56.624  85.905  46.035  1.00 34.11           C  
ANISOU 4069  CA  GLY B  59     2921   2725   7312    587  -2025    430       C  
ATOM   4070  C   GLY B  59      56.416  85.447  44.604  1.00 34.91           C  
ANISOU 4070  C   GLY B  59     3098   2819   7347    608  -2143    486       C  
ATOM   4071  O   GLY B  59      56.525  84.252  44.328  1.00 34.24           O  
ANISOU 4071  O   GLY B  59     2959   2772   7278    550  -2166    489       O  
ATOM   4072  N   ASN B  60      56.119  86.384  43.703  1.00 36.01           N  
ANISOU 4072  N   ASN B  60     3259   2932   7490    710  -2257    538       N  
ATOM   4073  CA  ASN B  60      56.080  86.095  42.269  1.00 37.11           C  
ANISOU 4073  CA  ASN B  60     3498   3046   7554    762  -2299    579       C  
ATOM   4074  C   ASN B  60      57.251  86.706  41.518  1.00 37.87           C  
ANISOU 4074  C   ASN B  60     3720   3083   7584    764  -2329    612       C  
ATOM   4075  O   ASN B  60      57.857  87.664  41.993  1.00 38.41           O  
ANISOU 4075  O   ASN B  60     3841   3138   7614    729  -2239    615       O  
ATOM   4076  CB  ASN B  60      54.790  86.622  41.640  1.00 37.19           C  
ANISOU 4076  CB  ASN B  60     3442   3108   7578    781  -2327    579       C  
ATOM   4077  CG  ASN B  60      53.551  86.009  42.246  1.00 38.22           C  
ANISOU 4077  CG  ASN B  60     3413   3323   7782    835  -2245    584       C  
ATOM   4078  OD1 ASN B  60      52.574  86.711  42.505  1.00 41.50           O  
ANISOU 4078  OD1 ASN B  60     3797   3876   8094    825  -1841    282       O  
ATOM   4079  ND2 ASN B  60      53.573  84.703  42.469  1.00 37.71           N  
ANISOU 4079  ND2 ASN B  60     3025   3319   7985    794  -2152    458       N  
ATOM   4080  N   LYS B  61      57.542  86.162  40.339  1.00 38.92           N  
ANISOU 4080  N   LYS B  61     4027   3080   7679    792  -2319    623       N  
ATOM   4081  CA  LYS B  61      58.590  86.674  39.462  1.00 39.56           C  
ANISOU 4081  CA  LYS B  61     4239   3131   7660    835  -2351    671       C  
ATOM   4082  C   LYS B  61      58.451  88.189  39.338  1.00 39.71           C  
ANISOU 4082  C   LYS B  61     4311   3137   7637    814  -2369    683       C  
ATOM   4083  O   LYS B  61      57.366  88.699  39.062  1.00 39.46           O  
ANISOU 4083  O   LYS B  61     4321   3020   7650    857  -2361    711       O  
ATOM   4084  CB  LYS B  61      58.534  85.995  38.088  1.00 39.72           C  
ANISOU 4084  CB  LYS B  61     4299   3128   7664    861  -2355    674       C  
ATOM   4085  CG  LYS B  61      59.635  86.438  37.132  1.00 41.73           C  
ANISOU 4085  CG  LYS B  61     4682   3455   7717    784  -2248    633       C  
ATOM   4086  CD  LYS B  61      59.768  85.510  35.928  1.00 44.32           C  
ANISOU 4086  CD  LYS B  61     5404   3552   7884    638  -2119    482       C  
ATOM   4087  CE  LYS B  61      60.225  86.302  34.709  1.00 46.29           C  
ANISOU 4087  CE  LYS B  61     5697   3919   7971    632  -1982    463       C  
ATOM   4088  NZ  LYS B  61      60.878  85.459  33.669  1.00 47.66           N  
ANISOU 4088  NZ  LYS B  61     5914   3937   8258    640  -1863    373       N  
ATOM   4089  N   GLY B  62      59.543  88.901  39.588  1.00 39.88           N  
ANISOU 4089  N   GLY B  62     4346   3174   7629    807  -2357    697       N  
ATOM   4090  CA  GLY B  62      59.529  90.350  39.469  1.00 40.30           C  
ANISOU 4090  CA  GLY B  62     4419   3237   7655    784  -2282    625       C  
ATOM   4091  C   GLY B  62      59.137  91.108  40.724  1.00 40.29           C  
ANISOU 4091  C   GLY B  62     4396   3278   7632    780  -2275    627       C  
ATOM   4092  O   GLY B  62      59.276  92.330  40.762  1.00 40.05           O  
ANISOU 4092  O   GLY B  62     4502   3147   7567    899  -2314    678       O  
ATOM   4093  N   ASP B  63      58.662  90.408  41.754  1.00 39.69           N  
ANISOU 4093  N   ASP B  63     4216   3290   7574    767  -2257    619       N  
ATOM   4094  CA  ASP B  63      58.230  91.095  42.972  1.00 38.90           C  
ANISOU 4094  CA  ASP B  63     4012   3205   7561    776  -2204    554       C  
ATOM   4095  C   ASP B  63      59.393  91.807  43.658  1.00 38.24           C  
ANISOU 4095  C   ASP B  63     3908   3127   7493    774  -2128    548       C  
ATOM   4096  O   ASP B  63      60.536  91.336  43.667  1.00 38.05           O  
ANISOU 4096  O   ASP B  63     3935   3072   7449    671  -2069    497       O  
ATOM   4097  CB  ASP B  63      57.579  90.137  43.975  1.00 39.05           C  
ANISOU 4097  CB  ASP B  63     3950   3293   7593    777  -2207    549       C  
ATOM   4098  CG  ASP B  63      56.110  89.856  43.684  1.00 40.48           C  
ANISOU 4098  CG  ASP B  63     4127   3445   7808    787  -2156    501       C  
ATOM   4099  OD1 ASP B  63      55.545  90.398  42.708  1.00 40.22           O  
ANISOU 4099  OD1 ASP B  63     3753   3617   7911    826  -2279    444       O  
ATOM   4100  OD2 ASP B  63      55.511  89.074  44.456  1.00 42.02           O  
ANISOU 4100  OD2 ASP B  63     4364   3541   8061    565  -1936    232       O  
ATOM   4101  N   ASN B  64      59.068  92.953  44.239  1.00 37.60           N  
ANISOU 4101  N   ASN B  64     3727   3094   7465    776  -2076    546       N  
ATOM   4102  CA  ASN B  64      59.926  93.614  45.207  1.00 37.42           C  
ANISOU 4102  CA  ASN B  64     3651   3156   7410    778  -1966    516       C  
ATOM   4103  C   ASN B  64      59.672  93.011  46.579  1.00 36.72           C  
ANISOU 4103  C   ASN B  64     3474   3108   7368    792  -1849    446       C  
ATOM   4104  O   ASN B  64      58.534  92.998  47.058  1.00 36.92           O  
ANISOU 4104  O   ASN B  64     3347   3280   7401    875  -1826    467       O  
ATOM   4105  CB  ASN B  64      59.643  95.115  45.224  1.00 37.87           C  
ANISOU 4105  CB  ASN B  64     3678   3225   7483    733  -1981    472       C  
ATOM   4106  CG  ASN B  64      59.922  95.753  43.887  1.00 39.45           C  
ANISOU 4106  CG  ASN B  64     3967   3410   7608    682  -2023    565       C  
ATOM   4107  OD1 ASN B  64      61.053  95.718  43.403  1.00 42.23           O  
ANISOU 4107  OD1 ASN B  64     4407   3957   7680    384  -1798    476       O  
ATOM   4108  ND2 ASN B  64      58.886  96.298  43.261  1.00 41.96           N  
ANISOU 4108  ND2 ASN B  64     4331   3761   7849    849  -2011    633       N  
ATOM   4109  N   PHE B  65      60.745  92.515  47.186  1.00 34.53           N  
ANISOU 4109  N   PHE B  65     3156   2777   7184    905  -1722    391       N  
ATOM   4110  CA  PHE B  65      60.715  91.984  48.543  1.00 33.58           C  
ANISOU 4110  CA  PHE B  65     3024   2618   7117    831  -1602    337       C  
ATOM   4111  C   PHE B  65      61.162  93.045  49.534  1.00 32.95           C  
ANISOU 4111  C   PHE B  65     2963   2514   7041    858  -1477    319       C  
ATOM   4112  O   PHE B  65      62.120  93.784  49.287  1.00 33.15           O  
ANISOU 4112  O   PHE B  65     3046   2467   7082    770  -1519    299       O  
ATOM   4113  CB  PHE B  65      61.606  90.740  48.648  1.00 33.36           C  
ANISOU 4113  CB  PHE B  65     3105   2516   7053    804  -1541    325       C  
ATOM   4114  CG  PHE B  65      61.046  89.574  47.899  1.00 33.63           C  
ANISOU 4114  CG  PHE B  65     3170   2504   7104    763  -1555    292       C  
ATOM   4115  CD1 PHE B  65      61.218  89.474  46.525  1.00 34.70           C  
ANISOU 4115  CD1 PHE B  65     3462   2584   7136    587  -1554    237       C  
ATOM   4116  CD2 PHE B  65      60.268  88.629  48.548  1.00 32.17           C  
ANISOU 4116  CD2 PHE B  65     3001   2206   7016    948  -1514    294       C  
ATOM   4117  CE1 PHE B  65      60.658  88.422  45.813  1.00 33.44           C  
ANISOU 4117  CE1 PHE B  65     3375   2186   7141    858  -1720    366       C  
ATOM   4118  CE2 PHE B  65      59.694  87.583  47.843  1.00 32.48           C  
ANISOU 4118  CE2 PHE B  65     2890   2328   7120    868  -1651    267       C  
ATOM   4119  CZ  PHE B  65      59.891  87.481  46.473  1.00 32.58           C  
ANISOU 4119  CZ  PHE B  65     2884   2325   7170    810  -1645    321       C  
ATOM   4120  N   ARG B  66      60.468  93.086  50.663  1.00 31.91           N  
ANISOU 4120  N   ARG B  66     2711   2439   6972    877  -1372    287       N  
ATOM   4121  CA  ARG B  66      60.858  93.928  51.791  1.00 31.55           C  
ANISOU 4121  CA  ARG B  66     2633   2451   6903    765  -1252    318       C  
ATOM   4122  C   ARG B  66      60.794  93.034  53.024  1.00 30.31           C  
ANISOU 4122  C   ARG B  66     2368   2412   6735    756  -1192    265       C  
ATOM   4123  O   ARG B  66      59.734  92.828  53.625  1.00 30.27           O  
ANISOU 4123  O   ARG B  66     2292   2548   6661    740  -1191    329       O  
ATOM   4124  CB  ARG B  66      59.942  95.149  51.922  1.00 31.61           C  
ANISOU 4124  CB  ARG B  66     2639   2388   6982    821  -1250    292       C  
ATOM   4125  CG  ARG B  66      59.918  96.015  50.663  1.00 34.96           C  
ANISOU 4125  CG  ARG B  66     3284   2723   7276    818  -1128    340       C  
ATOM   4126  CD  ARG B  66      58.989  97.213  50.807  1.00 39.62           C  
ANISOU 4126  CD  ARG B  66     4211   2871   7970    923   -997    216       C  
ATOM   4127  NE  ARG B  66      59.420  98.092  51.890  1.00 44.85           N  
ANISOU 4127  NE  ARG B  66     4968   3560   8512    726   -862   -119       N  
ATOM   4128  CZ  ARG B  66      60.335  99.052  51.770  1.00 47.94           C  
ANISOU 4128  CZ  ARG B  66     5291   4118   8804    481   -722   -274       C  
ATOM   4129  NH1 ARG B  66      60.932  99.294  50.606  1.00 50.06           N  
ANISOU 4129  NH1 ARG B  66     5581   4542   8896    522   -543   -344       N  
ATOM   4130  NH2 ARG B  66      60.647  99.788  52.827  1.00 49.94           N  
ANISOU 4130  NH2 ARG B  66     5467   4634   8871    515   -802   -503       N  
ATOM   4131  N   LEU B  67      61.945  92.474  53.369  1.00 28.55           N  
ANISOU 4131  N   LEU B  67     2129   2208   6510    695  -1077    195       N  
ATOM   4132  CA  LEU B  67      61.999  91.461  54.411  1.00 27.34           C  
ANISOU 4132  CA  LEU B  67     1863   2199   6325    553   -935     98       C  
ATOM   4133  C   LEU B  67      62.689  92.107  55.595  1.00 26.82           C  
ANISOU 4133  C   LEU B  67     1845   2142   6202    583   -839      9       C  
ATOM   4134  O   LEU B  67      63.905  92.334  55.596  1.00 26.02           O  
ANISOU 4134  O   LEU B  67     1745   2086   6054    488   -846      0       O  
ATOM   4135  CB  LEU B  67      62.729  90.210  53.918  1.00 26.14           C  
ANISOU 4135  CB  LEU B  67     1662   2004   6265    546   -926    167       C  
ATOM   4136  CG  LEU B  67      62.027  89.608  52.699  1.00 26.55           C  
ANISOU 4136  CG  LEU B  67     1524   2204   6360    367   -829    119       C  
ATOM   4137  CD1 LEU B  67      62.867  88.528  52.047  1.00 26.21           C  
ANISOU 4137  CD1 LEU B  67     1306   2246   6405    357   -780    207       C  
ATOM   4138  CD2 LEU B  67      60.641  89.066  53.079  1.00 26.32           C  
ANISOU 4138  CD2 LEU B  67     1456   2262   6280    140   -908    131       C  
ATOM   4139  N   ASN B  68      61.862  92.424  56.583  1.00 26.26           N  
ANISOU 4139  N   ASN B  68     1735   2084   6157    549   -718    -76       N  
ATOM   4140  CA  ASN B  68      62.318  93.155  57.750  1.00 26.41           C  
ANISOU 4140  CA  ASN B  68     1731   2154   6149    519   -558   -184       C  
ATOM   4141  C   ASN B  68      62.755  92.159  58.822  1.00 25.77           C  
ANISOU 4141  C   ASN B  68     1658   2064   6068    458   -463   -217       C  
ATOM   4142  O   ASN B  68      61.917  91.485  59.435  1.00 26.18           O  
ANISOU 4142  O   ASN B  68     1652   2266   6030    464   -447   -195       O  
ATOM   4143  CB  ASN B  68      61.193  94.055  58.268  1.00 26.27           C  
ANISOU 4143  CB  ASN B  68     1679   2096   6205    457   -550   -200       C  
ATOM   4144  CG  ASN B  68      61.617  94.843  59.481  1.00 27.92           C  
ANISOU 4144  CG  ASN B  68     1830   2368   6410    418   -396   -334       C  
ATOM   4145  OD1 ASN B  68      62.778  95.248  59.609  1.00 29.52           O  
ANISOU 4145  OD1 ASN B  68     1907   2399   6907    177   -730   -375       O  
ATOM   4146  ND2 ASN B  68      60.680  95.056  60.387  1.00 29.38           N  
ANISOU 4146  ND2 ASN B  68     1634   2710   6816    331   -144   -409       N  
ATOM   4147  N   VAL B  69      64.069  92.062  59.010  1.00 24.76           N  
ANISOU 4147  N   VAL B  69     1510   1972   5925    369   -419   -234       N  
ATOM   4148  CA  VAL B  69      64.679  91.086  59.911  1.00 24.52           C  
ANISOU 4148  CA  VAL B  69     1489   2037   5788    235   -255   -225       C  
ATOM   4149  C   VAL B  69      64.843  91.738  61.282  1.00 24.16           C  
ANISOU 4149  C   VAL B  69     1390   2070   5718    120   -187   -285       C  
ATOM   4150  O   VAL B  69      65.552  92.735  61.437  1.00 24.05           O  
ANISOU 4150  O   VAL B  69     1421   1959   5757    116   -100   -294       O  
ATOM   4151  CB  VAL B  69      66.006  90.523  59.332  1.00 23.74           C  
ANISOU 4151  CB  VAL B  69     1361   1922   5734    280   -301   -181       C  
ATOM   4152  CG1 VAL B  69      66.750  89.636  60.345  1.00 24.15           C  
ANISOU 4152  CG1 VAL B  69     1413   2078   5685    332   -230   -141       C  
ATOM   4153  CG2 VAL B  69      65.722  89.730  58.049  1.00 23.90           C  
ANISOU 4153  CG2 VAL B  69     1476   1994   5607    219   -420   -133       C  
ATOM   4154  N   ILE B  70      64.133  91.190  62.261  1.00 23.34           N  
ANISOU 4154  N   ILE B  70     1261   2048   5556     23    -42   -333       N  
ATOM   4155  CA  ILE B  70      64.080  91.747  63.604  1.00 23.67           C  
ANISOU 4155  CA  ILE B  70     1237   2187   5569     -4     45   -423       C  
ATOM   4156  C   ILE B  70      64.904  90.823  64.496  1.00 23.38           C  
ANISOU 4156  C   ILE B  70     1259   2150   5475    -16    143   -435       C  
ATOM   4157  O   ILE B  70      64.481  89.709  64.778  1.00 24.99           O  
ANISOU 4157  O   ILE B  70     1622   2331   5539    -52    110   -502       O  
ATOM   4158  CB  ILE B  70      62.621  91.810  64.119  1.00 23.32           C  
ANISOU 4158  CB  ILE B  70     1225   2126   5507    109     77   -401       C  
ATOM   4159  CG1 ILE B  70      61.743  92.599  63.138  1.00 24.77           C  
ANISOU 4159  CG1 ILE B  70     1341   2616   5453     87    -23   -496       C  
ATOM   4160  CG2 ILE B  70      62.578  92.418  65.522  1.00 23.49           C  
ANISOU 4160  CG2 ILE B  70     1215   2163   5543    -19    -13   -441       C  
ATOM   4161  CD1 ILE B  70      60.230  92.525  63.388  1.00 25.01           C  
ANISOU 4161  CD1 ILE B  70     1485   2811   5207    132    -52   -582       C  
ATOM   4162  N   ASP B  71      66.081  91.269  64.929  1.00 23.41           N  
ANISOU 4162  N   ASP B  71     1227   2223   5442     45    239   -507       N  
ATOM   4163  CA  ASP B  71      66.944  90.429  65.741  1.00 23.23           C  
ANISOU 4163  CA  ASP B  71     1188   2233   5404     56    356   -491       C  
ATOM   4164  C   ASP B  71      66.569  90.563  67.220  1.00 24.11           C  
ANISOU 4164  C   ASP B  71     1382   2323   5455     39    409   -501       C  
ATOM   4165  O   ASP B  71      66.724  91.639  67.795  1.00 24.60           O  
ANISOU 4165  O   ASP B  71     1625   2347   5375     48    455   -601       O  
ATOM   4166  CB  ASP B  71      68.400  90.832  65.477  1.00 22.32           C  
ANISOU 4166  CB  ASP B  71     1020   1977   5480    -27    295   -410       C  
ATOM   4167  CG  ASP B  71      69.410  89.998  66.241  1.00 23.17           C  
ANISOU 4167  CG  ASP B  71      957   2348   5496   -152    303   -469       C  
ATOM   4168  OD1 ASP B  71      69.008  89.167  67.092  1.00 22.51           O  
ANISOU 4168  OD1 ASP B  71      903   2215   5433    -34    -86   -388       O  
ATOM   4169  OD2 ASP B  71      70.624  90.180  65.962  1.00 23.32           O  
ANISOU 4169  OD2 ASP B  71      651   2531   5676   -260    -22   -705       O  
ATOM   4170  N   GLU B  72      66.065  89.480  67.813  1.00 24.00           N  
ANISOU 4170  N   GLU B  72     1333   2376   5407     71    469   -465       N  
ATOM   4171  CA  GLU B  72      65.704  89.418  69.230  1.00 24.66           C  
ANISOU 4171  CA  GLU B  72     1497   2516   5355     33    529   -434       C  
ATOM   4172  C   GLU B  72      66.551  88.381  69.966  1.00 24.26           C  
ANISOU 4172  C   GLU B  72     1697   2340   5177    -45    566   -460       C  
ATOM   4173  O   GLU B  72      66.188  87.930  71.047  1.00 25.47           O  
ANISOU 4173  O   GLU B  72     1960   2420   5295     -3    623   -466       O  
ATOM   4174  CB  GLU B  72      64.226  89.030  69.402  1.00 25.75           C  
ANISOU 4174  CB  GLU B  72     1640   2652   5490     50    546   -442       C  
ATOM   4175  CG  GLU B  72      63.275  89.813  68.529  1.00 29.62           C  
ANISOU 4175  CG  GLU B  72     1687   3532   6032    176    523   -228       C  
ATOM   4176  CD  GLU B  72      61.817  89.619  68.923  1.00 35.52           C  
ANISOU 4176  CD  GLU B  72     2301   4386   6808     57    879   -137       C  
ATOM   4177  OE1 GLU B  72      61.420  88.500  69.311  1.00 38.60           O  
ANISOU 4177  OE1 GLU B  72     2530   4838   7295   -269    892   -115       O  
ATOM   4178  OE2 GLU B  72      61.052  90.598  68.837  1.00 39.37           O  
ANISOU 4178  OE2 GLU B  72     2900   4964   7093    382    890   -126       O  
ATOM   4179  N   LEU B  73      67.685  88.006  69.393  1.00 23.80           N  
ANISOU 4179  N   LEU B  73     1832   2260   4950     23    581   -471       N  
ATOM   4180  CA  LEU B  73      68.514  86.945  69.959  1.00 23.66           C  
ANISOU 4180  CA  LEU B  73     2015   2267   4705    -38    554   -391       C  
ATOM   4181  C   LEU B  73      69.156  87.360  71.277  1.00 23.88           C  
ANISOU 4181  C   LEU B  73     2088   2274   4710    -41    521   -396       C  
ATOM   4182  O   LEU B  73      69.648  88.481  71.392  1.00 24.58           O  
ANISOU 4182  O   LEU B  73     2370   2343   4626    -41    533   -373       O  
ATOM   4183  CB  LEU B  73      69.606  86.557  68.966  1.00 23.15           C  
ANISOU 4183  CB  LEU B  73     1838   2183   4774    -34    543   -408       C  
ATOM   4184  CG  LEU B  73      69.135  85.899  67.671  1.00 22.46           C  
ANISOU 4184  CG  LEU B  73     1922   2083   4527   -274    665   -326       C  
ATOM   4185  CD1 LEU B  73      70.271  85.907  66.638  1.00 21.32           C  
ANISOU 4185  CD1 LEU B  73     1286   2124   4690     49    617   -490       C  
ATOM   4186  CD2 LEU B  73      68.660  84.459  67.962  1.00 21.77           C  
ANISOU 4186  CD2 LEU B  73     1805   2235   4230   -329    411    107       C  
ATOM   4187  N   THR B  74      69.168  86.456  72.253  1.00 23.23           N  
ANISOU 4187  N   THR B  74     2085   2203   4536     42    529   -372       N  
ATOM   4188  CA  THR B  74      69.728  86.736  73.570  1.00 24.15           C  
ANISOU 4188  CA  THR B  74     2319   2319   4538     67    493   -358       C  
ATOM   4189  C   THR B  74      70.895  85.834  73.943  1.00 24.32           C  
ANISOU 4189  C   THR B  74     2378   2357   4506     -4    374   -358       C  
ATOM   4190  O   THR B  74      71.518  86.042  74.986  1.00 24.82           O  
ANISOU 4190  O   THR B  74     2464   2553   4410     12    329   -443       O  
ATOM   4191  CB  THR B  74      68.666  86.611  74.680  1.00 24.62           C  
ANISOU 4191  CB  THR B  74     2474   2349   4531    103    513   -340       C  
ATOM   4192  OG1 THR B  74      68.095  85.295  74.637  1.00 26.58           O  
ANISOU 4192  OG1 THR B  74     2668   2574   4857     47    599   -144       O  
ATOM   4193  CG2 THR B  74      67.560  87.651  74.479  1.00 25.19           C  
ANISOU 4193  CG2 THR B  74     2556   2662   4353    501    567   -452       C  
ATOM   4194  N   ASN B  75      71.187  84.835  73.112  1.00 23.33           N  
ANISOU 4194  N   ASN B  75     2275   2175   4412    -39    372   -253       N  
ATOM   4195  CA  ASN B  75      72.140  83.800  73.497  1.00 23.14           C  
ANISOU 4195  CA  ASN B  75     2201   2127   4462   -140    219   -256       C  
ATOM   4196  C   ASN B  75      73.466  83.922  72.754  1.00 22.31           C  
ANISOU 4196  C   ASN B  75     2033   2015   4427   -217    177   -262       C  
ATOM   4197  O   ASN B  75      73.552  83.596  71.571  1.00 22.11           O  
ANISOU 4197  O   ASN B  75     1973   1904   4522   -223    121   -183       O  
ATOM   4198  CB  ASN B  75      71.508  82.414  73.300  1.00 22.69           C  
ANISOU 4198  CB  ASN B  75     2208   1993   4417   -109    259   -160       C  
ATOM   4199  CG  ASN B  75      72.380  81.286  73.844  1.00 23.65           C  
ANISOU 4199  CG  ASN B  75     2444   2123   4419    -78    196   -163       C  
ATOM   4200  OD1 ASN B  75      73.608  81.347  73.786  1.00 25.74           O  
ANISOU 4200  OD1 ASN B  75     2505   2449   4822    -76    165     22       O  
ATOM   4201  ND2 ASN B  75      71.744  80.252  74.380  1.00 22.88           N  
ANISOU 4201  ND2 ASN B  75     2534   2117   4040    -32    288     22       N  
ATOM   4202  N   HIS B  76      74.509  84.385  73.440  1.00 22.26           N  
ANISOU 4202  N   HIS B  76     1970   2031   4455   -197    118   -255       N  
ATOM   4203  CA  HIS B  76      75.787  84.624  72.759  1.00 21.85           C  
ANISOU 4203  CA  HIS B  76     1936   2038   4327   -254    128   -287       C  
ATOM   4204  C   HIS B  76      76.445  83.350  72.208  1.00 21.63           C  
ANISOU 4204  C   HIS B  76     1990   1987   4239   -303     70   -267       C  
ATOM   4205  O   HIS B  76      77.171  83.384  71.215  1.00 21.11           O  
ANISOU 4205  O   HIS B  76     1937   1891   4192   -342    131   -328       O  
ATOM   4206  CB  HIS B  76      76.741  85.430  73.648  1.00 21.65           C  
ANISOU 4206  CB  HIS B  76     1767   2058   4398   -244     63   -323       C  
ATOM   4207  CG  HIS B  76      78.137  85.525  73.108  1.00 23.71           C  
ANISOU 4207  CG  HIS B  76     2069   2365   4572   -206    328   -394       C  
ATOM   4208  ND1 HIS B  76      78.450  86.249  71.975  1.00 23.34           N  
ANISOU 4208  ND1 HIS B  76     2122   2050   4694   -116     93   -499       N  
ATOM   4209  CD2 HIS B  76      79.302  84.984  73.543  1.00 23.76           C  
ANISOU 4209  CD2 HIS B  76     2146   2318   4561   -372    221   -430       C  
ATOM   4210  CE1 HIS B  76      79.745  86.139  71.728  1.00 24.95           C  
ANISOU 4210  CE1 HIS B  76     2204   2553   4721   -283    233   -458       C  
ATOM   4211  NE2 HIS B  76      80.286  85.378  72.666  1.00 24.42           N  
ANISOU 4211  NE2 HIS B  76     1881   2479   4915   -135    180   -443       N  
ATOM   4212  N   THR B  77      76.159  82.207  72.820  1.00 21.76           N  
ANISOU 4212  N   THR B  77     2075   2084   4109   -258    -14   -245       N  
ATOM   4213  CA  THR B  77      76.734  80.938  72.378  1.00 20.90           C  
ANISOU 4213  CA  THR B  77     1890   2041   4009   -203    -67   -172       C  
ATOM   4214  C   THR B  77      76.320  80.573  70.954  1.00 20.59           C  
ANISOU 4214  C   THR B  77     1752   1991   4078   -193    -70   -168       C  
ATOM   4215  O   THR B  77      77.031  79.855  70.261  1.00 20.73           O  
ANISOU 4215  O   THR B  77     1588   2157   4131    -61   -159   -147       O  
ATOM   4216  CB  THR B  77      76.314  79.833  73.354  1.00 21.07           C  
ANISOU 4216  CB  THR B  77     1928   2084   3990   -242    -88   -204       C  
ATOM   4217  OG1 THR B  77      76.769  80.229  74.654  1.00 22.17           O  
ANISOU 4217  OG1 THR B  77     2137   2311   3974   -286   -123   -314       O  
ATOM   4218  CG2 THR B  77      76.936  78.494  72.982  1.00 21.39           C  
ANISOU 4218  CG2 THR B  77     1829   2236   4063   -233    -76   -144       C  
ATOM   4219  N   MET B  78      75.168  81.071  70.511  1.00 20.30           N  
ANISOU 4219  N   MET B  78     1664   2015   4032   -207   -141    -80       N  
ATOM   4220  CA  MET B  78      74.727  80.851  69.139  1.00 19.69           C  
ANISOU 4220  CA  MET B  78     1590   1874   4017   -246    -81    -57       C  
ATOM   4221  C   MET B  78      74.742  82.177  68.360  1.00 19.98           C  
ANISOU 4221  C   MET B  78     1586   1947   4059   -124    -42    -53       C  
ATOM   4222  O   MET B  78      74.268  82.226  67.230  1.00 19.08           O  
ANISOU 4222  O   MET B  78     1431   1711   4106    -18   -165     12       O  
ATOM   4223  CB  MET B  78      73.342  80.174  69.156  1.00 20.24           C  
ANISOU 4223  CB  MET B  78     1686   2004   3999   -254     18      2       C  
ATOM   4224  CG  MET B  78      73.375  78.828  69.883  1.00 19.16           C  
ANISOU 4224  CG  MET B  78     1605   1948   3726   -341     96   -157       C  
ATOM   4225  SD  MET B  78      71.816  77.924  69.765  1.00 20.41           S  
ANISOU 4225  SD  MET B  78     1447   2338   3969   -201    412   -252       S  
ATOM   4226  CE  MET B  78      70.756  78.930  70.804  1.00 18.83           C  
ANISOU 4226  CE  MET B  78     1205   2375   3573    -98    561   -263       C  
ATOM   4227  N   LEU B  79      75.361  83.199  68.964  1.00 20.23           N  
ANISOU 4227  N   LEU B  79     1651   1913   4122    -70     49    -87       N  
ATOM   4228  CA  LEU B  79      75.567  84.580  68.457  1.00 19.50           C  
ANISOU 4228  CA  LEU B  79     1547   1909   3952      7    150   -180       C  
ATOM   4229  C   LEU B  79      74.295  85.420  68.532  1.00 19.77           C  
ANISOU 4229  C   LEU B  79     1579   2001   3931     -8    127   -205       C  
ATOM   4230  O   LEU B  79      73.242  84.986  68.058  1.00 19.40           O  
ANISOU 4230  O   LEU B  79     1542   2019   3808     55    121   -243       O  
ATOM   4231  CB  LEU B  79      76.163  84.638  67.040  1.00 19.04           C  
ANISOU 4231  CB  LEU B  79     1401   1891   3940    -28    213   -143       C  
ATOM   4232  CG  LEU B  79      77.489  83.888  66.855  1.00 19.79           C  
ANISOU 4232  CG  LEU B  79     1451   2215   3852     66    258   -172       C  
ATOM   4233  CD1 LEU B  79      78.001  84.012  65.420  1.00 20.31           C  
ANISOU 4233  CD1 LEU B  79     1355   2461   3900    139    634   -372       C  
ATOM   4234  CD2 LEU B  79      78.543  84.404  67.832  1.00 20.39           C  
ANISOU 4234  CD2 LEU B  79     1301   2408   4037   -249    282   -106       C  
ATOM   4235  N   LYS B  80      74.413  86.594  69.156  1.00 20.17           N  
ANISOU 4235  N   LYS B  80     1641   2099   3921    -32     70   -306       N  
ATOM   4236  CA  LYS B  80      73.300  87.535  69.310  1.00 21.09           C  
ANISOU 4236  CA  LYS B  80     1720   2278   4013    -75     89   -407       C  
ATOM   4237  C   LYS B  80      73.042  88.360  68.049  1.00 20.74           C  
ANISOU 4237  C   LYS B  80     1635   2177   4067   -117     96   -361       C  
ATOM   4238  O   LYS B  80      71.938  88.881  67.837  1.00 20.80           O  
ANISOU 4238  O   LYS B  80     1582   2344   3977   -267     13   -375       O  
ATOM   4239  CB  LYS B  80      73.531  88.465  70.504  1.00 21.75           C  
ANISOU 4239  CB  LYS B  80     1825   2400   4037   -184     88   -417       C  
ATOM   4240  CG  LYS B  80      73.566  87.763  71.856  1.00 22.60           C  
ANISOU 4240  CG  LYS B  80     1984   2611   3989   -225     81   -489       C  
ATOM   4241  CD  LYS B  80      73.506  88.807  72.964  1.00 25.35           C  
ANISOU 4241  CD  LYS B  80     2219   3512   3900   -286    411   -737       C  
ATOM   4242  CE  LYS B  80      73.904  88.202  74.291  1.00 29.41           C  
ANISOU 4242  CE  LYS B  80     3210   3982   3983   -540    493   -733       C  
ATOM   4243  NZ  LYS B  80      73.767  89.190  75.410  1.00 31.53           N  
ANISOU 4243  NZ  LYS B  80     3620   4112   4246   -627    566   -999       N  
ATOM   4244  N   SER B  81      74.071  88.476  67.222  1.00 20.40           N  
ANISOU 4244  N   SER B  81     1429   2172   4147   -168     68   -385       N  
ATOM   4245  CA  SER B  81      74.001  89.168  65.936  1.00 20.59           C  
ANISOU 4245  CA  SER B  81     1370   2139   4311   -122     18   -326       C  
ATOM   4246  C   SER B  81      73.545  88.222  64.820  1.00 20.81           C  
ANISOU 4246  C   SER B  81     1389   2099   4417   -123    -39   -315       C  
ATOM   4247  O   SER B  81      73.566  87.004  64.973  1.00 20.54           O  
ANISOU 4247  O   SER B  81     1465   1965   4372     -3    -58   -312       O  
ATOM   4248  CB  SER B  81      75.389  89.693  65.577  1.00 20.60           C  
ANISOU 4248  CB  SER B  81     1413   2088   4323   -295     -2   -273       C  
ATOM   4249  OG  SER B  81      75.862  90.534  66.609  1.00 22.09           O  
ANISOU 4249  OG  SER B  81     1151   2674   4568   -250    115   -265       O  
ATOM   4250  N   THR B  82      73.159  88.773  63.674  1.00 20.51           N  
ANISOU 4250  N   THR B  82     1297   2065   4429    -78    -55   -325       N  
ATOM   4251  CA  THR B  82      72.790  87.912  62.557  1.00 21.05           C  
ANISOU 4251  CA  THR B  82     1370   1984   4644   -112    -98   -310       C  
ATOM   4252  C   THR B  82      72.938  88.650  61.234  1.00 21.31           C  
ANISOU 4252  C   THR B  82     1437   2073   4586   -115      6   -305       C  
ATOM   4253  O   THR B  82      73.039  89.874  61.200  1.00 21.21           O  
ANISOU 4253  O   THR B  82     1487   1996   4574   -112    120   -200       O  
ATOM   4254  CB  THR B  82      71.356  87.335  62.722  1.00 20.52           C  
ANISOU 4254  CB  THR B  82     1216   1847   4732    -12   -112   -392       C  
ATOM   4255  OG1 THR B  82      71.191  86.225  61.835  1.00 21.85           O  
ANISOU 4255  OG1 THR B  82     1355   1941   5007   -241   -272   -407       O  
ATOM   4256  CG2 THR B  82      70.265  88.373  62.428  1.00 21.50           C  
ANISOU 4256  CG2 THR B  82     1129   2023   5014    -18   -349   -377       C  
ATOM   4257  N   SER B  83      72.906  87.901  60.142  1.00 21.56           N  
ANISOU 4257  N   SER B  83     1547   2103   4539    -67     18   -262       N  
ATOM   4258  CA  SER B  83      72.994  88.477  58.808  1.00 21.79           C  
ANISOU 4258  CA  SER B  83     1652   2118   4507    -32   -118   -154       C  
ATOM   4259  C   SER B  83      72.346  87.414  57.924  1.00 21.51           C  
ANISOU 4259  C   SER B  83     1602   2130   4437     -3   -132   -122       C  
ATOM   4260  O   SER B  83      72.701  86.245  58.027  1.00 21.52           O  
ANISOU 4260  O   SER B  83     1665   2129   4379      4   -194   -124       O  
ATOM   4261  CB  SER B  83      74.465  88.707  58.438  1.00 22.19           C  
ANISOU 4261  CB  SER B  83     1716   2175   4541    -68    -81    -71       C  
ATOM   4262  OG  SER B  83      74.610  89.358  57.181  1.00 24.07           O  
ANISOU 4262  OG  SER B  83     2368   2191   4585    -60    -80   -116       O  
ATOM   4263  N   ILE B  84      71.386  87.792  57.083  1.00 21.44           N  
ANISOU 4263  N   ILE B  84     1588   2125   4432     45   -138    -70       N  
ATOM   4264  CA  ILE B  84      70.642  86.791  56.329  1.00 21.99           C  
ANISOU 4264  CA  ILE B  84     1695   2358   4299    124   -256    -58       C  
ATOM   4265  C   ILE B  84      70.982  86.899  54.854  1.00 22.11           C  
ANISOU 4265  C   ILE B  84     1662   2326   4413    142   -244    -10       C  
ATOM   4266  O   ILE B  84      70.941  87.980  54.267  1.00 23.03           O  
ANISOU 4266  O   ILE B  84     1909   2431   4410    159   -183     36       O  
ATOM   4267  CB  ILE B  84      69.114  86.943  56.449  1.00 22.77           C  
ANISOU 4267  CB  ILE B  84     1854   2461   4333     41   -160    -80       C  
ATOM   4268  CG1 ILE B  84      68.656  87.119  57.908  1.00 26.11           C  
ANISOU 4268  CG1 ILE B  84     2438   2950   4532    308   -105     -8       C  
ATOM   4269  CG2 ILE B  84      68.429  85.782  55.728  1.00 21.76           C  
ANISOU 4269  CG2 ILE B  84     1610   2198   4459     32   -511     76       C  
ATOM   4270  CD1 ILE B  84      69.239  86.148  58.913  1.00 27.74           C  
ANISOU 4270  CD1 ILE B  84     3058   2385   5093    324    -18    159       C  
ATOM   4271  N   HIS B  85      71.307  85.752  54.273  1.00 21.70           N  
ANISOU 4271  N   HIS B  85     1640   2203   4401    124   -358    -18       N  
ATOM   4272  CA  HIS B  85      71.550  85.647  52.848  1.00 21.71           C  
ANISOU 4272  CA  HIS B  85     1673   2216   4358    167   -496     46       C  
ATOM   4273  C   HIS B  85      70.360  84.976  52.165  1.00 22.03           C  
ANISOU 4273  C   HIS B  85     1808   2185   4376    186   -601     44       C  
ATOM   4274  O   HIS B  85      69.804  84.009  52.693  1.00 22.19           O  
ANISOU 4274  O   HIS B  85     1796   2313   4321     35   -666     91       O  
ATOM   4275  CB  HIS B  85      72.846  84.855  52.647  1.00 21.62           C  
ANISOU 4275  CB  HIS B  85     1542   2315   4356    282   -587    120       C  
ATOM   4276  CG  HIS B  85      73.126  84.505  51.223  1.00 22.54           C  
ANISOU 4276  CG  HIS B  85     1629   2487   4446    240   -513    160       C  
ATOM   4277  ND1 HIS B  85      73.205  85.456  50.228  1.00 23.61           N  
ANISOU 4277  ND1 HIS B  85     1939   2491   4539     81   -549    252       N  
ATOM   4278  CD2 HIS B  85      73.334  83.308  50.625  1.00 23.04           C  
ANISOU 4278  CD2 HIS B  85     1642   2592   4518    218   -861    297       C  
ATOM   4279  CE1 HIS B  85      73.471  84.864  49.079  1.00 24.20           C  
ANISOU 4279  CE1 HIS B  85     2216   2575   4403    121   -495    336       C  
ATOM   4280  NE2 HIS B  85      73.550  83.564  49.294  1.00 25.45           N  
ANISOU 4280  NE2 HIS B  85     1936   3007   4725     42   -355     57       N  
ATOM   4281  N   TRP B  86      69.976  85.518  51.009  1.00 22.39           N  
ANISOU 4281  N   TRP B  86     2001   2143   4363    175   -694    -28       N  
ATOM   4282  CA  TRP B  86      68.842  85.048  50.205  1.00 22.50           C  
ANISOU 4282  CA  TRP B  86     2079   2053   4414    318   -632    -12       C  
ATOM   4283  C   TRP B  86      69.474  84.270  49.054  1.00 22.80           C  
ANISOU 4283  C   TRP B  86     2271   2060   4328    308   -681    -10       C  
ATOM   4284  O   TRP B  86      69.847  84.842  48.019  1.00 22.59           O  
ANISOU 4284  O   TRP B  86     2246   1944   4390    338   -636    -17       O  
ATOM   4285  CB  TRP B  86      67.997  86.254  49.753  1.00 22.25           C  
ANISOU 4285  CB  TRP B  86     2107   2002   4343    367   -643    -12       C  
ATOM   4286  CG  TRP B  86      67.903  87.244  50.885  1.00 22.86           C  
ANISOU 4286  CG  TRP B  86     2121   1837   4726    287   -621      2       C  
ATOM   4287  CD1 TRP B  86      68.690  88.337  51.079  1.00 22.73           C  
ANISOU 4287  CD1 TRP B  86     2209   1409   5015    368   -406     -8       C  
ATOM   4288  CD2 TRP B  86      67.049  87.155  52.036  1.00 22.99           C  
ANISOU 4288  CD2 TRP B  86     2206   1707   4819    429   -541     50       C  
ATOM   4289  NE1 TRP B  86      68.367  88.950  52.265  1.00 23.78           N  
ANISOU 4289  NE1 TRP B  86     2122   1774   5138    249   -307      3       N  
ATOM   4290  CE2 TRP B  86      67.365  88.242  52.875  1.00 23.19           C  
ANISOU 4290  CE2 TRP B  86     2185   1546   5080    412   -481    172       C  
ATOM   4291  CE3 TRP B  86      66.048  86.264  52.437  1.00 25.09           C  
ANISOU 4291  CE3 TRP B  86     2388   2098   5044    249   -613    -44       C  
ATOM   4292  CZ2 TRP B  86      66.697  88.479  54.076  1.00 23.96           C  
ANISOU 4292  CZ2 TRP B  86     2255   1666   5181    364   -381    244       C  
ATOM   4293  CZ3 TRP B  86      65.380  86.495  53.636  1.00 23.33           C  
ANISOU 4293  CZ3 TRP B  86     1981   1845   5036    403   -586     89       C  
ATOM   4294  CH2 TRP B  86      65.713  87.591  54.444  1.00 24.73           C  
ANISOU 4294  CH2 TRP B  86     2370   1508   5517    348   -420    163       C  
ATOM   4295  N   HIS B  87      69.654  82.969  49.292  1.00 22.48           N  
ANISOU 4295  N   HIS B  87     2293   2006   4240    383   -685     15       N  
ATOM   4296  CA  HIS B  87      70.502  82.130  48.451  1.00 23.07           C  
ANISOU 4296  CA  HIS B  87     2418   2159   4186    382   -677    114       C  
ATOM   4297  C   HIS B  87      69.922  81.972  47.046  1.00 23.60           C  
ANISOU 4297  C   HIS B  87     2540   2282   4144    347   -715    168       C  
ATOM   4298  O   HIS B  87      68.811  81.458  46.876  1.00 24.02           O  
ANISOU 4298  O   HIS B  87     2582   2297   4248    462   -754    146       O  
ATOM   4299  CB  HIS B  87      70.717  80.773  49.119  1.00 22.56           C  
ANISOU 4299  CB  HIS B  87     2389   2064   4118    397   -566     91       C  
ATOM   4300  CG  HIS B  87      71.618  79.855  48.354  1.00 22.98           C  
ANISOU 4300  CG  HIS B  87     2436   2181   4112    476   -480    161       C  
ATOM   4301  ND1 HIS B  87      72.764  79.309  48.898  1.00 23.20           N  
ANISOU 4301  ND1 HIS B  87     2646   2340   3826    579   -351    208       N  
ATOM   4302  CD2 HIS B  87      71.559  79.415  47.073  1.00 22.06           C  
ANISOU 4302  CD2 HIS B  87     2279   1979   4123    343   -540    193       C  
ATOM   4303  CE1 HIS B  87      73.358  78.554  47.988  1.00 23.31           C  
ANISOU 4303  CE1 HIS B  87     2770   2077   4006    622   -319    127       C  
ATOM   4304  NE2 HIS B  87      72.642  78.595  46.876  1.00 23.45           N  
ANISOU 4304  NE2 HIS B  87     2780   2159   3970    657   -139     27       N  
ATOM   4305  N   GLY B  88      70.672  82.435  46.048  1.00 24.40           N  
ANISOU 4305  N   GLY B  88     2671   2376   4220    338   -792    273       N  
ATOM   4306  CA  GLY B  88      70.266  82.285  44.648  1.00 24.70           C  
ANISOU 4306  CA  GLY B  88     2713   2484   4186    316   -889    448       C  
ATOM   4307  C   GLY B  88      69.872  83.581  43.951  1.00 25.52           C  
ANISOU 4307  C   GLY B  88     2883   2492   4319    301   -907    504       C  
ATOM   4308  O   GLY B  88      69.876  83.654  42.721  1.00 25.68           O  
ANISOU 4308  O   GLY B  88     2921   2583   4250    317   -875    619       O  
ATOM   4309  N   PHE B  89      69.523  84.603  44.724  1.00 26.20           N  
ANISOU 4309  N   PHE B  89     2983   2507   4465    302   -893    554       N  
ATOM   4310  CA  PHE B  89      69.129  85.899  44.167  1.00 27.23           C  
ANISOU 4310  CA  PHE B  89     3114   2599   4631    299   -936    517       C  
ATOM   4311  C   PHE B  89      70.332  86.694  43.674  1.00 27.65           C  
ANISOU 4311  C   PHE B  89     3320   2535   4651    265   -945    488       C  
ATOM   4312  O   PHE B  89      71.349  86.776  44.359  1.00 28.81           O  
ANISOU 4312  O   PHE B  89     3472   2722   4750    197   -949    461       O  
ATOM   4313  CB  PHE B  89      68.342  86.693  45.206  1.00 26.70           C  
ANISOU 4313  CB  PHE B  89     3000   2506   4637    317   -918    595       C  
ATOM   4314  CG  PHE B  89      66.958  86.153  45.437  1.00 28.00           C  
ANISOU 4314  CG  PHE B  89     2824   2847   4965    335   -983    464       C  
ATOM   4315  CD1 PHE B  89      65.904  86.574  44.641  1.00 30.86           C  
ANISOU 4315  CD1 PHE B  89     2924   3546   5253     87  -1002    623       C  
ATOM   4316  CD2 PHE B  89      66.715  85.222  46.440  1.00 28.83           C  
ANISOU 4316  CD2 PHE B  89     2574   3171   5209    169   -816    449       C  
ATOM   4317  CE1 PHE B  89      64.624  86.080  44.846  1.00 32.75           C  
ANISOU 4317  CE1 PHE B  89     2896   4019   5527     10  -1070    666       C  
ATOM   4318  CE2 PHE B  89      65.436  84.716  46.653  1.00 29.90           C  
ANISOU 4318  CE2 PHE B  89     2619   3460   5279     40  -1164    382       C  
ATOM   4319  CZ  PHE B  89      64.389  85.152  45.851  1.00 31.30           C  
ANISOU 4319  CZ  PHE B  89     2782   3611   5500    186  -1120    750       C  
ATOM   4320  N   PHE B  90      70.216  87.267  42.482  1.00 28.68           N  
ANISOU 4320  N   PHE B  90     3570   2657   4667    199   -945    419       N  
ATOM   4321  CA  PHE B  90      71.324  87.992  41.861  1.00 29.54           C  
ANISOU 4321  CA  PHE B  90     3747   2786   4691    206   -922    452       C  
ATOM   4322  C   PHE B  90      71.691  89.290  42.583  1.00 29.23           C  
ANISOU 4322  C   PHE B  90     3754   2754   4597    238   -931    508       C  
ATOM   4323  O   PHE B  90      72.855  89.704  42.561  1.00 28.83           O  
ANISOU 4323  O   PHE B  90     3709   2708   4534    276   -861    530       O  
ATOM   4324  CB  PHE B  90      71.025  88.273  40.383  1.00 30.05           C  
ANISOU 4324  CB  PHE B  90     3828   2888   4700    157   -961    375       C  
ATOM   4325  CG  PHE B  90      70.882  87.033  39.540  1.00 32.53           C  
ANISOU 4325  CG  PHE B  90     4123   3320   4917     37   -966    202       C  
ATOM   4326  CD1 PHE B  90      71.588  85.875  39.839  1.00 34.09           C  
ANISOU 4326  CD1 PHE B  90     4123   3608   5220    165  -1163     25       C  
ATOM   4327  CD2 PHE B  90      70.051  87.039  38.426  1.00 34.20           C  
ANISOU 4327  CD2 PHE B  90     4219   3658   5115    -32  -1140    100       C  
ATOM   4328  CE1 PHE B  90      71.458  84.728  39.046  1.00 35.55           C  
ANISOU 4328  CE1 PHE B  90     4226   3976   5303     85  -1221   -157       C  
ATOM   4329  CE2 PHE B  90      69.924  85.910  37.625  1.00 36.19           C  
ANISOU 4329  CE2 PHE B  90     4578   4034   5139    -15  -1178    -77       C  
ATOM   4330  CZ  PHE B  90      70.625  84.753  37.934  1.00 36.09           C  
ANISOU 4330  CZ  PHE B  90     4476   4048   5186    105  -1160   -217       C  
ATOM   4331  N   GLN B  91      70.706  89.927  43.215  1.00 28.60           N  
ANISOU 4331  N   GLN B  91     3696   2608   4562    306   -930    634       N  
ATOM   4332  CA  GLN B  91      70.938  91.175  43.948  1.00 28.83           C  
ANISOU 4332  CA  GLN B  91     3772   2621   4560    328   -899    741       C  
ATOM   4333  C   GLN B  91      71.566  92.257  43.068  1.00 29.41           C  
ANISOU 4333  C   GLN B  91     3827   2624   4723    344   -839    754       C  
ATOM   4334  O   GLN B  91      72.416  93.014  43.529  1.00 28.81           O  
ANISOU 4334  O   GLN B  91     3666   2578   4701    443   -907    884       O  
ATOM   4335  CB  GLN B  91      71.803  90.935  45.196  1.00 28.60           C  
ANISOU 4335  CB  GLN B  91     3729   2617   4518    221   -883    692       C  
ATOM   4336  CG  GLN B  91      71.192  89.979  46.228  1.00 28.97           C  
ANISOU 4336  CG  GLN B  91     3767   2726   4513    303   -860    716       C  
ATOM   4337  CD  GLN B  91      69.936  90.526  46.907  1.00 29.62           C  
ANISOU 4337  CD  GLN B  91     3825   2724   4704    264   -750    618       C  
ATOM   4338  OE1 GLN B  91      69.542  91.672  46.691  1.00 29.19           O  
ANISOU 4338  OE1 GLN B  91     3720   2748   4621    255   -866    495       O  
ATOM   4339  NE2 GLN B  91      69.300  89.695  47.733  1.00 28.69           N  
ANISOU 4339  NE2 GLN B  91     3628   2575   4695    236   -693    505       N  
ATOM   4340  N   HIS B  92      71.148  92.340  41.806  1.00 30.44           N  
ANISOU 4340  N   HIS B  92     4029   2726   4810    343   -759    832       N  
ATOM   4341  CA  HIS B  92      71.718  93.319  40.883  1.00 32.31           C  
ANISOU 4341  CA  HIS B  92     4267   2940   5066    360   -644    835       C  
ATOM   4342  C   HIS B  92      71.415  94.724  41.401  1.00 31.87           C  
ANISOU 4342  C   HIS B  92     4207   2857   5042    313   -665    839       C  
ATOM   4343  O   HIS B  92      70.250  95.093  41.589  1.00 31.78           O  
ANISOU 4343  O   HIS B  92     4198   2781   5093    389   -630    852       O  
ATOM   4344  CB  HIS B  92      71.186  93.086  39.462  1.00 33.71           C  
ANISOU 4344  CB  HIS B  92     4431   3169   5208    400   -616    904       C  
ATOM   4345  CG  HIS B  92      71.952  93.814  38.402  1.00 39.47           C  
ANISOU 4345  CG  HIS B  92     5114   4006   5877    413   -206    941       C  
ATOM   4346  ND1 HIS B  92      71.780  95.159  38.150  1.00 43.50           N  
ANISOU 4346  ND1 HIS B  92     5739   4198   6591    539     44    874       N  
ATOM   4347  CD2 HIS B  92      72.890  93.386  37.523  1.00 43.66           C  
ANISOU 4347  CD2 HIS B  92     5605   4576   6406    577     38    863       C  
ATOM   4348  CE1 HIS B  92      72.581  95.531  37.166  1.00 45.31           C  
ANISOU 4348  CE1 HIS B  92     5914   4507   6794    470    202    871       C  
ATOM   4349  NE2 HIS B  92      73.267  94.473  36.769  1.00 45.86           N  
ANISOU 4349  NE2 HIS B  92     5906   4586   6933    530    156    970       N  
ATOM   4350  N   GLY B  93      72.468  95.483  41.692  1.00 31.29           N  
ANISOU 4350  N   GLY B  93     4183   2732   4974    302   -636    762       N  
ATOM   4351  CA  GLY B  93      72.317  96.835  42.230  1.00 30.22           C  
ANISOU 4351  CA  GLY B  93     4014   2554   4911    225   -636    781       C  
ATOM   4352  C   GLY B  93      71.882  96.897  43.689  1.00 29.42           C  
ANISOU 4352  C   GLY B  93     3796   2468   4914    220   -635    688       C  
ATOM   4353  O   GLY B  93      71.626  97.983  44.210  1.00 28.61           O  
ANISOU 4353  O   GLY B  93     3704   2265   4902    181   -559    797       O  
ATOM   4354  N   THR B  94      71.775  95.737  44.339  1.00 28.26           N  
ANISOU 4354  N   THR B  94     3601   2345   4790    276   -733    699       N  
ATOM   4355  CA  THR B  94      71.443  95.651  45.762  1.00 27.79           C  
ANISOU 4355  CA  THR B  94     3378   2411   4770    342   -776    545       C  
ATOM   4356  C   THR B  94      72.446  94.735  46.472  1.00 27.76           C  
ANISOU 4356  C   THR B  94     3333   2491   4720    261   -735    512       C  
ATOM   4357  O   THR B  94      72.078  93.894  47.291  1.00 27.31           O  
ANISOU 4357  O   THR B  94     3203   2496   4677    226   -780    469       O  
ATOM   4358  CB  THR B  94      69.980  95.211  46.029  1.00 28.14           C  
ANISOU 4358  CB  THR B  94     3489   2353   4848    354   -759    554       C  
ATOM   4359  OG1 THR B  94      69.695  93.965  45.375  1.00 26.95           O  
ANISOU 4359  OG1 THR B  94     3181   2400   4659    687   -893    526       O  
ATOM   4360  CG2 THR B  94      68.981  96.286  45.558  1.00 27.92           C  
ANISOU 4360  CG2 THR B  94     3479   2378   4751    363   -881    576       C  
ATOM   4361  N   ASN B  95      73.725  94.901  46.143  1.00 27.03           N  
ANISOU 4361  N   ASN B  95     3091   2515   4664    250   -700    451       N  
ATOM   4362  CA  ASN B  95      74.778  94.101  46.766  1.00 26.44           C  
ANISOU 4362  CA  ASN B  95     3000   2396   4649    245   -609    407       C  
ATOM   4363  C   ASN B  95      74.717  94.163  48.289  1.00 26.19           C  
ANISOU 4363  C   ASN B  95     2893   2341   4716    223   -558    377       C  
ATOM   4364  O   ASN B  95      75.023  93.179  48.957  1.00 26.36           O  
ANISOU 4364  O   ASN B  95     2867   2379   4767    189   -513    344       O  
ATOM   4365  CB  ASN B  95      76.157  94.548  46.288  1.00 25.76           C  
ANISOU 4365  CB  ASN B  95     2957   2320   4511    253   -580    450       C  
ATOM   4366  CG  ASN B  95      77.269  93.668  46.825  1.00 26.07           C  
ANISOU 4366  CG  ASN B  95     3019   2368   4517    162   -486    424       C  
ATOM   4367  OD1 ASN B  95      77.765  93.873  47.939  1.00 24.44           O  
ANISOU 4367  OD1 ASN B  95     2798   2133   4352    247   -615    491       O  
ATOM   4368  ND2 ASN B  95      77.658  92.668  46.038  1.00 26.16           N  
ANISOU 4368  ND2 ASN B  95     3150   2323   4466    208   -240    460       N  
ATOM   4369  N   TRP B  96      74.315  95.318  48.818  1.00 26.04           N  
ANISOU 4369  N   TRP B  96     2811   2265   4816    198   -536    318       N  
ATOM   4370  CA  TRP B  96      74.230  95.567  50.259  1.00 25.78           C  
ANISOU 4370  CA  TRP B  96     2722   2190   4882    210   -484    265       C  
ATOM   4371  C   TRP B  96      73.205  94.674  50.950  1.00 25.65           C  
ANISOU 4371  C   TRP B  96     2647   2231   4867    189   -508    294       C  
ATOM   4372  O   TRP B  96      73.187  94.605  52.182  1.00 25.31           O  
ANISOU 4372  O   TRP B  96     2547   2248   4821    194   -512    312       O  
ATOM   4373  CB  TRP B  96      73.870  97.036  50.527  1.00 26.11           C  
ANISOU 4373  CB  TRP B  96     2804   2146   4970    179   -515    223       C  
ATOM   4374  CG  TRP B  96      72.529  97.442  49.959  1.00 26.78           C  
ANISOU 4374  CG  TRP B  96     2919   2179   5076    306   -556     45       C  
ATOM   4375  CD1 TRP B  96      72.304  98.043  48.747  1.00 26.97           C  
ANISOU 4375  CD1 TRP B  96     3104   2017   5124    430   -725   -159       C  
ATOM   4376  CD2 TRP B  96      71.243  97.299  50.579  1.00 26.73           C  
ANISOU 4376  CD2 TRP B  96     2965   1947   5242    202   -617   -118       C  
ATOM   4377  NE1 TRP B  96      70.961  98.255  48.567  1.00 27.13           N  
ANISOU 4377  NE1 TRP B  96     3077   1945   5287    380   -517   -243       N  
ATOM   4378  CE2 TRP B  96      70.287  97.811  49.676  1.00 27.90           C  
ANISOU 4378  CE2 TRP B  96     2992   2281   5327    214   -632   -178       C  
ATOM   4379  CE3 TRP B  96      70.805  96.785  51.806  1.00 26.96           C  
ANISOU 4379  CE3 TRP B  96     2814   2182   5246    110   -598   -285       C  
ATOM   4380  CZ2 TRP B  96      68.919  97.835  49.965  1.00 28.23           C  
ANISOU 4380  CZ2 TRP B  96     3038   2282   5403    375   -538   -255       C  
ATOM   4381  CZ3 TRP B  96      69.444  96.802  52.091  1.00 27.25           C  
ANISOU 4381  CZ3 TRP B  96     2870   2180   5300    236   -779   -295       C  
ATOM   4382  CH2 TRP B  96      68.518  97.323  51.171  1.00 28.37           C  
ANISOU 4382  CH2 TRP B  96     2988   2323   5467    341   -671   -105       C  
ATOM   4383  N   ALA B  97      72.339  94.036  50.164  1.00 25.17           N  
ANISOU 4383  N   ALA B  97     2555   2211   4798     99   -487    279       N  
ATOM   4384  CA  ALA B  97      71.287  93.165  50.699  1.00 25.24           C  
ANISOU 4384  CA  ALA B  97     2430   2350   4810    158   -497    282       C  
ATOM   4385  C   ALA B  97      71.634  91.670  50.608  1.00 24.49           C  
ANISOU 4385  C   ALA B  97     2337   2297   4668    142   -450    230       C  
ATOM   4386  O   ALA B  97      70.844  90.816  51.009  1.00 24.46           O  
ANISOU 4386  O   ALA B  97     2285   2249   4759     89   -521    267       O  
ATOM   4387  CB  ALA B  97      69.959  93.447  49.982  1.00 25.25           C  
ANISOU 4387  CB  ALA B  97     2366   2425   4802    177   -505    263       C  
ATOM   4388  N   ASP B  98      72.806  91.344  50.073  1.00 24.64           N  
ANISOU 4388  N   ASP B  98     2306   2381   4674    158   -484    211       N  
ATOM   4389  CA  ASP B  98      73.147  89.947  49.790  1.00 23.90           C  
ANISOU 4389  CA  ASP B  98     2239   2316   4526    149   -355    135       C  
ATOM   4390  C   ASP B  98      73.392  89.113  51.051  1.00 23.65           C  
ANISOU 4390  C   ASP B  98     2199   2436   4349    147   -326    115       C  
ATOM   4391  O   ASP B  98      73.213  87.892  51.036  1.00 23.67           O  
ANISOU 4391  O   ASP B  98     2296   2442   4253    153   -300    232       O  
ATOM   4392  CB  ASP B  98      74.334  89.857  48.828  1.00 24.29           C  
ANISOU 4392  CB  ASP B  98     2267   2375   4584     93   -352     91       C  
ATOM   4393  CG  ASP B  98      74.527  88.459  48.245  1.00 24.42           C  
ANISOU 4393  CG  ASP B  98     2257   2222   4797    173   -295    204       C  
ATOM   4394  OD1 ASP B  98      73.524  87.780  47.902  1.00 25.16           O  
ANISOU 4394  OD1 ASP B  98     2416   2449   4692    219   -552    278       O  
ATOM   4395  OD2 ASP B  98      75.704  88.062  48.093  1.00 24.19           O  
ANISOU 4395  OD2 ASP B  98     2209   2123   4856    -66    -92    333       O  
ATOM   4396  N   GLY B  99      73.814  89.755  52.140  1.00 23.72           N  
ANISOU 4396  N   GLY B  99     2141   2518   4354    140   -258    107       N  
ATOM   4397  CA  GLY B  99      73.822  89.074  53.440  1.00 22.99           C  
ANISOU 4397  CA  GLY B  99     2063   2481   4190     93   -190     88       C  
ATOM   4398  C   GLY B  99      75.094  88.426  53.950  1.00 23.10           C  
ANISOU 4398  C   GLY B  99     2104   2447   4223     54   -142     61       C  
ATOM   4399  O   GLY B  99      75.145  87.972  55.101  1.00 22.80           O  
ANISOU 4399  O   GLY B  99     2051   2479   4132     45   -100      4       O  
ATOM   4400  N   GLY B 100      76.124  88.375  53.109  1.00 22.73           N  
ANISOU 4400  N   GLY B 100     1939   2492   4205     79   -109     29       N  
ATOM   4401  CA  GLY B 100      77.396  87.771  53.514  1.00 23.03           C  
ANISOU 4401  CA  GLY B 100     2062   2472   4214      7   -183    166       C  
ATOM   4402  C   GLY B 100      78.041  88.628  54.592  1.00 22.53           C  
ANISOU 4402  C   GLY B 100     1993   2418   4149     -4   -156    197       C  
ATOM   4403  O   GLY B 100      78.419  89.776  54.336  1.00 22.29           O  
ANISOU 4403  O   GLY B 100     1902   2340   4225     72   -179    236       O  
ATOM   4404  N   ALA B 101      78.134  88.095  55.808  1.00 21.77           N  
ANISOU 4404  N   ALA B 101     1876   2307   4088     47   -120    276       N  
ATOM   4405  CA  ALA B 101      78.725  88.865  56.898  1.00 21.85           C  
ANISOU 4405  CA  ALA B 101     1838   2305   4159   -126    -64    293       C  
ATOM   4406  C   ALA B 101      80.167  89.277  56.598  1.00 22.09           C  
ANISOU 4406  C   ALA B 101     1831   2326   4235    -19     50    285       C  
ATOM   4407  O   ALA B 101      80.996  88.443  56.220  1.00 22.04           O  
ANISOU 4407  O   ALA B 101     1833   2174   4366    -75     35    305       O  
ATOM   4408  CB  ALA B 101      78.660  88.102  58.220  1.00 22.27           C  
ANISOU 4408  CB  ALA B 101     2014   2318   4129    -75    -50    340       C  
ATOM   4409  N   PHE B 102      80.424  90.576  56.768  1.00 21.30           N  
ANISOU 4409  N   PHE B 102     1641   2224   4225    -74     26    293       N  
ATOM   4410  CA  PHE B 102      81.718  91.218  56.522  1.00 21.53           C  
ANISOU 4410  CA  PHE B 102     1637   2349   4193     56     20    291       C  
ATOM   4411  C   PHE B 102      82.132  91.227  55.055  1.00 21.75           C  
ANISOU 4411  C   PHE B 102     1738   2320   4204     76     25    291       C  
ATOM   4412  O   PHE B 102      83.267  91.562  54.712  1.00 21.79           O  
ANISOU 4412  O   PHE B 102     1840   2226   4209      1    178    301       O  
ATOM   4413  CB  PHE B 102      82.790  90.681  57.479  1.00 21.66           C  
ANISOU 4413  CB  PHE B 102     1602   2387   4239     62    -61    243       C  
ATOM   4414  CG  PHE B 102      82.350  90.707  58.916  1.00 22.47           C  
ANISOU 4414  CG  PHE B 102     1480   2710   4344    198   -249    143       C  
ATOM   4415  CD1 PHE B 102      82.330  91.905  59.620  1.00 23.62           C  
ANISOU 4415  CD1 PHE B 102     1396   3019   4558    341   -293    -66       C  
ATOM   4416  CD2 PHE B 102      81.914  89.546  59.550  1.00 23.13           C  
ANISOU 4416  CD2 PHE B 102     1209   2960   4618    417   -132     75       C  
ATOM   4417  CE1 PHE B 102      81.899  91.951  60.937  1.00 24.49           C  
ANISOU 4417  CE1 PHE B 102     1462   3306   4536     44   -465    -43       C  
ATOM   4418  CE2 PHE B 102      81.498  89.575  60.879  1.00 24.50           C  
ANISOU 4418  CE2 PHE B 102     1411   3225   4672    328   -209    -89       C  
ATOM   4419  CZ  PHE B 102      81.496  90.787  61.577  1.00 24.57           C  
ANISOU 4419  CZ  PHE B 102     1350   3067   4917     61   -347   -167       C  
ATOM   4420  N   VAL B 103      81.187  90.890  54.184  1.00 22.20           N  
ANISOU 4420  N   VAL B 103     1931   2342   4161    127     82    318       N  
ATOM   4421  CA  VAL B 103      81.420  91.058  52.757  1.00 22.14           C  
ANISOU 4421  CA  VAL B 103     1979   2319   4113    189    105    346       C  
ATOM   4422  C   VAL B 103      80.419  92.082  52.244  1.00 22.28           C  
ANISOU 4422  C   VAL B 103     1888   2352   4221    171    141    339       C  
ATOM   4423  O   VAL B 103      80.787  93.101  51.640  1.00 22.73           O  
ANISOU 4423  O   VAL B 103     1863   2470   4301    241    212    419       O  
ATOM   4424  CB  VAL B 103      81.296  89.726  52.011  1.00 21.89           C  
ANISOU 4424  CB  VAL B 103     2021   2258   4039    213    128    380       C  
ATOM   4425  CG1 VAL B 103      81.429  89.933  50.504  1.00 22.85           C  
ANISOU 4425  CG1 VAL B 103     2299   2356   4025    268    139    394       C  
ATOM   4426  CG2 VAL B 103      82.361  88.767  52.512  1.00 21.11           C  
ANISOU 4426  CG2 VAL B 103     1908   2218   3895    276    232    264       C  
ATOM   4427  N   ASN B 104      79.145  91.826  52.520  1.00 22.16           N  
ANISOU 4427  N   ASN B 104     1911   2323   4182    156    184    285       N  
ATOM   4428  CA  ASN B 104      78.101  92.713  52.031  1.00 21.95           C  
ANISOU 4428  CA  ASN B 104     1869   2410   4062     66    125    197       C  
ATOM   4429  C   ASN B 104      77.522  93.626  53.104  1.00 22.09           C  
ANISOU 4429  C   ASN B 104     1819   2398   4175     20    110    130       C  
ATOM   4430  O   ASN B 104      76.855  94.584  52.751  1.00 22.10           O  
ANISOU 4430  O   ASN B 104     1887   2383   4124     80     53     39       O  
ATOM   4431  CB  ASN B 104      76.996  91.897  51.359  1.00 21.69           C  
ANISOU 4431  CB  ASN B 104     1924   2293   4021     37    167    230       C  
ATOM   4432  CG  ASN B 104      77.559  90.873  50.414  1.00 21.70           C  
ANISOU 4432  CG  ASN B 104     2095   2329   3819     59    366    359       C  
ATOM   4433  OD1 ASN B 104      77.631  89.700  50.769  1.00 21.24           O  
ANISOU 4433  OD1 ASN B 104     2117   2587   3367   -191    365    378       O  
ATOM   4434  ND2 ASN B 104      78.040  91.313  49.246  1.00 23.26           N  
ANISOU 4434  ND2 ASN B 104     2817   2074   3944    -57    324    823       N  
ATOM   4435  N   GLN B 105      77.791  93.338  54.381  1.00 21.78           N  
ANISOU 4435  N   GLN B 105     1687   2459   4126   -116     85     62       N  
ATOM   4436  CA  GLN B 105      77.256  94.143  55.487  1.00 21.94           C  
ANISOU 4436  CA  GLN B 105     1580   2393   4361   -106     96     78       C  
ATOM   4437  C   GLN B 105      77.979  93.791  56.781  1.00 22.32           C  
ANISOU 4437  C   GLN B 105     1616   2396   4468   -103     50     46       C  
ATOM   4438  O   GLN B 105      78.616  92.735  56.849  1.00 23.20           O  
ANISOU 4438  O   GLN B 105     1615   2642   4557     68    104    -43       O  
ATOM   4439  CB  GLN B 105      75.759  93.867  55.693  1.00 20.82           C  
ANISOU 4439  CB  GLN B 105     1448   2239   4221   -245     60    149       C  
ATOM   4440  CG  GLN B 105      75.461  92.459  56.245  1.00 20.77           C  
ANISOU 4440  CG  GLN B 105     1484   2150   4257   -176    163    237       C  
ATOM   4441  CD  GLN B 105      73.992  92.279  56.614  1.00 21.54           C  
ANISOU 4441  CD  GLN B 105     1622   2307   4254   -307    -74    567       C  
ATOM   4442  OE1 GLN B 105      73.163  91.915  55.774  1.00 21.99           O  
ANISOU 4442  OE1 GLN B 105     1713   2345   4295    -79   -298    783       O  
ATOM   4443  NE2 GLN B 105      73.664  92.525  57.882  1.00 20.39           N  
ANISOU 4443  NE2 GLN B 105     1311   2511   3925   -124   -231    543       N  
ATOM   4444  N   CYS B 106      77.870  94.642  57.801  1.00 22.73           N  
ANISOU 4444  N   CYS B 106     1572   2333   4730   -137     85    -19       N  
ATOM   4445  CA  CYS B 106      78.141  94.207  59.175  1.00 23.34           C  
ANISOU 4445  CA  CYS B 106     1645   2312   4909   -141     24   -111       C  
ATOM   4446  C   CYS B 106      76.868  93.525  59.673  1.00 22.47           C  
ANISOU 4446  C   CYS B 106     1494   2140   4904   -127    -26   -112       C  
ATOM   4447  O   CYS B 106      75.760  93.839  59.199  1.00 23.23           O  
ANISOU 4447  O   CYS B 106     1732   2208   4884     10    -42   -151       O  
ATOM   4448  CB  CYS B 106      78.488  95.369  60.122  1.00 23.64           C  
ANISOU 4448  CB  CYS B 106     1724   2199   5058   -167     65   -115       C  
ATOM   4449  SG  CYS B 106      80.192  96.004  59.989  1.00 28.42           S  
ANISOU 4449  SG  CYS B 106     2183   2849   5767   -226    185   -373       S  
ATOM   4450  N   PRO B 107      77.004  92.605  60.642  1.00 22.20           N  
ANISOU 4450  N   PRO B 107     1347   2167   4919    -84    -79   -132       N  
ATOM   4451  CA  PRO B 107      75.790  91.938  61.120  1.00 21.78           C  
ANISOU 4451  CA  PRO B 107     1328   2018   4927    -90    -12   -134       C  
ATOM   4452  C   PRO B 107      74.797  92.927  61.735  1.00 21.58           C  
ANISOU 4452  C   PRO B 107     1337   1940   4919    -86    -78   -167       C  
ATOM   4453  O   PRO B 107      75.192  93.997  62.195  1.00 21.69           O  
ANISOU 4453  O   PRO B 107     1462   1818   4961   -106   -144   -132       O  
ATOM   4454  CB  PRO B 107      76.309  91.022  62.226  1.00 21.29           C  
ANISOU 4454  CB  PRO B 107     1232   1997   4859    -89    -44    -99       C  
ATOM   4455  CG  PRO B 107      77.764  90.801  61.913  1.00 21.92           C  
ANISOU 4455  CG  PRO B 107     1303   2104   4922   -193    -48   -212       C  
ATOM   4456  CD  PRO B 107      78.215  92.125  61.339  1.00 22.36           C  
ANISOU 4456  CD  PRO B 107     1411   2131   4953    -50    -94    -67       C  
ATOM   4457  N   ILE B 108      73.528  92.535  61.754  1.00 21.35           N  
ANISOU 4457  N   ILE B 108     1248   1976   4886    -15    -36   -230       N  
ATOM   4458  CA  ILE B 108      72.490  93.184  62.542  1.00 21.00           C  
ANISOU 4458  CA  ILE B 108     1176   1932   4868    -19    -29   -356       C  
ATOM   4459  C   ILE B 108      72.771  92.858  64.010  1.00 21.74           C  
ANISOU 4459  C   ILE B 108     1339   2007   4914     32     33   -318       C  
ATOM   4460  O   ILE B 108      73.195  91.742  64.326  1.00 21.44           O  
ANISOU 4460  O   ILE B 108     1292   1960   4892     37    116   -261       O  
ATOM   4461  CB  ILE B 108      71.099  92.644  62.142  1.00 21.10           C  
ANISOU 4461  CB  ILE B 108     1160   1942   4915    -19    -44   -400       C  
ATOM   4462  CG1 ILE B 108      70.884  92.754  60.625  1.00 19.46           C  
ANISOU 4462  CG1 ILE B 108      564   1856   4973   -108   -180   -499       C  
ATOM   4463  CG2 ILE B 108      70.000  93.386  62.894  1.00 20.02           C  
ANISOU 4463  CG2 ILE B 108      925   1898   4784   -185    -62   -634       C  
ATOM   4464  CD1 ILE B 108      69.727  91.886  60.111  1.00 22.43           C  
ANISOU 4464  CD1 ILE B 108     1534   1684   5305   -435   -569   -594       C  
ATOM   4465  N   SER B 109      72.551  93.827  64.897  1.00 21.45           N  
ANISOU 4465  N   SER B 109     1286   2023   4839     -9     70   -323       N  
ATOM   4466  CA  SER B 109      72.830  93.663  66.319  1.00 21.88           C  
ANISOU 4466  CA  SER B 109     1429   2080   4803    -21    199   -275       C  
ATOM   4467  C   SER B 109      71.535  93.331  67.035  1.00 22.53           C  
ANISOU 4467  C   SER B 109     1555   2113   4891     -2    234   -272       C  
ATOM   4468  O   SER B 109      70.463  93.727  66.573  1.00 22.75           O  
ANISOU 4468  O   SER B 109     1554   2176   4910    208    366   -264       O  
ATOM   4469  CB  SER B 109      73.435  94.951  66.882  1.00 21.58           C  
ANISOU 4469  CB  SER B 109     1308   2183   4708    -63    169   -214       C  
ATOM   4470  OG  SER B 109      74.714  95.182  66.309  1.00 20.87           O  
ANISOU 4470  OG  SER B 109     1132   2215   4582   -109    161   -232       O  
ATOM   4471  N   SER B 110      71.604  92.587  68.137  1.00 22.71           N  
ANISOU 4471  N   SER B 110     1662   2046   4919    -37    325   -269       N  
ATOM   4472  CA  SER B 110      70.372  92.250  68.849  1.00 23.36           C  
ANISOU 4472  CA  SER B 110     1754   2065   5054      7    451   -240       C  
ATOM   4473  C   SER B 110      69.652  93.522  69.292  1.00 23.62           C  
ANISOU 4473  C   SER B 110     1734   2075   5165    -10    407   -183       C  
ATOM   4474  O   SER B 110      70.285  94.520  69.644  1.00 22.71           O  
ANISOU 4474  O   SER B 110     1816   1895   4917    -10    476   -107       O  
ATOM   4475  CB  SER B 110      70.663  91.366  70.071  1.00 23.56           C  
ANISOU 4475  CB  SER B 110     1843   2062   5044    -28    473   -208       C  
ATOM   4476  OG  SER B 110      69.440  90.963  70.685  1.00 24.95           O  
ANISOU 4476  OG  SER B 110     1798   2439   5241    -74    475   -254       O  
ATOM   4477  N   GLY B 111      68.323  93.477  69.289  1.00 24.36           N  
ANISOU 4477  N   GLY B 111     1724   2164   5368     56    399   -200       N  
ATOM   4478  CA  GLY B 111      67.544  94.651  69.670  1.00 25.00           C  
ANISOU 4478  CA  GLY B 111     1694   2097   5707     25    379   -272       C  
ATOM   4479  C   GLY B 111      67.300  95.569  68.486  1.00 25.56           C  
ANISOU 4479  C   GLY B 111     1684   2122   5903    -34    358   -283       C  
ATOM   4480  O   GLY B 111      66.684  96.624  68.646  1.00 26.91           O  
ANISOU 4480  O   GLY B 111     2047   2217   5959    -88    217   -304       O  
ATOM   4481  N   HIS B 112      67.744  95.168  67.297  1.00 25.55           N  
ANISOU 4481  N   HIS B 112     1567   2098   6042   -145    363   -337       N  
ATOM   4482  CA  HIS B 112      67.610  96.006  66.107  1.00 25.59           C  
ANISOU 4482  CA  HIS B 112     1452   2078   6191    -83    367   -343       C  
ATOM   4483  C   HIS B 112      66.946  95.260  64.969  1.00 26.22           C  
ANISOU 4483  C   HIS B 112     1525   2206   6232     -5    311   -353       C  
ATOM   4484  O   HIS B 112      66.927  94.027  64.953  1.00 27.32           O  
ANISOU 4484  O   HIS B 112     1755   2262   6363    -67    286   -333       O  
ATOM   4485  CB  HIS B 112      68.984  96.483  65.626  1.00 25.01           C  
ANISOU 4485  CB  HIS B 112     1289   1937   6274    -56    304   -361       C  
ATOM   4486  CG  HIS B 112      69.709  97.309  66.633  1.00 25.48           C  
ANISOU 4486  CG  HIS B 112     1324   1887   6468   -168    527   -483       C  
ATOM   4487  ND1 HIS B 112      70.415  96.755  67.680  1.00 26.41           N  
ANISOU 4487  ND1 HIS B 112     1741   1704   6589   -267    355   -497       N  
ATOM   4488  CD2 HIS B 112      69.852  98.651  66.746  1.00 26.26           C  
ANISOU 4488  CD2 HIS B 112     1594   1744   6636   -278    491   -651       C  
ATOM   4489  CE1 HIS B 112      70.962  97.722  68.398  1.00 26.50           C  
ANISOU 4489  CE1 HIS B 112     1690   1703   6673   -218    366   -635       C  
ATOM   4490  NE2 HIS B 112      70.642  98.880  67.848  1.00 27.85           N  
ANISOU 4490  NE2 HIS B 112     1931   1811   6840   -414    240   -613       N  
ATOM   4491  N   SER B 113      66.406  96.020  64.020  1.00 26.65           N  
ANISOU 4491  N   SER B 113     1597   2300   6228     52    214   -354       N  
ATOM   4492  CA  SER B 113      65.805  95.462  62.812  1.00 26.73           C  
ANISOU 4492  CA  SER B 113     1587   2341   6225     52     65   -352       C  
ATOM   4493  C   SER B 113      66.591  95.994  61.621  1.00 26.43           C  
ANISOU 4493  C   SER B 113     1525   2315   6200     71     -5   -355       C  
ATOM   4494  O   SER B 113      67.244  97.035  61.727  1.00 27.30           O  
ANISOU 4494  O   SER B 113     1793   2391   6188     36    -68   -410       O  
ATOM   4495  CB  SER B 113      64.360  95.934  62.676  1.00 26.78           C  
ANISOU 4495  CB  SER B 113     1455   2489   6232   -100     84   -317       C  
ATOM   4496  OG  SER B 113      63.560  95.461  63.744  1.00 29.55           O  
ANISOU 4496  OG  SER B 113     2067   2914   6244     45      2   -249       O  
ATOM   4497  N   PHE B 114      66.509  95.288  60.500  1.00 25.35           N  
ANISOU 4497  N   PHE B 114     1356   2131   6145    189    -52   -413       N  
ATOM   4498  CA  PHE B 114      67.101  95.724  59.249  1.00 25.41           C  
ANISOU 4498  CA  PHE B 114     1526   2044   6085    282   -204   -297       C  
ATOM   4499  C   PHE B 114      66.303  95.133  58.097  1.00 25.73           C  
ANISOU 4499  C   PHE B 114     1655   2070   6048    351   -303   -264       C  
ATOM   4500  O   PHE B 114      66.105  93.910  58.031  1.00 26.31           O  
ANISOU 4500  O   PHE B 114     1819   2106   6070    402   -405   -199       O  
ATOM   4501  CB  PHE B 114      68.572  95.279  59.166  1.00 25.31           C  
ANISOU 4501  CB  PHE B 114     1480   2053   6081    339   -116   -313       C  
ATOM   4502  CG  PHE B 114      69.264  95.706  57.896  1.00 25.73           C  
ANISOU 4502  CG  PHE B 114     1425   2138   6211    267   -104   -247       C  
ATOM   4503  CD1 PHE B 114      69.483  97.061  57.623  1.00 25.71           C  
ANISOU 4503  CD1 PHE B 114     1459   2241   6067    122    -77   -212       C  
ATOM   4504  CD2 PHE B 114      69.659  94.752  56.959  1.00 25.84           C  
ANISOU 4504  CD2 PHE B 114     1396   2254   6165    206   -151   -146       C  
ATOM   4505  CE1 PHE B 114      70.111  97.462  56.453  1.00 24.92           C  
ANISOU 4505  CE1 PHE B 114     1409   1968   6091     79   -269    -36       C  
ATOM   4506  CE2 PHE B 114      70.287  95.138  55.777  1.00 26.72           C  
ANISOU 4506  CE2 PHE B 114     1455   2548   6146    253   -103   -159       C  
ATOM   4507  CZ  PHE B 114      70.515  96.505  55.527  1.00 26.34           C  
ANISOU 4507  CZ  PHE B 114     1449   2370   6189    156    -54   -183       C  
ATOM   4508  N   SER B 115      65.853  95.996  57.188  1.00 25.61           N  
ANISOU 4508  N   SER B 115     1753   2024   5952    462   -410   -275       N  
ATOM   4509  CA  SER B 115      64.998  95.560  56.083  1.00 25.77           C  
ANISOU 4509  CA  SER B 115     1788   2076   5924    405   -497   -240       C  
ATOM   4510  C   SER B 115      65.809  95.293  54.814  1.00 26.30           C  
ANISOU 4510  C   SER B 115     2054   2108   5829    349   -554   -197       C  
ATOM   4511  O   SER B 115      66.486  96.196  54.291  1.00 26.91           O  
ANISOU 4511  O   SER B 115     2243   2095   5883    452   -371   -220       O  
ATOM   4512  CB  SER B 115      63.905  96.594  55.797  1.00 26.29           C  
ANISOU 4512  CB  SER B 115     1844   2208   5936    338   -563   -248       C  
ATOM   4513  OG  SER B 115      62.895  96.013  54.990  1.00 28.08           O  
ANISOU 4513  OG  SER B 115     1912   2606   6151    551   -850   -286       O  
ATOM   4514  N   TYR B 116      65.787  94.037  54.374  1.00 25.46           N  
ANISOU 4514  N   TYR B 116     1981   1996   5695    291   -687    -87       N  
ATOM   4515  CA  TYR B 116      66.375  93.635  53.099  1.00 25.64           C  
ANISOU 4515  CA  TYR B 116     2147   2059   5536    267   -803     48       C  
ATOM   4516  C   TYR B 116      65.370  93.902  51.983  1.00 26.71           C  
ANISOU 4516  C   TYR B 116     2313   2220   5614    216   -918     61       C  
ATOM   4517  O   TYR B 116      64.326  93.249  51.902  1.00 26.97           O  
ANISOU 4517  O   TYR B 116     2323   2272   5651    224   -993     89       O  
ATOM   4518  CB  TYR B 116      66.768  92.154  53.115  1.00 24.64           C  
ANISOU 4518  CB  TYR B 116     2016   1945   5400    119   -724     43       C  
ATOM   4519  CG  TYR B 116      67.877  91.820  54.090  1.00 23.54           C  
ANISOU 4519  CG  TYR B 116     2086   1922   4934     12   -754     72       C  
ATOM   4520  CD1 TYR B 116      67.603  91.594  55.437  1.00 22.32           C  
ANISOU 4520  CD1 TYR B 116     1926   1951   4603   -183   -830   -161       C  
ATOM   4521  CD2 TYR B 116      69.203  91.718  53.667  1.00 21.50           C  
ANISOU 4521  CD2 TYR B 116     1845   1998   4323   -257   -837   -239       C  
ATOM   4522  CE1 TYR B 116      68.626  91.257  56.335  1.00 21.30           C  
ANISOU 4522  CE1 TYR B 116     1586   2005   4502   -342   -880    -46       C  
ATOM   4523  CE2 TYR B 116      70.231  91.378  54.553  1.00 21.81           C  
ANISOU 4523  CE2 TYR B 116     1949   1929   4406   -300   -775    -38       C  
ATOM   4524  CZ  TYR B 116      69.936  91.158  55.889  1.00 22.58           C  
ANISOU 4524  CZ  TYR B 116     1818   2393   4366   -226   -974    -26       C  
ATOM   4525  OH  TYR B 116      70.939  90.820  56.778  1.00 21.68           O  
ANISOU 4525  OH  TYR B 116     1786   2356   4093   -297   -899    -97       O  
ATOM   4526  N   ASN B 117      65.671  94.890  51.146  1.00 27.02           N  
ANISOU 4526  N   ASN B 117     2441   2252   5574    269  -1052    184       N  
ATOM   4527  CA  ASN B 117      64.747  95.306  50.100  1.00 28.76           C  
ANISOU 4527  CA  ASN B 117     2855   2431   5641    264  -1086    214       C  
ATOM   4528  C   ASN B 117      65.378  95.019  48.751  1.00 29.34           C  
ANISOU 4528  C   ASN B 117     2975   2517   5653    292  -1184    272       C  
ATOM   4529  O   ASN B 117      66.341  95.675  48.364  1.00 29.99           O  
ANISOU 4529  O   ASN B 117     3076   2629   5686    208  -1191    267       O  
ATOM   4530  CB  ASN B 117      64.409  96.791  50.236  1.00 28.63           C  
ANISOU 4530  CB  ASN B 117     2900   2376   5599    239  -1028    178       C  
ATOM   4531  CG  ASN B 117      63.928  97.154  51.628  1.00 29.05           C  
ANISOU 4531  CG  ASN B 117     3027   2361   5649    246   -863    222       C  
ATOM   4532  OD1 ASN B 117      63.355  96.321  52.328  1.00 29.60           O  
ANISOU 4532  OD1 ASN B 117     2923   2390   5933    250   -673    123       O  
ATOM   4533  ND2 ASN B 117      64.163  98.401  52.039  1.00 29.20           N  
ANISOU 4533  ND2 ASN B 117     3482   2453   5158    -25   -685    102       N  
ATOM   4534  N   PHE B 118      64.844  94.025  48.053  1.00 29.91           N  
ANISOU 4534  N   PHE B 118     3103   2547   5712    380  -1376    347       N  
ATOM   4535  CA  PHE B 118      65.447  93.578  46.805  1.00 30.81           C  
ANISOU 4535  CA  PHE B 118     3300   2678   5726    357  -1491    440       C  
ATOM   4536  C   PHE B 118      64.371  93.062  45.869  1.00 32.15           C  
ANISOU 4536  C   PHE B 118     3553   2844   5817    340  -1618    461       C  
ATOM   4537  O   PHE B 118      63.229  92.884  46.293  1.00 32.26           O  
ANISOU 4537  O   PHE B 118     3526   2896   5834    332  -1638    485       O  
ATOM   4538  CB  PHE B 118      66.535  92.530  47.068  1.00 30.13           C  
ANISOU 4538  CB  PHE B 118     3199   2573   5674    363  -1499    455       C  
ATOM   4539  CG  PHE B 118      66.061  91.309  47.811  1.00 30.31           C  
ANISOU 4539  CG  PHE B 118     3308   2531   5676    509  -1499    512       C  
ATOM   4540  CD1 PHE B 118      66.069  91.273  49.204  1.00 30.51           C  
ANISOU 4540  CD1 PHE B 118     3474   2438   5678    454  -1484    426       C  
ATOM   4541  CD2 PHE B 118      65.640  90.178  47.114  1.00 29.40           C  
ANISOU 4541  CD2 PHE B 118     3150   2378   5639    674  -1410    478       C  
ATOM   4542  CE1 PHE B 118      65.644  90.132  49.893  1.00 30.43           C  
ANISOU 4542  CE1 PHE B 118     3594   2481   5487    453  -1473    492       C  
ATOM   4543  CE2 PHE B 118      65.213  89.028  47.791  1.00 30.30           C  
ANISOU 4543  CE2 PHE B 118     3484   2363   5663    691  -1437    494       C  
ATOM   4544  CZ  PHE B 118      65.214  89.007  49.182  1.00 30.29           C  
ANISOU 4544  CZ  PHE B 118     3626   2260   5621    771  -1431    521       C  
ATOM   4545  N   GLN B 119      64.728  92.846  44.606  1.00 33.54           N  
ANISOU 4545  N   GLN B 119     3809   3080   5853    343  -1691    522       N  
ATOM   4546  CA  GLN B 119      63.751  92.398  43.613  1.00 35.34           C  
ANISOU 4546  CA  GLN B 119     4144   3300   5984    339  -1840    574       C  
ATOM   4547  C   GLN B 119      64.102  91.011  43.073  1.00 36.08           C  
ANISOU 4547  C   GLN B 119     4280   3387   6039    410  -1877    588       C  
ATOM   4548  O   GLN B 119      65.276  90.667  42.943  1.00 36.48           O  
ANISOU 4548  O   GLN B 119     4280   3483   6097    417  -1854    570       O  
ATOM   4549  CB  GLN B 119      63.650  93.404  42.461  1.00 35.62           C  
ANISOU 4549  CB  GLN B 119     4142   3416   5975    376  -1884    561       C  
ATOM   4550  CG  GLN B 119      62.396  93.238  41.611  1.00 37.29           C  
ANISOU 4550  CG  GLN B 119     4376   3702   6090    158  -2004    719       C  
ATOM   4551  CD  GLN B 119      62.416  94.049  40.327  1.00 39.93           C  
ANISOU 4551  CD  GLN B 119     4651   4249   6268     82  -2186    904       C  
ATOM   4552  OE1 GLN B 119      63.431  94.645  39.955  1.00 40.58           O  
ANISOU 4552  OE1 GLN B 119     5091   4044   6283    -66  -2126   1045       O  
ATOM   4553  NE2 GLN B 119      61.288  94.054  39.627  1.00 40.63           N  
ANISOU 4553  NE2 GLN B 119     4589   4574   6273    192  -2228   1187       N  
ATOM   4554  N   ALA B 120      63.089  90.207  42.770  1.00 36.80           N  
ANISOU 4554  N   ALA B 120     4474   3420   6088    400  -1955    655       N  
ATOM   4555  CA  ALA B 120      63.322  88.973  42.028  1.00 37.98           C  
ANISOU 4555  CA  ALA B 120     4701   3579   6147    393  -2021    679       C  
ATOM   4556  C   ALA B 120      63.284  89.313  40.542  1.00 38.86           C  
ANISOU 4556  C   ALA B 120     4903   3678   6182    405  -2068    724       C  
ATOM   4557  O   ALA B 120      62.336  88.951  39.834  1.00 39.50           O  
ANISOU 4557  O   ALA B 120     4957   3807   6242    329  -2066    655       O  
ATOM   4558  CB  ALA B 120      62.289  87.913  42.388  1.00 37.68           C  
ANISOU 4558  CB  ALA B 120     4663   3506   6147    424  -2030    719       C  
ATOM   4559  N   LYS B 121      64.315  90.024  40.090  1.00 39.41           N  
ANISOU 4559  N   LYS B 121     5033   3748   6192    378  -2100    791       N  
ATOM   4560  CA  LYS B 121      64.388  90.547  38.728  1.00 40.65           C  
ANISOU 4560  CA  LYS B 121     5299   3875   6271    382  -2108    877       C  
ATOM   4561  C   LYS B 121      64.748  89.445  37.739  1.00 40.53           C  
ANISOU 4561  C   LYS B 121     5338   3819   6239    360  -2118    902       C  
ATOM   4562  O   LYS B 121      65.851  88.892  37.772  1.00 40.21           O  
ANISOU 4562  O   LYS B 121     5376   3692   6209    330  -2138    861       O  
ATOM   4563  CB  LYS B 121      65.386  91.706  38.647  1.00 41.10           C  
ANISOU 4563  CB  LYS B 121     5359   3950   6307    385  -2108    854       C  
ATOM   4564  CG  LYS B 121      64.965  92.852  37.745  1.00 44.25           C  
ANISOU 4564  CG  LYS B 121     5905   4411   6495    367  -1991   1010       C  
ATOM   4565  CD  LYS B 121      65.609  92.756  36.376  1.00 48.96           C  
ANISOU 4565  CD  LYS B 121     6526   5294   6781    425  -1806   1035       C  
ATOM   4566  CE  LYS B 121      65.403  94.030  35.557  1.00 50.53           C  
ANISOU 4566  CE  LYS B 121     6731   5515   6951    548  -1920   1277       C  
ATOM   4567  NZ  LYS B 121      64.031  94.134  34.960  1.00 52.23           N  
ANISOU 4567  NZ  LYS B 121     6807   5993   7042    408  -1973   1297       N  
ATOM   4568  N   ASP B 122      63.793  89.125  36.872  1.00 40.98           N  
ANISOU 4568  N   ASP B 122     5460   3864   6247    371  -2117    939       N  
ATOM   4569  CA  ASP B 122      63.940  88.066  35.879  1.00 41.29           C  
ANISOU 4569  CA  ASP B 122     5493   3942   6252    389  -2098    947       C  
ATOM   4570  C   ASP B 122      64.301  86.738  36.543  1.00 40.24           C  
ANISOU 4570  C   ASP B 122     5344   3835   6111    350  -2138    909       C  
ATOM   4571  O   ASP B 122      65.033  85.928  35.970  1.00 40.60           O  
ANISOU 4571  O   ASP B 122     5524   3862   6039    381  -2124    937       O  
ATOM   4572  CB  ASP B 122      65.004  88.444  34.840  1.00 42.71           C  
ANISOU 4572  CB  ASP B 122     5678   4138   6409    349  -2018    982       C  
ATOM   4573  CG  ASP B 122      64.680  89.732  34.101  1.00 45.39           C  
ANISOU 4573  CG  ASP B 122     6018   4565   6661    372  -1989   1025       C  
ATOM   4574  OD1 ASP B 122      63.495  89.965  33.774  1.00 48.00           O  
ANISOU 4574  OD1 ASP B 122     6038   5344   6855    362  -1995    967       O  
ATOM   4575  OD2 ASP B 122      65.619  90.519  33.839  1.00 49.77           O  
ANISOU 4575  OD2 ASP B 122     6631   5156   7123     26  -1667    881       O  
ATOM   4576  N   GLN B 123      63.825  86.527  37.767  1.00 38.59           N  
ANISOU 4576  N   GLN B 123     5010   3658   5993    318  -2205    816       N  
ATOM   4577  CA  GLN B 123      64.096  85.275  38.472  1.00 37.12           C  
ANISOU 4577  CA  GLN B 123     4772   3470   5859    276  -2254    733       C  
ATOM   4578  C   GLN B 123      62.821  84.654  39.024  1.00 35.92           C  
ANISOU 4578  C   GLN B 123     4573   3317   5754    292  -2289    713       C  
ATOM   4579  O   GLN B 123      61.958  85.359  39.545  1.00 35.90           O  
ANISOU 4579  O   GLN B 123     4611   3191   5835    256  -2253    666       O  
ATOM   4580  CB  GLN B 123      65.085  85.467  39.623  1.00 36.83           C  
ANISOU 4580  CB  GLN B 123     4704   3450   5837    250  -2271    683       C  
ATOM   4581  CG  GLN B 123      66.511  85.796  39.212  1.00 37.17           C  
ANISOU 4581  CG  GLN B 123     4783   3461   5877    194  -2339    568       C  
ATOM   4582  CD  GLN B 123      67.473  85.637  40.365  1.00 36.83           C  
ANISOU 4582  CD  GLN B 123     4597   3379   6016    -14  -2362    421       C  
ATOM   4583  OE1 GLN B 123      67.800  86.608  41.052  1.00 37.06           O  
ANISOU 4583  OE1 GLN B 123     4854   3280   5947      0  -2289    352       O  
ATOM   4584  NE2 GLN B 123      67.920  84.404  40.598  1.00 34.68           N  
ANISOU 4584  NE2 GLN B 123     4242   3057   5875   -334  -2492    409       N  
ATOM   4585  N   ALA B 124      62.724  83.332  38.909  1.00 34.32           N  
ANISOU 4585  N   ALA B 124     4278   3214   5544    338  -2350    699       N  
ATOM   4586  CA  ALA B 124      61.657  82.563  39.540  1.00 32.78           C  
ANISOU 4586  CA  ALA B 124     4054   3048   5353    384  -2337    710       C  
ATOM   4587  C   ALA B 124      62.162  81.147  39.732  1.00 32.08           C  
ANISOU 4587  C   ALA B 124     3929   3032   5227    409  -2256    692       C  
ATOM   4588  O   ALA B 124      62.954  80.650  38.926  1.00 33.11           O  
ANISOU 4588  O   ALA B 124     4082   3102   5394    425  -2162    763       O  
ATOM   4589  CB  ALA B 124      60.392  82.547  38.672  1.00 32.07           C  
ANISOU 4589  CB  ALA B 124     3923   3046   5214    447  -2489    770       C  
ATOM   4590  N   GLY B 125      61.671  80.494  40.778  1.00 30.46           N  
ANISOU 4590  N   GLY B 125     3711   2849   5011    352  -2193    586       N  
ATOM   4591  CA  GLY B 125      62.081  79.132  41.077  1.00 28.58           C  
ANISOU 4591  CA  GLY B 125     3341   2779   4739    348  -2102    531       C  
ATOM   4592  C   GLY B 125      62.198  78.949  42.575  1.00 27.99           C  
ANISOU 4592  C   GLY B 125     3186   2686   4761    266  -1911    494       C  
ATOM   4593  O   GLY B 125      61.560  79.666  43.350  1.00 27.65           O  
ANISOU 4593  O   GLY B 125     3184   2687   4635    244  -1919    429       O  
ATOM   4594  N   THR B 126      63.037  77.991  42.956  1.00 26.76           N  
ANISOU 4594  N   THR B 126     2907   2610   4649    224  -1830    485       N  
ATOM   4595  CA  THR B 126      63.174  77.540  44.331  1.00 25.54           C  
ANISOU 4595  CA  THR B 126     2732   2456   4514    115  -1640    423       C  
ATOM   4596  C   THR B 126      64.497  78.023  44.921  1.00 25.00           C  
ANISOU 4596  C   THR B 126     2637   2376   4483    146  -1473    343       C  
ATOM   4597  O   THR B 126      65.568  77.724  44.384  1.00 24.96           O  
ANISOU 4597  O   THR B 126     2608   2323   4552     57  -1379    408       O  
ATOM   4598  CB  THR B 126      63.087  75.992  44.381  1.00 25.71           C  
ANISOU 4598  CB  THR B 126     2822   2427   4518     93  -1701    406       C  
ATOM   4599  OG1 THR B 126      61.944  75.555  43.626  1.00 25.88           O  
ANISOU 4599  OG1 THR B 126     2677   2490   4663     38  -1612    456       O  
ATOM   4600  CG2 THR B 126      62.962  75.506  45.808  1.00 24.57           C  
ANISOU 4600  CG2 THR B 126     2726   2130   4477      8  -1686    439       C  
ATOM   4601  N   PHE B 127      64.404  78.761  46.027  1.00 23.69           N  
ANISOU 4601  N   PHE B 127     2383   2375   4241    214  -1370    262       N  
ATOM   4602  CA  PHE B 127      65.551  79.391  46.663  1.00 22.87           C  
ANISOU 4602  CA  PHE B 127     2292   2263   4131    258  -1188    190       C  
ATOM   4603  C   PHE B 127      65.491  79.015  48.135  1.00 22.43           C  
ANISOU 4603  C   PHE B 127     2108   2294   4117    260  -1177    114       C  
ATOM   4604  O   PHE B 127      64.695  78.153  48.526  1.00 22.59           O  
ANISOU 4604  O   PHE B 127     2094   2295   4192    227  -1110    -22       O  
ATOM   4605  CB  PHE B 127      65.462  80.913  46.506  1.00 22.41           C  
ANISOU 4605  CB  PHE B 127     2277   2291   3944    342  -1189    307       C  
ATOM   4606  CG  PHE B 127      65.389  81.375  45.082  1.00 23.83           C  
ANISOU 4606  CG  PHE B 127     2585   2569   3898    347  -1190    234       C  
ATOM   4607  CD1 PHE B 127      64.161  81.516  44.453  1.00 23.50           C  
ANISOU 4607  CD1 PHE B 127     2814   2513   3601    432  -1303    225       C  
ATOM   4608  CD2 PHE B 127      66.548  81.714  44.384  1.00 24.21           C  
ANISOU 4608  CD2 PHE B 127     2961   2779   3457    204  -1184    373       C  
ATOM   4609  CE1 PHE B 127      64.078  81.973  43.142  1.00 24.01           C  
ANISOU 4609  CE1 PHE B 127     2799   2796   3524    333  -1164    184       C  
ATOM   4610  CE2 PHE B 127      66.465  82.170  43.063  1.00 24.86           C  
ANISOU 4610  CE2 PHE B 127     2859   3071   3515    167  -1124    440       C  
ATOM   4611  CZ  PHE B 127      65.224  82.298  42.448  1.00 24.14           C  
ANISOU 4611  CZ  PHE B 127     2909   2747   3514    242  -1174    172       C  
ATOM   4612  N   TRP B 128      66.362  79.610  48.945  1.00 21.81           N  
ANISOU 4612  N   TRP B 128     1903   2192   4192    213  -1043     42       N  
ATOM   4613  CA  TRP B 128      66.264  79.464  50.399  1.00 21.45           C  
ANISOU 4613  CA  TRP B 128     1891   2153   4106    199  -1015     64       C  
ATOM   4614  C   TRP B 128      66.961  80.640  51.057  1.00 21.43           C  
ANISOU 4614  C   TRP B 128     1719   2226   4198    112   -919     52       C  
ATOM   4615  O   TRP B 128      67.546  81.480  50.375  1.00 22.82           O  
ANISOU 4615  O   TRP B 128     1968   2412   4287    136   -848    101       O  
ATOM   4616  CB  TRP B 128      66.816  78.123  50.933  1.00 20.97           C  
ANISOU 4616  CB  TRP B 128     1632   2154   4180    186  -1030     26       C  
ATOM   4617  CG  TRP B 128      68.274  77.806  50.716  1.00 20.64           C  
ANISOU 4617  CG  TRP B 128     1872   2164   3805    222   -815     19       C  
ATOM   4618  CD1 TRP B 128      68.924  77.699  49.517  1.00 19.89           C  
ANISOU 4618  CD1 TRP B 128     1524   2250   3784   -139   -754     -4       C  
ATOM   4619  CD2 TRP B 128      69.234  77.452  51.724  1.00 19.03           C  
ANISOU 4619  CD2 TRP B 128     1630   2085   3514   -115   -883   -109       C  
ATOM   4620  NE1 TRP B 128      70.233  77.315  49.719  1.00 19.70           N  
ANISOU 4620  NE1 TRP B 128     1819   2304   3362    365  -1099    152       N  
ATOM   4621  CE2 TRP B 128      70.450  77.162  51.064  1.00 19.27           C  
ANISOU 4621  CE2 TRP B 128     1746   2270   3304    -51   -881    -62       C  
ATOM   4622  CE3 TRP B 128      69.183  77.347  53.122  1.00 17.93           C  
ANISOU 4622  CE3 TRP B 128     1523   1782   3505   -405   -743    -98       C  
ATOM   4623  CZ2 TRP B 128      71.610  76.781  51.752  1.00 19.62           C  
ANISOU 4623  CZ2 TRP B 128     1993   2051   3408     19   -826    -36       C  
ATOM   4624  CZ3 TRP B 128      70.334  76.958  53.810  1.00 18.72           C  
ANISOU 4624  CZ3 TRP B 128     1823   1916   3374    -69   -790     36       C  
ATOM   4625  CH2 TRP B 128      71.544  76.689  53.121  1.00 17.89           C  
ANISOU 4625  CH2 TRP B 128     1668   1961   3168   -104   -862    157       C  
ATOM   4626  N   TYR B 129      66.861  80.724  52.376  1.00 20.91           N  
ANISOU 4626  N   TYR B 129     1619   2196   4127     36   -896    -10       N  
ATOM   4627  CA  TYR B 129      67.484  81.828  53.097  1.00 20.91           C  
ANISOU 4627  CA  TYR B 129     1502   2282   4161     68   -790     13       C  
ATOM   4628  C   TYR B 129      68.125  81.233  54.338  1.00 20.58           C  
ANISOU 4628  C   TYR B 129     1463   2323   4031     14   -733    -24       C  
ATOM   4629  O   TYR B 129      67.644  80.233  54.881  1.00 20.64           O  
ANISOU 4629  O   TYR B 129     1401   2325   4116    -11   -806     20       O  
ATOM   4630  CB  TYR B 129      66.464  82.925  53.445  1.00 20.68           C  
ANISOU 4630  CB  TYR B 129     1468   2254   4133     57   -718     64       C  
ATOM   4631  CG  TYR B 129      65.379  82.485  54.401  1.00 20.79           C  
ANISOU 4631  CG  TYR B 129     1212   2357   4329    136   -667    -29       C  
ATOM   4632  CD1 TYR B 129      64.237  81.839  53.931  1.00 19.28           C  
ANISOU 4632  CD1 TYR B 129      939   1837   4547    206   -666    110       C  
ATOM   4633  CD2 TYR B 129      65.500  82.707  55.772  1.00 20.43           C  
ANISOU 4633  CD2 TYR B 129     1388   2052   4320    229   -342    -18       C  
ATOM   4634  CE1 TYR B 129      63.229  81.447  54.804  1.00 21.36           C  
ANISOU 4634  CE1 TYR B 129     1531   2181   4403    146   -443     77       C  
ATOM   4635  CE2 TYR B 129      64.499  82.311  56.652  1.00 21.61           C  
ANISOU 4635  CE2 TYR B 129     1450   2414   4347     61   -416     28       C  
ATOM   4636  CZ  TYR B 129      63.370  81.679  56.159  1.00 21.86           C  
ANISOU 4636  CZ  TYR B 129     1555   2256   4494     -1   -294    -30       C  
ATOM   4637  OH  TYR B 129      62.375  81.286  57.022  1.00 22.67           O  
ANISOU 4637  OH  TYR B 129     1686   2252   4672    234     81   -100       O  
ATOM   4638  N   HIS B 130      69.233  81.832  54.757  1.00 20.50           N  
ANISOU 4638  N   HIS B 130     1415   2360   4011     83   -640    -52       N  
ATOM   4639  CA  HIS B 130      69.982  81.301  55.886  1.00 19.18           C  
ANISOU 4639  CA  HIS B 130     1422   2174   3691     74   -552     23       C  
ATOM   4640  C   HIS B 130      70.884  82.366  56.490  1.00 18.63           C  
ANISOU 4640  C   HIS B 130     1181   2111   3786     71   -445     29       C  
ATOM   4641  O   HIS B 130      71.307  83.285  55.796  1.00 18.98           O  
ANISOU 4641  O   HIS B 130     1344   2060   3807    235   -366    -22       O  
ATOM   4642  CB  HIS B 130      70.803  80.051  55.505  1.00 18.51           C  
ANISOU 4642  CB  HIS B 130     1351   2046   3633     31   -383     81       C  
ATOM   4643  CG  HIS B 130      71.774  80.240  54.376  1.00 17.60           C  
ANISOU 4643  CG  HIS B 130     1554   2160   2973      0   -497    203       C  
ATOM   4644  ND1 HIS B 130      73.078  80.649  54.575  1.00 15.63           N  
ANISOU 4644  ND1 HIS B 130     1470   1859   2610     71   -144    576       N  
ATOM   4645  CD2 HIS B 130      71.651  80.007  53.044  1.00 16.31           C  
ANISOU 4645  CD2 HIS B 130     1783   1877   2537   -100    -61    674       C  
ATOM   4646  CE1 HIS B 130      73.704  80.693  53.412  1.00 17.01           C  
ANISOU 4646  CE1 HIS B 130     1698   2112   2651    -11    -90    590       C  
ATOM   4647  NE2 HIS B 130      72.869  80.285  52.468  1.00 18.87           N  
ANISOU 4647  NE2 HIS B 130     1462   2629   3078    -55   -255    433       N  
ATOM   4648  N   SER B 131      71.157  82.256  57.785  1.00 17.76           N  
ANISOU 4648  N   SER B 131     1029   2073   3644     32   -551    -27       N  
ATOM   4649  CA  SER B 131      72.196  83.096  58.369  1.00 19.19           C  
ANISOU 4649  CA  SER B 131     1061   2301   3927    -42   -482     33       C  
ATOM   4650  C   SER B 131      73.485  82.937  57.569  1.00 19.46           C  
ANISOU 4650  C   SER B 131     1155   2285   3951     -2   -353     22       C  
ATOM   4651  O   SER B 131      73.844  81.820  57.179  1.00 20.76           O  
ANISOU 4651  O   SER B 131     1461   2233   4191    -37   -268     67       O  
ATOM   4652  CB  SER B 131      72.467  82.751  59.834  1.00 18.36           C  
ANISOU 4652  CB  SER B 131      940   2314   3721   -146   -637    -69       C  
ATOM   4653  OG  SER B 131      73.502  83.613  60.330  1.00 19.85           O  
ANISOU 4653  OG  SER B 131      873   2318   4350   -251   -801    105       O  
ATOM   4654  N   HIS B 132      74.183  84.045  57.335  1.00 19.53           N  
ANISOU 4654  N   HIS B 132     1122   2325   3972     44   -255    123       N  
ATOM   4655  CA  HIS B 132      75.491  83.962  56.700  1.00 20.50           C  
ANISOU 4655  CA  HIS B 132     1443   2460   3886   -120   -123    128       C  
ATOM   4656  C   HIS B 132      76.497  84.607  57.647  1.00 20.33           C  
ANISOU 4656  C   HIS B 132     1319   2517   3887    -63   -130    154       C  
ATOM   4657  O   HIS B 132      77.420  85.311  57.219  1.00 21.33           O  
ANISOU 4657  O   HIS B 132     1584   2574   3944   -209   -181    173       O  
ATOM   4658  CB  HIS B 132      75.455  84.640  55.330  1.00 20.84           C  
ANISOU 4658  CB  HIS B 132     1526   2553   3836    -54    -76    164       C  
ATOM   4659  CG  HIS B 132      76.415  84.057  54.337  1.00 22.54           C  
ANISOU 4659  CG  HIS B 132     1937   2696   3931     43     22    123       C  
ATOM   4660  ND1 HIS B 132      77.778  84.022  54.540  1.00 22.74           N  
ANISOU 4660  ND1 HIS B 132     2008   3112   3520     63   -208    315       N  
ATOM   4661  CD2 HIS B 132      76.204  83.514  53.113  1.00 21.94           C  
ANISOU 4661  CD2 HIS B 132     2079   2707   3548   -277    -83    436       C  
ATOM   4662  CE1 HIS B 132      78.360  83.450  53.498  1.00 23.84           C  
ANISOU 4662  CE1 HIS B 132     2255   2903   3898    189   -149    345       C  
ATOM   4663  NE2 HIS B 132      77.427  83.130  52.617  1.00 24.15           N  
ANISOU 4663  NE2 HIS B 132     2189   3010   3974    235   -201    394       N  
ATOM   4664  N   LEU B 133      76.288  84.376  58.941  1.00 20.03           N  
ANISOU 4664  N   LEU B 133     1310   2418   3881    -13   -101    160       N  
ATOM   4665  CA  LEU B 133      77.208  84.811  59.993  1.00 19.48           C  
ANISOU 4665  CA  LEU B 133     1320   2239   3842    -26    -56     75       C  
ATOM   4666  C   LEU B 133      77.801  83.577  60.673  1.00 20.09           C  
ANISOU 4666  C   LEU B 133     1314   2319   3997      8   -142    105       C  
ATOM   4667  O   LEU B 133      77.089  82.836  61.366  1.00 19.75           O  
ANISOU 4667  O   LEU B 133     1139   2409   3955     79    -92    128       O  
ATOM   4668  CB  LEU B 133      76.502  85.702  61.027  1.00 19.52           C  
ANISOU 4668  CB  LEU B 133     1349   2336   3728    -77     15    112       C  
ATOM   4669  CG  LEU B 133      77.367  86.102  62.230  1.00 18.53           C  
ANISOU 4669  CG  LEU B 133     1396   2194   3450   -305    396   -140       C  
ATOM   4670  CD1 LEU B 133      78.537  87.017  61.810  1.00 20.15           C  
ANISOU 4670  CD1 LEU B 133     1943   2551   3162   -394    519    147       C  
ATOM   4671  CD2 LEU B 133      76.525  86.781  63.309  1.00 19.35           C  
ANISOU 4671  CD2 LEU B 133     1771   2503   3077   -296    421    -89       C  
ATOM   4672  N   SER B 134      79.089  83.337  60.436  1.00 20.16           N  
ANISOU 4672  N   SER B 134     1326   2196   4138     86   -154    104       N  
ATOM   4673  CA  SER B 134      79.769  82.170  61.000  1.00 21.30           C  
ANISOU 4673  CA  SER B 134     1407   2234   4450     74   -252     61       C  
ATOM   4674  C   SER B 134      78.957  80.907  60.700  1.00 21.02           C  
ANISOU 4674  C   SER B 134     1293   2221   4473     75   -222     17       C  
ATOM   4675  O   SER B 134      78.456  80.742  59.583  1.00 22.08           O  
ANISOU 4675  O   SER B 134     1561   2258   4568    131   -166     -7       O  
ATOM   4676  CB  SER B 134      79.974  82.343  62.511  1.00 21.27           C  
ANISOU 4676  CB  SER B 134     1502   2210   4368    172   -227     62       C  
ATOM   4677  OG  SER B 134      80.916  81.412  63.030  1.00 22.39           O  
ANISOU 4677  OG  SER B 134     1297   2338   4871   -145   -518    150       O  
ATOM   4678  N   THR B 135      78.798  80.035  61.693  1.00 20.27           N  
ANISOU 4678  N   THR B 135     1069   2206   4426     55   -159    -22       N  
ATOM   4679  CA  THR B 135      78.041  78.794  61.483  1.00 19.63           C  
ANISOU 4679  CA  THR B 135      953   2203   4301     25   -226   -119       C  
ATOM   4680  C   THR B 135      76.631  78.855  62.060  1.00 18.84           C  
ANISOU 4680  C   THR B 135      973   2154   4028      4   -295   -158       C  
ATOM   4681  O   THR B 135      76.026  77.821  62.395  1.00 19.56           O  
ANISOU 4681  O   THR B 135      766   2387   4277    -64   -357   -256       O  
ATOM   4682  CB  THR B 135      78.768  77.598  62.101  1.00 19.69           C  
ANISOU 4682  CB  THR B 135     1014   2161   4305     -3   -219    -85       C  
ATOM   4683  OG1 THR B 135      79.173  77.933  63.433  1.00 21.56           O  
ANISOU 4683  OG1 THR B 135     1179   2453   4558     44   -195   -104       O  
ATOM   4684  CG2 THR B 135      80.002  77.267  61.272  1.00 21.40           C  
ANISOU 4684  CG2 THR B 135     1014   2347   4768    147   -150   -124       C  
ATOM   4685  N   GLN B 136      76.107  80.067  62.167  1.00 17.52           N  
ANISOU 4685  N   GLN B 136      859   2052   3745     57   -357   -179       N  
ATOM   4686  CA  GLN B 136      74.846  80.263  62.868  1.00 17.24           C  
ANISOU 4686  CA  GLN B 136     1017   1913   3620     64   -262   -227       C  
ATOM   4687  C   GLN B 136      73.692  79.562  62.150  1.00 16.96           C  
ANISOU 4687  C   GLN B 136     1023   1880   3541     63   -238   -195       C  
ATOM   4688  O   GLN B 136      72.757  79.113  62.805  1.00 17.25           O  
ANISOU 4688  O   GLN B 136     1155   1899   3498     61   -263   -225       O  
ATOM   4689  CB  GLN B 136      74.570  81.753  63.091  1.00 17.56           C  
ANISOU 4689  CB  GLN B 136     1018   1938   3715    134   -214   -209       C  
ATOM   4690  CG  GLN B 136      73.232  82.079  63.748  1.00 16.85           C  
ANISOU 4690  CG  GLN B 136     1210   1795   3395    -49   -192   -264       C  
ATOM   4691  CD  GLN B 136      73.026  83.576  63.855  1.00 18.19           C  
ANISOU 4691  CD  GLN B 136     1353   2049   3507    325   -271   -412       C  
ATOM   4692  OE1 GLN B 136      72.826  84.250  62.840  1.00 20.72           O  
ANISOU 4692  OE1 GLN B 136     1808   2172   3890   -154     31   -206       O  
ATOM   4693  NE2 GLN B 136      73.091  84.107  65.079  1.00 17.83           N  
ANISOU 4693  NE2 GLN B 136     1186   2027   3559     32    -74   -743       N  
ATOM   4694  N   TYR B 137      73.744  79.396  60.832  1.00 16.92           N  
ANISOU 4694  N   TYR B 137     1158   1788   3482     50   -140   -205       N  
ATOM   4695  CA  TYR B 137      72.593  78.732  60.206  1.00 17.80           C  
ANISOU 4695  CA  TYR B 137     1300   1980   3481    149    -97   -220       C  
ATOM   4696  C   TYR B 137      72.427  77.272  60.657  1.00 18.06           C  
ANISOU 4696  C   TYR B 137     1332   1989   3538    187    -65   -299       C  
ATOM   4697  O   TYR B 137      71.305  76.759  60.723  1.00 17.50           O  
ANISOU 4697  O   TYR B 137     1166   1964   3518    281   -115   -361       O  
ATOM   4698  CB  TYR B 137      72.503  78.973  58.690  1.00 18.31           C  
ANISOU 4698  CB  TYR B 137     1440   2001   3514    154    -70   -158       C  
ATOM   4699  CG  TYR B 137      73.168  77.996  57.728  1.00 18.76           C  
ANISOU 4699  CG  TYR B 137     1311   2028   3787    120    143   -107       C  
ATOM   4700  CD1 TYR B 137      72.625  76.725  57.475  1.00 19.83           C  
ANISOU 4700  CD1 TYR B 137     1380   1999   4156    191    153   -182       C  
ATOM   4701  CD2 TYR B 137      74.271  78.396  56.977  1.00 20.25           C  
ANISOU 4701  CD2 TYR B 137     1381   2021   4292     77     18     88       C  
ATOM   4702  CE1 TYR B 137      73.199  75.861  56.547  1.00 19.63           C  
ANISOU 4702  CE1 TYR B 137     1265   1593   4597     14    125    -79       C  
ATOM   4703  CE2 TYR B 137      74.849  77.547  56.047  1.00 20.88           C  
ANISOU 4703  CE2 TYR B 137     1443   1919   4568    298    -51    -29       C  
ATOM   4704  CZ  TYR B 137      74.315  76.279  55.841  1.00 20.26           C  
ANISOU 4704  CZ  TYR B 137     1308   1839   4549    329    103     14       C  
ATOM   4705  OH  TYR B 137      74.897  75.460  54.907  1.00 21.01           O  
ANISOU 4705  OH  TYR B 137     1570   2025   4386    339     44   -145       O  
ATOM   4706  N   CYS B 138      73.528  76.639  61.061  1.00 18.41           N  
ANISOU 4706  N   CYS B 138     1255   2020   3719    249     -9   -250       N  
ATOM   4707  CA  CYS B 138      73.465  75.264  61.575  1.00 19.55           C  
ANISOU 4707  CA  CYS B 138     1341   2208   3878    206     39    -82       C  
ATOM   4708  C   CYS B 138      72.634  75.197  62.851  1.00 19.10           C  
ANISOU 4708  C   CYS B 138     1194   2119   3944    125     -3    -85       C  
ATOM   4709  O   CYS B 138      71.987  74.187  63.099  1.00 19.93           O  
ANISOU 4709  O   CYS B 138     1682   1923   3967    177     34     12       O  
ATOM   4710  CB  CYS B 138      74.861  74.700  61.859  1.00 20.02           C  
ANISOU 4710  CB  CYS B 138     1288   2287   4030    197     40    -61       C  
ATOM   4711  SG  CYS B 138      76.027  74.913  60.496  1.00 24.52           S  
ANISOU 4711  SG  CYS B 138     1727   3020   4568    -30    -55    -78       S  
ATOM   4712  N   ASP B 139      72.650  76.269  63.640  1.00 18.95           N  
ANISOU 4712  N   ASP B 139     1212   2060   3928    119     39   -153       N  
ATOM   4713  CA  ASP B 139      71.884  76.336  64.887  1.00 18.29           C  
ANISOU 4713  CA  ASP B 139      970   1937   4043     -7    -78   -210       C  
ATOM   4714  C   ASP B 139      70.419  76.658  64.644  1.00 18.46           C  
ANISOU 4714  C   ASP B 139     1018   1914   4080     49    -44   -203       C  
ATOM   4715  O   ASP B 139      69.669  76.760  65.603  1.00 18.23           O  
ANISOU 4715  O   ASP B 139      741   2073   4110     -7     -4   -161       O  
ATOM   4716  CB  ASP B 139      72.499  77.344  65.873  1.00 18.47           C  
ANISOU 4716  CB  ASP B 139     1060   1909   4047     48   -123   -224       C  
ATOM   4717  CG  ASP B 139      73.751  76.817  66.543  1.00 18.94           C  
ANISOU 4717  CG  ASP B 139     1001   1894   4299    -38   -120   -308       C  
ATOM   4718  OD1 ASP B 139      73.861  75.593  66.815  1.00 19.22           O  
ANISOU 4718  OD1 ASP B 139     1189   1764   4348    228   -308   -468       O  
ATOM   4719  OD2 ASP B 139      74.626  77.660  66.828  1.00 21.24           O  
ANISOU 4719  OD2 ASP B 139     1133   2068   4869      3    -76   -317       O  
ATOM   4720  N   GLY B 140      70.013  76.800  63.383  1.00 18.14           N  
ANISOU 4720  N   GLY B 140      912   1868   4110      8   -179   -167       N  
ATOM   4721  CA  GLY B 140      68.591  76.801  63.048  1.00 19.42           C  
ANISOU 4721  CA  GLY B 140     1135   1949   4291     46   -135   -135       C  
ATOM   4722  C   GLY B 140      68.075  77.870  62.102  1.00 19.40           C  
ANISOU 4722  C   GLY B 140     1158   1931   4278     12   -198   -158       C  
ATOM   4723  O   GLY B 140      66.928  77.789  61.652  1.00 19.31           O  
ANISOU 4723  O   GLY B 140     1096   2011   4229    182    -46   -181       O  
ATOM   4724  N   LEU B 141      68.900  78.879  61.810  1.00 19.36           N  
ANISOU 4724  N   LEU B 141     1168   1893   4295    -21   -159   -119       N  
ATOM   4725  CA  LEU B 141      68.413  80.003  61.013  1.00 18.93           C  
ANISOU 4725  CA  LEU B 141     1073   1877   4240     13   -380   -131       C  
ATOM   4726  C   LEU B 141      68.520  79.672  59.520  1.00 19.58           C  
ANISOU 4726  C   LEU B 141     1138   2008   4291     13   -441   -206       C  
ATOM   4727  O   LEU B 141      69.494  80.034  58.847  1.00 19.96           O  
ANISOU 4727  O   LEU B 141     1293   2084   4206      2   -507   -299       O  
ATOM   4728  CB  LEU B 141      69.121  81.326  61.371  1.00 18.37           C  
ANISOU 4728  CB  LEU B 141     1003   1694   4280     97   -317    -81       C  
ATOM   4729  CG  LEU B 141      68.272  82.593  61.191  1.00 18.19           C  
ANISOU 4729  CG  LEU B 141     1173   1533   4204    -17   -475    -31       C  
ATOM   4730  CD1 LEU B 141      69.120  83.816  61.518  1.00 18.35           C  
ANISOU 4730  CD1 LEU B 141     1279   1631   4060   -186   -206    166       C  
ATOM   4731  CD2 LEU B 141      67.686  82.724  59.773  1.00 17.93           C  
ANISOU 4731  CD2 LEU B 141      947   1676   4187    145   -385    -25       C  
ATOM   4732  N   ARG B 142      67.497  78.981  59.025  1.00 19.58           N  
ANISOU 4732  N   ARG B 142     1088   2096   4255      3   -538   -186       N  
ATOM   4733  CA  ARG B 142      67.436  78.500  57.649  1.00 19.82           C  
ANISOU 4733  CA  ARG B 142     1087   2126   4315     37   -652    -98       C  
ATOM   4734  C   ARG B 142      65.989  78.154  57.311  1.00 19.84           C  
ANISOU 4734  C   ARG B 142      993   2106   4436    -51   -753    -93       C  
ATOM   4735  O   ARG B 142      65.253  77.641  58.156  1.00 19.97           O  
ANISOU 4735  O   ARG B 142      970   2143   4473   -117   -842    -53       O  
ATOM   4736  CB  ARG B 142      68.326  77.275  57.441  1.00 18.98           C  
ANISOU 4736  CB  ARG B 142      924   2132   4153    230   -561    -32       C  
ATOM   4737  CG  ARG B 142      68.331  76.255  58.592  1.00 21.11           C  
ANISOU 4737  CG  ARG B 142     1595   2169   4255    253   -354     -6       C  
ATOM   4738  CD  ARG B 142      69.326  75.123  58.340  1.00 21.64           C  
ANISOU 4738  CD  ARG B 142     1931   2403   3886    829   -517    159       C  
ATOM   4739  NE  ARG B 142      69.707  74.428  59.568  1.00 26.59           N  
ANISOU 4739  NE  ARG B 142     3089   2768   4245   1060    -85    247       N  
ATOM   4740  CZ  ARG B 142      70.429  73.311  59.630  1.00 25.69           C  
ANISOU 4740  CZ  ARG B 142     2967   2797   3996   1099   -375    288       C  
ATOM   4741  NH1 ARG B 142      70.839  72.710  58.531  1.00 24.02           N  
ANISOU 4741  NH1 ARG B 142     2198   3023   3904   1139   -126    436       N  
ATOM   4742  NH2 ARG B 142      70.724  72.771  60.801  1.00 30.17           N  
ANISOU 4742  NH2 ARG B 142     4172   3206   4082    733   -113    407       N  
ATOM   4743  N   GLY B 143      65.569  78.477  56.092  1.00 20.00           N  
ANISOU 4743  N   GLY B 143      944   2087   4569   -134   -865   -142       N  
ATOM   4744  CA  GLY B 143      64.208  78.156  55.675  1.00 20.53           C  
ANISOU 4744  CA  GLY B 143     1019   2056   4722   -151   -987   -115       C  
ATOM   4745  C   GLY B 143      64.132  78.254  54.168  1.00 21.15           C  
ANISOU 4745  C   GLY B 143     1184   2013   4837   -145  -1086    -52       C  
ATOM   4746  O   GLY B 143      65.070  78.751  53.545  1.00 22.44           O  
ANISOU 4746  O   GLY B 143     1365   2179   4982   -140   -968    -49       O  
ATOM   4747  N   PRO B 144      63.032  77.773  53.578  1.00 21.92           N  
ANISOU 4747  N   PRO B 144     1264   2148   4914   -133  -1237     -6       N  
ATOM   4748  CA  PRO B 144      62.806  77.753  52.131  1.00 22.68           C  
ANISOU 4748  CA  PRO B 144     1445   2194   4976   -159  -1329    -15       C  
ATOM   4749  C   PRO B 144      62.234  79.075  51.617  1.00 23.81           C  
ANISOU 4749  C   PRO B 144     1620   2259   5164    -61  -1419     25       C  
ATOM   4750  O   PRO B 144      61.637  79.837  52.390  1.00 23.88           O  
ANISOU 4750  O   PRO B 144     1673   2258   5143    -27  -1392    -50       O  
ATOM   4751  CB  PRO B 144      61.794  76.614  51.951  1.00 22.92           C  
ANISOU 4751  CB  PRO B 144     1477   2265   4964   -212  -1309      9       C  
ATOM   4752  CG  PRO B 144      60.994  76.632  53.229  1.00 22.35           C  
ANISOU 4752  CG  PRO B 144     1301   2330   4860   -242  -1341   -128       C  
ATOM   4753  CD  PRO B 144      61.965  77.081  54.321  1.00 21.36           C  
ANISOU 4753  CD  PRO B 144     1122   2134   4859   -270  -1299      3       C  
ATOM   4754  N   PHE B 145      62.402  79.341  50.321  1.00 24.46           N  
ANISOU 4754  N   PHE B 145     1786   2214   5293      6  -1458    115       N  
ATOM   4755  CA  PHE B 145      62.001  80.623  49.739  1.00 25.63           C  
ANISOU 4755  CA  PHE B 145     1929   2309   5500    216  -1576    220       C  
ATOM   4756  C   PHE B 145      61.603  80.317  48.303  1.00 26.74           C  
ANISOU 4756  C   PHE B 145     2117   2395   5647    273  -1672    226       C  
ATOM   4757  O   PHE B 145      62.449  79.915  47.508  1.00 27.13           O  
ANISOU 4757  O   PHE B 145     2085   2632   5591    351  -1689    356       O  
ATOM   4758  CB  PHE B 145      63.205  81.577  49.813  1.00 25.82           C  
ANISOU 4758  CB  PHE B 145     2033   2235   5540    189  -1493    249       C  
ATOM   4759  CG  PHE B 145      62.931  83.033  49.488  1.00 24.84           C  
ANISOU 4759  CG  PHE B 145     1892   2176   5370    246  -1436    207       C  
ATOM   4760  CD1 PHE B 145      62.028  83.419  48.505  1.00 25.05           C  
ANISOU 4760  CD1 PHE B 145     2019   1962   5535    586  -1405    486       C  
ATOM   4761  CD2 PHE B 145      63.692  84.017  50.104  1.00 25.45           C  
ANISOU 4761  CD2 PHE B 145     2134   2069   5465    107  -1313    309       C  
ATOM   4762  CE1 PHE B 145      61.834  84.774  48.199  1.00 25.60           C  
ANISOU 4762  CE1 PHE B 145     2040   2180   5504    218  -1460    412       C  
ATOM   4763  CE2 PHE B 145      63.506  85.381  49.813  1.00 25.05           C  
ANISOU 4763  CE2 PHE B 145     2036   2114   5368    226  -1460    490       C  
ATOM   4764  CZ  PHE B 145      62.566  85.760  48.857  1.00 25.96           C  
ANISOU 4764  CZ  PHE B 145     1984   2281   5596     37  -1360    513       C  
ATOM   4765  N   VAL B 146      60.327  80.493  47.964  1.00 27.86           N  
ANISOU 4765  N   VAL B 146     2282   2457   5845    153  -1839    198       N  
ATOM   4766  CA  VAL B 146      59.854  80.192  46.616  1.00 28.74           C  
ANISOU 4766  CA  VAL B 146     2412   2463   6044    190  -1977    195       C  
ATOM   4767  C   VAL B 146      59.299  81.411  45.878  1.00 29.89           C  
ANISOU 4767  C   VAL B 146     2566   2501   6290    245  -2070    224       C  
ATOM   4768  O   VAL B 146      58.440  82.134  46.385  1.00 30.28           O  
ANISOU 4768  O   VAL B 146     2835   2298   6372    282  -1988    208       O  
ATOM   4769  CB  VAL B 146      58.838  79.027  46.624  1.00 29.07           C  
ANISOU 4769  CB  VAL B 146     2397   2622   6026    170  -2003    162       C  
ATOM   4770  CG1 VAL B 146      58.250  78.797  45.225  1.00 28.76           C  
ANISOU 4770  CG1 VAL B 146     2256   2742   5929    146  -2040     61       C  
ATOM   4771  CG2 VAL B 146      59.499  77.752  47.144  1.00 27.23           C  
ANISOU 4771  CG2 VAL B 146     2119   2460   5768     23  -2044    143       C  
ATOM   4772  N   VAL B 147      59.793  81.626  44.663  1.00 30.84           N  
ANISOU 4772  N   VAL B 147     2780   2474   6461    310  -2165    298       N  
ATOM   4773  CA  VAL B 147      59.276  82.678  43.789  1.00 31.68           C  
ANISOU 4773  CA  VAL B 147     2810   2532   6694    469  -2385    363       C  
ATOM   4774  C   VAL B 147      58.507  82.015  42.648  1.00 33.05           C  
ANISOU 4774  C   VAL B 147     3040   2604   6912    447  -2490    365       C  
ATOM   4775  O   VAL B 147      59.107  81.413  41.758  1.00 32.67           O  
ANISOU 4775  O   VAL B 147     2876   2544   6990    469  -2441    370       O  
ATOM   4776  CB  VAL B 147      60.407  83.577  43.224  1.00 31.57           C  
ANISOU 4776  CB  VAL B 147     2875   2461   6658    467  -2384    419       C  
ATOM   4777  CG1 VAL B 147      59.838  84.673  42.305  1.00 30.89           C  
ANISOU 4777  CG1 VAL B 147     2831   2285   6620    575  -2352    313       C  
ATOM   4778  CG2 VAL B 147      61.239  84.196  44.347  1.00 30.80           C  
ANISOU 4778  CG2 VAL B 147     2661   2389   6651    490  -2214    309       C  
ATOM   4779  N   TYR B 148      57.180  82.135  42.681  1.00 34.30           N  
ANISOU 4779  N   TYR B 148     3195   2736   7099    532  -2733    414       N  
ATOM   4780  CA  TYR B 148      56.302  81.496  41.705  1.00 36.05           C  
ANISOU 4780  CA  TYR B 148     3487   2904   7305    556  -2971    372       C  
ATOM   4781  C   TYR B 148      56.334  82.250  40.381  1.00 37.53           C  
ANISOU 4781  C   TYR B 148     3759   3049   7451    583  -3101    413       C  
ATOM   4782  O   TYR B 148      56.504  83.471  40.358  1.00 37.66           O  
ANISOU 4782  O   TYR B 148     3720   3070   7516    606  -3112    362       O  
ATOM   4783  CB  TYR B 148      54.870  81.398  42.259  1.00 36.03           C  
ANISOU 4783  CB  TYR B 148     3541   2822   7324    497  -2922    366       C  
ATOM   4784  CG  TYR B 148      54.814  80.488  43.463  1.00 35.41           C  
ANISOU 4784  CG  TYR B 148     3343   2921   7188    526  -3128    377       C  
ATOM   4785  CD1 TYR B 148      54.828  79.106  43.307  1.00 34.96           C  
ANISOU 4785  CD1 TYR B 148     3160   2897   7226    627  -3054    404       C  
ATOM   4786  CD2 TYR B 148      54.828  81.001  44.757  1.00 36.71           C  
ANISOU 4786  CD2 TYR B 148     3750   2868   7328    565  -2833    342       C  
ATOM   4787  CE1 TYR B 148      54.819  78.256  44.407  1.00 34.79           C  
ANISOU 4787  CE1 TYR B 148     3104   2900   7211    713  -3081    403       C  
ATOM   4788  CE2 TYR B 148      54.838  80.155  45.871  1.00 34.64           C  
ANISOU 4788  CE2 TYR B 148     3179   2765   7216    627  -3170    481       C  
ATOM   4789  CZ  TYR B 148      54.819  78.779  45.688  1.00 35.17           C  
ANISOU 4789  CZ  TYR B 148     3374   2798   7190    762  -3031    419       C  
ATOM   4790  OH  TYR B 148      54.831  77.911  46.767  1.00 34.50           O  
ANISOU 4790  OH  TYR B 148     3322   2538   7246    623  -2804    489       O  
ATOM   4791  N   ASP B 149      56.167  81.517  39.284  1.00 39.56           N  
ANISOU 4791  N   ASP B 149     4160   3256   7614    645  -3262    401       N  
ATOM   4792  CA  ASP B 149      56.042  82.118  37.958  1.00 41.49           C  
ANISOU 4792  CA  ASP B 149     4556   3438   7769    739  -3459    452       C  
ATOM   4793  C   ASP B 149      54.605  81.955  37.446  1.00 42.36           C  
ANISOU 4793  C   ASP B 149     4756   3488   7851    787  -3593    442       C  
ATOM   4794  O   ASP B 149      54.191  80.837  37.135  1.00 43.09           O  
ANISOU 4794  O   ASP B 149     4842   3591   7936    825  -3566    445       O  
ATOM   4795  CB  ASP B 149      57.040  81.442  37.012  1.00 41.65           C  
ANISOU 4795  CB  ASP B 149     4568   3476   7778    688  -3430    415       C  
ATOM   4796  CG  ASP B 149      57.132  82.117  35.650  1.00 42.88           C  
ANISOU 4796  CG  ASP B 149     4793   3558   7939    773  -3418    523       C  
ATOM   4797  OD1 ASP B 149      56.286  82.971  35.319  1.00 42.14           O  
ANISOU 4797  OD1 ASP B 149     4787   3190   8034    668  -3395    508       O  
ATOM   4798  OD2 ASP B 149      58.071  81.780  34.893  1.00 44.75           O  
ANISOU 4798  OD2 ASP B 149     5128   3912   7961    659  -3267    429       O  
ATOM   4799  N   PRO B 150      53.827  83.053  37.372  1.00 43.39           N  
ANISOU 4799  N   PRO B 150     5037   3556   7892    840  -3755    496       N  
ATOM   4800  CA  PRO B 150      52.464  82.956  36.839  1.00 44.00           C  
ANISOU 4800  CA  PRO B 150     5172   3614   7931    878  -3812    514       C  
ATOM   4801  C   PRO B 150      52.437  82.459  35.394  1.00 44.88           C  
ANISOU 4801  C   PRO B 150     5417   3677   7958    887  -3865    556       C  
ATOM   4802  O   PRO B 150      51.395  82.003  34.923  1.00 44.83           O  
ANISOU 4802  O   PRO B 150     5356   3668   8009    857  -3857    535       O  
ATOM   4803  CB  PRO B 150      51.948  84.399  36.884  1.00 44.19           C  
ANISOU 4803  CB  PRO B 150     5206   3642   7941    878  -3842    516       C  
ATOM   4804  CG  PRO B 150      52.814  85.115  37.836  1.00 43.79           C  
ANISOU 4804  CG  PRO B 150     5052   3575   8008    835  -3773    429       C  
ATOM   4805  CD  PRO B 150      54.153  84.422  37.817  1.00 43.61           C  
ANISOU 4805  CD  PRO B 150     5092   3545   7931    895  -3753    516       C  
ATOM   4806  N   LYS B 151      53.569  82.550  34.697  1.00 45.49           N  
ANISOU 4806  N   LYS B 151     5676   3729   7876    885  -3908    662       N  
ATOM   4807  CA  LYS B 151      53.675  82.027  33.336  1.00 46.37           C  
ANISOU 4807  CA  LYS B 151     5982   3763   7871    940  -3856    764       C  
ATOM   4808  C   LYS B 151      54.666  80.872  33.231  1.00 45.58           C  
ANISOU 4808  C   LYS B 151     5839   3756   7722    915  -3997    800       C  
ATOM   4809  O   LYS B 151      55.289  80.685  32.182  1.00 44.93           O  
ANISOU 4809  O   LYS B 151     5749   3674   7649    937  -4036    864       O  
ATOM   4810  CB  LYS B 151      54.049  83.135  32.349  1.00 46.93           C  
ANISOU 4810  CB  LYS B 151     6099   3827   7904    964  -3815    801       C  
ATOM   4811  CG  LYS B 151      52.994  84.218  32.204  1.00 49.20           C  
ANISOU 4811  CG  LYS B 151     6596   3946   8150   1098  -3641    855       C  
ATOM   4812  CD  LYS B 151      53.519  85.362  31.366  1.00 52.81           C  
ANISOU 4812  CD  LYS B 151     7410   4082   8573   1067  -3291   1005       C  
ATOM   4813  CE  LYS B 151      52.360  86.191  30.851  1.00 54.09           C  
ANISOU 4813  CE  LYS B 151     7560   4215   8776   1134  -3157   1112       C  
ATOM   4814  NZ  LYS B 151      52.845  87.532  30.457  1.00 56.04           N  
ANISOU 4814  NZ  LYS B 151     8010   4189   9092   1045  -2854   1111       N  
ATOM   4815  N   ASP B 152      54.776  80.088  34.305  1.00 45.26           N  
ANISOU 4815  N   ASP B 152     5868   3698   7628    829  -4074    755       N  
ATOM   4816  CA  ASP B 152      55.729  78.990  34.362  1.00 44.94           C  
ANISOU 4816  CA  ASP B 152     5882   3687   7507    795  -4140    748       C  
ATOM   4817  C   ASP B 152      55.591  78.096  33.135  1.00 45.35           C  
ANISOU 4817  C   ASP B 152     5930   3708   7592    752  -4177    719       C  
ATOM   4818  O   ASP B 152      54.508  77.579  32.859  1.00 44.69           O  
ANISOU 4818  O   ASP B 152     5932   3589   7460    727  -4217    716       O  
ATOM   4819  CB  ASP B 152      55.562  78.173  35.647  1.00 44.94           C  
ANISOU 4819  CB  ASP B 152     5883   3669   7523    778  -4086    746       C  
ATOM   4820  CG  ASP B 152      56.795  77.354  35.982  1.00 43.80           C  
ANISOU 4820  CG  ASP B 152     5762   3604   7273    695  -4085    773       C  
ATOM   4821  OD1 ASP B 152      57.269  76.595  35.110  1.00 43.87           O  
ANISOU 4821  OD1 ASP B 152     5735   3754   7179    682  -3915    845       O  
ATOM   4822  OD2 ASP B 152      57.293  77.451  37.126  1.00 41.72           O  
ANISOU 4822  OD2 ASP B 152     5221   3434   7194    560  -4067    948       O  
ATOM   4823  N   PRO B 153      56.688  77.943  32.376  1.00 45.90           N  
ANISOU 4823  N   PRO B 153     5979   3793   7667    700  -4201    656       N  
ATOM   4824  CA  PRO B 153      56.661  77.126  31.167  1.00 46.09           C  
ANISOU 4824  CA  PRO B 153     5959   3818   7733    643  -4241    595       C  
ATOM   4825  C   PRO B 153      56.368  75.654  31.445  1.00 46.43           C  
ANISOU 4825  C   PRO B 153     5945   3878   7815    560  -4253    560       C  
ATOM   4826  O   PRO B 153      55.993  74.928  30.520  1.00 46.61           O  
ANISOU 4826  O   PRO B 153     6011   3850   7849    499  -4213    509       O  
ATOM   4827  CB  PRO B 153      58.068  77.296  30.586  1.00 46.44           C  
ANISOU 4827  CB  PRO B 153     6013   3874   7757    630  -4209    573       C  
ATOM   4828  CG  PRO B 153      58.909  77.843  31.707  1.00 46.27           C  
ANISOU 4828  CG  PRO B 153     5988   3890   7702    707  -4216    608       C  
ATOM   4829  CD  PRO B 153      57.974  78.646  32.549  1.00 46.25           C  
ANISOU 4829  CD  PRO B 153     5984   3875   7713    697  -4205    630       C  
ATOM   4830  N   HIS B 154      56.528  75.224  32.695  1.00 46.10           N  
ANISOU 4830  N   HIS B 154     5801   3848   7864    554  -4335    557       N  
ATOM   4831  CA  HIS B 154      56.261  73.839  33.071  1.00 46.54           C  
ANISOU 4831  CA  HIS B 154     5780   3938   7964    526  -4345    544       C  
ATOM   4832  C   HIS B 154      54.876  73.619  33.677  1.00 47.17           C  
ANISOU 4832  C   HIS B 154     5776   3998   8145    527  -4314    482       C  
ATOM   4833  O   HIS B 154      54.575  72.512  34.121  1.00 46.78           O  
ANISOU 4833  O   HIS B 154     5674   3969   8129    585  -4355    500       O  
ATOM   4834  CB  HIS B 154      57.320  73.338  34.056  1.00 46.00           C  
ANISOU 4834  CB  HIS B 154     5752   3837   7889    510  -4368    559       C  
ATOM   4835  CG  HIS B 154      58.655  73.065  33.436  1.00 45.98           C  
ANISOU 4835  CG  HIS B 154     5930   3873   7664    385  -4311    630       C  
ATOM   4836  ND1 HIS B 154      58.802  72.397  32.239  1.00 45.72           N  
ANISOU 4836  ND1 HIS B 154     5925   3900   7547    225  -4396    729       N  
ATOM   4837  CD2 HIS B 154      59.909  73.334  33.873  1.00 45.42           C  
ANISOU 4837  CD2 HIS B 154     5916   3863   7479    269  -4321    673       C  
ATOM   4838  CE1 HIS B 154      60.088  72.279  31.961  1.00 46.08           C  
ANISOU 4838  CE1 HIS B 154     6000   3901   7606    129  -4238    621       C  
ATOM   4839  NE2 HIS B 154      60.782  72.834  32.939  1.00 45.14           N  
ANISOU 4839  NE2 HIS B 154     5982   3936   7230    219  -4367    753       N  
ATOM   4840  N   LYS B 155      54.032  74.650  33.685  1.00 47.70           N  
ANISOU 4840  N   LYS B 155     5693   4063   8365    531  -4331    416       N  
ATOM   4841  CA  LYS B 155      52.789  74.612  34.454  1.00 49.07           C  
ANISOU 4841  CA  LYS B 155     5766   4223   8652    489  -4246    324       C  
ATOM   4842  C   LYS B 155      51.856  73.468  34.052  1.00 49.11           C  
ANISOU 4842  C   LYS B 155     5678   4214   8765    496  -4284    271       C  
ATOM   4843  O   LYS B 155      51.194  72.880  34.906  1.00 48.36           O  
ANISOU 4843  O   LYS B 155     5468   4168   8735    461  -4356    255       O  
ATOM   4844  CB  LYS B 155      52.034  75.947  34.363  1.00 50.14           C  
ANISOU 4844  CB  LYS B 155     5955   4275   8819    443  -4098    295       C  
ATOM   4845  CG  LYS B 155      51.432  76.407  35.693  1.00 52.93           C  
ANISOU 4845  CG  LYS B 155     6405   4648   9056    347  -3822    257       C  
ATOM   4846  CD  LYS B 155      50.144  75.662  36.047  1.00 56.54           C  
ANISOU 4846  CD  LYS B 155     6757   5233   9491    191  -3572    329       C  
ATOM   4847  CE  LYS B 155      50.146  75.237  37.513  1.00 57.43           C  
ANISOU 4847  CE  LYS B 155     7018   5141   9661    356  -3431    497       C  
ATOM   4848  NZ  LYS B 155      49.247  74.078  37.777  1.00 57.93           N  
ANISOU 4848  NZ  LYS B 155     7069   4920  10022    456  -3232    419       N  
ATOM   4849  N   LYS B 156      51.812  73.148  32.762  1.00 49.20           N  
ANISOU 4849  N   LYS B 156     5550   4270   8871    507  -4356    197       N  
ATOM   4850  CA  LYS B 156      50.966  72.052  32.291  1.00 50.10           C  
ANISOU 4850  CA  LYS B 156     5649   4356   9027    495  -4340    167       C  
ATOM   4851  C   LYS B 156      51.393  70.657  32.757  1.00 49.50           C  
ANISOU 4851  C   LYS B 156     5430   4307   9069    474  -4370     64       C  
ATOM   4852  O   LYS B 156      50.661  69.688  32.553  1.00 49.39           O  
ANISOU 4852  O   LYS B 156     5422   4266   9078    445  -4381     30       O  
ATOM   4853  CB  LYS B 156      50.777  72.101  30.774  1.00 50.70           C  
ANISOU 4853  CB  LYS B 156     5791   4450   9022    480  -4323    163       C  
ATOM   4854  CG  LYS B 156      49.806  73.198  30.338  1.00 53.21           C  
ANISOU 4854  CG  LYS B 156     6161   4709   9344    639  -4197    315       C  
ATOM   4855  CD  LYS B 156      48.987  72.790  29.112  1.00 56.61           C  
ANISOU 4855  CD  LYS B 156     6838   5238   9431    815  -4174    487       C  
ATOM   4856  CE  LYS B 156      49.521  73.418  27.830  1.00 58.98           C  
ANISOU 4856  CE  LYS B 156     7271   5249   9888    894  -3818    699       C  
ATOM   4857  NZ  LYS B 156      49.107  74.845  27.707  1.00 60.39           N  
ANISOU 4857  NZ  LYS B 156     7573   5219  10152    815  -3606    663       N  
ATOM   4858  N   LEU B 157      52.550  70.552  33.405  1.00 48.85           N  
ANISOU 4858  N   LEU B 157     5248   4249   9062    454  -4386     -6       N  
ATOM   4859  CA  LEU B 157      53.029  69.257  33.884  1.00 48.01           C  
ANISOU 4859  CA  LEU B 157     5014   4164   9062    425  -4368   -106       C  
ATOM   4860  C   LEU B 157      52.501  68.869  35.268  1.00 47.43           C  
ANISOU 4860  C   LEU B 157     4846   4102   9071    419  -4319   -152       C  
ATOM   4861  O   LEU B 157      52.724  67.744  35.711  1.00 47.29           O  
ANISOU 4861  O   LEU B 157     4810   4062   9095    475  -4293   -133       O  
ATOM   4862  CB  LEU B 157      54.567  69.171  33.844  1.00 47.73           C  
ANISOU 4862  CB  LEU B 157     5009   4112   9014    441  -4423   -112       C  
ATOM   4863  CG  LEU B 157      55.239  69.308  32.473  1.00 47.82           C  
ANISOU 4863  CG  LEU B 157     4976   4158   9033    390  -4438   -216       C  
ATOM   4864  CD1 LEU B 157      56.750  69.241  32.574  1.00 47.26           C  
ANISOU 4864  CD1 LEU B 157     5022   4227   8708    482  -4872   -132       C  
ATOM   4865  CD2 LEU B 157      54.739  68.273  31.469  1.00 50.25           C  
ANISOU 4865  CD2 LEU B 157     5482   4604   9004    294  -4473   -332       C  
ATOM   4866  N   TYR B 158      51.807  69.778  35.953  1.00 46.64           N  
ANISOU 4866  N   TYR B 158     4584   4051   9083    424  -4302   -163       N  
ATOM   4867  CA  TYR B 158      51.387  69.508  37.333  1.00 45.49           C  
ANISOU 4867  CA  TYR B 158     4316   3951   9017    401  -4297   -220       C  
ATOM   4868  C   TYR B 158      50.089  70.183  37.766  1.00 45.00           C  
ANISOU 4868  C   TYR B 158     4137   3922   9037    359  -4261   -230       C  
ATOM   4869  O   TYR B 158      49.648  71.162  37.152  1.00 44.52           O  
ANISOU 4869  O   TYR B 158     4012   3918   8983    381  -4372   -217       O  
ATOM   4870  CB  TYR B 158      52.518  69.812  38.328  1.00 45.78           C  
ANISOU 4870  CB  TYR B 158     4443   3961   8990    394  -4280   -233       C  
ATOM   4871  CG  TYR B 158      53.062  71.217  38.247  1.00 44.90           C  
ANISOU 4871  CG  TYR B 158     4349   3926   8783    404  -4391   -213       C  
ATOM   4872  CD1 TYR B 158      52.452  72.258  38.939  1.00 44.82           C  
ANISOU 4872  CD1 TYR B 158     4386   3967   8675    478  -4438   -147       C  
ATOM   4873  CD2 TYR B 158      54.191  71.504  37.489  1.00 44.91           C  
ANISOU 4873  CD2 TYR B 158     4546   3893   8625    548  -4301   -221       C  
ATOM   4874  CE1 TYR B 158      52.945  73.549  38.868  1.00 45.54           C  
ANISOU 4874  CE1 TYR B 158     4569   3981   8751    445  -4298   -168       C  
ATOM   4875  CE2 TYR B 158      54.705  72.791  37.422  1.00 45.60           C  
ANISOU 4875  CE2 TYR B 158     4765   3866   8693    488  -4244    -92       C  
ATOM   4876  CZ  TYR B 158      54.071  73.809  38.112  1.00 45.95           C  
ANISOU 4876  CZ  TYR B 158     4752   3940   8765    439  -4194   -124       C  
ATOM   4877  OH  TYR B 158      54.558  75.094  38.055  1.00 46.02           O  
ANISOU 4877  OH  TYR B 158     4757   3814   8911    517  -4062     34       O  
ATOM   4878  N   ASP B 159      49.499  69.661  38.838  1.00 44.01           N  
ANISOU 4878  N   ASP B 159     3842   3821   9058    361  -4180   -249       N  
ATOM   4879  CA  ASP B 159      48.237  70.169  39.371  1.00 43.86           C  
ANISOU 4879  CA  ASP B 159     3716   3807   9140    294  -4005   -296       C  
ATOM   4880  C   ASP B 159      48.388  70.927  40.683  1.00 43.19           C  
ANISOU 4880  C   ASP B 159     3530   3751   9126    352  -3863   -269       C  
ATOM   4881  O   ASP B 159      47.593  71.820  40.981  1.00 43.22           O  
ANISOU 4881  O   ASP B 159     3461   3800   9159    410  -3810   -326       O  
ATOM   4882  CB  ASP B 159      47.266  69.009  39.579  1.00 44.61           C  
ANISOU 4882  CB  ASP B 159     3825   3849   9275    303  -3943   -286       C  
ATOM   4883  CG  ASP B 159      47.116  68.162  38.335  1.00 44.45           C  
ANISOU 4883  CG  ASP B 159     3719   3902   9267    288  -4174   -197       C  
ATOM   4884  OD1 ASP B 159      46.732  68.732  37.296  1.00 45.34           O  
ANISOU 4884  OD1 ASP B 159     3594   3982   9648    780  -4320    119       O  
ATOM   4885  OD2 ASP B 159      47.431  66.954  38.383  1.00 44.31           O  
ANISOU 4885  OD2 ASP B 159     3580   3683   9572     94  -4159   -260       O  
ATOM   4886  N   VAL B 160      49.392  70.556  41.471  1.00 41.57           N  
ANISOU 4886  N   VAL B 160     3129   3636   9029    320  -3722   -291       N  
ATOM   4887  CA  VAL B 160      49.539  71.107  42.812  1.00 40.63           C  
ANISOU 4887  CA  VAL B 160     2927   3553   8954    308  -3553   -257       C  
ATOM   4888  C   VAL B 160      50.954  71.635  42.987  1.00 39.72           C  
ANISOU 4888  C   VAL B 160     2804   3463   8824    310  -3413   -243       C  
ATOM   4889  O   VAL B 160      51.938  70.933  42.740  1.00 39.33           O  
ANISOU 4889  O   VAL B 160     2742   3444   8756    349  -3434   -161       O  
ATOM   4890  CB  VAL B 160      49.213  70.066  43.914  1.00 40.77           C  
ANISOU 4890  CB  VAL B 160     2940   3573   8977    286  -3543   -278       C  
ATOM   4891  CG1 VAL B 160      49.250  70.693  45.297  1.00 40.02           C  
ANISOU 4891  CG1 VAL B 160     2791   3472   8940    258  -3639   -274       C  
ATOM   4892  CG2 VAL B 160      47.844  69.431  43.681  1.00 42.06           C  
ANISOU 4892  CG2 VAL B 160     3098   3758   9122     92  -3430   -299       C  
ATOM   4893  N   ASP B 161      51.043  72.888  43.412  1.00 38.77           N  
ANISOU 4893  N   ASP B 161     2650   3419   8661    344  -3230   -192       N  
ATOM   4894  CA  ASP B 161      52.324  73.506  43.751  1.00 37.36           C  
ANISOU 4894  CA  ASP B 161     2458   3301   8435    352  -3102   -137       C  
ATOM   4895  C   ASP B 161      52.060  74.585  44.788  1.00 37.04           C  
ANISOU 4895  C   ASP B 161     2381   3334   8357    330  -2910   -130       C  
ATOM   4896  O   ASP B 161      51.547  75.652  44.455  1.00 37.49           O  
ANISOU 4896  O   ASP B 161     2595   3334   8312    366  -2834   -133       O  
ATOM   4897  CB  ASP B 161      52.960  74.107  42.495  1.00 37.56           C  
ANISOU 4897  CB  ASP B 161     2470   3356   8444    358  -3135   -146       C  
ATOM   4898  CG  ASP B 161      54.223  74.897  42.787  1.00 37.31           C  
ANISOU 4898  CG  ASP B 161     2762   3171   8240    333  -3282    -28       C  
ATOM   4899  OD1 ASP B 161      54.896  74.612  43.803  1.00 36.85           O  
ANISOU 4899  OD1 ASP B 161     2921   2904   8174    583  -3370    270       O  
ATOM   4900  OD2 ASP B 161      54.539  75.809  41.987  1.00 38.14           O  
ANISOU 4900  OD2 ASP B 161     3422   3159   7909    673  -3517    138       O  
ATOM   4901  N   ASN B 162      52.393  74.316  46.046  1.00 36.39           N  
ANISOU 4901  N   ASN B 162     2319   3274   8233    327  -2659   -147       N  
ATOM   4902  CA  ASN B 162      52.072  75.246  47.121  1.00 35.80           C  
ANISOU 4902  CA  ASN B 162     2220   3248   8134    346  -2475   -187       C  
ATOM   4903  C   ASN B 162      52.958  74.963  48.328  1.00 35.35           C  
ANISOU 4903  C   ASN B 162     2233   3205   7991    351  -2289   -185       C  
ATOM   4904  O   ASN B 162      53.938  74.219  48.215  1.00 34.75           O  
ANISOU 4904  O   ASN B 162     2074   3119   8009    462  -2269   -126       O  
ATOM   4905  CB  ASN B 162      50.575  75.186  47.467  1.00 36.52           C  
ANISOU 4905  CB  ASN B 162     2445   3285   8143    349  -2432   -223       C  
ATOM   4906  CG  ASN B 162      50.128  73.813  47.951  1.00 37.30           C  
ANISOU 4906  CG  ASN B 162     2439   3464   8266    303  -2503   -230       C  
ATOM   4907  OD1 ASN B 162      50.907  73.056  48.538  1.00 37.40           O  
ANISOU 4907  OD1 ASN B 162     2725   3220   8264    343  -2777   -355       O  
ATOM   4908  ND2 ASN B 162      48.854  73.496  47.727  1.00 38.13           N  
ANISOU 4908  ND2 ASN B 162     2438   3886   8162    494  -2888   -315       N  
ATOM   4909  N   GLU B 163      52.623  75.537  49.479  1.00 34.70           N  
ANISOU 4909  N   GLU B 163     2173   3107   7904    308  -2122   -237       N  
ATOM   4910  CA  GLU B 163      53.431  75.339  50.683  1.00 34.27           C  
ANISOU 4910  CA  GLU B 163     2151   3154   7714    232  -1983   -269       C  
ATOM   4911  C   GLU B 163      53.658  73.862  50.993  1.00 33.50           C  
ANISOU 4911  C   GLU B 163     1973   3119   7637    173  -1928   -275       C  
ATOM   4912  O   GLU B 163      54.763  73.470  51.390  1.00 33.40           O  
ANISOU 4912  O   GLU B 163     2046   3035   7607    127  -1932   -272       O  
ATOM   4913  CB  GLU B 163      52.783  76.045  51.879  1.00 34.91           C  
ANISOU 4913  CB  GLU B 163     2273   3225   7766    255  -1921   -311       C  
ATOM   4914  CG  GLU B 163      53.620  76.090  53.150  1.00 37.26           C  
ANISOU 4914  CG  GLU B 163     2884   3659   7612    376  -1754   -388       C  
ATOM   4915  CD  GLU B 163      53.343  77.340  53.979  1.00 41.96           C  
ANISOU 4915  CD  GLU B 163     4075   4271   7597    661  -1511   -547       C  
ATOM   4916  OE1 GLU B 163      53.010  78.386  53.390  1.00 44.34           O  
ANISOU 4916  OE1 GLU B 163     4592   4563   7689    839  -1165   -698       O  
ATOM   4917  OE2 GLU B 163      53.459  77.308  55.221  1.00 44.27           O  
ANISOU 4917  OE2 GLU B 163     4427   4808   7585    633  -1496   -606       O  
ATOM   4918  N   SER B 164      52.624  73.045  50.799  1.00 32.40           N  
ANISOU 4918  N   SER B 164     1808   3004   7496     98  -1880   -243       N  
ATOM   4919  CA  SER B 164      52.693  71.628  51.157  1.00 32.05           C  
ANISOU 4919  CA  SER B 164     1697   3116   7363     19  -1804   -178       C  
ATOM   4920  C   SER B 164      53.507  70.789  50.169  1.00 30.88           C  
ANISOU 4920  C   SER B 164     1651   2886   7193     51  -1757   -179       C  
ATOM   4921  O   SER B 164      53.783  69.628  50.449  1.00 31.03           O  
ANISOU 4921  O   SER B 164     1722   2828   7240    -80  -1720   -144       O  
ATOM   4922  CB  SER B 164      51.292  71.022  51.338  1.00 32.53           C  
ANISOU 4922  CB  SER B 164     1726   3240   7391    -56  -1883   -159       C  
ATOM   4923  OG  SER B 164      50.608  70.943  50.096  1.00 33.66           O  
ANISOU 4923  OG  SER B 164     1679   3641   7468   -145  -1903      6       O  
ATOM   4924  N   THR B 165      53.919  71.362  49.041  1.00 29.64           N  
ANISOU 4924  N   THR B 165     1565   2757   6937     87  -1710   -227       N  
ATOM   4925  CA  THR B 165      54.822  70.661  48.134  1.00 28.97           C  
ANISOU 4925  CA  THR B 165     1594   2753   6659     42  -1673   -232       C  
ATOM   4926  C   THR B 165      56.302  71.062  48.269  1.00 28.20           C  
ANISOU 4926  C   THR B 165     1620   2643   6452      3  -1583   -302       C  
ATOM   4927  O   THR B 165      57.139  70.576  47.507  1.00 28.63           O  
ANISOU 4927  O   THR B 165     1582   2781   6512     56  -1539   -392       O  
ATOM   4928  CB  THR B 165      54.365  70.731  46.660  1.00 28.89           C  
ANISOU 4928  CB  THR B 165     1543   2730   6704    -18  -1728   -282       C  
ATOM   4929  OG1 THR B 165      54.555  72.055  46.152  1.00 28.91           O  
ANISOU 4929  OG1 THR B 165     1560   2736   6687    190  -1841   -263       O  
ATOM   4930  CG2 THR B 165      52.897  70.319  46.496  1.00 29.61           C  
ANISOU 4930  CG2 THR B 165     1578   2961   6709     23  -1656   -248       C  
ATOM   4931  N   VAL B 166      56.640  71.932  49.223  1.00 26.88           N  
ANISOU 4931  N   VAL B 166     1597   2487   6129      4  -1495   -274       N  
ATOM   4932  CA  VAL B 166      58.038  72.247  49.513  1.00 24.83           C  
ANISOU 4932  CA  VAL B 166     1494   2200   5739     33  -1446   -215       C  
ATOM   4933  C   VAL B 166      58.582  71.173  50.458  1.00 24.21           C  
ANISOU 4933  C   VAL B 166     1427   2230   5542     43  -1326   -229       C  
ATOM   4934  O   VAL B 166      57.929  70.838  51.454  1.00 24.40           O  
ANISOU 4934  O   VAL B 166     1581   2267   5423    130  -1190   -213       O  
ATOM   4935  CB  VAL B 166      58.199  73.644  50.188  1.00 25.06           C  
ANISOU 4935  CB  VAL B 166     1497   2210   5814    -11  -1534   -209       C  
ATOM   4936  CG1 VAL B 166      59.668  73.950  50.496  1.00 23.80           C  
ANISOU 4936  CG1 VAL B 166     1268   2209   5565     75  -1527   -219       C  
ATOM   4937  CG2 VAL B 166      57.607  74.744  49.311  1.00 25.64           C  
ANISOU 4937  CG2 VAL B 166     1815   2077   5849     32  -1477   -220       C  
ATOM   4938  N   ILE B 167      59.739  70.607  50.125  1.00 22.13           N  
ANISOU 4938  N   ILE B 167     1159   2114   5132     61  -1238   -237       N  
ATOM   4939  CA  ILE B 167      60.351  69.575  50.959  1.00 21.23           C  
ANISOU 4939  CA  ILE B 167     1114   2073   4877    -47  -1135   -142       C  
ATOM   4940  C   ILE B 167      61.729  70.091  51.346  1.00 21.29           C  
ANISOU 4940  C   ILE B 167     1151   2213   4725     30   -975    -74       C  
ATOM   4941  O   ILE B 167      62.577  70.290  50.465  1.00 21.41           O  
ANISOU 4941  O   ILE B 167     1249   2336   4547    182   -823    -58       O  
ATOM   4942  CB  ILE B 167      60.519  68.231  50.207  1.00 21.02           C  
ANISOU 4942  CB  ILE B 167      890   2173   4922    -16  -1185   -141       C  
ATOM   4943  CG1 ILE B 167      59.157  67.652  49.780  1.00 22.29           C  
ANISOU 4943  CG1 ILE B 167     1389   1987   5091   -342  -1427   -470       C  
ATOM   4944  CG2 ILE B 167      61.229  67.206  51.094  1.00 21.51           C  
ANISOU 4944  CG2 ILE B 167     1182   1926   5062   -212  -1078    -18       C  
ATOM   4945  CD1 ILE B 167      59.300  66.434  48.859  1.00 24.15           C  
ANISOU 4945  CD1 ILE B 167     1795   2557   4821   -263  -1415   -790       C  
ATOM   4946  N   THR B 168      61.966  70.299  52.643  1.00 20.73           N  
ANISOU 4946  N   THR B 168     1141   2187   4546     75   -776    -43       N  
ATOM   4947  CA  THR B 168      63.272  70.760  53.109  1.00 20.04           C  
ANISOU 4947  CA  THR B 168     1070   2113   4431    163   -725      5       C  
ATOM   4948  C   THR B 168      64.055  69.587  53.705  1.00 19.63           C  
ANISOU 4948  C   THR B 168     1007   2070   4381    149   -612     43       C  
ATOM   4949  O   THR B 168      63.472  68.700  54.338  1.00 19.15           O  
ANISOU 4949  O   THR B 168      881   2028   4364    146   -624     29       O  
ATOM   4950  CB  THR B 168      63.181  71.898  54.166  1.00 20.41           C  
ANISOU 4950  CB  THR B 168     1198   2076   4479    249   -648     79       C  
ATOM   4951  OG1 THR B 168      62.439  71.442  55.306  1.00 19.75           O  
ANISOU 4951  OG1 THR B 168     1306   2203   3995    242   -849     16       O  
ATOM   4952  CG2 THR B 168      62.490  73.143  53.575  1.00 20.77           C  
ANISOU 4952  CG2 THR B 168     1325   2038   4527    388   -785    -76       C  
ATOM   4953  N   LEU B 169      65.368  69.573  53.479  1.00 18.79           N  
ANISOU 4953  N   LEU B 169      878   2007   4253     70   -602     38       N  
ATOM   4954  CA  LEU B 169      66.232  68.582  54.097  1.00 18.96           C  
ANISOU 4954  CA  LEU B 169      924   2136   4141     60   -511     70       C  
ATOM   4955  C   LEU B 169      67.196  69.334  54.991  1.00 19.65           C  
ANISOU 4955  C   LEU B 169     1028   2128   4309      2   -439     84       C  
ATOM   4956  O   LEU B 169      67.787  70.333  54.566  1.00 19.21           O  
ANISOU 4956  O   LEU B 169      794   2134   4371    -22   -464    181       O  
ATOM   4957  CB  LEU B 169      67.038  67.797  53.050  1.00 19.30           C  
ANISOU 4957  CB  LEU B 169     1122   2156   4054     88   -536     21       C  
ATOM   4958  CG  LEU B 169      66.267  67.106  51.916  1.00 18.39           C  
ANISOU 4958  CG  LEU B 169     1111   2183   3691    -24   -481    -12       C  
ATOM   4959  CD1 LEU B 169      67.240  66.348  51.028  1.00 18.51           C  
ANISOU 4959  CD1 LEU B 169     1453   2006   3572    175    -86    164       C  
ATOM   4960  CD2 LEU B 169      65.205  66.133  52.428  1.00 18.64           C  
ANISOU 4960  CD2 LEU B 169     1613   1837   3632     33   -231     25       C  
ATOM   4961  N   GLU B 170      67.371  68.847  56.217  1.00 19.63           N  
ANISOU 4961  N   GLU B 170     1001   2176   4280    -61   -323    140       N  
ATOM   4962  CA  GLU B 170      68.383  69.434  57.073  1.00 20.81           C  
ANISOU 4962  CA  GLU B 170     1169   2273   4462    -90   -283     98       C  
ATOM   4963  C   GLU B 170      69.110  68.468  58.011  1.00 20.13           C  
ANISOU 4963  C   GLU B 170     1061   2210   4375   -145   -214     40       C  
ATOM   4964  O   GLU B 170      68.545  67.461  58.444  1.00 20.24           O  
ANISOU 4964  O   GLU B 170     1020   2225   4442    -14   -193    158       O  
ATOM   4965  CB  GLU B 170      67.817  70.687  57.748  1.00 23.71           C  
ANISOU 4965  CB  GLU B 170     1523   2783   4702   -261   -151     29       C  
ATOM   4966  CG  GLU B 170      67.126  70.525  59.045  1.00 26.65           C  
ANISOU 4966  CG  GLU B 170     1699   3329   5097   -212    -57    210       C  
ATOM   4967  CD  GLU B 170      66.174  71.687  59.293  1.00 30.07           C  
ANISOU 4967  CD  GLU B 170     2124   3342   5958   -152   -122    185       C  
ATOM   4968  OE1 GLU B 170      66.645  72.776  59.708  1.00 28.65           O  
ANISOU 4968  OE1 GLU B 170     1934   3383   5568   -483    123    217       O  
ATOM   4969  OE2 GLU B 170      64.953  71.479  59.088  1.00 29.76           O  
ANISOU 4969  OE2 GLU B 170     1954   3780   5572   -241     82    336       O  
ATOM   4970  N   ASP B 171      70.393  68.741  58.234  1.00 18.37           N  
ANISOU 4970  N   ASP B 171      763   2044   4173   -135   -166    -45       N  
ATOM   4971  CA  ASP B 171      71.195  68.020  59.221  1.00 17.82           C  
ANISOU 4971  CA  ASP B 171      765   2018   3986   -199    -88   -185       C  
ATOM   4972  C   ASP B 171      70.963  68.666  60.583  1.00 18.25           C  
ANISOU 4972  C   ASP B 171      865   2101   3967   -201    -18   -145       C  
ATOM   4973  O   ASP B 171      70.905  69.906  60.695  1.00 19.95           O  
ANISOU 4973  O   ASP B 171     1286   2102   4191   -131    -29   -219       O  
ATOM   4974  CB  ASP B 171      72.690  67.986  58.826  1.00 17.85           C  
ANISOU 4974  CB  ASP B 171      753   2101   3927   -214     -9   -269       C  
ATOM   4975  CG  ASP B 171      73.278  69.360  58.461  1.00 18.69           C  
ANISOU 4975  CG  ASP B 171      887   2502   3710   -170     87   -127       C  
ATOM   4976  OD1 ASP B 171      72.542  70.283  58.049  1.00 17.36           O  
ANISOU 4976  OD1 ASP B 171     1029   2376   3190   -325   -187   -212       O  
ATOM   4977  OD2 ASP B 171      74.522  69.532  58.587  1.00 18.72           O  
ANISOU 4977  OD2 ASP B 171      844   2825   3440    -68    191   -109       O  
ATOM   4978  N   TRP B 172      70.801  67.852  61.619  1.00 16.91           N  
ANISOU 4978  N   TRP B 172      648   2010   3764   -263     78   -188       N  
ATOM   4979  CA  TRP B 172      70.506  68.419  62.930  1.00 17.29           C  
ANISOU 4979  CA  TRP B 172      806   2176   3586   -284     61    -89       C  
ATOM   4980  C   TRP B 172      71.457  67.834  63.963  1.00 17.08           C  
ANISOU 4980  C   TRP B 172      851   2180   3456   -416     49   -156       C  
ATOM   4981  O   TRP B 172      71.710  66.626  63.972  1.00 17.19           O  
ANISOU 4981  O   TRP B 172      946   2119   3467   -422    -91   -217       O  
ATOM   4982  CB  TRP B 172      69.030  68.186  63.305  1.00 17.44           C  
ANISOU 4982  CB  TRP B 172      783   2238   3605   -200    169   -109       C  
ATOM   4983  CG  TRP B 172      68.617  68.968  64.525  1.00 18.02           C  
ANISOU 4983  CG  TRP B 172      973   2413   3459    -24    -88   -203       C  
ATOM   4984  CD1 TRP B 172      68.290  68.467  65.761  1.00 20.43           C  
ANISOU 4984  CD1 TRP B 172     1231   2655   3874    -89     99   -378       C  
ATOM   4985  CD2 TRP B 172      68.487  70.391  64.624  1.00 18.19           C  
ANISOU 4985  CD2 TRP B 172      855   2363   3694    -59    -26   -196       C  
ATOM   4986  NE1 TRP B 172      67.974  69.499  66.619  1.00 18.60           N  
ANISOU 4986  NE1 TRP B 172      932   2702   3432    131     68   -342       N  
ATOM   4987  CE2 TRP B 172      68.093  70.688  65.948  1.00 19.43           C  
ANISOU 4987  CE2 TRP B 172     1096   2543   3743    172      6   -268       C  
ATOM   4988  CE3 TRP B 172      68.658  71.447  63.716  1.00 20.30           C  
ANISOU 4988  CE3 TRP B 172     1131   2532   4048    102     21    -57       C  
ATOM   4989  CZ2 TRP B 172      67.875  72.002  66.397  1.00 20.14           C  
ANISOU 4989  CZ2 TRP B 172     1380   2393   3876     61     57   -231       C  
ATOM   4990  CZ3 TRP B 172      68.439  72.762  64.162  1.00 20.56           C  
ANISOU 4990  CZ3 TRP B 172     1554   2403   3853    285    257   -207       C  
ATOM   4991  CH2 TRP B 172      68.045  73.021  65.494  1.00 21.74           C  
ANISOU 4991  CH2 TRP B 172     1677   2698   3883    184    232   -139       C  
ATOM   4992  N   TYR B 173      71.958  68.692  64.845  1.00 17.22           N  
ANISOU 4992  N   TYR B 173      998   2195   3348   -588     49   -107       N  
ATOM   4993  CA  TYR B 173      73.019  68.315  65.769  1.00 17.79           C  
ANISOU 4993  CA  TYR B 173     1149   2253   3354   -512     20   -128       C  
ATOM   4994  C   TYR B 173      72.490  68.524  67.183  1.00 18.16           C  
ANISOU 4994  C   TYR B 173     1274   2287   3336   -499    -10   -118       C  
ATOM   4995  O   TYR B 173      71.807  69.505  67.451  1.00 19.22           O  
ANISOU 4995  O   TYR B 173     1565   2373   3362   -384     -4   -125       O  
ATOM   4996  CB  TYR B 173      74.263  69.191  65.528  1.00 17.71           C  
ANISOU 4996  CB  TYR B 173     1218   2214   3296   -579     79   -183       C  
ATOM   4997  CG  TYR B 173      74.796  69.036  64.128  1.00 17.69           C  
ANISOU 4997  CG  TYR B 173     1127   2337   3257   -593    131   -121       C  
ATOM   4998  CD1 TYR B 173      74.228  69.753  63.073  1.00 17.25           C  
ANISOU 4998  CD1 TYR B 173      848   2454   3251   -206    198   -328       C  
ATOM   4999  CD2 TYR B 173      75.828  68.140  63.848  1.00 16.08           C  
ANISOU 4999  CD2 TYR B 173      837   2181   3089   -687     80   -161       C  
ATOM   5000  CE1 TYR B 173      74.687  69.596  61.774  1.00 17.37           C  
ANISOU 5000  CE1 TYR B 173      880   2602   3115   -290    343   -107       C  
ATOM   5001  CE2 TYR B 173      76.307  67.973  62.541  1.00 15.74           C  
ANISOU 5001  CE2 TYR B 173      474   2494   3010   -598    220    -65       C  
ATOM   5002  CZ  TYR B 173      75.716  68.697  61.516  1.00 16.59           C  
ANISOU 5002  CZ  TYR B 173      703   2593   3004   -105    368    -30       C  
ATOM   5003  OH  TYR B 173      76.149  68.543  60.217  1.00 16.16           O  
ANISOU 5003  OH  TYR B 173      815   2291   3033    504    -11   -283       O  
ATOM   5004  N   HIS B 174      72.788  67.614  68.098  1.00 18.41           N  
ANISOU 5004  N   HIS B 174     1268   2271   3454   -626    -78   -119       N  
ATOM   5005  CA  HIS B 174      72.410  67.834  69.489  1.00 18.39           C  
ANISOU 5005  CA  HIS B 174     1290   2217   3480   -629   -102   -183       C  
ATOM   5006  C   HIS B 174      73.322  68.777  70.253  1.00 19.62           C  
ANISOU 5006  C   HIS B 174     1535   2256   3661   -493   -105   -191       C  
ATOM   5007  O   HIS B 174      72.886  69.347  71.256  1.00 20.62           O  
ANISOU 5007  O   HIS B 174     1758   2463   3614   -541   -106   -317       O  
ATOM   5008  CB  HIS B 174      72.236  66.492  70.208  1.00 19.27           C  
ANISOU 5008  CB  HIS B 174     1499   2298   3525   -671   -115   -183       C  
ATOM   5009  CG  HIS B 174      71.071  65.710  69.676  1.00 18.85           C  
ANISOU 5009  CG  HIS B 174     1336   2231   3595   -810    -98   -195       C  
ATOM   5010  ND1 HIS B 174      70.766  64.431  70.088  1.00 18.17           N  
ANISOU 5010  ND1 HIS B 174     1570   1914   3417   -381   -125    -13       N  
ATOM   5011  CD2 HIS B 174      70.164  66.024  68.719  1.00 18.41           C  
ANISOU 5011  CD2 HIS B 174     1386   2136   3473   -440    -39   -253       C  
ATOM   5012  CE1 HIS B 174      69.696  64.004  69.437  1.00 19.89           C  
ANISOU 5012  CE1 HIS B 174     1578   2259   3717   -561   -122   -144       C  
ATOM   5013  NE2 HIS B 174      69.315  64.948  68.593  1.00 18.33           N  
ANISOU 5013  NE2 HIS B 174     1256   2132   3575   -679     26    -94       N  
ATOM   5014  N   THR B 175      74.562  68.936  69.791  1.00 19.04           N  
ANISOU 5014  N   THR B 175     1333   2158   3742   -390   -217    -88       N  
ATOM   5015  CA  THR B 175      75.491  69.898  70.369  1.00 19.28           C  
ANISOU 5015  CA  THR B 175     1253   2150   3921   -323   -281   -109       C  
ATOM   5016  C   THR B 175      75.550  71.110  69.454  1.00 19.41           C  
ANISOU 5016  C   THR B 175     1228   2202   3943   -288   -281   -167       C  
ATOM   5017  O   THR B 175      75.670  70.950  68.236  1.00 19.74           O  
ANISOU 5017  O   THR B 175     1347   2130   4022   -265   -163    -97       O  
ATOM   5018  CB  THR B 175      76.898  69.275  70.509  1.00 19.86           C  
ANISOU 5018  CB  THR B 175     1306   2242   3997   -382   -348    -10       C  
ATOM   5019  OG1 THR B 175      76.822  68.147  71.391  1.00 22.12           O  
ANISOU 5019  OG1 THR B 175     1644   2116   4642   -315   -293     70       O  
ATOM   5020  CG2 THR B 175      77.926  70.300  71.021  1.00 19.43           C  
ANISOU 5020  CG2 THR B 175     1205   2422   3755   -376   -482   -299       C  
ATOM   5021  N   ALA B 176      75.462  72.308  70.033  1.00 19.09           N  
ANISOU 5021  N   ALA B 176     1143   2130   3978   -293   -337   -249       N  
ATOM   5022  CA  ALA B 176      75.427  73.534  69.248  1.00 19.14           C  
ANISOU 5022  CA  ALA B 176     1337   2150   3785   -298   -238   -240       C  
ATOM   5023  C   ALA B 176      76.722  73.761  68.463  1.00 18.95           C  
ANISOU 5023  C   ALA B 176     1219   2211   3770   -295   -309   -306       C  
ATOM   5024  O   ALA B 176      77.783  73.226  68.808  1.00 18.71           O  
ANISOU 5024  O   ALA B 176     1300   2153   3653   -451   -355   -274       O  
ATOM   5025  CB  ALA B 176      75.126  74.736  70.141  1.00 19.67           C  
ANISOU 5025  CB  ALA B 176     1510   2095   3868   -189   -131   -192       C  
ATOM   5026  N   ALA B 177      76.601  74.511  67.371  1.00 18.61           N  
ANISOU 5026  N   ALA B 177     1182   2156   3731   -250   -311   -276       N  
ATOM   5027  CA  ALA B 177      77.682  74.679  66.400  1.00 19.90           C  
ANISOU 5027  CA  ALA B 177     1278   2489   3792   -130   -336   -287       C  
ATOM   5028  C   ALA B 177      78.975  75.189  67.027  1.00 20.38           C  
ANISOU 5028  C   ALA B 177     1296   2572   3874   -157   -355   -321       C  
ATOM   5029  O   ALA B 177      80.071  74.732  66.676  1.00 20.53           O  
ANISOU 5029  O   ALA B 177     1252   2679   3867    -44   -308   -307       O  
ATOM   5030  CB  ALA B 177      77.249  75.592  65.260  1.00 20.46           C  
ANISOU 5030  CB  ALA B 177     1338   2579   3855   -112   -311   -231       C  
ATOM   5031  N   ARG B 178      78.853  76.115  67.974  1.00 20.69           N  
ANISOU 5031  N   ARG B 178     1350   2547   3960   -154   -434   -377       N  
ATOM   5032  CA  ARG B 178      80.050  76.702  68.605  1.00 21.45           C  
ANISOU 5032  CA  ARG B 178     1439   2641   4070   -181   -437   -356       C  
ATOM   5033  C   ARG B 178      80.530  75.921  69.827  1.00 22.11           C  
ANISOU 5033  C   ARG B 178     1452   2730   4215   -174   -429   -311       C  
ATOM   5034  O   ARG B 178      81.567  76.252  70.415  1.00 22.10           O  
ANISOU 5034  O   ARG B 178     1402   2717   4275   -370   -539   -321       O  
ATOM   5035  CB  ARG B 178      79.815  78.184  68.950  1.00 21.41           C  
ANISOU 5035  CB  ARG B 178     1562   2522   4048   -216   -477   -346       C  
ATOM   5036  CG  ARG B 178      79.294  79.014  67.781  1.00 21.49           C  
ANISOU 5036  CG  ARG B 178     1555   2573   4034    -93   -422   -411       C  
ATOM   5037  CD  ARG B 178      79.206  80.519  68.100  1.00 21.95           C  
ANISOU 5037  CD  ARG B 178     1683   2587   4069   -515   -455   -520       C  
ATOM   5038  NE  ARG B 178      80.523  81.148  68.168  1.00 22.16           N  
ANISOU 5038  NE  ARG B 178     1753   2639   4026   -461   -608   -199       N  
ATOM   5039  CZ  ARG B 178      81.226  81.496  67.094  1.00 23.99           C  
ANISOU 5039  CZ  ARG B 178     1738   3108   4269   -608   -676   -148       C  
ATOM   5040  NH1 ARG B 178      80.750  81.278  65.869  1.00 23.23           N  
ANISOU 5040  NH1 ARG B 178     1877   2875   4072   -319   -692     59       N  
ATOM   5041  NH2 ARG B 178      82.404  82.075  67.246  1.00 24.60           N  
ANISOU 5041  NH2 ARG B 178     2050   3319   3978   -827  -1120     36       N  
ATOM   5042  N   LEU B 179      79.797  74.874  70.200  1.00 22.63           N  
ANISOU 5042  N   LEU B 179     1536   2751   4311   -154   -338   -226       N  
ATOM   5043  CA  LEU B 179      80.168  74.045  71.347  1.00 22.98           C  
ANISOU 5043  CA  LEU B 179     1586   2818   4325    -30   -222   -184       C  
ATOM   5044  C   LEU B 179      80.728  72.678  70.964  1.00 23.65           C  
ANISOU 5044  C   LEU B 179     1688   2881   4413     23   -186    -96       C  
ATOM   5045  O   LEU B 179      81.365  72.029  71.791  1.00 24.72           O  
ANISOU 5045  O   LEU B 179     1913   3024   4454    181   -281    -82       O  
ATOM   5046  CB  LEU B 179      78.982  73.834  72.294  1.00 22.87           C  
ANISOU 5046  CB  LEU B 179     1566   2769   4354    -77   -129   -201       C  
ATOM   5047  CG  LEU B 179      78.483  75.063  73.057  1.00 22.27           C  
ANISOU 5047  CG  LEU B 179     1360   2826   4276   -271   -240   -229       C  
ATOM   5048  CD1 LEU B 179      77.289  74.668  73.898  1.00 23.33           C  
ANISOU 5048  CD1 LEU B 179     1310   3073   4479   -113     13   -137       C  
ATOM   5049  CD2 LEU B 179      79.585  75.687  73.941  1.00 25.97           C  
ANISOU 5049  CD2 LEU B 179     1594   3601   4670   -605   -480   -199       C  
ATOM   5050  N   GLY B 180      80.510  72.231  69.732  1.00 22.93           N  
ANISOU 5050  N   GLY B 180     1505   2809   4396    -80   -134   -121       N  
ATOM   5051  CA  GLY B 180      81.031  70.922  69.340  1.00 23.11           C  
ANISOU 5051  CA  GLY B 180     1344   2954   4481    -60     93    -16       C  
ATOM   5052  C   GLY B 180      82.347  71.035  68.593  1.00 23.70           C  
ANISOU 5052  C   GLY B 180     1508   2982   4515    -58    176     66       C  
ATOM   5053  O   GLY B 180      83.050  72.050  68.708  1.00 23.78           O  
ANISOU 5053  O   GLY B 180     1351   3103   4581   -171    243     64       O  
ATOM   5054  N   PRO B 181      82.694  69.982  67.834  1.00 24.07           N  
ANISOU 5054  N   PRO B 181     1531   2982   4630    -24    272    136       N  
ATOM   5055  CA  PRO B 181      83.935  69.977  67.058  1.00 23.70           C  
ANISOU 5055  CA  PRO B 181     1504   2920   4580    -63    369    203       C  
ATOM   5056  C   PRO B 181      83.946  71.072  65.993  1.00 23.41           C  
ANISOU 5056  C   PRO B 181     1426   2840   4628    -75    248    219       C  
ATOM   5057  O   PRO B 181      82.890  71.458  65.474  1.00 23.18           O  
ANISOU 5057  O   PRO B 181     1399   2860   4545    -39    283    190       O  
ATOM   5058  CB  PRO B 181      83.906  68.611  66.356  1.00 23.78           C  
ANISOU 5058  CB  PRO B 181     1590   2850   4593   -108    443    216       C  
ATOM   5059  CG  PRO B 181      82.989  67.768  67.171  1.00 24.71           C  
ANISOU 5059  CG  PRO B 181     1648   3035   4703    -68    393    141       C  
ATOM   5060  CD  PRO B 181      81.937  68.728  67.670  1.00 23.16           C  
ANISOU 5060  CD  PRO B 181     1345   2867   4586    -24    278    113       C  
ATOM   5061  N   ARG B 182      85.143  71.534  65.650  1.00 22.81           N  
ANISOU 5061  N   ARG B 182     1266   2864   4535    -98    228    262       N  
ATOM   5062  CA  ARG B 182      85.334  72.478  64.552  1.00 22.84           C  
ANISOU 5062  CA  ARG B 182     1248   2818   4611   -194     91    293       C  
ATOM   5063  C   ARG B 182      84.846  71.856  63.246  1.00 22.78           C  
ANISOU 5063  C   ARG B 182     1231   2828   4597   -142     57    334       C  
ATOM   5064  O   ARG B 182      84.247  72.540  62.409  1.00 23.16           O  
ANISOU 5064  O   ARG B 182     1339   2742   4719    -87     25    434       O  
ATOM   5065  CB  ARG B 182      86.817  72.811  64.422  1.00 23.25           C  
ANISOU 5065  CB  ARG B 182     1202   2971   4660   -314    118    275       C  
ATOM   5066  CG  ARG B 182      87.165  73.825  63.341  1.00 23.31           C  
ANISOU 5066  CG  ARG B 182     1254   2939   4662   -335    -67    335       C  
ATOM   5067  CD  ARG B 182      88.607  74.306  63.527  1.00 24.59           C  
ANISOU 5067  CD  ARG B 182     1242   3171   4927   -760    258    233       C  
ATOM   5068  NE  ARG B 182      89.073  75.221  62.481  1.00 26.69           N  
ANISOU 5068  NE  ARG B 182     1854   3498   4788   -650    189    313       N  
ATOM   5069  CZ  ARG B 182      88.786  76.523  62.424  1.00 26.97           C  
ANISOU 5069  CZ  ARG B 182     1712   3809   4726   -435     73    227       C  
ATOM   5070  NH1 ARG B 182      87.981  77.086  63.318  1.00 26.91           N  
ANISOU 5070  NH1 ARG B 182     1579   3918   4727   -451    326    242       N  
ATOM   5071  NH2 ARG B 182      89.279  77.280  61.451  1.00 26.82           N  
ANISOU 5071  NH2 ARG B 182     1413   3754   5022   -597     21    239       N  
ATOM   5072  N   PHE B 183      85.081  70.552  63.098  1.00 21.77           N  
ANISOU 5072  N   PHE B 183     1070   2653   4548    -87     36    287       N  
ATOM   5073  CA  PHE B 183      84.610  69.816  61.934  1.00 21.95           C  
ANISOU 5073  CA  PHE B 183     1074   2667   4598   -162     87    296       C  
ATOM   5074  C   PHE B 183      83.822  68.588  62.369  1.00 22.10           C  
ANISOU 5074  C   PHE B 183     1038   2709   4650    -95    176    350       C  
ATOM   5075  O   PHE B 183      84.384  67.491  62.490  1.00 22.32           O  
ANISOU 5075  O   PHE B 183     1054   2768   4658   -164    215    360       O  
ATOM   5076  CB  PHE B 183      85.762  69.397  61.023  1.00 20.94           C  
ANISOU 5076  CB  PHE B 183      891   2552   4511   -110    102    275       C  
ATOM   5077  CG  PHE B 183      86.640  70.541  60.595  1.00 22.02           C  
ANISOU 5077  CG  PHE B 183     1255   2489   4619   -332    -99    186       C  
ATOM   5078  CD1 PHE B 183      86.142  71.556  59.785  1.00 22.12           C  
ANISOU 5078  CD1 PHE B 183     1387   2452   4565   -560   -241    167       C  
ATOM   5079  CD2 PHE B 183      87.962  70.601  60.995  1.00 22.41           C  
ANISOU 5079  CD2 PHE B 183     1297   2539   4679   -503    -18     53       C  
ATOM   5080  CE1 PHE B 183      86.950  72.617  59.395  1.00 21.82           C  
ANISOU 5080  CE1 PHE B 183     1153   2684   4453   -639   -263    123       C  
ATOM   5081  CE2 PHE B 183      88.782  71.664  60.609  1.00 23.20           C  
ANISOU 5081  CE2 PHE B 183     1452   2672   4688   -613   -118    194       C  
ATOM   5082  CZ  PHE B 183      88.281  72.663  59.804  1.00 23.11           C  
ANISOU 5082  CZ  PHE B 183     1224   2673   4883   -643   -365    193       C  
ATOM   5083  N   PRO B 184      82.512  68.764  62.592  1.00 23.01           N  
ANISOU 5083  N   PRO B 184     1193   2806   4744     -6    182    312       N  
ATOM   5084  CA  PRO B 184      81.694  67.635  63.016  1.00 23.17           C  
ANISOU 5084  CA  PRO B 184     1144   2809   4849    -40    235    302       C  
ATOM   5085  C   PRO B 184      81.847  66.459  62.059  1.00 24.54           C  
ANISOU 5085  C   PRO B 184     1312   3029   4980     15    231    284       C  
ATOM   5086  O   PRO B 184      81.891  66.651  60.843  1.00 23.64           O  
ANISOU 5086  O   PRO B 184     1218   3013   4748    101    255    316       O  
ATOM   5087  CB  PRO B 184      80.272  68.206  62.973  1.00 23.90           C  
ANISOU 5087  CB  PRO B 184     1343   2802   4936     94    168    264       C  
ATOM   5088  CG  PRO B 184      80.504  69.670  63.326  1.00 23.14           C  
ANISOU 5088  CG  PRO B 184     1197   2721   4871    -47    312    337       C  
ATOM   5089  CD  PRO B 184      81.745  70.022  62.557  1.00 21.91           C  
ANISOU 5089  CD  PRO B 184      955   2678   4691     88    202    328       C  
ATOM   5090  N   LEU B 185      81.941  65.259  62.626  1.00 25.27           N  
ANISOU 5090  N   LEU B 185     1338   3061   5201    -83    188    236       N  
ATOM   5091  CA  LEU B 185      82.153  64.047  61.851  1.00 26.59           C  
ANISOU 5091  CA  LEU B 185     1496   3224   5382   -154    179    190       C  
ATOM   5092  C   LEU B 185      80.835  63.307  61.610  1.00 26.58           C  
ANISOU 5092  C   LEU B 185     1605   3137   5356   -193    255    119       C  
ATOM   5093  O   LEU B 185      80.845  62.151  61.195  1.00 27.92           O  
ANISOU 5093  O   LEU B 185     1961   3304   5342   -253    427    169       O  
ATOM   5094  CB  LEU B 185      83.198  63.157  62.534  1.00 27.11           C  
ANISOU 5094  CB  LEU B 185     1515   3259   5524   -104    177    171       C  
ATOM   5095  CG  LEU B 185      84.593  63.783  62.713  1.00 29.23           C  
ANISOU 5095  CG  LEU B 185     1578   3772   5753   -214    -10    339       C  
ATOM   5096  CD1 LEU B 185      85.559  62.895  63.521  1.00 32.04           C  
ANISOU 5096  CD1 LEU B 185     2065   3824   6283    184    176    463       C  
ATOM   5097  CD2 LEU B 185      85.221  64.150  61.366  1.00 31.73           C  
ANISOU 5097  CD2 LEU B 185     1898   4264   5891   -270    102    247       C  
ATOM   5098  N   GLY B 186      79.710  63.971  61.865  1.00 26.29           N  
ANISOU 5098  N   GLY B 186     1518   3076   5396   -182    174     68       N  
ATOM   5099  CA  GLY B 186      78.397  63.433  61.508  1.00 26.19           C  
ANISOU 5099  CA  GLY B 186     1672   3070   5208    -76    193    -94       C  
ATOM   5100  C   GLY B 186      77.289  64.162  62.246  1.00 25.08           C  
ANISOU 5100  C   GLY B 186     1549   2883   5094    -41     94   -144       C  
ATOM   5101  O   GLY B 186      77.551  64.815  63.251  1.00 25.54           O  
ANISOU 5101  O   GLY B 186     1666   2810   5227    198    170   -181       O  
ATOM   5102  N   SER B 187      76.054  64.015  61.788  1.00 24.45           N  
ANISOU 5102  N   SER B 187     1742   2765   4781   -166     17    -97       N  
ATOM   5103  CA  SER B 187      74.925  64.677  62.440  1.00 22.73           C  
ANISOU 5103  CA  SER B 187     1544   2612   4479   -348    -53   -105       C  
ATOM   5104  C   SER B 187      74.129  63.711  63.313  1.00 21.83           C  
ANISOU 5104  C   SER B 187     1498   2483   4313   -266    -90   -103       C  
ATOM   5105  O   SER B 187      74.338  62.503  63.257  1.00 21.40           O  
ANISOU 5105  O   SER B 187     1347   2491   4291   -361     23   -165       O  
ATOM   5106  CB  SER B 187      74.018  65.298  61.388  1.00 23.24           C  
ANISOU 5106  CB  SER B 187     1867   2596   4366   -449    -40     24       C  
ATOM   5107  OG  SER B 187      73.506  64.271  60.552  1.00 26.04           O  
ANISOU 5107  OG  SER B 187     2428   3114   4352  -1040   -234    210       O  
ATOM   5108  N   ASP B 188      73.223  64.229  64.135  1.00 20.68           N  
ANISOU 5108  N   ASP B 188     1275   2332   4251   -257   -210    -95       N  
ATOM   5109  CA  ASP B 188      72.438  63.357  65.000  1.00 20.92           C  
ANISOU 5109  CA  ASP B 188     1364   2368   4213   -244   -282   -103       C  
ATOM   5110  C   ASP B 188      71.081  62.978  64.431  1.00 20.57           C  
ANISOU 5110  C   ASP B 188     1340   2327   4149   -322   -294   -164       C  
ATOM   5111  O   ASP B 188      70.471  62.006  64.888  1.00 20.86           O  
ANISOU 5111  O   ASP B 188     1412   2351   4162   -342   -232   -165       O  
ATOM   5112  CB  ASP B 188      72.280  63.947  66.400  1.00 20.59           C  
ANISOU 5112  CB  ASP B 188     1420   2274   4129   -280   -401   -102       C  
ATOM   5113  CG  ASP B 188      73.616  64.130  67.077  1.00 21.86           C  
ANISOU 5113  CG  ASP B 188     1508   2503   4292   -246   -515   -101       C  
ATOM   5114  OD1 ASP B 188      74.365  63.131  67.143  1.00 23.47           O  
ANISOU 5114  OD1 ASP B 188     1644   2623   4649   -228  -1018   -171       O  
ATOM   5115  OD2 ASP B 188      73.934  65.270  67.484  1.00 22.30           O  
ANISOU 5115  OD2 ASP B 188     1574   2754   4143   -466   -464    -67       O  
ATOM   5116  N   SER B 189      70.590  63.749  63.467  1.00 19.89           N  
ANISOU 5116  N   SER B 189     1139   2243   4175   -254   -228   -193       N  
ATOM   5117  CA  SER B 189      69.380  63.336  62.767  1.00 19.77           C  
ANISOU 5117  CA  SER B 189     1043   2259   4207   -156   -192   -153       C  
ATOM   5118  C   SER B 189      69.293  64.086  61.445  1.00 19.51           C  
ANISOU 5118  C   SER B 189     1003   2223   4185    -90   -198   -179       C  
ATOM   5119  O   SER B 189      69.973  65.099  61.241  1.00 18.93           O  
ANISOU 5119  O   SER B 189      984   2189   4016   -147   -191    -78       O  
ATOM   5120  CB  SER B 189      68.144  63.577  63.646  1.00 19.80           C  
ANISOU 5120  CB  SER B 189     1070   2185   4266   -184   -128   -266       C  
ATOM   5121  OG  SER B 189      68.026  64.958  63.938  1.00 21.03           O  
ANISOU 5121  OG  SER B 189     1154   2631   4203   -286   -142   -211       O  
ATOM   5122  N   THR B 190      68.468  63.556  60.551  1.00 18.50           N  
ANISOU 5122  N   THR B 190      766   2091   4171    -65   -213   -183       N  
ATOM   5123  CA  THR B 190      68.094  64.243  59.323  1.00 17.89           C  
ANISOU 5123  CA  THR B 190      647   2020   4129     59   -142   -160       C  
ATOM   5124  C   THR B 190      66.645  64.673  59.537  1.00 17.57           C  
ANISOU 5124  C   THR B 190      643   1884   4146    107   -136   -303       C  
ATOM   5125  O   THR B 190      65.805  63.856  59.936  1.00 17.65           O  
ANISOU 5125  O   THR B 190      640   1832   4232     69    -84   -352       O  
ATOM   5126  CB  THR B 190      68.167  63.290  58.104  1.00 17.64           C  
ANISOU 5126  CB  THR B 190      590   2008   4104    114   -173   -164       C  
ATOM   5127  OG1 THR B 190      69.508  62.793  57.934  1.00 17.88           O  
ANISOU 5127  OG1 THR B 190      576   2268   3948    -97    -32    -63       O  
ATOM   5128  CG2 THR B 190      67.696  63.983  56.815  1.00 18.45           C  
ANISOU 5128  CG2 THR B 190      829   2128   4053     40    -95    -32       C  
ATOM   5129  N   LEU B 191      66.349  65.938  59.243  1.00 17.34           N  
ANISOU 5129  N   LEU B 191      620   1893   4072    184   -250   -370       N  
ATOM   5130  CA  LEU B 191      64.986  66.455  59.375  1.00 18.00           C  
ANISOU 5130  CA  LEU B 191      701   1967   4170    148   -350   -397       C  
ATOM   5131  C   LEU B 191      64.435  66.658  57.973  1.00 18.43           C  
ANISOU 5131  C   LEU B 191      720   2029   4251    196   -374   -362       C  
ATOM   5132  O   LEU B 191      65.113  67.229  57.107  1.00 18.55           O  
ANISOU 5132  O   LEU B 191      731   2028   4285    136   -342   -237       O  
ATOM   5133  CB  LEU B 191      64.968  67.787  60.131  1.00 18.20           C  
ANISOU 5133  CB  LEU B 191      821   1949   4145    167   -303   -359       C  
ATOM   5134  CG  LEU B 191      65.685  67.819  61.485  1.00 18.61           C  
ANISOU 5134  CG  LEU B 191      978   1924   4165   -149   -416   -391       C  
ATOM   5135  CD1 LEU B 191      65.604  69.237  62.055  1.00 20.34           C  
ANISOU 5135  CD1 LEU B 191     1369   1935   4421    178   -455   -292       C  
ATOM   5136  CD2 LEU B 191      65.099  66.777  62.472  1.00 19.50           C  
ANISOU 5136  CD2 LEU B 191     1275   2138   3993    -84   -416   -240       C  
ATOM   5137  N   ILE B 192      63.241  66.124  57.741  1.00 17.91           N  
ANISOU 5137  N   ILE B 192      444   2130   4230    246   -424   -424       N  
ATOM   5138  CA  ILE B 192      62.561  66.326  56.467  1.00 18.75           C  
ANISOU 5138  CA  ILE B 192      602   2176   4344    310   -508   -346       C  
ATOM   5139  C   ILE B 192      61.320  67.147  56.824  1.00 19.24           C  
ANISOU 5139  C   ILE B 192      585   2321   4403    338   -490   -382       C  
ATOM   5140  O   ILE B 192      60.534  66.743  57.686  1.00 19.10           O  
ANISOU 5140  O   ILE B 192      604   2283   4368    431   -518   -349       O  
ATOM   5141  CB  ILE B 192      62.197  64.998  55.748  1.00 19.11           C  
ANISOU 5141  CB  ILE B 192      669   2294   4297    361   -599   -389       C  
ATOM   5142  CG1 ILE B 192      63.460  64.193  55.390  1.00 18.63           C  
ANISOU 5142  CG1 ILE B 192      750   2010   4317    281   -417   -435       C  
ATOM   5143  CG2 ILE B 192      61.278  65.255  54.526  1.00 20.67           C  
ANISOU 5143  CG2 ILE B 192      835   2563   4454     37   -766   -389       C  
ATOM   5144  CD1 ILE B 192      63.175  62.742  54.965  1.00 19.66           C  
ANISOU 5144  CD1 ILE B 192      978   2160   4328    458   -466   -710       C  
ATOM   5145  N   ASN B 193      61.176  68.309  56.191  1.00 19.43           N  
ANISOU 5145  N   ASN B 193      609   2282   4492    336   -465   -330       N  
ATOM   5146  CA  ASN B 193      60.143  69.268  56.595  1.00 20.04           C  
ANISOU 5146  CA  ASN B 193      519   2515   4579    307   -314   -301       C  
ATOM   5147  C   ASN B 193      60.151  69.447  58.109  1.00 20.55           C  
ANISOU 5147  C   ASN B 193      617   2551   4638    256   -272   -283       C  
ATOM   5148  O   ASN B 193      59.101  69.433  58.771  1.00 21.14           O  
ANISOU 5148  O   ASN B 193      540   2753   4740    406   -100   -321       O  
ATOM   5149  CB  ASN B 193      58.755  68.822  56.111  1.00 20.79           C  
ANISOU 5149  CB  ASN B 193      572   2641   4687    336   -398   -261       C  
ATOM   5150  CG  ASN B 193      58.629  68.885  54.601  1.00 22.41           C  
ANISOU 5150  CG  ASN B 193      815   2884   4813    245   -405   -198       C  
ATOM   5151  OD1 ASN B 193      59.487  69.469  53.931  1.00 24.37           O  
ANISOU 5151  OD1 ASN B 193     1079   3102   5078     -4   -563    123       O  
ATOM   5152  ND2 ASN B 193      57.582  68.269  54.055  1.00 23.61           N  
ANISOU 5152  ND2 ASN B 193     1185   2572   5211    114   -442   -244       N  
ATOM   5153  N   GLY B 194      61.350  69.548  58.667  1.00 19.89           N  
ANISOU 5153  N   GLY B 194      617   2398   4541    230   -202   -225       N  
ATOM   5154  CA  GLY B 194      61.480  69.932  60.069  1.00 20.46           C  
ANISOU 5154  CA  GLY B 194      920   2263   4589     65   -183   -236       C  
ATOM   5155  C   GLY B 194      61.376  68.823  61.102  1.00 19.95           C  
ANISOU 5155  C   GLY B 194      773   2208   4598     -5   -106   -208       C  
ATOM   5156  O   GLY B 194      61.514  69.089  62.289  1.00 20.25           O  
ANISOU 5156  O   GLY B 194      963   2143   4585    -80   -211   -193       O  
ATOM   5157  N   LEU B 195      61.121  67.591  60.672  1.00 19.94           N  
ANISOU 5157  N   LEU B 195      679   2213   4685     58    -69   -246       N  
ATOM   5158  CA  LEU B 195      60.924  66.475  61.597  1.00 19.11           C  
ANISOU 5158  CA  LEU B 195      456   2083   4719     28    -11   -213       C  
ATOM   5159  C   LEU B 195      61.755  65.273  61.203  1.00 19.26           C  
ANISOU 5159  C   LEU B 195      490   2073   4754     86    -60   -153       C  
ATOM   5160  O   LEU B 195      61.992  65.025  60.024  1.00 19.20           O  
ANISOU 5160  O   LEU B 195      622   2007   4665     23    -89    -99       O  
ATOM   5161  CB  LEU B 195      59.457  66.008  61.602  1.00 19.18           C  
ANISOU 5161  CB  LEU B 195      299   2169   4817    132    -59   -300       C  
ATOM   5162  CG  LEU B 195      58.429  67.054  62.005  1.00 19.54           C  
ANISOU 5162  CG  LEU B 195      291   2281   4851      3    113   -371       C  
ATOM   5163  CD1 LEU B 195      57.030  66.487  61.797  1.00 20.76           C  
ANISOU 5163  CD1 LEU B 195      312   2464   5111   -222     81   -394       C  
ATOM   5164  CD2 LEU B 195      58.698  67.455  63.454  1.00 22.09           C  
ANISOU 5164  CD2 LEU B 195      642   2772   4977   -334    134   -403       C  
ATOM   5165  N   GLY B 196      62.159  64.487  62.190  1.00 19.51           N  
ANISOU 5165  N   GLY B 196      592   2098   4723     85    -85   -106       N  
ATOM   5166  CA  GLY B 196      62.816  63.225  61.845  1.00 19.73           C  
ANISOU 5166  CA  GLY B 196      578   2103   4815     48    -98    -56       C  
ATOM   5167  C   GLY B 196      63.228  62.455  63.077  1.00 20.40           C  
ANISOU 5167  C   GLY B 196      738   2184   4826    -21    -12      5       C  
ATOM   5168  O   GLY B 196      63.120  62.951  64.197  1.00 21.82           O  
ANISOU 5168  O   GLY B 196     1014   2397   4879    -74    -37     -1       O  
ATOM   5169  N   ARG B 197      63.711  61.237  62.876  1.00 20.35           N  
ANISOU 5169  N   ARG B 197      745   2120   4864    -47    -31     43       N  
ATOM   5170  CA  ARG B 197      64.105  60.403  64.008  1.00 19.79           C  
ANISOU 5170  CA  ARG B 197      623   2162   4731   -110    -78     84       C  
ATOM   5171  C   ARG B 197      65.596  60.504  64.311  1.00 19.74           C  
ANISOU 5171  C   ARG B 197      727   2081   4693    -84   -123    -22       C  
ATOM   5172  O   ARG B 197      66.407  60.577  63.388  1.00 19.28           O  
ANISOU 5172  O   ARG B 197      699   1981   4643   -121    -97    -84       O  
ATOM   5173  CB  ARG B 197      63.685  58.961  63.741  1.00 19.40           C  
ANISOU 5173  CB  ARG B 197      393   2164   4812   -214   -109    117       C  
ATOM   5174  CG  ARG B 197      62.156  58.877  63.790  1.00 21.01           C  
ANISOU 5174  CG  ARG B 197      415   2525   5042   -295    114    356       C  
ATOM   5175  CD  ARG B 197      61.650  57.578  64.353  1.00 22.56           C  
ANISOU 5175  CD  ARG B 197      623   2281   5665   -472     15    170       C  
ATOM   5176  NE  ARG B 197      60.191  57.593  64.531  1.00 22.00           N  
ANISOU 5176  NE  ARG B 197      427   2320   5611   -495     42    155       N  
ATOM   5177  CZ  ARG B 197      59.366  56.731  63.950  1.00 22.69           C  
ANISOU 5177  CZ  ARG B 197      352   2456   5810   -288      1    255       C  
ATOM   5178  NH1 ARG B 197      59.881  55.792  63.158  1.00 23.52           N  
ANISOU 5178  NH1 ARG B 197     1016   2119   5801   -288    -22    236       N  
ATOM   5179  NH2 ARG B 197      58.048  56.793  64.179  1.00 22.62           N  
ANISOU 5179  NH2 ARG B 197      329   2627   5637   -228    214    316       N  
ATOM   5180  N   SER B 198      65.936  60.517  65.598  1.00 20.08           N  
ANISOU 5180  N   SER B 198      922   2134   4572      1   -148    -61       N  
ATOM   5181  CA  SER B 198      67.326  60.555  66.040  1.00 21.52           C  
ANISOU 5181  CA  SER B 198     1265   2240   4672    -27   -272    -67       C  
ATOM   5182  C   SER B 198      67.737  59.175  66.553  1.00 22.10           C  
ANISOU 5182  C   SER B 198     1373   2379   4643    -32   -198    -44       C  
ATOM   5183  O   SER B 198      67.132  58.661  67.505  1.00 22.37           O  
ANISOU 5183  O   SER B 198     1404   2441   4655   -144   -160    -60       O  
ATOM   5184  CB  SER B 198      67.517  61.574  67.164  1.00 21.47           C  
ANISOU 5184  CB  SER B 198     1309   2217   4630    -51   -300    -36       C  
ATOM   5185  OG  SER B 198      68.848  61.496  67.659  1.00 24.07           O  
ANISOU 5185  OG  SER B 198     1678   2441   5024    103   -596    -93       O  
ATOM   5186  N   ALA B 199      68.745  58.580  65.919  1.00 21.50           N  
ANISOU 5186  N   ALA B 199     1148   2474   4544    -45   -175   -102       N  
ATOM   5187  CA  ALA B 199      69.224  57.256  66.337  1.00 23.34           C  
ANISOU 5187  CA  ALA B 199     1481   2785   4600     77    -80     10       C  
ATOM   5188  C   ALA B 199      69.809  57.327  67.753  1.00 23.98           C  
ANISOU 5188  C   ALA B 199     1584   2880   4645     71    -58     84       C  
ATOM   5189  O   ALA B 199      69.532  56.474  68.594  1.00 25.07           O  
ANISOU 5189  O   ALA B 199     1775   2996   4753    115     76    170       O  
ATOM   5190  CB  ALA B 199      70.274  56.721  65.355  1.00 22.48           C  
ANISOU 5190  CB  ALA B 199     1329   2631   4580     70    -43    -53       C  
ATOM   5191  N   THR B 200      70.570  58.374  68.039  1.00 24.59           N  
ANISOU 5191  N   THR B 200     1622   3040   4679      1    -94     81       N  
ATOM   5192  CA  THR B 200      71.314  58.424  69.300  1.00 25.93           C  
ANISOU 5192  CA  THR B 200     1865   3221   4765   -101   -109     95       C  
ATOM   5193  C   THR B 200      70.439  58.600  70.549  1.00 25.68           C  
ANISOU 5193  C   THR B 200     1876   3128   4752   -112   -110    141       C  
ATOM   5194  O   THR B 200      70.805  58.129  71.634  1.00 26.33           O  
ANISOU 5194  O   THR B 200     2013   3216   4776    -85   -222    133       O  
ATOM   5195  CB  THR B 200      72.469  59.448  69.237  1.00 26.88           C  
ANISOU 5195  CB  THR B 200     1942   3372   4898   -116   -188     72       C  
ATOM   5196  OG1 THR B 200      73.320  59.273  70.377  1.00 29.36           O  
ANISOU 5196  OG1 THR B 200     2276   3852   5027   -132   -297    121       O  
ATOM   5197  CG2 THR B 200      71.964  60.881  69.174  1.00 26.73           C  
ANISOU 5197  CG2 THR B 200     2006   3149   5001   -121   -230     49       C  
ATOM   5198  N   THR B 201      69.275  59.229  70.389  1.00 23.89           N  
ANISOU 5198  N   THR B 201     1583   2830   4663   -184      0    154       N  
ATOM   5199  CA  THR B 201      68.357  59.387  71.511  1.00 24.07           C  
ANISOU 5199  CA  THR B 201     1608   2829   4707   -207     59    217       C  
ATOM   5200  C   THR B 201      67.122  58.491  71.435  1.00 24.07           C  
ANISOU 5200  C   THR B 201     1600   2862   4681   -256    161    253       C  
ATOM   5201  O   THR B 201      66.348  58.429  72.402  1.00 24.38           O  
ANISOU 5201  O   THR B 201     1541   2932   4789   -297    271    309       O  
ATOM   5202  CB  THR B 201      67.902  60.857  71.699  1.00 24.28           C  
ANISOU 5202  CB  THR B 201     1674   2827   4720   -159     34    198       C  
ATOM   5203  OG1 THR B 201      67.426  61.392  70.454  1.00 23.62           O  
ANISOU 5203  OG1 THR B 201     1247   2833   4893     72    -27    240       O  
ATOM   5204  CG2 THR B 201      69.067  61.704  72.209  1.00 23.56           C  
ANISOU 5204  CG2 THR B 201     1492   2773   4683   -352    105    167       C  
ATOM   5205  N   ALA B 202      66.951  57.803  70.307  1.00 23.65           N  
ANISOU 5205  N   ALA B 202     1554   2756   4676   -261    249    248       N  
ATOM   5206  CA  ALA B 202      65.790  56.935  70.075  1.00 23.50           C  
ANISOU 5206  CA  ALA B 202     1632   2697   4600   -262    216    272       C  
ATOM   5207  C   ALA B 202      64.478  57.715  70.195  1.00 23.43           C  
ANISOU 5207  C   ALA B 202     1630   2730   4542   -247    244    290       C  
ATOM   5208  O   ALA B 202      63.503  57.247  70.803  1.00 23.41           O  
ANISOU 5208  O   ALA B 202     1685   2710   4497   -285    237    433       O  
ATOM   5209  CB  ALA B 202      65.817  55.734  71.030  1.00 23.30           C  
ANISOU 5209  CB  ALA B 202     1674   2664   4515   -259    265    258       C  
ATOM   5210  N   THR B 203      64.457  58.918  69.616  1.00 22.16           N  
ANISOU 5210  N   THR B 203     1485   2616   4317   -209    225    259       N  
ATOM   5211  CA  THR B 203      63.304  59.806  69.716  1.00 21.94           C  
ANISOU 5211  CA  THR B 203     1541   2591   4204   -104    179    149       C  
ATOM   5212  C   THR B 203      62.911  60.332  68.339  1.00 21.08           C  
ANISOU 5212  C   THR B 203     1324   2468   4217   -111    214    114       C  
ATOM   5213  O   THR B 203      63.652  60.160  67.364  1.00 20.13           O  
ANISOU 5213  O   THR B 203     1174   2380   4093     44    308     94       O  
ATOM   5214  CB  THR B 203      63.606  61.046  70.600  1.00 21.97           C  
ANISOU 5214  CB  THR B 203     1573   2573   4198   -160    211    185       C  
ATOM   5215  OG1 THR B 203      64.780  61.723  70.119  1.00 21.29           O  
ANISOU 5215  OG1 THR B 203     1192   2654   4243   -153    139     98       O  
ATOM   5216  CG2 THR B 203      63.806  60.648  72.065  1.00 24.28           C  
ANISOU 5216  CG2 THR B 203     2082   2961   4182      7    201    185       C  
ATOM   5217  N   GLY B 204      61.750  60.978  68.271  1.00 19.89           N  
ANISOU 5217  N   GLY B 204      920   2401   4234   -151    245     27       N  
ATOM   5218  CA  GLY B 204      61.386  61.715  67.071  1.00 21.18           C  
ANISOU 5218  CA  GLY B 204     1014   2539   4492    -87    213     30       C  
ATOM   5219  C   GLY B 204      60.209  61.174  66.287  1.00 21.82           C  
ANISOU 5219  C   GLY B 204      934   2645   4710   -117    243      3       C  
ATOM   5220  O   GLY B 204      59.873  59.978  66.340  1.00 22.34           O  
ANISOU 5220  O   GLY B 204     1024   2740   4721    -40    266     65       O  
ATOM   5221  N   ASP B 205      59.588  62.081  65.544  1.00 22.27           N  
ANISOU 5221  N   ASP B 205      900   2710   4852   -102    186    -50       N  
ATOM   5222  CA  ASP B 205      58.437  61.754  64.716  1.00 23.35           C  
ANISOU 5222  CA  ASP B 205      899   2836   5134   -134    126   -149       C  
ATOM   5223  C   ASP B 205      58.789  61.868  63.238  1.00 22.99           C  
ANISOU 5223  C   ASP B 205      756   2808   5168   -199     46   -169       C  
ATOM   5224  O   ASP B 205      59.861  62.344  62.863  1.00 23.51           O  
ANISOU 5224  O   ASP B 205      860   2915   5155   -336    -48   -104       O  
ATOM   5225  CB  ASP B 205      57.227  62.635  65.079  1.00 23.83           C  
ANISOU 5225  CB  ASP B 205      981   2954   5118    -52    183   -170       C  
ATOM   5226  CG  ASP B 205      56.734  62.394  66.505  1.00 26.38           C  
ANISOU 5226  CG  ASP B 205     1550   3195   5276    -97    282   -144       C  
ATOM   5227  OD1 ASP B 205      56.722  61.235  66.978  1.00 27.07           O  
ANISOU 5227  OD1 ASP B 205     1962   3192   5130     45    406   -131       O  
ATOM   5228  OD2 ASP B 205      56.343  63.381  67.167  1.00 29.34           O  
ANISOU 5228  OD2 ASP B 205     2229   3538   5378   -152    494   -112       O  
ATOM   5229  N   LEU B 206      57.882  61.399  62.395  1.00 23.10           N  
ANISOU 5229  N   LEU B 206      684   2774   5318   -315    -24   -316       N  
ATOM   5230  CA  LEU B 206      58.067  61.432  60.955  1.00 22.80           C  
ANISOU 5230  CA  LEU B 206      585   2603   5473   -251    -49   -381       C  
ATOM   5231  C   LEU B 206      57.130  62.471  60.335  1.00 22.84           C  
ANISOU 5231  C   LEU B 206      552   2518   5606   -244   -117   -486       C  
ATOM   5232  O   LEU B 206      55.932  62.520  60.638  1.00 23.50           O  
ANISOU 5232  O   LEU B 206      720   2633   5576   -366    -57   -565       O  
ATOM   5233  CB  LEU B 206      57.754  60.045  60.388  1.00 22.41           C  
ANISOU 5233  CB  LEU B 206      514   2491   5510   -147    -27   -446       C  
ATOM   5234  CG  LEU B 206      58.614  58.860  60.868  1.00 22.07           C  
ANISOU 5234  CG  LEU B 206      446   2445   5492   -336     10   -304       C  
ATOM   5235  CD1 LEU B 206      57.934  57.543  60.480  1.00 23.14           C  
ANISOU 5235  CD1 LEU B 206      766   2524   5500   -385     56    -76       C  
ATOM   5236  CD2 LEU B 206      59.993  58.938  60.244  1.00 24.33           C  
ANISOU 5236  CD2 LEU B 206      297   2934   6011    106    128   -276       C  
ATOM   5237  N   ALA B 207      57.679  63.287  59.445  1.00 22.64           N  
ANISOU 5237  N   ALA B 207      544   2348   5709   -291   -257   -498       N  
ATOM   5238  CA  ALA B 207      56.891  64.180  58.609  1.00 23.16           C  
ANISOU 5238  CA  ALA B 207      481   2385   5932   -237   -348   -502       C  
ATOM   5239  C   ALA B 207      56.004  63.346  57.684  1.00 23.53           C  
ANISOU 5239  C   ALA B 207      599   2315   6026   -193   -438   -538       C  
ATOM   5240  O   ALA B 207      56.405  62.262  57.252  1.00 23.21           O  
ANISOU 5240  O   ALA B 207      572   2267   5979     21   -472   -477       O  
ATOM   5241  CB  ALA B 207      57.798  65.061  57.777  1.00 22.96           C  
ANISOU 5241  CB  ALA B 207      519   2294   5909   -343   -365   -469       C  
ATOM   5242  N   VAL B 208      54.818  63.877  57.390  1.00 24.13           N  
ANISOU 5242  N   VAL B 208      593   2346   6228   -153   -535   -538       N  
ATOM   5243  CA  VAL B 208      53.873  63.274  56.453  1.00 24.99           C  
ANISOU 5243  CA  VAL B 208      640   2361   6492   -130   -624   -529       C  
ATOM   5244  C   VAL B 208      53.647  64.248  55.304  1.00 25.75           C  
ANISOU 5244  C   VAL B 208      712   2397   6674    -23   -713   -523       C  
ATOM   5245  O   VAL B 208      53.341  65.421  55.528  1.00 25.91           O  
ANISOU 5245  O   VAL B 208      801   2302   6740    117   -590   -381       O  
ATOM   5246  CB  VAL B 208      52.536  62.921  57.131  1.00 24.87           C  
ANISOU 5246  CB  VAL B 208      605   2405   6438   -123   -626   -548       C  
ATOM   5247  CG1 VAL B 208      51.553  62.315  56.109  1.00 25.73           C  
ANISOU 5247  CG1 VAL B 208      595   2602   6576   -420   -504   -605       C  
ATOM   5248  CG2 VAL B 208      52.779  61.912  58.259  1.00 26.08           C  
ANISOU 5248  CG2 VAL B 208      935   2542   6431   -155   -617   -501       C  
ATOM   5249  N   ILE B 209      53.840  63.769  54.081  1.00 26.60           N  
ANISOU 5249  N   ILE B 209      815   2435   6855     43   -864   -582       N  
ATOM   5250  CA  ILE B 209      53.587  64.551  52.880  1.00 27.78           C  
ANISOU 5250  CA  ILE B 209      905   2620   7030     57  -1063   -596       C  
ATOM   5251  C   ILE B 209      52.369  63.919  52.202  1.00 29.25           C  
ANISOU 5251  C   ILE B 209     1136   2703   7274     86  -1202   -594       C  
ATOM   5252  O   ILE B 209      52.403  62.757  51.802  1.00 28.95           O  
ANISOU 5252  O   ILE B 209     1167   2610   7220    236  -1186   -492       O  
ATOM   5253  CB  ILE B 209      54.828  64.523  51.954  1.00 27.53           C  
ANISOU 5253  CB  ILE B 209      913   2557   6987     31  -1091   -654       C  
ATOM   5254  CG1 ILE B 209      56.046  65.133  52.653  1.00 27.05           C  
ANISOU 5254  CG1 ILE B 209      668   2705   6903    126  -1022   -652       C  
ATOM   5255  CG2 ILE B 209      54.546  65.263  50.656  1.00 29.55           C  
ANISOU 5255  CG2 ILE B 209     1312   2840   7075     -3  -1061   -517       C  
ATOM   5256  CD1 ILE B 209      57.367  64.897  51.920  1.00 27.25           C  
ANISOU 5256  CD1 ILE B 209      931   2846   6576     79   -902   -590       C  
ATOM   5257  N   LYS B 210      51.285  64.678  52.059  1.00 30.46           N  
ANISOU 5257  N   LYS B 210     1108   2919   7546     91  -1336   -657       N  
ATOM   5258  CA  LYS B 210      50.043  64.082  51.577  1.00 33.25           C  
ANISOU 5258  CA  LYS B 210     1549   3145   7939     80  -1598   -667       C  
ATOM   5259  C   LYS B 210      49.901  64.241  50.079  1.00 34.15           C  
ANISOU 5259  C   LYS B 210     1698   3161   8116      5  -1803   -691       C  
ATOM   5260  O   LYS B 210      50.257  65.279  49.511  1.00 34.68           O  
ANISOU 5260  O   LYS B 210     1972   3182   8021    -88  -1941   -680       O  
ATOM   5261  CB  LYS B 210      48.829  64.733  52.221  1.00 33.41           C  
ANISOU 5261  CB  LYS B 210     1489   3226   7980    136  -1492   -691       C  
ATOM   5262  CG  LYS B 210      48.705  64.558  53.712  1.00 36.16           C  
ANISOU 5262  CG  LYS B 210     1853   3791   8093    187  -1408   -618       C  
ATOM   5263  CD  LYS B 210      47.645  65.557  54.183  1.00 40.58           C  
ANISOU 5263  CD  LYS B 210     2368   4584   8464    306   -983   -677       C  
ATOM   5264  CE  LYS B 210      47.069  65.189  55.535  1.00 43.15           C  
ANISOU 5264  CE  LYS B 210     2859   5044   8491    232  -1048   -531       C  
ATOM   5265  NZ  LYS B 210      48.133  64.648  56.420  1.00 44.18           N  
ANISOU 5265  NZ  LYS B 210     2815   5248   8720    488  -1009   -602       N  
ATOM   5266  N   VAL B 211      49.357  63.206  49.452  1.00 34.87           N  
ANISOU 5266  N   VAL B 211     1614   3135   8500      2  -1999   -661       N  
ATOM   5267  CA  VAL B 211      49.040  63.276  48.040  1.00 35.47           C  
ANISOU 5267  CA  VAL B 211     1554   3182   8738     69  -2249   -666       C  
ATOM   5268  C   VAL B 211      47.691  62.618  47.816  1.00 36.32           C  
ANISOU 5268  C   VAL B 211     1597   3208   8994     79  -2378   -678       C  
ATOM   5269  O   VAL B 211      47.232  61.804  48.622  1.00 36.25           O  
ANISOU 5269  O   VAL B 211     1418   3351   9003    191  -2433   -627       O  
ATOM   5270  CB  VAL B 211      50.126  62.653  47.134  1.00 35.39           C  
ANISOU 5270  CB  VAL B 211     1525   3127   8792     47  -2188   -644       C  
ATOM   5271  CG1 VAL B 211      51.389  63.515  47.140  1.00 34.76           C  
ANISOU 5271  CG1 VAL B 211     1452   3103   8651     82  -2301   -684       C  
ATOM   5272  CG2 VAL B 211      50.443  61.201  47.536  1.00 36.11           C  
ANISOU 5272  CG2 VAL B 211     1730   3181   8810      1  -2158   -604       C  
ATOM   5273  N   THR B 212      47.066  62.997  46.709  1.00 37.50           N  
ANISOU 5273  N   THR B 212     1749   3266   9230     70  -2572   -667       N  
ATOM   5274  CA  THR B 212      45.769  62.458  46.319  1.00 38.95           C  
ANISOU 5274  CA  THR B 212     1951   3362   9483     19  -2761   -695       C  
ATOM   5275  C   THR B 212      45.975  61.702  45.022  1.00 39.75           C  
ANISOU 5275  C   THR B 212     2136   3392   9574    -26  -2826   -703       C  
ATOM   5276  O   THR B 212      46.451  62.287  44.046  1.00 40.10           O  
ANISOU 5276  O   THR B 212     2236   3392   9607   -209  -2809   -765       O  
ATOM   5277  CB  THR B 212      44.780  63.598  46.012  1.00 38.82           C  
ANISOU 5277  CB  THR B 212     1968   3293   9489     51  -2750   -700       C  
ATOM   5278  OG1 THR B 212      44.836  64.578  47.058  1.00 40.61           O  
ANISOU 5278  OG1 THR B 212     2392   3431   9608    137  -2768   -574       O  
ATOM   5279  CG2 THR B 212      43.378  63.052  45.874  1.00 39.39           C  
ANISOU 5279  CG2 THR B 212     1796   3614   9554    190  -2782   -645       C  
ATOM   5280  N   ARG B 213      45.611  60.423  45.006  1.00 40.82           N  
ANISOU 5280  N   ARG B 213     2372   3433   9702   -120  -2949   -664       N  
ATOM   5281  CA  ARG B 213      45.763  59.618  43.799  1.00 42.11           C  
ANISOU 5281  CA  ARG B 213     2721   3514   9763   -105  -3040   -652       C  
ATOM   5282  C   ARG B 213      45.144  60.332  42.604  1.00 42.56           C  
ANISOU 5282  C   ARG B 213     2850   3558   9763    -87  -3164   -603       C  
ATOM   5283  O   ARG B 213      44.024  60.839  42.678  1.00 42.65           O  
ANISOU 5283  O   ARG B 213     2898   3581   9724    -72  -3190   -586       O  
ATOM   5284  CB  ARG B 213      45.149  58.224  43.962  1.00 42.89           C  
ANISOU 5284  CB  ARG B 213     2865   3589   9841   -172  -2990   -642       C  
ATOM   5285  CG  ARG B 213      45.584  57.230  42.887  1.00 44.02           C  
ANISOU 5285  CG  ARG B 213     3087   3604  10034   -172  -2844   -780       C  
ATOM   5286  CD  ARG B 213      45.142  55.815  43.218  1.00 47.89           C  
ANISOU 5286  CD  ARG B 213     3845   3935  10416   -275  -2678   -691       C  
ATOM   5287  NE  ARG B 213      45.799  54.825  42.363  1.00 51.08           N  
ANISOU 5287  NE  ARG B 213     4344   4239  10824   -315  -2489   -847       N  
ATOM   5288  CZ  ARG B 213      45.194  54.182  41.369  1.00 53.74           C  
ANISOU 5288  CZ  ARG B 213     4833   4659  10924   -103  -2449   -921       C  
ATOM   5289  NH1 ARG B 213      43.915  54.414  41.115  1.00 54.81           N  
ANISOU 5289  NH1 ARG B 213     4770   4893  11160   -173  -2537   -893       N  
ATOM   5290  NH2 ARG B 213      45.857  53.299  40.634  1.00 56.10           N  
ANISOU 5290  NH2 ARG B 213     5301   4769  11246    154  -2186   -893       N  
ATOM   5291  N   GLY B 214      45.899  60.376  41.513  1.00 43.05           N  
ANISOU 5291  N   GLY B 214     3041   3607   9706    -49  -3290   -535       N  
ATOM   5292  CA  GLY B 214      45.426  60.973  40.272  1.00 44.22           C  
ANISOU 5292  CA  GLY B 214     3328   3735   9739    -43  -3379   -509       C  
ATOM   5293  C   GLY B 214      45.881  62.403  40.034  1.00 44.28           C  
ANISOU 5293  C   GLY B 214     3433   3716   9674    -11  -3488   -502       C  
ATOM   5294  O   GLY B 214      45.618  62.962  38.965  1.00 45.15           O  
ANISOU 5294  O   GLY B 214     3671   3809   9671   -110  -3545   -505       O  
ATOM   5295  N   LYS B 215      46.498  63.019  41.037  1.00 43.41           N  
ANISOU 5295  N   LYS B 215     3156   3780   9557     92  -3616   -434       N  
ATOM   5296  CA  LYS B 215      47.023  64.377  40.892  1.00 43.38           C  
ANISOU 5296  CA  LYS B 215     3252   3740   9488    202  -3555   -440       C  
ATOM   5297  C   LYS B 215      48.545  64.352  40.750  1.00 42.67           C  
ANISOU 5297  C   LYS B 215     3259   3655   9297    162  -3599   -436       C  
ATOM   5298  O   LYS B 215      49.209  63.427  41.228  1.00 42.37           O  
ANISOU 5298  O   LYS B 215     3303   3510   9284    213  -3552   -501       O  
ATOM   5299  CB  LYS B 215      46.576  65.283  42.048  1.00 43.73           C  
ANISOU 5299  CB  LYS B 215     3235   3847   9530    207  -3549   -433       C  
ATOM   5300  CG  LYS B 215      45.054  65.519  42.097  1.00 46.02           C  
ANISOU 5300  CG  LYS B 215     3466   4164   9853    422  -3348   -434       C  
ATOM   5301  CD  LYS B 215      44.635  66.450  43.232  1.00 48.30           C  
ANISOU 5301  CD  LYS B 215     3753   4308  10289    525  -3109   -470       C  
ATOM   5302  CE  LYS B 215      43.112  66.603  43.293  1.00 49.95           C  
ANISOU 5302  CE  LYS B 215     3966   4425  10587    518  -2836   -369       C  
ATOM   5303  NZ  LYS B 215      42.659  67.489  44.410  1.00 51.02           N  
ANISOU 5303  NZ  LYS B 215     4324   4441  10618    494  -2720   -410       N  
ATOM   5304  N   ARG B 216      49.073  65.363  40.061  1.00 41.91           N  
ANISOU 5304  N   ARG B 216     3306   3535   9081    168  -3602   -449       N  
ATOM   5305  CA  ARG B 216      50.503  65.521  39.817  1.00 41.24           C  
ANISOU 5305  CA  ARG B 216     3315   3486   8865    169  -3577   -422       C  
ATOM   5306  C   ARG B 216      51.016  66.696  40.647  1.00 40.50           C  
ANISOU 5306  C   ARG B 216     3268   3469   8649    183  -3494   -372       C  
ATOM   5307  O   ARG B 216      50.342  67.729  40.742  1.00 39.98           O  
ANISOU 5307  O   ARG B 216     3234   3413   8543    177  -3580   -389       O  
ATOM   5308  CB  ARG B 216      50.783  65.752  38.327  1.00 41.49           C  
ANISOU 5308  CB  ARG B 216     3377   3492   8892    176  -3610   -416       C  
ATOM   5309  CG  ARG B 216      50.202  64.681  37.395  1.00 42.91           C  
ANISOU 5309  CG  ARG B 216     3550   3678   9075    114  -3681   -406       C  
ATOM   5310  CD  ARG B 216      50.029  65.196  35.974  1.00 44.50           C  
ANISOU 5310  CD  ARG B 216     3731   3992   9185    205  -3918   -251       C  
ATOM   5311  NE  ARG B 216      49.106  66.330  35.938  1.00 47.07           N  
ANISOU 5311  NE  ARG B 216     4003   4408   9472    243  -3920   -213       N  
ATOM   5312  CZ  ARG B 216      49.061  67.252  34.980  1.00 47.46           C  
ANISOU 5312  CZ  ARG B 216     3997   4549   9483    336  -4008   -147       C  
ATOM   5313  NH1 ARG B 216      49.873  67.188  33.934  1.00 48.21           N  
ANISOU 5313  NH1 ARG B 216     4183   4693   9439    175  -3907   -107       N  
ATOM   5314  NH2 ARG B 216      48.188  68.246  35.063  1.00 48.31           N  
ANISOU 5314  NH2 ARG B 216     4309   4482   9562    408  -4024   -120       N  
ATOM   5315  N   TYR B 217      52.201  66.528  41.234  1.00 38.86           N  
ANISOU 5315  N   TYR B 217     3112   3354   8299    188  -3393   -316       N  
ATOM   5316  CA  TYR B 217      52.739  67.452  42.225  1.00 37.86           C  
ANISOU 5316  CA  TYR B 217     3073   3252   8059    128  -3160   -270       C  
ATOM   5317  C   TYR B 217      54.091  67.990  41.780  1.00 37.08           C  
ANISOU 5317  C   TYR B 217     3037   3222   7830    170  -3053   -276       C  
ATOM   5318  O   TYR B 217      54.938  67.232  41.314  1.00 36.73           O  
ANISOU 5318  O   TYR B 217     2901   3193   7861    161  -2982   -264       O  
ATOM   5319  CB  TYR B 217      52.906  66.746  43.585  1.00 37.84           C  
ANISOU 5319  CB  TYR B 217     3116   3199   8060    153  -3218   -276       C  
ATOM   5320  CG  TYR B 217      51.569  66.378  44.185  1.00 38.24           C  
ANISOU 5320  CG  TYR B 217     3188   3128   8213    148  -3125   -222       C  
ATOM   5321  CD1 TYR B 217      50.858  65.272  43.719  1.00 37.98           C  
ANISOU 5321  CD1 TYR B 217     3102   3156   8172     66  -3330   -310       C  
ATOM   5322  CD2 TYR B 217      50.989  67.164  45.180  1.00 39.07           C  
ANISOU 5322  CD2 TYR B 217     3371   3211   8260    148  -3062   -265       C  
ATOM   5323  CE1 TYR B 217      49.605  64.962  44.230  1.00 39.47           C  
ANISOU 5323  CE1 TYR B 217     3317   3297   8383      0  -3084   -442       C  
ATOM   5324  CE2 TYR B 217      49.731  66.853  45.699  1.00 39.23           C  
ANISOU 5324  CE2 TYR B 217     3253   3192   8458     25  -3083   -387       C  
ATOM   5325  CZ  TYR B 217      49.047  65.753  45.223  1.00 40.28           C  
ANISOU 5325  CZ  TYR B 217     3365   3438   8498    -63  -3026   -503       C  
ATOM   5326  OH  TYR B 217      47.800  65.441  45.731  1.00 39.98           O  
ANISOU 5326  OH  TYR B 217     3102   3567   8521   -200  -3218   -651       O  
ATOM   5327  N   ARG B 218      54.274  69.300  41.918  1.00 35.66           N  
ANISOU 5327  N   ARG B 218     2925   3126   7498    147  -2880   -244       N  
ATOM   5328  CA  ARG B 218      55.591  69.902  41.782  1.00 34.08           C  
ANISOU 5328  CA  ARG B 218     2769   3115   7063    230  -2823   -243       C  
ATOM   5329  C   ARG B 218      56.174  70.009  43.178  1.00 33.16           C  
ANISOU 5329  C   ARG B 218     2755   3018   6825    303  -2658   -220       C  
ATOM   5330  O   ARG B 218      55.911  70.987  43.888  1.00 33.12           O  
ANISOU 5330  O   ARG B 218     2730   3066   6784    411  -2679   -223       O  
ATOM   5331  CB  ARG B 218      55.507  71.305  41.169  1.00 33.82           C  
ANISOU 5331  CB  ARG B 218     2739   3039   7070    212  -2822   -213       C  
ATOM   5332  CG  ARG B 218      56.864  71.861  40.747  1.00 34.04           C  
ANISOU 5332  CG  ARG B 218     2795   3158   6979    235  -2857   -220       C  
ATOM   5333  CD  ARG B 218      56.868  73.375  40.721  1.00 34.65           C  
ANISOU 5333  CD  ARG B 218     3096   3115   6954    270  -2753   -269       C  
ATOM   5334  NE  ARG B 218      58.186  73.936  40.414  1.00 35.06           N  
ANISOU 5334  NE  ARG B 218     3010   3300   7009    509  -2710   -255       N  
ATOM   5335  CZ  ARG B 218      58.437  74.715  39.363  1.00 36.25           C  
ANISOU 5335  CZ  ARG B 218     3208   3355   7211    444  -2495   -313       C  
ATOM   5336  NH1 ARG B 218      57.462  75.028  38.510  1.00 37.08           N  
ANISOU 5336  NH1 ARG B 218     3356   3495   7236    503  -2471   -290       N  
ATOM   5337  NH2 ARG B 218      59.658  75.191  39.165  1.00 35.73           N  
ANISOU 5337  NH2 ARG B 218     3336   3003   7235    481  -2464   -459       N  
ATOM   5338  N   PHE B 219      56.976  69.019  43.560  1.00 31.27           N  
ANISOU 5338  N   PHE B 219     2589   2859   6433    300  -2517   -230       N  
ATOM   5339  CA  PHE B 219      57.703  69.102  44.813  1.00 29.73           C  
ANISOU 5339  CA  PHE B 219     2467   2683   6146    213  -2312   -247       C  
ATOM   5340  C   PHE B 219      58.966  69.931  44.625  1.00 28.90           C  
ANISOU 5340  C   PHE B 219     2441   2585   5954    239  -2147   -279       C  
ATOM   5341  O   PHE B 219      59.664  69.796  43.618  1.00 29.61           O  
ANISOU 5341  O   PHE B 219     2589   2727   5935    118  -2137   -339       O  
ATOM   5342  CB  PHE B 219      58.019  67.696  45.339  1.00 29.57           C  
ANISOU 5342  CB  PHE B 219     2506   2620   6108    231  -2305   -252       C  
ATOM   5343  CG  PHE B 219      56.815  66.998  45.909  1.00 29.14           C  
ANISOU 5343  CG  PHE B 219     2355   2505   6210    173  -2285   -256       C  
ATOM   5344  CD1 PHE B 219      56.244  67.453  47.087  1.00 29.19           C  
ANISOU 5344  CD1 PHE B 219     2351   2529   6209    140  -2260   -187       C  
ATOM   5345  CD2 PHE B 219      56.230  65.916  45.258  1.00 30.91           C  
ANISOU 5345  CD2 PHE B 219     2411   2676   6655     86  -2086   -248       C  
ATOM   5346  CE1 PHE B 219      55.115  66.848  47.619  1.00 28.17           C  
ANISOU 5346  CE1 PHE B 219     2375   2179   6147   -129  -2387    -90       C  
ATOM   5347  CE2 PHE B 219      55.112  65.284  45.795  1.00 29.87           C  
ANISOU 5347  CE2 PHE B 219     2310   2413   6625    190  -2164   -230       C  
ATOM   5348  CZ  PHE B 219      54.558  65.746  46.982  1.00 28.41           C  
ANISOU 5348  CZ  PHE B 219     2338   2431   6025     64  -2603   -246       C  
ATOM   5349  N   ARG B 220      59.249  70.788  45.602  1.00 26.80           N  
ANISOU 5349  N   ARG B 220     2105   2378   5699    282  -2028   -210       N  
ATOM   5350  CA  ARG B 220      60.341  71.732  45.515  1.00 25.40           C  
ANISOU 5350  CA  ARG B 220     1950   2209   5488    401  -1894   -175       C  
ATOM   5351  C   ARG B 220      61.261  71.305  46.645  1.00 24.66           C  
ANISOU 5351  C   ARG B 220     1847   2196   5324    325  -1707   -180       C  
ATOM   5352  O   ARG B 220      60.995  71.567  47.821  1.00 25.11           O  
ANISOU 5352  O   ARG B 220     1839   2214   5485    333  -1528   -227       O  
ATOM   5353  CB  ARG B 220      59.834  73.170  45.673  1.00 25.29           C  
ANISOU 5353  CB  ARG B 220     1845   2249   5513    353  -1986   -163       C  
ATOM   5354  CG  ARG B 220      58.953  73.648  44.513  1.00 25.60           C  
ANISOU 5354  CG  ARG B 220     2150   1949   5626    625  -2059    -43       C  
ATOM   5355  CD  ARG B 220      58.451  75.069  44.767  1.00 26.12           C  
ANISOU 5355  CD  ARG B 220     2018   1996   5911    750  -2375    -56       C  
ATOM   5356  NE  ARG B 220      57.622  75.582  43.680  1.00 27.90           N  
ANISOU 5356  NE  ARG B 220     2299   2234   6065    667  -2422    -26       N  
ATOM   5357  CZ  ARG B 220      58.058  76.378  42.707  1.00 29.37           C  
ANISOU 5357  CZ  ARG B 220     2530   2438   6190    425  -2605    -55       C  
ATOM   5358  NH1 ARG B 220      59.331  76.752  42.644  1.00 29.80           N  
ANISOU 5358  NH1 ARG B 220     2490   2583   6250    437  -2392   -245       N  
ATOM   5359  NH2 ARG B 220      57.217  76.813  41.786  1.00 28.64           N  
ANISOU 5359  NH2 ARG B 220     2877   2002   6000    470  -2755   -209       N  
ATOM   5360  N   LEU B 221      62.321  70.599  46.261  1.00 23.79           N  
ANISOU 5360  N   LEU B 221     1896   2058   5086    369  -1495   -131       N  
ATOM   5361  CA  LEU B 221      63.244  69.986  47.205  1.00 23.15           C  
ANISOU 5361  CA  LEU B 221     1801   2120   4875    326  -1340   -163       C  
ATOM   5362  C   LEU B 221      64.417  70.921  47.473  1.00 22.92           C  
ANISOU 5362  C   LEU B 221     1882   2064   4763    233  -1203   -206       C  
ATOM   5363  O   LEU B 221      65.112  71.321  46.539  1.00 24.07           O  
ANISOU 5363  O   LEU B 221     2118   2168   4858    176  -1133   -209       O  
ATOM   5364  CB  LEU B 221      63.739  68.650  46.632  1.00 22.79           C  
ANISOU 5364  CB  LEU B 221     1851   1989   4816    323  -1293   -133       C  
ATOM   5365  CG  LEU B 221      64.767  67.865  47.460  1.00 22.11           C  
ANISOU 5365  CG  LEU B 221     1820   1988   4590    353  -1255   -173       C  
ATOM   5366  CD1 LEU B 221      64.112  67.358  48.730  1.00 22.61           C  
ANISOU 5366  CD1 LEU B 221     1946   2244   4399     19  -1225   -137       C  
ATOM   5367  CD2 LEU B 221      65.353  66.689  46.684  1.00 23.92           C  
ANISOU 5367  CD2 LEU B 221     2239   2231   4617    408   -958   -340       C  
ATOM   5368  N   VAL B 222      64.675  71.212  48.744  1.00 21.94           N  
ANISOU 5368  N   VAL B 222     1652   2073   4610    291  -1110   -229       N  
ATOM   5369  CA  VAL B 222      65.652  72.232  49.115  1.00 21.60           C  
ANISOU 5369  CA  VAL B 222     1636   2079   4492    330  -1040   -222       C  
ATOM   5370  C   VAL B 222      66.589  71.661  50.175  1.00 20.91           C  
ANISOU 5370  C   VAL B 222     1424   2207   4312    316   -910   -223       C  
ATOM   5371  O   VAL B 222      66.122  71.202  51.221  1.00 21.07           O  
ANISOU 5371  O   VAL B 222     1300   2352   4353    350   -767   -235       O  
ATOM   5372  CB  VAL B 222      64.958  73.511  49.675  1.00 21.53           C  
ANISOU 5372  CB  VAL B 222     1556   2068   4556    303  -1167   -212       C  
ATOM   5373  CG1 VAL B 222      65.995  74.610  49.902  1.00 23.02           C  
ANISOU 5373  CG1 VAL B 222     2205   1790   4751    266  -1044   -284       C  
ATOM   5374  CG2 VAL B 222      63.873  73.996  48.741  1.00 24.75           C  
ANISOU 5374  CG2 VAL B 222     2287   2250   4867    395  -1047   -171       C  
ATOM   5375  N   SER B 223      67.895  71.633  49.901  1.00 19.77           N  
ANISOU 5375  N   SER B 223     1329   2140   4043    321   -858   -219       N  
ATOM   5376  CA  SER B 223      68.837  71.247  50.939  1.00 19.42           C  
ANISOU 5376  CA  SER B 223     1186   2264   3928    252   -768   -237       C  
ATOM   5377  C   SER B 223      69.201  72.482  51.749  1.00 19.72           C  
ANISOU 5377  C   SER B 223     1266   2315   3909    196   -689   -201       C  
ATOM   5378  O   SER B 223      69.785  73.435  51.210  1.00 20.64           O  
ANISOU 5378  O   SER B 223     1521   2399   3921    231   -549   -204       O  
ATOM   5379  CB  SER B 223      70.111  70.623  50.386  1.00 18.85           C  
ANISOU 5379  CB  SER B 223     1015   2287   3858    246   -876   -180       C  
ATOM   5380  OG  SER B 223      71.059  70.572  51.451  1.00 20.28           O  
ANISOU 5380  OG  SER B 223     1128   2519   4057     24   -882   -258       O  
ATOM   5381  N   LEU B 224      68.859  72.448  53.035  1.00 19.73           N  
ANISOU 5381  N   LEU B 224     1224   2361   3912    204   -493   -214       N  
ATOM   5382  CA  LEU B 224      69.307  73.442  54.019  1.00 19.25           C  
ANISOU 5382  CA  LEU B 224     1082   2415   3815    185   -458   -204       C  
ATOM   5383  C   LEU B 224      70.506  72.911  54.807  1.00 19.23           C  
ANISOU 5383  C   LEU B 224     1069   2322   3914    161   -383   -152       C  
ATOM   5384  O   LEU B 224      70.790  73.370  55.920  1.00 19.11           O  
ANISOU 5384  O   LEU B 224     1058   2317   3886    244   -488   -180       O  
ATOM   5385  CB  LEU B 224      68.176  73.760  55.009  1.00 18.64           C  
ANISOU 5385  CB  LEU B 224      983   2319   3779    230   -448   -217       C  
ATOM   5386  CG  LEU B 224      66.762  73.944  54.451  1.00 19.44           C  
ANISOU 5386  CG  LEU B 224     1166   2740   3478    283   -355   -136       C  
ATOM   5387  CD1 LEU B 224      65.813  74.129  55.629  1.00 18.13           C  
ANISOU 5387  CD1 LEU B 224     1360   3332   2195    298   -555   -325       C  
ATOM   5388  CD2 LEU B 224      66.642  75.141  53.509  1.00 19.17           C  
ANISOU 5388  CD2 LEU B 224     1281   2879   3121    424   -494   -184       C  
ATOM   5389  N   SER B 225      71.214  71.943  54.234  1.00 18.92           N  
ANISOU 5389  N   SER B 225     1057   2165   3966    137   -340   -122       N  
ATOM   5390  CA  SER B 225      72.292  71.272  54.952  1.00 19.13           C  
ANISOU 5390  CA  SER B 225     1044   2222   3999    114   -433   -166       C  
ATOM   5391  C   SER B 225      73.461  72.192  55.290  1.00 19.59           C  
ANISOU 5391  C   SER B 225     1156   2242   4043    145   -365   -185       C  
ATOM   5392  O   SER B 225      73.868  73.016  54.479  1.00 20.26           O  
ANISOU 5392  O   SER B 225     1216   2435   4043     46   -341   -195       O  
ATOM   5393  CB  SER B 225      72.816  70.098  54.124  1.00 18.74           C  
ANISOU 5393  CB  SER B 225      988   2122   4010    161   -474   -165       C  
ATOM   5394  OG  SER B 225      73.794  69.365  54.844  1.00 18.51           O  
ANISOU 5394  OG  SER B 225      984   2178   3869    107   -547   -102       O  
ATOM   5395  N   CYS B 226      73.994  72.043  56.496  1.00 20.00           N  
ANISOU 5395  N   CYS B 226     1185   2332   4081    181   -373   -288       N  
ATOM   5396  CA  CYS B 226      75.291  72.623  56.824  1.00 21.56           C  
ANISOU 5396  CA  CYS B 226     1388   2566   4236    105   -263   -196       C  
ATOM   5397  C   CYS B 226      76.483  71.811  56.338  1.00 21.38           C  
ANISOU 5397  C   CYS B 226     1403   2517   4200    113   -256   -140       C  
ATOM   5398  O   CYS B 226      77.601  72.323  56.368  1.00 21.23           O  
ANISOU 5398  O   CYS B 226     1295   2507   4262     85    -89    -26       O  
ATOM   5399  CB  CYS B 226      75.432  72.810  58.335  1.00 22.82           C  
ANISOU 5399  CB  CYS B 226     1608   2775   4285     35   -329   -195       C  
ATOM   5400  SG  CYS B 226      74.966  74.496  58.808  1.00 27.95           S  
ANISOU 5400  SG  CYS B 226     2264   3400   4954    362   -319   -161       S  
ATOM   5401  N   ASP B 227      76.272  70.552  55.957  1.00 21.12           N  
ANISOU 5401  N   ASP B 227     1476   2426   4120    141   -190    -51       N  
ATOM   5402  CA  ASP B 227      77.403  69.675  55.606  1.00 21.12           C  
ANISOU 5402  CA  ASP B 227     1440   2486   4098    140   -168    -64       C  
ATOM   5403  C   ASP B 227      77.074  68.496  54.675  1.00 20.40           C  
ANISOU 5403  C   ASP B 227     1271   2477   4002     74   -131    -50       C  
ATOM   5404  O   ASP B 227      77.484  68.498  53.514  1.00 20.89           O  
ANISOU 5404  O   ASP B 227     1343   2568   4026     31    -44   -104       O  
ATOM   5405  CB  ASP B 227      78.096  69.200  56.888  1.00 21.38           C  
ANISOU 5405  CB  ASP B 227     1583   2477   4063    114   -188      7       C  
ATOM   5406  CG  ASP B 227      79.422  68.504  56.641  1.00 25.19           C  
ANISOU 5406  CG  ASP B 227     2188   3005   4375    280   -269    118       C  
ATOM   5407  OD1 ASP B 227      79.759  68.134  55.486  1.00 26.63           O  
ANISOU 5407  OD1 ASP B 227     2956   2870   4291    490    -82    532       O  
ATOM   5408  OD2 ASP B 227      80.147  68.308  57.646  1.00 30.47           O  
ANISOU 5408  OD2 ASP B 227     3124   3690   4761    482   -657    478       O  
ATOM   5409  N   PRO B 228      76.367  67.465  55.168  1.00 19.77           N  
ANISOU 5409  N   PRO B 228     1154   2396   3958     22    -59    -72       N  
ATOM   5410  CA  PRO B 228      76.219  66.289  54.298  1.00 19.31           C  
ANISOU 5410  CA  PRO B 228     1140   2321   3874     60    -14    -75       C  
ATOM   5411  C   PRO B 228      75.421  66.518  53.013  1.00 19.18           C  
ANISOU 5411  C   PRO B 228     1146   2265   3874     49    -38    -72       C  
ATOM   5412  O   PRO B 228      74.555  67.409  52.959  1.00 18.50           O  
ANISOU 5412  O   PRO B 228     1166   2012   3849     96   -118    -23       O  
ATOM   5413  CB  PRO B 228      75.513  65.267  55.194  1.00 19.16           C  
ANISOU 5413  CB  PRO B 228     1092   2263   3922      2     23   -118       C  
ATOM   5414  CG  PRO B 228      74.797  66.108  56.215  1.00 19.63           C  
ANISOU 5414  CG  PRO B 228     1145   2366   3946    -99    139    -92       C  
ATOM   5415  CD  PRO B 228      75.748  67.245  56.490  1.00 19.63           C  
ANISOU 5415  CD  PRO B 228     1167   2424   3866    -36    -44   -191       C  
ATOM   5416  N   PHE B 229      75.733  65.720  51.990  1.00 19.06           N  
ANISOU 5416  N   PHE B 229     1205   2262   3775    103      0     -9       N  
ATOM   5417  CA  PHE B 229      74.844  65.602  50.827  1.00 18.34           C  
ANISOU 5417  CA  PHE B 229     1092   2176   3697    119    -57     95       C  
ATOM   5418  C   PHE B 229      73.827  64.499  51.114  1.00 18.51           C  
ANISOU 5418  C   PHE B 229     1119   2200   3713    104   -236    105       C  
ATOM   5419  O   PHE B 229      74.113  63.623  51.931  1.00 18.93           O  
ANISOU 5419  O   PHE B 229     1046   2359   3784   -114   -337    370       O  
ATOM   5420  CB  PHE B 229      75.596  65.486  49.485  1.00 18.80           C  
ANISOU 5420  CB  PHE B 229     1398   2093   3649    289    -49    113       C  
ATOM   5421  CG  PHE B 229      76.261  64.153  49.206  1.00 19.30           C  
ANISOU 5421  CG  PHE B 229     1594   2106   3633    224    138     60       C  
ATOM   5422  CD1 PHE B 229      75.524  63.072  48.729  1.00 20.62           C  
ANISOU 5422  CD1 PHE B 229     1946   2182   3706    202    102    145       C  
ATOM   5423  CD2 PHE B 229      77.637  64.008  49.325  1.00 18.54           C  
ANISOU 5423  CD2 PHE B 229     1594   1840   3611    416    616    259       C  
ATOM   5424  CE1 PHE B 229      76.135  61.853  48.418  1.00 20.37           C  
ANISOU 5424  CE1 PHE B 229     1700   2215   3825    452     64     63       C  
ATOM   5425  CE2 PHE B 229      78.272  62.786  49.003  1.00 19.25           C  
ANISOU 5425  CE2 PHE B 229     1815   1986   3510    210    638     41       C  
ATOM   5426  CZ  PHE B 229      77.518  61.710  48.555  1.00 20.20           C  
ANISOU 5426  CZ  PHE B 229     1594   2343   3736     -5    766     35       C  
ATOM   5427  N   TYR B 230      72.641  64.566  50.510  1.00 17.44           N  
ANISOU 5427  N   TYR B 230      917   2252   3457     32   -286     33       N  
ATOM   5428  CA  TYR B 230      71.623  63.555  50.753  1.00 17.72           C  
ANISOU 5428  CA  TYR B 230     1039   2258   3433     95   -426   -138       C  
ATOM   5429  C   TYR B 230      71.381  62.781  49.469  1.00 18.24           C  
ANISOU 5429  C   TYR B 230     1164   2305   3459    105   -501   -174       C  
ATOM   5430  O   TYR B 230      71.378  63.364  48.377  1.00 18.75           O  
ANISOU 5430  O   TYR B 230     1320   2247   3557     -1   -524    -82       O  
ATOM   5431  CB  TYR B 230      70.306  64.206  51.216  1.00 17.16           C  
ANISOU 5431  CB  TYR B 230      984   2380   3155    109   -352   -157       C  
ATOM   5432  CG  TYR B 230      70.488  64.726  52.615  1.00 17.78           C  
ANISOU 5432  CG  TYR B 230     1217   2608   2928    -94   -402   -252       C  
ATOM   5433  CD1 TYR B 230      70.455  63.841  53.689  1.00 15.56           C  
ANISOU 5433  CD1 TYR B 230      797   2612   2502   -168   -525   -468       C  
ATOM   5434  CD2 TYR B 230      70.808  66.069  52.856  1.00 16.37           C  
ANISOU 5434  CD2 TYR B 230     1226   2782   2209   -134   -409   -516       C  
ATOM   5435  CE1 TYR B 230      70.679  64.287  54.968  1.00 15.66           C  
ANISOU 5435  CE1 TYR B 230      878   2966   2104   -126   -525   -630       C  
ATOM   5436  CE2 TYR B 230      71.036  66.526  54.143  1.00 17.91           C  
ANISOU 5436  CE2 TYR B 230     1253   2973   2578   -240   -332   -554       C  
ATOM   5437  CZ  TYR B 230      70.977  65.629  55.178  1.00 17.01           C  
ANISOU 5437  CZ  TYR B 230     1019   3100   2343    -61   -354   -580       C  
ATOM   5438  OH  TYR B 230      71.220  66.068  56.450  1.00 19.33           O  
ANISOU 5438  OH  TYR B 230     1171   3352   2820   -374   -376  -1011       O  
ATOM   5439  N   THR B 231      71.167  61.477  49.612  1.00 18.07           N  
ANISOU 5439  N   THR B 231     1088   2211   3567    161   -615   -209       N  
ATOM   5440  CA  THR B 231      70.646  60.685  48.502  1.00 18.67           C  
ANISOU 5440  CA  THR B 231     1244   2302   3547    217   -681   -233       C  
ATOM   5441  C   THR B 231      69.146  60.578  48.766  1.00 19.03           C  
ANISOU 5441  C   THR B 231     1230   2294   3706    210   -743   -209       C  
ATOM   5442  O   THR B 231      68.726  60.010  49.778  1.00 18.88           O  
ANISOU 5442  O   THR B 231     1181   2309   3680    219   -817   -177       O  
ATOM   5443  CB  THR B 231      71.307  59.296  48.418  1.00 18.91           C  
ANISOU 5443  CB  THR B 231     1272   2355   3558    236   -723   -256       C  
ATOM   5444  OG1 THR B 231      72.722  59.472  48.261  1.00 18.96           O  
ANISOU 5444  OG1 THR B 231     1463   2493   3248    299   -319     -7       O  
ATOM   5445  CG2 THR B 231      70.754  58.489  47.231  1.00 19.41           C  
ANISOU 5445  CG2 THR B 231     1712   2174   3490    141   -571   -350       C  
ATOM   5446  N   PHE B 232      68.367  61.185  47.874  1.00 19.55           N  
ANISOU 5446  N   PHE B 232     1281   2412   3734    251   -892   -217       N  
ATOM   5447  CA  PHE B 232      66.936  61.405  48.067  1.00 20.32           C  
ANISOU 5447  CA  PHE B 232     1379   2297   4043    117   -926   -227       C  
ATOM   5448  C   PHE B 232      66.159  60.572  47.071  1.00 21.21           C  
ANISOU 5448  C   PHE B 232     1483   2409   4166    110   -999   -207       C  
ATOM   5449  O   PHE B 232      66.505  60.544  45.886  1.00 21.89           O  
ANISOU 5449  O   PHE B 232     1697   2397   4223     27   -979   -161       O  
ATOM   5450  CB  PHE B 232      66.560  62.883  47.864  1.00 20.58           C  
ANISOU 5450  CB  PHE B 232     1329   2409   4081    212   -943   -201       C  
ATOM   5451  CG  PHE B 232      65.099  63.167  48.082  1.00 20.60           C  
ANISOU 5451  CG  PHE B 232     1241   2366   4219    116   -853   -143       C  
ATOM   5452  CD1 PHE B 232      64.615  63.487  49.343  1.00 19.57           C  
ANISOU 5452  CD1 PHE B 232     1131   2026   4279    219   -681   -112       C  
ATOM   5453  CD2 PHE B 232      64.200  63.077  47.024  1.00 20.39           C  
ANISOU 5453  CD2 PHE B 232      886   2504   4355    182  -1018    117       C  
ATOM   5454  CE1 PHE B 232      63.250  63.729  49.537  1.00 19.72           C  
ANISOU 5454  CE1 PHE B 232      900   2269   4322    164   -915     16       C  
ATOM   5455  CE2 PHE B 232      62.839  63.312  47.214  1.00 21.72           C  
ANISOU 5455  CE2 PHE B 232     1325   2531   4393    291   -376    -71       C  
ATOM   5456  CZ  PHE B 232      62.366  63.634  48.469  1.00 21.27           C  
ANISOU 5456  CZ  PHE B 232     1614   2308   4158    175   -643    -42       C  
ATOM   5457  N   SER B 233      65.142  59.874  47.571  1.00 21.37           N  
ANISOU 5457  N   SER B 233     1319   2402   4396     91  -1021   -275       N  
ATOM   5458  CA  SER B 233      64.241  59.106  46.720  1.00 22.41           C  
ANISOU 5458  CA  SER B 233     1445   2530   4539     94  -1185   -279       C  
ATOM   5459  C   SER B 233      62.894  58.899  47.407  1.00 22.78           C  
ANISOU 5459  C   SER B 233     1391   2540   4721     75  -1265   -329       C  
ATOM   5460  O   SER B 233      62.750  59.114  48.615  1.00 22.52           O  
ANISOU 5460  O   SER B 233     1286   2549   4722    144  -1287   -322       O  
ATOM   5461  CB  SER B 233      64.839  57.745  46.370  1.00 22.56           C  
ANISOU 5461  CB  SER B 233     1481   2521   4569     87  -1134   -249       C  
ATOM   5462  OG  SER B 233      64.950  56.935  47.536  1.00 24.71           O  
ANISOU 5462  OG  SER B 233     2148   2748   4493    196  -1038   -304       O  
ATOM   5463  N   ILE B 234      61.918  58.442  46.630  1.00 22.98           N  
ANISOU 5463  N   ILE B 234     1411   2487   4832     64  -1444   -361       N  
ATOM   5464  CA  ILE B 234      60.589  58.169  47.162  1.00 23.42           C  
ANISOU 5464  CA  ILE B 234     1419   2519   4961    -10  -1507   -431       C  
ATOM   5465  C   ILE B 234      60.176  56.789  46.677  1.00 24.57           C  
ANISOU 5465  C   ILE B 234     1579   2679   5075     21  -1542   -475       C  
ATOM   5466  O   ILE B 234      60.088  56.572  45.464  1.00 24.99           O  
ANISOU 5466  O   ILE B 234     1695   2767   5032    -32  -1614   -562       O  
ATOM   5467  CB  ILE B 234      59.572  59.227  46.701  1.00 23.22           C  
ANISOU 5467  CB  ILE B 234     1415   2521   4883    -24  -1586   -406       C  
ATOM   5468  CG1 ILE B 234      59.987  60.620  47.196  1.00 23.23           C  
ANISOU 5468  CG1 ILE B 234     1401   2306   5118     23  -1580   -309       C  
ATOM   5469  CG2 ILE B 234      58.159  58.886  47.197  1.00 22.84           C  
ANISOU 5469  CG2 ILE B 234     1278   2582   4816   -115  -1796   -481       C  
ATOM   5470  CD1 ILE B 234      59.197  61.780  46.555  1.00 23.84           C  
ANISOU 5470  CD1 ILE B 234     1467   2495   5094    445  -1744   -370       C  
ATOM   5471  N   ASP B 235      59.946  55.862  47.605  1.00 24.65           N  
ANISOU 5471  N   ASP B 235     1574   2661   5129     11  -1603   -425       N  
ATOM   5472  CA  ASP B 235      59.643  54.484  47.213  1.00 25.42           C  
ANISOU 5472  CA  ASP B 235     1731   2710   5215     17  -1656   -455       C  
ATOM   5473  C   ASP B 235      58.455  54.451  46.247  1.00 26.38           C  
ANISOU 5473  C   ASP B 235     1908   2815   5298     28  -1703   -387       C  
ATOM   5474  O   ASP B 235      57.479  55.179  46.439  1.00 26.13           O  
ANISOU 5474  O   ASP B 235     1688   2916   5323     50  -1760   -380       O  
ATOM   5475  CB  ASP B 235      59.309  53.629  48.436  1.00 25.71           C  
ANISOU 5475  CB  ASP B 235     1815   2726   5227    114  -1590   -438       C  
ATOM   5476  CG  ASP B 235      60.527  53.272  49.282  1.00 25.19           C  
ANISOU 5476  CG  ASP B 235     1653   2729   5190     77  -1569   -493       C  
ATOM   5477  OD1 ASP B 235      61.648  53.777  49.047  1.00 24.09           O  
ANISOU 5477  OD1 ASP B 235     1754   2525   4872    386  -1173   -459       O  
ATOM   5478  OD2 ASP B 235      60.352  52.458  50.218  1.00 25.29           O  
ANISOU 5478  OD2 ASP B 235     1522   2816   5270     98  -1392   -523       O  
ATOM   5479  N   GLY B 236      58.561  53.629  45.204  1.00 26.93           N  
ANISOU 5479  N   GLY B 236     2123   2821   5285    -92  -1821   -402       N  
ATOM   5480  CA  GLY B 236      57.476  53.387  44.249  1.00 28.38           C  
ANISOU 5480  CA  GLY B 236     2317   3033   5430      0  -1895   -324       C  
ATOM   5481  C   GLY B 236      57.165  54.508  43.278  1.00 29.59           C  
ANISOU 5481  C   GLY B 236     2636   3145   5462    -37  -1914   -308       C  
ATOM   5482  O   GLY B 236      56.210  54.405  42.492  1.00 29.75           O  
ANISOU 5482  O   GLY B 236     2580   3151   5571   -188  -1916   -321       O  
ATOM   5483  N   HIS B 237      57.944  55.587  43.340  1.00 29.91           N  
ANISOU 5483  N   HIS B 237     2716   3185   5462     39  -1878   -288       N  
ATOM   5484  CA  HIS B 237      57.667  56.775  42.533  1.00 30.66           C  
ANISOU 5484  CA  HIS B 237     2979   3276   5394    100  -1898   -281       C  
ATOM   5485  C   HIS B 237      58.930  57.321  41.889  1.00 30.96           C  
ANISOU 5485  C   HIS B 237     3125   3322   5314    172  -1860   -225       C  
ATOM   5486  O   HIS B 237      59.964  57.423  42.540  1.00 32.26           O  
ANISOU 5486  O   HIS B 237     3335   3529   5391    137  -1802   -268       O  
ATOM   5487  CB  HIS B 237      57.041  57.886  43.383  1.00 30.48           C  
ANISOU 5487  CB  HIS B 237     2803   3284   5493     85  -1914   -269       C  
ATOM   5488  CG  HIS B 237      55.717  57.523  43.982  1.00 31.05           C  
ANISOU 5488  CG  HIS B 237     2764   3333   5701    112  -1889   -327       C  
ATOM   5489  ND1 HIS B 237      55.597  56.710  45.088  1.00 30.19           N  
ANISOU 5489  ND1 HIS B 237     2512   3017   5941    181  -1914   -310       N  
ATOM   5490  CD2 HIS B 237      54.458  57.886  43.638  1.00 30.31           C  
ANISOU 5490  CD2 HIS B 237     2525   3134   5854     64  -1993   -394       C  
ATOM   5491  CE1 HIS B 237      54.316  56.575  45.390  1.00 30.48           C  
ANISOU 5491  CE1 HIS B 237     2634   2992   5953    142  -1949   -472       C  
ATOM   5492  NE2 HIS B 237      53.605  57.279  44.527  1.00 30.01           N  
ANISOU 5492  NE2 HIS B 237     2480   3009   5911    193  -1931   -475       N  
ATOM   5493  N   ASN B 238      58.840  57.675  40.612  1.00 31.53           N  
ANISOU 5493  N   ASN B 238     3394   3321   5262    245  -1807   -176       N  
ATOM   5494  CA  ASN B 238      59.912  58.405  39.946  1.00 31.72           C  
ANISOU 5494  CA  ASN B 238     3626   3250   5176    260  -1793    -90       C  
ATOM   5495  C   ASN B 238      59.735  59.903  40.110  1.00 31.21           C  
ANISOU 5495  C   ASN B 238     3643   3239   4975    250  -1872    -30       C  
ATOM   5496  O   ASN B 238      58.665  60.372  40.505  1.00 30.83           O  
ANISOU 5496  O   ASN B 238     3622   3249   4841    285  -1905     80       O  
ATOM   5497  CB  ASN B 238      59.970  58.025  38.466  1.00 32.63           C  
ANISOU 5497  CB  ASN B 238     3810   3315   5272    303  -1682    -73       C  
ATOM   5498  CG  ASN B 238      60.463  56.607  38.260  1.00 35.89           C  
ANISOU 5498  CG  ASN B 238     4248   3555   5830    413  -1399   -159       C  
ATOM   5499  OD1 ASN B 238      61.254  56.109  39.062  1.00 36.34           O  
ANISOU 5499  OD1 ASN B 238     4609   3271   5924    629  -1466     -9       O  
ATOM   5500  ND2 ASN B 238      60.004  55.951  37.199  1.00 40.18           N  
ANISOU 5500  ND2 ASN B 238     4894   4101   6270    157  -1126   -531       N  
ATOM   5501  N   MET B 239      60.803  60.637  39.815  1.00 30.55           N  
ANISOU 5501  N   MET B 239     3643   3126   4837    200  -1944      1       N  
ATOM   5502  CA  MET B 239      60.848  62.084  39.982  1.00 30.42           C  
ANISOU 5502  CA  MET B 239     3746   3127   4684    179  -1981    -34       C  
ATOM   5503  C   MET B 239      61.263  62.710  38.654  1.00 31.16           C  
ANISOU 5503  C   MET B 239     3893   3171   4774    140  -2081     28       C  
ATOM   5504  O   MET B 239      62.356  62.436  38.143  1.00 31.57           O  
ANISOU 5504  O   MET B 239     3957   3295   4741    144  -1994     41       O  
ATOM   5505  CB  MET B 239      61.861  62.441  41.071  1.00 29.92           C  
ANISOU 5505  CB  MET B 239     3731   2993   4642    145  -1925    -91       C  
ATOM   5506  CG  MET B 239      61.552  61.823  42.423  1.00 28.86           C  
ANISOU 5506  CG  MET B 239     3635   3017   4311    262  -1901   -284       C  
ATOM   5507  SD  MET B 239      62.749  62.199  43.719  1.00 27.46           S  
ANISOU 5507  SD  MET B 239     3362   3264   3804    373  -1530   -606       S  
ATOM   5508  CE  MET B 239      64.109  61.141  43.221  1.00 28.50           C  
ANISOU 5508  CE  MET B 239     3219   3163   4444    442  -1474   -263       C  
ATOM   5509  N   THR B 240      60.392  63.540  38.090  1.00 31.18           N  
ANISOU 5509  N   THR B 240     3949   3152   4746     80  -2220     89       N  
ATOM   5510  CA  THR B 240      60.723  64.217  36.843  1.00 31.41           C  
ANISOU 5510  CA  THR B 240     4058   3171   4705     41  -2381     82       C  
ATOM   5511  C   THR B 240      61.263  65.615  37.137  1.00 31.12           C  
ANISOU 5511  C   THR B 240     4106   3091   4627     27  -2383    135       C  
ATOM   5512  O   THR B 240      60.494  66.536  37.408  1.00 31.89           O  
ANISOU 5512  O   THR B 240     4212   3228   4674      1  -2360    139       O  
ATOM   5513  CB  THR B 240      59.521  64.245  35.879  1.00 31.58           C  
ANISOU 5513  CB  THR B 240     4098   3142   4758     36  -2380     47       C  
ATOM   5514  OG1 THR B 240      59.140  62.895  35.594  1.00 33.00           O  
ANISOU 5514  OG1 THR B 240     4052   3427   5059    -99  -2530    -18       O  
ATOM   5515  CG2 THR B 240      59.901  64.928  34.576  1.00 30.89           C  
ANISOU 5515  CG2 THR B 240     4162   2967   4605    154  -2504     22       C  
ATOM   5516  N   ILE B 241      62.584  65.764  37.077  1.00 30.53           N  
ANISOU 5516  N   ILE B 241     4096   3020   4483    -21  -2460    173       N  
ATOM   5517  CA  ILE B 241      63.244  67.040  37.351  1.00 30.47           C  
ANISOU 5517  CA  ILE B 241     4074   3065   4439    -37  -2490    161       C  
ATOM   5518  C   ILE B 241      62.916  68.072  36.276  1.00 31.32           C  
ANISOU 5518  C   ILE B 241     4220   3179   4500    -78  -2439    120       C  
ATOM   5519  O   ILE B 241      63.003  67.781  35.081  1.00 31.67           O  
ANISOU 5519  O   ILE B 241     4366   3255   4410    -85  -2443    187       O  
ATOM   5520  CB  ILE B 241      64.765  66.847  37.534  1.00 30.37           C  
ANISOU 5520  CB  ILE B 241     4121   3005   4413   -102  -2525    171       C  
ATOM   5521  CG1 ILE B 241      64.997  65.913  38.723  1.00 30.31           C  
ANISOU 5521  CG1 ILE B 241     4011   2904   4600    -57  -2510    337       C  
ATOM   5522  CG2 ILE B 241      65.482  68.190  37.771  1.00 29.31           C  
ANISOU 5522  CG2 ILE B 241     3894   2908   4334    -86  -2495    136       C  
ATOM   5523  CD1 ILE B 241      66.409  65.438  38.836  1.00 32.76           C  
ANISOU 5523  CD1 ILE B 241     4282   3458   4704   -136  -2585    337       C  
ATOM   5524  N   ILE B 242      62.491  69.255  36.713  1.00 31.54           N  
ANISOU 5524  N   ILE B 242     4170   3222   4588     35  -2436     88       N  
ATOM   5525  CA  ILE B 242      62.142  70.358  35.821  1.00 32.25           C  
ANISOU 5525  CA  ILE B 242     4200   3372   4679     20  -2399     31       C  
ATOM   5526  C   ILE B 242      62.836  71.660  36.207  1.00 32.20           C  
ANISOU 5526  C   ILE B 242     4199   3315   4718     12  -2391      0       C  
ATOM   5527  O   ILE B 242      62.730  72.652  35.485  1.00 32.87           O  
ANISOU 5527  O   ILE B 242     4264   3360   4864     32  -2399    -46       O  
ATOM   5528  CB  ILE B 242      60.617  70.612  35.770  1.00 31.81           C  
ANISOU 5528  CB  ILE B 242     4132   3319   4633     69  -2479     43       C  
ATOM   5529  CG1 ILE B 242      60.049  70.796  37.182  1.00 32.09           C  
ANISOU 5529  CG1 ILE B 242     3985   3459   4747    301  -2423    162       C  
ATOM   5530  CG2 ILE B 242      59.921  69.495  34.991  1.00 32.77           C  
ANISOU 5530  CG2 ILE B 242     4242   3555   4651   -134  -2399     -1       C  
ATOM   5531  CD1 ILE B 242      58.763  71.604  37.238  1.00 33.37           C  
ANISOU 5531  CD1 ILE B 242     4326   3385   4968    517  -2418    349       C  
ATOM   5532  N   GLU B 243      63.539  71.654  37.339  1.00 32.30           N  
ANISOU 5532  N   GLU B 243     4158   3326   4786     28  -2278    -30       N  
ATOM   5533  CA  GLU B 243      64.252  72.838  37.813  1.00 31.74           C  
ANISOU 5533  CA  GLU B 243     4121   3199   4740     95  -2213    -59       C  
ATOM   5534  C   GLU B 243      65.486  72.416  38.610  1.00 30.71           C  
ANISOU 5534  C   GLU B 243     3912   3011   4744    117  -2158    -22       C  
ATOM   5535  O   GLU B 243      65.416  71.490  39.422  1.00 29.81           O  
ANISOU 5535  O   GLU B 243     3785   2938   4601     36  -2119    -97       O  
ATOM   5536  CB  GLU B 243      63.328  73.718  38.667  1.00 32.05           C  
ANISOU 5536  CB  GLU B 243     4138   3267   4771    151  -2156    -90       C  
ATOM   5537  CG  GLU B 243      63.965  75.003  39.226  1.00 32.17           C  
ANISOU 5537  CG  GLU B 243     4364   3212   4644    294  -2246   -134       C  
ATOM   5538  CD  GLU B 243      63.509  75.366  40.638  1.00 33.63           C  
ANISOU 5538  CD  GLU B 243     4549   3346   4880    445  -2235   -481       C  
ATOM   5539  OE1 GLU B 243      62.364  75.075  41.035  1.00 32.61           O  
ANISOU 5539  OE1 GLU B 243     4357   3200   4832    449  -2196   -729       O  
ATOM   5540  OE2 GLU B 243      64.314  75.961  41.386  1.00 35.34           O  
ANISOU 5540  OE2 GLU B 243     5314   3713   4399    643  -2190   -543       O  
ATOM   5541  N   ALA B 244      66.608  73.096  38.376  1.00 30.34           N  
ANISOU 5541  N   ALA B 244     3858   2912   4755    187  -2048     74       N  
ATOM   5542  CA  ALA B 244      67.801  72.963  39.216  1.00 29.62           C  
ANISOU 5542  CA  ALA B 244     3725   2825   4704    189  -2003     89       C  
ATOM   5543  C   ALA B 244      68.304  74.343  39.654  1.00 29.53           C  
ANISOU 5543  C   ALA B 244     3647   2848   4725    192  -1946    133       C  
ATOM   5544  O   ALA B 244      68.512  75.233  38.816  1.00 30.30           O  
ANISOU 5544  O   ALA B 244     3690   2859   4960    140  -1884    183       O  
ATOM   5545  CB  ALA B 244      68.884  72.203  38.476  1.00 29.47           C  
ANISOU 5545  CB  ALA B 244     3707   2772   4717    249  -2034    152       C  
ATOM   5546  N   ASP B 245      68.455  74.528  40.966  1.00 28.73           N  
ANISOU 5546  N   ASP B 245     3504   2741   4670    226  -1901     77       N  
ATOM   5547  CA  ASP B 245      68.873  75.807  41.549  1.00 28.44           C  
ANISOU 5547  CA  ASP B 245     3595   2686   4524    232  -1848     33       C  
ATOM   5548  C   ASP B 245      68.174  77.012  40.896  1.00 29.07           C  
ANISOU 5548  C   ASP B 245     3843   2646   4554    251  -1833     41       C  
ATOM   5549  O   ASP B 245      68.835  77.945  40.436  1.00 28.35           O  
ANISOU 5549  O   ASP B 245     3705   2495   4569    299  -1803    -44       O  
ATOM   5550  CB  ASP B 245      70.401  75.990  41.467  1.00 28.49           C  
ANISOU 5550  CB  ASP B 245     3569   2786   4468    222  -1792     32       C  
ATOM   5551  CG  ASP B 245      71.196  74.857  42.109  1.00 27.46           C  
ANISOU 5551  CG  ASP B 245     3253   2725   4453    132  -1601    -42       C  
ATOM   5552  OD1 ASP B 245      70.613  73.931  42.715  1.00 25.59           O  
ANISOU 5552  OD1 ASP B 245     2849   2464   4408      1  -1486   -245       O  
ATOM   5553  OD2 ASP B 245      72.449  74.903  42.022  1.00 26.59           O  
ANISOU 5553  OD2 ASP B 245     2973   3016   4115    -42  -1596    123       O  
ATOM   5554  N   ALA B 246      66.845  76.977  40.826  1.00 29.39           N  
ANISOU 5554  N   ALA B 246     4051   2661   4455    272  -1901     41       N  
ATOM   5555  CA  ALA B 246      66.042  78.072  40.267  1.00 31.09           C  
ANISOU 5555  CA  ALA B 246     4444   2881   4487    248  -1901    126       C  
ATOM   5556  C   ALA B 246      66.190  78.350  38.767  1.00 32.38           C  
ANISOU 5556  C   ALA B 246     4726   3040   4537    244  -1936    222       C  
ATOM   5557  O   ALA B 246      65.790  79.415  38.292  1.00 34.32           O  
ANISOU 5557  O   ALA B 246     5008   3274   4759    266  -1821    294       O  
ATOM   5558  CB  ALA B 246      66.228  79.356  41.078  1.00 30.94           C  
ANISOU 5558  CB  ALA B 246     4418   2787   4549    283  -1861    104       C  
ATOM   5559  N   VAL B 247      66.760  77.417  38.010  1.00 32.70           N  
ANISOU 5559  N   VAL B 247     4974   3118   4333    158  -2042    224       N  
ATOM   5560  CA  VAL B 247      66.790  77.556  36.555  1.00 33.15           C  
ANISOU 5560  CA  VAL B 247     5156   3266   4170    108  -2176    283       C  
ATOM   5561  C   VAL B 247      66.046  76.381  35.924  1.00 33.53           C  
ANISOU 5561  C   VAL B 247     5324   3299   4116    126  -2295    390       C  
ATOM   5562  O   VAL B 247      66.296  75.225  36.262  1.00 33.03           O  
ANISOU 5562  O   VAL B 247     5296   3252   3999    186  -2355    439       O  
ATOM   5563  CB  VAL B 247      68.234  77.631  36.003  1.00 33.54           C  
ANISOU 5563  CB  VAL B 247     5241   3311   4192     70  -2100    228       C  
ATOM   5564  CG1 VAL B 247      68.208  77.765  34.479  1.00 32.83           C  
ANISOU 5564  CG1 VAL B 247     5175   3267   4030     76  -2209    437       C  
ATOM   5565  CG2 VAL B 247      69.011  78.801  36.621  1.00 33.25           C  
ANISOU 5565  CG2 VAL B 247     5156   3351   4124     86  -2067    125       C  
ATOM   5566  N   ASN B 248      65.134  76.669  35.001  1.00 33.43           N  
ANISOU 5566  N   ASN B 248     5478   3322   3898    122  -2462    472       N  
ATOM   5567  CA  ASN B 248      64.348  75.620  34.366  1.00 34.36           C  
ANISOU 5567  CA  ASN B 248     5696   3347   4010    107  -2519    481       C  
ATOM   5568  C   ASN B 248      65.176  74.694  33.484  1.00 35.21           C  
ANISOU 5568  C   ASN B 248     5882   3421   4074     81  -2496    450       C  
ATOM   5569  O   ASN B 248      66.001  75.156  32.685  1.00 35.14           O  
ANISOU 5569  O   ASN B 248     5984   3313   4053     16  -2449    443       O  
ATOM   5570  CB  ASN B 248      63.219  76.218  33.523  1.00 33.73           C  
ANISOU 5570  CB  ASN B 248     5668   3368   3779    124  -2589    536       C  
ATOM   5571  CG  ASN B 248      62.274  77.060  34.351  1.00 33.09           C  
ANISOU 5571  CG  ASN B 248     5632   3335   3603     91  -2609    549       C  
ATOM   5572  OD1 ASN B 248      62.131  76.851  35.559  1.00 31.43           O  
ANISOU 5572  OD1 ASN B 248     5557   3268   3116   -194  -2656    162       O  
ATOM   5573  ND2 ASN B 248      61.645  78.035  33.713  1.00 33.53           N  
ANISOU 5573  ND2 ASN B 248     5543   3535   3661    133  -2641    628       N  
ATOM   5574  N   THR B 249      64.927  73.396  33.642  1.00 35.60           N  
ANISOU 5574  N   THR B 249     5997   3405   4123     43  -2573    529       N  
ATOM   5575  CA  THR B 249      65.566  72.373  32.821  1.00 36.12           C  
ANISOU 5575  CA  THR B 249     6112   3444   4167     10  -2627    501       C  
ATOM   5576  C   THR B 249      64.538  71.720  31.907  1.00 37.09           C  
ANISOU 5576  C   THR B 249     6243   3595   4252     24  -2599    524       C  
ATOM   5577  O   THR B 249      63.333  71.830  32.148  1.00 37.74           O  
ANISOU 5577  O   THR B 249     6370   3676   4291     30  -2587    574       O  
ATOM   5578  CB  THR B 249      66.232  71.278  33.684  1.00 35.90           C  
ANISOU 5578  CB  THR B 249     6055   3472   4111    -32  -2652    471       C  
ATOM   5579  OG1 THR B 249      65.233  70.483  34.334  1.00 35.14           O  
ANISOU 5579  OG1 THR B 249     6037   3260   4053     47  -2760    640       O  
ATOM   5580  CG2 THR B 249      67.153  71.903  34.728  1.00 35.72           C  
ANISOU 5580  CG2 THR B 249     6015   3411   4144    -52  -2783    445       C  
ATOM   5581  N   LYS B 250      65.011  71.045  30.863  1.00 38.12           N  
ANISOU 5581  N   LYS B 250     6347   3734   4401      5  -2523    477       N  
ATOM   5582  CA  LYS B 250      64.167  70.100  30.136  1.00 39.07           C  
ANISOU 5582  CA  LYS B 250     6461   3836   4545    -15  -2420    406       C  
ATOM   5583  C   LYS B 250      63.826  68.993  31.135  1.00 38.78           C  
ANISOU 5583  C   LYS B 250     6333   3825   4577    -23  -2402    393       C  
ATOM   5584  O   LYS B 250      64.680  68.610  31.941  1.00 39.19           O  
ANISOU 5584  O   LYS B 250     6414   3865   4610    -36  -2319    442       O  
ATOM   5585  CB  LYS B 250      64.897  69.492  28.936  1.00 39.57           C  
ANISOU 5585  CB  LYS B 250     6567   3951   4515      4  -2430    426       C  
ATOM   5586  CG  LYS B 250      65.540  70.471  27.970  1.00 41.31           C  
ANISOU 5586  CG  LYS B 250     6912   4081   4700    -49  -2279    417       C  
ATOM   5587  CD  LYS B 250      65.642  69.817  26.595  1.00 45.37           C  
ANISOU 5587  CD  LYS B 250     7669   4661   4907    -68  -1978    371       C  
ATOM   5588  CE  LYS B 250      66.713  70.453  25.721  1.00 47.34           C  
ANISOU 5588  CE  LYS B 250     8049   4870   5066    -50  -1829    534       C  
ATOM   5589  NZ  LYS B 250      66.293  71.791  25.226  1.00 48.86           N  
ANISOU 5589  NZ  LYS B 250     8413   5131   5018     26  -1783    567       N  
ATOM   5590  N   PRO B 251      62.585  68.475  31.092  1.00 38.55           N  
ANISOU 5590  N   PRO B 251     6199   3826   4619      1  -2352    369       N  
ATOM   5591  CA  PRO B 251      62.211  67.423  32.035  1.00 37.84           C  
ANISOU 5591  CA  PRO B 251     6034   3757   4585    -13  -2337    300       C  
ATOM   5592  C   PRO B 251      63.118  66.204  31.914  1.00 36.87           C  
ANISOU 5592  C   PRO B 251     5832   3691   4483    -64  -2306    231       C  
ATOM   5593  O   PRO B 251      63.489  65.802  30.808  1.00 37.21           O  
ANISOU 5593  O   PRO B 251     5931   3650   4557    -84  -2204    176       O  
ATOM   5594  CB  PRO B 251      60.780  67.062  31.629  1.00 37.26           C  
ANISOU 5594  CB  PRO B 251     5970   3705   4481    -20  -2440    270       C  
ATOM   5595  CG  PRO B 251      60.269  68.286  30.943  1.00 38.74           C  
ANISOU 5595  CG  PRO B 251     6145   3835   4739     21  -2345    402       C  
ATOM   5596  CD  PRO B 251      61.453  68.885  30.242  1.00 38.69           C  
ANISOU 5596  CD  PRO B 251     6198   3866   4636      5  -2384    382       C  
ATOM   5597  N   HIS B 252      63.489  65.640  33.054  1.00 35.56           N  
ANISOU 5597  N   HIS B 252     5534   3619   4356    -94  -2243    173       N  
ATOM   5598  CA  HIS B 252      64.361  64.478  33.065  1.00 34.54           C  
ANISOU 5598  CA  HIS B 252     5237   3640   4246    -52  -2191    178       C  
ATOM   5599  C   HIS B 252      64.007  63.613  34.261  1.00 33.95           C  
ANISOU 5599  C   HIS B 252     5042   3584   4271    -39  -2145    144       C  
ATOM   5600  O   HIS B 252      64.118  64.046  35.415  1.00 33.54           O  
ANISOU 5600  O   HIS B 252     4968   3679   4096     -2  -2277    272       O  
ATOM   5601  CB  HIS B 252      65.839  64.875  33.074  1.00 34.82           C  
ANISOU 5601  CB  HIS B 252     5280   3676   4271    -75  -2106    195       C  
ATOM   5602  CG  HIS B 252      66.768  63.709  33.221  1.00 35.04           C  
ANISOU 5602  CG  HIS B 252     5059   3834   4418   -112  -1949    341       C  
ATOM   5603  ND1 HIS B 252      66.845  62.695  32.290  1.00 35.55           N  
ANISOU 5603  ND1 HIS B 252     5023   4111   4370    -22  -1630    372       N  
ATOM   5604  CD2 HIS B 252      67.641  63.382  34.204  1.00 35.80           C  
ANISOU 5604  CD2 HIS B 252     5189   3971   4442   -201  -1841    378       C  
ATOM   5605  CE1 HIS B 252      67.735  61.802  32.684  1.00 35.58           C  
ANISOU 5605  CE1 HIS B 252     5284   3971   4264    -54  -1653    476       C  
ATOM   5606  NE2 HIS B 252      68.234  62.196  33.842  1.00 35.74           N  
ANISOU 5606  NE2 HIS B 252     4972   3999   4608   -142  -1792    472       N  
ATOM   5607  N   THR B 253      63.569  62.393  33.965  1.00 33.24           N  
ANISOU 5607  N   THR B 253     4771   3534   4322     56  -2074    109       N  
ATOM   5608  CA  THR B 253      63.038  61.512  35.000  1.00 32.26           C  
ANISOU 5608  CA  THR B 253     4527   3421   4308     82  -2002     88       C  
ATOM   5609  C   THR B 253      64.108  60.608  35.593  1.00 31.40           C  
ANISOU 5609  C   THR B 253     4316   3335   4277     81  -1908     -1       C  
ATOM   5610  O   THR B 253      64.857  59.967  34.862  1.00 31.84           O  
ANISOU 5610  O   THR B 253     4402   3463   4231     71  -1875    -52       O  
ATOM   5611  CB  THR B 253      61.840  60.703  34.467  1.00 32.17           C  
ANISOU 5611  CB  THR B 253     4496   3417   4309    151  -2021    116       C  
ATOM   5612  OG1 THR B 253      60.858  61.626  33.981  1.00 33.12           O  
ANISOU 5612  OG1 THR B 253     4541   3728   4316    162  -2184    196       O  
ATOM   5613  CG2 THR B 253      61.223  59.859  35.568  1.00 31.71           C  
ANISOU 5613  CG2 THR B 253     4326   3345   4374    200  -1972    182       C  
ATOM   5614  N   VAL B 254      64.167  60.571  36.923  1.00 30.54           N  
ANISOU 5614  N   VAL B 254     4071   3206   4324     63  -1788    -77       N  
ATOM   5615  CA  VAL B 254      65.140  59.783  37.685  1.00 29.08           C  
ANISOU 5615  CA  VAL B 254     3845   2902   4301     58  -1671   -110       C  
ATOM   5616  C   VAL B 254      64.411  59.063  38.822  1.00 28.27           C  
ANISOU 5616  C   VAL B 254     3665   2732   4344     31  -1637   -123       C  
ATOM   5617  O   VAL B 254      63.276  59.415  39.124  1.00 28.05           O  
ANISOU 5617  O   VAL B 254     3613   2623   4420      7  -1685    -85       O  
ATOM   5618  CB  VAL B 254      66.240  60.696  38.288  1.00 29.00           C  
ANISOU 5618  CB  VAL B 254     3776   2942   4297     45  -1636   -178       C  
ATOM   5619  CG1 VAL B 254      67.059  61.375  37.190  1.00 28.80           C  
ANISOU 5619  CG1 VAL B 254     3875   2932   4133    168  -1614    -95       C  
ATOM   5620  CG2 VAL B 254      65.646  61.762  39.214  1.00 28.08           C  
ANISOU 5620  CG2 VAL B 254     3640   2768   4261    -17  -1652   -258       C  
ATOM   5621  N   ASP B 255      65.041  58.080  39.465  1.00 27.11           N  
ANISOU 5621  N   ASP B 255     3425   2570   4305    -13  -1588   -149       N  
ATOM   5622  CA  ASP B 255      64.429  57.436  40.628  1.00 26.27           C  
ANISOU 5622  CA  ASP B 255     3205   2508   4267      9  -1467   -103       C  
ATOM   5623  C   ASP B 255      65.161  57.690  41.951  1.00 26.18           C  
ANISOU 5623  C   ASP B 255     3140   2495   4310    -19  -1366   -104       C  
ATOM   5624  O   ASP B 255      64.760  57.205  43.016  1.00 26.01           O  
ANISOU 5624  O   ASP B 255     3097   2601   4182     90  -1466    -18       O  
ATOM   5625  CB  ASP B 255      64.186  55.934  40.384  1.00 26.44           C  
ANISOU 5625  CB  ASP B 255     3208   2504   4331    -43  -1447    -94       C  
ATOM   5626  CG  ASP B 255      65.467  55.105  40.326  1.00 27.02           C  
ANISOU 5626  CG  ASP B 255     3283   2649   4334    -40  -1342    -92       C  
ATOM   5627  OD1 ASP B 255      66.590  55.662  40.347  1.00 26.40           O  
ANISOU 5627  OD1 ASP B 255     3373   2852   3803   -119  -1229    109       O  
ATOM   5628  OD2 ASP B 255      65.344  53.857  40.275  1.00 27.63           O  
ANISOU 5628  OD2 ASP B 255     3135   2965   4397   -287  -1302    -94       O  
ATOM   5629  N   SER B 256      66.242  58.456  41.867  1.00 25.81           N  
ANISOU 5629  N   SER B 256     2993   2498   4313     76  -1243    -84       N  
ATOM   5630  CA  SER B 256      66.941  58.968  43.042  1.00 25.16           C  
ANISOU 5630  CA  SER B 256     2860   2368   4329     40  -1129    -60       C  
ATOM   5631  C   SER B 256      67.861  60.104  42.602  1.00 24.70           C  
ANISOU 5631  C   SER B 256     2784   2358   4239     51  -1080    -61       C  
ATOM   5632  O   SER B 256      68.141  60.263  41.407  1.00 24.33           O  
ANISOU 5632  O   SER B 256     2720   2251   4273     65  -1170     10       O  
ATOM   5633  CB  SER B 256      67.732  57.858  43.737  1.00 25.80           C  
ANISOU 5633  CB  SER B 256     2955   2455   4391     86  -1059    -36       C  
ATOM   5634  OG  SER B 256      68.934  57.575  43.048  1.00 27.70           O  
ANISOU 5634  OG  SER B 256     3110   2386   5027     78   -832     13       O  
ATOM   5635  N   LEU B 257      68.339  60.884  43.568  1.00 23.27           N  
ANISOU 5635  N   LEU B 257     2537   2163   4139     58   -953    -22       N  
ATOM   5636  CA  LEU B 257      69.233  61.987  43.260  1.00 22.54           C  
ANISOU 5636  CA  LEU B 257     2274   2246   4042    104   -890    -71       C  
ATOM   5637  C   LEU B 257      70.088  62.279  44.478  1.00 22.17           C  
ANISOU 5637  C   LEU B 257     2222   2261   3939     76   -772    -51       C  
ATOM   5638  O   LEU B 257      69.674  62.017  45.611  1.00 22.16           O  
ANISOU 5638  O   LEU B 257     2103   2363   3954     44   -798    -96       O  
ATOM   5639  CB  LEU B 257      68.448  63.230  42.811  1.00 22.56           C  
ANISOU 5639  CB  LEU B 257     2339   2153   4078    113   -887    -70       C  
ATOM   5640  CG  LEU B 257      67.417  63.879  43.744  1.00 22.25           C  
ANISOU 5640  CG  LEU B 257     2141   2211   4100    104  -1081    -92       C  
ATOM   5641  CD1 LEU B 257      68.070  64.850  44.753  1.00 22.89           C  
ANISOU 5641  CD1 LEU B 257     2136   2249   4311    297  -1224   -141       C  
ATOM   5642  CD2 LEU B 257      66.371  64.616  42.911  1.00 24.28           C  
ANISOU 5642  CD2 LEU B 257     2494   2568   4161    267  -1123    198       C  
ATOM   5643  N   GLU B 258      71.293  62.780  44.216  1.00 21.50           N  
ANISOU 5643  N   GLU B 258     2083   2270   3815    158   -625    -27       N  
ATOM   5644  CA  GLU B 258      72.141  63.342  45.253  1.00 20.82           C  
ANISOU 5644  CA  GLU B 258     2109   2211   3588    125   -539     31       C  
ATOM   5645  C   GLU B 258      71.916  64.851  45.240  1.00 20.91           C  
ANISOU 5645  C   GLU B 258     2126   2245   3570    114   -536     98       C  
ATOM   5646  O   GLU B 258      71.878  65.477  44.171  1.00 21.83           O  
ANISOU 5646  O   GLU B 258     2483   2279   3533     67   -575     71       O  
ATOM   5647  CB  GLU B 258      73.620  63.013  45.014  1.00 20.75           C  
ANISOU 5647  CB  GLU B 258     2059   2275   3547    193   -568     76       C  
ATOM   5648  CG  GLU B 258      73.952  61.529  45.177  1.00 23.50           C  
ANISOU 5648  CG  GLU B 258     2295   2602   4030    214   -188     51       C  
ATOM   5649  CD  GLU B 258      75.418  61.208  44.975  1.00 27.64           C  
ANISOU 5649  CD  GLU B 258     2663   3077   4761    402    100    234       C  
ATOM   5650  OE1 GLU B 258      76.204  62.122  44.629  1.00 27.64           O  
ANISOU 5650  OE1 GLU B 258     2176   3274   5050    250    383    159       O  
ATOM   5651  OE2 GLU B 258      75.781  60.026  45.164  1.00 29.95           O  
ANISOU 5651  OE2 GLU B 258     2944   3401   5033    882    451     31       O  
ATOM   5652  N   ILE B 259      71.758  65.422  46.428  1.00 19.54           N  
ANISOU 5652  N   ILE B 259     1924   2098   3403    107   -461     71       N  
ATOM   5653  CA  ILE B 259      71.546  66.863  46.575  1.00 19.56           C  
ANISOU 5653  CA  ILE B 259     1831   2128   3472    115   -474    171       C  
ATOM   5654  C   ILE B 259      72.534  67.418  47.584  1.00 19.86           C  
ANISOU 5654  C   ILE B 259     1805   2209   3531     76   -390    142       C  
ATOM   5655  O   ILE B 259      72.538  67.010  48.746  1.00 20.06           O  
ANISOU 5655  O   ILE B 259     1716   2364   3539    -25   -392    170       O  
ATOM   5656  CB  ILE B 259      70.076  67.235  46.945  1.00 19.43           C  
ANISOU 5656  CB  ILE B 259     1824   2067   3489    204   -432    202       C  
ATOM   5657  CG1 ILE B 259      69.875  68.753  46.911  1.00 18.73           C  
ANISOU 5657  CG1 ILE B 259     1454   2068   3594    306   -639    137       C  
ATOM   5658  CG2 ILE B 259      69.624  66.649  48.303  1.00 18.94           C  
ANISOU 5658  CG2 ILE B 259     2081   1763   3352    116   -347    210       C  
ATOM   5659  CD1 ILE B 259      68.399  69.184  47.018  1.00 21.05           C  
ANISOU 5659  CD1 ILE B 259     1307   2349   4343    324   -509    155       C  
ATOM   5660  N   PHE B 260      73.382  68.330  47.111  1.00 19.97           N  
ANISOU 5660  N   PHE B 260     1701   2337   3549     12   -347     50       N  
ATOM   5661  CA  PHE B 260      74.439  68.899  47.930  1.00 19.58           C  
ANISOU 5661  CA  PHE B 260     1674   2408   3356     44   -415     49       C  
ATOM   5662  C   PHE B 260      73.944  70.131  48.678  1.00 19.08           C  
ANISOU 5662  C   PHE B 260     1600   2318   3329    -13   -403     53       C  
ATOM   5663  O   PHE B 260      72.908  70.695  48.338  1.00 19.51           O  
ANISOU 5663  O   PHE B 260     1800   2192   3420     28   -340     68       O  
ATOM   5664  CB  PHE B 260      75.658  69.206  47.049  1.00 18.87           C  
ANISOU 5664  CB  PHE B 260     1557   2458   3151     68   -360     68       C  
ATOM   5665  CG  PHE B 260      76.241  67.967  46.414  1.00 20.04           C  
ANISOU 5665  CG  PHE B 260     1778   2760   3076    186   -396    -45       C  
ATOM   5666  CD1 PHE B 260      75.759  67.493  45.199  1.00 20.94           C  
ANISOU 5666  CD1 PHE B 260     1932   2982   3042    304   -235   -145       C  
ATOM   5667  CD2 PHE B 260      77.247  67.253  47.053  1.00 21.36           C  
ANISOU 5667  CD2 PHE B 260     1945   2992   3176    282   -171     42       C  
ATOM   5668  CE1 PHE B 260      76.264  66.323  44.642  1.00 22.31           C  
ANISOU 5668  CE1 PHE B 260     2114   3354   3007    252   -184   -188       C  
ATOM   5669  CE2 PHE B 260      77.772  66.105  46.497  1.00 22.81           C  
ANISOU 5669  CE2 PHE B 260     2330   3072   3263    482   -424    -22       C  
ATOM   5670  CZ  PHE B 260      77.267  65.621  45.289  1.00 23.13           C  
ANISOU 5670  CZ  PHE B 260     2448   3075   3262    456   -245    -93       C  
ATOM   5671  N   ALA B 261      74.690  70.531  49.701  1.00 19.07           N  
ANISOU 5671  N   ALA B 261     1724   2184   3337   -139   -415     52       N  
ATOM   5672  CA  ALA B 261      74.318  71.650  50.560  1.00 18.34           C  
ANISOU 5672  CA  ALA B 261     1506   2156   3304    -92   -478     55       C  
ATOM   5673  C   ALA B 261      73.921  72.895  49.768  1.00 19.08           C  
ANISOU 5673  C   ALA B 261     1574   2200   3475   -115   -518      7       C  
ATOM   5674  O   ALA B 261      74.709  73.439  48.991  1.00 18.84           O  
ANISOU 5674  O   ALA B 261     1483   2132   3541    -67   -518    162       O  
ATOM   5675  CB  ALA B 261      75.465  71.950  51.519  1.00 18.29           C  
ANISOU 5675  CB  ALA B 261     1591   2093   3264   -245   -565     17       C  
ATOM   5676  N   GLY B 262      72.668  73.308  49.937  1.00 18.85           N  
ANISOU 5676  N   GLY B 262     1484   2104   3575    -11   -607    -47       N  
ATOM   5677  CA  GLY B 262      72.136  74.499  49.289  1.00 19.71           C  
ANISOU 5677  CA  GLY B 262     1807   2277   3404     19   -706     36       C  
ATOM   5678  C   GLY B 262      71.657  74.409  47.851  1.00 20.64           C  
ANISOU 5678  C   GLY B 262     1927   2400   3513     67   -709     12       C  
ATOM   5679  O   GLY B 262      71.222  75.428  47.284  1.00 20.46           O  
ANISOU 5679  O   GLY B 262     1975   2381   3416     96   -765     70       O  
ATOM   5680  N   GLN B 263      71.729  73.217  47.259  1.00 20.41           N  
ANISOU 5680  N   GLN B 263     2007   2339   3406    205   -653    -25       N  
ATOM   5681  CA  GLN B 263      71.094  72.980  45.964  1.00 20.58           C  
ANISOU 5681  CA  GLN B 263     2001   2432   3383    245   -741     12       C  
ATOM   5682  C   GLN B 263      69.576  72.851  46.121  1.00 21.41           C  
ANISOU 5682  C   GLN B 263     2119   2484   3532    205   -735    -53       C  
ATOM   5683  O   GLN B 263      69.077  72.544  47.216  1.00 21.72           O  
ANISOU 5683  O   GLN B 263     2265   2511   3475    164   -825    -23       O  
ATOM   5684  CB  GLN B 263      71.627  71.717  45.279  1.00 19.96           C  
ANISOU 5684  CB  GLN B 263     1975   2422   3184    280   -671     51       C  
ATOM   5685  CG  GLN B 263      73.088  71.824  44.845  1.00 20.67           C  
ANISOU 5685  CG  GLN B 263     2110   2562   3180    252   -519    138       C  
ATOM   5686  CD  GLN B 263      73.629  70.566  44.172  1.00 20.14           C  
ANISOU 5686  CD  GLN B 263     2178   2649   2824    307   -199    379       C  
ATOM   5687  OE1 GLN B 263      73.207  69.448  44.475  1.00 20.55           O  
ANISOU 5687  OE1 GLN B 263     2089   2778   2939    235   -424    760       O  
ATOM   5688  NE2 GLN B 263      74.558  70.749  43.236  1.00 17.80           N  
ANISOU 5688  NE2 GLN B 263     2220   2672   1869    440   -318    313       N  
ATOM   5689  N   ARG B 264      68.874  73.076  45.012  1.00 21.13           N  
ANISOU 5689  N   ARG B 264     2134   2337   3556    312   -869    -38       N  
ATOM   5690  CA  ARG B 264      67.428  72.893  44.901  1.00 22.24           C  
ANISOU 5690  CA  ARG B 264     2219   2355   3875    170   -929   -153       C  
ATOM   5691  C   ARG B 264      67.069  72.143  43.624  1.00 23.23           C  
ANISOU 5691  C   ARG B 264     2358   2492   3973    179  -1018   -182       C  
ATOM   5692  O   ARG B 264      67.714  72.318  42.591  1.00 24.04           O  
ANISOU 5692  O   ARG B 264     2400   2617   4114    -19   -922   -221       O  
ATOM   5693  CB  ARG B 264      66.695  74.245  44.880  1.00 21.99           C  
ANISOU 5693  CB  ARG B 264     2235   2331   3789    226   -960   -143       C  
ATOM   5694  CG  ARG B 264      66.755  75.024  46.206  1.00 23.20           C  
ANISOU 5694  CG  ARG B 264     2346   2436   4033    156   -786   -226       C  
ATOM   5695  CD  ARG B 264      68.003  75.885  46.294  1.00 23.13           C  
ANISOU 5695  CD  ARG B 264     2412   2345   4030    166  -1113    -88       C  
ATOM   5696  NE  ARG B 264      68.029  76.931  45.275  1.00 24.43           N  
ANISOU 5696  NE  ARG B 264     2537   2438   4306    313   -826     75       N  
ATOM   5697  CZ  ARG B 264      69.136  77.430  44.730  1.00 25.11           C  
ANISOU 5697  CZ  ARG B 264     2859   2458   4223    325   -883    265       C  
ATOM   5698  NH1 ARG B 264      70.340  76.979  45.087  1.00 24.58           N  
ANISOU 5698  NH1 ARG B 264     2857   2366   4117    414   -961    153       N  
ATOM   5699  NH2 ARG B 264      69.039  78.390  43.818  1.00 25.17           N  
ANISOU 5699  NH2 ARG B 264     3124   2562   3877    341   -829    437       N  
ATOM   5700  N   TYR B 265      66.025  71.318  43.686  1.00 24.03           N  
ANISOU 5700  N   TYR B 265     2487   2526   4117    147  -1203   -287       N  
ATOM   5701  CA  TYR B 265      65.437  70.708  42.501  1.00 24.78           C  
ANISOU 5701  CA  TYR B 265     2544   2681   4187    229  -1461   -299       C  
ATOM   5702  C   TYR B 265      63.925  70.772  42.666  1.00 25.87           C  
ANISOU 5702  C   TYR B 265     2600   2873   4355    297  -1610   -290       C  
ATOM   5703  O   TYR B 265      63.423  70.549  43.772  1.00 26.16           O  
ANISOU 5703  O   TYR B 265     2698   3096   4142    347  -1744   -264       O  
ATOM   5704  CB  TYR B 265      65.826  69.225  42.382  1.00 24.76           C  
ANISOU 5704  CB  TYR B 265     2527   2681   4200    251  -1405   -427       C  
ATOM   5705  CG  TYR B 265      67.266  68.956  42.014  1.00 25.69           C  
ANISOU 5705  CG  TYR B 265     2779   2681   4299    142  -1063   -466       C  
ATOM   5706  CD1 TYR B 265      67.740  69.235  40.736  1.00 26.55           C  
ANISOU 5706  CD1 TYR B 265     3022   2786   4279    170   -856   -522       C  
ATOM   5707  CD2 TYR B 265      68.144  68.404  42.937  1.00 25.17           C  
ANISOU 5707  CD2 TYR B 265     2470   2638   4455    321   -883   -350       C  
ATOM   5708  CE1 TYR B 265      69.064  68.997  40.391  1.00 26.15           C  
ANISOU 5708  CE1 TYR B 265     2872   2980   4082    169   -835   -524       C  
ATOM   5709  CE2 TYR B 265      69.476  68.144  42.595  1.00 26.16           C  
ANISOU 5709  CE2 TYR B 265     2791   2761   4386     98   -537   -370       C  
ATOM   5710  CZ  TYR B 265      69.923  68.450  41.324  1.00 25.41           C  
ANISOU 5710  CZ  TYR B 265     2770   2605   4277    246   -562   -358       C  
ATOM   5711  OH  TYR B 265      71.233  68.214  40.984  1.00 24.26           O  
ANISOU 5711  OH  TYR B 265     2720   2391   4106   -121    -93   -100       O  
ATOM   5712  N   SER B 266      63.211  71.094  41.587  1.00 25.96           N  
ANISOU 5712  N   SER B 266     2640   2800   4423    274  -1879   -329       N  
ATOM   5713  CA  SER B 266      61.770  70.841  41.504  1.00 27.57           C  
ANISOU 5713  CA  SER B 266     2718   2925   4832    340  -1979   -307       C  
ATOM   5714  C   SER B 266      61.643  69.565  40.698  1.00 27.91           C  
ANISOU 5714  C   SER B 266     2688   3002   4913    241  -2167   -311       C  
ATOM   5715  O   SER B 266      62.352  69.384  39.708  1.00 28.66           O  
ANISOU 5715  O   SER B 266     2767   3174   4947    224  -2167   -298       O  
ATOM   5716  CB  SER B 266      61.002  71.937  40.756  1.00 27.36           C  
ANISOU 5716  CB  SER B 266     2686   2934   4774    351  -1998   -330       C  
ATOM   5717  OG  SER B 266      60.880  73.103  41.552  1.00 28.80           O  
ANISOU 5717  OG  SER B 266     2870   2936   5134    487  -1853   -291       O  
ATOM   5718  N   PHE B 267      60.776  68.663  41.138  1.00 28.38           N  
ANISOU 5718  N   PHE B 267     2621   2998   5161    272  -2301   -253       N  
ATOM   5719  CA  PHE B 267      60.524  67.456  40.371  1.00 29.05           C  
ANISOU 5719  CA  PHE B 267     2645   3014   5376    198  -2453   -224       C  
ATOM   5720  C   PHE B 267      59.032  67.205  40.390  1.00 29.98           C  
ANISOU 5720  C   PHE B 267     2707   3087   5594    152  -2575   -201       C  
ATOM   5721  O   PHE B 267      58.368  67.551  41.368  1.00 30.37           O  
ANISOU 5721  O   PHE B 267     2773   3182   5581    134  -2599   -156       O  
ATOM   5722  CB  PHE B 267      61.311  66.263  40.926  1.00 28.41           C  
ANISOU 5722  CB  PHE B 267     2560   2863   5370    166  -2422   -233       C  
ATOM   5723  CG  PHE B 267      60.914  65.848  42.325  1.00 28.06           C  
ANISOU 5723  CG  PHE B 267     2426   2802   5434    224  -2362   -225       C  
ATOM   5724  CD1 PHE B 267      59.831  64.996  42.537  1.00 27.71           C  
ANISOU 5724  CD1 PHE B 267     2173   2786   5567    388  -2052   -369       C  
ATOM   5725  CD2 PHE B 267      61.660  66.266  43.421  1.00 28.05           C  
ANISOU 5725  CD2 PHE B 267     2343   2836   5476    287  -2123   -386       C  
ATOM   5726  CE1 PHE B 267      59.488  64.578  43.822  1.00 26.68           C  
ANISOU 5726  CE1 PHE B 267     2049   2568   5518    351  -2076   -421       C  
ATOM   5727  CE2 PHE B 267      61.327  65.865  44.713  1.00 27.15           C  
ANISOU 5727  CE2 PHE B 267     2163   2694   5458    414  -2039   -368       C  
ATOM   5728  CZ  PHE B 267      60.234  65.014  44.916  1.00 25.48           C  
ANISOU 5728  CZ  PHE B 267     1753   2383   5543    593  -2136   -478       C  
ATOM   5729  N   ILE B 268      58.509  66.657  39.297  1.00 31.13           N  
ANISOU 5729  N   ILE B 268     2899   3167   5760    209  -2765    -98       N  
ATOM   5730  CA  ILE B 268      57.124  66.220  39.269  1.00 32.58           C  
ANISOU 5730  CA  ILE B 268     2936   3330   6110    154  -2855   -106       C  
ATOM   5731  C   ILE B 268      56.990  64.808  39.830  1.00 33.40           C  
ANISOU 5731  C   ILE B 268     3063   3420   6206    194  -2972   -105       C  
ATOM   5732  O   ILE B 268      57.751  63.906  39.456  1.00 33.67           O  
ANISOU 5732  O   ILE B 268     3204   3377   6212    209  -2961    -47       O  
ATOM   5733  CB  ILE B 268      56.545  66.217  37.837  1.00 32.73           C  
ANISOU 5733  CB  ILE B 268     2962   3373   6098    152  -2889    -69       C  
ATOM   5734  CG1 ILE B 268      56.835  67.540  37.125  1.00 35.09           C  
ANISOU 5734  CG1 ILE B 268     3257   3515   6558    -59  -2598   -137       C  
ATOM   5735  CG2 ILE B 268      55.035  65.937  37.862  1.00 33.69           C  
ANISOU 5735  CG2 ILE B 268     3013   3492   6296     71  -2819    -89       C  
ATOM   5736  CD1 ILE B 268      56.393  68.792  37.881  1.00 37.29           C  
ANISOU 5736  CD1 ILE B 268     3490   3531   7145     36  -2275    -80       C  
ATOM   5737  N   LEU B 269      56.032  64.642  40.737  1.00 33.85           N  
ANISOU 5737  N   LEU B 269     2940   3499   6421    166  -3051   -175       N  
ATOM   5738  CA  LEU B 269      55.610  63.331  41.200  1.00 34.55           C  
ANISOU 5738  CA  LEU B 269     3008   3519   6601     84  -3150   -246       C  
ATOM   5739  C   LEU B 269      54.182  63.104  40.731  1.00 35.82           C  
ANISOU 5739  C   LEU B 269     3160   3649   6798     64  -3162   -344       C  
ATOM   5740  O   LEU B 269      53.284  63.894  41.024  1.00 35.83           O  
ANISOU 5740  O   LEU B 269     3202   3612   6799    106  -3186   -342       O  
ATOM   5741  CB  LEU B 269      55.692  63.202  42.725  1.00 34.66           C  
ANISOU 5741  CB  LEU B 269     3056   3505   6609     54  -3089   -253       C  
ATOM   5742  CG  LEU B 269      55.302  61.822  43.289  1.00 33.54           C  
ANISOU 5742  CG  LEU B 269     2863   3474   6405      9  -3200   -158       C  
ATOM   5743  CD1 LEU B 269      56.199  61.437  44.464  1.00 33.16           C  
ANISOU 5743  CD1 LEU B 269     2721   3521   6355    -92  -3158   -152       C  
ATOM   5744  CD2 LEU B 269      53.813  61.744  43.668  1.00 31.92           C  
ANISOU 5744  CD2 LEU B 269     2964   2975   6189   -261  -3214   -261       C  
ATOM   5745  N   ASN B 270      53.983  62.022  39.990  1.00 37.02           N  
ANISOU 5745  N   ASN B 270     3297   3748   7019     13  -3223   -490       N  
ATOM   5746  CA  ASN B 270      52.643  61.603  39.598  1.00 38.13           C  
ANISOU 5746  CA  ASN B 270     3388   3878   7221     -2  -3269   -570       C  
ATOM   5747  C   ASN B 270      52.130  60.606  40.634  1.00 38.74           C  
ANISOU 5747  C   ASN B 270     3462   3847   7410    -11  -3226   -645       C  
ATOM   5748  O   ASN B 270      52.740  59.554  40.845  1.00 38.29           O  
ANISOU 5748  O   ASN B 270     3439   3739   7371     68  -3305   -602       O  
ATOM   5749  CB  ASN B 270      52.695  60.964  38.214  1.00 38.63           C  
ANISOU 5749  CB  ASN B 270     3498   3979   7198    -32  -3280   -574       C  
ATOM   5750  CG  ASN B 270      51.321  60.736  37.628  1.00 40.67           C  
ANISOU 5750  CG  ASN B 270     3702   4473   7276    -88  -3299   -669       C  
ATOM   5751  OD1 ASN B 270      50.300  60.841  38.314  1.00 41.79           O  
ANISOU 5751  OD1 ASN B 270     3804   4782   7292   -153  -3250   -595       O  
ATOM   5752  ND2 ASN B 270      51.286  60.418  36.342  1.00 44.10           N  
ANISOU 5752  ND2 ASN B 270     4363   5107   7284   -199  -3124   -757       N  
ATOM   5753  N   ALA B 271      51.047  60.960  41.319  1.00 39.11           N  
ANISOU 5753  N   ALA B 271     3372   3864   7623     -4  -3250   -715       N  
ATOM   5754  CA  ALA B 271      50.513  60.103  42.374  1.00 40.00           C  
ANISOU 5754  CA  ALA B 271     3550   3860   7786    -63  -3152   -799       C  
ATOM   5755  C   ALA B 271      49.591  59.042  41.776  1.00 40.31           C  
ANISOU 5755  C   ALA B 271     3538   3880   7895   -101  -3126   -898       C  
ATOM   5756  O   ALA B 271      48.378  59.035  41.985  1.00 40.87           O  
ANISOU 5756  O   ALA B 271     3664   3902   7961    -92  -3056   -873       O  
ATOM   5757  CB  ALA B 271      49.817  60.922  43.452  1.00 39.72           C  
ANISOU 5757  CB  ALA B 271     3444   3879   7766     54  -3201   -749       C  
ATOM   5758  N   ASN B 272      50.202  58.141  41.018  1.00 40.50           N  
ANISOU 5758  N   ASN B 272     3602   3743   8043   -126  -3055   -997       N  
ATOM   5759  CA  ASN B 272      49.474  57.156  40.222  1.00 41.29           C  
ANISOU 5759  CA  ASN B 272     3714   3760   8213   -126  -2947  -1109       C  
ATOM   5760  C   ASN B 272      49.651  55.753  40.793  1.00 41.01           C  
ANISOU 5760  C   ASN B 272     3613   3665   8301   -142  -2868  -1218       C  
ATOM   5761  O   ASN B 272      49.196  54.787  40.195  1.00 41.46           O  
ANISOU 5761  O   ASN B 272     3722   3704   8324   -166  -2860  -1210       O  
ATOM   5762  CB  ASN B 272      49.986  57.181  38.780  1.00 41.46           C  
ANISOU 5762  CB  ASN B 272     3836   3754   8162   -165  -3012  -1115       C  
ATOM   5763  CG  ASN B 272      51.468  56.865  38.684  1.00 43.80           C  
ANISOU 5763  CG  ASN B 272     4306   4006   8331     33  -2810  -1047       C  
ATOM   5764  OD1 ASN B 272      52.135  56.618  39.689  1.00 45.40           O  
ANISOU 5764  OD1 ASN B 272     4525   4297   8426     30  -2954   -991       O  
ATOM   5765  ND2 ASN B 272      51.995  56.871  37.466  1.00 47.51           N  
ANISOU 5765  ND2 ASN B 272     5332   4345   8372    169  -2595   -845       N  
ATOM   5766  N   GLN B 273      50.334  55.637  41.928  1.00 39.99           N  
ANISOU 5766  N   GLN B 273     3248   3565   8379    -69  -2813  -1302       N  
ATOM   5767  CA  GLN B 273      50.524  54.345  42.585  1.00 40.00           C  
ANISOU 5767  CA  GLN B 273     3141   3571   8484   -118  -2672  -1361       C  
ATOM   5768  C   GLN B 273      49.322  53.955  43.444  1.00 39.54           C  
ANISOU 5768  C   GLN B 273     2925   3537   8558   -111  -2628  -1409       C  
ATOM   5769  O   GLN B 273      48.440  54.780  43.654  1.00 39.92           O  
ANISOU 5769  O   GLN B 273     3059   3475   8631   -155  -2591  -1459       O  
ATOM   5770  CB  GLN B 273      51.816  54.382  43.407  1.00 39.62           C  
ANISOU 5770  CB  GLN B 273     3101   3514   8438    -53  -2729  -1378       C  
ATOM   5771  CG  GLN B 273      53.060  54.535  42.536  1.00 40.91           C  
ANISOU 5771  CG  GLN B 273     3464   3565   8512   -174  -2515  -1396       C  
ATOM   5772  CD  GLN B 273      53.135  53.482  41.437  1.00 43.12           C  
ANISOU 5772  CD  GLN B 273     4030   3707   8645    113  -2221  -1391       C  
ATOM   5773  OE1 GLN B 273      53.355  52.308  41.709  1.00 43.43           O  
ANISOU 5773  OE1 GLN B 273     4171   3676   8654    253  -2168  -1419       O  
ATOM   5774  NE2 GLN B 273      52.925  53.897  40.194  1.00 43.99           N  
ANISOU 5774  NE2 GLN B 273     3997   4111   8603     13  -2040  -1383       N  
ATOM   5775  N   PRO B 274      49.256  52.701  43.928  1.00 39.38           N  
ANISOU 5775  N   PRO B 274     2762   3564   8634    -96  -2477  -1414       N  
ATOM   5776  CA  PRO B 274      48.140  52.374  44.819  1.00 38.97           C  
ANISOU 5776  CA  PRO B 274     2566   3551   8687    -73  -2392  -1401       C  
ATOM   5777  C   PRO B 274      48.110  53.221  46.088  1.00 38.30           C  
ANISOU 5777  C   PRO B 274     2328   3578   8644    -43  -2271  -1389       C  
ATOM   5778  O   PRO B 274      49.161  53.632  46.602  1.00 37.71           O  
ANISOU 5778  O   PRO B 274     2247   3488   8591     17  -2327  -1327       O  
ATOM   5779  CB  PRO B 274      48.399  50.916  45.192  1.00 39.29           C  
ANISOU 5779  CB  PRO B 274     2643   3552   8732    -98  -2349  -1409       C  
ATOM   5780  CG  PRO B 274      49.185  50.386  44.052  1.00 40.24           C  
ANISOU 5780  CG  PRO B 274     2890   3602   8797    -71  -2278  -1387       C  
ATOM   5781  CD  PRO B 274      50.087  51.517  43.650  1.00 39.36           C  
ANISOU 5781  CD  PRO B 274     2762   3527   8663   -129  -2469  -1460       C  
ATOM   5782  N   VAL B 275      46.896  53.481  46.568  1.00 37.52           N  
ANISOU 5782  N   VAL B 275     2161   3501   8591      2  -2197  -1352       N  
ATOM   5783  CA  VAL B 275      46.675  54.192  47.826  1.00 36.34           C  
ANISOU 5783  CA  VAL B 275     1858   3413   8534     -6  -2030  -1340       C  
ATOM   5784  C   VAL B 275      47.362  53.441  48.961  1.00 35.17           C  
ANISOU 5784  C   VAL B 275     1768   3217   8377    -83  -1932  -1322       C  
ATOM   5785  O   VAL B 275      47.019  52.294  49.250  1.00 34.67           O  
ANISOU 5785  O   VAL B 275     1651   3171   8349   -275  -1971  -1443       O  
ATOM   5786  CB  VAL B 275      45.161  54.325  48.121  1.00 36.37           C  
ANISOU 5786  CB  VAL B 275     1830   3438   8548    -43  -2030  -1299       C  
ATOM   5787  CG1 VAL B 275      44.942  54.933  49.498  1.00 36.70           C  
ANISOU 5787  CG1 VAL B 275     1861   3465   8616     89  -1926  -1324       C  
ATOM   5788  CG2 VAL B 275      44.496  55.192  47.067  1.00 35.86           C  
ANISOU 5788  CG2 VAL B 275     1529   3589   8506      8  -2089  -1314       C  
ATOM   5789  N   ASP B 276      48.351  54.089  49.575  1.00 34.44           N  
ANISOU 5789  N   ASP B 276     1744   3081   8258    -14  -1766  -1243       N  
ATOM   5790  CA  ASP B 276      49.218  53.473  50.572  1.00 32.99           C  
ANISOU 5790  CA  ASP B 276     1553   2939   8041      8  -1615  -1162       C  
ATOM   5791  C   ASP B 276      50.163  54.522  51.170  1.00 31.62           C  
ANISOU 5791  C   ASP B 276     1338   2812   7865     24  -1427  -1077       C  
ATOM   5792  O   ASP B 276      50.112  55.699  50.809  1.00 30.39           O  
ANISOU 5792  O   ASP B 276     1040   2694   7812      8  -1449  -1083       O  
ATOM   5793  CB  ASP B 276      50.048  52.379  49.895  1.00 33.17           C  
ANISOU 5793  CB  ASP B 276     1747   2795   8058     90  -1642  -1142       C  
ATOM   5794  CG  ASP B 276      50.422  51.237  50.827  1.00 36.07           C  
ANISOU 5794  CG  ASP B 276     2444   3028   8231     53  -1584  -1032       C  
ATOM   5795  OD1 ASP B 276      50.476  51.411  52.067  1.00 36.34           O  
ANISOU 5795  OD1 ASP B 276     2499   3021   8288    -39  -1447  -1040       O  
ATOM   5796  OD2 ASP B 276      50.685  50.142  50.282  1.00 38.47           O  
ANISOU 5796  OD2 ASP B 276     3411   2932   8271    495  -1686   -653       O  
ATOM   5797  N   ASN B 277      51.017  54.070  52.087  1.00 29.71           N  
ANISOU 5797  N   ASN B 277     1023   2736   7529     20  -1288  -1030       N  
ATOM   5798  CA  ASN B 277      52.084  54.865  52.671  1.00 28.50           C  
ANISOU 5798  CA  ASN B 277      931   2653   7244     44  -1055   -971       C  
ATOM   5799  C   ASN B 277      53.399  54.424  52.056  1.00 27.32           C  
ANISOU 5799  C   ASN B 277      890   2575   6913     70  -1034   -933       C  
ATOM   5800  O   ASN B 277      53.678  53.223  52.020  1.00 27.58           O  
ANISOU 5800  O   ASN B 277     1054   2492   6930     26   -916   -932       O  
ATOM   5801  CB  ASN B 277      52.150  54.643  54.180  1.00 28.40           C  
ANISOU 5801  CB  ASN B 277      831   2713   7244     86  -1005   -984       C  
ATOM   5802  CG  ASN B 277      50.918  55.167  54.889  1.00 29.25           C  
ANISOU 5802  CG  ASN B 277      980   2670   7464    142   -907  -1042       C  
ATOM   5803  OD1 ASN B 277      50.744  56.373  55.019  1.00 29.55           O  
ANISOU 5803  OD1 ASN B 277      907   2666   7651    269   -588  -1130       O  
ATOM   5804  ND2 ASN B 277      50.054  54.263  55.341  1.00 28.98           N  
ANISOU 5804  ND2 ASN B 277      849   2403   7757    161   -963  -1163       N  
ATOM   5805  N   TYR B 278      54.199  55.390  51.608  1.00 25.93           N  
ANISOU 5805  N   TYR B 278      776   2574   6501     27  -1067   -860       N  
ATOM   5806  CA  TYR B 278      55.474  55.116  50.933  1.00 24.91           C  
ANISOU 5806  CA  TYR B 278      810   2554   6100    -19  -1111   -814       C  
ATOM   5807  C   TYR B 278      56.593  55.863  51.637  1.00 23.98           C  
ANISOU 5807  C   TYR B 278      739   2498   5873    -24  -1028   -745       C  
ATOM   5808  O   TYR B 278      56.422  57.033  51.994  1.00 24.40           O  
ANISOU 5808  O   TYR B 278      887   2631   5750      7  -1054   -769       O  
ATOM   5809  CB  TYR B 278      55.411  55.599  49.485  1.00 25.36           C  
ANISOU 5809  CB  TYR B 278      943   2570   6122    -98  -1062   -844       C  
ATOM   5810  CG  TYR B 278      54.389  54.847  48.669  1.00 25.77           C  
ANISOU 5810  CG  TYR B 278      943   2689   6156    -26  -1466   -782       C  
ATOM   5811  CD1 TYR B 278      53.049  55.235  48.667  1.00 27.12           C  
ANISOU 5811  CD1 TYR B 278     1096   2789   6418   -204  -1524   -798       C  
ATOM   5812  CD2 TYR B 278      54.756  53.731  47.927  1.00 27.99           C  
ANISOU 5812  CD2 TYR B 278     1382   2914   6337   -173  -1520  -1008       C  
ATOM   5813  CE1 TYR B 278      52.095  54.543  47.930  1.00 27.30           C  
ANISOU 5813  CE1 TYR B 278     1446   2798   6128    -80  -1887   -850       C  
ATOM   5814  CE2 TYR B 278      53.813  53.022  47.193  1.00 28.61           C  
ANISOU 5814  CE2 TYR B 278     1286   3135   6447   -208  -1810   -750       C  
ATOM   5815  CZ  TYR B 278      52.488  53.433  47.203  1.00 28.71           C  
ANISOU 5815  CZ  TYR B 278     1570   2856   6481    -54  -1728   -774       C  
ATOM   5816  OH  TYR B 278      51.549  52.747  46.468  1.00 29.43           O  
ANISOU 5816  OH  TYR B 278     1741   2833   6608    -27  -1920   -761       O  
ATOM   5817  N   TRP B 279      57.738  55.205  51.810  1.00 23.16           N  
ANISOU 5817  N   TRP B 279      781   2444   5573    -34   -924   -700       N  
ATOM   5818  CA  TRP B 279      58.865  55.880  52.440  1.00 21.77           C  
ANISOU 5818  CA  TRP B 279      638   2324   5307    -46   -773   -575       C  
ATOM   5819  C   TRP B 279      59.470  56.954  51.534  1.00 22.16           C  
ANISOU 5819  C   TRP B 279      772   2358   5289     26   -720   -546       C  
ATOM   5820  O   TRP B 279      59.721  56.713  50.342  1.00 22.68           O  
ANISOU 5820  O   TRP B 279      893   2407   5317     16   -543   -506       O  
ATOM   5821  CB  TRP B 279      59.952  54.883  52.810  1.00 22.45           C  
ANISOU 5821  CB  TRP B 279      810   2351   5367    -79   -774   -591       C  
ATOM   5822  CG  TRP B 279      59.723  54.026  54.033  1.00 22.97           C  
ANISOU 5822  CG  TRP B 279      806   2590   5330    -91   -648   -446       C  
ATOM   5823  CD1 TRP B 279      59.739  52.654  54.077  1.00 22.79           C  
ANISOU 5823  CD1 TRP B 279      611   2623   5425   -180   -519   -370       C  
ATOM   5824  CD2 TRP B 279      59.533  54.467  55.388  1.00 23.07           C  
ANISOU 5824  CD2 TRP B 279      751   2690   5322    -96   -578   -517       C  
ATOM   5825  NE1 TRP B 279      59.555  52.221  55.370  1.00 22.55           N  
ANISOU 5825  NE1 TRP B 279      789   2331   5446     67   -682   -280       N  
ATOM   5826  CE2 TRP B 279      59.424  53.309  56.193  1.00 23.87           C  
ANISOU 5826  CE2 TRP B 279      864   2859   5347    -69   -536   -518       C  
ATOM   5827  CE3 TRP B 279      59.425  55.724  55.997  1.00 23.34           C  
ANISOU 5827  CE3 TRP B 279      576   2998   5291   -260   -635   -502       C  
ATOM   5828  CZ2 TRP B 279      59.217  53.370  57.580  1.00 23.69           C  
ANISOU 5828  CZ2 TRP B 279      617   3069   5314    -57   -652   -676       C  
ATOM   5829  CZ3 TRP B 279      59.226  55.786  57.372  1.00 24.36           C  
ANISOU 5829  CZ3 TRP B 279      737   3117   5401   -135   -311   -685       C  
ATOM   5830  CH2 TRP B 279      59.116  54.615  58.146  1.00 23.89           C  
ANISOU 5830  CH2 TRP B 279      668   2975   5431     13   -537   -630       C  
ATOM   5831  N   VAL B 280      59.678  58.135  52.112  1.00 20.81           N  
ANISOU 5831  N   VAL B 280      635   2137   5133    119   -660   -461       N  
ATOM   5832  CA  VAL B 280      60.485  59.201  51.513  1.00 20.64           C  
ANISOU 5832  CA  VAL B 280      623   2209   5008    197   -686   -394       C  
ATOM   5833  C   VAL B 280      61.846  59.113  52.193  1.00 20.73           C  
ANISOU 5833  C   VAL B 280      725   2288   4861    191   -657   -367       C  
ATOM   5834  O   VAL B 280      61.926  59.109  53.423  1.00 21.79           O  
ANISOU 5834  O   VAL B 280      839   2597   4842    262   -688   -273       O  
ATOM   5835  CB  VAL B 280      59.852  60.597  51.748  1.00 20.35           C  
ANISOU 5835  CB  VAL B 280      561   2137   5035     98   -800   -362       C  
ATOM   5836  CG1 VAL B 280      60.798  61.712  51.293  1.00 20.51           C  
ANISOU 5836  CG1 VAL B 280      969   1938   4886    304   -719   -329       C  
ATOM   5837  CG2 VAL B 280      58.466  60.677  51.066  1.00 21.85           C  
ANISOU 5837  CG2 VAL B 280      658   2516   5127    223   -895   -401       C  
ATOM   5838  N   ARG B 281      62.917  59.014  51.415  1.00 19.82           N  
ANISOU 5838  N   ARG B 281      610   2255   4664    175   -593   -273       N  
ATOM   5839  CA  ARG B 281      64.237  58.742  51.999  1.00 18.94           C  
ANISOU 5839  CA  ARG B 281      668   2017   4509    108   -555   -297       C  
ATOM   5840  C   ARG B 281      65.190  59.888  51.718  1.00 18.62           C  
ANISOU 5840  C   ARG B 281      676   1995   4403    126   -617   -254       C  
ATOM   5841  O   ARG B 281      65.262  60.365  50.584  1.00 19.96           O  
ANISOU 5841  O   ARG B 281      848   2257   4478    182   -742   -229       O  
ATOM   5842  CB  ARG B 281      64.824  57.438  51.447  1.00 18.66           C  
ANISOU 5842  CB  ARG B 281      581   1904   4603     64   -536   -343       C  
ATOM   5843  CG  ARG B 281      63.939  56.207  51.684  1.00 19.03           C  
ANISOU 5843  CG  ARG B 281      946   1755   4529     99   -422   -393       C  
ATOM   5844  CD  ARG B 281      64.490  54.990  50.952  1.00 19.79           C  
ANISOU 5844  CD  ARG B 281     1280   1757   4480    -36   -660   -491       C  
ATOM   5845  NE  ARG B 281      63.543  53.883  51.047  1.00 19.19           N  
ANISOU 5845  NE  ARG B 281     1037   1850   4401    -35   -573   -226       N  
ATOM   5846  CZ  ARG B 281      63.494  53.038  52.073  1.00 19.96           C  
ANISOU 5846  CZ  ARG B 281     1244   2107   4232     69   -715   -231       C  
ATOM   5847  NH1 ARG B 281      64.364  53.164  53.079  1.00 19.45           N  
ANISOU 5847  NH1 ARG B 281      997   2267   4123    128   -644   -166       N  
ATOM   5848  NH2 ARG B 281      62.577  52.075  52.093  1.00 19.36           N  
ANISOU 5848  NH2 ARG B 281     1307   1988   4059    173   -550   -202       N  
ATOM   5849  N   ALA B 282      65.909  60.320  52.747  1.00 17.21           N  
ANISOU 5849  N   ALA B 282      667   1803   4069     67   -635   -247       N  
ATOM   5850  CA  ALA B 282      66.986  61.300  52.576  1.00 17.15           C  
ANISOU 5850  CA  ALA B 282      745   1837   3931     91   -623   -196       C  
ATOM   5851  C   ALA B 282      68.185  60.858  53.413  1.00 16.65           C  
ANISOU 5851  C   ALA B 282      689   1865   3771     56   -605   -177       C  
ATOM   5852  O   ALA B 282      68.267  61.127  54.614  1.00 17.00           O  
ANISOU 5852  O   ALA B 282      697   1949   3810    -47   -529   -193       O  
ATOM   5853  CB  ALA B 282      66.506  62.700  52.958  1.00 17.24           C  
ANISOU 5853  CB  ALA B 282      962   1638   3951    -33   -631   -199       C  
ATOM   5854  N   ASN B 283      69.083  60.129  52.757  1.00 16.47           N  
ANISOU 5854  N   ASN B 283      613   2024   3618    155   -592    -55       N  
ATOM   5855  CA  ASN B 283      70.181  59.422  53.420  1.00 15.82           C  
ANISOU 5855  CA  ASN B 283      707   2012   3289    178   -541    -77       C  
ATOM   5856  C   ASN B 283      71.456  60.237  53.304  1.00 15.15           C  
ANISOU 5856  C   ASN B 283      597   2028   3130    192   -465    -43       C  
ATOM   5857  O   ASN B 283      71.911  60.533  52.199  1.00 17.17           O  
ANISOU 5857  O   ASN B 283     1046   2268   3207    214   -482   -147       O  
ATOM   5858  CB  ASN B 283      70.363  58.058  52.751  1.00 16.54           C  
ANISOU 5858  CB  ASN B 283      823   1996   3466    226   -559    -50       C  
ATOM   5859  CG  ASN B 283      70.965  57.017  53.669  1.00 16.03           C  
ANISOU 5859  CG  ASN B 283      838   2082   3167    187   -567    -22       C  
ATOM   5860  OD1 ASN B 283      71.053  57.209  54.885  1.00 16.74           O  
ANISOU 5860  OD1 ASN B 283      919   2144   3297    100   -586    -26       O  
ATOM   5861  ND2 ASN B 283      71.345  55.876  53.087  1.00 17.37           N  
ANISOU 5861  ND2 ASN B 283      998   2220   3381    231   -409     14       N  
ATOM   5862  N   PRO B 284      72.034  60.647  54.439  1.00 14.95           N  
ANISOU 5862  N   PRO B 284      508   2152   3020     58   -457    -11       N  
ATOM   5863  CA  PRO B 284      73.251  61.469  54.364  1.00 15.53           C  
ANISOU 5863  CA  PRO B 284      594   2187   3116     12   -322    -27       C  
ATOM   5864  C   PRO B 284      74.466  60.633  53.974  1.00 16.82           C  
ANISOU 5864  C   PRO B 284      692   2379   3319     61   -236     10       C  
ATOM   5865  O   PRO B 284      74.430  59.404  54.066  1.00 18.09           O  
ANISOU 5865  O   PRO B 284      832   2542   3497    205   -124     89       O  
ATOM   5866  CB  PRO B 284      73.419  61.962  55.805  1.00 15.13           C  
ANISOU 5866  CB  PRO B 284      675   2205   2869    -57   -453    102       C  
ATOM   5867  CG  PRO B 284      72.827  60.833  56.632  1.00 14.91           C  
ANISOU 5867  CG  PRO B 284      570   2190   2904   -267   -477     40       C  
ATOM   5868  CD  PRO B 284      71.591  60.442  55.830  1.00 13.91           C  
ANISOU 5868  CD  PRO B 284      369   2075   2841     -3   -435     10       C  
ATOM   5869  N   ASN B 285      75.525  61.294  53.523  1.00 17.59           N  
ANISOU 5869  N   ASN B 285      684   2529   3467    169   -116     -2       N  
ATOM   5870  CA  ASN B 285      76.704  60.569  53.055  1.00 17.87           C  
ANISOU 5870  CA  ASN B 285      730   2542   3518    154   -107    -33       C  
ATOM   5871  C   ASN B 285      77.561  60.086  54.206  1.00 17.77           C  
ANISOU 5871  C   ASN B 285      697   2473   3580    141   -124      7       C  
ATOM   5872  O   ASN B 285      78.383  59.193  54.018  1.00 18.23           O  
ANISOU 5872  O   ASN B 285      755   2595   3575    243   -127    -22       O  
ATOM   5873  CB  ASN B 285      77.515  61.374  52.034  1.00 18.61           C  
ANISOU 5873  CB  ASN B 285      904   2548   3618     62    -32    -69       C  
ATOM   5874  CG  ASN B 285      77.989  62.711  52.558  1.00 19.43           C  
ANISOU 5874  CG  ASN B 285      852   2778   3750     52    -27    -52       C  
ATOM   5875  OD1 ASN B 285      77.200  63.487  53.073  1.00 20.33           O  
ANISOU 5875  OD1 ASN B 285     1522   2365   3835    -59     55   -381       O  
ATOM   5876  ND2 ASN B 285      79.281  62.998  52.406  1.00 21.02           N  
ANISOU 5876  ND2 ASN B 285      657   3193   4134   -220     79     77       N  
ATOM   5877  N   PHE B 286      77.360  60.651  55.391  1.00 17.21           N  
ANISOU 5877  N   PHE B 286      657   2323   3557     47   -111     27       N  
ATOM   5878  CA  PHE B 286      78.044  60.128  56.580  1.00 17.71           C  
ANISOU 5878  CA  PHE B 286      748   2307   3672    -59   -148    -37       C  
ATOM   5879  C   PHE B 286      77.183  60.475  57.784  1.00 17.28           C  
ANISOU 5879  C   PHE B 286      667   2211   3688     17   -159    -71       C  
ATOM   5880  O   PHE B 286      76.256  61.268  57.650  1.00 18.04           O  
ANISOU 5880  O   PHE B 286      878   2200   3775    165   -292   -160       O  
ATOM   5881  CB  PHE B 286      79.466  60.697  56.720  1.00 18.90           C  
ANISOU 5881  CB  PHE B 286      950   2373   3856   -149    -12     85       C  
ATOM   5882  CG  PHE B 286      79.522  62.196  56.845  1.00 21.06           C  
ANISOU 5882  CG  PHE B 286     1447   2450   4103   -510      9     -2       C  
ATOM   5883  CD1 PHE B 286      79.397  63.015  55.730  1.00 23.68           C  
ANISOU 5883  CD1 PHE B 286     1943   2544   4508   -526    -20    127       C  
ATOM   5884  CD2 PHE B 286      79.755  62.790  58.078  1.00 25.32           C  
ANISOU 5884  CD2 PHE B 286     2490   2777   4353   -436    531    -42       C  
ATOM   5885  CE1 PHE B 286      79.472  64.410  55.845  1.00 23.88           C  
ANISOU 5885  CE1 PHE B 286     2059   2595   4417   -568     85    156       C  
ATOM   5886  CE2 PHE B 286      79.845  64.177  58.205  1.00 26.56           C  
ANISOU 5886  CE2 PHE B 286     2746   2734   4609   -265    543     35       C  
ATOM   5887  CZ  PHE B 286      79.689  64.990  57.082  1.00 25.48           C  
ANISOU 5887  CZ  PHE B 286     2486   2636   4558   -452    491     89       C  
ATOM   5888  N   GLY B 287      77.505  59.932  58.954  1.00 17.25           N  
ANISOU 5888  N   GLY B 287      652   2109   3794    107    -48     24       N  
ATOM   5889  CA  GLY B 287      76.661  60.075  60.131  1.00 17.02           C  
ANISOU 5889  CA  GLY B 287      586   2143   3737    139     55    -46       C  
ATOM   5890  C   GLY B 287      75.917  58.769  60.327  1.00 17.59           C  
ANISOU 5890  C   GLY B 287      616   2302   3765    147    117    -36       C  
ATOM   5891  O   GLY B 287      76.515  57.693  60.214  1.00 18.50           O  
ANISOU 5891  O   GLY B 287      585   2415   4029    104    271   -118       O  
ATOM   5892  N   ASN B 288      74.622  58.845  60.632  1.00 17.97           N  
ANISOU 5892  N   ASN B 288      607   2416   3804    128     69    -66       N  
ATOM   5893  CA  ASN B 288      73.779  57.658  60.638  1.00 18.40           C  
ANISOU 5893  CA  ASN B 288      738   2487   3764     63     61    -51       C  
ATOM   5894  C   ASN B 288      73.266  57.449  59.223  1.00 18.57           C  
ANISOU 5894  C   ASN B 288      705   2522   3827    127     -2      2       C  
ATOM   5895  O   ASN B 288      72.453  58.221  58.713  1.00 18.91           O  
ANISOU 5895  O   ASN B 288      650   2579   3954    294     20    -22       O  
ATOM   5896  CB  ASN B 288      72.613  57.790  61.625  1.00 18.46           C  
ANISOU 5896  CB  ASN B 288      599   2589   3824    149     38   -115       C  
ATOM   5897  CG  ASN B 288      73.090  58.179  63.016  1.00 21.75           C  
ANISOU 5897  CG  ASN B 288     1476   2884   3903    132    138    -68       C  
ATOM   5898  OD1 ASN B 288      73.415  57.318  63.831  1.00 25.53           O  
ANISOU 5898  OD1 ASN B 288     2012   3363   4323     79   -178     80       O  
ATOM   5899  ND2 ASN B 288      73.207  59.480  63.266  1.00 24.30           N  
ANISOU 5899  ND2 ASN B 288     1864   3123   4244    518     16   -420       N  
ATOM   5900  N   VAL B 289      73.795  56.422  58.573  1.00 18.19           N  
ANISOU 5900  N   VAL B 289      710   2392   3810     75   -113      2       N  
ATOM   5901  CA  VAL B 289      73.482  56.147  57.179  1.00 17.11           C  
ANISOU 5901  CA  VAL B 289      540   2302   3658    -38   -306     45       C  
ATOM   5902  C   VAL B 289      72.634  54.880  57.169  1.00 17.84           C  
ANISOU 5902  C   VAL B 289      593   2379   3805   -108   -334     33       C  
ATOM   5903  O   VAL B 289      73.022  53.840  57.714  1.00 17.53           O  
ANISOU 5903  O   VAL B 289      490   2353   3817   -245   -416     89       O  
ATOM   5904  CB  VAL B 289      74.789  55.983  56.370  1.00 16.85           C  
ANISOU 5904  CB  VAL B 289      563   2287   3552      4   -330     62       C  
ATOM   5905  CG1 VAL B 289      74.533  55.488  54.940  1.00 17.00           C  
ANISOU 5905  CG1 VAL B 289      704   2281   3473    -89   -463   -113       C  
ATOM   5906  CG2 VAL B 289      75.581  57.297  56.371  1.00 15.37           C  
ANISOU 5906  CG2 VAL B 289      508   2158   3172     36   -510    257       C  
ATOM   5907  N   GLY B 290      71.480  54.965  56.523  1.00 17.43           N  
ANISOU 5907  N   GLY B 290      448   2314   3860    -76   -304     -9       N  
ATOM   5908  CA  GLY B 290      70.554  53.838  56.512  1.00 18.13           C  
ANISOU 5908  CA  GLY B 290      554   2456   3876   -160   -146   -104       C  
ATOM   5909  C   GLY B 290      69.236  54.289  57.093  1.00 18.86           C  
ANISOU 5909  C   GLY B 290      646   2470   4047   -114   -181   -131       C  
ATOM   5910  O   GLY B 290      68.994  55.491  57.219  1.00 18.87           O  
ANISOU 5910  O   GLY B 290      636   2425   4109   -159   -127   -212       O  
ATOM   5911  N   PHE B 291      68.373  53.325  57.414  1.00 19.24           N  
ANISOU 5911  N   PHE B 291      725   2493   4090   -122    -75   -131       N  
ATOM   5912  CA  PHE B 291      66.987  53.655  57.748  1.00 19.39           C  
ANISOU 5912  CA  PHE B 291      750   2511   4104    -22    -83   -141       C  
ATOM   5913  C   PHE B 291      66.441  52.921  58.958  1.00 20.14           C  
ANISOU 5913  C   PHE B 291      943   2511   4198     33    -27    -73       C  
ATOM   5914  O   PHE B 291      65.227  52.868  59.145  1.00 20.23           O  
ANISOU 5914  O   PHE B 291      846   2501   4338      2     -5    -98       O  
ATOM   5915  CB  PHE B 291      66.088  53.423  56.530  1.00 19.02           C  
ANISOU 5915  CB  PHE B 291      661   2478   4084     71   -145    -46       C  
ATOM   5916  CG  PHE B 291      66.585  54.136  55.311  1.00 20.26           C  
ANISOU 5916  CG  PHE B 291      934   2561   4204    -83   -389    -32       C  
ATOM   5917  CD1 PHE B 291      66.277  55.475  55.113  1.00 18.71           C  
ANISOU 5917  CD1 PHE B 291      770   2247   4092    -34   -697     -5       C  
ATOM   5918  CD2 PHE B 291      67.416  53.490  54.405  1.00 20.19           C  
ANISOU 5918  CD2 PHE B 291      974   2474   4222    -57   -580   -150       C  
ATOM   5919  CE1 PHE B 291      66.774  56.156  54.013  1.00 19.61           C  
ANISOU 5919  CE1 PHE B 291     1152   2112   4184    -17   -717    -37       C  
ATOM   5920  CE2 PHE B 291      67.927  54.166  53.306  1.00 20.40           C  
ANISOU 5920  CE2 PHE B 291     1184   2513   4053    -75   -808    -62       C  
ATOM   5921  CZ  PHE B 291      67.595  55.506  53.101  1.00 20.61           C  
ANISOU 5921  CZ  PHE B 291     1017   2501   4312     46   -884   -179       C  
ATOM   5922  N   THR B 292      67.318  52.373  59.791  1.00 20.89           N  
ANISOU 5922  N   THR B 292     1119   2632   4187     67     40    -25       N  
ATOM   5923  CA  THR B 292      66.866  51.699  61.014  1.00 21.74           C  
ANISOU 5923  CA  THR B 292     1299   2698   4262    120    134      3       C  
ATOM   5924  C   THR B 292      65.929  52.595  61.814  1.00 20.85           C  
ANISOU 5924  C   THR B 292     1119   2621   4181     59    133     11       C  
ATOM   5925  O   THR B 292      66.225  53.768  62.059  1.00 19.44           O  
ANISOU 5925  O   THR B 292      977   2455   3951    147    214    131       O  
ATOM   5926  CB  THR B 292      68.079  51.315  61.893  1.00 22.29           C  
ANISOU 5926  CB  THR B 292     1391   2770   4307    212    138     40       C  
ATOM   5927  OG1 THR B 292      68.908  50.411  61.155  1.00 23.40           O  
ANISOU 5927  OG1 THR B 292     1426   2858   4606    420    335    176       O  
ATOM   5928  CG2 THR B 292      67.636  50.644  63.193  1.00 23.75           C  
ANISOU 5928  CG2 THR B 292     1705   2863   4454    200    280    144       C  
ATOM   5929  N   ASN B 293      64.805  52.020  62.236  1.00 21.57           N  
ANISOU 5929  N   ASN B 293     1420   2603   4169    -27     99    -84       N  
ATOM   5930  CA  ASN B 293      63.787  52.736  63.000  1.00 21.63           C  
ANISOU 5930  CA  ASN B 293     1381   2649   4188    -18     24    -81       C  
ATOM   5931  C   ASN B 293      63.221  53.961  62.293  1.00 21.06           C  
ANISOU 5931  C   ASN B 293     1330   2567   4104    -86    -16   -132       C  
ATOM   5932  O   ASN B 293      62.646  54.836  62.929  1.00 21.64           O  
ANISOU 5932  O   ASN B 293     1611   2579   4030     58   -110   -149       O  
ATOM   5933  CB  ASN B 293      64.321  53.098  64.399  1.00 22.41           C  
ANISOU 5933  CB  ASN B 293     1633   2649   4230      4     10   -140       C  
ATOM   5934  CG  ASN B 293      64.649  51.867  65.237  1.00 25.10           C  
ANISOU 5934  CG  ASN B 293     1946   3060   4528    -53    -19      4       C  
ATOM   5935  OD1 ASN B 293      65.638  51.840  65.981  1.00 27.73           O  
ANISOU 5935  OD1 ASN B 293     2219   3539   4776   -340   -216     19       O  
ATOM   5936  ND2 ASN B 293      63.829  50.828  65.098  1.00 25.45           N  
ANISOU 5936  ND2 ASN B 293     1980   2780   4910    -60    -59    185       N  
ATOM   5937  N   GLY B 294      63.342  54.031  60.974  1.00 20.14           N  
ANISOU 5937  N   GLY B 294     1118   2449   4084   -180    -74   -116       N  
ATOM   5938  CA  GLY B 294      62.765  55.160  60.257  1.00 19.30           C  
ANISOU 5938  CA  GLY B 294      777   2400   4156   -206   -185   -131       C  
ATOM   5939  C   GLY B 294      63.574  56.445  60.332  1.00 19.24           C  
ANISOU 5939  C   GLY B 294      668   2437   4202    -85   -207    -99       C  
ATOM   5940  O   GLY B 294      63.044  57.515  60.021  1.00 18.94           O  
ANISOU 5940  O   GLY B 294      525   2400   4270   -100   -124   -143       O  
ATOM   5941  N   ILE B 295      64.851  56.355  60.714  1.00 18.77           N  
ANISOU 5941  N   ILE B 295      537   2510   4081    -95   -258   -144       N  
ATOM   5942  CA  ILE B 295      65.721  57.523  60.595  1.00 17.81           C  
ANISOU 5942  CA  ILE B 295      360   2379   4028     80   -226    -98       C  
ATOM   5943  C   ILE B 295      65.848  57.885  59.121  1.00 17.87           C  
ANISOU 5943  C   ILE B 295      322   2359   4107    120   -244   -103       C  
ATOM   5944  O   ILE B 295      65.582  57.048  58.249  1.00 18.06           O  
ANISOU 5944  O   ILE B 295      439   2331   4090     95   -162     20       O  
ATOM   5945  CB  ILE B 295      67.123  57.343  61.235  1.00 18.50           C  
ANISOU 5945  CB  ILE B 295      525   2502   4002    178   -296   -104       C  
ATOM   5946  CG1 ILE B 295      67.924  56.226  60.541  1.00 16.93           C  
ANISOU 5946  CG1 ILE B 295      322   2306   3803    182   -220   -128       C  
ATOM   5947  CG2 ILE B 295      66.995  57.151  62.748  1.00 18.33           C  
ANISOU 5947  CG2 ILE B 295      783   2282   3898    100   -311   -275       C  
ATOM   5948  CD1 ILE B 295      69.441  56.270  60.904  1.00 17.25           C  
ANISOU 5948  CD1 ILE B 295      394   2432   3728    273   -489   -261       C  
ATOM   5949  N   ASN B 296      66.233  59.133  58.855  1.00 18.02           N  
ANISOU 5949  N   ASN B 296      326   2313   4207    202   -257   -120       N  
ATOM   5950  CA  ASN B 296      66.486  59.601  57.495  1.00 18.08           C  
ANISOU 5950  CA  ASN B 296      354   2185   4327    259   -295   -177       C  
ATOM   5951  C   ASN B 296      65.274  59.402  56.590  1.00 18.14           C  
ANISOU 5951  C   ASN B 296      400   2066   4423    236   -304   -288       C  
ATOM   5952  O   ASN B 296      65.433  59.205  55.384  1.00 18.24           O  
ANISOU 5952  O   ASN B 296      390   2080   4460    417   -205   -373       O  
ATOM   5953  CB  ASN B 296      67.708  58.882  56.928  1.00 18.03           C  
ANISOU 5953  CB  ASN B 296      385   2189   4274    122   -251   -199       C  
ATOM   5954  CG  ASN B 296      68.945  59.135  57.758  1.00 18.30           C  
ANISOU 5954  CG  ASN B 296      483   2244   4223    287   -295   -164       C  
ATOM   5955  OD1 ASN B 296      69.105  60.225  58.328  1.00 17.73           O  
ANISOU 5955  OD1 ASN B 296      466   1799   4469    504     80    -61       O  
ATOM   5956  ND2 ASN B 296      69.809  58.125  57.862  1.00 17.81           N  
ANISOU 5956  ND2 ASN B 296      508   2406   3851    326     22   -441       N  
ATOM   5957  N   SER B 297      64.079  59.521  57.170  1.00 18.28           N  
ANISOU 5957  N   SER B 297      405   1992   4548    258   -272   -302       N  
ATOM   5958  CA  SER B 297      62.850  59.153  56.476  1.00 18.85           C  
ANISOU 5958  CA  SER B 297      466   2042   4654    243   -356   -348       C  
ATOM   5959  C   SER B 297      61.677  60.075  56.776  1.00 19.33           C  
ANISOU 5959  C   SER B 297      510   2005   4826    237   -419   -319       C  
ATOM   5960  O   SER B 297      61.613  60.695  57.841  1.00 19.76           O  
ANISOU 5960  O   SER B 297      602   2056   4848    239   -582   -286       O  
ATOM   5961  CB  SER B 297      62.409  57.720  56.821  1.00 18.90           C  
ANISOU 5961  CB  SER B 297      603   1925   4653    332   -276   -284       C  
ATOM   5962  OG  SER B 297      63.444  56.779  56.584  1.00 19.93           O  
ANISOU 5962  OG  SER B 297      717   2349   4506    310   -159   -388       O  
ATOM   5963  N   ALA B 298      60.753  60.128  55.822  1.00 19.79           N  
ANISOU 5963  N   ALA B 298      452   2144   4920    214   -525   -365       N  
ATOM   5964  CA  ALA B 298      59.417  60.698  56.002  1.00 20.96           C  
ANISOU 5964  CA  ALA B 298      442   2340   5180    125   -547   -366       C  
ATOM   5965  C   ALA B 298      58.399  59.796  55.296  1.00 21.52           C  
ANISOU 5965  C   ALA B 298      477   2459   5238    123   -611   -432       C  
ATOM   5966  O   ALA B 298      58.775  58.780  54.704  1.00 21.79           O  
ANISOU 5966  O   ALA B 298      393   2602   5283     92   -645   -418       O  
ATOM   5967  CB  ALA B 298      59.356  62.142  55.479  1.00 20.19           C  
ANISOU 5967  CB  ALA B 298      361   2180   5129    139   -495   -416       C  
ATOM   5968  N   ILE B 299      57.113  60.139  55.391  1.00 21.75           N  
ANISOU 5968  N   ILE B 299      375   2545   5344     10   -603   -496       N  
ATOM   5969  CA  ILE B 299      56.050  59.321  54.811  1.00 22.57           C  
ANISOU 5969  CA  ILE B 299      533   2506   5534     25   -595   -538       C  
ATOM   5970  C   ILE B 299      55.321  60.086  53.712  1.00 23.78           C  
ANISOU 5970  C   ILE B 299      654   2576   5805     91   -741   -541       C  
ATOM   5971  O   ILE B 299      54.866  61.216  53.938  1.00 24.16           O  
ANISOU 5971  O   ILE B 299      805   2605   5768    201   -787   -541       O  
ATOM   5972  CB  ILE B 299      55.020  58.917  55.885  1.00 22.09           C  
ANISOU 5972  CB  ILE B 299      457   2478   5458    -93   -556   -590       C  
ATOM   5973  CG1 ILE B 299      55.741  58.318  57.106  1.00 22.08           C  
ANISOU 5973  CG1 ILE B 299      549   2593   5244    -89   -274   -506       C  
ATOM   5974  CG2 ILE B 299      53.946  57.974  55.305  1.00 21.89           C  
ANISOU 5974  CG2 ILE B 299      328   2432   5555   -135   -354   -649       C  
ATOM   5975  CD1 ILE B 299      54.798  57.942  58.261  1.00 21.61           C  
ANISOU 5975  CD1 ILE B 299      289   2706   5215    -27     92   -448       C  
ATOM   5976  N   LEU B 300      55.216  59.464  52.539  1.00 24.62           N  
ANISOU 5976  N   LEU B 300      737   2583   6033    144   -806   -596       N  
ATOM   5977  CA  LEU B 300      54.336  59.927  51.475  1.00 25.72           C  
ANISOU 5977  CA  LEU B 300      751   2686   6333     84  -1009   -614       C  
ATOM   5978  C   LEU B 300      53.028  59.185  51.669  1.00 27.06           C  
ANISOU 5978  C   LEU B 300      888   2731   6662     46  -1001   -643       C  
ATOM   5979  O   LEU B 300      52.968  57.972  51.460  1.00 27.76           O  
ANISOU 5979  O   LEU B 300      911   2816   6819     76   -977   -630       O  
ATOM   5980  CB  LEU B 300      54.888  59.627  50.079  1.00 25.79           C  
ANISOU 5980  CB  LEU B 300      869   2679   6248    171  -1062   -560       C  
ATOM   5981  CG  LEU B 300      54.031  60.219  48.945  1.00 26.43           C  
ANISOU 5981  CG  LEU B 300     1077   2782   6181     94  -1224   -660       C  
ATOM   5982  CD1 LEU B 300      54.313  61.711  48.773  1.00 26.87           C  
ANISOU 5982  CD1 LEU B 300     1665   2715   5826    158  -1410   -509       C  
ATOM   5983  CD2 LEU B 300      54.263  59.499  47.626  1.00 26.72           C  
ANISOU 5983  CD2 LEU B 300     1255   2663   6233    -21  -1347   -668       C  
ATOM   5984  N   ARG B 301      51.997  59.909  52.086  1.00 27.39           N  
ANISOU 5984  N   ARG B 301      755   2696   6956    119  -1163   -639       N  
ATOM   5985  CA  ARG B 301      50.720  59.279  52.412  1.00 28.90           C  
ANISOU 5985  CA  ARG B 301      861   2821   7296    130  -1177   -709       C  
ATOM   5986  C   ARG B 301      49.633  59.678  51.426  1.00 29.96           C  
ANISOU 5986  C   ARG B 301      924   2900   7560    170  -1299   -781       C  
ATOM   5987  O   ARG B 301      49.286  60.859  51.325  1.00 29.78           O  
ANISOU 5987  O   ARG B 301      974   2805   7537    255  -1341   -810       O  
ATOM   5988  CB  ARG B 301      50.291  59.612  53.846  1.00 28.55           C  
ANISOU 5988  CB  ARG B 301      826   2740   7280     70  -1119   -716       C  
ATOM   5989  CG  ARG B 301      48.925  59.036  54.232  1.00 29.61           C  
ANISOU 5989  CG  ARG B 301      949   3073   7229     97  -1002   -666       C  
ATOM   5990  CD  ARG B 301      48.675  59.164  55.736  1.00 29.79           C  
ANISOU 5990  CD  ARG B 301     1134   3132   7050    183   -695   -890       C  
ATOM   5991  NE  ARG B 301      49.699  58.431  56.489  1.00 28.11           N  
ANISOU 5991  NE  ARG B 301      735   3088   6855    382   -353  -1142       N  
ATOM   5992  CZ  ARG B 301      50.067  58.723  57.734  1.00 28.25           C  
ANISOU 5992  CZ  ARG B 301      979   2887   6867    400   -130  -1403       C  
ATOM   5993  NH1 ARG B 301      49.507  59.747  58.376  1.00 27.01           N  
ANISOU 5993  NH1 ARG B 301      767   2724   6770    379    156  -1488       N  
ATOM   5994  NH2 ARG B 301      51.013  58.001  58.328  1.00 28.13           N  
ANISOU 5994  NH2 ARG B 301     1317   2583   6785    346    118  -1471       N  
ATOM   5995  N   TYR B 302      49.100  58.685  50.713  1.00 30.90           N  
ANISOU 5995  N   TYR B 302      913   2962   7864    163  -1401   -858       N  
ATOM   5996  CA  TYR B 302      47.943  58.897  49.851  1.00 32.24           C  
ANISOU 5996  CA  TYR B 302      927   3081   8242    266  -1480   -923       C  
ATOM   5997  C   TYR B 302      46.681  59.125  50.679  1.00 32.96           C  
ANISOU 5997  C   TYR B 302      876   3149   8496    185  -1484   -956       C  
ATOM   5998  O   TYR B 302      46.470  58.448  51.686  1.00 32.65           O  
ANISOU 5998  O   TYR B 302      708   3131   8565    102  -1560   -983       O  
ATOM   5999  CB  TYR B 302      47.724  57.688  48.933  1.00 32.11           C  
ANISOU 5999  CB  TYR B 302      960   3021   8217    233  -1525   -903       C  
ATOM   6000  CG  TYR B 302      48.612  57.647  47.703  1.00 32.58           C  
ANISOU 6000  CG  TYR B 302     1083   3095   8199    267  -1633   -914       C  
ATOM   6001  CD1 TYR B 302      50.005  57.566  47.801  1.00 32.63           C  
ANISOU 6001  CD1 TYR B 302     1141   3037   8218    519  -1697   -778       C  
ATOM   6002  CD2 TYR B 302      48.042  57.677  46.434  1.00 34.05           C  
ANISOU 6002  CD2 TYR B 302     1353   3305   8277    477  -1745   -801       C  
ATOM   6003  CE1 TYR B 302      50.804  57.522  46.658  1.00 32.05           C  
ANISOU 6003  CE1 TYR B 302     1088   2962   8127    211  -1847   -637       C  
ATOM   6004  CE2 TYR B 302      48.823  57.630  45.293  1.00 33.99           C  
ANISOU 6004  CE2 TYR B 302     1420   3168   8325    231  -1654   -675       C  
ATOM   6005  CZ  TYR B 302      50.195  57.547  45.411  1.00 32.46           C  
ANISOU 6005  CZ  TYR B 302     1340   2895   8097    409  -1790   -650       C  
ATOM   6006  OH  TYR B 302      50.944  57.506  44.262  1.00 33.40           O  
ANISOU 6006  OH  TYR B 302     1753   2979   7956    282  -1802   -666       O  
ATOM   6007  N   ASP B 303      45.867  60.094  50.266  1.00 33.94           N  
ANISOU 6007  N   ASP B 303      928   3185   8780    314  -1455   -995       N  
ATOM   6008  CA  ASP B 303      44.513  60.240  50.804  1.00 35.23           C  
ANISOU 6008  CA  ASP B 303      996   3328   9059    326  -1381   -979       C  
ATOM   6009  C   ASP B 303      43.820  58.878  50.845  1.00 35.83           C  
ANISOU 6009  C   ASP B 303     1029   3379   9203    274  -1304  -1018       C  
ATOM   6010  O   ASP B 303      43.742  58.177  49.829  1.00 35.52           O  
ANISOU 6010  O   ASP B 303      955   3386   9155    213  -1472  -1020       O  
ATOM   6011  CB  ASP B 303      43.665  61.210  49.969  1.00 36.33           C  
ANISOU 6011  CB  ASP B 303     1246   3445   9111    439  -1395   -961       C  
ATOM   6012  CG  ASP B 303      44.152  62.646  50.031  1.00 37.82           C  
ANISOU 6012  CG  ASP B 303     1459   3570   9340    618  -1442   -803       C  
ATOM   6013  OD1 ASP B 303      45.0