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***  OXYGEN TRANSPORT 11-APR-14 3WTG  ***

elNémo ID: 210803214731129569

Job options:

ID        	=	 210803214731129569
JOBID     	=	 OXYGEN TRANSPORT 11-APR-14 3WTG
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    OXYGEN TRANSPORT                        11-APR-14   3WTG              
TITLE     CRYSTAL STRUCTURE OF EMU (DROMAIUS NOVAEHOLLANDIAE) HEMOGLOBIN AT 2.3 
TITLE    2 ANGSTROM RESOLUTION                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA-A;                                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: HEMOGLOBIN;                                                
COMPND   6 CHAIN: B, D                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROMAIUS NOVAEHOLLANDIAE;                       
SOURCE   3 ORGANISM_COMMON: EMU;                                                
SOURCE   4 ORGANISM_TAXID: 8790;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: DROMAIUS NOVAEHOLLANDIAE;                       
SOURCE   7 ORGANISM_COMMON: EMU;                                                
SOURCE   8 ORGANISM_TAXID: 8790                                                 
KEYWDS    HEMOGLOBIN, OXYGEN AFFINITY, AVIAN, OXYGEN TRANSPORT, OXYGEN          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.M.ABUBAKKAR,V.MAHESHWARAN,M.N.PONNUSWAMY,K.SARABOJI                 
REVDAT   1   02-JUL-14 3WTG    0                                                
JRNL        AUTH   M.M.ABUBAKKAR,K.SARABOJI,M.N.PONNUSWAMY                      
JRNL        TITL   PURIFICATION AND PRELIMINARY STRUCTURAL STUDIES OF           
JRNL        TITL 2 HEMOGLOBIN FROM HIGH OXYGEN AFFINITY SPECIES EMU (DROMAIUS   
JRNL        TITL 3 NOVAEHOLLANDIAE) AT NEUTRAL PH                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 23787                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1259                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1717                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 92                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4419                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 180                                     
REMARK   3   SOLVENT ATOMS            : 360                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : 0.08000                                              
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): 0.505         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.275         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.179         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.922        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4727 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3038 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6472 ; 1.579 ; 2.053       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7430 ; 0.991 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   564 ; 5.726 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   190 ;35.810 ;24.105       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   752 ;17.603 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.438 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   716 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5166 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   902 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2833 ; 0.789 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1136 ; 0.188 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4552 ; 1.483 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1894 ; 2.347 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1920 ; 3.515 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   138                          
REMARK   3    RESIDUE RANGE :   A   201        A   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6816   6.4500   2.4989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0814 T22:   0.0225                                     
REMARK   3      T33:   0.0240 T12:  -0.0171                                     
REMARK   3      T13:  -0.0295 T23:   0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2887 L22:   2.0188                                     
REMARK   3      L33:   1.8311 L12:   0.3389                                     
REMARK   3      L13:  -0.1034 L23:   0.1896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0723 S12:   0.1013 S13:   0.0574                       
REMARK   3      S21:  -0.2357 S22:   0.0956 S23:   0.0461                       
REMARK   3      S31:  -0.1282 S32:   0.0408 S33:  -0.0233                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   146                          
REMARK   3    RESIDUE RANGE :   B   201        B   202                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2566   7.0154  26.5259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0244 T22:   0.1010                                     
REMARK   3      T33:   0.0227 T12:   0.0007                                     
REMARK   3      T13:  -0.0004 T23:  -0.0243                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5524 L22:   1.1985                                     
REMARK   3      L33:   1.5338 L12:   0.0138                                     
REMARK   3      L13:  -0.1020 L23:  -0.1473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0498 S12:  -0.4132 S13:   0.0057                       
REMARK   3      S21:   0.0710 S22:  -0.0423 S23:  -0.0006                       
REMARK   3      S31:   0.0017 S32:   0.0134 S33:   0.0921                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   138                          
REMARK   3    RESIDUE RANGE :   C   201        C   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.0472  -0.4100  10.3389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0180 T22:   0.0143                                     
REMARK   3      T33:   0.0705 T12:   0.0066                                     
REMARK   3      T13:  -0.0055 T23:  -0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8393 L22:   2.0096                                     
REMARK   3      L33:   1.8046 L12:   0.6071                                     
REMARK   3      L13:   0.5287 L23:   0.6702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0659 S12:  -0.1112 S13:   0.2552                       
REMARK   3      S21:  -0.0398 S22:  -0.0841 S23:   0.0991                       
REMARK   3      S31:  -0.0715 S32:  -0.0823 S33:   0.0183                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   146                          
REMARK   3    RESIDUE RANGE :   D   201        D   202                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.0377 -19.1356  14.2114              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0363 T22:   0.0377                                     
REMARK   3      T33:   0.0334 T12:   0.0086                                     
REMARK   3      T13:   0.0012 T23:   0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6712 L22:   0.8571                                     
REMARK   3      L33:   1.3141 L12:  -0.2111                                     
REMARK   3      L13:  -0.4835 L23:  -0.1629                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0679 S12:  -0.2300 S13:  -0.2118                       
REMARK   3      S21:   0.0106 S22:  -0.0189 S23:  -0.0176                       
REMARK   3      S31:   0.0560 S32:   0.0201 S33:   0.0868                       
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 3WTG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB096770.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR-H             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AUTOMAR                            
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25129                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.06100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.06100                            
REMARK 200   FOR SHELL         : 6.400                              
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: 3FS4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 3350, PH 7.0, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.13550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.77950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.00500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.77950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.13550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.00500            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     0                                                      
REMARK 465     LYS A   139                                                      
REMARK 465     TYR A   140                                                      
REMARK 465     ARG A   141                                                      
REMARK 465     MET C     0                                                      
REMARK 465     LYS C   139                                                      
REMARK 465     TYR C   140                                                      
REMARK 465     ARG C   141                                                      
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  FE    HEM D   201     O1   OXY D   202              1.56            
REMARK 500  FE    HEM A   201     O1   OXY A   202              1.62            
REMARK 500  FE    HEM C   201     O1   OXY C   202              1.68            
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    HIS A  72       48.82   -106.08                                   
REMARK 500    ASP A  75       58.59   -142.60                                   
REMARK 500    LEU A  80       42.35    -98.50                                   
REMARK 500    TYR B  35       77.42   -119.86                                   
REMARK 500    ASN B  77       74.05   -158.24                                   
REMARK 500    ALA B 119     -130.74     51.57                                   
REMARK 500    SER C 115        0.87     83.42                                   
REMARK 500    ASN D  77       59.13   -159.43                                   
REMARK 500    CYS D  93      -74.08    -84.11                                   
REMARK 500    ALA D 119     -134.25     57.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A   82     LEU A   83                  143.15                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 OXY B 202   O1                                                     
REMARK 620 2 HEM B 201   NA   84.6                                              
REMARK 620 3 HEM B 201   NB   84.5  88.1                                        
REMARK 620 4 HEM B 201   NC   95.1 178.0  89.9                                  
REMARK 620 5 HEM B 201   ND   93.1  91.1 177.6  90.9                            
REMARK 620 6 HIS B  92   NE2 166.0  84.0  86.9  95.9  95.3                      
REMARK 620 7 OXY B 202   O2   28.0 107.9 100.5  72.4  77.5 166.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  87   NE2                                                    
REMARK 620 2 HEM A 201   NA   95.1                                              
REMARK 620 3 HEM A 201   NB   92.1  89.3                                        
REMARK 620 4 HEM A 201   NC   86.5 177.5  92.6                                  
REMARK 620 5 HEM A 201   ND   89.7  88.7 177.5  89.3                            
REMARK 620 6 OXY A 202   O2  165.2  98.8  93.1  79.4  85.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  92   NE2                                                    
REMARK 620 2 HEM D 201   NA   91.5                                              
REMARK 620 3 HEM D 201   NB   95.5  90.3                                        
REMARK 620 4 HEM D 201   NC   89.1 177.2  86.9                                  
REMARK 620 5 HEM D 201   ND   86.9  90.2 177.5  92.6                            
REMARK 620 6 OXY D 202   O2  171.2  92.6  92.2  87.1  85.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  87   NE2                                                    
REMARK 620 2 HEM C 201   NA   85.6                                              
REMARK 620 3 HEM C 201   NB   89.3  87.9                                        
REMARK 620 4 HEM C 201   NC   95.5 178.2  90.6                                  
REMARK 620 5 HEM C 201   ND   91.8  91.6 178.7  89.8                            
REMARK 620 6 OXY C 202   O2  163.2 110.0  97.1  69.0  82.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY D 202                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 A SEQUENCE REFERENCE FOR THE CHAINS B AND D DOES NOT CURRENTLY       
REMARK 999 EXIST.                                                               
DBREF  3WTG A    0   141  UNP    C6L8R0   C6L8R0_DRONO     1    142             
DBREF  3WTG C    0   141  UNP    C6L8R0   C6L8R0_DRONO     1    142             
DBREF  3WTG B    1   146  PDB    3WTG     3WTG             1    146             
DBREF  3WTG D    1   146  PDB    3WTG     3WTG             1    146             
SEQRES   1 A  142  MET VAL LEU SER ALA ALA ASP LYS THR ASN THR LYS SER          
SEQRES   2 A  142  VAL PHE ALA LYS ILE GLY PRO HIS ALA GLU GLU TYR GLY          
SEQRES   3 A  142  ALA GLU THR LEU GLU ARG LEU PHE THR THR TYR PRO GLN          
SEQRES   4 A  142  THR LYS THR TYR PHE PRO HIS PHE ASP LEU HIS HIS GLY          
SEQRES   5 A  142  SER ALA GLN VAL LYS ALA HIS GLY LYS LYS VAL ALA ALA          
SEQRES   6 A  142  ALA LEU VAL GLU ALA ALA ASN HIS ILE ASP ASP ILE SER          
SEQRES   7 A  142  THR ALA LEU SER LYS LEU SER ASP LEU HIS ALA GLN LYS          
SEQRES   8 A  142  LEU ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU GLY GLN          
SEQRES   9 A  142  CYS PHE LEU VAL VAL VAL ALA ILE HIS HIS PRO SER LEU          
SEQRES  10 A  142  LEU THR PRO GLU VAL HIS ALA SER LEU ASP LYS PHE LEU          
SEQRES  11 A  142  CYS ALA VAL ALA ASN VAL LEU THR ALA LYS TYR ARG              
SEQRES   1 B  146  VAL GLN TRP SER ALA GLU GLU LYS GLN LEU ILE SER SER          
SEQRES   2 B  146  LEU TRP GLY LYS VAL ASN VAL ALA GLU CYS GLY ALA GLU          
SEQRES   3 B  146  ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN          
SEQRES   4 B  146  ARG PHE PHE THR SER PHE GLY ASN LEU SER SER ALA SER          
SEQRES   5 B  146  ALA ILE ILE GLY ASN PRO MET VAL ARG ALA HIS GLY LYS          
SEQRES   6 B  146  LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU          
SEQRES   7 B  146  ASP ASN ILE LYS ASN THR PHE ALA GLN LEU SER GLU LEU          
SEQRES   8 B  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 B  146  LEU LEU GLY ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS          
SEQRES  10 B  146  PHE ALA LYS GLU PHE THR PRO GLU CYS GLN ALA ALA TRP          
SEQRES  11 B  146  GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG          
SEQRES  12 B  146  LYS TYR HIS                                                  
SEQRES   1 C  142  MET VAL LEU SER ALA ALA ASP LYS THR ASN THR LYS SER          
SEQRES   2 C  142  VAL PHE ALA LYS ILE GLY PRO HIS ALA GLU GLU TYR GLY          
SEQRES   3 C  142  ALA GLU THR LEU GLU ARG LEU PHE THR THR TYR PRO GLN          
SEQRES   4 C  142  THR LYS THR TYR PHE PRO HIS PHE ASP LEU HIS HIS GLY          
SEQRES   5 C  142  SER ALA GLN VAL LYS ALA HIS GLY LYS LYS VAL ALA ALA          
SEQRES   6 C  142  ALA LEU VAL GLU ALA ALA ASN HIS ILE ASP ASP ILE SER          
SEQRES   7 C  142  THR ALA LEU SER LYS LEU SER ASP LEU HIS ALA GLN LYS          
SEQRES   8 C  142  LEU ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU GLY GLN          
SEQRES   9 C  142  CYS PHE LEU VAL VAL VAL ALA ILE HIS HIS PRO SER LEU          
SEQRES  10 C  142  LEU THR PRO GLU VAL HIS ALA SER LEU ASP LYS PHE LEU          
SEQRES  11 C  142  CYS ALA VAL ALA ASN VAL LEU THR ALA LYS TYR ARG              
SEQRES   1 D  146  VAL GLN TRP SER ALA GLU GLU LYS GLN LEU ILE SER SER          
SEQRES   2 D  146  LEU TRP GLY LYS VAL ASN VAL ALA GLU CYS GLY ALA GLU          
SEQRES   3 D  146  ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN          
SEQRES   4 D  146  ARG PHE PHE THR SER PHE GLY ASN LEU SER SER ALA SER          
SEQRES   5 D  146  ALA ILE ILE GLY ASN PRO MET VAL ARG ALA HIS GLY LYS          
SEQRES   6 D  146  LYS VAL LEU THR SER PHE GLY ASP ALA VAL LYS ASN LEU          
SEQRES   7 D  146  ASP ASN ILE LYS ASN THR PHE ALA GLN LEU SER GLU LEU          
SEQRES   8 D  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 D  146  LEU LEU GLY ASP ILE LEU ILE ILE VAL LEU ALA ALA HIS          
SEQRES  10 D  146  PHE ALA LYS GLU PHE THR PRO GLU CYS GLN ALA ALA TRP          
SEQRES  11 D  146  GLN LYS LEU VAL ARG VAL VAL ALA HIS ALA LEU ALA ARG          
SEQRES  12 D  146  LYS TYR HIS                                                  
HET    HEM  A 201      43                                                       
HET    OXY  A 202       2                                                       
HET    HEM  B 201      43                                                       
HET    OXY  B 202       2                                                       
HET    HEM  C 201      43                                                       
HET    OXY  C 202       2                                                       
HET    HEM  D 201      43                                                       
HET    OXY  D 202       2                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     OXY OXYGEN MOLECULE                                                  
HETSYN     HEM HEME                                                             
FORMUL   5  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL   6  OXY    4(O2)                                                        
FORMUL  13  HOH   *360(H2 O)                                                    
HELIX    1   1 SER A    3  GLY A   18  1                                  16    
HELIX    2   2 HIS A   20  TYR A   36  1                                  17    
HELIX    3   3 PRO A   37  PHE A   43  5                                   7    
HELIX    4   4 SER A   52  HIS A   72  1                                  21    
HELIX    5   5 ASP A   75  LEU A   80  1                                   6    
HELIX    6   6 LEU A   83  GLN A   89  1                                   7    
HELIX    7   7 PRO A   95  HIS A  113  1                                  19    
HELIX    8   8 THR A  118  THR A  137  1                                  20    
HELIX    9   9 SER B    4  GLY B   16  1                                  13    
HELIX   10  10 ASN B   19  TYR B   35  1                                  17    
HELIX   11  11 PRO B   36  GLY B   46  5                                  11    
HELIX   12  12 SER B   50  GLY B   56  1                                   7    
HELIX   13  13 ASN B   57  LYS B   76  1                                  20    
HELIX   14  14 ASN B   77  ASP B   79  5                                   3    
HELIX   15  15 ASN B   80  PHE B   85  1                                   6    
HELIX   16  16 PHE B   85  LYS B   95  1                                  11    
HELIX   17  17 PRO B  100  ALA B  119  1                                  20    
HELIX   18  18 LYS B  120  PHE B  122  5                                   3    
HELIX   19  19 THR B  123  ALA B  142  1                                  20    
HELIX   20  20 ARG B  143  HIS B  146  5                                   4    
HELIX   21  21 SER C    3  GLY C   18  1                                  16    
HELIX   22  22 HIS C   20  TYR C   36  1                                  17    
HELIX   23  23 PRO C   37  PHE C   43  5                                   7    
HELIX   24  24 SER C   52  HIS C   72  1                                  21    
HELIX   25  25 ASP C   75  LEU C   80  1                                   6    
HELIX   26  26 LYS C   82  GLN C   89  1                                   8    
HELIX   27  27 PRO C   95  HIS C  113  1                                  19    
HELIX   28  28 THR C  118  THR C  137  1                                  20    
HELIX   29  29 SER D    4  GLY D   16  1                                  13    
HELIX   30  30 ASN D   19  TYR D   35  1                                  17    
HELIX   31  31 PRO D   36  GLY D   46  5                                  11    
HELIX   32  32 SER D   50  GLY D   56  1                                   7    
HELIX   33  33 ASN D   57  LYS D   76  1                                  20    
HELIX   34  34 ASN D   77  ASP D   79  5                                   3    
HELIX   35  35 ASN D   80  PHE D   85  1                                   6    
HELIX   36  36 PHE D   85  CYS D   93  1                                   9    
HELIX   37  37 PRO D  100  ALA D  119  1                                  20    
HELIX   38  38 LYS D  120  PHE D  122  5                                   3    
HELIX   39  39 THR D  123  ALA D  142  1                                  20    
LINK        FE   HEM B 201                 O1  OXY B 202     1555   1555  1.90  
LINK         NE2 HIS A  87                FE   HEM A 201     1555   1555  1.96  
LINK         NE2 HIS D  92                FE   HEM D 201     1555   1555  2.01  
LINK         NE2 HIS C  87                FE   HEM C 201     1555   1555  2.07  
LINK         NE2 HIS B  92                FE   HEM B 201     1555   1555  2.08  
LINK        FE   HEM B 201                 O2  OXY B 202     1555   1555  2.51  
LINK        FE   HEM A 201                 O2  OXY A 202     1555   1555  2.62  
LINK        FE   HEM D 201                 O2  OXY D 202     1555   1555  2.66  
LINK        FE   HEM C 201                 O2  OXY C 202     1555   1555  2.69  
SITE     1 AC1 15 TYR A  42  PHE A  43  PHE A  46  HIS A  58                    
SITE     2 AC1 15 LYS A  61  LEU A  66  LEU A  86  HIS A  87                    
SITE     3 AC1 15 LEU A  91  VAL A  93  ASN A  97  PHE A  98                    
SITE     4 AC1 15 LEU A 136  OXY A 202  HOH A 358                               
SITE     1 AC2  4 HIS A  58  VAL A  62  HIS A  87  HEM A 201                    
SITE     1 AC3 13 THR B  38  PHE B  41  PHE B  42  HIS B  63                    
SITE     2 AC3 13 LYS B  66  HIS B  92  LEU B  96  VAL B  98                    
SITE     3 AC3 13 ASN B 102  PHE B 103  LEU B 141  OXY B 202                    
SITE     4 AC3 13 HOH B 344                                                     
SITE     1 AC4  4 PHE B  42  HIS B  63  VAL B  67  HEM B 201                    
SITE     1 AC5 15 TYR C  42  PHE C  43  HIS C  45  HIS C  58                    
SITE     2 AC5 15 LYS C  61  LEU C  83  LEU C  86  HIS C  87                    
SITE     3 AC5 15 LEU C  91  VAL C  93  ASN C  97  PHE C  98                    
SITE     4 AC5 15 LEU C 101  LEU C 136  OXY C 202                               
SITE     1 AC6  4 PHE C  43  HIS C  58  VAL C  62  HEM C 201                    
SITE     1 AC7 16 LYS C  16  THR D  38  PHE D  41  PHE D  42                    
SITE     2 AC7 16 HIS D  63  LYS D  66  SER D  70  HIS D  92                    
SITE     3 AC7 16 LEU D  96  ASN D 102  PHE D 103  LEU D 106                    
SITE     4 AC7 16 LEU D 141  OXY D 202  HOH D 316  HOH D 368                    
SITE     1 AC8  4 HIS D  63  VAL D  67  HIS D  92  HEM D 201                    
CRYST1   66.271   80.010  103.559  90.00  90.00  90.00 P 21 21 21    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      0.015090  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012498  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009656        0.00000                         
ATOM      1  N   VAL A   1     -22.502  12.969   3.439  1.00 65.81           N  
ANISOU    1  N   VAL A   1     7456   8084   9464    903  -1060    440       N  
ATOM      2  CA  VAL A   1     -21.416  13.350   2.482  1.00 64.99           C  
ANISOU    2  CA  VAL A   1     7569   7907   9217    859  -1141    500       C  
ATOM      3  C   VAL A   1     -20.420  14.305   3.156  1.00 63.85           C  
ANISOU    3  C   VAL A   1     7580   7648   9031    892  -1029    480       C  
ATOM      4  O   VAL A   1     -20.702  14.836   4.236  1.00 64.45           O  
ANISOU    4  O   VAL A   1     7602   7692   9196    972   -916    426       O  
ATOM      5  CB  VAL A   1     -22.003  14.015   1.192  1.00 66.88           C  
ANISOU    5  CB  VAL A   1     7816   8119   9476    935  -1343    592       C  
ATOM      6  CG1 VAL A   1     -23.069  13.108   0.539  1.00 68.08           C  
ANISOU    6  CG1 VAL A   1     7798   8393   9676    900  -1473    606       C  
ATOM      7  CG2 VAL A   1     -22.582  15.426   1.486  1.00 68.03           C  
ANISOU    7  CG2 VAL A   1     7931   8166   9753   1117  -1357    616       C  
ATOM      8  N   LEU A   2     -19.264  14.529   2.523  1.00 62.27           N  
ANISOU    8  N   LEU A   2     7572   7391   8697    823  -1055    516       N  
ATOM      9  CA  LEU A   2     -18.312  15.566   2.993  1.00 60.86           C  
ANISOU    9  CA  LEU A   2     7547   7095   8482    844   -973    505       C  
ATOM     10  C   LEU A   2     -18.902  16.963   2.800  1.00 61.59           C  
ANISOU   10  C   LEU A   2     7659   7073   8670    992  -1035    550       C  
ATOM     11  O   LEU A   2     -19.374  17.318   1.709  1.00 62.95           O  
ANISOU   11  O   LEU A   2     7846   7221   8849   1040  -1186    636       O  
ATOM     12  CB  LEU A   2     -16.981  15.494   2.245  1.00 59.77           C  
ANISOU   12  CB  LEU A   2     7595   6929   8188    728   -988    539       C  
ATOM     13  CG  LEU A   2     -16.296  14.130   2.237  1.00 57.86           C  
ANISOU   13  CG  LEU A   2     7352   6786   7848    592   -941    502       C  
ATOM     14  CD1 LEU A   2     -15.304  14.071   1.094  1.00 57.39           C  
ANISOU   14  CD1 LEU A   2     7448   6709   7650    498   -994    551       C  
ATOM     15  CD2 LEU A   2     -15.646  13.869   3.576  1.00 55.08           C  
ANISOU   15  CD2 LEU A   2     6993   6442   7492    559   -788    421       C  
ATOM     16  N   SER A   3     -18.867  17.757   3.860  1.00 60.44           N  
ANISOU   16  N   SER A   3     7523   6849   8594   1067   -921    493       N  
ATOM     17  CA  SER A   3     -19.386  19.108   3.808  1.00 60.90           C  
ANISOU   17  CA  SER A   3     7609   6776   8753   1219   -960    522       C  
ATOM     18  C   SER A   3     -18.432  20.003   3.010  1.00 59.75           C  
ANISOU   18  C   SER A   3     7689   6499   8514   1186  -1018    595       C  
ATOM     19  O   SER A   3     -17.310  19.607   2.714  1.00 58.11           O  
ANISOU   19  O   SER A   3     7601   6311   8168   1044   -995    600       O  
ATOM     20  CB  SER A   3     -19.597  19.642   5.230  1.00 61.33           C  
ANISOU   20  CB  SER A   3     7620   6782   8900   1298   -803    422       C  
ATOM     21  OG  SER A   3     -18.433  19.485   6.025  1.00 59.97           O  
ANISOU   21  OG  SER A   3     7561   6603   8623   1185   -675    354       O  
ATOM     22  N   ALA A   4     -18.892  21.206   2.666  1.00 59.96           N  
ANISOU   22  N   ALA A   4     7771   6390   8620   1319  -1088    652       N  
ATOM     23  CA  ALA A   4     -18.071  22.178   1.946  1.00 58.86           C  
ANISOU   23  CA  ALA A   4     7859   6105   8402   1292  -1137    728       C  
ATOM     24  C   ALA A   4     -16.895  22.643   2.803  1.00 56.56           C  
ANISOU   24  C   ALA A   4     7704   5731   8055   1208   -986    653       C  
ATOM     25  O   ALA A   4     -15.817  22.953   2.284  1.00 55.83           O  
ANISOU   25  O   ALA A   4     7787   5577   7848   1096   -987    692       O  
ATOM     26  CB  ALA A   4     -18.915  23.353   1.523  1.00 61.02           C  
ANISOU   26  CB  ALA A   4     8157   6238   8792   1470  -1241    804       C  
ATOM     27  N   ALA A   5     -17.125  22.700   4.113  1.00 54.95           N  
ANISOU   27  N   ALA A   5     7416   5530   7930   1256   -856    541       N  
ATOM     28  CA  ALA A   5     -16.079  22.950   5.090  1.00 53.09           C  
ANISOU   28  CA  ALA A   5     7281   5252   7638   1167   -716    450       C  
ATOM     29  C   ALA A   5     -15.061  21.812   5.019  1.00 49.97           C  
ANISOU   29  C   ALA A   5     6893   4991   7103    988   -685    433       C  
ATOM     30  O   ALA A   5     -13.866  22.049   4.892  1.00 49.26           O  
ANISOU   30  O   ALA A   5     6943   4859   6916    870   -655    434       O  
ATOM     31  CB  ALA A   5     -16.675  23.052   6.507  1.00 53.35           C  
ANISOU   31  CB  ALA A   5     7209   5293   7770   1255   -588    330       C  
ATOM     32  N   ASP A   6     -15.547  20.578   5.083  1.00 48.32           N  
ANISOU   32  N   ASP A   6     6528   4939   6892    969   -691    419       N  
ATOM     33  CA  ASP A   6     -14.683  19.381   4.988  1.00 45.37           C  
ANISOU   33  CA  ASP A   6     6149   4690   6398    817   -666    404       C  
ATOM     34  C   ASP A   6     -13.760  19.442   3.785  1.00 44.14           C  
ANISOU   34  C   ASP A   6     6132   4511   6130    716   -736    482       C  
ATOM     35  O   ASP A   6     -12.570  19.246   3.937  1.00 41.69           O  
ANISOU   35  O   ASP A   6     5898   4213   5728    598   -675    453       O  
ATOM     36  CB  ASP A   6     -15.516  18.101   4.914  1.00 45.10           C  
ANISOU   36  CB  ASP A   6     5944   4804   6389    819   -694    402       C  
ATOM     37  CG  ASP A   6     -16.171  17.741   6.235  1.00 45.44           C  
ANISOU   37  CG  ASP A   6     5852   4903   6510    869   -586    314       C  
ATOM     38  OD1 ASP A   6     -15.659  18.172   7.311  1.00 43.59           O  
ANISOU   38  OD1 ASP A   6     5672   4625   6265    863   -474    240       O  
ATOM     39  OD2 ASP A   6     -17.184  16.987   6.181  1.00 45.79           O  
ANISOU   39  OD2 ASP A   6     5739   5040   6618    903   -612    317       O  
ATOM     40  N   LYS A   7     -14.324  19.774   2.612  1.00 44.65           N  
ANISOU   40  N   LYS A   7     6226   4537   6201    765   -863    579       N  
ATOM     41  CA  LYS A   7     -13.581  19.855   1.338  1.00 43.96           C  
ANISOU   41  CA  LYS A   7     6282   4428   5994    671   -933    664       C  
ATOM     42  C   LYS A   7     -12.515  20.960   1.345  1.00 43.26           C  
ANISOU   42  C   LYS A   7     6376   4203   5860    614   -879    675       C  
ATOM     43  O   LYS A   7     -11.399  20.770   0.843  1.00 41.68           O  
ANISOU   43  O   LYS A   7     6273   4019   5545    480   -851    689       O  
ATOM     44  CB  LYS A   7     -14.540  20.078   0.161  1.00 45.73           C  
ANISOU   44  CB  LYS A   7     6508   4634   6233    751  -1093    771       C  
ATOM     45  CG  LYS A   7     -15.516  18.929  -0.086  1.00 47.11           C  
ANISOU   45  CG  LYS A   7     6510   4953   6436    774  -1167    768       C  
ATOM     46  CD  LYS A   7     -16.823  19.417  -0.713  1.00 52.58           C  
ANISOU   46  CD  LYS A   7     7142   5616   7219    914  -1320    847       C  
ATOM     47  CE  LYS A   7     -17.766  18.260  -1.082  1.00 54.78           C  
ANISOU   47  CE  LYS A   7     7249   6046   7521    912  -1410    845       C  
ATOM     48  NZ  LYS A   7     -17.460  17.676  -2.441  1.00 55.92           N  
ANISOU   48  NZ  LYS A   7     7486   6247   7514    807  -1523    913       N  
ATOM     49  N   THR A   8     -12.846  22.113   1.915  1.00 43.35           N  
ANISOU   49  N   THR A   8     6431   4075   5964    712   -859    663       N  
ATOM     50  CA  THR A   8     -11.863  23.200   2.029  1.00 43.18           C  
ANISOU   50  CA  THR A   8     6586   3910   5911    648   -801    662       C  
ATOM     51  C   THR A   8     -10.723  22.838   2.992  1.00 41.06           C  
ANISOU   51  C   THR A   8     6311   3697   5594    523   -673    555       C  
ATOM     52  O   THR A   8      -9.566  23.258   2.794  1.00 40.86           O  
ANISOU   52  O   THR A   8     6409   3620   5494    399   -631    558       O  
ATOM     53  CB  THR A   8     -12.527  24.493   2.500  1.00 44.69           C  
ANISOU   53  CB  THR A   8     6829   3927   6224    789   -803    660       C  
ATOM     54  OG1 THR A   8     -13.623  24.816   1.621  1.00 47.34           O  
ANISOU   54  OG1 THR A   8     7154   4215   6618    923   -938    765       O  
ATOM     55  CG2 THR A   8     -11.496  25.656   2.511  1.00 45.76           C  
ANISOU   55  CG2 THR A   8     7170   3894   6324    704   -750    665       C  
ATOM     56  N   ASN A   9     -11.071  22.074   4.031  1.00 39.08           N  
ANISOU   56  N   ASN A   9     5914   3551   5383    555   -616    465       N  
ATOM     57  CA  ASN A   9     -10.119  21.645   5.050  1.00 37.69           C  
ANISOU   57  CA  ASN A   9     5718   3441   5162    457   -512    366       C  
ATOM     58  C   ASN A   9      -9.168  20.624   4.481  1.00 36.50           C  
ANISOU   58  C   ASN A   9     5555   3411   4904    323   -512    382       C  
ATOM     59  O   ASN A   9      -7.943  20.753   4.617  1.00 35.22           O  
ANISOU   59  O   ASN A   9     5457   3246   4679    205   -460    353       O  
ATOM     60  CB  ASN A   9     -10.839  21.104   6.304  1.00 37.43           C  
ANISOU   60  CB  ASN A   9     5548   3483   5192    533   -452    278       C  
ATOM     61  CG  ASN A   9     -11.407  22.249   7.216  1.00 37.89           C  
ANISOU   61  CG  ASN A   9     5641   3410   5345    641   -401    218       C  
ATOM     62  OD1 ASN A   9     -10.943  23.372   7.144  1.00 38.16           O  
ANISOU   62  OD1 ASN A   9     5815   3301   5384    626   -393    220       O  
ATOM     63  ND2 ASN A   9     -12.382  21.934   8.079  1.00 37.10           N  
ANISOU   63  ND2 ASN A   9     5419   3360   5317    741   -355    160       N  
ATOM     64  N   THR A  10      -9.716  19.632   3.786  1.00 36.77           N  
ANISOU   64  N   THR A  10     5505   3546   4919    340   -572    427       N  
ATOM     65  CA  THR A  10      -8.864  18.598   3.238  1.00 35.93           C  
ANISOU   65  CA  THR A  10     5387   3549   4715    226   -563    432       C  
ATOM     66  C   THR A  10      -7.977  19.178   2.114  1.00 37.04           C  
ANISOU   66  C   THR A  10     5672   3628   4773    130   -579    498       C  
ATOM     67  O   THR A  10      -6.799  18.903   2.071  1.00 37.05           O  
ANISOU   67  O   THR A  10     5698   3671   4708     16   -520    470       O  
ATOM     68  CB  THR A  10      -9.611  17.273   2.882  1.00 35.53           C  
ANISOU   68  CB  THR A  10     5217   3623   4661    251   -610    444       C  
ATOM     69  OG1 THR A  10      -9.097  16.728   1.655  1.00 36.95           O  
ANISOU   69  OG1 THR A  10     5448   3848   4744    167   -648    494       O  
ATOM     70  CG2 THR A  10     -11.068  17.429   2.796  1.00 34.42           C  
ANISOU   70  CG2 THR A  10     5004   3466   4609    375   -682    475       C  
ATOM     71  N   LYS A  11      -8.521  20.036   1.269  1.00 38.54           N  
ANISOU   71  N   LYS A  11     5958   3716   4971    178   -654    584       N  
ATOM     72  CA  LYS A  11      -7.723  20.783   0.293  1.00 39.83           C  
ANISOU   72  CA  LYS A  11     6284   3796   5053     86   -658    654       C  
ATOM     73  C   LYS A  11      -6.581  21.602   0.910  1.00 39.75           C  
ANISOU   73  C   LYS A  11     6355   3708   5042     -8   -563    604       C  
ATOM     74  O   LYS A  11      -5.478  21.634   0.381  1.00 39.40           O  
ANISOU   74  O   LYS A  11     6380   3674   4916   -141   -516    616       O  
ATOM     75  CB  LYS A  11      -8.635  21.688  -0.557  1.00 41.72           C  
ANISOU   75  CB  LYS A  11     6624   3916   5314    177   -765    763       C  
ATOM     76  CG  LYS A  11      -9.477  20.898  -1.583  1.00 42.82           C  
ANISOU   76  CG  LYS A  11     6719   4142   5410    218   -879    832       C  
ATOM     77  CD  LYS A  11     -10.206  21.802  -2.589  1.00 45.59           C  
ANISOU   77  CD  LYS A  11     7191   4379   5753    292  -1004    958       C  
ATOM     78  CE  LYS A  11     -10.486  21.035  -3.891  1.00 46.00           C  
ANISOU   78  CE  LYS A  11     7263   4525   5691    256  -1105   1030       C  
ATOM     79  NZ  LYS A  11      -9.212  20.669  -4.626  1.00 45.99           N  
ANISOU   79  NZ  LYS A  11     7370   4570   5535     84  -1030   1035       N  
ATOM     80  N   SER A  12      -6.837  22.235   2.049  1.00 40.20           N  
ANISOU   80  N   SER A  12     6395   3692   5188     55   -530    540       N  
ATOM     81  CA  SER A  12      -5.794  22.999   2.725  1.00 40.49           C  
ANISOU   81  CA  SER A  12     6503   3655   5224    -41   -449    479       C  
ATOM     82  C   SER A  12      -4.626  22.121   3.209  1.00 37.92           C  
ANISOU   82  C   SER A  12     6093   3469   4846   -163   -378    401       C  
ATOM     83  O   SER A  12      -3.455  22.505   3.055  1.00 38.05           O  
ANISOU   83  O   SER A  12     6172   3466   4819   -297   -327    389       O  
ATOM     84  CB  SER A  12      -6.372  23.836   3.883  1.00 41.81           C  
ANISOU   84  CB  SER A  12     6680   3716   5492     55   -427    414       C  
ATOM     85  OG  SER A  12      -6.452  23.089   5.092  1.00 44.79           O  
ANISOU   85  OG  SER A  12     6925   4203   5891     81   -381    311       O  
ATOM     86  N   VAL A  13      -4.913  20.941   3.757  1.00 35.52           N  
ANISOU   86  N   VAL A  13     5646   3304   4548   -119   -375    353       N  
ATOM     87  CA  VAL A  13      -3.828  20.098   4.236  1.00 32.86           C  
ANISOU   87  CA  VAL A  13     5229   3090   4168   -214   -320    286       C  
ATOM     88  C   VAL A  13      -3.054  19.547   3.077  1.00 32.82           C  
ANISOU   88  C   VAL A  13     5236   3150   4084   -310   -312    333       C  
ATOM     89  O   VAL A  13      -1.814  19.496   3.166  1.00 31.49           O  
ANISOU   89  O   VAL A  13     5059   3024   3884   -425   -255    295       O  
ATOM     90  CB  VAL A  13      -4.222  18.975   5.256  1.00 32.26           C  
ANISOU   90  CB  VAL A  13     5012   3133   4114   -149   -312    222       C  
ATOM     91  CG1 VAL A  13      -5.715  19.023   5.638  1.00 31.06           C  
ANISOU   91  CG1 VAL A  13     4822   2949   4030     -7   -346    229       C  
ATOM     92  CG2 VAL A  13      -3.711  17.587   4.803  1.00 26.93           C  
ANISOU   92  CG2 VAL A  13     4251   2597   3384   -194   -307    226       C  
ATOM     93  N   PHE A  14      -3.748  19.152   1.999  1.00 32.20           N  
ANISOU   93  N   PHE A  14     5176   3086   3974   -268   -367    408       N  
ATOM     94  CA  PHE A  14      -3.040  18.687   0.821  1.00 32.36           C  
ANISOU   94  CA  PHE A  14     5231   3161   3904   -363   -350    449       C  
ATOM     95  C   PHE A  14      -2.261  19.780   0.152  1.00 34.06           C  
ANISOU   95  C   PHE A  14     5585   3280   4076   -470   -314    494       C  
ATOM     96  O   PHE A  14      -1.158  19.519  -0.338  1.00 33.80           O  
ANISOU   96  O   PHE A  14     5557   3304   3983   -588   -247    483       O  
ATOM     97  CB  PHE A  14      -3.948  17.968  -0.173  1.00 32.58           C  
ANISOU   97  CB  PHE A  14     5256   3232   3890   -306   -422    510       C  
ATOM     98  CG  PHE A  14      -4.225  16.558   0.243  1.00 31.22           C  
ANISOU   98  CG  PHE A  14     4946   3186   3732   -264   -424    457       C  
ATOM     99  CD1 PHE A  14      -3.342  15.549  -0.088  1.00 32.74           C  
ANISOU   99  CD1 PHE A  14     5095   3478   3867   -336   -371    422       C  
ATOM    100  CD2 PHE A  14      -5.288  16.264   1.081  1.00 30.80           C  
ANISOU  100  CD2 PHE A  14     4803   3143   3756   -155   -464    434       C  
ATOM    101  CE1 PHE A  14      -3.551  14.256   0.367  1.00 32.52           C  
ANISOU  101  CE1 PHE A  14     4952   3546   3857   -297   -369    373       C  
ATOM    102  CE2 PHE A  14      -5.498  14.953   1.548  1.00 31.83           C  
ANISOU  102  CE2 PHE A  14     4815   3380   3900   -130   -455    386       C  
ATOM    103  CZ  PHE A  14      -4.642  13.971   1.196  1.00 32.29           C  
ANISOU  103  CZ  PHE A  14     4846   3521   3900   -199   -413    359       C  
ATOM    104  N   ALA A  15      -2.802  20.999   0.147  1.00 35.26           N  
ANISOU  104  N   ALA A  15     5850   3282   4264   -431   -351    542       N  
ATOM    105  CA  ALA A  15      -2.067  22.112  -0.386  1.00 37.91           C  
ANISOU  105  CA  ALA A  15     6334   3505   4565   -541   -312    587       C  
ATOM    106  C   ALA A  15      -0.757  22.257   0.402  1.00 39.12           C  
ANISOU  106  C   ALA A  15     6440   3689   4734   -666   -218    496       C  
ATOM    107  O   ALA A  15       0.316  22.388  -0.201  1.00 40.12           O  
ANISOU  107  O   ALA A  15     6606   3833   4804   -809   -150    506       O  
ATOM    108  CB  ALA A  15      -2.893  23.398  -0.306  1.00 39.20           C  
ANISOU  108  CB  ALA A  15     6624   3484   4786   -461   -367    643       C  
ATOM    109  N   LYS A  16      -0.837  22.185   1.735  1.00 39.06           N  
ANISOU  109  N   LYS A  16     6341   3700   4800   -617   -214    405       N  
ATOM    110  CA  LYS A  16       0.346  22.328   2.585  1.00 40.40           C  
ANISOU  110  CA  LYS A  16     6458   3906   4987   -729   -149    314       C  
ATOM    111  C   LYS A  16       1.341  21.161   2.470  1.00 40.54           C  
ANISOU  111  C   LYS A  16     6341   4097   4965   -801   -103    272       C  
ATOM    112  O   LYS A  16       2.534  21.416   2.410  1.00 42.08           O  
ANISOU  112  O   LYS A  16     6525   4315   5148   -938    -42    242       O  
ATOM    113  CB  LYS A  16      -0.047  22.517   4.053  1.00 40.61           C  
ANISOU  113  CB  LYS A  16     6436   3913   5082   -654   -164    227       C  
ATOM    114  CG  LYS A  16       1.119  22.890   5.007  1.00 42.68           C  
ANISOU  114  CG  LYS A  16     6668   4192   5358   -775   -119    130       C  
ATOM    115  CD  LYS A  16       1.348  24.406   5.066  1.00 45.48           C  
ANISOU  115  CD  LYS A  16     7176   4365   5738   -854    -99    129       C  
ATOM    116  CE  LYS A  16       2.702  24.783   5.699  1.00 49.27           C  
ANISOU  116  CE  LYS A  16     7628   4870   6220  -1021    -55     42       C  
ATOM    117  NZ  LYS A  16       3.802  25.224   4.740  1.00 50.34           N  
ANISOU  117  NZ  LYS A  16     7812   4989   6327  -1199      3     82       N  
ATOM    118  N   ILE A  17       0.873  19.909   2.432  1.00 39.27           N  
ANISOU  118  N   ILE A  17     6077   4052   4792   -713   -130    268       N  
ATOM    119  CA  ILE A  17       1.775  18.731   2.460  1.00 38.70           C  
ANISOU  119  CA  ILE A  17     5873   4134   4699   -755    -89    220       C  
ATOM    120  C   ILE A  17       2.174  18.206   1.089  1.00 38.86           C  
ANISOU  120  C   ILE A  17     5912   4206   4646   -813    -49    268       C  
ATOM    121  O   ILE A  17       2.975  17.263   1.011  1.00 38.47           O  
ANISOU  121  O   ILE A  17     5757   4275   4585   -845     -3    225       O  
ATOM    122  CB  ILE A  17       1.163  17.492   3.218  1.00 37.53           C  
ANISOU  122  CB  ILE A  17     5602   4083   4575   -636   -128    182       C  
ATOM    123  CG1 ILE A  17       0.268  16.642   2.283  1.00 36.83           C  
ANISOU  123  CG1 ILE A  17     5519   4024   4450   -563   -162    238       C  
ATOM    124  CG2 ILE A  17       0.411  17.929   4.489  1.00 36.91           C  
ANISOU  124  CG2 ILE A  17     5522   3952   4552   -555   -167    144       C  
ATOM    125  CD1 ILE A  17      -0.535  15.549   2.982  1.00 34.92           C  
ANISOU  125  CD1 ILE A  17     5180   3850   4238   -452   -202    212       C  
ATOM    126  N   GLY A  18       1.607  18.777   0.018  1.00 39.33           N  
ANISOU  126  N   GLY A  18     6110   4180   4655   -818    -68    355       N  
ATOM    127  CA  GLY A  18       1.860  18.283  -1.367  1.00 38.94           C  
ANISOU  127  CA  GLY A  18     6107   4177   4511   -872    -33    404       C  
ATOM    128  C   GLY A  18       3.320  18.081  -1.777  1.00 38.75           C  
ANISOU  128  C   GLY A  18     6039   4231   4453  -1011     82    366       C  
ATOM    129  O   GLY A  18       3.667  17.053  -2.348  1.00 38.74           O  
ANISOU  129  O   GLY A  18     5980   4333   4408  -1016    124    345       O  
ATOM    130  N   PRO A  19       4.190  19.060  -1.492  1.00 38.93           N  
ANISOU  130  N   PRO A  19     6086   4203   4502  -1126    138    350       N  
ATOM    131  CA  PRO A  19       5.626  18.922  -1.779  1.00 39.68           C  
ANISOU  131  CA  PRO A  19     6108   4381   4586  -1266    253    304       C  
ATOM    132  C   PRO A  19       6.285  17.746  -1.071  1.00 39.21           C  
ANISOU  132  C   PRO A  19     5845   4470   4581  -1228    272    209       C  
ATOM    133  O   PRO A  19       7.363  17.310  -1.479  1.00 39.97           O  
ANISOU  133  O   PRO A  19     5856   4661   4669  -1309    366    171       O  
ATOM    134  CB  PRO A  19       6.238  20.252  -1.283  1.00 40.93           C  
ANISOU  134  CB  PRO A  19     6316   4444   4790  -1386    280    294       C  
ATOM    135  CG  PRO A  19       5.123  21.234  -1.311  1.00 41.03           C  
ANISOU  135  CG  PRO A  19     6500   4291   4798  -1328    202    370       C  
ATOM    136  CD  PRO A  19       3.821  20.443  -1.129  1.00 40.24           C  
ANISOU  136  CD  PRO A  19     6375   4213   4702  -1144    102    386       C  
ATOM    137  N   HIS A  20       5.630  17.232  -0.027  1.00 38.22           N  
ANISOU  137  N   HIS A  20     5647   4364   4512  -1102    187    176       N  
ATOM    138  CA  HIS A  20       6.165  16.160   0.787  1.00 37.37           C  
ANISOU  138  CA  HIS A  20     5363   4378   4456  -1051    185     98       C  
ATOM    139  C   HIS A  20       5.340  14.886   0.741  1.00 36.17           C  
ANISOU  139  C   HIS A  20     5175   4277   4292   -917    138    102       C  
ATOM    140  O   HIS A  20       5.620  13.947   1.503  1.00 33.78           O  
ANISOU  140  O   HIS A  20     4744   4057   4033   -855    123     49       O  
ATOM    141  CB  HIS A  20       6.231  16.631   2.228  1.00 37.72           C  
ANISOU  141  CB  HIS A  20     5357   4405   4570  -1037    128     49       C  
ATOM    142  CG  HIS A  20       7.047  17.864   2.419  1.00 38.93           C  
ANISOU  142  CG  HIS A  20     5542   4505   4745  -1178    164     30       C  
ATOM    143  ND1 HIS A  20       8.422  17.847   2.410  1.00 41.39           N  
ANISOU  143  ND1 HIS A  20     5741   4901   5084  -1295    231    -22       N  
ATOM    144  CD2 HIS A  20       6.681  19.147   2.647  1.00 41.68           C  
ANISOU  144  CD2 HIS A  20     6019   4719   5101  -1223    143     51       C  
ATOM    145  CE1 HIS A  20       8.870  19.073   2.625  1.00 45.06           C  
ANISOU  145  CE1 HIS A  20     6265   5289   5568  -1421    248    -32       C  
ATOM    146  NE2 HIS A  20       7.832  19.881   2.772  1.00 42.78           N  
ANISOU  146  NE2 HIS A  20     6131   4857   5264  -1378    197     11       N  
ATOM    147  N   ALA A  21       4.344  14.860  -0.158  1.00 36.49           N  
ANISOU  147  N   ALA A  21     5330   4264   4271   -877    111    168       N  
ATOM    148  CA  ALA A  21       3.367  13.742  -0.256  1.00 35.90           C  
ANISOU  148  CA  ALA A  21     5237   4221   4184   -761     56    176       C  
ATOM    149  C   ALA A  21       4.056  12.393  -0.432  1.00 35.59           C  
ANISOU  149  C   ALA A  21     5089   4290   4145   -745    108    122       C  
ATOM    150  O   ALA A  21       3.746  11.430   0.241  1.00 34.95           O  
ANISOU  150  O   ALA A  21     4927   4250   4103   -657     70     92       O  
ATOM    151  CB  ALA A  21       2.376  13.991  -1.388  1.00 36.50           C  
ANISOU  151  CB  ALA A  21     5451   4234   4184   -749     17    254       C  
ATOM    152  N   GLU A  22       5.056  12.364  -1.282  1.00 36.74           N  
ANISOU  152  N   GLU A  22     5231   4477   4250   -834    204    106       N  
ATOM    153  CA  GLU A  22       5.851  11.169  -1.514  1.00 36.96           C  
ANISOU  153  CA  GLU A  22     5153   4601   4287   -819    273     46       C  
ATOM    154  C   GLU A  22       6.463  10.593  -0.255  1.00 36.23           C  
ANISOU  154  C   GLU A  22     4901   4573   4293   -763    254    -14       C  
ATOM    155  O   GLU A  22       6.282   9.422   0.028  1.00 36.19           O  
ANISOU  155  O   GLU A  22     4834   4604   4311   -671    233    -41       O  
ATOM    156  CB  GLU A  22       6.966  11.515  -2.495  1.00 38.51           C  
ANISOU  156  CB  GLU A  22     5360   4833   4440   -941    400     33       C  
ATOM    157  CG  GLU A  22       7.685  10.350  -3.115  1.00 39.90           C  
ANISOU  157  CG  GLU A  22     5460   5095   4604   -927    494    -27       C  
ATOM    158  CD  GLU A  22       8.557  10.801  -4.279  1.00 41.94           C  
ANISOU  158  CD  GLU A  22     5765   5379   4792  -1058    633    -30       C  
ATOM    159  OE1 GLU A  22       8.018  11.446  -5.218  1.00 39.70           O  
ANISOU  159  OE1 GLU A  22     5651   5033   4399  -1122    639     36       O  
ATOM    160  OE2 GLU A  22       9.776  10.533  -4.226  1.00 46.09           O  
ANISOU  160  OE2 GLU A  22     6154   5986   5372  -1095    735    -95       O  
ATOM    161  N   GLU A  23       7.200  11.406   0.492  1.00 36.66           N  
ANISOU  161  N   GLU A  23     4895   4634   4398   -823    257    -35       N  
ATOM    162  CA  GLU A  23       7.874  10.910   1.683  1.00 36.72           C  
ANISOU  162  CA  GLU A  23     4751   4711   4488   -778    226    -90       C  
ATOM    163  C   GLU A  23       6.817  10.536   2.724  1.00 33.77           C  
ANISOU  163  C   GLU A  23     4394   4306   4131   -667    120    -74       C  
ATOM    164  O   GLU A  23       6.974   9.515   3.401  1.00 33.96           O  
ANISOU  164  O   GLU A  23     4327   4383   4193   -583     90   -101       O  
ATOM    165  CB  GLU A  23       8.908  11.884   2.273  1.00 38.28           C  
ANISOU  165  CB  GLU A  23     4880   4932   4733   -881    240   -122       C  
ATOM    166  CG  GLU A  23       9.802  12.707   1.289  1.00 44.75           C  
ANISOU  166  CG  GLU A  23     5716   5755   5532  -1032    350   -124       C  
ATOM    167  CD  GLU A  23      10.759  11.897   0.338  1.00 51.83           C  
ANISOU  167  CD  GLU A  23     6520   6745   6429  -1054    470   -161       C  
ATOM    168  OE1 GLU A  23      11.733  11.256   0.833  1.00 54.41           O  
ANISOU  168  OE1 GLU A  23     6669   7171   6834  -1027    484   -222       O  
ATOM    169  OE2 GLU A  23      10.584  11.971  -0.919  1.00 53.47           O  
ANISOU  169  OE2 GLU A  23     6833   6926   6557  -1103    553   -131       O  
ATOM    170  N   TYR A  24       5.730  11.309   2.809  1.00 31.30           N  
ANISOU  170  N   TYR A  24     4198   3906   3790   -661     71    -29       N  
ATOM    171  CA  TYR A  24       4.662  11.024   3.759  1.00 29.29           C  
ANISOU  171  CA  TYR A  24     3957   3622   3551   -564    -11    -17       C  
ATOM    172  C   TYR A  24       3.851   9.774   3.409  1.00 27.92           C  
ANISOU  172  C   TYR A  24     3787   3460   3362   -474    -27      0       C  
ATOM    173  O   TYR A  24       3.293   9.141   4.297  1.00 26.43           O  
ANISOU  173  O   TYR A  24     3567   3278   3196   -396    -76     -3       O  
ATOM    174  CB  TYR A  24       3.694  12.200   3.966  1.00 29.07           C  
ANISOU  174  CB  TYR A  24     4038   3496   3512   -569    -52     19       C  
ATOM    175  CG  TYR A  24       4.283  13.502   4.511  1.00 28.79           C  
ANISOU  175  CG  TYR A  24     4024   3421   3496   -653    -47     -2       C  
ATOM    176  CD1 TYR A  24       5.546  13.561   5.096  1.00 28.82           C  
ANISOU  176  CD1 TYR A  24     3930   3490   3530   -717    -30    -57       C  
ATOM    177  CD2 TYR A  24       3.538  14.666   4.476  1.00 26.98           C  
ANISOU  177  CD2 TYR A  24     3910   3082   3260   -665    -68     30       C  
ATOM    178  CE1 TYR A  24       6.070  14.777   5.579  1.00 29.23           C  
ANISOU  178  CE1 TYR A  24     4007   3500   3598   -812    -30    -84       C  
ATOM    179  CE2 TYR A  24       4.043  15.876   4.970  1.00 29.26           C  
ANISOU  179  CE2 TYR A  24     4236   3314   3568   -747    -61      4       C  
ATOM    180  CZ  TYR A  24       5.299  15.930   5.496  1.00 29.03           C  
ANISOU  180  CZ  TYR A  24     4118   3352   3561   -829    -41    -54       C  
ATOM    181  OH  TYR A  24       5.750  17.135   5.957  1.00 30.38           O  
ANISOU  181  OH  TYR A  24     4335   3460   3749   -924    -39    -84       O  
ATOM    182  N   GLY A  25       3.781   9.414   2.136  1.00 27.43           N  
ANISOU  182  N   GLY A  25     3771   3397   3254   -494     15     15       N  
ATOM    183  CA  GLY A  25       3.206   8.120   1.762  1.00 26.10           C  
ANISOU  183  CA  GLY A  25     3600   3243   3072   -426      6     15       C  
ATOM    184  C   GLY A  25       4.062   6.945   2.210  1.00 25.45           C  
ANISOU  184  C   GLY A  25     3409   3226   3034   -379     33    -35       C  
ATOM    185  O   GLY A  25       3.537   5.917   2.654  1.00 23.53           O  
ANISOU  185  O   GLY A  25     3148   2982   2811   -302     -1    -36       O  
ATOM    186  N   ALA A  26       5.383   7.095   2.061  1.00 25.62           N  
ANISOU  186  N   ALA A  26     3357   3301   3077   -426     96    -73       N  
ATOM    187  CA  ALA A  26       6.321   6.064   2.462  1.00 26.22           C  
ANISOU  187  CA  ALA A  26     3313   3439   3208   -372    120   -119       C  
ATOM    188  C   ALA A  26       6.221   5.917   3.964  1.00 25.19           C  
ANISOU  188  C   ALA A  26     3126   3319   3126   -310     36   -115       C  
ATOM    189  O   ALA A  26       6.053   4.804   4.461  1.00 24.93           O  
ANISOU  189  O   ALA A  26     3063   3292   3119   -222      6   -116       O  
ATOM    190  CB  ALA A  26       7.796   6.414   2.022  1.00 27.85           C  
ANISOU  190  CB  ALA A  26     3428   3712   3440   -443    207   -164       C  
ATOM    191  N   GLU A  27       6.272   7.042   4.682  1.00 24.52           N  
ANISOU  191  N   GLU A  27     3044   3228   3043   -360     -2   -108       N  
ATOM    192  CA  GLU A  27       6.179   7.004   6.141  1.00 23.49           C  
ANISOU  192  CA  GLU A  27     2877   3111   2937   -313    -80   -108       C  
ATOM    193  C   GLU A  27       4.846   6.352   6.623  1.00 22.21           C  
ANISOU  193  C   GLU A  27     2782   2901   2756   -233   -127    -72       C  
ATOM    194  O   GLU A  27       4.839   5.493   7.502  1.00 22.44           O  
ANISOU  194  O   GLU A  27     2775   2950   2801   -162   -168    -68       O  
ATOM    195  CB  GLU A  27       6.380   8.413   6.730  1.00 23.49           C  
ANISOU  195  CB  GLU A  27     2893   3098   2932   -393   -104   -118       C  
ATOM    196  CG  GLU A  27       6.824   8.341   8.150  1.00 23.56           C  
ANISOU  196  CG  GLU A  27     2838   3153   2961   -367   -175   -140       C  
ATOM    197  CD  GLU A  27       6.789   9.625   8.897  1.00 27.17           C  
ANISOU  197  CD  GLU A  27     3336   3584   3402   -436   -209   -158       C  
ATOM    198  OE1 GLU A  27       7.163  10.718   8.341  1.00 25.25           O  
ANISOU  198  OE1 GLU A  27     3118   3314   3162   -538   -170   -171       O  
ATOM    199  OE2 GLU A  27       6.414   9.520  10.098  1.00 29.57           O  
ANISOU  199  OE2 GLU A  27     3655   3892   3687   -392   -272   -160       O  
ATOM    200  N   THR A  28       3.726   6.739   6.026  1.00 21.36           N  
ANISOU  200  N   THR A  28     2768   2733   2616   -245   -123    -41       N  
ATOM    201  CA  THR A  28       2.406   6.115   6.297  1.00 19.68           C  
ANISOU  201  CA  THR A  28     2602   2480   2393   -183   -156    -10       C  
ATOM    202  C   THR A  28       2.430   4.588   6.250  1.00 19.81           C  
ANISOU  202  C   THR A  28     2590   2512   2425   -120   -151    -12       C  
ATOM    203  O   THR A  28       1.922   3.915   7.145  1.00 21.01           O  
ANISOU  203  O   THR A  28     2740   2656   2586    -66   -184      4       O  
ATOM    204  CB  THR A  28       1.333   6.650   5.306  1.00 18.51           C  
ANISOU  204  CB  THR A  28     2540   2277   2216   -208   -153     21       C  
ATOM    205  OG1 THR A  28       1.206   8.050   5.534  1.00 20.27           O  
ANISOU  205  OG1 THR A  28     2801   2466   2434   -249   -164     28       O  
ATOM    206  CG2 THR A  28      -0.052   5.956   5.484  1.00 13.78           C  
ANISOU  206  CG2 THR A  28     1967   1649   1620   -154   -187     48       C  
ATOM    207  N   LEU A  29       3.004   4.044   5.200  1.00 20.57           N  
ANISOU  207  N   LEU A  29     2675   2620   2521   -130   -103    -33       N  
ATOM    208  CA  LEU A  29       2.998   2.618   4.972  1.00 21.03           C  
ANISOU  208  CA  LEU A  29     2724   2670   2595    -72    -89    -43       C  
ATOM    209  C   LEU A  29       3.905   1.948   5.959  1.00 21.43           C  
ANISOU  209  C   LEU A  29     2693   2756   2692     -9   -107    -54       C  
ATOM    210  O   LEU A  29       3.606   0.884   6.431  1.00 22.35           O  
ANISOU  210  O   LEU A  29     2818   2848   2827     55   -128    -39       O  
ATOM    211  CB  LEU A  29       3.480   2.325   3.558  1.00 21.99           C  
ANISOU  211  CB  LEU A  29     2862   2797   2698   -101    -19    -75       C  
ATOM    212  CG  LEU A  29       2.378   2.432   2.522  1.00 24.03           C  
ANISOU  212  CG  LEU A  29     3220   3013   2899   -141    -21    -58       C  
ATOM    213  CD1 LEU A  29       3.042   2.347   1.141  1.00 28.87           C  
ANISOU  213  CD1 LEU A  29     3859   3641   3469   -187     57    -95       C  
ATOM    214  CD2 LEU A  29       1.342   1.282   2.690  1.00 23.52           C  
ANISOU  214  CD2 LEU A  29     3191   2905   2843    -95    -56    -47       C  
ATOM    215  N   GLU A  30       5.018   2.576   6.283  1.00 22.02           N  
ANISOU  215  N   GLU A  30     2690   2886   2788    -30   -106    -76       N  
ATOM    216  CA  GLU A  30       5.943   2.008   7.250  1.00 23.36           C  
ANISOU  216  CA  GLU A  30     2771   3102   3005     33   -144    -84       C  
ATOM    217  C   GLU A  30       5.286   1.937   8.617  1.00 22.54           C  
ANISOU  217  C   GLU A  30     2701   2983   2880     67   -221    -44       C  
ATOM    218  O   GLU A  30       5.409   0.909   9.309  1.00 23.63           O  
ANISOU  218  O   GLU A  30     2826   3116   3036    145   -258    -23       O  
ATOM    219  CB  GLU A  30       7.215   2.841   7.297  1.00 24.73           C  
ANISOU  219  CB  GLU A  30     2843   3347   3205    -17   -135   -120       C  
ATOM    220  CG  GLU A  30       8.304   2.229   8.101  1.00 28.26           C  
ANISOU  220  CG  GLU A  30     3174   3854   3710     51   -182   -132       C  
ATOM    221  CD  GLU A  30       9.594   3.012   8.015  1.00 33.44           C  
ANISOU  221  CD  GLU A  30     3706   4592   4406    -10   -168   -177       C  
ATOM    222  OE1 GLU A  30       9.914   3.550   6.935  1.00 39.98           O  
ANISOU  222  OE1 GLU A  30     4524   5430   5237    -86    -80   -207       O  
ATOM    223  OE2 GLU A  30      10.300   3.096   9.036  1.00 39.55           O  
ANISOU  223  OE2 GLU A  30     4394   5426   5208      9   -247   -181       O  
ATOM    224  N   ARG A  31       4.555   3.004   8.990  1.00 19.77           N  
ANISOU  224  N   ARG A  31     2405   2618   2488     12   -239    -32       N  
ATOM    225  CA  ARG A  31       3.782   3.004  10.223  1.00 17.56           C  
ANISOU  225  CA  ARG A  31     2171   2323   2176     36   -289     -1       C  
ATOM    226  C   ARG A  31       2.729   1.908  10.214  1.00 18.27           C  
ANISOU  226  C   ARG A  31     2320   2360   2262     85   -281     35       C  
ATOM    227  O   ARG A  31       2.540   1.221  11.226  1.00 16.44           O  
ANISOU  227  O   ARG A  31     2105   2123   2017    131   -315     66       O  
ATOM    228  CB  ARG A  31       3.157   4.374  10.476  1.00 16.23           C  
ANISOU  228  CB  ARG A  31     2052   2138   1975    -25   -291     -8       C  
ATOM    229  CG  ARG A  31       4.266   5.454  10.773  1.00 14.77           C  
ANISOU  229  CG  ARG A  31     1818   2001   1794    -85   -310    -47       C  
ATOM    230  CD  ARG A  31       3.841   6.900  10.928  1.00 12.72           C  
ANISOU  230  CD  ARG A  31     1614   1708   1510   -152   -306    -64       C  
ATOM    231  NE  ARG A  31       5.029   7.633  11.353  1.00 18.08           N  
ANISOU  231  NE  ARG A  31     2237   2437   2195   -212   -333   -105       N  
ATOM    232  CZ  ARG A  31       5.548   7.687  12.595  1.00 17.31           C  
ANISOU  232  CZ  ARG A  31     2114   2387   2077   -209   -398   -124       C  
ATOM    233  NH1 ARG A  31       4.967   7.073  13.621  1.00 12.08           N  
ANISOU  233  NH1 ARG A  31     1491   1728   1373   -147   -436   -101       N  
ATOM    234  NH2 ARG A  31       6.692   8.373  12.806  1.00 18.99           N  
ANISOU  234  NH2 ARG A  31     2261   2651   2305   -280   -426   -168       N  
ATOM    235  N   LEU A  32       2.064   1.739   9.061  1.00 18.99           N  
ANISOU  235  N   LEU A  32     2447   2411   2358     64   -238     33       N  
ATOM    236  CA  LEU A  32       1.033   0.717   8.888  1.00 19.95           C  
ANISOU  236  CA  LEU A  32     2618   2479   2481     89   -229     59       C  
ATOM    237  C   LEU A  32       1.612  -0.680   9.152  1.00 20.52           C  
ANISOU  237  C   LEU A  32     2678   2538   2582    156   -234     68       C  
ATOM    238  O   LEU A  32       1.081  -1.453   9.939  1.00 21.26           O  
ANISOU  238  O   LEU A  32     2809   2600   2671    189   -252    105       O  
ATOM    239  CB  LEU A  32       0.467   0.775   7.472  1.00 19.03           C  
ANISOU  239  CB  LEU A  32     2535   2334   2361     49   -195     45       C  
ATOM    240  CG  LEU A  32      -0.625  -0.239   7.199  1.00 21.29           C  
ANISOU  240  CG  LEU A  32     2869   2569   2651     55   -193     63       C  
ATOM    241  CD1 LEU A  32      -1.835   0.083   8.109  1.00 21.34           C  
ANISOU  241  CD1 LEU A  32     2892   2565   2650     48   -214     98       C  
ATOM    242  CD2 LEU A  32      -1.025  -0.314   5.682  1.00 16.81           C  
ANISOU  242  CD2 LEU A  32     2338   1981   2068     12   -172     40       C  
ATOM    243  N   PHE A  33       2.728  -0.977   8.524  1.00 21.03           N  
ANISOU  243  N   PHE A  33     2691   2622   2678    179   -213     34       N  
ATOM    244  CA  PHE A  33       3.344  -2.290   8.669  1.00 21.47           C  
ANISOU  244  CA  PHE A  33     2731   2653   2776    260   -215     37       C  
ATOM    245  C   PHE A  33       3.930  -2.561  10.059  1.00 23.10           C  
ANISOU  245  C   PHE A  33     2906   2884   2988    323   -282     74       C  
ATOM    246  O   PHE A  33       3.840  -3.710  10.556  1.00 23.97           O  
ANISOU  246  O   PHE A  33     3052   2942   3112    389   -303    111       O  
ATOM    247  CB  PHE A  33       4.404  -2.455   7.619  1.00 21.00           C  
ANISOU  247  CB  PHE A  33     2611   2613   2754    274   -163    -18       C  
ATOM    248  CG  PHE A  33       3.855  -2.451   6.215  1.00 20.95           C  
ANISOU  248  CG  PHE A  33     2661   2576   2725    219    -99    -52       C  
ATOM    249  CD1 PHE A  33       2.640  -2.981   5.939  1.00 21.97           C  
ANISOU  249  CD1 PHE A  33     2879   2640   2831    199   -100    -35       C  
ATOM    250  CD2 PHE A  33       4.556  -1.870   5.180  1.00 23.41           C  
ANISOU  250  CD2 PHE A  33     2937   2928   3031    177    -40   -100       C  
ATOM    251  CE1 PHE A  33       2.128  -2.957   4.629  1.00 24.73           C  
ANISOU  251  CE1 PHE A  33     3283   2967   3146    142    -59    -67       C  
ATOM    252  CE2 PHE A  33       4.055  -1.832   3.874  1.00 23.99           C  
ANISOU  252  CE2 PHE A  33     3079   2976   3061    120     13   -127       C  
ATOM    253  CZ  PHE A  33       2.867  -2.365   3.595  1.00 24.55           C  
ANISOU  253  CZ  PHE A  33     3238   2985   3103    105     -4   -112       C  
ATOM    254  N   THR A  34       4.489  -1.516  10.701  1.00 23.15           N  
ANISOU  254  N   THR A  34     2859   2963   2976    296   -322     67       N  
ATOM    255  CA  THR A  34       5.067  -1.659  12.036  1.00 23.32           C  
ANISOU  255  CA  THR A  34     2854   3021   2984    345   -402     99       C  
ATOM    256  C   THR A  34       3.987  -1.744  13.108  1.00 23.06           C  
ANISOU  256  C   THR A  34     2919   2957   2885    335   -429    153       C  
ATOM    257  O   THR A  34       4.007  -2.665  13.959  1.00 23.22           O  
ANISOU  257  O   THR A  34     2978   2953   2891    397   -473    205       O  
ATOM    258  CB  THR A  34       6.057  -0.504  12.326  1.00 24.39           C  
ANISOU  258  CB  THR A  34     2900   3248   3120    303   -439     62       C  
ATOM    259  OG1 THR A  34       7.037  -0.467  11.286  1.00 22.47           O  
ANISOU  259  OG1 THR A  34     2559   3036   2942    303   -394     12       O  
ATOM    260  CG2 THR A  34       6.790  -0.678  13.687  1.00 24.30           C  
ANISOU  260  CG2 THR A  34     2854   3289   3091    353   -543     91       C  
ATOM    261  N   THR A  35       3.047  -0.792  13.061  1.00 21.82           N  
ANISOU  261  N   THR A  35     2804   2799   2688    261   -399    141       N  
ATOM    262  CA  THR A  35       2.042  -0.610  14.113  1.00 21.06           C  
ANISOU  262  CA  THR A  35     2785   2690   2527    242   -407    176       C  
ATOM    263  C   THR A  35       0.995  -1.729  14.013  1.00 21.69           C  
ANISOU  263  C   THR A  35     2933   2696   2612    257   -369    220       C  
ATOM    264  O   THR A  35       0.475  -2.191  15.022  1.00 21.11           O  
ANISOU  264  O   THR A  35     2922   2605   2492    267   -378    267       O  
ATOM    265  CB  THR A  35       1.379   0.820  14.025  1.00 20.61           C  
ANISOU  265  CB  THR A  35     2739   2647   2443    170   -378    141       C  
ATOM    266  OG1 THR A  35       2.381   1.834  14.186  1.00 20.81           O  
ANISOU  266  OG1 THR A  35     2714   2731   2464    142   -413    100       O  
ATOM    267  CG2 THR A  35       0.269   1.078  15.115  1.00 21.03           C  
ANISOU  267  CG2 THR A  35     2866   2691   2434    153   -365    164       C  
ATOM    268  N   TYR A  36       0.707  -2.175  12.781  1.00 21.89           N  
ANISOU  268  N   TYR A  36     2952   2677   2688    250   -325    201       N  
ATOM    269  CA  TYR A  36      -0.326  -3.190  12.511  1.00 21.19           C  
ANISOU  269  CA  TYR A  36     2924   2515   2613    243   -290    229       C  
ATOM    270  C   TYR A  36       0.245  -4.308  11.623  1.00 21.49           C  
ANISOU  270  C   TYR A  36     2960   2501   2705    286   -278    216       C  
ATOM    271  O   TYR A  36      -0.156  -4.458  10.466  1.00 20.50           O  
ANISOU  271  O   TYR A  36     2840   2345   2603    254   -240    181       O  
ATOM    272  CB  TYR A  36      -1.546  -2.523  11.803  1.00 20.52           C  
ANISOU  272  CB  TYR A  36     2844   2423   2528    173   -250    207       C  
ATOM    273  CG  TYR A  36      -2.134  -1.344  12.519  1.00 19.01           C  
ANISOU  273  CG  TYR A  36     2650   2273   2300    141   -248    207       C  
ATOM    274  CD1 TYR A  36      -3.056  -1.516  13.555  1.00 22.03           C  
ANISOU  274  CD1 TYR A  36     3073   2647   2650    129   -229    242       C  
ATOM    275  CD2 TYR A  36      -1.796  -0.065  12.166  1.00 18.22           C  
ANISOU  275  CD2 TYR A  36     2515   2212   2197    119   -255    169       C  
ATOM    276  CE1 TYR A  36      -3.589  -0.417  14.244  1.00 21.46           C  
ANISOU  276  CE1 TYR A  36     3001   2609   2543    107   -213    229       C  
ATOM    277  CE2 TYR A  36      -2.338   1.041  12.833  1.00 17.99           C  
ANISOU  277  CE2 TYR A  36     2493   2204   2138     96   -248    160       C  
ATOM    278  CZ  TYR A  36      -3.200   0.868  13.868  1.00 19.10           C  
ANISOU  278  CZ  TYR A  36     2669   2341   2248     96   -227    185       C  
ATOM    279  OH  TYR A  36      -3.684   1.986  14.528  1.00 22.69           O  
ANISOU  279  OH  TYR A  36     3133   2813   2674     81   -209    163       O  
ATOM    280  N   PRO A  37       1.169  -5.125  12.150  1.00 24.03           N  
ANISOU  280  N   PRO A  37     3279   2807   3044    365   -312    241       N  
ATOM    281  CA  PRO A  37       1.930  -6.080  11.288  1.00 24.45           C  
ANISOU  281  CA  PRO A  37     3316   2812   3161    426   -294    213       C  
ATOM    282  C   PRO A  37       1.075  -7.032  10.489  1.00 24.57           C  
ANISOU  282  C   PRO A  37     3404   2731   3199    400   -244    204       C  
ATOM    283  O   PRO A  37       1.522  -7.535   9.469  1.00 25.93           O  
ANISOU  283  O   PRO A  37     3569   2869   3413    424   -209    154       O  
ATOM    284  CB  PRO A  37       2.774  -6.902  12.291  1.00 25.62           C  
ANISOU  284  CB  PRO A  37     3467   2941   3324    526   -354    265       C  
ATOM    285  CG  PRO A  37       2.547  -6.272  13.627  1.00 26.72           C  
ANISOU  285  CG  PRO A  37     3625   3135   3391    505   -408    316       C  
ATOM    286  CD  PRO A  37       1.288  -5.480  13.575  1.00 24.96           C  
ANISOU  286  CD  PRO A  37     3437   2925   3121    405   -364    307       C  
ATOM    287  N   GLN A  38      -0.144  -7.309  10.927  1.00 24.56           N  
ANISOU  287  N   GLN A  38     3475   2688   3171    347   -236    245       N  
ATOM    288  CA  GLN A  38      -1.000  -8.210  10.143  1.00 24.58           C  
ANISOU  288  CA  GLN A  38     3542   2601   3197    303   -195    230       C  
ATOM    289  C   GLN A  38      -1.260  -7.688   8.727  1.00 23.81           C  
ANISOU  289  C   GLN A  38     3418   2527   3103    245   -165    158       C  
ATOM    290  O   GLN A  38      -1.576  -8.470   7.826  1.00 25.69           O  
ANISOU  290  O   GLN A  38     3703   2697   3361    222   -137    122       O  
ATOM    291  CB  GLN A  38      -2.296  -8.562  10.886  1.00 24.17           C  
ANISOU  291  CB  GLN A  38     3553   2508   3122    240   -185    286       C  
ATOM    292  CG  GLN A  38      -3.333  -7.498  10.914  1.00 24.47           C  
ANISOU  292  CG  GLN A  38     3554   2613   3129    160   -174    279       C  
ATOM    293  CD  GLN A  38      -3.169  -6.457  12.033  1.00 25.54           C  
ANISOU  293  CD  GLN A  38     3657   2831   3217    173   -195    308       C  
ATOM    294  OE1 GLN A  38      -2.084  -6.312  12.679  1.00 23.79           O  
ANISOU  294  OE1 GLN A  38     3423   2641   2977    240   -233    323       O  
ATOM    295  NE2 GLN A  38      -4.249  -5.669  12.227  1.00 21.08           N  
ANISOU  295  NE2 GLN A  38     3071   2305   2633    111   -174    307       N  
ATOM    296  N   THR A  39      -1.089  -6.391   8.507  1.00 22.23           N  
ANISOU  296  N   THR A  39     3154   2417   2877    220   -173    137       N  
ATOM    297  CA  THR A  39      -1.249  -5.829   7.151  1.00 21.44           C  
ANISOU  297  CA  THR A  39     3042   2340   2765    167   -151     80       C  
ATOM    298  C   THR A  39      -0.184  -6.292   6.178  1.00 21.82           C  
ANISOU  298  C   THR A  39     3084   2374   2833    206   -115     22       C  
ATOM    299  O   THR A  39      -0.370  -6.237   4.959  1.00 21.24           O  
ANISOU  299  O   THR A  39     3035   2295   2739    160    -86    -28       O  
ATOM    300  CB  THR A  39      -1.354  -4.255   7.145  1.00 20.05           C  
ANISOU  300  CB  THR A  39     2815   2248   2555    128   -166     79       C  
ATOM    301  OG1 THR A  39      -0.169  -3.645   7.726  1.00 19.34           O  
ANISOU  301  OG1 THR A  39     2666   2214   2467    172   -178     78       O  
ATOM    302  CG2 THR A  39      -2.588  -3.857   7.901  1.00 15.65           C  
ANISOU  302  CG2 THR A  39     2266   1696   1985     90   -185    120       C  
ATOM    303  N   LYS A  40       0.929  -6.771   6.723  1.00 23.17           N  
ANISOU  303  N   LYS A  40     3221   2540   3041    294   -116     27       N  
ATOM    304  CA  LYS A  40       2.066  -7.237   5.908  1.00 23.20           C  
ANISOU  304  CA  LYS A  40     3199   2536   3082    351    -69    -34       C  
ATOM    305  C   LYS A  40       1.669  -8.448   5.077  1.00 22.95           C  
ANISOU  305  C   LYS A  40     3254   2401   3063    349    -27    -75       C  
ATOM    306  O   LYS A  40       2.302  -8.714   4.063  1.00 22.56           O  
ANISOU  306  O   LYS A  40     3205   2343   3023    365     31   -145       O  
ATOM    307  CB  LYS A  40       3.262  -7.607   6.793  1.00 24.30           C  
ANISOU  307  CB  LYS A  40     3271   2686   3275    461    -94    -13       C  
ATOM    308  CG  LYS A  40       3.881  -6.413   7.552  1.00 26.42           C  
ANISOU  308  CG  LYS A  40     3445   3065   3530    458   -139      9       C  
ATOM    309  CD  LYS A  40       4.612  -6.820   8.841  1.00 29.51           C  
ANISOU  309  CD  LYS A  40     3796   3465   3953    553   -208     61       C  
ATOM    310  CE  LYS A  40       6.022  -7.335   8.634  1.00 34.26           C  
ANISOU  310  CE  LYS A  40     4305   4080   4632    658   -199     27       C  
ATOM    311  NZ  LYS A  40       6.710  -7.846   9.929  1.00 32.72           N  
ANISOU  311  NZ  LYS A  40     4076   3888   4470    766   -291     90       N  
ATOM    312  N   THR A  41       0.614  -9.173   5.481  1.00 21.95           N  
ANISOU  312  N   THR A  41     3208   2195   2936    319    -49    -37       N  
ATOM    313  CA  THR A  41       0.203 -10.375   4.714  1.00 21.72           C  
ANISOU  313  CA  THR A  41     3275   2055   2923    303    -13    -81       C  
ATOM    314  C   THR A  41      -0.321 -10.023   3.305  1.00 21.27           C  
ANISOU  314  C   THR A  41     3251   2019   2812    209     14   -151       C  
ATOM    315  O   THR A  41      -0.350 -10.854   2.433  1.00 20.57           O  
ANISOU  315  O   THR A  41     3235   1858   2723    197     53   -215       O  
ATOM    316  CB  THR A  41      -0.807 -11.293   5.444  1.00 21.60           C  
ANISOU  316  CB  THR A  41     3342   1942   2925    274    -38    -26       C  
ATOM    317  OG1 THR A  41      -2.025 -10.608   5.716  1.00 18.02           O  
ANISOU  317  OG1 THR A  41     2879   1537   2432    175    -69     12       O  
ATOM    318  CG2 THR A  41      -0.219 -11.844   6.748  1.00 24.22           C  
ANISOU  318  CG2 THR A  41     3674   2232   3297    374    -64     48       C  
ATOM    319  N   TYR A  42      -0.729  -8.780   3.100  1.00 20.79           N  
ANISOU  319  N   TYR A  42     3146   2054   2701    143    -12   -138       N  
ATOM    320  CA  TYR A  42      -1.195  -8.359   1.793  1.00 20.87           C  
ANISOU  320  CA  TYR A  42     3193   2090   2648     59     -2   -189       C  
ATOM    321  C   TYR A  42       0.008  -8.102   0.838  1.00 22.12           C  
ANISOU  321  C   TYR A  42     3337   2286   2782     87     66   -257       C  
ATOM    322  O   TYR A  42      -0.162  -7.940  -0.358  1.00 23.39           O  
ANISOU  322  O   TYR A  42     3551   2459   2877     24     90   -310       O  
ATOM    323  CB  TYR A  42      -2.057  -7.090   1.945  1.00 19.48           C  
ANISOU  323  CB  TYR A  42     2978   1992   2432     -8    -59   -141       C  
ATOM    324  CG  TYR A  42      -3.412  -7.325   2.578  1.00 17.64           C  
ANISOU  324  CG  TYR A  42     2755   1731   2217    -56   -109    -93       C  
ATOM    325  CD1 TYR A  42      -4.450  -7.871   1.841  1.00 15.34           C  
ANISOU  325  CD1 TYR A  42     2521   1400   1909   -136   -132   -119       C  
ATOM    326  CD2 TYR A  42      -3.651  -7.018   3.925  1.00 18.55           C  
ANISOU  326  CD2 TYR A  42     2821   1864   2363    -28   -130    -25       C  
ATOM    327  CE1 TYR A  42      -5.672  -8.086   2.401  1.00 18.76           C  
ANISOU  327  CE1 TYR A  42     2943   1817   2369   -188   -170    -80       C  
ATOM    328  CE2 TYR A  42      -4.905  -7.271   4.522  1.00 17.34           C  
ANISOU  328  CE2 TYR A  42     2671   1689   2228    -77   -156     15       C  
ATOM    329  CZ  TYR A  42      -5.914  -7.778   3.739  1.00 17.92           C  
ANISOU  329  CZ  TYR A  42     2782   1729   2298   -158   -174    -12       C  
ATOM    330  OH  TYR A  42      -7.171  -7.991   4.246  1.00 17.37           O  
ANISOU  330  OH  TYR A  42     2694   1649   2255   -219   -195     21       O  
ATOM    331  N   PHE A  43       1.219  -8.057   1.380  1.00 22.68           N  
ANISOU  331  N   PHE A  43     3332   2382   2904    177     97   -256       N  
ATOM    332  CA  PHE A  43       2.413  -7.750   0.594  1.00 22.74           C  
ANISOU  332  CA  PHE A  43     3298   2440   2903    202    175   -319       C  
ATOM    333  C   PHE A  43       3.429  -8.866   0.795  1.00 24.31           C  
ANISOU  333  C   PHE A  43     3474   2581   3184    318    227   -359       C  
ATOM    334  O   PHE A  43       4.564  -8.626   1.173  1.00 24.12           O  
ANISOU  334  O   PHE A  43     3344   2609   3213    392    250   -362       O  
ATOM    335  CB  PHE A  43       2.998  -6.399   0.979  1.00 21.62           C  
ANISOU  335  CB  PHE A  43     3056   2405   2754    191    162   -284       C  
ATOM    336  CG  PHE A  43       2.024  -5.248   0.884  1.00 19.57           C  
ANISOU  336  CG  PHE A  43     2820   2188   2428     96    107   -238       C  
ATOM    337  CD1 PHE A  43       2.090  -4.345  -0.178  1.00 21.79           C  
ANISOU  337  CD1 PHE A  43     3126   2520   2635     20    139   -261       C  
ATOM    338  CD2 PHE A  43       1.052  -5.063   1.844  1.00 16.25           C  
ANISOU  338  CD2 PHE A  43     2401   1755   2018     85     30   -172       C  
ATOM    339  CE1 PHE A  43       1.221  -3.258  -0.262  1.00 19.68           C  
ANISOU  339  CE1 PHE A  43     2881   2281   2315    -51     81   -212       C  
ATOM    340  CE2 PHE A  43       0.162  -4.010   1.759  1.00 18.07           C  
ANISOU  340  CE2 PHE A  43     2643   2020   2203     15    -17   -134       C  
ATOM    341  CZ  PHE A  43       0.257  -3.101   0.710  1.00 20.49           C  
ANISOU  341  CZ  PHE A  43     2971   2368   2445    -46      2   -152       C  
ATOM    342  N   PRO A  44       3.023 -10.108   0.495  1.00 26.20           N  
ANISOU  342  N   PRO A  44     3810   2706   3439    335    245   -395       N  
ATOM    343  CA  PRO A  44       3.896 -11.255   0.766  1.00 28.27           C  
ANISOU  343  CA  PRO A  44     4064   2886   3792    463    288   -426       C  
ATOM    344  C   PRO A  44       5.218 -11.177   0.015  1.00 29.94           C  
ANISOU  344  C   PRO A  44     4203   3145   4027    525    390   -510       C  
ATOM    345  O   PRO A  44       6.180 -11.812   0.422  1.00 31.32           O  
ANISOU  345  O   PRO A  44     4314   3289   4298    654    416   -524       O  
ATOM    346  CB  PRO A  44       3.064 -12.466   0.288  1.00 28.15           C  
ANISOU  346  CB  PRO A  44     4195   2731   3769    433    300   -466       C  
ATOM    347  CG  PRO A  44       2.199 -11.950  -0.720  1.00 27.86           C  
ANISOU  347  CG  PRO A  44     4226   2731   3629    297    300   -501       C  
ATOM    348  CD  PRO A  44       1.865 -10.498  -0.320  1.00 26.73           C  
ANISOU  348  CD  PRO A  44     4001   2714   3440    235    237   -426       C  
ATOM    349  N   HIS A  45       5.260 -10.408  -1.073  1.00 30.32           N  
ANISOU  349  N   HIS A  45     4261   3268   3991    435    449   -564       N  
ATOM    350  CA  HIS A  45       6.448 -10.395  -1.919  1.00 32.53           C  
ANISOU  350  CA  HIS A  45     4486   3592   4282    475    573   -656       C  
ATOM    351  C   HIS A  45       7.222  -9.056  -1.981  1.00 31.48           C  
ANISOU  351  C   HIS A  45     4226   3603   4131    436    600   -642       C  
ATOM    352  O   HIS A  45       8.018  -8.871  -2.868  1.00 31.85           O  
ANISOU  352  O   HIS A  45     4242   3699   4159    427    716   -718       O  
ATOM    353  CB  HIS A  45       6.075 -10.928  -3.297  1.00 34.01           C  
ANISOU  353  CB  HIS A  45     4816   3724   4384    411    657   -755       C  
ATOM    354  CG  HIS A  45       5.600 -12.358  -3.260  1.00 38.07           C  
ANISOU  354  CG  HIS A  45     5444   4084   4939    461    652   -791       C  
ATOM    355  ND1 HIS A  45       4.340 -12.748  -3.666  1.00 37.32           N  
ANISOU  355  ND1 HIS A  45     5496   3916   4768    359    603   -796       N  
ATOM    356  CD2 HIS A  45       6.217 -13.487  -2.824  1.00 41.08           C  
ANISOU  356  CD2 HIS A  45     5811   4362   5434    601    685   -818       C  
ATOM    357  CE1 HIS A  45       4.213 -14.055  -3.507  1.00 38.44           C  
ANISOU  357  CE1 HIS A  45     5719   3913   4974    422    614   -832       C  
ATOM    358  NE2 HIS A  45       5.340 -14.529  -3.003  1.00 39.43           N  
ANISOU  358  NE2 HIS A  45     5756   4010   5214    575    665   -843       N  
ATOM    359  N   PHE A  46       7.007  -8.185  -0.985  1.00 30.01           N  
ANISOU  359  N   PHE A  46     3970   3476   3955    414    501   -549       N  
ATOM    360  CA  PHE A  46       7.708  -6.898  -0.825  1.00 29.52           C  
ANISOU  360  CA  PHE A  46     3789   3536   3889    373    508   -527       C  
ATOM    361  C   PHE A  46       8.838  -7.077   0.173  1.00 30.42           C  
ANISOU  361  C   PHE A  46     3744   3689   4126    489    488   -514       C  
ATOM    362  O   PHE A  46       8.725  -7.916   1.093  1.00 28.06           O  
ANISOU  362  O   PHE A  46     3443   3323   3894    588    417   -475       O  
ATOM    363  CB  PHE A  46       6.775  -5.824  -0.221  1.00 27.97           C  
ANISOU  363  CB  PHE A  46     3618   3373   3637    284    401   -438       C  
ATOM    364  CG  PHE A  46       5.949  -5.069  -1.227  1.00 29.09           C  
ANISOU  364  CG  PHE A  46     3866   3528   3659    157    412   -438       C  
ATOM    365  CD1 PHE A  46       5.373  -5.709  -2.310  1.00 30.15           C  
ANISOU  365  CD1 PHE A  46     4126   3606   3723    119    454   -490       C  
ATOM    366  CD2 PHE A  46       5.720  -3.714  -1.066  1.00 30.27           C  
ANISOU  366  CD2 PHE A  46     3998   3740   3765     76    371   -385       C  
ATOM    367  CE1 PHE A  46       4.616  -5.007  -3.220  1.00 31.45           C  
ANISOU  367  CE1 PHE A  46     4389   3788   3772      6    444   -481       C  
ATOM    368  CE2 PHE A  46       4.946  -3.005  -1.981  1.00 30.96           C  
ANISOU  368  CE2 PHE A  46     4187   3831   3744    -29    367   -373       C  
ATOM    369  CZ  PHE A  46       4.398  -3.655  -3.055  1.00 29.67           C  
ANISOU  369  CZ  PHE A  46     4142   3623   3508    -63    398   -417       C  
ATOM    370  N   ASP A  47       9.907  -6.287  -0.011  1.00 31.51           N  
ANISOU  370  N   ASP A  47     3750   3933   4288    471    547   -543       N  
ATOM    371  CA  ASP A  47      10.861  -6.013   1.066  1.00 33.72           C  
ANISOU  371  CA  ASP A  47     3859   4284   4668    542    489   -512       C  
ATOM    372  C   ASP A  47      10.160  -5.056   1.995  1.00 32.64           C  
ANISOU  372  C   ASP A  47     3744   4175   4483    469    367   -424       C  
ATOM    373  O   ASP A  47       9.885  -3.933   1.601  1.00 32.28           O  
ANISOU  373  O   ASP A  47     3724   4177   4365    348    382   -415       O  
ATOM    374  CB  ASP A  47      12.129  -5.306   0.562  1.00 35.17           C  
ANISOU  374  CB  ASP A  47     3890   4583   4888    510    588   -571       C  
ATOM    375  CG  ASP A  47      13.106  -6.254  -0.063  1.00 39.08           C  
ANISOU  375  CG  ASP A  47     4306   5072   5469    616    709   -663       C  
ATOM    376  OD1 ASP A  47      14.277  -5.869  -0.319  1.00 45.60           O  
ANISOU  376  OD1 ASP A  47     4969   5998   6360    618    794   -715       O  
ATOM    377  OD2 ASP A  47      12.697  -7.401  -0.299  1.00 39.70           O  
ANISOU  377  OD2 ASP A  47     4484   5042   5557    698    726   -688       O  
ATOM    378  N   LEU A  48       9.888  -5.487   3.223  1.00 33.19           N  
ANISOU  378  N   LEU A  48     3811   4211   4591    543    253   -359       N  
ATOM    379  CA  LEU A  48       9.128  -4.664   4.179  1.00 32.65           C  
ANISOU  379  CA  LEU A  48     3778   4159   4470    480    146   -282       C  
ATOM    380  C   LEU A  48       9.995  -4.095   5.303  1.00 34.11           C  
ANISOU  380  C   LEU A  48     3826   4431   4705    508     66   -253       C  
ATOM    381  O   LEU A  48       9.456  -3.502   6.259  1.00 33.18           O  
ANISOU  381  O   LEU A  48     3737   4324   4545    471    -26   -195       O  
ATOM    382  CB  LEU A  48       7.924  -5.480   4.733  1.00 31.83           C  
ANISOU  382  CB  LEU A  48     3804   3951   4339    510     80   -225       C  
ATOM    383  CG  LEU A  48       6.915  -5.884   3.631  1.00 31.16           C  
ANISOU  383  CG  LEU A  48     3856   3789   4194    452    140   -254       C  
ATOM    384  CD1 LEU A  48       5.747  -6.782   4.112  1.00 30.89           C  
ANISOU  384  CD1 LEU A  48     3940   3651   4148    468     87   -206       C  
ATOM    385  CD2 LEU A  48       6.353  -4.626   2.952  1.00 25.70           C  
ANISOU  385  CD2 LEU A  48     3201   3146   3416    321    157   -255       C  
ATOM    386  N   HIS A  49      11.327  -4.253   5.196  1.00 36.79           N  
ANISOU  386  N   HIS A  49     4012   4835   5132    569    100   -300       N  
ATOM    387  CA  HIS A  49      12.270  -3.650   6.188  1.00 38.40           C  
ANISOU  387  CA  HIS A  49     4062   5140   5387    582     16   -284       C  
ATOM    388  C   HIS A  49      12.198  -2.128   6.203  1.00 38.01           C  
ANISOU  388  C   HIS A  49     4002   5162   5278    433     11   -284       C  
ATOM    389  O   HIS A  49      11.943  -1.520   5.158  1.00 37.13           O  
ANISOU  389  O   HIS A  49     3941   5049   5117    332    108   -315       O  
ATOM    390  CB  HIS A  49      13.724  -4.101   5.945  1.00 40.19           C  
ANISOU  390  CB  HIS A  49     4102   5433   5736    674     62   -343       C  
ATOM    391  CG  HIS A  49      14.299  -3.675   4.622  1.00 42.95           C  
ANISOU  391  CG  HIS A  49     4391   5832   6095    601    219   -427       C  
ATOM    392  ND1 HIS A  49      15.082  -2.544   4.473  1.00 44.86           N  
ANISOU  392  ND1 HIS A  49     4506   6186   6350    495    252   -458       N  
ATOM    393  CD2 HIS A  49      14.246  -4.259   3.397  1.00 44.06           C  
ANISOU  393  CD2 HIS A  49     4587   5925   6230    613    358   -489       C  
ATOM    394  CE1 HIS A  49      15.469  -2.443   3.210  1.00 46.21           C  
ANISOU  394  CE1 HIS A  49     4659   6379   6521    444    411   -529       C  
ATOM    395  NE2 HIS A  49      14.972  -3.468   2.536  1.00 44.98           N  
ANISOU  395  NE2 HIS A  49     4614   6129   6347    516    477   -551       N  
ATOM    396  N   HIS A  50      12.392  -1.520   7.389  1.00 39.02           N  
ANISOU  396  N   HIS A  50     4079   5343   5402    417   -104   -246       N  
ATOM    397  CA  HIS A  50      12.531  -0.040   7.519  1.00 39.28           C  
ANISOU  397  CA  HIS A  50     4086   5442   5396    278   -114   -256       C  
ATOM    398  C   HIS A  50      13.478   0.481   6.461  1.00 39.01           C  
ANISOU  398  C   HIS A  50     3942   5474   5404    205      3   -324       C  
ATOM    399  O   HIS A  50      14.584  -0.022   6.321  1.00 40.90           O  
ANISOU  399  O   HIS A  50     4025   5775   5739    271     33   -366       O  
ATOM    400  CB  HIS A  50      13.085   0.441   8.876  1.00 40.58           C  
ANISOU  400  CB  HIS A  50     4162   5680   5575    277   -246   -236       C  
ATOM    401  CG  HIS A  50      13.077  -0.590   9.964  1.00 46.19           C  
ANISOU  401  CG  HIS A  50     4873   6373   6303    412   -361   -185       C  
ATOM    402  ND1 HIS A  50      12.003  -0.782  10.810  1.00 48.66           N  
ANISOU  402  ND1 HIS A  50     5333   6621   6536    429   -434   -120       N  
ATOM    403  CD2 HIS A  50      14.029  -1.481  10.350  1.00 51.62           C  
ANISOU  403  CD2 HIS A  50     5434   7098   7081    539   -416   -183       C  
ATOM    404  CE1 HIS A  50      12.296  -1.747  11.669  1.00 51.83           C  
ANISOU  404  CE1 HIS A  50     5713   7017   6965    551   -527    -76       C  
ATOM    405  NE2 HIS A  50      13.518  -2.184  11.414  1.00 53.04           N  
ANISOU  405  NE2 HIS A  50     5702   7228   7223    626   -527   -111       N  
ATOM    406  N   GLY A  51      13.053   1.490   5.718  1.00 37.84           N  
ANISOU  406  N   GLY A  51     3874   5313   5189     73     74   -333       N  
ATOM    407  CA  GLY A  51      13.873   2.041   4.670  1.00 37.80           C  
ANISOU  407  CA  GLY A  51     3792   5365   5206    -17    199   -389       C  
ATOM    408  C   GLY A  51      13.692   1.442   3.292  1.00 37.76           C  
ANISOU  408  C   GLY A  51     3853   5319   5175     -7    338   -422       C  
ATOM    409  O   GLY A  51      14.018   2.100   2.302  1.00 39.53           O  
ANISOU  409  O   GLY A  51     4081   5570   5369   -115    453   -454       O  
ATOM    410  N   SER A  52      13.173   0.222   3.181  1.00 36.40           N  
ANISOU  410  N   SER A  52     3748   5079   5005    109    334   -417       N  
ATOM    411  CA  SER A  52      13.189  -0.469   1.892  1.00 35.85           C  
ANISOU  411  CA  SER A  52     3727   4977   4917    126    468   -469       C  
ATOM    412  C   SER A  52      12.724   0.386   0.732  1.00 35.70           C  
ANISOU  412  C   SER A  52     3829   4946   4789    -15    561   -474       C  
ATOM    413  O   SER A  52      11.718   1.084   0.822  1.00 34.34           O  
ANISOU  413  O   SER A  52     3786   4728   4533    -86    500   -419       O  
ATOM    414  CB  SER A  52      12.363  -1.757   1.922  1.00 35.53           C  
ANISOU  414  CB  SER A  52     3797   4836   4867    239    438   -456       C  
ATOM    415  OG  SER A  52      11.009  -1.568   1.586  1.00 31.28           O  
ANISOU  415  OG  SER A  52     3441   4221   4222    177    413   -416       O  
ATOM    416  N   ALA A  53      13.479   0.312  -0.352  1.00 37.11           N  
ANISOU  416  N   ALA A  53     3966   5166   4969    -49    710   -540       N  
ATOM    417  CA  ALA A  53      13.173   0.984  -1.607  1.00 37.44           C  
ANISOU  417  CA  ALA A  53     4133   5199   4895   -180    817   -548       C  
ATOM    418  C   ALA A  53      11.734   0.767  -2.071  1.00 36.11           C  
ANISOU  418  C   ALA A  53     4178   4933   4611   -191    771   -507       C  
ATOM    419  O   ALA A  53      11.108   1.655  -2.646  1.00 37.30           O  
ANISOU  419  O   ALA A  53     4454   5062   4657   -302    773   -468       O  
ATOM    420  CB  ALA A  53      14.176   0.502  -2.712  1.00 39.11           C  
ANISOU  420  CB  ALA A  53     4276   5462   5124   -180   1003   -640       C  
ATOM    421  N   GLN A  54      11.202  -0.407  -1.804  1.00 35.38           N  
ANISOU  421  N   GLN A  54     4124   4778   4541    -77    721   -513       N  
ATOM    422  CA  GLN A  54       9.976  -0.855  -2.436  1.00 34.23           C  
ANISOU  422  CA  GLN A  54     4160   4549   4297    -88    700   -499       C  
ATOM    423  C   GLN A  54       8.749  -0.335  -1.688  1.00 32.71           C  
ANISOU  423  C   GLN A  54     4048   4309   4070   -110    556   -412       C  
ATOM    424  O   GLN A  54       7.694  -0.087  -2.305  1.00 32.24           O  
ANISOU  424  O   GLN A  54     4131   4205   3913   -170    529   -383       O  
ATOM    425  CB  GLN A  54      10.022  -2.368  -2.454  1.00 34.93           C  
ANISOU  425  CB  GLN A  54     4249   4584   4440     36    721   -551       C  
ATOM    426  CG  GLN A  54       8.909  -3.047  -3.182  1.00 35.49           C  
ANISOU  426  CG  GLN A  54     4493   4569   4421     24    713   -560       C  
ATOM    427  CD  GLN A  54       9.165  -4.537  -3.415  1.00 38.15           C  
ANISOU  427  CD  GLN A  54     4839   4844   4810    133    771   -634       C  
ATOM    428  OE1 GLN A  54      10.129  -5.160  -2.876  1.00 37.37           O  
ANISOU  428  OE1 GLN A  54     4608   4757   4833    247    800   -667       O  
ATOM    429  NE2 GLN A  54       8.307  -5.119  -4.251  1.00 38.02           N  
ANISOU  429  NE2 GLN A  54     4982   4758   4705    101    783   -663       N  
ATOM    430  N   VAL A  55       8.880  -0.198  -0.360  1.00 31.39           N  
ANISOU  430  N   VAL A  55     3788   4156   3982    -58    462   -374       N  
ATOM    431  CA  VAL A  55       7.853   0.416   0.461  1.00 29.67           C  
ANISOU  431  CA  VAL A  55     3628   3906   3740    -79    343   -301       C  
ATOM    432  C   VAL A  55       7.760   1.901   0.112  1.00 29.53           C  
ANISOU  432  C   VAL A  55     3647   3910   3661   -199    351   -272       C  
ATOM    433  O   VAL A  55       6.668   2.440   0.016  1.00 26.69           O  
ANISOU  433  O   VAL A  55     3394   3505   3240   -240    294   -223       O  
ATOM    434  CB  VAL A  55       8.081   0.163   1.976  1.00 30.01           C  
ANISOU  434  CB  VAL A  55     3575   3961   3865      3    249   -274       C  
ATOM    435  CG1 VAL A  55       7.334   1.200   2.868  1.00 27.61           C  
ANISOU  435  CG1 VAL A  55     3307   3650   3533    -44    154   -213       C  
ATOM    436  CG2 VAL A  55       7.661  -1.265   2.335  1.00 29.80           C  
ANISOU  436  CG2 VAL A  55     3576   3872   3872    112    217   -272       C  
ATOM    437  N   LYS A  56       8.916   2.523  -0.129  1.00 31.66           N  
ANISOU  437  N   LYS A  56     3828   4246   3954   -255    426   -303       N  
ATOM    438  CA  LYS A  56       9.010   3.899  -0.657  1.00 32.96           C  
ANISOU  438  CA  LYS A  56     4041   4422   4060   -385    461   -281       C  
ATOM    439  C   LYS A  56       8.306   4.102  -2.009  1.00 32.49           C  
ANISOU  439  C   LYS A  56     4141   4320   3882   -453    511   -265       C  
ATOM    440  O   LYS A  56       7.566   5.070  -2.184  1.00 31.92           O  
ANISOU  440  O   LYS A  56     4173   4207   3747   -519    464   -207       O  
ATOM    441  CB  LYS A  56      10.466   4.299  -0.851  1.00 34.90           C  
ANISOU  441  CB  LYS A  56     4155   4751   4356   -442    561   -329       C  
ATOM    442  CG  LYS A  56      11.118   4.999   0.338  1.00 38.79           C  
ANISOU  442  CG  LYS A  56     4520   5288   4929   -460    497   -324       C  
ATOM    443  CD  LYS A  56      12.601   5.335   0.004  1.00 44.41           C  
ANISOU  443  CD  LYS A  56     5082   6093   5699   -530    607   -381       C  
ATOM    444  CE  LYS A  56      13.476   5.511   1.235  1.00 47.31           C  
ANISOU  444  CE  LYS A  56     5271   6531   6174   -510    534   -400       C  
ATOM    445  NZ  LYS A  56      14.907   5.727   0.821  1.00 51.52           N  
ANISOU  445  NZ  LYS A  56     5635   7164   6777   -577    648   -462       N  
ATOM    446  N   ALA A  57       8.577   3.217  -2.968  1.00 32.94           N  
ANISOU  446  N   ALA A  57     4222   4388   3906   -437    604   -318       N  
ATOM    447  CA  ALA A  57       7.949   3.296  -4.311  1.00 32.93           C  
ANISOU  447  CA  ALA A  57     4385   4354   3772   -504    647   -310       C  
ATOM    448  C   ALA A  57       6.428   3.161  -4.204  1.00 31.66           C  
ANISOU  448  C   ALA A  57     4342   4123   3564   -477    519   -254       C  
ATOM    449  O   ALA A  57       5.688   3.909  -4.857  1.00 32.00           O  
ANISOU  449  O   ALA A  57     4511   4136   3511   -547    484   -201       O  
ATOM    450  CB  ALA A  57       8.519   2.232  -5.268  1.00 33.51           C  
ANISOU  450  CB  ALA A  57     4465   4449   3819   -482    773   -394       C  
ATOM    451  N   HIS A  58       5.969   2.222  -3.365  1.00 30.25           N  
ANISOU  451  N   HIS A  58     4119   3918   3456   -377    447   -261       N  
ATOM    452  CA  HIS A  58       4.555   2.026  -3.148  1.00 28.50           C  
ANISOU  452  CA  HIS A  58     3980   3639   3211   -354    333   -214       C  
ATOM    453  C   HIS A  58       3.912   3.189  -2.405  1.00 27.84           C  
ANISOU  453  C   HIS A  58     3900   3539   3139   -375    240   -141       C  
ATOM    454  O   HIS A  58       2.782   3.563  -2.693  1.00 27.00           O  
ANISOU  454  O   HIS A  58     3883   3394   2982   -395    168    -93       O  
ATOM    455  CB  HIS A  58       4.306   0.736  -2.395  1.00 28.22           C  
ANISOU  455  CB  HIS A  58     3896   3575   3250   -254    296   -238       C  
ATOM    456  CG  HIS A  58       2.860   0.381  -2.309  1.00 27.19           C  
ANISOU  456  CG  HIS A  58     3844   3390   3095   -245    200   -202       C  
ATOM    457  ND1 HIS A  58       2.135  -0.005  -3.415  1.00 27.73           N  
ANISOU  457  ND1 HIS A  58     4027   3433   3078   -287    194   -217       N  
ATOM    458  CD2 HIS A  58       1.984   0.428  -1.280  1.00 25.65           C  
ANISOU  458  CD2 HIS A  58     3628   3170   2947   -210    106   -153       C  
ATOM    459  CE1 HIS A  58       0.879  -0.201  -3.067  1.00 25.19           C  
ANISOU  459  CE1 HIS A  58     3735   3074   2763   -278     95   -178       C  
ATOM    460  NE2 HIS A  58       0.757   0.052  -1.776  1.00 25.52           N  
ANISOU  460  NE2 HIS A  58     3695   3115   2887   -230     49   -140       N  
ATOM    461  N   GLY A  59       4.628   3.735  -1.436  1.00 28.57           N  
ANISOU  461  N   GLY A  59     3892   3660   3304   -365    240   -137       N  
ATOM    462  CA  GLY A  59       4.181   4.902  -0.670  1.00 29.03           C  
ANISOU  462  CA  GLY A  59     3955   3698   3377   -387    168    -84       C  
ATOM    463  C   GLY A  59       3.881   6.079  -1.571  1.00 30.19           C  
ANISOU  463  C   GLY A  59     4209   3818   3445   -477    176    -41       C  
ATOM    464  O   GLY A  59       2.860   6.764  -1.420  1.00 29.55           O  
ANISOU  464  O   GLY A  59     4194   3687   3348   -476     97     14       O  
ATOM    465  N   LYS A  60       4.779   6.301  -2.523  1.00 32.44           N  
ANISOU  465  N   LYS A  60     4512   4132   3681   -550    275    -64       N  
ATOM    466  CA  LYS A  60       4.684   7.418  -3.456  1.00 33.55           C  
ANISOU  466  CA  LYS A  60     4769   4245   3734   -648    298    -17       C  
ATOM    467  C   LYS A  60       3.358   7.369  -4.198  1.00 33.31           C  
ANISOU  467  C   LYS A  60     4873   4164   3619   -639    220     34       C  
ATOM    468  O   LYS A  60       2.665   8.365  -4.316  1.00 33.68           O  
ANISOU  468  O   LYS A  60     5004   4158   3635   -663    156    102       O  
ATOM    469  CB  LYS A  60       5.859   7.363  -4.435  1.00 35.66           C  
ANISOU  469  CB  LYS A  60     5035   4563   3952   -729    439    -59       C  
ATOM    470  CG  LYS A  60       5.689   8.172  -5.740  1.00 37.55           C  
ANISOU  470  CG  LYS A  60     5435   4773   4058   -835    480     -9       C  
ATOM    471  CD  LYS A  60       6.772   7.781  -6.765  1.00 41.23           C  
ANISOU  471  CD  LYS A  60     5902   5302   4463   -904    641    -68       C  
ATOM    472  CE  LYS A  60       6.780   8.716  -8.004  1.00 43.91           C  
ANISOU  472  CE  LYS A  60     6410   5615   4657  -1031    698    -10       C  
ATOM    473  NZ  LYS A  60       7.114  10.148  -7.625  1.00 44.14           N  
ANISOU  473  NZ  LYS A  60     6449   5607   4715  -1115    697     49       N  
ATOM    474  N   LYS A  61       3.007   6.186  -4.693  1.00 33.45           N  
ANISOU  474  N   LYS A  61     4909   4196   3605   -601    221     -2       N  
ATOM    475  CA  LYS A  61       1.738   5.968  -5.387  1.00 32.50           C  
ANISOU  475  CA  LYS A  61     4899   4041   3409   -595    134     35       C  
ATOM    476  C   LYS A  61       0.503   6.099  -4.477  1.00 30.29           C  
ANISOU  476  C   LYS A  61     4590   3722   3197   -526      5     79       C  
ATOM    477  O   LYS A  61      -0.507   6.595  -4.920  1.00 30.54           O  
ANISOU  477  O   LYS A  61     4700   3719   3182   -533    -81    137       O  
ATOM    478  CB  LYS A  61       1.747   4.597  -6.054  1.00 33.58           C  
ANISOU  478  CB  LYS A  61     5057   4198   3502   -581    173    -32       C  
ATOM    479  CG  LYS A  61       2.777   4.487  -7.194  1.00 36.07           C  
ANISOU  479  CG  LYS A  61     5431   4551   3724   -654    308    -79       C  
ATOM    480  CD  LYS A  61       2.513   3.260  -8.094  1.00 37.57           C  
ANISOU  480  CD  LYS A  61     5694   4745   3837   -651    332   -143       C  
ATOM    481  CE  LYS A  61       2.740   1.924  -7.371  1.00 38.80           C  
ANISOU  481  CE  LYS A  61     5745   4898   4100   -561    354   -218       C  
ATOM    482  NZ  LYS A  61       2.934   0.739  -8.319  1.00 40.66           N  
ANISOU  482  NZ  LYS A  61     6050   5132   4266   -566    431   -308       N  
ATOM    483  N   VAL A  62       0.579   5.661  -3.220  1.00 28.13           N  
ANISOU  483  N   VAL A  62     4202   3456   3030   -459     -6     55       N  
ATOM    484  CA  VAL A  62      -0.570   5.761  -2.304  1.00 26.06           C  
ANISOU  484  CA  VAL A  62     3908   3163   2831   -398   -106     90       C  
ATOM    485  C   VAL A  62      -0.896   7.234  -2.033  1.00 25.12           C  
ANISOU  485  C   VAL A  62     3819   3004   2720   -411   -148    149       C  
ATOM    486  O   VAL A  62      -2.046   7.660  -2.138  1.00 23.58           O  
ANISOU  486  O   VAL A  62     3664   2774   2523   -388   -233    198       O  
ATOM    487  CB  VAL A  62      -0.304   4.993  -0.974  1.00 25.54           C  
ANISOU  487  CB  VAL A  62     3730   3115   2860   -331    -96     54       C  
ATOM    488  CG1 VAL A  62      -1.316   5.326   0.087  1.00 23.83           C  
ANISOU  488  CG1 VAL A  62     3479   2872   2702   -282   -171     88       C  
ATOM    489  CG2 VAL A  62      -0.271   3.456  -1.229  1.00 24.27           C  
ANISOU  489  CG2 VAL A  62     3556   2964   2700   -303    -72      5       C  
ATOM    490  N   ALA A  63       0.144   7.993  -1.698  1.00 24.50           N  
ANISOU  490  N   ALA A  63     3719   2931   2659   -449    -88    140       N  
ATOM    491  CA  ALA A  63       0.051   9.439  -1.514  1.00 24.70           C  
ANISOU  491  CA  ALA A  63     3793   2903   2689   -477   -110    188       C  
ATOM    492  C   ALA A  63      -0.462  10.147  -2.782  1.00 25.69           C  
ANISOU  492  C   ALA A  63     4054   2984   2725   -523   -141    253       C  
ATOM    493  O   ALA A  63      -1.267  11.075  -2.673  1.00 24.97           O  
ANISOU  493  O   ALA A  63     4014   2828   2646   -499   -212    310       O  
ATOM    494  CB  ALA A  63       1.421  10.017  -1.096  1.00 24.00           C  
ANISOU  494  CB  ALA A  63     3659   2833   2626   -537    -30    156       C  
ATOM    495  N   ALA A  64      -0.003   9.687  -3.959  1.00 26.34           N  
ANISOU  495  N   ALA A  64     4198   3098   2714   -582    -89    244       N  
ATOM    496  CA  ALA A  64      -0.403  10.267  -5.243  1.00 27.96           C  
ANISOU  496  CA  ALA A  64     4550   3269   2806   -635   -118    309       C  
ATOM    497  C   ALA A  64      -1.896  10.070  -5.480  1.00 27.23           C  
ANISOU  497  C   ALA A  64     4491   3152   2702   -571   -251    354       C  
ATOM    498  O   ALA A  64      -2.580  10.982  -5.963  1.00 27.33           O  
ANISOU  498  O   ALA A  64     4598   3108   2677   -571   -329    433       O  
ATOM    499  CB  ALA A  64       0.414   9.675  -6.396  1.00 29.20           C  
ANISOU  499  CB  ALA A  64     4765   3477   2853   -714    -20    274       C  
ATOM    500  N   ALA A  65      -2.402   8.903  -5.082  1.00 25.35           N  
ANISOU  500  N   ALA A  65     4170   2954   2510   -516   -280    306       N  
ATOM    501  CA  ALA A  65      -3.834   8.619  -5.169  1.00 25.29           C  
ANISOU  501  CA  ALA A  65     4159   2936   2515   -461   -405    337       C  
ATOM    502  C   ALA A  65      -4.625   9.433  -4.149  1.00 24.51           C  
ANISOU  502  C   ALA A  65     3999   2790   2522   -386   -471    376       C  
ATOM    503  O   ALA A  65      -5.662   9.988  -4.478  1.00 26.14           O  
ANISOU  503  O   ALA A  65     4241   2963   2728   -352   -573    437       O  
ATOM    504  CB  ALA A  65      -4.128   7.109  -5.035  1.00 24.65           C  
ANISOU  504  CB  ALA A  65     4010   2901   2454   -440   -405    271       C  
ATOM    505  N   LEU A  66      -4.135   9.574  -2.929  1.00 23.69           N  
ANISOU  505  N   LEU A  66     3810   2683   2507   -358   -414    340       N  
ATOM    506  CA  LEU A  66      -4.763  10.544  -2.010  1.00 23.10           C  
ANISOU  506  CA  LEU A  66     3704   2555   2518   -296   -457    370       C  
ATOM    507  C   LEU A  66      -4.758  11.974  -2.607  1.00 24.81           C  
ANISOU  507  C   LEU A  66     4035   2694   2698   -318   -484    441       C  
ATOM    508  O   LEU A  66      -5.749  12.725  -2.495  1.00 26.11           O  
ANISOU  508  O   LEU A  66     4215   2800   2907   -253   -565    491       O  
ATOM    509  CB  LEU A  66      -4.128  10.489  -0.618  1.00 21.17           C  
ANISOU  509  CB  LEU A  66     3371   2323   2351   -276   -390    315       C  
ATOM    510  CG  LEU A  66      -4.366   9.217   0.196  1.00 19.02           C  
ANISOU  510  CG  LEU A  66     2994   2106   2128   -235   -380    265       C  
ATOM    511  CD1 LEU A  66      -3.606   9.228   1.510  1.00 16.62           C  
ANISOU  511  CD1 LEU A  66     2623   1816   1876   -223   -323    220       C  
ATOM    512  CD2 LEU A  66      -5.833   8.984   0.468  1.00 16.09           C  
ANISOU  512  CD2 LEU A  66     2579   1728   1808   -170   -455    286       C  
ATOM    513  N   VAL A  67      -3.691  12.342  -3.308  1.00 25.82           N  
ANISOU  513  N   VAL A  67     4248   2814   2746   -407   -417    449       N  
ATOM    514  CA  VAL A  67      -3.619  13.719  -3.862  1.00 27.22           C  
ANISOU  514  CA  VAL A  67     4553   2903   2885   -441   -434    524       C  
ATOM    515  C   VAL A  67      -4.598  13.933  -5.003  1.00 29.33           C  
ANISOU  515  C   VAL A  67     4924   3141   3078   -422   -544    608       C  
ATOM    516  O   VAL A  67      -5.207  15.004  -5.133  1.00 30.78           O  
ANISOU  516  O   VAL A  67     5180   3236   3278   -381   -616    682       O  
ATOM    517  CB  VAL A  67      -2.189  14.087  -4.281  1.00 28.12           C  
ANISOU  517  CB  VAL A  67     4728   3019   2935   -558   -320    512       C  
ATOM    518  CG1 VAL A  67      -2.165  15.293  -5.299  1.00 27.10           C  
ANISOU  518  CG1 VAL A  67     4775   2800   2720   -619   -337    608       C  
ATOM    519  CG2 VAL A  67      -1.373  14.347  -3.001  1.00 23.65           C  
ANISOU  519  CG2 VAL A  67     4067   2456   2464   -567   -248    447       C  
ATOM    520  N   GLU A  68      -4.793  12.904  -5.810  1.00 30.69           N  
ANISOU  520  N   GLU A  68     5104   3386   3172   -445   -566    594       N  
ATOM    521  CA  GLU A  68      -5.797  12.970  -6.867  1.00 32.04           C  
ANISOU  521  CA  GLU A  68     5362   3546   3266   -428   -693    667       C  
ATOM    522  C   GLU A  68      -7.199  13.072  -6.240  1.00 31.98           C  
ANISOU  522  C   GLU A  68     5257   3519   3373   -308   -815    689       C  
ATOM    523  O   GLU A  68      -8.019  13.895  -6.639  1.00 32.31           O  
ANISOU  523  O   GLU A  68     5357   3501   3416   -257   -926    772       O  
ATOM    524  CB  GLU A  68      -5.665  11.761  -7.785  1.00 32.15           C  
ANISOU  524  CB  GLU A  68     5403   3645   3169   -487   -684    627       C  
ATOM    525  CG  GLU A  68      -6.561  11.791  -8.989  1.00 37.14           C  
ANISOU  525  CG  GLU A  68     6143   4278   3691   -493   -818    696       C  
ATOM    526  CD  GLU A  68      -5.973  12.599 -10.149  1.00 42.71           C  
ANISOU  526  CD  GLU A  68     7044   4945   4240   -579   -798    772       C  
ATOM    527  OE1 GLU A  68      -6.372  12.338 -11.296  1.00 46.31           O  
ANISOU  527  OE1 GLU A  68     7611   5427   4556   -618   -877    808       O  
ATOM    528  OE2 GLU A  68      -5.092  13.460  -9.918  1.00 45.30           O  
ANISOU  528  OE2 GLU A  68     7419   5218   4575   -620   -701    791       O  
ATOM    529  N   ALA A  69      -7.467  12.273  -5.214  1.00 31.37           N  
ANISOU  529  N   ALA A  69     5030   3490   3398   -261   -791    616       N  
ATOM    530  CA  ALA A  69      -8.803  12.255  -4.689  1.00 31.71           C  
ANISOU  530  CA  ALA A  69     4971   3531   3546   -161   -889    629       C  
ATOM    531  C   ALA A  69      -9.121  13.612  -4.082  1.00 32.53           C  
ANISOU  531  C   ALA A  69     5084   3539   3736    -85   -908    675       C  
ATOM    532  O   ALA A  69     -10.239  14.098  -4.253  1.00 34.85           O  
ANISOU  532  O   ALA A  69     5362   3801   4080     -2  -1021    730       O  
ATOM    533  CB  ALA A  69      -8.996  11.139  -3.708  1.00 30.77           C  
ANISOU  533  CB  ALA A  69     4705   3476   3508   -140   -844    547       C  
ATOM    534  N   ALA A  70      -8.142  14.233  -3.429  1.00 31.99           N  
ANISOU  534  N   ALA A  70     5045   3424   3687   -113   -804    649       N  
ATOM    535  CA  ALA A  70      -8.289  15.587  -2.876  1.00 32.97           C  
ANISOU  535  CA  ALA A  70     5206   3438   3883    -56   -807    682       C  
ATOM    536  C   ALA A  70      -8.553  16.627  -3.969  1.00 34.84           C  
ANISOU  536  C   ALA A  70     5595   3583   4060    -52   -892    791       C  
ATOM    537  O   ALA A  70      -9.418  17.486  -3.814  1.00 33.94           O  
ANISOU  537  O   ALA A  70     5489   3386   4022     49   -969    841       O  
ATOM    538  CB  ALA A  70      -7.033  16.001  -2.063  1.00 32.29           C  
ANISOU  538  CB  ALA A  70     5135   3323   3809   -118   -680    627       C  
ATOM    539  N   ASN A  71      -7.800  16.538  -5.062  1.00 36.14           N  
ANISOU  539  N   ASN A  71     5884   3761   4087   -158   -874    826       N  
ATOM    540  CA  ASN A  71      -8.046  17.421  -6.213  1.00 38.87           C  
ANISOU  540  CA  ASN A  71     6397   4026   4346   -166   -961    942       C  
ATOM    541  C   ASN A  71      -9.446  17.326  -6.766  1.00 40.40           C  
ANISOU  541  C   ASN A  71     6570   4229   4552    -67  -1131   1008       C  
ATOM    542  O   ASN A  71     -10.066  18.365  -7.035  1.00 42.26           O  
ANISOU  542  O   ASN A  71     6881   4361   4814      9  -1227   1100       O  
ATOM    543  CB  ASN A  71      -7.034  17.197  -7.332  1.00 39.12           C  
ANISOU  543  CB  ASN A  71     6566   4089   4208   -307   -900    964       C  
ATOM    544  CG  ASN A  71      -5.711  17.751  -6.972  1.00 39.81           C  
ANISOU  544  CG  ASN A  71     6702   4134   4289   -403   -753    934       C  
ATOM    545  OD1 ASN A  71      -5.621  18.684  -6.161  1.00 41.45           O  
ANISOU  545  OD1 ASN A  71     6909   4247   4593   -370   -728    934       O  
ATOM    546  ND2 ASN A  71      -4.658  17.169  -7.516  1.00 42.56           N  
ANISOU  546  ND2 ASN A  71     7084   4555   4533   -525   -648    896       N  
ATOM    547  N   HIS A  72      -9.946  16.096  -6.886  1.00 40.09           N  
ANISOU  547  N   HIS A  72     6421   4308   4504    -66  -1171    959       N  
ATOM    548  CA  HIS A  72     -11.276  15.838  -7.438  1.00 41.15           C  
ANISOU  548  CA  HIS A  72     6509   4476   4649     10  -1341   1008       C  
ATOM    549  C   HIS A  72     -12.241  15.459  -6.363  1.00 40.75           C  
ANISOU  549  C   HIS A  72     6254   4461   4767    115  -1363    951       C  
ATOM    550  O   HIS A  72     -12.984  14.490  -6.489  1.00 40.83           O  
ANISOU  550  O   HIS A  72     6156   4565   4793    121  -1430    921       O  
ATOM    551  CB  HIS A  72     -11.155  14.756  -8.479  1.00 41.21           C  
ANISOU  551  CB  HIS A  72     6562   4585   4511    -87  -1375    994       C  
ATOM    552  CG  HIS A  72     -10.215  15.148  -9.552  1.00 43.39           C  
ANISOU  552  CG  HIS A  72     7045   4830   4611   -194  -1336   1048       C  
ATOM    553  ND1 HIS A  72     -10.619  15.876 -10.646  1.00 46.18           N  
ANISOU  553  ND1 HIS A  72     7556   5133   4858   -190  -1465   1168       N  
ATOM    554  CD2 HIS A  72      -8.871  15.036  -9.639  1.00 45.21           C  
ANISOU  554  CD2 HIS A  72     7352   5066   4760   -306  -1177   1006       C  
ATOM    555  CE1 HIS A  72      -9.564  16.146 -11.395  1.00 50.00           C  
ANISOU  555  CE1 HIS A  72     8217   5594   5188   -307  -1377   1196       C  
ATOM    556  NE2 HIS A  72      -8.492  15.641 -10.810  1.00 48.65           N  
ANISOU  556  NE2 HIS A  72     7990   5460   5035   -380  -1197   1094       N  
ATOM    557  N   ILE A  73     -12.246  16.260  -5.305  1.00 41.06           N  
ANISOU  557  N   ILE A  73     6249   4423   4930    191  -1302    935       N  
ATOM    558  CA  ILE A  73     -12.946  15.912  -4.071  1.00 40.62           C  
ANISOU  558  CA  ILE A  73     6004   4401   5028    276  -1271    862       C  
ATOM    559  C   ILE A  73     -14.469  15.667  -4.328  1.00 42.16           C  
ANISOU  559  C   ILE A  73     6073   4642   5304    374  -1421    894       C  
ATOM    560  O   ILE A  73     -15.108  14.872  -3.631  1.00 40.46           O  
ANISOU  560  O   ILE A  73     5688   4506   5180    400  -1404    829       O  
ATOM    561  CB  ILE A  73     -12.596  16.949  -2.922  1.00 40.00           C  
ANISOU  561  CB  ILE A  73     5931   4219   5048    332  -1170    834       C  
ATOM    562  CG1 ILE A  73     -12.656  16.272  -1.541  1.00 39.24           C  
ANISOU  562  CG1 ILE A  73     5678   4184   5045    350  -1065    727       C  
ATOM    563  CG2 ILE A  73     -13.450  18.271  -3.021  1.00 41.38           C  
ANISOU  563  CG2 ILE A  73     6142   4270   5311    466  -1264    912       C  
ATOM    564  CD1 ILE A  73     -11.869  17.018  -0.427  1.00 36.98           C  
ANISOU  564  CD1 ILE A  73     5427   3822   4801    349   -940    673       C  
ATOM    565  N   ASP A  74     -15.012  16.288  -5.381  1.00 44.78           N  
ANISOU  565  N   ASP A  74     6488   4932   5593    415  -1572    997       N  
ATOM    566  CA  ASP A  74     -16.423  16.145  -5.718  1.00 47.09           C  
ANISOU  566  CA  ASP A  74     6657   5273   5964    509  -1736   1036       C  
ATOM    567  C   ASP A  74     -16.720  14.883  -6.515  1.00 47.94           C  
ANISOU  567  C   ASP A  74     6727   5509   5980    418  -1818   1018       C  
ATOM    568  O   ASP A  74     -17.880  14.501  -6.637  1.00 48.74           O  
ANISOU  568  O   ASP A  74     6684   5678   6158    471  -1941   1023       O  
ATOM    569  CB  ASP A  74     -16.918  17.354  -6.516  1.00 49.71           C  
ANISOU  569  CB  ASP A  74     7096   5502   6289    604  -1886   1163       C  
ATOM    570  CG  ASP A  74     -16.812  18.654  -5.740  1.00 51.70           C  
ANISOU  570  CG  ASP A  74     7384   5608   6654    712  -1821   1180       C  
ATOM    571  OD1 ASP A  74     -17.132  18.668  -4.518  1.00 54.56           O  
ANISOU  571  OD1 ASP A  74     7598   5969   7164    785  -1726   1099       O  
ATOM    572  OD2 ASP A  74     -16.416  19.658  -6.357  1.00 52.55           O  
ANISOU  572  OD2 ASP A  74     7678   5594   6693    720  -1860   1273       O  
ATOM    573  N   ASP A  75     -15.697  14.262  -7.104  1.00 48.16           N  
ANISOU  573  N   ASP A  75     6883   5568   5846    279  -1755    995       N  
ATOM    574  CA  ASP A  75     -15.882  12.972  -7.786  1.00 48.68           C  
ANISOU  574  CA  ASP A  75     6926   5748   5822    182  -1809    955       C  
ATOM    575  C   ASP A  75     -14.684  12.040  -7.580  1.00 46.96           C  
ANISOU  575  C   ASP A  75     6756   5567   5522     60  -1642    865       C  
ATOM    576  O   ASP A  75     -14.045  11.558  -8.531  1.00 46.77           O  
ANISOU  576  O   ASP A  75     6864   5571   5337    -45  -1637    862       O  
ATOM    577  CB  ASP A  75     -16.201  13.167  -9.281  1.00 51.11           C  
ANISOU  577  CB  ASP A  75     7371   6066   5981    152  -1985   1047       C  
ATOM    578  CG  ASP A  75     -16.787  11.896  -9.933  1.00 53.02           C  
ANISOU  578  CG  ASP A  75     7557   6427   6162     73  -2084   1002       C  
ATOM    579  OD1 ASP A  75     -17.079  10.905  -9.215  1.00 55.01           O  
ANISOU  579  OD1 ASP A  75     7649   6744   6507     52  -2026    908       O  
ATOM    580  OD2 ASP A  75     -16.954  11.886 -11.169  1.00 56.52           O  
ANISOU  580  OD2 ASP A  75     8126   6894   6455     24  -2222   1060       O  
ATOM    581  N   ILE A  76     -14.424  11.769  -6.307  1.00 46.08           N  
ANISOU  581  N   ILE A  76     6530   5455   5522     81  -1507    790       N  
ATOM    582  CA  ILE A  76     -13.397  10.807  -5.868  1.00 44.80           C  
ANISOU  582  CA  ILE A  76     6371   5330   5321     -8  -1355    700       C  
ATOM    583  C   ILE A  76     -13.591   9.460  -6.513  1.00 44.72           C  
ANISOU  583  C   ILE A  76     6350   5404   5239    -92  -1392    652       C  
ATOM    584  O   ILE A  76     -12.626   8.825  -6.879  1.00 44.44           O  
ANISOU  584  O   ILE A  76     6401   5385   5101   -179  -1308    608       O  
ATOM    585  CB  ILE A  76     -13.433  10.590  -4.338  1.00 43.41           C  
ANISOU  585  CB  ILE A  76     6049   5156   5287     42  -1244    634       C  
ATOM    586  CG1 ILE A  76     -13.049  11.860  -3.612  1.00 43.10           C  
ANISOU  586  CG1 ILE A  76     6039   5029   5307    109  -1182    657       C  
ATOM    587  CG2 ILE A  76     -12.482   9.444  -3.916  1.00 42.88           C  
ANISOU  587  CG2 ILE A  76     5977   5131   5183    -40  -1114    549       C  
ATOM    588  CD1 ILE A  76     -13.522  11.906  -2.171  1.00 43.93           C  
ANISOU  588  CD1 ILE A  76     6000   5132   5558    185  -1115    608       C  
ATOM    589  N   SER A  77     -14.840   9.026  -6.633  1.00 46.47           N  
ANISOU  589  N   SER A  77     6459   5676   5523    -67  -1515    655       N  
ATOM    590  CA  SER A  77     -15.196   7.734  -7.289  1.00 47.88           C  
ANISOU  590  CA  SER A  77     6625   5929   5639   -157  -1572    605       C  
ATOM    591  C   SER A  77     -14.591   7.504  -8.691  1.00 48.55           C  
ANISOU  591  C   SER A  77     6898   6024   5523   -253  -1612    616       C  
ATOM    592  O   SER A  77     -14.054   6.432  -8.985  1.00 48.34           O  
ANISOU  592  O   SER A  77     6921   6028   5420   -344  -1546    542       O  
ATOM    593  CB  SER A  77     -16.712   7.622  -7.384  1.00 49.14           C  
ANISOU  593  CB  SER A  77     6639   6138   5892   -115  -1733    627       C  
ATOM    594  OG  SER A  77     -17.300   8.690  -6.655  1.00 51.95           O  
ANISOU  594  OG  SER A  77     6894   6456   6387     12  -1752    678       O  
ATOM    595  N   THR A  78     -14.668   8.512  -9.549  1.00 50.51           N  
ANISOU  595  N   THR A  78     7264   6242   5685   -232  -1713    709       N  
ATOM    596  CA  THR A  78     -14.088   8.404 -10.885  1.00 51.88           C  
ANISOU  596  CA  THR A  78     7637   6426   5650   -327  -1742    727       C  
ATOM    597  C   THR A  78     -12.585   8.637 -10.845  1.00 50.80           C  
ANISOU  597  C   THR A  78     7625   6245   5433   -376  -1558    707       C  
ATOM    598  O   THR A  78     -11.843   8.008 -11.583  1.00 50.95           O  
ANISOU  598  O   THR A  78     7761   6290   5309   -473  -1493    660       O  
ATOM    599  CB  THR A  78     -14.728   9.381 -11.874  1.00 54.21           C  
ANISOU  599  CB  THR A  78     8030   6703   5863   -294  -1926    846       C  
ATOM    600  OG1 THR A  78     -14.283  10.719 -11.592  1.00 55.51           O  
ANISOU  600  OG1 THR A  78     8260   6777   6056   -224  -1882    928       O  
ATOM    601  CG2 THR A  78     -16.253   9.296 -11.797  1.00 55.54           C  
ANISOU  601  CG2 THR A  78     8037   6919   6148   -224  -2117    872       C  
ATOM    602  N   ALA A  79     -12.154   9.553  -9.984  1.00 50.49           N  
ANISOU  602  N   ALA A  79     7553   6141   5488   -310  -1473    736       N  
ATOM    603  CA  ALA A  79     -10.724   9.797  -9.703  1.00 49.89           C  
ANISOU  603  CA  ALA A  79     7551   6030   5376   -355  -1292    707       C  
ATOM    604  C   ALA A  79      -9.933   8.509  -9.469  1.00 49.32           C  
ANISOU  604  C   ALA A  79     7445   6008   5287   -422  -1158    593       C  
ATOM    605  O   ALA A  79      -8.909   8.268 -10.133  1.00 49.14           O  
ANISOU  605  O   ALA A  79     7538   5995   5138   -503  -1061    565       O  
ATOM    606  CB  ALA A  79     -10.584  10.714  -8.476  1.00 48.52           C  
ANISOU  606  CB  ALA A  79     7294   5791   5351   -270  -1229    724       C  
ATOM    607  N   LEU A  80     -10.434   7.700  -8.525  1.00 48.85           N  
ANISOU  607  N   LEU A  80     7227   5975   5356   -383  -1149    532       N  
ATOM    608  CA  LEU A  80      -9.797   6.445  -8.087  1.00 48.47           C  
ANISOU  608  CA  LEU A  80     7131   5959   5325   -423  -1030    430       C  
ATOM    609  C   LEU A  80     -10.385   5.180  -8.737  1.00 50.23           C  
ANISOU  609  C   LEU A  80     7359   6230   5497   -480  -1093    374       C  
ATOM    610  O   LEU A  80     -10.577   4.146  -8.068  1.00 50.01           O  
ANISOU  610  O   LEU A  80     7234   6216   5551   -479  -1056    307       O  
ATOM    611  CB  LEU A  80      -9.882   6.335  -6.557  1.00 47.18           C  
ANISOU  611  CB  LEU A  80     6813   5784   5328   -353   -966    401       C  
ATOM    612  CG  LEU A  80      -8.793   7.042  -5.761  1.00 44.66           C  
ANISOU  612  CG  LEU A  80     6493   5430   5048   -331   -843    400       C  
ATOM    613  CD1 LEU A  80      -8.410   8.375  -6.373  1.00 45.77           C  
ANISOU  613  CD1 LEU A  80     6747   5524   5118   -340   -857    473       C  
ATOM    614  CD2 LEU A  80      -9.239   7.199  -4.336  1.00 42.92           C  
ANISOU  614  CD2 LEU A  80     6136   5197   4975   -254   -826    392       C  
ATOM    615  N   SER A  81     -10.647   5.259 -10.047  1.00 52.74           N  
ANISOU  615  N   SER A  81     7805   6566   5668   -537  -1189    402       N  
ATOM    616  CA  SER A  81     -11.203   4.128 -10.802  1.00 53.79           C  
ANISOU  616  CA  SER A  81     7968   6743   5729   -608  -1263    344       C  
ATOM    617  C   SER A  81     -10.107   3.102 -11.030  1.00 53.43           C  
ANISOU  617  C   SER A  81     7994   6697   5611   -673  -1111    243       C  
ATOM    618  O   SER A  81      -8.953   3.450 -11.303  1.00 53.90           O  
ANISOU  618  O   SER A  81     8144   6741   5593   -692   -990    238       O  
ATOM    619  CB  SER A  81     -11.764   4.570 -12.163  1.00 56.00           C  
ANISOU  619  CB  SER A  81     8380   7046   5851   -653  -1420    405       C  
ATOM    620  OG  SER A  81     -12.656   5.655 -12.025  1.00 57.17           O  
ANISOU  620  OG  SER A  81     8474   7183   6065   -576  -1560    510       O  
ATOM    621  N   LYS A  82     -10.474   1.831 -10.917  1.00 53.16           N  
ANISOU  621  N   LYS A  82     7915   6674   5609   -707  -1114    160       N  
ATOM    622  CA  LYS A  82      -9.539   0.719 -11.073  1.00 52.30           C  
ANISOU  622  CA  LYS A  82     7865   6551   5455   -753   -975     55       C  
ATOM    623  C   LYS A  82      -8.355   0.856 -10.122  1.00 50.24           C  
ANISOU  623  C   LYS A  82     7548   6263   5280   -695   -806     39       C  
ATOM    624  O   LYS A  82      -7.229   0.405 -10.410  1.00 50.84           O  
ANISOU  624  O   LYS A  82     7690   6330   5298   -717   -670    -25       O  
ATOM    625  CB  LYS A  82      -9.145   0.527 -12.547  1.00 54.04           C  
ANISOU  625  CB  LYS A  82     8276   6790   5468   -842   -974     19       C  
ATOM    626  CG  LYS A  82     -10.108  -0.385 -13.381  1.00 55.87           C  
ANISOU  626  CG  LYS A  82     8565   7044   5618   -924  -1104    -35       C  
ATOM    627  CD  LYS A  82     -11.453  -0.714 -12.681  1.00 56.15           C  
ANISOU  627  CD  LYS A  82     8443   7090   5802   -905  -1240    -19       C  
ATOM    628  CE  LYS A  82     -12.543  -1.160 -13.645  1.00 58.75           C  
ANISOU  628  CE  LYS A  82     8824   7459   6039   -993  -1420    -38       C  
ATOM    629  NZ  LYS A  82     -13.681  -1.913 -12.987  1.00 58.78           N  
ANISOU  629  NZ  LYS A  82     8671   7469   6192  -1007  -1508    -66       N  
ATOM    630  N   LEU A  83      -8.647   1.510  -8.994  1.00 47.70           N  
ANISOU  630  N   LEU A  83     7099   5930   5095   -620   -820     97       N  
ATOM    631  CA  LEU A  83      -8.081   1.148  -7.710  1.00 45.08           C  
ANISOU  631  CA  LEU A  83     6659   5576   4893   -563   -711     67       C  
ATOM    632  C   LEU A  83      -9.096   0.295  -6.977  1.00 44.11           C  
ANISOU  632  C   LEU A  83     6431   5448   4880   -551   -765     47       C  
ATOM    633  O   LEU A  83      -8.722  -0.507  -6.135  1.00 43.18           O  
ANISOU  633  O   LEU A  83     6258   5306   4841   -528   -682      4       O  
ATOM    634  CB  LEU A  83      -7.731   2.373  -6.867  1.00 43.81           C  
ANISOU  634  CB  LEU A  83     6437   5405   4802   -499   -681    132       C  
ATOM    635  CG  LEU A  83      -6.526   3.181  -7.345  1.00 42.56           C  
ANISOU  635  CG  LEU A  83     6365   5245   4562   -518   -593    147       C  
ATOM    636  CD1 LEU A  83      -6.281   4.393  -6.450  1.00 38.92           C  
ANISOU  636  CD1 LEU A  83     5845   4763   4180   -465   -576    205       C  
ATOM    637  CD2 LEU A  83      -5.293   2.287  -7.430  1.00 41.55           C  
ANISOU  637  CD2 LEU A  83     6256   5121   4409   -539   -452     62       C  
ATOM    638  N   SER A  84     -10.379   0.465  -7.298  1.00 44.32           N  
ANISOU  638  N   SER A  84     6428   5497   4915   -569   -907     82       N  
ATOM    639  CA  SER A  84     -11.458  -0.235  -6.574  1.00 43.55           C  
ANISOU  639  CA  SER A  84     6210   5403   4934   -569   -958     70       C  
ATOM    640  C   SER A  84     -11.539  -1.739  -6.863  1.00 42.16           C  
ANISOU  640  C   SER A  84     6071   5208   4741   -642   -938    -17       C  
ATOM    641  O   SER A  84     -11.724  -2.518  -5.926  1.00 40.43           O  
ANISOU  641  O   SER A  84     5774   4961   4625   -634   -889    -42       O  
ATOM    642  CB  SER A  84     -12.837   0.403  -6.840  1.00 44.97           C  
ANISOU  642  CB  SER A  84     6321   5623   5145   -564  -1119    129       C  
ATOM    643  OG  SER A  84     -13.859  -0.240  -6.070  1.00 46.28           O  
ANISOU  643  OG  SER A  84     6349   5799   5437   -570  -1149    114       O  
ATOM    644  N   ASP A  85     -11.450  -2.143  -8.138  1.00 40.93           N  
ANISOU  644  N   ASP A  85     6042   5058   4451   -718   -979    -62       N  
ATOM    645  CA  ASP A  85     -11.457  -3.573  -8.458  1.00 40.33           C  
ANISOU  645  CA  ASP A  85     6023   4948   4354   -791   -951   -157       C  
ATOM    646  C   ASP A  85     -10.180  -4.194  -7.889  1.00 37.45           C  
ANISOU  646  C   ASP A  85     5685   4526   4018   -747   -780   -208       C  
ATOM    647  O   ASP A  85     -10.212  -5.299  -7.343  1.00 37.01           O  
ANISOU  647  O   ASP A  85     5609   4418   4034   -757   -730   -258       O  
ATOM    648  CB  ASP A  85     -11.608  -3.870  -9.978  1.00 42.59           C  
ANISOU  648  CB  ASP A  85     6457   5253   4472   -886  -1028   -206       C  
ATOM    649  CG  ASP A  85     -13.088  -3.956 -10.449  1.00 46.17           C  
ANISOU  649  CG  ASP A  85     6867   5752   4924   -957  -1216   -192       C  
ATOM    650  OD1 ASP A  85     -14.006  -3.527  -9.704  1.00 49.90           O  
ANISOU  650  OD1 ASP A  85     7185   6251   5523   -920  -1291   -130       O  
ATOM    651  OD2 ASP A  85     -13.342  -4.440 -11.590  1.00 52.11           O  
ANISOU  651  OD2 ASP A  85     7736   6517   5545  -1052  -1293   -248       O  
ATOM    652  N   LEU A  86      -9.068  -3.464  -7.971  1.00 34.70           N  
ANISOU  652  N   LEU A  86     5375   4187   3623   -698   -694   -189       N  
ATOM    653  CA  LEU A  86      -7.822  -3.940  -7.414  1.00 32.43           C  
ANISOU  653  CA  LEU A  86     5088   3860   3375   -645   -543   -232       C  
ATOM    654  C   LEU A  86      -8.026  -4.305  -5.939  1.00 30.57           C  
ANISOU  654  C   LEU A  86     4729   3594   3292   -586   -518   -207       C  
ATOM    655  O   LEU A  86      -7.772  -5.419  -5.564  1.00 30.36           O  
ANISOU  655  O   LEU A  86     4711   3511   3314   -580   -458   -259       O  
ATOM    656  CB  LEU A  86      -6.718  -2.893  -7.552  1.00 31.90           C  
ANISOU  656  CB  LEU A  86     5039   3821   3259   -606   -468   -201       C  
ATOM    657  CG  LEU A  86      -5.308  -3.361  -7.145  1.00 32.24           C  
ANISOU  657  CG  LEU A  86     5075   3839   3337   -553   -315   -253       C  
ATOM    658  CD1 LEU A  86      -4.881  -4.600  -7.962  1.00 34.21           C  
ANISOU  658  CD1 LEU A  86     5426   4049   3524   -588   -246   -360       C  
ATOM    659  CD2 LEU A  86      -4.257  -2.248  -7.242  1.00 31.32           C  
ANISOU  659  CD2 LEU A  86     4956   3761   3185   -531   -243   -221       C  
ATOM    660  N   HIS A  87      -8.501  -3.363  -5.130  1.00 27.78           N  
ANISOU  660  N   HIS A  87     4276   3272   3009   -543   -562   -129       N  
ATOM    661  CA  HIS A  87      -8.576  -3.558  -3.704  1.00 26.55           C  
ANISOU  661  CA  HIS A  87     4018   3096   2975   -487   -523   -103       C  
ATOM    662  C   HIS A  87      -9.715  -4.458  -3.251  1.00 27.02           C  
ANISOU  662  C   HIS A  87     4028   3131   3108   -528   -569   -110       C  
ATOM    663  O   HIS A  87      -9.530  -5.189  -2.278  1.00 25.86           O  
ANISOU  663  O   HIS A  87     3850   2940   3034   -502   -507   -115       O  
ATOM    664  CB  HIS A  87      -8.662  -2.233  -2.954  1.00 25.40           C  
ANISOU  664  CB  HIS A  87     3791   2987   2874   -429   -539    -29       C  
ATOM    665  CG  HIS A  87      -7.365  -1.489  -2.892  1.00 24.53           C  
ANISOU  665  CG  HIS A  87     3703   2886   2731   -385   -463    -22       C  
ATOM    666  ND1 HIS A  87      -6.927  -0.682  -3.914  1.00 24.17           N  
ANISOU  666  ND1 HIS A  87     3730   2863   2590   -409   -470    -14       N  
ATOM    667  CD2 HIS A  87      -6.411  -1.426  -1.932  1.00 25.89           C  
ANISOU  667  CD2 HIS A  87     3834   3050   2952   -328   -382    -22       C  
ATOM    668  CE1 HIS A  87      -5.762  -0.148  -3.588  1.00 23.96           C  
ANISOU  668  CE1 HIS A  87     3697   2841   2564   -376   -388    -12       C  
ATOM    669  NE2 HIS A  87      -5.426  -0.577  -2.385  1.00 24.78           N  
ANISOU  669  NE2 HIS A  87     3727   2932   2758   -324   -340    -19       N  
ATOM    670  N   ALA A  88     -10.860  -4.425  -3.941  1.00 27.84           N  
ANISOU  670  N   ALA A  88     4124   3263   3191   -595   -679   -108       N  
ATOM    671  CA  ALA A  88     -12.066  -5.140  -3.498  1.00 28.88           C  
ANISOU  671  CA  ALA A  88     4183   3387   3406   -649   -728   -111       C  
ATOM    672  C   ALA A  88     -12.251  -6.496  -4.140  1.00 30.24           C  
ANISOU  672  C   ALA A  88     4437   3506   3548   -740   -734   -189       C  
ATOM    673  O   ALA A  88     -12.752  -7.415  -3.504  1.00 31.26           O  
ANISOU  673  O   ALA A  88     4532   3590   3756   -779   -714   -202       O  
ATOM    674  CB  ALA A  88     -13.317  -4.295  -3.741  1.00 29.04           C  
ANISOU  674  CB  ALA A  88     4111   3475   3448   -666   -854    -63       C  
ATOM    675  N   GLN A  89     -11.871  -6.624  -5.400  1.00 31.90           N  
ANISOU  675  N   GLN A  89     4765   3716   3641   -783   -759   -241       N  
ATOM    676  CA  GLN A  89     -12.163  -7.824  -6.154  1.00 34.44           C  
ANISOU  676  CA  GLN A  89     5178   3989   3920   -882   -781   -326       C  
ATOM    677  C   GLN A  89     -10.953  -8.772  -6.234  1.00 33.89           C  
ANISOU  677  C   GLN A  89     5224   3829   3823   -857   -651   -400       C  
ATOM    678  O   GLN A  89     -11.110  -9.980  -6.124  1.00 34.99           O  
ANISOU  678  O   GLN A  89     5409   3886   3999   -906   -622   -458       O  
ATOM    679  CB  GLN A  89     -12.704  -7.462  -7.550  1.00 36.01           C  
ANISOU  679  CB  GLN A  89     5444   4246   3994   -961   -908   -348       C  
ATOM    680  CG  GLN A  89     -14.260  -7.696  -7.745  1.00 43.80           C  
ANISOU  680  CG  GLN A  89     6349   5272   5023  -1060  -1059   -345       C  
ATOM    681  CD  GLN A  89     -15.223  -6.639  -7.083  1.00 49.77           C  
ANISOU  681  CD  GLN A  89     6926   6107   5877  -1013  -1144   -247       C  
ATOM    682  OE1 GLN A  89     -14.963  -5.411  -7.076  1.00 51.20           O  
ANISOU  682  OE1 GLN A  89     7082   6334   6036   -929  -1160   -178       O  
ATOM    683  NE2 GLN A  89     -16.367  -7.140  -6.556  1.00 53.87           N  
ANISOU  683  NE2 GLN A  89     7323   6636   6510  -1074  -1195   -246       N  
ATOM    684  N   LYS A  90      -9.768  -8.227  -6.448  1.00 32.89           N  
ANISOU  684  N   LYS A  90     5142   3716   3639   -783   -572   -400       N  
ATOM    685  CA  LYS A  90      -8.559  -9.033  -6.683  1.00 33.17           C  
ANISOU  685  CA  LYS A  90     5276   3680   3648   -748   -447   -478       C  
ATOM    686  C   LYS A  90      -7.868  -9.319  -5.361  1.00 30.86           C  
ANISOU  686  C   LYS A  90     4913   3339   3473   -647   -354   -445       C  
ATOM    687  O   LYS A  90      -7.582 -10.457  -5.045  1.00 31.72           O  
ANISOU  687  O   LYS A  90     5065   3353   3634   -634   -293   -490       O  
ATOM    688  CB  LYS A  90      -7.604  -8.268  -7.618  1.00 33.83           C  
ANISOU  688  CB  LYS A  90     5430   3816   3610   -727   -401   -496       C  
ATOM    689  CG  LYS A  90      -6.211  -8.901  -7.855  1.00 37.15           C  
ANISOU  689  CG  LYS A  90     5923   4182   4011   -671   -251   -576       C  
ATOM    690  CD  LYS A  90      -5.492  -8.213  -9.050  1.00 40.72           C  
ANISOU  690  CD  LYS A  90     6463   4694   4316   -692   -208   -607       C  
ATOM    691  CE  LYS A  90      -4.035  -8.643  -9.228  1.00 42.44           C  
ANISOU  691  CE  LYS A  90     6717   4880   4529   -624    -43   -682       C  
ATOM    692  NZ  LYS A  90      -3.164  -8.365  -8.021  1.00 41.78           N  
ANISOU  692  NZ  LYS A  90     6502   4797   4574   -509     27   -630       N  
ATOM    693  N   LEU A  91      -7.610  -8.269  -4.586  1.00 28.36           N  
ANISOU  693  N   LEU A  91     4497   3082   3196   -577   -350   -364       N  
ATOM    694  CA  LEU A  91      -6.817  -8.374  -3.351  1.00 26.77           C  
ANISOU  694  CA  LEU A  91     4232   2852   3085   -478   -271   -328       C  
ATOM    695  C   LEU A  91      -7.688  -8.671  -2.123  1.00 25.02           C  
ANISOU  695  C   LEU A  91     3935   2607   2964   -480   -302   -269       C  
ATOM    696  O   LEU A  91      -7.171  -9.074  -1.092  1.00 25.48           O  
ANISOU  696  O   LEU A  91     3969   2624   3089   -413   -247   -244       O  
ATOM    697  CB  LEU A  91      -6.064  -7.068  -3.095  1.00 26.37           C  
ANISOU  697  CB  LEU A  91     4120   2878   3020   -413   -250   -278       C  
ATOM    698  CG  LEU A  91      -4.883  -6.626  -3.999  1.00 28.29           C  
ANISOU  698  CG  LEU A  91     4416   3153   3182   -395   -182   -320       C  
ATOM    699  CD1 LEU A  91      -4.507  -5.158  -3.696  1.00 26.45           C  
ANISOU  699  CD1 LEU A  91     4114   2995   2939   -364   -189   -254       C  
ATOM    700  CD2 LEU A  91      -3.696  -7.444  -3.747  1.00 30.10           C  
ANISOU  700  CD2 LEU A  91     4654   3331   3451   -323    -77   -371       C  
ATOM    701  N   ARG A  92      -8.989  -8.404  -2.221  1.00 23.92           N  
ANISOU  701  N   ARG A  92     3752   2504   2832   -555   -391   -244       N  
ATOM    702  CA  ARG A  92      -9.951  -8.617  -1.127  1.00 23.05           C  
ANISOU  702  CA  ARG A  92     3559   2386   2813   -574   -411   -191       C  
ATOM    703  C   ARG A  92      -9.535  -8.009   0.193  1.00 20.83           C  
ANISOU  703  C   ARG A  92     3201   2128   2586   -485   -365   -122       C  
ATOM    704  O   ARG A  92      -9.503  -8.701   1.219  1.00 19.92           O  
ANISOU  704  O   ARG A  92     3081   1959   2529   -466   -318    -98       O  
ATOM    705  CB  ARG A  92     -10.230 -10.113  -0.960  1.00 23.49           C  
ANISOU  705  CB  ARG A  92     3677   2336   2912   -630   -382   -231       C  
ATOM    706  CG  ARG A  92     -10.802 -10.698  -2.227  1.00 27.21           C  
ANISOU  706  CG  ARG A  92     4223   2786   3329   -738   -439   -307       C  
ATOM    707  CD  ARG A  92     -11.331 -12.062  -1.980  1.00 32.85           C  
ANISOU  707  CD  ARG A  92     4987   3395   4099   -816   -423   -340       C  
ATOM    708  NE  ARG A  92     -12.027 -12.646  -3.131  1.00 38.76           N  
ANISOU  708  NE  ARG A  92     5804   4124   4799   -942   -491   -420       N  
ATOM    709  CZ  ARG A  92     -11.577 -13.659  -3.865  1.00 40.21           C  
ANISOU  709  CZ  ARG A  92     6128   4209   4941   -976   -457   -512       C  
ATOM    710  NH1 ARG A  92     -10.382 -14.208  -3.648  1.00 40.40           N  
ANISOU  710  NH1 ARG A  92     6234   4144   4972   -881   -351   -538       N  
ATOM    711  NH2 ARG A  92     -12.337 -14.122  -4.837  1.00 44.98           N  
ANISOU  711  NH2 ARG A  92     6788   4804   5496  -1105   -533   -585       N  
ATOM    712  N   VAL A  93      -9.174  -6.720   0.168  1.00 19.71           N  
ANISOU  712  N   VAL A  93     3014   2059   2414   -434   -378    -91       N  
ATOM    713  CA  VAL A  93      -8.765  -6.036   1.386  1.00 17.68           C  
ANISOU  713  CA  VAL A  93     2692   1829   2196   -357   -341    -36       C  
ATOM    714  C   VAL A  93      -9.923  -5.882   2.401  1.00 18.20           C  
ANISOU  714  C   VAL A  93     2674   1914   2328   -376   -357     14       C  
ATOM    715  O   VAL A  93     -11.009  -5.385   2.098  1.00 18.55           O  
ANISOU  715  O   VAL A  93     2660   2002   2387   -418   -417     25       O  
ATOM    716  CB  VAL A  93      -8.111  -4.705   1.041  1.00 17.76           C  
ANISOU  716  CB  VAL A  93     2689   1901   2160   -314   -349    -23       C  
ATOM    717  CG1 VAL A  93      -7.493  -4.100   2.289  1.00 15.66           C  
ANISOU  717  CG1 VAL A  93     2371   1653   1926   -241   -308     18       C  
ATOM    718  CG2 VAL A  93      -7.033  -4.903  -0.017  1.00 13.33           C  
ANISOU  718  CG2 VAL A  93     2207   1328   1532   -312   -316    -76       C  
ATOM    719  N   ASP A  94      -9.715  -6.421   3.600  1.00 18.68           N  
ANISOU  719  N   ASP A  94     2730   1939   2428   -346   -301     42       N  
ATOM    720  CA  ASP A  94     -10.680  -6.318   4.681  1.00 18.26           C  
ANISOU  720  CA  ASP A  94     2607   1903   2426   -363   -288     87       C  
ATOM    721  C   ASP A  94     -10.932  -4.818   4.894  1.00 18.24           C  
ANISOU  721  C   ASP A  94     2526   1981   2423   -321   -312    111       C  
ATOM    722  O   ASP A  94      -9.985  -4.085   5.082  1.00 16.46           O  
ANISOU  722  O   ASP A  94     2315   1775   2166   -257   -298    117       O  
ATOM    723  CB  ASP A  94     -10.102  -6.912   5.960  1.00 17.90           C  
ANISOU  723  CB  ASP A  94     2594   1814   2393   -320   -222    122       C  
ATOM    724  CG  ASP A  94     -11.158  -7.177   7.038  1.00 19.03           C  
ANISOU  724  CG  ASP A  94     2693   1958   2578   -363   -187    164       C  
ATOM    725  OD1 ASP A  94     -11.974  -6.296   7.255  1.00 19.53           O  
ANISOU  725  OD1 ASP A  94     2670   2088   2663   -372   -197    175       O  
ATOM    726  OD2 ASP A  94     -11.199  -8.277   7.661  1.00 19.93           O  
ANISOU  726  OD2 ASP A  94     2863   2003   2708   -390   -144    187       O  
ATOM    727  N   PRO A  95     -12.205  -4.373   4.920  1.00 19.04           N  
ANISOU  727  N   PRO A  95     2542   2125   2568   -357   -344    124       N  
ATOM    728  CA  PRO A  95     -12.514  -2.965   5.201  1.00 19.44           C  
ANISOU  728  CA  PRO A  95     2521   2234   2631   -304   -360    146       C  
ATOM    729  C   PRO A  95     -11.869  -2.377   6.426  1.00 19.34           C  
ANISOU  729  C   PRO A  95     2511   2229   2609   -237   -296    168       C  
ATOM    730  O   PRO A  95     -11.588  -1.190   6.405  1.00 19.25           O  
ANISOU  730  O   PRO A  95     2485   2244   2584   -186   -311    172       O  
ATOM    731  CB  PRO A  95     -14.043  -2.956   5.400  1.00 19.49           C  
ANISOU  731  CB  PRO A  95     2418   2275   2712   -348   -377    155       C  
ATOM    732  CG  PRO A  95     -14.495  -4.101   4.609  1.00 21.11           C  
ANISOU  732  CG  PRO A  95     2643   2453   2924   -439   -414    129       C  
ATOM    733  CD  PRO A  95     -13.430  -5.153   4.729  1.00 19.76           C  
ANISOU  733  CD  PRO A  95     2588   2209   2709   -445   -364    115       C  
ATOM    734  N   VAL A  96     -11.639  -3.159   7.486  1.00 20.47           N  
ANISOU  734  N   VAL A  96     2680   2345   2753   -238   -232    184       N  
ATOM    735  CA  VAL A  96     -11.103  -2.559   8.704  1.00 21.08           C  
ANISOU  735  CA  VAL A  96     2763   2438   2807   -181   -184    204       C  
ATOM    736  C   VAL A  96      -9.732  -2.022   8.461  1.00 21.29           C  
ANISOU  736  C   VAL A  96     2838   2465   2785   -128   -202    192       C  
ATOM    737  O   VAL A  96      -9.302  -1.146   9.194  1.00 22.50           O  
ANISOU  737  O   VAL A  96     2987   2644   2919    -85   -186    196       O  
ATOM    738  CB  VAL A  96     -11.093  -3.498   9.970  1.00 22.45           C  
ANISOU  738  CB  VAL A  96     2973   2584   2972   -193   -117    235       C  
ATOM    739  CG1 VAL A  96     -12.482  -4.147  10.180  1.00 23.55           C  
ANISOU  739  CG1 VAL A  96     3062   2720   3165   -268    -84    246       C  
ATOM    740  CG2 VAL A  96     -10.000  -4.524   9.897  1.00 22.12           C  
ANISOU  740  CG2 VAL A  96     3020   2485   2901   -179   -120    241       C  
ATOM    741  N   ASN A  97      -9.038  -2.477   7.419  1.00 21.40           N  
ANISOU  741  N   ASN A  97     2896   2455   2780   -136   -230    170       N  
ATOM    742  CA  ASN A  97      -7.661  -2.060   7.285  1.00 21.86           C  
ANISOU  742  CA  ASN A  97     2986   2520   2800    -92   -230    157       C  
ATOM    743  C   ASN A  97      -7.536  -0.636   6.737  1.00 21.51           C  
ANISOU  743  C   ASN A  97     2922   2511   2740    -81   -258    148       C  
ATOM    744  O   ASN A  97      -6.520   0.019   6.977  1.00 21.18           O  
ANISOU  744  O   ASN A  97     2888   2485   2674    -51   -249    142       O  
ATOM    745  CB  ASN A  97      -6.821  -3.044   6.454  1.00 22.29           C  
ANISOU  745  CB  ASN A  97     3093   2536   2841    -95   -228    129       C  
ATOM    746  CG  ASN A  97      -6.754  -4.439   7.067  1.00 25.09           C  
ANISOU  746  CG  ASN A  97     3486   2833   3213    -91   -200    142       C  
ATOM    747  OD1 ASN A  97      -6.870  -5.424   6.354  1.00 31.32           O  
ANISOU  747  OD1 ASN A  97     4317   3571   4012   -121   -199    119       O  
ATOM    748  ND2 ASN A  97      -6.599  -4.532   8.372  1.00 26.73           N  
ANISOU  748  ND2 ASN A  97     3693   3042   3421    -59   -179    180       N  
ATOM    749  N   PHE A  98      -8.550  -0.148   6.023  1.00 21.45           N  
ANISOU  749  N   PHE A  98     2888   2514   2749   -106   -297    151       N  
ATOM    750  CA  PHE A  98      -8.502   1.217   5.530  1.00 21.10           C  
ANISOU  750  CA  PHE A  98     2839   2487   2692    -91   -327    155       C  
ATOM    751  C   PHE A  98      -8.428   2.202   6.668  1.00 20.42           C  
ANISOU  751  C   PHE A  98     2729   2412   2619    -49   -300    163       C  
ATOM    752  O   PHE A  98      -7.680   3.169   6.574  1.00 20.13           O  
ANISOU  752  O   PHE A  98     2716   2374   2558    -34   -301    158       O  
ATOM    753  CB  PHE A  98      -9.644   1.515   4.571  1.00 22.79           C  
ANISOU  753  CB  PHE A  98     3030   2707   2924   -114   -391    165       C  
ATOM    754  CG  PHE A  98      -9.482   0.818   3.247  1.00 22.11           C  
ANISOU  754  CG  PHE A  98     2995   2612   2793   -163   -428    148       C  
ATOM    755  CD1 PHE A  98      -8.859   1.455   2.197  1.00 23.40           C  
ANISOU  755  CD1 PHE A  98     3218   2777   2897   -172   -453    146       C  
ATOM    756  CD2 PHE A  98      -9.865  -0.499   3.097  1.00 23.62           C  
ANISOU  756  CD2 PHE A  98     3190   2788   2996   -207   -427    128       C  
ATOM    757  CE1 PHE A  98      -8.678   0.823   1.008  1.00 22.42           C  
ANISOU  757  CE1 PHE A  98     3154   2648   2716   -220   -475    123       C  
ATOM    758  CE2 PHE A  98      -9.697  -1.124   1.902  1.00 24.77           C  
ANISOU  758  CE2 PHE A  98     3397   2922   3095   -254   -456    100       C  
ATOM    759  CZ  PHE A  98      -9.088  -0.459   0.862  1.00 23.48           C  
ANISOU  759  CZ  PHE A  98     3291   2767   2861   -258   -478     95       C  
ATOM    760  N   LYS A  99      -9.115   1.880   7.763  1.00 20.37           N  
ANISOU  760  N   LYS A  99     2686   2412   2643    -39   -265    171       N  
ATOM    761  CA  LYS A  99      -9.095   2.659   8.995  1.00 20.69           C  
ANISOU  761  CA  LYS A  99     2716   2463   2683     -3   -226    169       C  
ATOM    762  C   LYS A  99      -7.716   2.741   9.632  1.00 19.27           C  
ANISOU  762  C   LYS A  99     2581   2288   2454     10   -209    159       C  
ATOM    763  O   LYS A  99      -7.367   3.788  10.151  1.00 18.74           O  
ANISOU  763  O   LYS A  99     2524   2225   2372     30   -202    145       O  
ATOM    764  CB  LYS A  99     -10.042   2.052  10.050  1.00 22.00           C  
ANISOU  764  CB  LYS A  99     2846   2640   2874     -8   -175    179       C  
ATOM    765  CG  LYS A  99     -11.544   2.121   9.716  1.00 27.28           C  
ANISOU  765  CG  LYS A  99     3435   3319   3610    -19   -181    184       C  
ATOM    766  CD  LYS A  99     -12.401   1.267  10.708  1.00 32.35           C  
ANISOU  766  CD  LYS A  99     4041   3975   4277    -48   -112    194       C  
ATOM    767  CE  LYS A  99     -13.922   1.254  10.340  1.00 36.27           C  
ANISOU  767  CE  LYS A  99     4428   4494   4858    -69   -118    194       C  
ATOM    768  NZ  LYS A  99     -14.827   1.199  11.568  1.00 36.86           N  
ANISOU  768  NZ  LYS A  99     4446   4596   4964    -73    -21    192       N  
ATOM    769  N   LEU A 100      -7.000   1.612   9.644  1.00 17.48           N  
ANISOU  769  N   LEU A 100     2379   2057   2207      2   -206    164       N  
ATOM    770  CA  LEU A 100      -5.627   1.517  10.095  1.00 17.55           C  
ANISOU  770  CA  LEU A 100     2411   2076   2180     20   -206    156       C  
ATOM    771  C   LEU A 100      -4.717   2.381   9.266  1.00 17.56           C  
ANISOU  771  C   LEU A 100     2415   2086   2172     13   -226    133       C  
ATOM    772  O   LEU A 100      -3.910   3.146   9.803  1.00 18.37           O  
ANISOU  772  O   LEU A 100     2517   2207   2254     19   -228    118       O  
ATOM    773  CB  LEU A 100      -5.132   0.084  10.057  1.00 17.14           C  
ANISOU  773  CB  LEU A 100     2379   2005   2128     27   -204    167       C  
ATOM    774  CG  LEU A 100      -6.025  -0.999  10.698  1.00 17.40           C  
ANISOU  774  CG  LEU A 100     2427   2012   2172     16   -179    198       C  
ATOM    775  CD1 LEU A 100      -5.252  -2.294  10.897  1.00 16.26           C  
ANISOU  775  CD1 LEU A 100     2322   1833   2022     39   -180    215       C  
ATOM    776  CD2 LEU A 100      -6.620  -0.574  12.013  1.00 15.94           C  
ANISOU  776  CD2 LEU A 100     2242   1849   1967     20   -149    215       C  
ATOM    777  N   LEU A 101      -4.849   2.290   7.954  1.00 17.66           N  
ANISOU  777  N   LEU A 101     2434   2085   2191    -10   -240    128       N  
ATOM    778  CA  LEU A 101      -4.049   3.151   7.083  1.00 17.67           C  
ANISOU  778  CA  LEU A 101     2448   2092   2173    -30   -246    113       C  
ATOM    779  C   LEU A 101      -4.410   4.612   7.307  1.00 16.60           C  
ANISOU  779  C   LEU A 101     2318   1947   2040    -31   -256    117       C  
ATOM    780  O   LEU A 101      -3.540   5.458   7.356  1.00 16.85           O  
ANISOU  780  O   LEU A 101     2361   1984   2057    -46   -251    103       O  
ATOM    781  CB  LEU A 101      -4.173   2.744   5.594  1.00 17.82           C  
ANISOU  781  CB  LEU A 101     2494   2098   2177    -60   -256    108       C  
ATOM    782  CG  LEU A 101      -3.205   3.452   4.648  1.00 18.26           C  
ANISOU  782  CG  LEU A 101     2576   2163   2199    -92   -243     94       C  
ATOM    783  CD1 LEU A 101      -2.920   2.604   3.365  1.00 18.93           C  
ANISOU  783  CD1 LEU A 101     2696   2246   2252   -118   -228     74       C  
ATOM    784  CD2 LEU A 101      -3.725   4.881   4.273  1.00 13.24           C  
ANISOU  784  CD2 LEU A 101     1969   1509   1554   -110   -271    118       C  
ATOM    785  N   GLY A 102      -5.674   4.928   7.483  1.00 17.10           N  
ANISOU  785  N   GLY A 102     2372   1996   2131    -15   -268    133       N  
ATOM    786  CA  GLY A 102      -6.033   6.332   7.721  1.00 17.80           C  
ANISOU  786  CA  GLY A 102     2471   2061   2233     -1   -274    133       C  
ATOM    787  C   GLY A 102      -5.395   6.864   8.992  1.00 18.58           C  
ANISOU  787  C   GLY A 102     2577   2167   2317      8   -246    106       C  
ATOM    788  O   GLY A 102      -4.853   7.979   9.032  1.00 20.45           O  
ANISOU  788  O   GLY A 102     2843   2382   2545     -6   -247     91       O  
ATOM    789  N   GLN A 103      -5.452   6.056  10.040  1.00 18.20           N  
ANISOU  789  N   GLN A 103     2511   2146   2260     23   -224    102       N  
ATOM    790  CA  GLN A 103      -4.869   6.416  11.300  1.00 18.57           C  
ANISOU  790  CA  GLN A 103     2572   2210   2274     28   -209     77       C  
ATOM    791  C   GLN A 103      -3.357   6.670  11.102  1.00 18.47           C  
ANISOU  791  C   GLN A 103     2567   2216   2237     -4   -229     58       C  
ATOM    792  O   GLN A 103      -2.795   7.603  11.706  1.00 17.15           O  
ANISOU  792  O   GLN A 103     2418   2048   2050    -21   -233     28       O  
ATOM    793  CB  GLN A 103      -5.142   5.330  12.350  1.00 18.36           C  
ANISOU  793  CB  GLN A 103     2541   2210   2226     44   -188     91       C  
ATOM    794  CG  GLN A 103      -4.282   5.413  13.609  1.00 19.60           C  
ANISOU  794  CG  GLN A 103     2724   2398   2326     44   -192     73       C  
ATOM    795  CD  GLN A 103      -4.760   6.489  14.589  1.00 19.11           C  
ANISOU  795  CD  GLN A 103     2694   2329   2240     49   -162     38       C  
ATOM    796  OE1 GLN A 103      -5.792   7.181  14.367  1.00 18.23           O  
ANISOU  796  OE1 GLN A 103     2576   2184   2168     65   -130     28       O  
ATOM    797  NE2 GLN A 103      -4.034   6.627  15.677  1.00 13.88           N  
ANISOU  797  NE2 GLN A 103     2066   1696   1513     39   -174     16       N  
ATOM    798  N   CYS A 104      -2.694   5.881  10.250  1.00 17.87           N  
ANISOU  798  N   CYS A 104     2470   2154   2164    -15   -239     69       N  
ATOM    799  CA  CYS A 104      -1.253   6.106  10.066  1.00 17.91           C  
ANISOU  799  CA  CYS A 104     2458   2188   2159    -44   -247     46       C  
ATOM    800  C   CYS A 104      -0.948   7.365   9.233  1.00 18.69           C  
ANISOU  800  C   CYS A 104     2580   2259   2261    -93   -241     34       C  
ATOM    801  O   CYS A 104       0.107   8.018   9.399  1.00 19.78           O  
ANISOU  801  O   CYS A 104     2708   2416   2393   -135   -242      6       O  
ATOM    802  CB  CYS A 104      -0.597   4.909   9.462  1.00 17.15           C  
ANISOU  802  CB  CYS A 104     2330   2114   2071    -33   -244     51       C  
ATOM    803  SG  CYS A 104      -0.584   3.556  10.544  1.00 19.87           S  
ANISOU  803  SG  CYS A 104     2662   2476   2411     21   -258     70       S  
ATOM    804  N   PHE A 105      -1.849   7.717   8.345  1.00 17.95           N  
ANISOU  804  N   PHE A 105     2519   2123   2177    -94   -240     57       N  
ATOM    805  CA  PHE A 105      -1.728   9.000   7.638  1.00 18.96           C  
ANISOU  805  CA  PHE A 105     2694   2207   2303   -136   -238     60       C  
ATOM    806  C   PHE A 105      -1.946  10.188   8.580  1.00 18.45           C  
ANISOU  806  C   PHE A 105     2660   2103   2247   -134   -240     39       C  
ATOM    807  O   PHE A 105      -1.213  11.174   8.542  1.00 19.38           O  
ANISOU  807  O   PHE A 105     2807   2196   2359   -186   -234     20       O  
ATOM    808  CB  PHE A 105      -2.693   9.076   6.457  1.00 18.27           C  
ANISOU  808  CB  PHE A 105     2642   2082   2218   -127   -255    100       C  
ATOM    809  CG  PHE A 105      -2.525  10.285   5.620  1.00 19.12           C  
ANISOU  809  CG  PHE A 105     2815   2137   2313   -169   -258    119       C  
ATOM    810  CD1 PHE A 105      -1.476  10.393   4.756  1.00 21.56           C  
ANISOU  810  CD1 PHE A 105     3144   2458   2588   -236   -231    118       C  
ATOM    811  CD2 PHE A 105      -3.479  11.297   5.644  1.00 20.95           C  
ANISOU  811  CD2 PHE A 105     3091   2300   2569   -138   -283    142       C  
ATOM    812  CE1 PHE A 105      -1.342  11.514   3.939  1.00 22.23           C  
ANISOU  812  CE1 PHE A 105     3307   2486   2652   -286   -229    147       C  
ATOM    813  CE2 PHE A 105      -3.363  12.401   4.835  1.00 20.84           C  
ANISOU  813  CE2 PHE A 105     3155   2221   2542   -172   -292    173       C  
ATOM    814  CZ  PHE A 105      -2.267  12.511   3.989  1.00 21.23           C  
ANISOU  814  CZ  PHE A 105     3239   2282   2546   -254   -264    178       C  
ATOM    815  N   LEU A 106      -2.932  10.083   9.434  1.00 18.40           N  
ANISOU  815  N   LEU A 106     2650   2089   2254    -80   -240     36       N  
ATOM    816  CA  LEU A 106      -3.176  11.147  10.404  1.00 18.45           C  
ANISOU  816  CA  LEU A 106     2692   2056   2263    -71   -229      3       C  
ATOM    817  C   LEU A 106      -1.990  11.375  11.358  1.00 18.31           C  
ANISOU  817  C   LEU A 106     2675   2072   2209   -117   -231    -45       C  
ATOM    818  O   LEU A 106      -1.623  12.522  11.605  1.00 19.05           O  
ANISOU  818  O   LEU A 106     2816   2121   2301   -155   -228    -79       O  
ATOM    819  CB  LEU A 106      -4.476  10.899  11.169  1.00 18.13           C  
ANISOU  819  CB  LEU A 106     2638   2011   2241     -5   -210      3       C  
ATOM    820  CG  LEU A 106      -5.745  11.114  10.324  1.00 17.09           C  
ANISOU  820  CG  LEU A 106     2498   1836   2161     41   -219     40       C  
ATOM    821  CD1 LEU A 106      -6.986  10.688  11.095  1.00 13.82           C  
ANISOU  821  CD1 LEU A 106     2039   1437   1774     99   -188     35       C  
ATOM    822  CD2 LEU A 106      -5.867  12.576   9.926  1.00 18.35           C  
ANISOU  822  CD2 LEU A 106     2717   1908   2346     46   -227     37       C  
ATOM    823  N   VAL A 107      -1.373  10.314  11.863  1.00 17.81           N  
ANISOU  823  N   VAL A 107     2564   2081   2120   -115   -243    -47       N  
ATOM    824  CA  VAL A 107      -0.167  10.459  12.710  1.00 18.36           C  
ANISOU  824  CA  VAL A 107     2620   2198   2157   -157   -268    -88       C  
ATOM    825  C   VAL A 107       0.932  11.223  11.956  1.00 19.21           C  
ANISOU  825  C   VAL A 107     2720   2299   2282   -235   -272   -105       C  
ATOM    826  O   VAL A 107       1.599  12.131  12.502  1.00 19.35           O  
ANISOU  826  O   VAL A 107     2756   2309   2286   -294   -285   -151       O  
ATOM    827  CB  VAL A 107       0.361   9.073  13.205  1.00 18.97           C  
ANISOU  827  CB  VAL A 107     2642   2353   2214   -128   -294    -71       C  
ATOM    828  CG1 VAL A 107       1.738   9.200  13.926  1.00 18.86           C  
ANISOU  828  CG1 VAL A 107     2592   2399   2173   -169   -341   -107       C  
ATOM    829  CG2 VAL A 107      -0.676   8.373  14.138  1.00 14.85           C  
ANISOU  829  CG2 VAL A 107     2144   1835   1662    -70   -282    -52       C  
ATOM    830  N   VAL A 108       1.076  10.877  10.680  1.00 19.03           N  
ANISOU  830  N   VAL A 108     2675   2274   2281   -245   -255    -72       N  
ATOM    831  CA  VAL A 108       2.086  11.456   9.838  1.00 19.35           C  
ANISOU  831  CA  VAL A 108     2706   2314   2334   -324   -239    -82       C  
ATOM    832  C   VAL A 108       1.850  12.954   9.620  1.00 20.65           C  
ANISOU  832  C   VAL A 108     2955   2388   2503   -377   -226    -89       C  
ATOM    833  O   VAL A 108       2.757  13.745   9.731  1.00 20.10           O  
ANISOU  833  O   VAL A 108     2889   2313   2435   -461   -222   -123       O  
ATOM    834  CB  VAL A 108       2.177  10.699   8.485  1.00 19.69           C  
ANISOU  834  CB  VAL A 108     2725   2372   2383   -321   -212    -46       C  
ATOM    835  CG1 VAL A 108       2.906  11.527   7.475  1.00 17.95           C  
ANISOU  835  CG1 VAL A 108     2526   2130   2162   -410   -175    -46       C  
ATOM    836  CG2 VAL A 108       2.855   9.337   8.713  1.00 16.89           C  
ANISOU  836  CG2 VAL A 108     2282   2101   2036   -283   -219    -54       C  
ATOM    837  N   VAL A 109       0.623  13.359   9.360  1.00 21.27           N  
ANISOU  837  N   VAL A 109     3100   2391   2589   -328   -222    -60       N  
ATOM    838  CA  VAL A 109       0.356  14.785   9.243  1.00 21.65           C  
ANISOU  838  CA  VAL A 109     3239   2336   2650   -360   -214    -65       C  
ATOM    839  C   VAL A 109       0.613  15.486  10.603  1.00 22.76           C  
ANISOU  839  C   VAL A 109     3405   2461   2784   -381   -221   -133       C  
ATOM    840  O   VAL A 109       1.186  16.622  10.672  1.00 24.11           O  
ANISOU  840  O   VAL A 109     3633   2569   2959   -461   -214   -166       O  
ATOM    841  CB  VAL A 109      -1.063  15.013   8.749  1.00 21.51           C  
ANISOU  841  CB  VAL A 109     3273   2246   2656   -280   -220    -18       C  
ATOM    842  CG1 VAL A 109      -1.403  16.537   8.762  1.00 22.84           C  
ANISOU  842  CG1 VAL A 109     3544   2286   2847   -291   -214    -23       C  
ATOM    843  CG2 VAL A 109      -1.215  14.371   7.362  1.00 18.95           C  
ANISOU  843  CG2 VAL A 109     2938   1941   2321   -279   -225     44       C  
ATOM    844  N   ALA A 110       0.252  14.806  11.688  1.00 21.97           N  
ANISOU  844  N   ALA A 110     3269   2414   2663   -323   -233   -157       N  
ATOM    845  CA  ALA A 110       0.392  15.402  13.026  1.00 22.53           C  
ANISOU  845  CA  ALA A 110     3378   2475   2705   -340   -239   -226       C  
ATOM    846  C   ALA A 110       1.866  15.642  13.353  1.00 23.02           C  
ANISOU  846  C   ALA A 110     3410   2590   2748   -445   -269   -273       C  
ATOM    847  O   ALA A 110       2.237  16.656  13.938  1.00 23.48           O  
ANISOU  847  O   ALA A 110     3526   2602   2794   -511   -275   -333       O  
ATOM    848  CB  ALA A 110      -0.261  14.517  14.085  1.00 21.25           C  
ANISOU  848  CB  ALA A 110     3193   2372   2508   -265   -241   -234       C  
ATOM    849  N   ILE A 111       2.704  14.709  12.930  1.00 23.26           N  
ANISOU  849  N   ILE A 111     3344   2712   2781   -462   -288   -249       N  
ATOM    850  CA  ILE A 111       4.108  14.737  13.277  1.00 24.22           C  
ANISOU  850  CA  ILE A 111     3399   2908   2896   -548   -324   -290       C  
ATOM    851  C   ILE A 111       4.776  15.932  12.648  1.00 25.15           C  
ANISOU  851  C   ILE A 111     3548   2965   3043   -665   -300   -313       C  
ATOM    852  O   ILE A 111       5.507  16.668  13.331  1.00 25.41           O  
ANISOU  852  O   ILE A 111     3589   3000   3065   -754   -328   -377       O  
ATOM    853  CB  ILE A 111       4.807  13.441  12.833  1.00 24.24           C  
ANISOU  853  CB  ILE A 111     3281   3015   2914   -521   -338   -257       C  
ATOM    854  CG1 ILE A 111       4.428  12.274  13.776  1.00 24.16           C  
ANISOU  854  CG1 ILE A 111     3245   3068   2869   -426   -377   -243       C  
ATOM    855  CG2 ILE A 111       6.297  13.653  12.772  1.00 26.08           C  
ANISOU  855  CG2 ILE A 111     3423   3317   3170   -618   -360   -295       C  
ATOM    856  CD1 ILE A 111       5.216  10.962  13.511  1.00 20.61           C  
ANISOU  856  CD1 ILE A 111     2681   2711   2440   -388   -401   -215       C  
ATOM    857  N   HIS A 112       4.522  16.124  11.348  1.00 25.54           N  
ANISOU  857  N   HIS A 112     3625   2959   3120   -673   -252   -261       N  
ATOM    858  CA  HIS A 112       5.229  17.133  10.545  1.00 27.11           C  
ANISOU  858  CA  HIS A 112     3857   3101   3342   -794   -216   -264       C  
ATOM    859  C   HIS A 112       4.564  18.520  10.523  1.00 28.21           C  
ANISOU  859  C   HIS A 112     4145   3087   3488   -820   -198   -269       C  
ATOM    860  O   HIS A 112       5.252  19.535  10.345  1.00 30.42           O  
ANISOU  860  O   HIS A 112     4470   3307   3781   -942   -180   -294       O  
ATOM    861  CB  HIS A 112       5.358  16.618   9.120  1.00 27.34           C  
ANISOU  861  CB  HIS A 112     3857   3150   3381   -796   -170   -201       C  
ATOM    862  CG  HIS A 112       6.115  15.338   9.017  1.00 27.36           C  
ANISOU  862  CG  HIS A 112     3719   3285   3390   -773   -173   -204       C  
ATOM    863  ND1 HIS A 112       7.488  15.281   9.108  1.00 30.85           N  
ANISOU  863  ND1 HIS A 112     4051   3814   3857   -861   -170   -246       N  
ATOM    864  CD2 HIS A 112       5.699  14.064   8.839  1.00 27.47           C  
ANISOU  864  CD2 HIS A 112     3683   3356   3398   -670   -180   -173       C  
ATOM    865  CE1 HIS A 112       7.888  14.027   8.969  1.00 27.99           C  
ANISOU  865  CE1 HIS A 112     3576   3553   3507   -799   -173   -239       C  
ATOM    866  NE2 HIS A 112       6.822  13.271   8.784  1.00 27.38           N  
ANISOU  866  NE2 HIS A 112     3542   3452   3408   -686   -176   -195       N  
ATOM    867  N   HIS A 113       3.240  18.547  10.693  1.00 27.16           N  
ANISOU  867  N   HIS A 113     4081   2885   3352   -707   -200   -244       N  
ATOM    868  CA  HIS A 113       2.436  19.757  10.655  1.00 27.21           C  
ANISOU  868  CA  HIS A 113     4222   2738   3378   -692   -184   -243       C  
ATOM    869  C   HIS A 113       1.359  19.749  11.707  1.00 27.73           C  
ANISOU  869  C   HIS A 113     4319   2776   3439   -582   -192   -278       C  
ATOM    870  O   HIS A 113       0.199  19.839  11.382  1.00 26.48           O  
ANISOU  870  O   HIS A 113     4202   2554   3307   -482   -181   -237       O  
ATOM    871  CB  HIS A 113       1.725  19.861   9.310  1.00 26.74           C  
ANISOU  871  CB  HIS A 113     4215   2608   3336   -648   -166   -152       C  
ATOM    872  CG  HIS A 113       2.627  19.667   8.141  1.00 25.39           C  
ANISOU  872  CG  HIS A 113     4018   2477   3154   -742   -142   -107       C  
ATOM    873  ND1 HIS A 113       3.481  20.648   7.695  1.00 29.57           N  
ANISOU  873  ND1 HIS A 113     4608   2940   3687   -877   -110   -111       N  
ATOM    874  CD2 HIS A 113       2.818  18.604   7.334  1.00 24.26           C  
ANISOU  874  CD2 HIS A 113     3796   2430   2992   -726   -133    -64       C  
ATOM    875  CE1 HIS A 113       4.169  20.192   6.665  1.00 27.72           C  
ANISOU  875  CE1 HIS A 113     4328   2770   3435   -941    -76    -70       C  
ATOM    876  NE2 HIS A 113       3.768  18.962   6.412  1.00 27.94           N  
ANISOU  876  NE2 HIS A 113     4275   2893   3447   -846    -90    -44       N  
ATOM    877  N   PRO A 114       1.741  19.679  12.986  1.00 29.52           N  
ANISOU  877  N   PRO A 114     4529   3057   3631   -604   -211   -357       N  
ATOM    878  CA  PRO A 114       0.788  19.614  14.098  1.00 30.26           C  
ANISOU  878  CA  PRO A 114     4655   3139   3702   -510   -203   -400       C  
ATOM    879  C   PRO A 114      -0.146  20.808  14.202  1.00 32.25           C  
ANISOU  879  C   PRO A 114     5030   3233   3990   -463   -165   -425       C  
ATOM    880  O   PRO A 114      -1.245  20.654  14.751  1.00 33.12           O  
ANISOU  880  O   PRO A 114     5150   3329   4104   -353   -138   -437       O  
ATOM    881  CB  PRO A 114       1.692  19.620  15.333  1.00 31.87           C  
ANISOU  881  CB  PRO A 114     4848   3414   3845   -587   -237   -487       C  
ATOM    882  CG  PRO A 114       2.955  20.363  14.854  1.00 32.62           C  
ANISOU  882  CG  PRO A 114     4948   3487   3960   -736   -254   -508       C  
ATOM    883  CD  PRO A 114       3.126  19.850  13.448  1.00 29.91           C  
ANISOU  883  CD  PRO A 114     4539   3168   3658   -734   -239   -417       C  
ATOM    884  N   SER A 115       0.272  21.991  13.733  1.00 33.76           N  
ANISOU  884  N   SER A 115     5313   3301   4212   -543   -156   -436       N  
ATOM    885  CA  SER A 115      -0.599  23.181  13.822  1.00 35.56           C  
ANISOU  885  CA  SER A 115     5671   3356   4486   -487   -121   -459       C  
ATOM    886  C   SER A 115      -1.640  23.202  12.710  1.00 35.33           C  
ANISOU  886  C   SER A 115     5651   3257   4518   -377   -116   -360       C  
ATOM    887  O   SER A 115      -2.683  23.809  12.871  1.00 36.30           O  
ANISOU  887  O   SER A 115     5834   3269   4687   -271    -92   -368       O  
ATOM    888  CB  SER A 115       0.198  24.487  13.857  1.00 37.02           C  
ANISOU  888  CB  SER A 115     5974   3412   4680   -616   -115   -513       C  
ATOM    889  OG  SER A 115       0.377  25.022  12.541  1.00 39.11           O  
ANISOU  889  OG  SER A 115     6290   3583   4989   -660   -112   -428       O  
ATOM    890  N   LEU A 116      -1.372  22.520  11.599  1.00 34.66           N  
ANISOU  890  N   LEU A 116     5500   3239   4429   -397   -140   -270       N  
ATOM    891  CA  LEU A 116      -2.397  22.284  10.570  1.00 33.93           C  
ANISOU  891  CA  LEU A 116     5398   3117   4377   -291   -154   -174       C  
ATOM    892  C   LEU A 116      -3.523  21.345  11.042  1.00 32.93           C  
ANISOU  892  C   LEU A 116     5177   3072   4262   -158   -153   -172       C  
ATOM    893  O   LEU A 116      -4.692  21.544  10.696  1.00 33.62           O  
ANISOU  893  O   LEU A 116     5270   3099   4405    -44   -158   -132       O  
ATOM    894  CB  LEU A 116      -1.722  21.669   9.349  1.00 33.76           C  
ANISOU  894  CB  LEU A 116     5334   3167   4327   -362   -174    -95       C  
ATOM    895  CG  LEU A 116      -2.469  21.203   8.112  1.00 33.13           C  
ANISOU  895  CG  LEU A 116     5237   3093   4256   -293   -204      7       C  
ATOM    896  CD1 LEU A 116      -3.005  22.397   7.301  1.00 34.51           C  
ANISOU  896  CD1 LEU A 116     5544   3100   4467   -265   -220     71       C  
ATOM    897  CD2 LEU A 116      -1.500  20.361   7.271  1.00 31.02           C  
ANISOU  897  CD2 LEU A 116     4913   2937   3937   -387   -203     43       C  
ATOM    898  N   LEU A 117      -3.195  20.313  11.815  1.00 31.28           N  
ANISOU  898  N   LEU A 117     4878   3001   4005   -173   -149   -211       N  
ATOM    899  CA  LEU A 117      -4.211  19.291  12.110  1.00 30.31           C  
ANISOU  899  CA  LEU A 117     4665   2960   3891    -68   -143   -194       C  
ATOM    900  C   LEU A 117      -4.985  19.670  13.359  1.00 30.74           C  
ANISOU  900  C   LEU A 117     4743   2982   3954      3    -94   -270       C  
ATOM    901  O   LEU A 117      -4.898  19.020  14.374  1.00 30.36           O  
ANISOU  901  O   LEU A 117     4658   3023   3855     -1    -73   -316       O  
ATOM    902  CB  LEU A 117      -3.585  17.904  12.243  1.00 28.57           C  
ANISOU  902  CB  LEU A 117     4347   2891   3616   -108   -159   -183       C  
ATOM    903  CG  LEU A 117      -4.507  16.696  12.011  1.00 29.41           C  
ANISOU  903  CG  LEU A 117     4363   3074   3736    -28   -163   -133       C  
ATOM    904  CD1 LEU A 117      -4.922  16.489  10.581  1.00 26.19           C  
ANISOU  904  CD1 LEU A 117     3938   2650   3362     -7   -197    -52       C  
ATOM    905  CD2 LEU A 117      -3.848  15.412  12.537  1.00 30.09           C  
ANISOU  905  CD2 LEU A 117     4379   3288   3766    -62   -170   -141       C  
ATOM    906  N   THR A 118      -5.764  20.736  13.274  1.00 31.33           N  
ANISOU  906  N   THR A 118     4886   2925   4093     74    -72   -281       N  
ATOM    907  CA  THR A 118      -6.603  21.111  14.391  1.00 31.64           C  
ANISOU  907  CA  THR A 118     4944   2929   4150    156     -8   -359       C  
ATOM    908  C   THR A 118      -7.657  20.036  14.535  1.00 31.01           C  
ANISOU  908  C   THR A 118     4743   2949   4089    246     12   -329       C  
ATOM    909  O   THR A 118      -7.825  19.191  13.646  1.00 30.26           O  
ANISOU  909  O   THR A 118     4568   2921   4009    252    -33   -247       O  
ATOM    910  CB  THR A 118      -7.273  22.463  14.147  1.00 33.21           C  
ANISOU  910  CB  THR A 118     5233   2952   4435    234     11   -372       C  
ATOM    911  OG1 THR A 118      -7.906  22.417  12.878  1.00 31.29           O  
ANISOU  911  OG1 THR A 118     4951   2676   4261    301    -40   -267       O  
ATOM    912  CG2 THR A 118      -6.203  23.643  14.192  1.00 33.58           C  
ANISOU  912  CG2 THR A 118     5424   2875   4460    126      5   -419       C  
ATOM    913  N   PRO A 119      -8.376  20.035  15.660  1.00 31.70           N  
ANISOU  913  N   PRO A 119     4821   3051   4173    308     87   -401       N  
ATOM    914  CA  PRO A 119      -9.419  19.000  15.771  1.00 30.79           C  
ANISOU  914  CA  PRO A 119     4584   3032   4084    380    117   -369       C  
ATOM    915  C   PRO A 119     -10.494  19.074  14.687  1.00 30.39           C  
ANISOU  915  C   PRO A 119     4457   2942   4147    479     85   -295       C  
ATOM    916  O   PRO A 119     -11.027  18.048  14.300  1.00 28.89           O  
ANISOU  916  O   PRO A 119     4159   2844   3974    495     66   -240       O  
ATOM    917  CB  PRO A 119     -10.020  19.249  17.159  1.00 31.46           C  
ANISOU  917  CB  PRO A 119     4690   3117   4147    427    223   -467       C  
ATOM    918  CG  PRO A 119      -8.893  19.928  17.919  1.00 32.61           C  
ANISOU  918  CG  PRO A 119     4966   3222   4201    336    225   -548       C  
ATOM    919  CD  PRO A 119      -8.231  20.815  16.906  1.00 32.73           C  
ANISOU  919  CD  PRO A 119     5047   3127   4261    298    155   -515       C  
ATOM    920  N   GLU A 120     -10.809  20.274  14.203  1.00 31.57           N  
ANISOU  920  N   GLU A 120     4667   2954   4374    542     71   -293       N  
ATOM    921  CA  GLU A 120     -11.783  20.409  13.116  1.00 31.98           C  
ANISOU  921  CA  GLU A 120     4653   2967   4531    640     16   -212       C  
ATOM    922  C   GLU A 120     -11.189  19.901  11.807  1.00 30.52           C  
ANISOU  922  C   GLU A 120     4465   2817   4313    568    -86   -112       C  
ATOM    923  O   GLU A 120     -11.876  19.240  11.047  1.00 30.08           O  
ANISOU  923  O   GLU A 120     4315   2820   4296    606   -138    -45       O  
ATOM    924  CB  GLU A 120     -12.312  21.850  12.989  1.00 33.92           C  
ANISOU  924  CB  GLU A 120     4973   3042   4871    744     24   -231       C  
ATOM    925  CG  GLU A 120     -13.493  22.128  13.974  1.00 37.00           C  
ANISOU  925  CG  GLU A 120     5299   3417   5341    874    126   -312       C  
ATOM    926  CD  GLU A 120     -13.668  23.586  14.337  1.00 39.68           C  
ANISOU  926  CD  GLU A 120     5754   3577   5745    955    173   -378       C  
ATOM    927  OE1 GLU A 120     -12.662  24.209  14.759  1.00 40.76           O  
ANISOU  927  OE1 GLU A 120     6037   3640   5809    865    191   -435       O  
ATOM    928  OE2 GLU A 120     -14.812  24.100  14.225  1.00 41.84           O  
ANISOU  928  OE2 GLU A 120     5967   3784   6147   1109    191   -379       O  
ATOM    929  N   VAL A 121      -9.918  20.176  11.554  1.00 30.02           N  
ANISOU  929  N   VAL A 121     4502   2727   4179    457   -111   -108       N  
ATOM    930  CA  VAL A 121      -9.290  19.703  10.320  1.00 29.85           C  
ANISOU  930  CA  VAL A 121     4485   2741   4117    383   -187    -23       C  
ATOM    931  C   VAL A 121      -9.108  18.190  10.374  1.00 29.32           C  
ANISOU  931  C   VAL A 121     4315   2830   3996    335   -190    -11       C  
ATOM    932  O   VAL A 121      -9.236  17.508   9.379  1.00 29.85           O  
ANISOU  932  O   VAL A 121     4338   2947   4058    324   -246     57       O  
ATOM    933  CB  VAL A 121      -7.954  20.398  10.090  1.00 29.44           C  
ANISOU  933  CB  VAL A 121     4552   2625   4009    269   -193    -30       C  
ATOM    934  CG1 VAL A 121      -7.172  19.788   8.941  1.00 27.58           C  
ANISOU  934  CG1 VAL A 121     4314   2449   3718    178   -245     43       C  
ATOM    935  CG2 VAL A 121      -8.191  21.876   9.845  1.00 33.42           C  
ANISOU  935  CG2 VAL A 121     5175   2952   4572    313   -198    -24       C  
ATOM    936  N   HIS A 122      -8.837  17.664  11.560  1.00 29.91           N  
ANISOU  936  N   HIS A 122     4362   2975   4027    309   -132    -78       N  
ATOM    937  CA  HIS A 122      -8.723  16.228  11.760  1.00 29.39           C  
ANISOU  937  CA  HIS A 122     4211   3040   3915    274   -129    -66       C  
ATOM    938  C   HIS A 122     -10.077  15.565  11.447  1.00 29.90           C  
ANISOU  938  C   HIS A 122     4169   3146   4045    353   -135    -28       C  
ATOM    939  O   HIS A 122     -10.128  14.530  10.742  1.00 30.02           O  
ANISOU  939  O   HIS A 122     4127   3231   4049    326   -177     22       O  
ATOM    940  CB  HIS A 122      -8.239  15.990  13.200  1.00 29.76           C  
ANISOU  940  CB  HIS A 122     4274   3136   3899    241    -69   -141       C  
ATOM    941  CG  HIS A 122      -8.230  14.560  13.638  1.00 29.63           C  
ANISOU  941  CG  HIS A 122     4185   3236   3836    219    -58   -129       C  
ATOM    942  ND1 HIS A 122      -7.720  14.181  14.859  1.00 30.85           N  
ANISOU  942  ND1 HIS A 122     4362   3446   3915    184    -21   -178       N  
ATOM    943  CD2 HIS A 122      -8.658  13.422  13.043  1.00 30.47           C  
ANISOU  943  CD2 HIS A 122     4212   3407   3958    225    -81    -73       C  
ATOM    944  CE1 HIS A 122      -7.875  12.880  15.015  1.00 30.62           C  
ANISOU  944  CE1 HIS A 122     4272   3502   3862    177    -18   -144       C  
ATOM    945  NE2 HIS A 122      -8.423  12.391  13.920  1.00 29.24           N  
ANISOU  945  NE2 HIS A 122     4035   3331   3744    197    -51    -85       N  
ATOM    946  N   ALA A 123     -11.175  16.180  11.896  1.00 30.13           N  
ANISOU  946  N   ALA A 123     4169   3128   4150    449    -96    -56       N  
ATOM    947  CA  ALA A 123     -12.511  15.658  11.557  1.00 30.50           C  
ANISOU  947  CA  ALA A 123     4094   3217   4279    523   -106    -22       C  
ATOM    948  C   ALA A 123     -12.757  15.647  10.043  1.00 30.31           C  
ANISOU  948  C   ALA A 123     4053   3175   4288    533   -215     63       C  
ATOM    949  O   ALA A 123     -13.206  14.644   9.496  1.00 29.87           O  
ANISOU  949  O   ALA A 123     3913   3197   4239    517   -255    103       O  
ATOM    950  CB  ALA A 123     -13.658  16.458  12.291  1.00 31.14           C  
ANISOU  950  CB  ALA A 123     4132   3247   4453    639    -36    -74       C  
ATOM    951  N   SER A 124     -12.486  16.759   9.369  1.00 31.15           N  
ANISOU  951  N   SER A 124     4251   3176   4409    554   -264     91       N  
ATOM    952  CA  SER A 124     -12.637  16.820   7.912  1.00 31.80           C  
ANISOU  952  CA  SER A 124     4347   3237   4498    556   -372    179       C  
ATOM    953  C   SER A 124     -11.777  15.714   7.238  1.00 31.37           C  
ANISOU  953  C   SER A 124     4303   3269   4348    442   -404    210       C  
ATOM    954  O   SER A 124     -12.262  14.935   6.419  1.00 30.61           O  
ANISOU  954  O   SER A 124     4147   3232   4252    436   -467    256       O  
ATOM    955  CB  SER A 124     -12.186  18.179   7.393  1.00 32.58           C  
ANISOU  955  CB  SER A 124     4581   3199   4599    569   -405    208       C  
ATOM    956  OG  SER A 124     -12.912  19.263   7.971  1.00 34.06           O  
ANISOU  956  OG  SER A 124     4778   3283   4880    682   -374    176       O  
ATOM    957  N   LEU A 125     -10.498  15.639   7.599  1.00 31.20           N  
ANISOU  957  N   LEU A 125     4351   3256   4249    353   -360    178       N  
ATOM    958  CA  LEU A 125      -9.616  14.631   6.986  1.00 31.39           C  
ANISOU  958  CA  LEU A 125     4380   3355   4193    258   -378    198       C  
ATOM    959  C   LEU A 125     -10.093  13.203   7.293  1.00 30.75           C  
ANISOU  959  C   LEU A 125     4193   3377   4113    255   -366    187       C  
ATOM    960  O   LEU A 125      -9.947  12.294   6.487  1.00 29.34           O  
ANISOU  960  O   LEU A 125     3999   3251   3899    210   -403    217       O  
ATOM    961  CB  LEU A 125      -8.198  14.824   7.482  1.00 30.91           C  
ANISOU  961  CB  LEU A 125     4384   3291   4069    176   -331    157       C  
ATOM    962  CG  LEU A 125      -7.021  14.463   6.600  1.00 31.86           C  
ANISOU  962  CG  LEU A 125     4547   3440   4118     80   -345    181       C  
ATOM    963  CD1 LEU A 125      -7.200  14.935   5.109  1.00 29.32           C  
ANISOU  963  CD1 LEU A 125     4291   3067   3781     71   -407    255       C  
ATOM    964  CD2 LEU A 125      -5.814  15.146   7.295  1.00 30.60           C  
ANISOU  964  CD2 LEU A 125     4443   3254   3931     16   -299    131       C  
ATOM    965  N   ASP A 126     -10.693  13.015   8.466  1.00 31.19           N  
ANISOU  965  N   ASP A 126     4187   3458   4207    297   -307    143       N  
ATOM    966  CA  ASP A 126     -11.158  11.705   8.832  1.00 30.47           C  
ANISOU  966  CA  ASP A 126     4009   3452   4117    284   -285    137       C  
ATOM    967  C   ASP A 126     -12.287  11.304   7.887  1.00 30.87           C  
ANISOU  967  C   ASP A 126     3982   3524   4224    313   -352    182       C  
ATOM    968  O   ASP A 126     -12.262  10.198   7.342  1.00 30.03           O  
ANISOU  968  O   ASP A 126     3849   3472   4091    262   -381    201       O  
ATOM    969  CB  ASP A 126     -11.625  11.689  10.282  1.00 30.71           C  
ANISOU  969  CB  ASP A 126     4000   3501   4168    319   -197     84       C  
ATOM    970  CG  ASP A 126     -12.284  10.397  10.648  1.00 31.75           C  
ANISOU  970  CG  ASP A 126     4045   3710   4310    302   -167     88       C  
ATOM    971  OD1 ASP A 126     -11.686   9.331  10.403  1.00 34.24           O  
ANISOU  971  OD1 ASP A 126     4370   4067   4574    240   -183    105       O  
ATOM    972  OD2 ASP A 126     -13.419  10.446  11.140  1.00 36.12           O  
ANISOU  972  OD2 ASP A 126     4518   4277   4930    352   -125     73       O  
ATOM    973  N   LYS A 127     -13.264  12.209   7.701  1.00 30.97           N  
ANISOU  973  N   LYS A 127     3960   3491   4318    396   -381    196       N  
ATOM    974  CA  LYS A 127     -14.374  11.981   6.769  1.00 31.78           C  
ANISOU  974  CA  LYS A 127     3979   3615   4481    431   -467    242       C  
ATOM    975  C   LYS A 127     -13.864  11.767   5.328  1.00 30.49           C  
ANISOU  975  C   LYS A 127     3886   3449   4248    374   -566    297       C  
ATOM    976  O   LYS A 127     -14.292  10.839   4.674  1.00 31.55           O  
ANISOU  976  O   LYS A 127     3970   3642   4376    337   -621    316       O  
ATOM    977  CB  LYS A 127     -15.435  13.105   6.823  1.00 33.85           C  
ANISOU  977  CB  LYS A 127     4189   3821   4852    550   -490    250       C  
ATOM    978  CG  LYS A 127     -15.720  13.631   8.238  1.00 37.16           C  
ANISOU  978  CG  LYS A 127     4579   4218   5323    611   -372    182       C  
ATOM    979  CD  LYS A 127     -17.199  13.891   8.542  1.00 42.49           C  
ANISOU  979  CD  LYS A 127     5107   4905   6131    718   -358    169       C  
ATOM    980  CE  LYS A 127     -17.367  14.639   9.890  1.00 44.64           C  
ANISOU  980  CE  LYS A 127     5384   5136   6443    785   -228     92       C  
ATOM    981  NZ  LYS A 127     -16.545  14.110  11.066  1.00 46.23           N  
ANISOU  981  NZ  LYS A 127     5647   5373   6544    703   -114     33       N  
ATOM    982  N   PHE A 128     -12.948  12.600   4.845  1.00 28.83           N  
ANISOU  982  N   PHE A 128     3799   3172   3981    356   -582    319       N  
ATOM    983  CA  PHE A 128     -12.274  12.373   3.542  1.00 28.08           C  
ANISOU  983  CA  PHE A 128     3792   3080   3798    285   -648    364       C  
ATOM    984  C   PHE A 128     -11.640  10.983   3.393  1.00 26.72           C  
ANISOU  984  C   PHE A 128     3611   2985   3557    196   -620    340       C  
ATOM    985  O   PHE A 128     -11.842  10.298   2.399  1.00 26.20           O  
ANISOU  985  O   PHE A 128     3548   2955   3452    157   -683    364       O  
ATOM    986  CB  PHE A 128     -11.214  13.462   3.311  1.00 27.87           C  
ANISOU  986  CB  PHE A 128     3899   2970   3719    260   -630    379       C  
ATOM    987  CG  PHE A 128     -10.327  13.224   2.124  1.00 26.83           C  
ANISOU  987  CG  PHE A 128     3864   2848   3483    172   -659    415       C  
ATOM    988  CD1 PHE A 128     -10.789  13.434   0.841  1.00 29.14           C  
ANISOU  988  CD1 PHE A 128     4207   3124   3741    174   -758    484       C  
ATOM    989  CD2 PHE A 128      -9.025  12.800   2.287  1.00 23.95           C  
ANISOU  989  CD2 PHE A 128     3537   2511   3052     87   -586    378       C  
ATOM    990  CE1 PHE A 128      -9.984  13.229  -0.266  1.00 26.68           C  
ANISOU  990  CE1 PHE A 128     3998   2823   3318     87   -771    512       C  
ATOM    991  CE2 PHE A 128      -8.221  12.577   1.185  1.00 24.26           C  
ANISOU  991  CE2 PHE A 128     3656   2563   2998      8   -594    402       C  
ATOM    992  CZ  PHE A 128      -8.702  12.810  -0.097  1.00 26.57           C  
ANISOU  992  CZ  PHE A 128     4015   2837   3244      4   -680    468       C  
ATOM    993  N   LEU A 129     -10.873  10.565   4.390  1.00 26.85           N  
ANISOU  993  N   LEU A 129     3622   3022   3556    167   -531    290       N  
ATOM    994  CA  LEU A 129     -10.287   9.211   4.388  1.00 26.46           C  
ANISOU  994  CA  LEU A 129     3561   3034   3458    102   -501    266       C  
ATOM    995  C   LEU A 129     -11.360   8.090   4.323  1.00 27.04           C  
ANISOU  995  C   LEU A 129     3544   3159   3570    100   -527    266       C  
ATOM    996  O   LEU A 129     -11.194   7.090   3.620  1.00 26.61           O  
ANISOU  996  O   LEU A 129     3502   3135   3474     46   -551    265       O  
ATOM    997  CB  LEU A 129      -9.353   9.034   5.588  1.00 25.56           C  
ANISOU  997  CB  LEU A 129     3452   2931   3327     87   -416    221       C  
ATOM    998  CG  LEU A 129      -8.084   9.899   5.576  1.00 25.34           C  
ANISOU  998  CG  LEU A 129     3505   2868   3255     57   -392    211       C  
ATOM    999  CD1 LEU A 129      -7.337   9.760   6.885  1.00 25.72           C  
ANISOU  999  CD1 LEU A 129     3543   2937   3294     50   -328    165       C  
ATOM   1000  CD2 LEU A 129      -7.198   9.578   4.412  1.00 23.94           C  
ANISOU 1000  CD2 LEU A 129     3382   2702   3012     -7   -407    227       C  
ATOM   1001  N   CYS A 130     -12.481   8.287   5.003  1.00 28.48           N  
ANISOU 1001  N   CYS A 130     3638   3349   3836    156   -521    262       N  
ATOM   1002  CA  CYS A 130     -13.555   7.306   4.961  1.00 30.20           C  
ANISOU 1002  CA  CYS A 130     3755   3616   4102    142   -542    260       C  
ATOM   1003  C   CYS A 130     -14.156   7.233   3.558  1.00 29.90           C  
ANISOU 1003  C   CYS A 130     3712   3589   4059    127   -660    297       C  
ATOM   1004  O   CYS A 130     -14.510   6.138   3.111  1.00 29.29           O  
ANISOU 1004  O   CYS A 130     3604   3551   3973     68   -690    290       O  
ATOM   1005  CB  CYS A 130     -14.621   7.582   6.045  1.00 31.49           C  
ANISOU 1005  CB  CYS A 130     3810   3794   4363    202   -490    242       C  
ATOM   1006  SG  CYS A 130     -14.010   7.187   7.778  1.00 39.32           S  
ANISOU 1006  SG  CYS A 130     4817   4795   5329    191   -349    196       S  
ATOM   1007  N   ALA A 131     -14.210   8.371   2.851  1.00 29.50           N  
ANISOU 1007  N   ALA A 131     3710   3497   4004    172   -729    337       N  
ATOM   1008  CA  ALA A 131     -14.817   8.423   1.526  1.00 29.78           C  
ANISOU 1008  CA  ALA A 131     3752   3542   4021    164   -858    382       C  
ATOM   1009  C   ALA A 131     -13.936   7.782   0.483  1.00 29.54           C  
ANISOU 1009  C   ALA A 131     3833   3522   3869     75   -882    384       C  
ATOM   1010  O   ALA A 131     -14.433   7.113  -0.418  1.00 32.03           O  
ANISOU 1010  O   ALA A 131     4141   3873   4154     29   -965    392       O  
ATOM   1011  CB  ALA A 131     -15.170   9.861   1.128  1.00 30.35           C  
ANISOU 1011  CB  ALA A 131     3853   3555   4123    249   -928    435       C  
ATOM   1012  N   VAL A 132     -12.630   8.004   0.566  1.00 29.10           N  
ANISOU 1012  N   VAL A 132     3879   3435   3742     46   -809    372       N  
ATOM   1013  CA  VAL A 132     -11.664   7.273  -0.265  1.00 27.56           C  
ANISOU 1013  CA  VAL A 132     3777   3254   3439    -37   -794    357       C  
ATOM   1014  C   VAL A 132     -11.751   5.765  -0.038  1.00 28.25           C  
ANISOU 1014  C   VAL A 132     3817   3386   3532    -86   -762    308       C  
ATOM   1015  O   VAL A 132     -11.727   4.949  -0.987  1.00 27.46           O  
ANISOU 1015  O   VAL A 132     3761   3306   3367   -148   -801    295       O  
ATOM   1016  CB  VAL A 132     -10.227   7.695   0.058  1.00 27.03           C  
ANISOU 1016  CB  VAL A 132     3787   3158   3324    -55   -700    341       C  
ATOM   1017  CG1 VAL A 132      -9.217   6.688  -0.552  1.00 24.72           C  
ANISOU 1017  CG1 VAL A 132     3554   2892   2946   -131   -655    305       C  
ATOM   1018  CG2 VAL A 132      -9.952   9.158  -0.419  1.00 24.77           C  
ANISOU 1018  CG2 VAL A 132     3588   2813   3011    -37   -728    392       C  
ATOM   1019  N   ALA A 133     -11.822   5.400   1.243  1.00 28.95           N  
ANISOU 1019  N   ALA A 133     3829   3480   3689    -62   -687    279       N  
ATOM   1020  CA  ALA A 133     -12.041   4.008   1.649  1.00 29.06           C  
ANISOU 1020  CA  ALA A 133     3798   3521   3724   -103   -653    243       C  
ATOM   1021  C   ALA A 133     -13.316   3.436   1.044  1.00 30.57           C  
ANISOU 1021  C   ALA A 133     3925   3742   3949   -134   -739    248       C  
ATOM   1022  O   ALA A 133     -13.304   2.354   0.467  1.00 30.56           O  
ANISOU 1022  O   ALA A 133     3952   3749   3911   -202   -756    221       O  
ATOM   1023  CB  ALA A 133     -12.114   3.915   3.167  1.00 28.67           C  
ANISOU 1023  CB  ALA A 133     3681   3471   3739    -67   -568    229       C  
ATOM   1024  N   ASN A 134     -14.420   4.155   1.194  1.00 31.99           N  
ANISOU 1024  N   ASN A 134     4014   3936   4204    -85   -795    276       N  
ATOM   1025  CA  ASN A 134     -15.697   3.671   0.667  1.00 34.58           C  
ANISOU 1025  CA  ASN A 134     4252   4305   4581   -115   -889    279       C  
ATOM   1026  C   ASN A 134     -15.684   3.469  -0.828  1.00 34.55           C  
ANISOU 1026  C   ASN A 134     4328   4311   4488   -170  -1002    290       C  
ATOM   1027  O   ASN A 134     -16.439   2.667  -1.303  1.00 35.84           O  
ANISOU 1027  O   ASN A 134     4446   4509   4663   -231  -1069    272       O  
ATOM   1028  CB  ASN A 134     -16.849   4.634   0.962  1.00 36.28           C  
ANISOU 1028  CB  ASN A 134     4345   4537   4902    -33   -940    311       C  
ATOM   1029  CG  ASN A 134     -17.332   4.544   2.385  1.00 39.76           C  
ANISOU 1029  CG  ASN A 134     4673   4990   5443      0   -834    288       C  
ATOM   1030  OD1 ASN A 134     -16.932   3.636   3.148  1.00 42.96           O  
ANISOU 1030  OD1 ASN A 134     5090   5395   5837    -48   -736    256       O  
ATOM   1031  ND2 ASN A 134     -18.221   5.480   2.761  1.00 42.60           N  
ANISOU 1031  ND2 ASN A 134     4927   5358   5901     88   -851    304       N  
ATOM   1032  N   VAL A 135     -14.874   4.228  -1.555  1.00 33.39           N  
ANISOU 1032  N   VAL A 135     4301   4135   4249   -156  -1023    317       N  
ATOM   1033  CA  VAL A 135     -14.725   4.013  -2.981  1.00 33.66           C  
ANISOU 1033  CA  VAL A 135     4441   4180   4169   -218  -1114    324       C  
ATOM   1034  C   VAL A 135     -13.945   2.744  -3.326  1.00 33.06           C  
ANISOU 1034  C   VAL A 135     4446   4102   4013   -305  -1051    262       C  
ATOM   1035  O   VAL A 135     -14.257   2.061  -4.299  1.00 34.26           O  
ANISOU 1035  O   VAL A 135     4643   4275   4099   -377  -1126    240       O  
ATOM   1036  CB  VAL A 135     -14.010   5.191  -3.610  1.00 33.54           C  
ANISOU 1036  CB  VAL A 135     4543   4129   4070   -187  -1130    375       C  
ATOM   1037  CG1 VAL A 135     -13.310   4.740  -4.858  1.00 34.12           C  
ANISOU 1037  CG1 VAL A 135     4763   4207   3993   -270  -1148    360       C  
ATOM   1038  CG2 VAL A 135     -14.982   6.304  -3.887  1.00 33.94           C  
ANISOU 1038  CG2 VAL A 135     4551   4176   4170   -114  -1252    444       C  
ATOM   1039  N   LEU A 136     -12.912   2.453  -2.539  1.00 32.16           N  
ANISOU 1039  N   LEU A 136     4356   3960   3903   -295   -920    231       N  
ATOM   1040  CA  LEU A 136     -11.951   1.383  -2.835  1.00 31.80           C  
ANISOU 1040  CA  LEU A 136     4396   3899   3789   -352   -846    174       C  
ATOM   1041  C   LEU A 136     -12.466   0.002  -2.344  1.00 32.40           C  
ANISOU 1041  C   LEU A 136     4415   3972   3924   -396   -824    128       C  
ATOM   1042  O   LEU A 136     -11.915  -1.028  -2.704  1.00 32.31           O  
ANISOU 1042  O   LEU A 136     4474   3936   3865   -445   -782     76       O  
ATOM   1043  CB  LEU A 136     -10.550   1.699  -2.211  1.00 30.01           C  
ANISOU 1043  CB  LEU A 136     4208   3647   3549   -315   -725    166       C  
ATOM   1044  CG  LEU A 136      -9.586   2.658  -2.950  1.00 30.06           C  
ANISOU 1044  CG  LEU A 136     4312   3645   3464   -315   -708    187       C  
ATOM   1045  CD1 LEU A 136     -10.219   4.013  -3.155  1.00 30.00           C  
ANISOU 1045  CD1 LEU A 136     4299   3634   3465   -278   -791    256       C  
ATOM   1046  CD2 LEU A 136      -8.249   2.836  -2.245  1.00 26.30           C  
ANISOU 1046  CD2 LEU A 136     3843   3155   2996   -290   -592    168       C  
ATOM   1047  N   THR A 137     -13.483   0.007  -1.487  1.00 33.39           N  
ANISOU 1047  N   THR A 137     4417   4113   4156   -377   -839    146       N  
ATOM   1048  CA  THR A 137     -14.140  -1.205  -1.015  1.00 34.36           C  
ANISOU 1048  CA  THR A 137     4482   4232   4342   -432   -822    113       C  
ATOM   1049  C   THR A 137     -15.468  -1.422  -1.738  1.00 36.89           C  
ANISOU 1049  C   THR A 137     4737   4593   4687   -493   -946    111       C  
ATOM   1050  O   THR A 137     -16.129  -2.424  -1.491  1.00 37.75           O  
ANISOU 1050  O   THR A 137     4794   4699   4849   -561   -944     81       O  
ATOM   1051  CB  THR A 137     -14.425  -1.163   0.507  1.00 33.61           C  
ANISOU 1051  CB  THR A 137     4287   4135   4348   -387   -738    130       C  
ATOM   1052  OG1 THR A 137     -15.309  -0.077   0.807  1.00 33.98           O  
ANISOU 1052  OG1 THR A 137     4228   4222   4463   -332   -783    170       O  
ATOM   1053  CG2 THR A 137     -13.132  -1.011   1.319  1.00 31.73           C  
ANISOU 1053  CG2 THR A 137     4107   3864   4085   -332   -631    131       C  
ATOM   1054  N   ALA A 138     -15.878  -0.490  -2.605  1.00 38.37           N  
ANISOU 1054  N   ALA A 138     4925   4816   4840   -472  -1061    146       N  
ATOM   1055  CA  ALA A 138     -17.100  -0.675  -3.401  1.00 40.63           C  
ANISOU 1055  CA  ALA A 138     5146   5151   5140   -530  -1206    146       C  
ATOM   1056  C   ALA A 138     -16.844  -1.675  -4.536  1.00 41.58           C  
ANISOU 1056  C   ALA A 138     5391   5260   5148   -637  -1251     89       C  
ATOM   1057  O   ALA A 138     -17.481  -2.743  -4.577  1.00 43.79           O  
ANISOU 1057  O   ALA A 138     5633   5543   5463   -728  -1274     42       O  
ATOM   1058  CB  ALA A 138     -17.634   0.679  -3.958  1.00 40.93           C  
ANISOU 1058  CB  ALA A 138     5151   5226   5176   -459  -1330    213       C  
TER    1059      ALA A 138                                                      
ATOM   1060  N   VAL B   1      -1.346 -10.485  28.604  1.00 56.80           N  
ANISOU 1060  N   VAL B   1     6923   6745   7914    541    451   1487       N  
ATOM   1061  CA  VAL B   1      -0.544  -9.915  27.469  1.00 55.70           C  
ANISOU 1061  CA  VAL B   1     6793   6586   7785    583    448   1314       C  
ATOM   1062  C   VAL B   1       0.963  -9.862  27.765  1.00 56.08           C  
ANISOU 1062  C   VAL B   1     6761   6720   7827    701    425   1402       C  
ATOM   1063  O   VAL B   1       1.368  -9.673  28.910  1.00 56.44           O  
ANISOU 1063  O   VAL B   1     6734   6933   7779    727    377   1549       O  
ATOM   1064  CB  VAL B   1      -1.017  -8.494  27.117  1.00 54.04           C  
ANISOU 1064  CB  VAL B   1     6591   6518   7425    499    407   1140       C  
ATOM   1065  CG1 VAL B   1      -0.832  -7.556  28.325  1.00 53.47           C  
ANISOU 1065  CG1 VAL B   1     6446   6693   7177    486    342   1209       C  
ATOM   1066  CG2 VAL B   1      -0.277  -7.962  25.864  1.00 53.27           C  
ANISOU 1066  CG2 VAL B   1     6508   6388   7342    531    414    979       C  
ATOM   1067  N   GLN B   2       1.768 -10.015  26.709  1.00 56.11           N  
ANISOU 1067  N   GLN B   2     6773   6623   7923    768    459   1305       N  
ATOM   1068  CA  GLN B   2       3.235 -10.018  26.793  1.00 56.78           C  
ANISOU 1068  CA  GLN B   2     6772   6774   8028    885    448   1372       C  
ATOM   1069  C   GLN B   2       3.865  -8.715  26.295  1.00 54.30           C  
ANISOU 1069  C   GLN B   2     6418   6616   7599    864    413   1234       C  
ATOM   1070  O   GLN B   2       3.500  -8.220  25.235  1.00 53.90           O  
ANISOU 1070  O   GLN B   2     6427   6517   7538    810    437   1059       O  
ATOM   1071  CB  GLN B   2       3.799 -11.181  25.979  1.00 58.32           C  
ANISOU 1071  CB  GLN B   2     6991   6745   8423    992    525   1369       C  
ATOM   1072  CG  GLN B   2       3.896 -12.484  26.786  1.00 62.39           C  
ANISOU 1072  CG  GLN B   2     7490   7139   9075   1073    546   1588       C  
ATOM   1073  CD  GLN B   2       3.776 -13.726  25.916  1.00 65.56           C  
ANISOU 1073  CD  GLN B   2     7967   7244   9700   1126    634   1539       C  
ATOM   1074  OE1 GLN B   2       4.459 -13.840  24.890  1.00 65.74           O  
ANISOU 1074  OE1 GLN B   2     7995   7186   9798   1197    684   1409       O  
ATOM   1075  NE2 GLN B   2       2.892 -14.664  26.318  1.00 67.36           N  
ANISOU 1075  NE2 GLN B   2     8251   7307  10034   1088    660   1638       N  
ATOM   1076  N   TRP B   3       4.805  -8.174  27.065  1.00 52.99           N  
ANISOU 1076  N   TRP B   3     6147   6639   7349    902    352   1321       N  
ATOM   1077  CA  TRP B   3       5.565  -6.989  26.678  1.00 50.97           C  
ANISOU 1077  CA  TRP B   3     5835   6526   7007    882    318   1214       C  
ATOM   1078  C   TRP B   3       7.023  -7.376  26.516  1.00 50.98           C  
ANISOU 1078  C   TRP B   3     5736   6544   7090   1005    333   1284       C  
ATOM   1079  O   TRP B   3       7.582  -7.975  27.424  1.00 51.76           O  
ANISOU 1079  O   TRP B   3     5759   6695   7213   1085    304   1458       O  
ATOM   1080  CB  TRP B   3       5.459  -5.907  27.765  1.00 50.49           C  
ANISOU 1080  CB  TRP B   3     5720   6691   6772    808    226   1235       C  
ATOM   1081  CG  TRP B   3       4.074  -5.403  27.989  1.00 49.47           C  
ANISOU 1081  CG  TRP B   3     5671   6572   6555    697    213   1160       C  
ATOM   1082  CD1 TRP B   3       3.257  -5.690  29.036  1.00 50.60           C  
ANISOU 1082  CD1 TRP B   3     5824   6765   6636    665    193   1258       C  
ATOM   1083  CD2 TRP B   3       3.336  -4.529  27.131  1.00 48.71           C  
ANISOU 1083  CD2 TRP B   3     5644   6439   6423    609    223    980       C  
ATOM   1084  NE1 TRP B   3       2.050  -5.061  28.880  1.00 49.71           N  
ANISOU 1084  NE1 TRP B   3     5779   6648   6458    565    194   1140       N  
ATOM   1085  CE2 TRP B   3       2.076  -4.337  27.720  1.00 49.24           C  
ANISOU 1085  CE2 TRP B   3     5758   6533   6418    532    208    971       C  
ATOM   1086  CE3 TRP B   3       3.627  -3.878  25.928  1.00 47.64           C  
ANISOU 1086  CE3 TRP B   3     5531   6261   6307    590    245    838       C  
ATOM   1087  CZ2 TRP B   3       1.101  -3.522  27.142  1.00 48.53           C  
ANISOU 1087  CZ2 TRP B   3     5732   6423   6286    446    208    822       C  
ATOM   1088  CZ3 TRP B   3       2.665  -3.081  25.353  1.00 46.82           C  
ANISOU 1088  CZ3 TRP B   3     5499   6137   6156    502    243    702       C  
ATOM   1089  CH2 TRP B   3       1.416  -2.908  25.958  1.00 47.24           C  
ANISOU 1089  CH2 TRP B   3     5592   6210   6147    435    222    693       C  
ATOM   1090  N   SER B   4       7.652  -7.028  25.391  1.00 49.48           N  
ANISOU 1090  N   SER B   4     5537   6326   6937   1024    377   1161       N  
ATOM   1091  CA  SER B   4       9.115  -7.194  25.284  1.00 50.20           C  
ANISOU 1091  CA  SER B   4     5505   6478   7089   1134    387   1221       C  
ATOM   1092  C   SER B   4       9.795  -6.072  26.066  1.00 48.87           C  
ANISOU 1092  C   SER B   4     5222   6554   6792   1086    291   1254       C  
ATOM   1093  O   SER B   4       9.153  -5.096  26.433  1.00 47.37           O  
ANISOU 1093  O   SER B   4     5064   6459   6475    969    233   1189       O  
ATOM   1094  CB  SER B   4       9.603  -7.243  23.818  1.00 50.38           C  
ANISOU 1094  CB  SER B   4     5547   6405   7191   1173    480   1084       C  
ATOM   1095  OG  SER B   4       9.577  -5.969  23.174  1.00 49.44           O  
ANISOU 1095  OG  SER B   4     5436   6381   6968   1071    468    946       O  
ATOM   1096  N   ALA B   5      11.083  -6.223  26.341  1.00 49.39           N  
ANISOU 1096  N   ALA B   5     5149   6719   6896   1178    272   1349       N  
ATOM   1097  CA  ALA B   5      11.866  -5.143  26.976  1.00 49.08           C  
ANISOU 1097  CA  ALA B   5     4985   6916   6747   1126    179   1361       C  
ATOM   1098  C   ALA B   5      11.889  -3.858  26.109  1.00 47.32           C  
ANISOU 1098  C   ALA B   5     4780   6732   6468   1012    188   1184       C  
ATOM   1099  O   ALA B   5      11.767  -2.749  26.639  1.00 45.84           O  
ANISOU 1099  O   ALA B   5     4571   6682   6164    903    107   1136       O  
ATOM   1100  CB  ALA B   5      13.277  -5.623  27.303  1.00 49.94           C  
ANISOU 1100  CB  ALA B   5     4928   7120   6927   1252    162   1496       C  
ATOM   1101  N   GLU B   6      12.001  -4.033  24.786  1.00 47.14           N  
ANISOU 1101  N   GLU B   6     4803   6582   6527   1039    288   1089       N  
ATOM   1102  CA  GLU B   6      11.939  -2.921  23.818  1.00 46.74           C  
ANISOU 1102  CA  GLU B   6     4785   6545   6430    938    312    940       C  
ATOM   1103  C   GLU B   6      10.676  -2.105  24.010  1.00 44.41           C  
ANISOU 1103  C   GLU B   6     4604   6239   6032    807    265    853       C  
ATOM   1104  O   GLU B   6      10.738  -0.880  24.139  1.00 44.05           O  
ANISOU 1104  O   GLU B   6     4533   6295   5909    705    210    792       O  
ATOM   1105  CB  GLU B   6      12.013  -3.402  22.351  1.00 47.33           C  
ANISOU 1105  CB  GLU B   6     4917   6479   6587    991    435    852       C  
ATOM   1106  CG  GLU B   6      13.011  -2.586  21.455  1.00 51.42           C  
ANISOU 1106  CG  GLU B   6     5349   7086   7102    968    476    792       C  
ATOM   1107  CD  GLU B   6      12.563  -2.427  19.962  1.00 54.71           C  
ANISOU 1107  CD  GLU B   6     5874   7403   7513    938    574    656       C  
ATOM   1108  OE1 GLU B   6      12.086  -1.331  19.564  1.00 52.40           O  
ANISOU 1108  OE1 GLU B   6     5632   7139   7137    818    552    580       O  
ATOM   1109  OE2 GLU B   6      12.689  -3.407  19.189  1.00 59.14           O  
ANISOU 1109  OE2 GLU B   6     6466   7856   8149   1039    672    626       O  
ATOM   1110  N   GLU B   7       9.531  -2.785  24.035  1.00 43.09           N  
ANISOU 1110  N   GLU B   7     4556   5943   5875    811    288    846       N  
ATOM   1111  CA  GLU B   7       8.242  -2.111  24.184  1.00 40.90           C  
ANISOU 1111  CA  GLU B   7     4381   5649   5510    700    253    765       C  
ATOM   1112  C   GLU B   7       8.139  -1.426  25.544  1.00 40.46           C  
ANISOU 1112  C   GLU B   7     4273   5750   5348    641    150    810       C  
ATOM   1113  O   GLU B   7       7.712  -0.272  25.620  1.00 39.75           O  
ANISOU 1113  O   GLU B   7     4206   5718   5179    541    106    717       O  
ATOM   1114  CB  GLU B   7       7.083  -3.110  24.031  1.00 40.79           C  
ANISOU 1114  CB  GLU B   7     4483   5475   5540    718    298    766       C  
ATOM   1115  CG  GLU B   7       6.787  -3.551  22.591  1.00 39.80           C  
ANISOU 1115  CG  GLU B   7     4445   5192   5486    735    389    661       C  
ATOM   1116  CD  GLU B   7       5.832  -4.727  22.518  1.00 38.65           C  
ANISOU 1116  CD  GLU B   7     4392   4881   5412    759    430    671       C  
ATOM   1117  OE1 GLU B   7       5.713  -5.464  23.518  1.00 37.06           O  
ANISOU 1117  OE1 GLU B   7     4170   4668   5243    798    410    796       O  
ATOM   1118  OE2 GLU B   7       5.196  -4.923  21.459  1.00 38.81           O  
ANISOU 1118  OE2 GLU B   7     4503   4786   5457    735    482    558       O  
ATOM   1119  N   LYS B   8       8.504  -2.156  26.605  1.00 40.31           N  
ANISOU 1119  N   LYS B   8     4187   5800   5329    708    114    950       N  
ATOM   1120  CA  LYS B   8       8.485  -1.640  27.977  1.00 40.18           C  
ANISOU 1120  CA  LYS B   8     4112   5962   5192    664     16   1001       C  
ATOM   1121  C   LYS B   8       9.227  -0.329  28.124  1.00 39.31           C  
ANISOU 1121  C   LYS B   8     3918   6002   5016    589    -52    924       C  
ATOM   1122  O   LYS B   8       8.713   0.613  28.731  1.00 38.47           O  
ANISOU 1122  O   LYS B   8     3829   5984   4806    496   -114    849       O  
ATOM   1123  CB  LYS B   8       9.093  -2.656  28.948  1.00 41.87           C  
ANISOU 1123  CB  LYS B   8     4240   6248   5421    766    -13   1188       C  
ATOM   1124  CG  LYS B   8       8.085  -3.356  29.841  1.00 44.54           C  
ANISOU 1124  CG  LYS B   8     4639   6571   5713    771    -20   1286       C  
ATOM   1125  CD  LYS B   8       8.392  -4.850  30.021  1.00 49.48           C  
ANISOU 1125  CD  LYS B   8     5244   7102   6452    899     21   1469       C  
ATOM   1126  CE  LYS B   8       7.496  -5.525  31.107  1.00 52.34           C  
ANISOU 1126  CE  LYS B   8     5645   7482   6758    898      6   1608       C  
ATOM   1127  NZ  LYS B   8       7.204  -6.983  30.832  1.00 53.38           N  
ANISOU 1127  NZ  LYS B   8     5831   7402   7049    985     85   1729       N  
ATOM   1128  N   GLN B   9      10.448  -0.294  27.586  1.00 39.34           N  
ANISOU 1128  N   GLN B   9     3824   6034   5090    629    -37    940       N  
ATOM   1129  CA  GLN B   9      11.286   0.913  27.542  1.00 39.11           C  
ANISOU 1129  CA  GLN B   9     3702   6127   5031    550    -89    869       C  
ATOM   1130  C   GLN B   9      10.678   2.031  26.689  1.00 36.30           C  
ANISOU 1130  C   GLN B   9     3435   5691   4665    441    -66    716       C  
ATOM   1131  O   GLN B   9      10.568   3.158  27.166  1.00 36.35           O  
ANISOU 1131  O   GLN B   9     3429   5778   4602    339   -136    636       O  
ATOM   1132  CB  GLN B   9      12.703   0.546  27.032  1.00 41.27           C  
ANISOU 1132  CB  GLN B   9     3844   6436   5399    628    -57    936       C  
ATOM   1133  CG  GLN B   9      13.771   1.628  27.204  1.00 43.19           C  
ANISOU 1133  CG  GLN B   9     3951   6837   5623    551   -124    901       C  
ATOM   1134  CD  GLN B   9      13.865   2.605  26.042  1.00 46.10           C  
ANISOU 1134  CD  GLN B   9     4348   7139   6030    462    -71    783       C  
ATOM   1135  OE1 GLN B   9      14.282   3.761  26.224  1.00 49.97           O  
ANISOU 1135  OE1 GLN B   9     4775   7717   6493    351   -132    719       O  
ATOM   1136  NE2 GLN B   9      13.501   2.149  24.835  1.00 48.72           N  
ANISOU 1136  NE2 GLN B   9     4771   7315   6425    507     41    756       N  
ATOM   1137  N   LEU B  10      10.252   1.733  25.457  1.00 33.93           N  
ANISOU 1137  N   LEU B  10     3228   5235   4431    462     29    671       N  
ATOM   1138  CA  LEU B  10       9.578   2.767  24.615  1.00 32.25           C  
ANISOU 1138  CA  LEU B  10     3104   4946   4203    365     48    545       C  
ATOM   1139  C   LEU B  10       8.339   3.417  25.290  1.00 30.54           C  
ANISOU 1139  C   LEU B  10     2973   4729   3904    288     -8    475       C  
ATOM   1140  O   LEU B  10       8.030   4.581  25.039  1.00 29.44           O  
ANISOU 1140  O   LEU B  10     2864   4579   3744    198    -31    380       O  
ATOM   1141  CB  LEU B  10       9.145   2.216  23.254  1.00 31.52           C  
ANISOU 1141  CB  LEU B  10     3107   4702   4169    405    151    512       C  
ATOM   1142  CG  LEU B  10      10.182   1.853  22.178  1.00 32.32           C  
ANISOU 1142  CG  LEU B  10     3152   4784   4344    465    235    529       C  
ATOM   1143  CD1 LEU B  10       9.498   1.029  21.069  1.00 32.60           C  
ANISOU 1143  CD1 LEU B  10     3302   4671   4414    517    329    486       C  
ATOM   1144  CD2 LEU B  10      10.854   3.098  21.596  1.00 30.04           C  
ANISOU 1144  CD2 LEU B  10     2807   4555   4051    380    232    485       C  
ATOM   1145  N   ILE B  11       7.648   2.654  26.132  1.00 29.41           N  
ANISOU 1145  N   ILE B  11     2862   4593   3720    327    -24    528       N  
ATOM   1146  CA  ILE B  11       6.452   3.136  26.824  1.00 28.39           C  
ANISOU 1146  CA  ILE B  11     2802   4477   3508    268    -64    468       C  
ATOM   1147  C   ILE B  11       6.767   3.992  28.072  1.00 28.05           C  
ANISOU 1147  C   ILE B  11     2685   4603   3370    210   -161    441       C  
ATOM   1148  O   ILE B  11       6.259   5.081  28.203  1.00 24.63           O  
ANISOU 1148  O   ILE B  11     2285   4178   2897    131   -194    328       O  
ATOM   1149  CB  ILE B  11       5.540   1.967  27.228  1.00 28.51           C  
ANISOU 1149  CB  ILE B  11     2877   4441   3516    322    -34    542       C  
ATOM   1150  CG1 ILE B  11       4.606   1.623  26.073  1.00 29.20           C  
ANISOU 1150  CG1 ILE B  11     3075   4356   3664    323     40    488       C  
ATOM   1151  CG2 ILE B  11       4.743   2.341  28.448  1.00 28.51           C  
ANISOU 1151  CG2 ILE B  11     2886   4543   3404    278    -90    527       C  
ATOM   1152  CD1 ILE B  11       4.199   0.175  26.036  1.00 30.66           C  
ANISOU 1152  CD1 ILE B  11     3299   4445   3906    393     94    576       C  
ATOM   1153  N   SER B  12       7.620   3.491  28.962  1.00 29.96           N  
ANISOU 1153  N   SER B  12     2825   4981   3579    254   -207    542       N  
ATOM   1154  CA  SER B  12       7.947   4.211  30.205  1.00 31.52           C  
ANISOU 1154  CA  SER B  12     2947   5365   3666    200   -306    512       C  
ATOM   1155  C   SER B  12       8.793   5.471  29.912  1.00 31.96           C  
ANISOU 1155  C   SER B  12     2937   5460   3748    112   -352    408       C  
ATOM   1156  O   SER B  12       8.599   6.522  30.504  1.00 33.19           O  
ANISOU 1156  O   SER B  12     3089   5684   3839     26   -415    294       O  
ATOM   1157  CB  SER B  12       8.637   3.282  31.201  1.00 32.92           C  
ANISOU 1157  CB  SER B  12     3026   5689   3793    275   -350    665       C  
ATOM   1158  OG  SER B  12       9.997   3.058  30.878  1.00 37.62           O  
ANISOU 1158  OG  SER B  12     3506   6328   4461    317   -360    735       O  
ATOM   1159  N   SER B  13       9.672   5.370  28.932  1.00 31.71           N  
ANISOU 1159  N   SER B  13     2859   5370   3821    132   -309    440       N  
ATOM   1160  CA  SER B  13      10.442   6.516  28.432  1.00 31.65           C  
ANISOU 1160  CA  SER B  13     2793   5368   3863     42   -330    358       C  
ATOM   1161  C   SER B  13       9.600   7.650  27.845  1.00 29.34           C  
ANISOU 1161  C   SER B  13     2604   4953   3590    -48   -315    224       C  
ATOM   1162  O   SER B  13       9.815   8.796  28.164  1.00 29.23           O  
ANISOU 1162  O   SER B  13     2560   4975   3570   -146   -374    127       O  
ATOM   1163  CB  SER B  13      11.418   6.040  27.369  1.00 31.46           C  
ANISOU 1163  CB  SER B  13     2707   5299   3947     94   -260    434       C  
ATOM   1164  OG  SER B  13      12.058   7.146  26.827  1.00 34.26           O  
ANISOU 1164  OG  SER B  13     3013   5652   4354     -2   -269    367       O  
ATOM   1165  N   LEU B  14       8.659   7.341  26.967  1.00 27.87           N  
ANISOU 1165  N   LEU B  14     2536   4617   3436    -16   -237    218       N  
ATOM   1166  CA  LEU B  14       7.800   8.385  26.404  1.00 26.82           C  
ANISOU 1166  CA  LEU B  14     2498   4370   3323    -87   -226    108       C  
ATOM   1167  C   LEU B  14       6.847   8.967  27.450  1.00 25.77           C  
ANISOU 1167  C   LEU B  14     2410   4275   3109   -127   -286     13       C  
ATOM   1168  O   LEU B  14       6.574  10.177  27.450  1.00 25.09           O  
ANISOU 1168  O   LEU B  14     2348   4147   3039   -206   -317    -97       O  
ATOM   1169  CB  LEU B  14       6.999   7.865  25.217  1.00 26.21           C  
ANISOU 1169  CB  LEU B  14     2527   4147   3286    -40   -139    127       C  
ATOM   1170  CG  LEU B  14       6.152   8.930  24.516  1.00 27.44           C  
ANISOU 1170  CG  LEU B  14     2772   4188   3467   -103   -130     37       C  
ATOM   1171  CD1 LEU B  14       7.021  10.156  24.191  1.00 31.86           C  
ANISOU 1171  CD1 LEU B  14     3274   4745   4084   -192   -154      1       C  
ATOM   1172  CD2 LEU B  14       5.548   8.364  23.248  1.00 28.53           C  
ANISOU 1172  CD2 LEU B  14     2996   4211   3634    -58    -50     64       C  
ATOM   1173  N   TRP B  15       6.328   8.104  28.319  1.00 25.08           N  
ANISOU 1173  N   TRP B  15     2332   4260   2939    -70   -295     59       N  
ATOM   1174  CA  TRP B  15       5.358   8.532  29.316  1.00 25.15           C  
ANISOU 1174  CA  TRP B  15     2379   4321   2854    -96   -334    -25       C  
ATOM   1175  C   TRP B  15       5.917   9.629  30.199  1.00 25.73           C  
ANISOU 1175  C   TRP B  15     2385   4509   2881   -177   -422   -132       C  
ATOM   1176  O   TRP B  15       5.244  10.622  30.436  1.00 24.86           O  
ANISOU 1176  O   TRP B  15     2322   4366   2759   -230   -443   -265       O  
ATOM   1177  CB  TRP B  15       4.849   7.392  30.190  1.00 25.61           C  
ANISOU 1177  CB  TRP B  15     2441   4467   2822    -28   -328     66       C  
ATOM   1178  CG  TRP B  15       3.943   7.925  31.200  1.00 25.58           C  
ANISOU 1178  CG  TRP B  15     2464   4543   2712    -59   -361    -28       C  
ATOM   1179  CD1 TRP B  15       4.196   8.085  32.517  1.00 28.16           C  
ANISOU 1179  CD1 TRP B  15     2729   5057   2913    -76   -428    -49       C  
ATOM   1180  CD2 TRP B  15       2.657   8.479  30.963  1.00 24.92           C  
ANISOU 1180  CD2 TRP B  15     2470   4365   2635    -78   -330   -129       C  
ATOM   1181  NE1 TRP B  15       3.148   8.702  33.119  1.00 28.12           N  
ANISOU 1181  NE1 TRP B  15     2772   5079   2832   -103   -432   -168       N  
ATOM   1182  CE2 TRP B  15       2.173   8.934  32.192  1.00 26.47           C  
ANISOU 1182  CE2 TRP B  15     2653   4695   2710   -101   -371   -214       C  
ATOM   1183  CE3 TRP B  15       1.866   8.616  29.834  1.00 22.78           C  
ANISOU 1183  CE3 TRP B  15     2280   3921   2453    -74   -273   -155       C  
ATOM   1184  CZ2 TRP B  15       0.923   9.525  32.332  1.00 27.47           C  
ANISOU 1184  CZ2 TRP B  15     2842   4780   2815   -112   -348   -326       C  
ATOM   1185  CZ3 TRP B  15       0.633   9.184  29.962  1.00 26.54           C  
ANISOU 1185  CZ3 TRP B  15     2815   4357   2911    -86   -261   -252       C  
ATOM   1186  CH2 TRP B  15       0.156   9.629  31.211  1.00 26.07           C  
ANISOU 1186  CH2 TRP B  15     2737   4425   2741   -102   -294   -337       C  
ATOM   1187  N   GLY B  16       7.173   9.473  30.601  1.00 27.16           N  
ANISOU 1187  N   GLY B  16     2453   4815   3050   -185   -472    -79       N  
ATOM   1188  CA  GLY B  16       7.848  10.425  31.481  1.00 29.14           C  
ANISOU 1188  CA  GLY B  16     2621   5196   3253   -270   -568   -181       C  
ATOM   1189  C   GLY B  16       8.187  11.743  30.813  1.00 29.50           C  
ANISOU 1189  C   GLY B  16     2669   5131   3410   -372   -580   -296       C  
ATOM   1190  O   GLY B  16       8.906  12.541  31.385  1.00 32.47           O  
ANISOU 1190  O   GLY B  16     2967   5593   3778   -457   -658   -383       O  
ATOM   1191  N   LYS B  17       7.690  11.965  29.605  1.00 28.01           N  
ANISOU 1191  N   LYS B  17     2565   4755   3325   -368   -505   -292       N  
ATOM   1192  CA  LYS B  17       7.830  13.224  28.892  1.00 27.54           C  
ANISOU 1192  CA  LYS B  17     2524   4562   3377   -458   -505   -379       C  
ATOM   1193  C   LYS B  17       6.472  13.832  28.516  1.00 26.78           C  
ANISOU 1193  C   LYS B  17     2556   4312   3308   -456   -470   -463       C  
ATOM   1194  O   LYS B  17       6.420  14.863  27.859  1.00 27.13           O  
ANISOU 1194  O   LYS B  17     2633   4222   3455   -519   -463   -519       O  
ATOM   1195  CB  LYS B  17       8.568  12.942  27.580  1.00 27.86           C  
ANISOU 1195  CB  LYS B  17     2540   4525   3521   -448   -439   -265       C  
ATOM   1196  CG  LYS B  17       9.950  12.274  27.745  1.00 28.96           C  
ANISOU 1196  CG  LYS B  17     2540   4803   3658   -433   -456   -164       C  
ATOM   1197  CD  LYS B  17      10.682  12.217  26.400  1.00 28.76           C  
ANISOU 1197  CD  LYS B  17     2486   4701   3741   -435   -380    -77       C  
ATOM   1198  CE  LYS B  17      12.032  11.560  26.556  1.00 29.67           C  
ANISOU 1198  CE  LYS B  17     2452   4957   3865   -408   -391     20       C  
ATOM   1199  NZ  LYS B  17      12.646  11.309  25.255  1.00 26.60           N  
ANISOU 1199  NZ  LYS B  17     2037   4508   3562   -385   -297    108       N  
ATOM   1200  N   VAL B  18       5.373  13.148  28.840  1.00 26.09           N  
ANISOU 1200  N   VAL B  18     2536   4238   3140   -380   -442   -453       N  
ATOM   1201  CA  VAL B  18       4.033  13.585  28.445  1.00 24.87           C  
ANISOU 1201  CA  VAL B  18     2487   3950   3010   -363   -405   -517       C  
ATOM   1202  C   VAL B  18       3.503  14.568  29.473  1.00 25.98           C  
ANISOU 1202  C   VAL B  18     2638   4121   3111   -405   -458   -683       C  
ATOM   1203  O   VAL B  18       3.474  14.262  30.645  1.00 25.51           O  
ANISOU 1203  O   VAL B  18     2543   4219   2933   -395   -496   -721       O  
ATOM   1204  CB  VAL B  18       3.049  12.372  28.321  1.00 24.13           C  
ANISOU 1204  CB  VAL B  18     2451   3861   2857   -269   -348   -433       C  
ATOM   1205  CG1 VAL B  18       1.611  12.785  28.493  1.00 24.32           C  
ANISOU 1205  CG1 VAL B  18     2551   3826   2864   -252   -333   -521       C  
ATOM   1206  CG2 VAL B  18       3.232  11.670  26.931  1.00 22.81           C  
ANISOU 1206  CG2 VAL B  18     2312   3592   2761   -231   -280   -313       C  
ATOM   1207  N   ASN B  19       3.124  15.757  29.002  1.00 26.69           N  
ANISOU 1207  N   ASN B  19     2776   4060   3304   -450   -459   -779       N  
ATOM   1208  CA  ASN B  19       2.414  16.764  29.797  1.00 28.13           C  
ANISOU 1208  CA  ASN B  19     2988   4224   3478   -474   -493   -956       C  
ATOM   1209  C   ASN B  19       0.971  16.245  29.846  1.00 26.75           C  
ANISOU 1209  C   ASN B  19     2880   4040   3244   -385   -441   -949       C  
ATOM   1210  O   ASN B  19       0.286  16.257  28.827  1.00 24.48           O  
ANISOU 1210  O   ASN B  19     2653   3615   3033   -350   -394   -896       O  
ATOM   1211  CB  ASN B  19       2.506  18.164  29.120  1.00 28.55           C  
ANISOU 1211  CB  ASN B  19     3071   4081   3694   -542   -503  -1035       C  
ATOM   1212  CG  ASN B  19       1.797  19.269  29.918  1.00 32.80           C  
ANISOU 1212  CG  ASN B  19     3641   4572   4250   -560   -534  -1237       C  
ATOM   1213  OD1 ASN B  19       0.648  19.123  30.384  1.00 36.66           O  
ANISOU 1213  OD1 ASN B  19     4171   5087   4670   -490   -509  -1298       O  
ATOM   1214  ND2 ASN B  19       2.483  20.381  30.090  1.00 36.99           N  
ANISOU 1214  ND2 ASN B  19     4146   5031   4878   -656   -584  -1349       N  
ATOM   1215  N   VAL B  20       0.542  15.761  31.013  1.00 27.34           N  
ANISOU 1215  N   VAL B  20     2936   4276   3177   -353   -451   -993       N  
ATOM   1216  CA  VAL B  20      -0.750  15.044  31.156  1.00 26.91           C  
ANISOU 1216  CA  VAL B  20     2924   4248   3053   -274   -396   -959       C  
ATOM   1217  C   VAL B  20      -1.952  15.990  30.997  1.00 26.57           C  
ANISOU 1217  C   VAL B  20     2937   4084   3073   -253   -374  -1083       C  
ATOM   1218  O   VAL B  20      -2.915  15.656  30.299  1.00 24.13           O  
ANISOU 1218  O   VAL B  20     2672   3693   2801   -200   -324  -1024       O  
ATOM   1219  CB  VAL B  20      -0.823  14.313  32.519  1.00 28.27           C  
ANISOU 1219  CB  VAL B  20     3050   4644   3047   -252   -409   -959       C  
ATOM   1220  CG1 VAL B  20      -2.115  13.481  32.687  1.00 28.30           C  
ANISOU 1220  CG1 VAL B  20     3085   4684   2982   -182   -344   -902       C  
ATOM   1221  CG2 VAL B  20       0.399  13.413  32.702  1.00 29.02           C  
ANISOU 1221  CG2 VAL B  20     3079   4857   3090   -262   -438   -825       C  
ATOM   1222  N   ALA B  21      -1.868  17.174  31.607  1.00 27.24           N  
ANISOU 1222  N   ALA B  21     3017   4152   3182   -294   -413  -1258       N  
ATOM   1223  CA  ALA B  21      -2.962  18.143  31.608  1.00 27.93           C  
ANISOU 1223  CA  ALA B  21     3149   4126   3338   -263   -394  -1395       C  
ATOM   1224  C   ALA B  21      -3.309  18.572  30.199  1.00 28.26           C  
ANISOU 1224  C   ALA B  21     3243   3949   3546   -247   -370  -1324       C  
ATOM   1225  O   ALA B  21      -4.497  18.549  29.783  1.00 26.92           O  
ANISOU 1225  O   ALA B  21     3109   3714   3407   -180   -328  -1311       O  
ATOM   1226  CB  ALA B  21      -2.595  19.374  32.435  1.00 29.33           C  
ANISOU 1226  CB  ALA B  21     3311   4296   3536   -318   -444  -1606       C  
ATOM   1227  N   GLU B  22      -2.260  18.957  29.480  1.00 28.73           N  
ANISOU 1227  N   GLU B  22     3298   3911   3705   -312   -397  -1271       N  
ATOM   1228  CA  GLU B  22      -2.355  19.453  28.122  1.00 29.57           C  
ANISOU 1228  CA  GLU B  22     3450   3824   3962   -313   -380  -1189       C  
ATOM   1229  C   GLU B  22      -2.737  18.355  27.123  1.00 28.30           C  
ANISOU 1229  C   GLU B  22     3312   3669   3773   -260   -334  -1015       C  
ATOM   1230  O   GLU B  22      -3.647  18.553  26.286  1.00 27.02           O  
ANISOU 1230  O   GLU B  22     3195   3397   3674   -213   -309   -976       O  
ATOM   1231  CB  GLU B  22      -0.996  20.039  27.754  1.00 31.04           C  
ANISOU 1231  CB  GLU B  22     3608   3945   4238   -409   -416  -1168       C  
ATOM   1232  CG  GLU B  22      -0.893  20.728  26.387  1.00 34.76           C  
ANISOU 1232  CG  GLU B  22     4120   4219   4869   -430   -400  -1077       C  
ATOM   1233  CD  GLU B  22       0.399  21.561  26.283  1.00 41.42           C  
ANISOU 1233  CD  GLU B  22     4926   4995   5818   -543   -437  -1093       C  
ATOM   1234  OE1 GLU B  22       1.484  20.980  26.002  1.00 44.56           O  
ANISOU 1234  OE1 GLU B  22     5271   5474   6184   -590   -436   -991       O  
ATOM   1235  OE2 GLU B  22       0.333  22.798  26.501  1.00 45.83           O  
ANISOU 1235  OE2 GLU B  22     5500   5413   6499   -587   -465  -1211       O  
ATOM   1236  N   CYS B  23      -2.048  17.208  27.198  1.00 27.20           N  
ANISOU 1236  N   CYS B  23     3139   3655   3542   -266   -325   -914       N  
ATOM   1237  CA  CYS B  23      -2.336  16.123  26.262  1.00 26.49           C  
ANISOU 1237  CA  CYS B  23     3072   3562   3430   -221   -280   -769       C  
ATOM   1238  C   CYS B  23      -3.715  15.534  26.551  1.00 25.56           C  
ANISOU 1238  C   CYS B  23     2976   3486   3250   -153   -250   -780       C  
ATOM   1239  O   CYS B  23      -4.434  15.166  25.628  1.00 23.64           O  
ANISOU 1239  O   CYS B  23     2769   3181   3033   -117   -221   -710       O  
ATOM   1240  CB  CYS B  23      -1.278  15.001  26.317  1.00 26.53           C  
ANISOU 1240  CB  CYS B  23     3033   3677   3369   -232   -273   -664       C  
ATOM   1241  SG  CYS B  23       0.327  15.431  25.506  1.00 27.91           S  
ANISOU 1241  SG  CYS B  23     3171   3801   3631   -304   -285   -599       S  
ATOM   1242  N   GLY B  24      -4.056  15.443  27.845  1.00 25.68           N  
ANISOU 1242  N   GLY B  24     2962   3621   3174   -141   -258   -867       N  
ATOM   1243  CA  GLY B  24      -5.308  14.867  28.283  1.00 24.59           C  
ANISOU 1243  CA  GLY B  24     2827   3549   2968    -86   -222   -875       C  
ATOM   1244  C   GLY B  24      -6.470  15.702  27.795  1.00 24.85           C  
ANISOU 1244  C   GLY B  24     2892   3466   3086    -47   -212   -940       C  
ATOM   1245  O   GLY B  24      -7.390  15.172  27.204  1.00 23.50           O  
ANISOU 1245  O   GLY B  24     2735   3273   2923     -8   -183   -878       O  
ATOM   1246  N   ALA B  25      -6.398  17.020  28.015  1.00 25.73           N  
ANISOU 1246  N   ALA B  25     3008   3495   3272    -60   -239  -1064       N  
ATOM   1247  CA  ALA B  25      -7.427  17.956  27.575  1.00 26.27           C  
ANISOU 1247  CA  ALA B  25     3103   3435   3445    -12   -234  -1126       C  
ATOM   1248  C   ALA B  25      -7.681  17.872  26.081  1.00 26.42           C  
ANISOU 1248  C   ALA B  25     3157   3330   3550      4   -230   -996       C  
ATOM   1249  O   ALA B  25      -8.838  17.820  25.616  1.00 26.03           O  
ANISOU 1249  O   ALA B  25     3114   3250   3526     62   -214   -975       O  
ATOM   1250  CB  ALA B  25      -7.018  19.347  27.878  1.00 27.39           C  
ANISOU 1250  CB  ALA B  25     3253   3471   3684    -39   -267  -1259       C  
ATOM   1251  N   GLU B  26      -6.585  17.915  25.351  1.00 26.05           N  
ANISOU 1251  N   GLU B  26     3128   3227   3544    -50   -246   -915       N  
ATOM   1252  CA  GLU B  26      -6.585  17.915  23.902  1.00 26.70           C  
ANISOU 1252  CA  GLU B  26     3245   3207   3691    -47   -243   -790       C  
ATOM   1253  C   GLU B  26      -7.153  16.625  23.287  1.00 24.96           C  
ANISOU 1253  C   GLU B  26     3032   3056   3396    -15   -215   -689       C  
ATOM   1254  O   GLU B  26      -7.869  16.691  22.281  1.00 22.76           O  
ANISOU 1254  O   GLU B  26     2778   2717   3154     17   -215   -629       O  
ATOM   1255  CB  GLU B  26      -5.155  18.113  23.438  1.00 27.48           C  
ANISOU 1255  CB  GLU B  26     3346   3270   3826   -118   -255   -730       C  
ATOM   1256  CG  GLU B  26      -4.951  18.444  21.995  1.00 31.71           C  
ANISOU 1256  CG  GLU B  26     3916   3698   4435   -128   -250   -612       C  
ATOM   1257  CD  GLU B  26      -3.483  18.874  21.736  1.00 38.61           C  
ANISOU 1257  CD  GLU B  26     4775   4537   5360   -210   -257   -572       C  
ATOM   1258  OE1 GLU B  26      -2.946  18.492  20.643  1.00 43.60           O  
ANISOU 1258  OE1 GLU B  26     5417   5166   5983   -227   -233   -447       O  
ATOM   1259  OE2 GLU B  26      -2.895  19.581  22.633  1.00 40.55           O  
ANISOU 1259  OE2 GLU B  26     4991   4767   5648   -260   -284   -672       O  
ATOM   1260  N   ALA B  27      -6.830  15.479  23.898  1.00 23.81           N  
ANISOU 1260  N   ALA B  27     2862   3035   3149    -26   -195   -669       N  
ATOM   1261  CA  ALA B  27      -7.362  14.169  23.475  1.00 22.65           C  
ANISOU 1261  CA  ALA B  27     2720   2945   2942     -4   -165   -588       C  
ATOM   1262  C   ALA B  27      -8.882  14.116  23.596  1.00 22.93           C  
ANISOU 1262  C   ALA B  27     2746   2992   2974     44   -157   -624       C  
ATOM   1263  O   ALA B  27      -9.585  13.685  22.670  1.00 21.78           O  
ANISOU 1263  O   ALA B  27     2615   2821   2838     62   -153   -567       O  
ATOM   1264  CB  ALA B  27      -6.816  13.081  24.339  1.00 22.18           C  
ANISOU 1264  CB  ALA B  27     2632   3002   2794    -18   -146   -566       C  
ATOM   1265  N   LEU B  28      -9.367  14.514  24.773  1.00 23.49           N  
ANISOU 1265  N   LEU B  28     2784   3120   3022     63   -153   -722       N  
ATOM   1266  CA  LEU B  28     -10.775  14.470  25.059  1.00 24.33           C  
ANISOU 1266  CA  LEU B  28     2862   3261   3122    110   -135   -763       C  
ATOM   1267  C   LEU B  28     -11.529  15.530  24.220  1.00 24.22           C  
ANISOU 1267  C   LEU B  28     2860   3128   3214    154   -160   -782       C  
ATOM   1268  O   LEU B  28     -12.634  15.260  23.731  1.00 25.31           O  
ANISOU 1268  O   LEU B  28     2980   3272   3365    190   -156   -754       O  
ATOM   1269  CB  LEU B  28     -11.037  14.593  26.568  1.00 25.21           C  
ANISOU 1269  CB  LEU B  28     2929   3485   3163    122   -114   -865       C  
ATOM   1270  CG  LEU B  28     -12.501  14.331  27.006  1.00 26.97           C  
ANISOU 1270  CG  LEU B  28     3104   3782   3359    168    -77   -897       C  
ATOM   1271  CD1 LEU B  28     -12.920  12.954  26.688  1.00 25.57           C  
ANISOU 1271  CD1 LEU B  28     2915   3662   3137    149    -51   -787       C  
ATOM   1272  CD2 LEU B  28     -12.730  14.584  28.504  1.00 30.33           C  
ANISOU 1272  CD2 LEU B  28     3487   4336   3702    184    -47  -1010       C  
ATOM   1273  N   ALA B  29     -10.934  16.695  24.009  1.00 23.73           N  
ANISOU 1273  N   ALA B  29     2824   2957   3235    149   -188   -818       N  
ATOM   1274  CA  ALA B  29     -11.498  17.695  23.081  1.00 24.63           C  
ANISOU 1274  CA  ALA B  29     2956   2939   3464    192   -215   -800       C  
ATOM   1275  C   ALA B  29     -11.618  17.123  21.673  1.00 24.33           C  
ANISOU 1275  C   ALA B  29     2943   2881   3420    186   -228   -665       C  
ATOM   1276  O   ALA B  29     -12.646  17.270  21.018  1.00 25.67           O  
ANISOU 1276  O   ALA B  29     3101   3029   3623    235   -244   -633       O  
ATOM   1277  CB  ALA B  29     -10.652  18.991  23.057  1.00 24.85           C  
ANISOU 1277  CB  ALA B  29     3012   2833   3595    171   -240   -842       C  
ATOM   1278  N   ARG B  30     -10.571  16.466  21.209  1.00 23.81           N  
ANISOU 1278  N   ARG B  30     2906   2834   3306    130   -221   -591       N  
ATOM   1279  CA  ARG B  30     -10.597  15.831  19.892  1.00 23.46           C  
ANISOU 1279  CA  ARG B  30     2890   2790   3236    121   -226   -481       C  
ATOM   1280  C   ARG B  30     -11.701  14.772  19.772  1.00 22.84           C  
ANISOU 1280  C   ARG B  30     2787   2795   3098    141   -218   -472       C  
ATOM   1281  O   ARG B  30     -12.425  14.720  18.780  1.00 24.08           O  
ANISOU 1281  O   ARG B  30     2947   2942   3261    161   -242   -422       O  
ATOM   1282  CB  ARG B  30      -9.257  15.200  19.590  1.00 23.14           C  
ANISOU 1282  CB  ARG B  30     2873   2770   3148     64   -206   -424       C  
ATOM   1283  CG  ARG B  30      -8.435  16.044  18.695  1.00 24.99           C  
ANISOU 1283  CG  ARG B  30     3139   2917   3438     40   -219   -360       C  
ATOM   1284  CD  ARG B  30      -7.009  15.536  18.439  1.00 22.22           C  
ANISOU 1284  CD  ARG B  30     2798   2595   3052    -14   -191   -309       C  
ATOM   1285  NE  ARG B  30      -6.254  16.734  18.160  1.00 24.55           N  
ANISOU 1285  NE  ARG B  30     3100   2797   3429    -46   -204   -283       N  
ATOM   1286  CZ  ARG B  30      -6.113  17.327  16.979  1.00 23.96           C  
ANISOU 1286  CZ  ARG B  30     3055   2659   3391    -53   -209   -188       C  
ATOM   1287  NH1 ARG B  30      -6.567  16.783  15.875  1.00 24.64           N  
ANISOU 1287  NH1 ARG B  30     3166   2782   3415    -30   -204   -114       N  
ATOM   1288  NH2 ARG B  30      -5.440  18.469  16.910  1.00 25.65           N  
ANISOU 1288  NH2 ARG B  30     3271   2775   3701    -91   -219   -166       N  
ATOM   1289  N   LEU B  31     -11.808  13.909  20.762  1.00 22.63           N  
ANISOU 1289  N   LEU B  31     2730   2854   3013    128   -186   -512       N  
ATOM   1290  CA  LEU B  31     -12.842  12.888  20.774  1.00 22.09           C  
ANISOU 1290  CA  LEU B  31     2631   2858   2903    132   -173   -504       C  
ATOM   1291  C   LEU B  31     -14.229  13.506  20.569  1.00 22.41           C  
ANISOU 1291  C   LEU B  31     2630   2893   2993    185   -198   -530       C  
ATOM   1292  O   LEU B  31     -14.994  13.037  19.736  1.00 23.62           O  
ANISOU 1292  O   LEU B  31     2771   3063   3139    187   -218   -491       O  
ATOM   1293  CB  LEU B  31     -12.818  12.125  22.096  1.00 22.20           C  
ANISOU 1293  CB  LEU B  31     2611   2964   2861    116   -131   -538       C  
ATOM   1294  CG  LEU B  31     -13.744  10.912  22.103  1.00 22.55           C  
ANISOU 1294  CG  LEU B  31     2624   3073   2872    100   -109   -510       C  
ATOM   1295  CD1 LEU B  31     -13.030   9.782  21.385  1.00 23.32           C  
ANISOU 1295  CD1 LEU B  31     2765   3152   2944     57   -100   -441       C  
ATOM   1296  CD2 LEU B  31     -14.162  10.509  23.530  1.00 22.34           C  
ANISOU 1296  CD2 LEU B  31     2543   3146   2798     99    -66   -543       C  
ATOM   1297  N   LEU B  32     -14.537  14.563  21.318  1.00 22.42           N  
ANISOU 1297  N   LEU B  32     2604   2870   3045    231   -198   -605       N  
ATOM   1298  CA  LEU B  32     -15.853  15.223  21.271  1.00 22.12           C  
ANISOU 1298  CA  LEU B  32     2512   2826   3067    300   -214   -639       C  
ATOM   1299  C   LEU B  32     -16.106  15.924  19.946  1.00 22.24           C  
ANISOU 1299  C   LEU B  32     2548   2754   3148    334   -269   -569       C  
ATOM   1300  O   LEU B  32     -17.246  16.058  19.527  1.00 22.92           O  
ANISOU 1300  O   LEU B  32     2584   2859   3266    382   -295   -555       O  
ATOM   1301  CB  LEU B  32     -16.006  16.215  22.433  1.00 22.42           C  
ANISOU 1301  CB  LEU B  32     2520   2849   3148    349   -193   -754       C  
ATOM   1302  CG  LEU B  32     -15.951  15.564  23.813  1.00 22.59           C  
ANISOU 1302  CG  LEU B  32     2509   2993   3082    324   -139   -822       C  
ATOM   1303  CD1 LEU B  32     -15.982  16.590  24.988  1.00 22.42           C  
ANISOU 1303  CD1 LEU B  32     2465   2971   3083    369   -116   -961       C  
ATOM   1304  CD2 LEU B  32     -17.049  14.564  23.993  1.00 23.53           C  
ANISOU 1304  CD2 LEU B  32     2563   3226   3153    323   -110   -799       C  
ATOM   1305  N   ILE B  33     -15.036  16.355  19.287  1.00 22.16           N  
ANISOU 1305  N   ILE B  33     2603   2661   3155    306   -287   -514       N  
ATOM   1306  CA  ILE B  33     -15.140  17.068  18.038  1.00 22.52           C  
ANISOU 1306  CA  ILE B  33     2675   2629   3253    334   -335   -426       C  
ATOM   1307  C   ILE B  33     -15.123  16.149  16.791  1.00 22.10           C  
ANISOU 1307  C   ILE B  33     2646   2635   3116    296   -357   -332       C  
ATOM   1308  O   ILE B  33     -15.884  16.374  15.837  1.00 22.60           O  
ANISOU 1308  O   ILE B  33     2695   2706   3188    331   -405   -270       O  
ATOM   1309  CB  ILE B  33     -14.014  18.132  17.937  1.00 23.24           C  
ANISOU 1309  CB  ILE B  33     2820   2597   3416    319   -338   -406       C  
ATOM   1310  CG1 ILE B  33     -14.214  19.247  18.977  1.00 23.60           C  
ANISOU 1310  CG1 ILE B  33     2842   2559   3565    367   -331   -513       C  
ATOM   1311  CG2 ILE B  33     -14.023  18.780  16.536  1.00 23.78           C  
ANISOU 1311  CG2 ILE B  33     2919   2593   3523    338   -383   -278       C  
ATOM   1312  CD1 ILE B  33     -13.057  20.282  19.063  1.00 20.98           C  
ANISOU 1312  CD1 ILE B  33     2558   2094   3320    333   -333   -518       C  
ATOM   1313  N   VAL B  34     -14.232  15.151  16.769  1.00 21.53           N  
ANISOU 1313  N   VAL B  34     2609   2606   2965    228   -324   -324       N  
ATOM   1314  CA  VAL B  34     -14.109  14.239  15.605  1.00 20.89           C  
ANISOU 1314  CA  VAL B  34     2558   2577   2802    191   -335   -261       C  
ATOM   1315  C   VAL B  34     -15.287  13.204  15.578  1.00 21.28           C  
ANISOU 1315  C   VAL B  34     2560   2716   2810    185   -346   -292       C  
ATOM   1316  O   VAL B  34     -15.818  12.911  14.532  1.00 21.29           O  
ANISOU 1316  O   VAL B  34     2560   2757   2771    181   -387   -254       O  
ATOM   1317  CB  VAL B  34     -12.695  13.517  15.598  1.00 20.34           C  
ANISOU 1317  CB  VAL B  34     2539   2512   2678    131   -287   -249       C  
ATOM   1318  CG1 VAL B  34     -12.609  12.491  14.485  1.00 19.03           C  
ANISOU 1318  CG1 VAL B  34     2403   2400   2427     99   -288   -214       C  
ATOM   1319  CG2 VAL B  34     -11.530  14.534  15.494  1.00 19.90           C  
ANISOU 1319  CG2 VAL B  34     2518   2377   2667    123   -280   -209       C  
ATOM   1320  N   TYR B  35     -15.697  12.718  16.762  1.00 21.13           N  
ANISOU 1320  N   TYR B  35     2495   2734   2800    180   -311   -359       N  
ATOM   1321  CA  TYR B  35     -16.768  11.770  16.931  1.00 21.34           C  
ANISOU 1321  CA  TYR B  35     2465   2837   2805    161   -311   -386       C  
ATOM   1322  C   TYR B  35     -17.913  12.314  17.801  1.00 21.67           C  
ANISOU 1322  C   TYR B  35     2421   2911   2902    213   -310   -435       C  
ATOM   1323  O   TYR B  35     -18.027  11.962  18.975  1.00 21.62           O  
ANISOU 1323  O   TYR B  35     2381   2944   2891    204   -259   -482       O  
ATOM   1324  CB  TYR B  35     -16.142  10.533  17.565  1.00 21.01           C  
ANISOU 1324  CB  TYR B  35     2444   2820   2720    101   -254   -403       C  
ATOM   1325  CG  TYR B  35     -15.020   9.996  16.728  1.00 22.46           C  
ANISOU 1325  CG  TYR B  35     2702   2972   2859     64   -246   -366       C  
ATOM   1326  CD1 TYR B  35     -15.245   9.590  15.409  1.00 24.42           C  
ANISOU 1326  CD1 TYR B  35     2975   3235   3069     44   -282   -344       C  
ATOM   1327  CD2 TYR B  35     -13.720   9.922  17.226  1.00 19.31           C  
ANISOU 1327  CD2 TYR B  35     2343   2543   2451     52   -204   -358       C  
ATOM   1328  CE1 TYR B  35     -14.203   9.077  14.625  1.00 25.27           C  
ANISOU 1328  CE1 TYR B  35     3149   3325   3126     16   -263   -322       C  
ATOM   1329  CE2 TYR B  35     -12.707   9.459  16.467  1.00 20.74           C  
ANISOU 1329  CE2 TYR B  35     2579   2703   2597     28   -189   -326       C  
ATOM   1330  CZ  TYR B  35     -12.924   9.020  15.167  1.00 24.54           C  
ANISOU 1330  CZ  TYR B  35     3089   3197   3038     12   -212   -312       C  
ATOM   1331  OH  TYR B  35     -11.861   8.518  14.441  1.00 20.81           O  
ANISOU 1331  OH  TYR B  35     2670   2713   2523     -7   -183   -292       O  
ATOM   1332  N   PRO B  36     -18.778  13.185  17.230  1.00 23.25           N  
ANISOU 1332  N   PRO B  36     2580   3102   3151    275   -363   -417       N  
ATOM   1333  CA  PRO B  36     -19.553  14.039  18.157  1.00 23.68           C  
ANISOU 1333  CA  PRO B  36     2562   3156   3277    349   -349   -474       C  
ATOM   1334  C   PRO B  36     -20.657  13.354  18.932  1.00 24.44           C  
ANISOU 1334  C   PRO B  36     2561   3357   3366    342   -317   -521       C  
ATOM   1335  O   PRO B  36     -21.217  13.947  19.862  1.00 25.52           O  
ANISOU 1335  O   PRO B  36     2636   3514   3547    401   -285   -583       O  
ATOM   1336  CB  PRO B  36     -20.145  15.138  17.253  1.00 25.08           C  
ANISOU 1336  CB  PRO B  36     2720   3287   3524    427   -416   -424       C  
ATOM   1337  CG  PRO B  36     -19.729  14.814  15.852  1.00 24.72           C  
ANISOU 1337  CG  PRO B  36     2732   3239   3420    387   -468   -335       C  
ATOM   1338  CD  PRO B  36     -18.639  13.789  15.893  1.00 23.11           C  
ANISOU 1338  CD  PRO B  36     2601   3045   3136    297   -426   -341       C  
ATOM   1339  N   TRP B  37     -21.000  12.134  18.557  1.00 24.08           N  
ANISOU 1339  N   TRP B  37     2499   3379   3271    270   -321   -498       N  
ATOM   1340  CA  TRP B  37     -22.010  11.418  19.320  1.00 24.53           C  
ANISOU 1340  CA  TRP B  37     2459   3533   3328    246   -284   -530       C  
ATOM   1341  C   TRP B  37     -21.455  11.120  20.726  1.00 23.93           C  
ANISOU 1341  C   TRP B  37     2394   3478   3220    227   -199   -569       C  
ATOM   1342  O   TRP B  37     -22.226  10.848  21.648  1.00 25.44           O  
ANISOU 1342  O   TRP B  37     2501   3755   3410    227   -150   -599       O  
ATOM   1343  CB  TRP B  37     -22.427  10.135  18.592  1.00 24.57           C  
ANISOU 1343  CB  TRP B  37     2449   3585   3300    157   -309   -500       C  
ATOM   1344  CG  TRP B  37     -21.261   9.215  18.391  1.00 23.78           C  
ANISOU 1344  CG  TRP B  37     2452   3436   3148     83   -285   -481       C  
ATOM   1345  CD1 TRP B  37     -20.754   8.359  19.305  1.00 24.33           C  
ANISOU 1345  CD1 TRP B  37     2540   3509   3194     32   -217   -482       C  
ATOM   1346  CD2 TRP B  37     -20.414   9.135  17.254  1.00 23.54           C  
ANISOU 1346  CD2 TRP B  37     2514   3348   3081     64   -325   -451       C  
ATOM   1347  NE1 TRP B  37     -19.658   7.710  18.807  1.00 26.20           N  
ANISOU 1347  NE1 TRP B  37     2872   3685   3397    -12   -212   -459       N  
ATOM   1348  CE2 TRP B  37     -19.428   8.158  17.537  1.00 24.51           C  
ANISOU 1348  CE2 TRP B  37     2705   3437   3171      5   -274   -447       C  
ATOM   1349  CE3 TRP B  37     -20.412   9.744  15.998  1.00 22.91           C  
ANISOU 1349  CE3 TRP B  37     2462   3253   2989     93   -396   -420       C  
ATOM   1350  CZ2 TRP B  37     -18.450   7.791  16.619  1.00 23.05           C  
ANISOU 1350  CZ2 TRP B  37     2609   3203   2946    -22   -285   -428       C  
ATOM   1351  CZ3 TRP B  37     -19.424   9.380  15.096  1.00 21.73           C  
ANISOU 1351  CZ3 TRP B  37     2406   3067   2784     58   -405   -396       C  
ATOM   1352  CH2 TRP B  37     -18.474   8.405  15.403  1.00 20.89           C  
ANISOU 1352  CH2 TRP B  37     2361   2927   2650      2   -347   -409       C  
ATOM   1353  N   THR B  38     -20.132  11.202  20.903  1.00 22.45           N  
ANISOU 1353  N   THR B  38     2301   3227   3001    211   -183   -564       N  
ATOM   1354  CA  THR B  38     -19.536  11.049  22.234  1.00 21.79           C  
ANISOU 1354  CA  THR B  38     2226   3177   2877    201   -117   -598       C  
ATOM   1355  C   THR B  38     -19.976  12.141  23.173  1.00 23.48           C  
ANISOU 1355  C   THR B  38     2387   3418   3116    277    -92   -679       C  
ATOM   1356  O   THR B  38     -19.964  11.929  24.373  1.00 24.29           O  
ANISOU 1356  O   THR B  38     2460   3599   3168    271    -33   -718       O  
ATOM   1357  CB  THR B  38     -17.983  10.929  22.223  1.00 20.63           C  
ANISOU 1357  CB  THR B  38     2178   2968   2694    169   -113   -575       C  
ATOM   1358  OG1 THR B  38     -17.365  12.113  21.697  1.00 20.69           O  
ANISOU 1358  OG1 THR B  38     2235   2884   2743    211   -153   -588       O  
ATOM   1359  CG2 THR B  38     -17.551   9.737  21.370  1.00 20.05           C  
ANISOU 1359  CG2 THR B  38     2151   2871   2595    101   -123   -508       C  
ATOM   1360  N   GLN B  39     -20.400  13.293  22.650  1.00 24.26           N  
ANISOU 1360  N   GLN B  39     2471   3455   3291    353   -134   -706       N  
ATOM   1361  CA  GLN B  39     -20.828  14.398  23.512  1.00 25.83           C  
ANISOU 1361  CA  GLN B  39     2623   3658   3533    438   -107   -802       C  
ATOM   1362  C   GLN B  39     -22.035  14.056  24.405  1.00 27.19           C  
ANISOU 1362  C   GLN B  39     2679   3967   3686    460    -48   -848       C  
ATOM   1363  O   GLN B  39     -22.204  14.653  25.450  1.00 28.21           O  
ANISOU 1363  O   GLN B  39     2772   4138   3808    512      2   -943       O  
ATOM   1364  CB  GLN B  39     -21.150  15.654  22.690  1.00 26.66           C  
ANISOU 1364  CB  GLN B  39     2728   3652   3748    524   -164   -804       C  
ATOM   1365  CG  GLN B  39     -19.975  16.284  21.964  1.00 25.62           C  
ANISOU 1365  CG  GLN B  39     2703   3384   3649    513   -209   -765       C  
ATOM   1366  CD  GLN B  39     -20.418  17.302  20.893  1.00 26.46           C  
ANISOU 1366  CD  GLN B  39     2806   3387   3860    588   -275   -715       C  
ATOM   1367  OE1 GLN B  39     -19.734  17.489  19.859  1.00 26.41           O  
ANISOU 1367  OE1 GLN B  39     2871   3301   3863    563   -322   -628       O  
ATOM   1368  NE2 GLN B  39     -21.560  17.951  21.129  1.00 22.79           N  
ANISOU 1368  NE2 GLN B  39     2253   2933   3473    683   -274   -759       N  
ATOM   1369  N   ARG B  40     -22.851  13.091  24.002  1.00 27.95           N  
ANISOU 1369  N   ARG B  40     2713   4136   3772    414    -51   -785       N  
ATOM   1370  CA  ARG B  40     -24.063  12.706  24.752  1.00 29.15           C  
ANISOU 1370  CA  ARG B  40     2738   4426   3913    423      7   -810       C  
ATOM   1371  C   ARG B  40     -23.753  12.104  26.118  1.00 29.26           C  
ANISOU 1371  C   ARG B  40     2744   4545   3829    379     95   -832       C  
ATOM   1372  O   ARG B  40     -24.563  12.197  27.039  1.00 29.69           O  
ANISOU 1372  O   ARG B  40     2701   4718   3862    413    163   -882       O  
ATOM   1373  CB  ARG B  40     -24.896  11.741  23.916  1.00 29.98           C  
ANISOU 1373  CB  ARG B  40     2782   4574   4037    360    -26   -732       C  
ATOM   1374  CG  ARG B  40     -26.145  11.181  24.564  1.00 31.87           C  
ANISOU 1374  CG  ARG B  40     2878   4956   4273    342     32   -735       C  
ATOM   1375  CD  ARG B  40     -26.839  10.230  23.591  1.00 33.70           C  
ANISOU 1375  CD  ARG B  40     3060   5209   4534    261    -19   -664       C  
ATOM   1376  NE  ARG B  40     -27.901   9.495  24.270  1.00 38.29           N  
ANISOU 1376  NE  ARG B  40     3508   5927   5115    212     45   -651       N  
ATOM   1377  CZ  ARG B  40     -27.723   8.387  24.984  1.00 38.34           C  
ANISOU 1377  CZ  ARG B  40     3516   5983   5067    113    114   -606       C  
ATOM   1378  NH1 ARG B  40     -26.531   7.835  25.100  1.00 39.57           N  
ANISOU 1378  NH1 ARG B  40     3799   6065   5169     59    122   -571       N  
ATOM   1379  NH2 ARG B  40     -28.755   7.814  25.581  1.00 39.85           N  
ANISOU 1379  NH2 ARG B  40     3574   6301   5267     69    176   -585       N  
ATOM   1380  N   PHE B  41     -22.562  11.535  26.283  1.00 28.18           N  
ANISOU 1380  N   PHE B  41     2705   4375   3627    313     98   -792       N  
ATOM   1381  CA  PHE B  41     -22.182  11.050  27.602  1.00 28.39           C  
ANISOU 1381  CA  PHE B  41     2727   4510   3552    282    172   -801       C  
ATOM   1382  C   PHE B  41     -21.711  12.159  28.547  1.00 29.37           C  
ANISOU 1382  C   PHE B  41     2868   4653   3638    350    196   -920       C  
ATOM   1383  O   PHE B  41     -21.371  11.846  29.669  1.00 30.20           O  
ANISOU 1383  O   PHE B  41     2968   4867   3638    329    251   -935       O  
ATOM   1384  CB  PHE B  41     -21.057  10.033  27.514  1.00 27.23           C  
ANISOU 1384  CB  PHE B  41     2667   4329   3352    197    164   -711       C  
ATOM   1385  CG  PHE B  41     -21.411   8.824  26.764  1.00 28.14           C  
ANISOU 1385  CG  PHE B  41     2774   4422   3496    120    151   -611       C  
ATOM   1386  CD1 PHE B  41     -22.204   7.857  27.344  1.00 32.44           C  
ANISOU 1386  CD1 PHE B  41     3240   5070   4018     66    211   -557       C  
ATOM   1387  CD2 PHE B  41     -20.964   8.644  25.478  1.00 27.64           C  
ANISOU 1387  CD2 PHE B  41     2780   4238   3484     96     84   -576       C  
ATOM   1388  CE1 PHE B  41     -22.564   6.733  26.621  1.00 34.43           C  
ANISOU 1388  CE1 PHE B  41     3484   5283   4316    -16    196   -478       C  
ATOM   1389  CE2 PHE B  41     -21.287   7.528  24.780  1.00 30.60           C  
ANISOU 1389  CE2 PHE B  41     3152   4591   3886     22     71   -509       C  
ATOM   1390  CZ  PHE B  41     -22.076   6.570  25.330  1.00 31.09           C  
ANISOU 1390  CZ  PHE B  41     3138   4733   3943    -37    123   -464       C  
ATOM   1391  N   PHE B  42     -21.664  13.419  28.115  1.00 29.94           N  
ANISOU 1391  N   PHE B  42     2962   4619   3793    428    154  -1003       N  
ATOM   1392  CA  PHE B  42     -21.072  14.485  28.920  1.00 31.16           C  
ANISOU 1392  CA  PHE B  42     3150   4760   3932    480    167  -1131       C  
ATOM   1393  C   PHE B  42     -21.974  15.720  28.952  1.00 33.30           C  
ANISOU 1393  C   PHE B  42     3361   4994   4299    593    175  -1247       C  
ATOM   1394  O   PHE B  42     -21.518  16.866  28.891  1.00 34.63           O  
ANISOU 1394  O   PHE B  42     3577   5042   4537    647    146  -1338       O  
ATOM   1395  CB  PHE B  42     -19.673  14.872  28.366  1.00 30.25           C  
ANISOU 1395  CB  PHE B  42     3151   4502   3843    449    102  -1117       C  
ATOM   1396  CG  PHE B  42     -18.642  13.728  28.359  1.00 28.78           C  
ANISOU 1396  CG  PHE B  42     3022   4343   3571    353     96  -1011       C  
ATOM   1397  CD1 PHE B  42     -17.966  13.368  29.520  1.00 28.96           C  
ANISOU 1397  CD1 PHE B  42     3052   4476   3474    319    132  -1032       C  
ATOM   1398  CD2 PHE B  42     -18.352  13.053  27.184  1.00 25.51           C  
ANISOU 1398  CD2 PHE B  42     2651   3846   3194    305     52   -894       C  
ATOM   1399  CE1 PHE B  42     -17.015  12.369  29.503  1.00 28.90           C  
ANISOU 1399  CE1 PHE B  42     3090   4485   3406    247    123   -927       C  
ATOM   1400  CE2 PHE B  42     -17.415  12.053  27.147  1.00 26.56           C  
ANISOU 1400  CE2 PHE B  42     2835   3989   3269    234     51   -808       C  
ATOM   1401  CZ  PHE B  42     -16.732  11.698  28.318  1.00 26.92           C  
ANISOU 1401  CZ  PHE B  42     2883   4134   3212    208     86   -817       C  
ATOM   1402  N   THR B  43     -23.267  15.504  29.086  1.00 34.79           N  
ANISOU 1402  N   THR B  43     3436   5281   4501    632    218  -1247       N  
ATOM   1403  CA  THR B  43     -24.205  16.608  29.149  1.00 36.79           C  
ANISOU 1403  CA  THR B  43     3614   5510   4854    754    233  -1353       C  
ATOM   1404  C   THR B  43     -24.016  17.474  30.440  1.00 37.31           C  
ANISOU 1404  C   THR B  43     3677   5625   4873    818    298  -1535       C  
ATOM   1405  O   THR B  43     -24.240  18.681  30.431  1.00 36.99           O  
ANISOU 1405  O   THR B  43     3631   5483   4939    920    292  -1653       O  
ATOM   1406  CB  THR B  43     -25.643  16.046  28.982  1.00 38.05           C  
ANISOU 1406  CB  THR B  43     3634   5788   5035    773    266  -1299       C  
ATOM   1407  OG1 THR B  43     -25.913  15.136  30.046  1.00 43.05           O  
ANISOU 1407  OG1 THR B  43     4207   6614   5537    715    355  -1292       O  
ATOM   1408  CG2 THR B  43     -25.791  15.251  27.653  1.00 38.31           C  
ANISOU 1408  CG2 THR B  43     3676   5767   5113    703    188  -1144       C  
ATOM   1409  N   SER B  44     -23.555  16.867  31.531  1.00 37.43           N  
ANISOU 1409  N   SER B  44     3701   5790   4731    756    356  -1558       N  
ATOM   1410  CA  SER B  44     -23.325  17.616  32.784  1.00 38.94           C  
ANISOU 1410  CA  SER B  44     3891   6057   4847    804    413  -1742       C  
ATOM   1411  C   SER B  44     -22.138  18.573  32.722  1.00 38.92           C  
ANISOU 1411  C   SER B  44     4003   5894   4892    805    352  -1840       C  
ATOM   1412  O   SER B  44     -21.890  19.295  33.675  1.00 40.57           O  
ANISOU 1412  O   SER B  44     4220   6141   5053    840    386  -2014       O  
ATOM   1413  CB  SER B  44     -23.099  16.653  33.952  1.00 39.03           C  
ANISOU 1413  CB  SER B  44     3882   6295   4654    731    483  -1718       C  
ATOM   1414  OG  SER B  44     -21.781  16.134  33.937  1.00 38.29           O  
ANISOU 1414  OG  SER B  44     3889   6174   4487    635    430  -1643       O  
ATOM   1415  N   PHE B  45     -21.395  18.554  31.612  1.00 38.19           N  
ANISOU 1415  N   PHE B  45     3993   5629   4887    758    264  -1731       N  
ATOM   1416  CA  PHE B  45     -20.197  19.390  31.421  1.00 37.89           C  
ANISOU 1416  CA  PHE B  45     4060   5429   4909    737    203  -1793       C  
ATOM   1417  C   PHE B  45     -20.566  20.730  30.822  1.00 38.59           C  
ANISOU 1417  C   PHE B  45     4156   5317   5190    836    172  -1873       C  
ATOM   1418  O   PHE B  45     -19.680  21.530  30.536  1.00 37.97           O  
ANISOU 1418  O   PHE B  45     4157   5072   5197    821    121  -1915       O  
ATOM   1419  CB  PHE B  45     -19.149  18.699  30.495  1.00 36.77           C  
ANISOU 1419  CB  PHE B  45     3999   5208   4764    637    133  -1624       C  
ATOM   1420  CG  PHE B  45     -18.338  17.585  31.144  1.00 36.46           C  
ANISOU 1420  CG  PHE B  45     3980   5316   4556    539    147  -1560       C  
ATOM   1421  CD1 PHE B  45     -18.675  17.027  32.377  1.00 39.27           C  
ANISOU 1421  CD1 PHE B  45     4279   5884   4759    532    218  -1603       C  
ATOM   1422  CD2 PHE B  45     -17.227  17.085  30.488  1.00 37.94           C  
ANISOU 1422  CD2 PHE B  45     4240   5434   4742    459     92  -1443       C  
ATOM   1423  CE1 PHE B  45     -17.902  16.001  32.943  1.00 37.85           C  
ANISOU 1423  CE1 PHE B  45     4117   5833   4432    449    225  -1518       C  
ATOM   1424  CE2 PHE B  45     -16.479  16.046  31.032  1.00 36.49           C  
ANISOU 1424  CE2 PHE B  45     4069   5373   4422    383    102  -1369       C  
ATOM   1425  CZ  PHE B  45     -16.815  15.518  32.270  1.00 36.88           C  
ANISOU 1425  CZ  PHE B  45     4064   5623   4325    380    165  -1402       C  
ATOM   1426  N   GLY B  46     -21.860  20.977  30.613  1.00 39.61           N  
ANISOU 1426  N   GLY B  46     4196   5456   5399    936    203  -1884       N  
ATOM   1427  CA  GLY B  46     -22.322  22.265  30.091  1.00 41.03           C  
ANISOU 1427  CA  GLY B  46     4370   5444   5775   1052    178  -1951       C  
ATOM   1428  C   GLY B  46     -22.199  22.488  28.582  1.00 40.35           C  
ANISOU 1428  C   GLY B  46     4328   5174   5831   1053     89  -1788       C  
ATOM   1429  O   GLY B  46     -22.818  21.793  27.785  1.00 40.08           O  
ANISOU 1429  O   GLY B  46     4248   5189   5793   1047     66  -1640       O  
ATOM   1430  N   ASN B  47     -21.417  23.485  28.191  1.00 41.07           N  
ANISOU 1430  N   ASN B  47     4504   5055   6044   1058     40  -1816       N  
ATOM   1431  CA  ASN B  47     -21.385  23.945  26.804  1.00 40.93           C  
ANISOU 1431  CA  ASN B  47     4524   4854   6175   1081    -37  -1668       C  
ATOM   1432  C   ASN B  47     -20.394  23.196  25.891  1.00 38.91           C  
ANISOU 1432  C   ASN B  47     4347   4585   5853    957    -96  -1494       C  
ATOM   1433  O   ASN B  47     -19.175  23.453  25.917  1.00 38.85           O  
ANISOU 1433  O   ASN B  47     4426   4490   5845    879   -118  -1505       O  
ATOM   1434  CB  ASN B  47     -21.063  25.432  26.744  1.00 42.32           C  
ANISOU 1434  CB  ASN B  47     4751   4790   6539   1148    -58  -1762       C  
ATOM   1435  CG  ASN B  47     -21.167  25.977  25.340  1.00 43.62           C  
ANISOU 1435  CG  ASN B  47     4942   4773   6860   1189   -132  -1591       C  
ATOM   1436  OD1 ASN B  47     -21.609  25.267  24.422  1.00 42.47           O  
ANISOU 1436  OD1 ASN B  47     4765   4701   6670   1179   -169  -1420       O  
ATOM   1437  ND2 ASN B  47     -20.762  27.235  25.152  1.00 43.71           N  
ANISOU 1437  ND2 ASN B  47     5009   4546   7051   1230   -157  -1633       N  
ATOM   1438  N   LEU B  48     -20.956  22.315  25.063  1.00 37.15           N  
ANISOU 1438  N   LEU B  48     4085   4446   5583    942   -120  -1342       N  
ATOM   1439  CA  LEU B  48     -20.260  21.561  24.057  1.00 34.53           C  
ANISOU 1439  CA  LEU B  48     3815   4113   5194    846   -171  -1179       C  
ATOM   1440  C   LEU B  48     -20.797  21.943  22.679  1.00 35.14           C  
ANISOU 1440  C   LEU B  48     3884   4096   5373    901   -238  -1040       C  
ATOM   1441  O   LEU B  48     -20.773  21.140  21.716  1.00 34.19           O  
ANISOU 1441  O   LEU B  48     3774   4028   5188    847   -278   -902       O  
ATOM   1442  CB  LEU B  48     -20.539  20.080  24.307  1.00 33.20           C  
ANISOU 1442  CB  LEU B  48     3604   4142   4869    776   -141  -1135       C  
ATOM   1443  CG  LEU B  48     -20.405  19.613  25.750  1.00 31.11           C  
ANISOU 1443  CG  LEU B  48     3314   4017   4490    745    -67  -1254       C  
ATOM   1444  CD1 LEU B  48     -20.994  18.223  25.877  1.00 27.47           C  
ANISOU 1444  CD1 LEU B  48     2792   3731   3913    693    -36  -1183       C  
ATOM   1445  CD2 LEU B  48     -18.936  19.686  26.263  1.00 25.10           C  
ANISOU 1445  CD2 LEU B  48     2642   3221   3673    665    -68  -1297       C  
ATOM   1446  N   SER B  49     -21.267  23.178  22.576  1.00 37.31           N  
ANISOU 1446  N   SER B  49     4139   4230   5805   1012   -252  -1076       N  
ATOM   1447  CA  SER B  49     -22.023  23.624  21.412  1.00 38.27           C  
ANISOU 1447  CA  SER B  49     4227   4284   6030   1094   -315   -944       C  
ATOM   1448  C   SER B  49     -21.148  23.766  20.193  1.00 38.48           C  
ANISOU 1448  C   SER B  49     4346   4206   6070   1034   -380   -783       C  
ATOM   1449  O   SER B  49     -21.648  23.731  19.091  1.00 39.77           O  
ANISOU 1449  O   SER B  49     4488   4376   6248   1066   -440   -640       O  
ATOM   1450  CB  SER B  49     -22.797  24.941  21.684  1.00 40.53           C  
ANISOU 1450  CB  SER B  49     4462   4436   6502   1248   -308  -1023       C  
ATOM   1451  OG  SER B  49     -21.962  26.101  21.853  1.00 40.02           O  
ANISOU 1451  OG  SER B  49     4482   4154   6571   1259   -309  -1079       O  
ATOM   1452  N   SER B  50     -19.845  23.929  20.376  1.00 38.55           N  
ANISOU 1452  N   SER B  50     4449   4133   6065    946   -369   -803       N  
ATOM   1453  CA  SER B  50     -18.957  24.186  19.247  1.00 38.82           C  
ANISOU 1453  CA  SER B  50     4566   4063   6121    891   -418   -649       C  
ATOM   1454  C   SER B  50     -17.530  23.659  19.521  1.00 37.46           C  
ANISOU 1454  C   SER B  50     4470   3912   5852    757   -393   -667       C  
ATOM   1455  O   SER B  50     -17.200  23.331  20.648  1.00 37.72           O  
ANISOU 1455  O   SER B  50     4497   4007   5826    718   -346   -804       O  
ATOM   1456  CB  SER B  50     -18.927  25.693  18.994  1.00 40.41           C  
ANISOU 1456  CB  SER B  50     4793   4037   6525    970   -442   -630       C  
ATOM   1457  OG  SER B  50     -18.254  26.348  20.078  1.00 41.72           O  
ANISOU 1457  OG  SER B  50     4994   4096   6763    949   -398   -796       O  
ATOM   1458  N   ALA B  51     -16.699  23.568  18.489  1.00 37.03           N  
ANISOU 1458  N   ALA B  51     4478   3819   5773    690   -423   -524       N  
ATOM   1459  CA  ALA B  51     -15.308  23.161  18.662  1.00 36.12           C  
ANISOU 1459  CA  ALA B  51     4423   3715   5585    572   -400   -529       C  
ATOM   1460  C   ALA B  51     -14.590  24.115  19.618  1.00 36.58           C  
ANISOU 1460  C   ALA B  51     4506   3642   5749    554   -379   -658       C  
ATOM   1461  O   ALA B  51     -13.896  23.672  20.532  1.00 36.35           O  
ANISOU 1461  O   ALA B  51     4482   3683   5645    487   -347   -762       O  
ATOM   1462  CB  ALA B  51     -14.593  23.103  17.326  1.00 35.68           C  
ANISOU 1462  CB  ALA B  51     4421   3630   5506    519   -430   -352       C  
ATOM   1463  N   SER B  52     -14.769  25.416  19.435  1.00 37.90           N  
ANISOU 1463  N   SER B  52     4687   3621   6094    613   -399   -654       N  
ATOM   1464  CA  SER B  52     -14.228  26.369  20.408  1.00 39.32           C  
ANISOU 1464  CA  SER B  52     4886   3664   6390    598   -380   -810       C  
ATOM   1465  C   SER B  52     -14.779  26.109  21.822  1.00 39.49           C  
ANISOU 1465  C   SER B  52     4858   3793   6355    636   -338  -1022       C  
ATOM   1466  O   SER B  52     -14.028  26.083  22.801  1.00 39.31           O  
ANISOU 1466  O   SER B  52     4847   3799   6289    569   -316  -1159       O  
ATOM   1467  CB  SER B  52     -14.536  27.807  19.984  1.00 41.56           C  
ANISOU 1467  CB  SER B  52     5187   3706   6898    674   -405   -776       C  
ATOM   1468  OG  SER B  52     -15.941  28.017  19.868  1.00 42.51           O  
ANISOU 1468  OG  SER B  52     5250   3829   7073    814   -414   -775       O  
ATOM   1469  N   ALA B  53     -16.090  25.912  21.938  1.00 39.77           N  
ANISOU 1469  N   ALA B  53     4829   3903   6380    742   -328  -1046       N  
ATOM   1470  CA  ALA B  53     -16.687  25.742  23.264  1.00 40.47           C  
ANISOU 1470  CA  ALA B  53     4861   4099   6415    786   -277  -1240       C  
ATOM   1471  C   ALA B  53     -16.065  24.526  23.925  1.00 39.11           C  
ANISOU 1471  C   ALA B  53     4690   4127   6044    684   -249  -1272       C  
ATOM   1472  O   ALA B  53     -15.688  24.563  25.102  1.00 39.68           O  
ANISOU 1472  O   ALA B  53     4758   4256   6062    655   -217  -1432       O  
ATOM   1473  CB  ALA B  53     -18.223  25.596  23.185  1.00 40.41           C  
ANISOU 1473  CB  ALA B  53     4766   4166   6420    910   -266  -1235       C  
ATOM   1474  N   ILE B  54     -15.918  23.461  23.143  1.00 37.81           N  
ANISOU 1474  N   ILE B  54     4530   4064   5771    631   -265  -1117       N  
ATOM   1475  CA  ILE B  54     -15.412  22.213  23.658  1.00 36.45           C  
ANISOU 1475  CA  ILE B  54     4355   4068   5425    547   -239  -1119       C  
ATOM   1476  C   ILE B  54     -13.974  22.372  24.169  1.00 36.79           C  
ANISOU 1476  C   ILE B  54     4449   4085   5446    452   -241  -1171       C  
ATOM   1477  O   ILE B  54     -13.654  21.940  25.283  1.00 37.71           O  
ANISOU 1477  O   ILE B  54     4547   4322   5458    417   -212  -1276       O  
ATOM   1478  CB  ILE B  54     -15.451  21.106  22.570  1.00 35.31           C  
ANISOU 1478  CB  ILE B  54     4217   4001   5197    508   -258   -947       C  
ATOM   1479  CG1 ILE B  54     -16.902  20.725  22.286  1.00 35.69           C  
ANISOU 1479  CG1 ILE B  54     4196   4127   5238    583   -258   -917       C  
ATOM   1480  CG2 ILE B  54     -14.607  19.902  23.015  1.00 31.92           C  
ANISOU 1480  CG2 ILE B  54     3802   3706   4620    415   -234   -935       C  
ATOM   1481  CD1 ILE B  54     -17.088  20.046  20.987  1.00 34.61           C  
ANISOU 1481  CD1 ILE B  54     4069   4019   5064    562   -296   -761       C  
ATOM   1482  N   ILE B  55     -13.114  22.993  23.380  1.00 36.56           N  
ANISOU 1482  N   ILE B  55     4472   3910   5508    408   -275  -1093       N  
ATOM   1483  CA  ILE B  55     -11.684  23.084  23.739  1.00 37.57           C  
ANISOU 1483  CA  ILE B  55     4635   4022   5618    305   -282  -1123       C  
ATOM   1484  C   ILE B  55     -11.419  23.889  25.047  1.00 39.10           C  
ANISOU 1484  C   ILE B  55     4820   4186   5849    297   -274  -1332       C  
ATOM   1485  O   ILE B  55     -10.627  23.492  25.908  1.00 39.87           O  
ANISOU 1485  O   ILE B  55     4909   4392   5846    228   -269  -1408       O  
ATOM   1486  CB  ILE B  55     -10.879  23.688  22.558  1.00 37.92           C  
ANISOU 1486  CB  ILE B  55     4728   3909   5769    257   -313   -987       C  
ATOM   1487  CG1 ILE B  55     -10.682  22.644  21.457  1.00 35.54           C  
ANISOU 1487  CG1 ILE B  55     4439   3695   5370    229   -315   -807       C  
ATOM   1488  CG2 ILE B  55      -9.529  24.236  23.017  1.00 39.98           C  
ANISOU 1488  CG2 ILE B  55     5010   4105   6075    159   -324  -1050       C  
ATOM   1489  CD1 ILE B  55     -10.669  23.244  20.026  1.00 35.04           C  
ANISOU 1489  CD1 ILE B  55     4411   3500   5401    239   -342   -643       C  
ATOM   1490  N   GLY B  56     -12.099  25.008  25.199  1.00 40.38           N  
ANISOU 1490  N   GLY B  56     4981   4206   6155    373   -274  -1429       N  
ATOM   1491  CA  GLY B  56     -11.984  25.813  26.412  1.00 41.51           C  
ANISOU 1491  CA  GLY B  56     5118   4315   6338    377   -263  -1655       C  
ATOM   1492  C   GLY B  56     -13.001  25.504  27.489  1.00 41.05           C  
ANISOU 1492  C   GLY B  56     5004   4411   6181    456   -216  -1803       C  
ATOM   1493  O   GLY B  56     -13.096  26.246  28.457  1.00 43.37           O  
ANISOU 1493  O   GLY B  56     5291   4678   6509    481   -200  -2008       O  
ATOM   1494  N   ASN B  57     -13.792  24.450  27.321  1.00 38.74           N  
ANISOU 1494  N   ASN B  57     4671   4278   5772    496   -190  -1708       N  
ATOM   1495  CA  ASN B  57     -14.709  24.038  28.381  1.00 38.18           C  
ANISOU 1495  CA  ASN B  57     4537   4383   5588    556   -135  -1829       C  
ATOM   1496  C   ASN B  57     -13.844  23.489  29.514  1.00 37.16           C  
ANISOU 1496  C   ASN B  57     4406   4424   5289    471   -124  -1919       C  
ATOM   1497  O   ASN B  57     -13.013  22.633  29.280  1.00 35.30           O  
ANISOU 1497  O   ASN B  57     4188   4263   4960    386   -144  -1799       O  
ATOM   1498  CB  ASN B  57     -15.700  22.991  27.862  1.00 36.94           C  
ANISOU 1498  CB  ASN B  57     4330   4348   5358    597   -113  -1687       C  
ATOM   1499  CG  ASN B  57     -16.731  22.607  28.889  1.00 37.65           C  
ANISOU 1499  CG  ASN B  57     4342   4615   5346    659    -48  -1793       C  
ATOM   1500  OD1 ASN B  57     -17.930  22.875  28.725  1.00 36.93           O  
ANISOU 1500  OD1 ASN B  57     4194   4514   5323    760    -23  -1808       O  
ATOM   1501  ND2 ASN B  57     -16.275  21.995  29.971  1.00 35.41           N  
ANISOU 1501  ND2 ASN B  57     4049   4508   4898    602    -18  -1862       N  
ATOM   1502  N   PRO B  58     -13.991  24.024  30.733  1.00 37.92           N  
ANISOU 1502  N   PRO B  58     4481   4579   5346    496    -95  -2133       N  
ATOM   1503  CA  PRO B  58     -13.048  23.572  31.761  1.00 37.55           C  
ANISOU 1503  CA  PRO B  58     4434   4700   5132    407   -100  -2208       C  
ATOM   1504  C   PRO B  58     -13.352  22.187  32.353  1.00 36.44           C  
ANISOU 1504  C   PRO B  58     4246   4825   4776    396    -58  -2129       C  
ATOM   1505  O   PRO B  58     -12.427  21.545  32.851  1.00 35.76           O  
ANISOU 1505  O   PRO B  58     4163   4870   4556    315    -78  -2099       O  
ATOM   1506  CB  PRO B  58     -13.124  24.686  32.837  1.00 40.38           C  
ANISOU 1506  CB  PRO B  58     4789   5035   5518    437    -86  -2482       C  
ATOM   1507  CG  PRO B  58     -14.377  25.450  32.550  1.00 40.64           C  
ANISOU 1507  CG  PRO B  58     4802   4938   5701    566    -47  -2547       C  
ATOM   1508  CD  PRO B  58     -14.648  25.301  31.090  1.00 39.75           C  
ANISOU 1508  CD  PRO B  58     4706   4677   5719    588    -75  -2323       C  
ATOM   1509  N   MET B  59     -14.616  21.748  32.345  1.00 35.86           N  
ANISOU 1509  N   MET B  59     4120   4830   4675    476     -2  -2094       N  
ATOM   1510  CA  MET B  59     -14.926  20.332  32.624  1.00 35.37           C  
ANISOU 1510  CA  MET B  59     4016   4980   4445    453     36  -1965       C  
ATOM   1511  C   MET B  59     -14.242  19.368  31.650  1.00 32.67           C  
ANISOU 1511  C   MET B  59     3708   4605   4100    381     -4  -1748       C  
ATOM   1512  O   MET B  59     -13.848  18.260  32.071  1.00 33.22           O  
ANISOU 1512  O   MET B  59     3766   4830   4028    328      7  -1658       O  
ATOM   1513  CB  MET B  59     -16.435  20.014  32.575  1.00 36.06           C  
ANISOU 1513  CB  MET B  59     4032   5135   4534    538     99  -1941       C  
ATOM   1514  CG  MET B  59     -17.166  20.190  33.860  1.00 39.55           C  
ANISOU 1514  CG  MET B  59     4410   5751   4868    593    174  -2103       C  
ATOM   1515  SD  MET B  59     -16.931  21.889  34.256  1.00 48.25           S  
ANISOU 1515  SD  MET B  59     5545   6698   6091    647    158  -2361       S  
ATOM   1516  CE  MET B  59     -18.015  22.774  33.088  1.00 43.50           C  
ANISOU 1516  CE  MET B  59     4927   5857   5743    765    154  -2341       C  
ATOM   1517  N   VAL B  60     -14.168  19.729  30.362  1.00 30.04           N  
ANISOU 1517  N   VAL B  60     3413   4081   3918    387    -45  -1657       N  
ATOM   1518  CA  VAL B  60     -13.493  18.857  29.376  1.00 27.89           C  
ANISOU 1518  CA  VAL B  60     3176   3779   3641    323    -77  -1469       C  
ATOM   1519  C   VAL B  60     -12.003  18.786  29.757  1.00 27.68           C  
ANISOU 1519  C   VAL B  60     3182   3776   3559    238   -111  -1475       C  
ATOM   1520  O   VAL B  60     -11.449  17.720  29.871  1.00 25.98           O  
ANISOU 1520  O   VAL B  60     2963   3667   3240    189   -109  -1374       O  
ATOM   1521  CB  VAL B  60     -13.696  19.337  27.886  1.00 26.78           C  
ANISOU 1521  CB  VAL B  60     3070   3447   3657    347   -114  -1371       C  
ATOM   1522  CG1 VAL B  60     -12.783  18.544  26.884  1.00 24.90           C  
ANISOU 1522  CG1 VAL B  60     2875   3182   3403    276   -144  -1203       C  
ATOM   1523  CG2 VAL B  60     -15.140  19.241  27.493  1.00 25.20           C  
ANISOU 1523  CG2 VAL B  60     2823   3256   3497    427    -91  -1345       C  
ATOM   1524  N   ARG B  61     -11.390  19.929  30.042  1.00 30.16           N  
ANISOU 1524  N   ARG B  61     3519   3995   3946    221   -142  -1604       N  
ATOM   1525  CA  ARG B  61      -9.960  19.964  30.325  1.00 31.18           C  
ANISOU 1525  CA  ARG B  61     3666   4141   4041    133   -184  -1613       C  
ATOM   1526  C   ARG B  61      -9.628  19.204  31.593  1.00 31.78           C  
ANISOU 1526  C   ARG B  61     3703   4446   3926    105   -171  -1652       C  
ATOM   1527  O   ARG B  61      -8.692  18.419  31.596  1.00 32.21           O  
ANISOU 1527  O   ARG B  61     3754   4578   3908     47   -192  -1548       O  
ATOM   1528  CB  ARG B  61      -9.437  21.393  30.395  1.00 32.95           C  
ANISOU 1528  CB  ARG B  61     3917   4207   4398    110   -222  -1756       C  
ATOM   1529  CG  ARG B  61      -9.563  22.122  29.064  1.00 35.79           C  
ANISOU 1529  CG  ARG B  61     4317   4332   4949    128   -240  -1674       C  
ATOM   1530  CD  ARG B  61      -8.919  23.547  29.039  1.00 40.26           C  
ANISOU 1530  CD  ARG B  61     4914   4704   5677     88   -279  -1790       C  
ATOM   1531  NE  ARG B  61      -7.472  23.482  28.806  1.00 42.67           N  
ANISOU 1531  NE  ARG B  61     5229   4997   5987    -24   -320  -1729       N  
ATOM   1532  CZ  ARG B  61      -6.912  23.057  27.664  1.00 41.48           C  
ANISOU 1532  CZ  ARG B  61     5096   4796   5869    -61   -329  -1537       C  
ATOM   1533  NH1 ARG B  61      -7.656  22.672  26.626  1.00 41.94           N  
ANISOU 1533  NH1 ARG B  61     5172   4812   5953     -1   -308  -1392       N  
ATOM   1534  NH2 ARG B  61      -5.599  23.012  27.552  1.00 41.58           N  
ANISOU 1534  NH2 ARG B  61     5101   4815   5884   -158   -359  -1493       N  
ATOM   1535  N   ALA B  62     -10.381  19.421  32.662  1.00 32.57           N  
ANISOU 1535  N   ALA B  62     3769   4663   3942    150   -135  -1793       N  
ATOM   1536  CA  ALA B  62     -10.084  18.771  33.923  1.00 33.31           C  
ANISOU 1536  CA  ALA B  62     3825   4995   3837    124   -123  -1828       C  
ATOM   1537  C   ALA B  62     -10.304  17.256  33.795  1.00 32.51           C  
ANISOU 1537  C   ALA B  62     3702   5019   3633    122    -90  -1626       C  
ATOM   1538  O   ALA B  62      -9.532  16.473  34.343  1.00 32.98           O  
ANISOU 1538  O   ALA B  62     3745   5220   3567     77   -105  -1553       O  
ATOM   1539  CB  ALA B  62     -10.945  19.376  35.081  1.00 34.40           C  
ANISOU 1539  CB  ALA B  62     3930   5245   3897    179    -78  -2033       C  
ATOM   1540  N   HIS B  63     -11.339  16.846  33.056  1.00 31.54           N  
ANISOU 1540  N   HIS B  63     3575   4836   3572    169    -50  -1535       N  
ATOM   1541  CA  HIS B  63     -11.647  15.430  32.891  1.00 30.58           C  
ANISOU 1541  CA  HIS B  63     3435   4807   3378    161    -16  -1357       C  
ATOM   1542  C   HIS B  63     -10.642  14.765  31.915  1.00 29.99           C  
ANISOU 1542  C   HIS B  63     3398   4641   3354    111    -56  -1199       C  
ATOM   1543  O   HIS B  63     -10.305  13.584  32.082  1.00 29.79           O  
ANISOU 1543  O   HIS B  63     3363   4708   3249     87    -44  -1068       O  
ATOM   1544  CB  HIS B  63     -13.116  15.218  32.392  1.00 30.76           C  
ANISOU 1544  CB  HIS B  63     3431   4799   3458    217     35  -1323       C  
ATOM   1545  CG  HIS B  63     -13.478  13.777  32.192  1.00 27.12           C  
ANISOU 1545  CG  HIS B  63     2949   4410   2943    196     68  -1151       C  
ATOM   1546  ND1 HIS B  63     -13.835  12.954  33.241  1.00 28.55           N  
ANISOU 1546  ND1 HIS B  63     3082   4783   2983    188    121  -1113       N  
ATOM   1547  CD2 HIS B  63     -13.493  12.999  31.082  1.00 26.89           C  
ANISOU 1547  CD2 HIS B  63     2945   4287   2985    175     57  -1009       C  
ATOM   1548  CE1 HIS B  63     -14.059  11.733  32.786  1.00 28.24           C  
ANISOU 1548  CE1 HIS B  63     3038   4744   2948    160    141   -950       C  
ATOM   1549  NE2 HIS B  63     -13.872  11.733  31.476  1.00 28.29           N  
ANISOU 1549  NE2 HIS B  63     3089   4578   3081    153    102   -897       N  
ATOM   1550  N   GLY B  64     -10.190  15.505  30.897  1.00 29.48           N  
ANISOU 1550  N   GLY B  64     3377   4398   3427    102    -96  -1206       N  
ATOM   1551  CA  GLY B  64      -9.123  15.023  30.014  1.00 28.74           C  
ANISOU 1551  CA  GLY B  64     3314   4230   3374     56   -128  -1079       C  
ATOM   1552  C   GLY B  64      -7.903  14.614  30.837  1.00 29.15           C  
ANISOU 1552  C   GLY B  64     3345   4405   3325      8   -153  -1064       C  
ATOM   1553  O   GLY B  64      -7.428  13.458  30.748  1.00 28.97           O  
ANISOU 1553  O   GLY B  64     3315   4443   3249     -6   -145   -927       O  
ATOM   1554  N   LYS B  65      -7.424  15.549  31.655  1.00 29.41           N  
ANISOU 1554  N   LYS B  65     3365   4476   3333    -14   -186  -1207       N  
ATOM   1555  CA  LYS B  65      -6.305  15.307  32.558  1.00 30.71           C  
ANISOU 1555  CA  LYS B  65     3495   4783   3389    -61   -223  -1215       C  
ATOM   1556  C   LYS B  65      -6.458  14.027  33.355  1.00 30.08           C  
ANISOU 1556  C   LYS B  65     3380   4896   3153    -46   -193  -1110       C  
ATOM   1557  O   LYS B  65      -5.513  13.259  33.505  1.00 29.60           O  
ANISOU 1557  O   LYS B  65     3297   4910   3038    -70   -216  -1000       O  
ATOM   1558  CB  LYS B  65      -6.129  16.478  33.537  1.00 32.64           C  
ANISOU 1558  CB  LYS B  65     3725   5075   3602    -82   -256  -1424       C  
ATOM   1559  CG  LYS B  65      -5.110  16.195  34.675  1.00 34.71           C  
ANISOU 1559  CG  LYS B  65     3939   5539   3711   -129   -302  -1448       C  
ATOM   1560  CD  LYS B  65      -4.752  17.451  35.444  1.00 36.05           C  
ANISOU 1560  CD  LYS B  65     4099   5727   3873   -169   -350  -1674       C  
ATOM   1561  CE  LYS B  65      -3.957  17.090  36.692  1.00 38.49           C  
ANISOU 1561  CE  LYS B  65     4350   6284   3991   -209   -397  -1703       C  
ATOM   1562  NZ  LYS B  65      -3.223  18.260  37.280  1.00 39.36           N  
ANISOU 1562  NZ  LYS B  65     4445   6401   4108   -278   -468  -1915       N  
ATOM   1563  N   LYS B  66      -7.651  13.810  33.865  1.00 30.74           N  
ANISOU 1563  N   LYS B  66     3451   5057   3172     -3   -140  -1136       N  
ATOM   1564  CA  LYS B  66      -7.964  12.590  34.598  1.00 31.36           C  
ANISOU 1564  CA  LYS B  66     3495   5307   3112      9   -100  -1018       C  
ATOM   1565  C   LYS B  66      -7.951  11.347  33.721  1.00 29.66           C  
ANISOU 1565  C   LYS B  66     3297   5018   2956     11    -77   -820       C  
ATOM   1566  O   LYS B  66      -7.481  10.308  34.161  1.00 31.16           O  
ANISOU 1566  O   LYS B  66     3464   5310   3065      3    -73   -689       O  
ATOM   1567  CB  LYS B  66      -9.326  12.723  35.277  1.00 33.13           C  
ANISOU 1567  CB  LYS B  66     3694   5626   3268     49    -37  -1095       C  
ATOM   1568  CG  LYS B  66      -9.428  13.945  36.155  1.00 36.63           C  
ANISOU 1568  CG  LYS B  66     4123   6141   3654     58    -49  -1316       C  
ATOM   1569  CD  LYS B  66     -10.378  13.737  37.341  1.00 42.04           C  
ANISOU 1569  CD  LYS B  66     4759   7037   4176     90     17  -1367       C  
ATOM   1570  CE  LYS B  66     -11.826  13.778  36.909  1.00 43.46           C  
ANISOU 1570  CE  LYS B  66     4927   7152   4433    143     88  -1377       C  
ATOM   1571  NZ  LYS B  66     -12.729  13.189  37.951  1.00 45.66           N  
ANISOU 1571  NZ  LYS B  66     5146   7653   4551    164    168  -1355       N  
ATOM   1572  N   VAL B  67      -8.433  11.442  32.482  1.00 27.58           N  
ANISOU 1572  N   VAL B  67     3070   4578   2830     22    -65   -799       N  
ATOM   1573  CA  VAL B  67      -8.416  10.283  31.561  1.00 25.65           C  
ANISOU 1573  CA  VAL B  67     2847   4253   2644     20    -44   -637       C  
ATOM   1574  C   VAL B  67      -6.964   9.824  31.284  1.00 25.37           C  
ANISOU 1574  C   VAL B  67     2818   4202   2621     -3    -80   -547       C  
ATOM   1575  O   VAL B  67      -6.659   8.638  31.339  1.00 25.20           O  
ANISOU 1575  O   VAL B  67     2788   4212   2574      0    -62   -412       O  
ATOM   1576  CB  VAL B  67      -9.219  10.589  30.252  1.00 24.59           C  
ANISOU 1576  CB  VAL B  67     2750   3953   2641     34    -34   -650       C  
ATOM   1577  CG1 VAL B  67      -8.956   9.560  29.147  1.00 21.65           C  
ANISOU 1577  CG1 VAL B  67     2409   3485   2333     24    -26   -518       C  
ATOM   1578  CG2 VAL B  67     -10.740  10.713  30.577  1.00 22.85           C  
ANISOU 1578  CG2 VAL B  67     2501   3775   2407     64      9   -703       C  
ATOM   1579  N   LEU B  68      -6.078  10.775  31.055  1.00 25.24           N  
ANISOU 1579  N   LEU B  68     2808   4136   2647    -25   -129   -624       N  
ATOM   1580  CA  LEU B  68      -4.732  10.471  30.631  1.00 25.54           C  
ANISOU 1580  CA  LEU B  68     2840   4147   2716    -45   -159   -547       C  
ATOM   1581  C   LEU B  68      -3.950  10.025  31.840  1.00 26.92           C  
ANISOU 1581  C   LEU B  68     2959   4499   2769    -53   -185   -510       C  
ATOM   1582  O   LEU B  68      -3.218   9.040  31.778  1.00 27.86           O  
ANISOU 1582  O   LEU B  68     3059   4647   2880    -42   -184   -377       O  
ATOM   1583  CB  LEU B  68      -4.112  11.671  29.904  1.00 25.15           C  
ANISOU 1583  CB  LEU B  68     2809   3980   2767    -77   -197   -630       C  
ATOM   1584  CG  LEU B  68      -2.746  11.560  29.220  1.00 25.63           C  
ANISOU 1584  CG  LEU B  68     2857   3994   2885   -104   -219   -560       C  
ATOM   1585  CD1 LEU B  68      -2.528  10.253  28.478  1.00 25.09           C  
ANISOU 1585  CD1 LEU B  68     2801   3895   2838    -74   -180   -411       C  
ATOM   1586  CD2 LEU B  68      -2.518  12.743  28.278  1.00 22.59           C  
ANISOU 1586  CD2 LEU B  68     2502   3463   2618   -136   -237   -623       C  
ATOM   1587  N   THR B  69      -4.143  10.700  32.970  1.00 28.58           N  
ANISOU 1587  N   THR B  69     3142   4839   2879    -64   -208   -625       N  
ATOM   1588  CA  THR B  69      -3.617  10.210  34.225  1.00 29.84           C  
ANISOU 1588  CA  THR B  69     3246   5204   2888    -66   -232   -583       C  
ATOM   1589  C   THR B  69      -3.954   8.727  34.389  1.00 30.31           C  
ANISOU 1589  C   THR B  69     3298   5316   2902    -31   -184   -397       C  
ATOM   1590  O   THR B  69      -3.125   7.944  34.862  1.00 30.41           O  
ANISOU 1590  O   THR B  69     3271   5429   2854    -22   -206   -274       O  
ATOM   1591  CB  THR B  69      -4.151  11.013  35.456  1.00 31.52           C  
ANISOU 1591  CB  THR B  69     3437   5571   2970    -75   -243   -743       C  
ATOM   1592  OG1 THR B  69      -3.646  12.357  35.435  1.00 31.50           O  
ANISOU 1592  OG1 THR B  69     3436   5519   3015   -115   -297   -921       O  
ATOM   1593  CG2 THR B  69      -3.702  10.360  36.757  1.00 33.46           C  
ANISOU 1593  CG2 THR B  69     3623   6060   3029    -73   -265   -674       C  
ATOM   1594  N   SER B  70      -5.158   8.328  33.998  1.00 31.21           N  
ANISOU 1594  N   SER B  70     3446   5358   3056    -11   -121   -370       N  
ATOM   1595  CA  SER B  70      -5.555   6.925  34.128  1.00 32.61           C  
ANISOU 1595  CA  SER B  70     3618   5560   3213     10    -71   -197       C  
ATOM   1596  C   SER B  70      -4.599   6.046  33.317  1.00 33.36           C  
ANISOU 1596  C   SER B  70     3723   5548   3402     23    -78    -62       C  
ATOM   1597  O   SER B  70      -4.020   5.097  33.847  1.00 33.14           O  
ANISOU 1597  O   SER B  70     3664   5599   3328     43    -81     81       O  
ATOM   1598  CB  SER B  70      -7.008   6.730  33.707  1.00 32.99           C  
ANISOU 1598  CB  SER B  70     3692   5532   3310     15     -7   -208       C  
ATOM   1599  OG  SER B  70      -7.540   5.557  34.293  1.00 34.63           O  
ANISOU 1599  OG  SER B  70     3878   5818   3462     21     43    -64       O  
ATOM   1600  N   PHE B  71      -4.363   6.410  32.054  1.00 33.74           N  
ANISOU 1600  N   PHE B  71     3812   5428   3581     17    -83   -106       N  
ATOM   1601  CA  PHE B  71      -3.324   5.742  31.256  1.00 33.98           C  
ANISOU 1601  CA  PHE B  71     3846   5369   3695     33    -87     -8       C  
ATOM   1602  C   PHE B  71      -1.967   5.662  31.929  1.00 34.87           C  
ANISOU 1602  C   PHE B  71     3897   5599   3752     40   -137     46       C  
ATOM   1603  O   PHE B  71      -1.250   4.684  31.780  1.00 34.63           O  
ANISOU 1603  O   PHE B  71     3847   5555   3755     75   -129    178       O  
ATOM   1604  CB  PHE B  71      -3.159   6.449  29.914  1.00 33.65           C  
ANISOU 1604  CB  PHE B  71     3847   5171   3767     19    -91    -86       C  
ATOM   1605  CG  PHE B  71      -4.161   6.028  28.896  1.00 35.22           C  
ANISOU 1605  CG  PHE B  71     4102   5235   4044     25    -43    -78       C  
ATOM   1606  CD1 PHE B  71      -3.950   4.883  28.138  1.00 36.88           C  
ANISOU 1606  CD1 PHE B  71     4335   5355   4322     47     -7     21       C  
ATOM   1607  CD2 PHE B  71      -5.308   6.764  28.689  1.00 35.96           C  
ANISOU 1607  CD2 PHE B  71     4221   5294   4147     11    -37   -175       C  
ATOM   1608  CE1 PHE B  71      -4.877   4.482  27.205  1.00 37.02           C  
ANISOU 1608  CE1 PHE B  71     4402   5260   4403     42     28     13       C  
ATOM   1609  CE2 PHE B  71      -6.234   6.361  27.736  1.00 38.08           C  
ANISOU 1609  CE2 PHE B  71     4530   5456   4482     13     -5   -166       C  
ATOM   1610  CZ  PHE B  71      -6.024   5.227  27.004  1.00 35.74           C  
ANISOU 1610  CZ  PHE B  71     4259   5081   4241     22     25    -78       C  
ATOM   1611  N   GLY B  72      -1.594   6.715  32.638  1.00 36.84           N  
ANISOU 1611  N   GLY B  72     4111   5960   3926      9   -193    -64       N  
ATOM   1612  CA  GLY B  72      -0.348   6.718  33.434  1.00 38.53           C  
ANISOU 1612  CA  GLY B  72     4250   6324   4064      6   -256    -26       C  
ATOM   1613  C   GLY B  72      -0.286   5.580  34.416  1.00 39.88           C  
ANISOU 1613  C   GLY B  72     4381   6639   4133     46   -252    131       C  
ATOM   1614  O   GLY B  72       0.765   5.031  34.685  1.00 40.64           O  
ANISOU 1614  O   GLY B  72     4418   6807   4215     72   -286    243       O  
ATOM   1615  N   ASP B  73      -1.436   5.210  34.954  1.00 41.46           N  
ANISOU 1615  N   ASP B  73     4604   6883   4264     53   -206    154       N  
ATOM   1616  CA  ASP B  73      -1.505   4.097  35.905  1.00 43.31           C  
ANISOU 1616  CA  ASP B  73     4804   7251   4400     87   -192    328       C  
ATOM   1617  C   ASP B  73      -1.313   2.771  35.178  1.00 42.22           C  
ANISOU 1617  C   ASP B  73     4685   6964   4391    133   -146    505       C  
ATOM   1618  O   ASP B  73      -0.874   1.786  35.764  1.00 43.26           O  
ANISOU 1618  O   ASP B  73     4779   7170   4489    174   -148    681       O  
ATOM   1619  CB  ASP B  73      -2.830   4.138  36.695  1.00 44.08           C  
ANISOU 1619  CB  ASP B  73     4914   7447   4385     72   -146    300       C  
ATOM   1620  CG  ASP B  73      -2.848   5.243  37.767  1.00 48.50           C  
ANISOU 1620  CG  ASP B  73     5439   8213   4777     42   -193    145       C  
ATOM   1621  OD1 ASP B  73      -1.798   5.464  38.432  1.00 53.45           O  
ANISOU 1621  OD1 ASP B  73     6008   8990   5309     38   -268    147       O  
ATOM   1622  OD2 ASP B  73      -3.921   5.874  37.978  1.00 53.11           O  
ANISOU 1622  OD2 ASP B  73     6045   8816   5320     25   -156     16       O  
ATOM   1623  N   ALA B  74      -1.650   2.749  33.902  1.00 40.75           N  
ANISOU 1623  N   ALA B  74     4559   6570   4352    129   -105    457       N  
ATOM   1624  CA  ALA B  74      -1.402   1.578  33.082  1.00 41.09           C  
ANISOU 1624  CA  ALA B  74     4627   6455   4529    171    -61    584       C  
ATOM   1625  C   ALA B  74       0.099   1.436  32.798  1.00 41.66           C  
ANISOU 1625  C   ALA B  74     4651   6527   4651    211    -99    637       C  
ATOM   1626  O   ALA B  74       0.649   0.342  32.857  1.00 41.85           O  
ANISOU 1626  O   ALA B  74     4651   6525   4724    269    -84    792       O  
ATOM   1627  CB  ALA B  74      -2.215   1.645  31.766  1.00 39.16           C  
ANISOU 1627  CB  ALA B  74     4460   6011   4410    150    -11    497       C  
ATOM   1628  N   VAL B  75       0.752   2.546  32.499  1.00 42.22           N  
ANISOU 1628  N   VAL B  75     4700   6622   4718    180   -147    511       N  
ATOM   1629  CA  VAL B  75       2.185   2.526  32.236  1.00 43.93           C  
ANISOU 1629  CA  VAL B  75     4854   6857   4982    208   -183    551       C  
ATOM   1630  C   VAL B  75       2.949   2.075  33.485  1.00 46.53           C  
ANISOU 1630  C   VAL B  75     5092   7381   5206    243   -239    678       C  
ATOM   1631  O   VAL B  75       3.901   1.284  33.404  1.00 47.00           O  
ANISOU 1631  O   VAL B  75     5097   7440   5322    307   -244    811       O  
ATOM   1632  CB  VAL B  75       2.720   3.905  31.801  1.00 43.08           C  
ANISOU 1632  CB  VAL B  75     4730   6753   4885    149   -227    394       C  
ATOM   1633  CG1 VAL B  75       4.205   3.795  31.433  1.00 43.80           C  
ANISOU 1633  CG1 VAL B  75     4743   6860   5039    175   -253    449       C  
ATOM   1634  CG2 VAL B  75       1.906   4.452  30.638  1.00 41.02           C  
ANISOU 1634  CG2 VAL B  75     4557   6319   4710    116   -180    281       C  
ATOM   1635  N   LYS B  76       2.533   2.579  34.639  1.00 48.65           N  
ANISOU 1635  N   LYS B  76     5340   7827   5319    207   -282    638       N  
ATOM   1636  CA  LYS B  76       3.226   2.261  35.896  1.00 51.60           C  
ANISOU 1636  CA  LYS B  76     5622   8425   5558    232   -348    752       C  
ATOM   1637  C   LYS B  76       3.004   0.822  36.392  1.00 52.62           C  
ANISOU 1637  C   LYS B  76     5747   8567   5680    304   -311    981       C  
ATOM   1638  O   LYS B  76       3.604   0.411  37.394  1.00 54.97           O  
ANISOU 1638  O   LYS B  76     5966   9050   5871    339   -364   1115       O  
ATOM   1639  CB  LYS B  76       2.799   3.240  36.999  1.00 53.01           C  
ANISOU 1639  CB  LYS B  76     5784   8805   5552    170   -401    624       C  
ATOM   1640  CG  LYS B  76       3.309   4.678  36.848  1.00 54.93           C  
ANISOU 1640  CG  LYS B  76     6006   9078   5788     99   -465    413       C  
ATOM   1641  CD  LYS B  76       2.712   5.531  37.991  1.00 59.04           C  
ANISOU 1641  CD  LYS B  76     6522   9786   6126     46   -503    273       C  
ATOM   1642  CE  LYS B  76       3.366   6.912  38.152  1.00 60.77           C  
ANISOU 1642  CE  LYS B  76     6702  10069   6319    -30   -585     68       C  
ATOM   1643  NZ  LYS B  76       2.538   7.806  39.042  1.00 62.02           N  
ANISOU 1643  NZ  LYS B  76     6884  10350   6331    -76   -597   -114       N  
ATOM   1644  N   ASN B  77       2.125   0.062  35.742  1.00 51.88           N  
ANISOU 1644  N   ASN B  77     5732   8286   5695    320   -223   1031       N  
ATOM   1645  CA  ASN B  77       1.990  -1.360  36.056  1.00 52.64           C  
ANISOU 1645  CA  ASN B  77     5827   8343   5831    385   -181   1255       C  
ATOM   1646  C   ASN B  77       1.358  -2.151  34.893  1.00 51.63           C  
ANISOU 1646  C   ASN B  77     5786   7942   5891    399    -89   1269       C  
ATOM   1647  O   ASN B  77       0.197  -2.556  34.953  1.00 51.63           O  
ANISOU 1647  O   ASN B  77     5841   7878   5898    370    -32   1291       O  
ATOM   1648  CB  ASN B  77       1.217  -1.529  37.375  1.00 53.72           C  
ANISOU 1648  CB  ASN B  77     5951   8668   5793    365   -183   1340       C  
ATOM   1649  CG  ASN B  77       1.711  -2.726  38.220  1.00 55.54           C  
ANISOU 1649  CG  ASN B  77     6124   8987   5993    438   -194   1612       C  
ATOM   1650  OD1 ASN B  77       2.495  -3.558  37.744  1.00 53.60           O  
ANISOU 1650  OD1 ASN B  77     5858   8619   5887    514   -188   1739       O  
ATOM   1651  ND2 ASN B  77       1.230  -2.812  39.478  1.00 53.63           N  
ANISOU 1651  ND2 ASN B  77     5853   8960   5563    422   -206   1704       N  
ATOM   1652  N   LEU B  78       2.162  -2.361  33.844  1.00 51.26           N  
ANISOU 1652  N   LEU B  78     5740   7748   5990    442    -77   1250       N  
ATOM   1653  CA  LEU B  78       1.743  -2.988  32.576  1.00 50.28           C  
ANISOU 1653  CA  LEU B  78     5695   7370   6038    454      2   1221       C  
ATOM   1654  C   LEU B  78       1.264  -4.436  32.727  1.00 51.90           C  
ANISOU 1654  C   LEU B  78     5931   7452   6336    497     62   1394       C  
ATOM   1655  O   LEU B  78       0.438  -4.929  31.927  1.00 52.15           O  
ANISOU 1655  O   LEU B  78     6041   7295   6479    474    127   1352       O  
ATOM   1656  CB  LEU B  78       2.897  -2.939  31.557  1.00 49.92           C  
ANISOU 1656  CB  LEU B  78     5627   7235   6106    504      4   1177       C  
ATOM   1657  CG  LEU B  78       3.144  -1.636  30.773  1.00 48.33           C  
ANISOU 1657  CG  LEU B  78     5432   7039   5891    447    -18    985       C  
ATOM   1658  CD1 LEU B  78       4.552  -1.578  30.227  1.00 45.76           C  
ANISOU 1658  CD1 LEU B  78     5038   6714   5634    499    -30    993       C  
ATOM   1659  CD2 LEU B  78       2.139  -1.517  29.645  1.00 46.32           C  
ANISOU 1659  CD2 LEU B  78     5279   6611   5708    403     41    862       C  
ATOM   1660  N   ASP B  79       1.782  -5.126  33.740  1.00 53.41           N  
ANISOU 1660  N   ASP B  79     6058   7748   6486    556     37   1592       N  
ATOM   1661  CA  ASP B  79       1.372  -6.499  34.005  1.00 54.78           C  
ANISOU 1661  CA  ASP B  79     6255   7803   6754    596     92   1785       C  
ATOM   1662  C   ASP B  79       0.091  -6.573  34.864  1.00 55.05           C  
ANISOU 1662  C   ASP B  79     6314   7918   6683    523    114   1840       C  
ATOM   1663  O   ASP B  79      -0.465  -7.654  35.045  1.00 56.25           O  
ANISOU 1663  O   ASP B  79     6494   7959   6921    530    169   1991       O  
ATOM   1664  CB  ASP B  79       2.519  -7.276  34.681  1.00 56.74           C  
ANISOU 1664  CB  ASP B  79     6419   8117   7022    704     58   2005       C  
ATOM   1665  CG  ASP B  79       3.735  -7.462  33.761  1.00 57.07           C  
ANISOU 1665  CG  ASP B  79     6430   8048   7206    792     59   1973       C  
ATOM   1666  OD1 ASP B  79       3.563  -7.620  32.529  1.00 54.86           O  
ANISOU 1666  OD1 ASP B  79     6218   7557   7070    789    121   1848       O  
ATOM   1667  OD2 ASP B  79       4.873  -7.450  34.283  1.00 59.28           O  
ANISOU 1667  OD2 ASP B  79     6609   8467   7447    864     -1   2074       O  
ATOM   1668  N   ASN B  80      -0.378  -5.441  35.388  1.00 53.97           N  
ANISOU 1668  N   ASN B  80     6165   7971   6371    454     78   1717       N  
ATOM   1669  CA  ASN B  80      -1.518  -5.440  36.316  1.00 54.16           C  
ANISOU 1669  CA  ASN B  80     6192   8116   6269    393    102   1768       C  
ATOM   1670  C   ASN B  80      -2.680  -4.589  35.774  1.00 51.98           C  
ANISOU 1670  C   ASN B  80     5971   7800   5978    306    132   1554       C  
ATOM   1671  O   ASN B  80      -3.415  -3.979  36.544  1.00 51.80           O  
ANISOU 1671  O   ASN B  80     5931   7946   5803    257    131   1508       O  
ATOM   1672  CB  ASN B  80      -1.057  -4.947  37.702  1.00 55.35           C  
ANISOU 1672  CB  ASN B  80     6262   8574   6193    403     33   1837       C  
ATOM   1673  CG  ASN B  80      -1.982  -5.395  38.833  1.00 56.71           C  
ANISOU 1673  CG  ASN B  80     6422   8888   6238    372     71   1987       C  
ATOM   1674  OD1 ASN B  80      -2.345  -6.571  38.931  1.00 56.14           O  
ANISOU 1674  OD1 ASN B  80     6365   8702   6263    387    128   2184       O  
ATOM   1675  ND2 ASN B  80      -2.366  -4.450  39.695  1.00 55.10           N  
ANISOU 1675  ND2 ASN B  80     6188   8931   5818    325     42   1890       N  
ATOM   1676  N   ILE B  81      -2.841  -4.593  34.447  1.00 50.08           N  
ANISOU 1676  N   ILE B  81     5790   7341   5895    296    161   1431       N  
ATOM   1677  CA  ILE B  81      -3.744  -3.674  33.739  1.00 48.25           C  
ANISOU 1677  CA  ILE B  81     5604   7065   5663    228    173   1221       C  
ATOM   1678  C   ILE B  81      -5.184  -4.094  33.980  1.00 48.45           C  
ANISOU 1678  C   ILE B  81     5651   7067   5693    167    233   1253       C  
ATOM   1679  O   ILE B  81      -5.969  -3.287  34.434  1.00 47.30           O  
ANISOU 1679  O   ILE B  81     5489   7049   5431    122    233   1161       O  
ATOM   1680  CB  ILE B  81      -3.384  -3.544  32.187  1.00 46.78           C  
ANISOU 1680  CB  ILE B  81     5471   6674   5628    239    179   1089       C  
ATOM   1681  CG1 ILE B  81      -2.184  -2.602  31.994  1.00 47.11           C  
ANISOU 1681  CG1 ILE B  81     5479   6792   5626    269    118   1001       C  
ATOM   1682  CG2 ILE B  81      -4.518  -2.970  31.363  1.00 44.43           C  
ANISOU 1682  CG2 ILE B  81     5226   6294   5361    173    202    925       C  
ATOM   1683  CD1 ILE B  81      -1.734  -2.371  30.510  1.00 43.80           C  
ANISOU 1683  CD1 ILE B  81     5103   6209   5329    279    128    881       C  
ATOM   1684  N   LYS B  82      -5.506  -5.365  33.716  1.00 49.97           N  
ANISOU 1684  N   LYS B  82     5870   7095   6023    167    288   1384       N  
ATOM   1685  CA  LYS B  82      -6.832  -5.938  34.035  1.00 50.99           C  
ANISOU 1685  CA  LYS B  82     6004   7200   6170     99    350   1452       C  
ATOM   1686  C   LYS B  82      -7.308  -5.411  35.374  1.00 50.99           C  
ANISOU 1686  C   LYS B  82     5945   7460   5969     76    348   1498       C  
ATOM   1687  O   LYS B  82      -8.307  -4.688  35.454  1.00 50.72           O  
ANISOU 1687  O   LYS B  82     5902   7504   5864     22    365   1376       O  
ATOM   1688  CB  LYS B  82      -6.799  -7.472  34.133  1.00 53.05           C  
ANISOU 1688  CB  LYS B  82     6277   7306   6575    112    399   1664       C  
ATOM   1689  CG  LYS B  82      -6.655  -8.270  32.811  1.00 55.46           C  
ANISOU 1689  CG  LYS B  82     6647   7319   7104    121    425   1617       C  
ATOM   1690  CD  LYS B  82      -6.572  -9.797  33.131  1.00 59.59           C  
ANISOU 1690  CD  LYS B  82     7178   7690   7774    140    475   1846       C  
ATOM   1691  CE  LYS B  82      -6.219 -10.712  31.925  1.00 61.36           C  
ANISOU 1691  CE  LYS B  82     7466   7618   8230    168    503   1805       C  
ATOM   1692  NZ  LYS B  82      -6.108 -12.201  32.320  1.00 62.29           N  
ANISOU 1692  NZ  LYS B  82     7590   7566   8510    193    553   2037       N  
ATOM   1693  N   ASN B  83      -6.561  -5.745  36.415  1.00 51.20           N  
ANISOU 1693  N   ASN B  83     5926   7632   5895    123    327   1668       N  
ATOM   1694  CA  ASN B  83      -6.973  -5.440  37.781  1.00 51.79           C  
ANISOU 1694  CA  ASN B  83     5944   7974   5761    104    332   1742       C  
ATOM   1695  C   ASN B  83      -7.030  -3.941  38.078  1.00 49.96           C  
ANISOU 1695  C   ASN B  83     5690   7935   5358     92    287   1526       C  
ATOM   1696  O   ASN B  83      -7.923  -3.493  38.803  1.00 50.16           O  
ANISOU 1696  O   ASN B  83     5686   8127   5246     52    319   1488       O  
ATOM   1697  CB  ASN B  83      -6.038  -6.134  38.794  1.00 53.88           C  
ANISOU 1697  CB  ASN B  83     6162   8365   5946    166    305   1982       C  
ATOM   1698  CG  ASN B  83      -6.581  -7.461  39.307  1.00 56.90           C  
ANISOU 1698  CG  ASN B  83     6537   8692   6388    150    375   2246       C  
ATOM   1699  OD1 ASN B  83      -5.968  -8.079  40.182  1.00 62.15           O  
ANISOU 1699  OD1 ASN B  83     7162   9465   6987    200    359   2472       O  
ATOM   1700  ND2 ASN B  83      -7.741  -7.891  38.804  1.00 56.84           N  
ANISOU 1700  ND2 ASN B  83     6562   8529   6506     77    450   2229       N  
ATOM   1701  N   THR B  84      -6.072  -3.188  37.528  1.00 47.48           N  
ANISOU 1701  N   THR B  84     5387   7595   5059    126    218   1387       N  
ATOM   1702  CA  THR B  84      -5.987  -1.730  37.720  1.00 45.89           C  
ANISOU 1702  CA  THR B  84     5170   7537   4727    113    168   1172       C  
ATOM   1703  C   THR B  84      -7.219  -0.988  37.203  1.00 43.86           C  
ANISOU 1703  C   THR B  84     4942   7226   4499     63    208    989       C  
ATOM   1704  O   THR B  84      -7.641   0.008  37.802  1.00 44.43           O  
ANISOU 1704  O   THR B  84     4989   7460   4434     47    200    856       O  
ATOM   1705  CB  THR B  84      -4.710  -1.119  37.033  1.00 45.05           C  
ANISOU 1705  CB  THR B  84     5071   7369   4677    147     93   1068       C  
ATOM   1706  OG1 THR B  84      -3.528  -1.541  37.737  1.00 46.72           O  
ANISOU 1706  OG1 THR B  84     5230   7701   4822    198     41   1214       O  
ATOM   1707  CG2 THR B  84      -4.771   0.403  37.027  1.00 42.94           C  
ANISOU 1707  CG2 THR B  84     4802   7188   4327    119     51    831       C  
ATOM   1708  N   PHE B  85      -7.811  -1.475  36.117  1.00 41.35           N  
ANISOU 1708  N   PHE B  85     4669   6687   4354     41    248    978       N  
ATOM   1709  CA  PHE B  85      -8.997  -0.820  35.532  1.00 39.77           C  
ANISOU 1709  CA  PHE B  85     4487   6431   4194     -2    278    817       C  
ATOM   1710  C   PHE B  85     -10.365  -1.443  35.889  1.00 39.98           C  
ANISOU 1710  C   PHE B  85     4489   6479   4224    -51    356    895       C  
ATOM   1711  O   PHE B  85     -11.396  -1.022  35.360  1.00 39.96           O  
ANISOU 1711  O   PHE B  85     4488   6426   4269    -84    381    779       O  
ATOM   1712  CB  PHE B  85      -8.815  -0.713  34.007  1.00 37.60           C  
ANISOU 1712  CB  PHE B  85     4271   5927   4089     -1    259    717       C  
ATOM   1713  CG  PHE B  85      -7.794   0.287  33.625  1.00 36.22           C  
ANISOU 1713  CG  PHE B  85     4109   5754   3898     29    193    593       C  
ATOM   1714  CD1 PHE B  85      -8.164   1.580  33.300  1.00 34.24           C  
ANISOU 1714  CD1 PHE B  85     3865   5517   3626     18    169    406       C  
ATOM   1715  CD2 PHE B  85      -6.444  -0.041  33.641  1.00 34.67           C  
ANISOU 1715  CD2 PHE B  85     3907   5551   3714     71    155    671       C  
ATOM   1716  CE1 PHE B  85      -7.214   2.512  32.971  1.00 32.01           C  
ANISOU 1716  CE1 PHE B  85     3593   5229   3342     34    110    302       C  
ATOM   1717  CE2 PHE B  85      -5.491   0.887  33.322  1.00 33.68           C  
ANISOU 1717  CE2 PHE B  85     3781   5438   3578     87     96    563       C  
ATOM   1718  CZ  PHE B  85      -5.874   2.171  32.992  1.00 32.23           C  
ANISOU 1718  CZ  PHE B  85     3611   5259   3378     62     75    379       C  
ATOM   1719  N   ALA B  86     -10.383  -2.414  36.800  1.00 41.15           N  
ANISOU 1719  N   ALA B  86     4605   6710   4319    -56    395   1101       N  
ATOM   1720  CA  ALA B  86     -11.613  -3.142  37.099  1.00 41.63           C  
ANISOU 1720  CA  ALA B  86     4637   6775   4405   -114    476   1205       C  
ATOM   1721  C   ALA B  86     -12.726  -2.179  37.468  1.00 41.66           C  
ANISOU 1721  C   ALA B  86     4596   6930   4303   -141    508   1058       C  
ATOM   1722  O   ALA B  86     -13.820  -2.273  36.933  1.00 41.04           O  
ANISOU 1722  O   ALA B  86     4507   6769   4318   -188    551   1012       O  
ATOM   1723  CB  ALA B  86     -11.382  -4.146  38.215  1.00 43.47           C  
ANISOU 1723  CB  ALA B  86     4835   7119   4562   -112    511   1459       C  
ATOM   1724  N   GLN B  87     -12.433  -1.235  38.362  1.00 42.37           N  
ANISOU 1724  N   GLN B  87     4654   7240   4203   -107    485    974       N  
ATOM   1725  CA  GLN B  87     -13.452  -0.278  38.822  1.00 43.12           C  
ANISOU 1725  CA  GLN B  87     4703   7492   4191   -117    523    823       C  
ATOM   1726  C   GLN B  87     -13.903   0.630  37.680  1.00 40.40           C  
ANISOU 1726  C   GLN B  87     4385   6996   3968   -114    497    608       C  
ATOM   1727  O   GLN B  87     -15.093   0.851  37.477  1.00 39.94           O  
ANISOU 1727  O   GLN B  87     4292   6937   3947   -138    545    541       O  
ATOM   1728  CB  GLN B  87     -12.980   0.534  40.054  1.00 45.04           C  
ANISOU 1728  CB  GLN B  87     4911   8005   4198    -81    501    758       C  
ATOM   1729  CG  GLN B  87     -13.723   0.197  41.358  1.00 49.35           C  
ANISOU 1729  CG  GLN B  87     5384   8804   4561   -100    584    870       C  
ATOM   1730  CD  GLN B  87     -15.180   0.684  41.343  1.00 54.34           C  
ANISOU 1730  CD  GLN B  87     5966   9484   5196   -123    664    750       C  
ATOM   1731  OE1 GLN B  87     -15.601   1.367  40.385  1.00 56.20           O  
ANISOU 1731  OE1 GLN B  87     6222   9568   5563   -116    646    575       O  
ATOM   1732  NE2 GLN B  87     -15.960   0.339  42.405  1.00 54.75           N  
ANISOU 1732  NE2 GLN B  87     5945   9758   5100   -146    755    853       N  
ATOM   1733  N   LEU B  88     -12.963   1.108  36.895  1.00 38.07           N  
ANISOU 1733  N   LEU B  88     4147   6572   3744    -84    421    517       N  
ATOM   1734  CA  LEU B  88     -13.345   1.922  35.755  1.00 36.58           C  
ANISOU 1734  CA  LEU B  88     3989   6236   3673    -79    394    342       C  
ATOM   1735  C   LEU B  88     -14.085   1.118  34.666  1.00 36.25           C  
ANISOU 1735  C   LEU B  88     3964   6004   3805   -122    419    393       C  
ATOM   1736  O   LEU B  88     -14.835   1.697  33.872  1.00 36.14           O  
ANISOU 1736  O   LEU B  88     3950   5915   3868   -127    413    270       O  
ATOM   1737  CB  LEU B  88     -12.137   2.614  35.149  1.00 34.85           C  
ANISOU 1737  CB  LEU B  88     3824   5930   3489    -46    313    249       C  
ATOM   1738  CG  LEU B  88     -11.423   3.591  36.045  1.00 34.14           C  
ANISOU 1738  CG  LEU B  88     3717   6003   3251    -16    272    152       C  
ATOM   1739  CD1 LEU B  88     -10.133   3.949  35.407  1.00 33.66           C  
ANISOU 1739  CD1 LEU B  88     3700   5840   3250      0    198    113       C  
ATOM   1740  CD2 LEU B  88     -12.251   4.850  36.273  1.00 33.74           C  
ANISOU 1740  CD2 LEU B  88     3642   6023   3154     -3    284    -44       C  
ATOM   1741  N   SER B  89     -13.880  -0.193  34.597  1.00 36.71           N  
ANISOU 1741  N   SER B  89     4037   5981   3931   -151    443    568       N  
ATOM   1742  CA  SER B  89     -14.646  -0.985  33.622  1.00 36.43           C  
ANISOU 1742  CA  SER B  89     4014   5770   4059   -204    467    599       C  
ATOM   1743  C   SER B  89     -16.127  -1.029  33.958  1.00 37.48           C  
ANISOU 1743  C   SER B  89     4072   5986   4183   -255    531    597       C  
ATOM   1744  O   SER B  89     -16.963  -0.956  33.065  1.00 37.38           O  
ANISOU 1744  O   SER B  89     4052   5876   4275   -287    528    519       O  
ATOM   1745  CB  SER B  89     -14.125  -2.407  33.517  1.00 36.89           C  
ANISOU 1745  CB  SER B  89     4103   5703   4210   -226    485    780       C  
ATOM   1746  OG  SER B  89     -14.783  -3.046  32.443  1.00 36.06           O  
ANISOU 1746  OG  SER B  89     4019   5413   4268   -281    495    763       O  
ATOM   1747  N   GLU B  90     -16.428  -1.155  35.255  1.00 39.09           N  
ANISOU 1747  N   GLU B  90     4215   6385   4252   -260    587    688       N  
ATOM   1748  CA  GLU B  90     -17.794  -1.165  35.778  1.00 40.03           C  
ANISOU 1748  CA  GLU B  90     4245   6628   4336   -304    663    698       C  
ATOM   1749  C   GLU B  90     -18.523   0.136  35.513  1.00 39.11           C  
ANISOU 1749  C   GLU B  90     4091   6572   4196   -269    652    489       C  
ATOM   1750  O   GLU B  90     -19.696   0.139  35.188  1.00 39.00           O  
ANISOU 1750  O   GLU B  90     4017   6554   4249   -305    687    454       O  
ATOM   1751  CB  GLU B  90     -17.794  -1.401  37.289  1.00 41.78           C  
ANISOU 1751  CB  GLU B  90     4410   7084   4379   -303    726    828       C  
ATOM   1752  CG  GLU B  90     -17.620  -2.810  37.678  1.00 44.12           C  
ANISOU 1752  CG  GLU B  90     4708   7342   4715   -354    768   1075       C  
ATOM   1753  CD  GLU B  90     -17.559  -2.993  39.178  1.00 49.52           C  
ANISOU 1753  CD  GLU B  90     5337   8281   5198   -347    826   1219       C  
ATOM   1754  OE1 GLU B  90     -16.469  -3.390  39.684  1.00 51.65           O  
ANISOU 1754  OE1 GLU B  90     5643   8584   5400   -312    794   1346       O  
ATOM   1755  OE2 GLU B  90     -18.595  -2.743  39.848  1.00 51.05           O  
ANISOU 1755  OE2 GLU B  90     5446   8655   5295   -372    903   1209       O  
ATOM   1756  N   LEU B  91     -17.825   1.236  35.731  1.00 38.46           N  
ANISOU 1756  N   LEU B  91     4038   6553   4020   -199    605    357       N  
ATOM   1757  CA  LEU B  91     -18.354   2.550  35.479  1.00 38.16           C  
ANISOU 1757  CA  LEU B  91     3978   6546   3976   -152    588    156       C  
ATOM   1758  C   LEU B  91     -18.766   2.652  34.033  1.00 36.97           C  
ANISOU 1758  C   LEU B  91     3853   6197   3998   -164    543     89       C  
ATOM   1759  O   LEU B  91     -19.900   2.994  33.728  1.00 37.35           O  
ANISOU 1759  O   LEU B  91     3838   6257   4095   -168    565     21       O  
ATOM   1760  CB  LEU B  91     -17.276   3.588  35.771  1.00 37.95           C  
ANISOU 1760  CB  LEU B  91     4000   6559   3860    -88    529     37       C  
ATOM   1761  CG  LEU B  91     -17.587   5.069  35.623  1.00 38.26           C  
ANISOU 1761  CG  LEU B  91     4030   6612   3893    -29    506   -179       C  
ATOM   1762  CD1 LEU B  91     -18.788   5.470  36.494  1.00 37.17           C  
ANISOU 1762  CD1 LEU B  91     3795   6660   3667    -11    588   -243       C  
ATOM   1763  CD2 LEU B  91     -16.322   5.871  36.007  1.00 39.68           C  
ANISOU 1763  CD2 LEU B  91     4263   6823   3991      9    445   -268       C  
ATOM   1764  N   HIS B  92     -17.834   2.358  33.135  1.00 36.42           N  
ANISOU 1764  N   HIS B  92     3868   5957   4013   -168    480    109       N  
ATOM   1765  CA  HIS B  92     -18.052   2.610  31.704  1.00 35.62           C  
ANISOU 1765  CA  HIS B  92     3802   5683   4047   -170    426     29       C  
ATOM   1766  C   HIS B  92     -19.124   1.671  31.098  1.00 36.65           C  
ANISOU 1766  C   HIS B  92     3892   5744   4288   -243    452     91       C  
ATOM   1767  O   HIS B  92     -19.948   2.092  30.290  1.00 36.18           O  
ANISOU 1767  O   HIS B  92     3804   5642   4302   -246    428      6       O  
ATOM   1768  CB  HIS B  92     -16.719   2.537  30.963  1.00 33.82           C  
ANISOU 1768  CB  HIS B  92     3671   5317   3862   -153    363     33       C  
ATOM   1769  CG  HIS B  92     -15.831   3.713  31.226  1.00 32.73           C  
ANISOU 1769  CG  HIS B  92     3563   5221   3652    -92    321    -67       C  
ATOM   1770  ND1 HIS B  92     -15.085   3.843  32.379  1.00 29.39           N  
ANISOU 1770  ND1 HIS B  92     3133   4928   3105    -71    329    -41       N  
ATOM   1771  CD2 HIS B  92     -15.580   4.822  30.489  1.00 30.60           C  
ANISOU 1771  CD2 HIS B  92     3327   4880   3421    -54    266   -192       C  
ATOM   1772  CE1 HIS B  92     -14.417   4.980  32.342  1.00 28.68           C  
ANISOU 1772  CE1 HIS B  92     3070   4840   2988    -30    281   -161       C  
ATOM   1773  NE2 HIS B  92     -14.706   5.598  31.210  1.00 29.67           N  
ANISOU 1773  NE2 HIS B  92     3221   4835   3216    -18    246   -248       N  
ATOM   1774  N   CYS B  93     -19.147   0.424  31.564  1.00 38.76           N  
ANISOU 1774  N   CYS B  93     4148   6011   4568   -305    502    243       N  
ATOM   1775  CA  CYS B  93     -19.982  -0.642  30.963  1.00 40.36           C  
ANISOU 1775  CA  CYS B  93     4323   6114   4897   -393    522    310       C  
ATOM   1776  C   CYS B  93     -21.343  -0.860  31.618  1.00 41.70           C  
ANISOU 1776  C   CYS B  93     4375   6414   5057   -447    595    353       C  
ATOM   1777  O   CYS B  93     -22.328  -1.088  30.926  1.00 41.81           O  
ANISOU 1777  O   CYS B  93     4337   6378   5171   -503    589    322       O  
ATOM   1778  CB  CYS B  93     -19.215  -1.969  30.955  1.00 40.87           C  
ANISOU 1778  CB  CYS B  93     4449   6057   5024   -436    535    458       C  
ATOM   1779  SG  CYS B  93     -17.592  -1.924  30.033  1.00 41.93           S  
ANISOU 1779  SG  CYS B  93     4711   6024   5195   -377    459    417       S  
ATOM   1780  N   ASP B  94     -21.385  -0.820  32.950  1.00 43.33           N  
ANISOU 1780  N   ASP B  94     4530   6797   5135   -433    663    427       N  
ATOM   1781  CA  ASP B  94     -22.604  -1.141  33.709  1.00 44.81           C  
ANISOU 1781  CA  ASP B  94     4597   7131   5298   -488    752    496       C  
ATOM   1782  C   ASP B  94     -23.445   0.108  33.996  1.00 44.18           C  
ANISOU 1782  C   ASP B  94     4431   7212   5145   -426    771    347       C  
ATOM   1783  O   ASP B  94     -24.685   0.074  33.895  1.00 45.52           O  
ANISOU 1783  O   ASP B  94     4493   7437   5367   -466    811    332       O  
ATOM   1784  CB  ASP B  94     -22.251  -1.863  35.026  1.00 46.85           C  
ANISOU 1784  CB  ASP B  94     4840   7515   5445   -510    828    678       C  
ATOM   1785  CG  ASP B  94     -21.927  -3.362  34.830  1.00 50.13           C  
ANISOU 1785  CG  ASP B  94     5299   7771   5979   -595    840    867       C  
ATOM   1786  OD1 ASP B  94     -22.720  -4.054  34.148  1.00 54.61           O  
ANISOU 1786  OD1 ASP B  94     5833   8218   6698   -685    849    890       O  
ATOM   1787  OD2 ASP B  94     -20.903  -3.853  35.378  1.00 52.65           O  
ANISOU 1787  OD2 ASP B  94     5677   8083   6244   -572    840    992       O  
ATOM   1788  N   LYS B  95     -22.779   1.194  34.379  1.00 42.64           N  
ANISOU 1788  N   LYS B  95     4274   7089   4837   -330    745    235       N  
ATOM   1789  CA  LYS B  95     -23.443   2.471  34.666  1.00 41.86           C  
ANISOU 1789  CA  LYS B  95     4107   7120   4679   -252    761     74       C  
ATOM   1790  C   LYS B  95     -23.631   3.324  33.405  1.00 39.40           C  
ANISOU 1790  C   LYS B  95     3819   6665   4485   -206    677    -74       C  
ATOM   1791  O   LYS B  95     -24.733   3.787  33.110  1.00 38.52           O  
ANISOU 1791  O   LYS B  95     3618   6591   4429   -189    689   -147       O  
ATOM   1792  CB  LYS B  95     -22.645   3.269  35.703  1.00 41.90           C  
ANISOU 1792  CB  LYS B  95     4144   7264   4514   -176    771      7       C  
ATOM   1793  CG  LYS B  95     -23.090   4.745  35.830  1.00 43.68           C  
ANISOU 1793  CG  LYS B  95     4329   7563   4704    -79    770   -201       C  
ATOM   1794  CD  LYS B  95     -22.550   5.461  37.096  1.00 46.20           C  
ANISOU 1794  CD  LYS B  95     4654   8067   4834    -18    802   -282       C  
ATOM   1795  CE  LYS B  95     -23.452   6.643  37.460  1.00 48.86           C  
ANISOU 1795  CE  LYS B  95     4908   8515   5140     65    848   -467       C  
ATOM   1796  NZ  LYS B  95     -22.784   7.680  38.277  1.00 49.37           N  
ANISOU 1796  NZ  LYS B  95     5008   8679   5070    138    842   -624       N  
ATOM   1797  N   LEU B  96     -22.543   3.544  32.675  1.00 37.29           N  
ANISOU 1797  N   LEU B  96     3668   6247   4253   -182    593   -107       N  
ATOM   1798  CA  LEU B  96     -22.569   4.458  31.529  1.00 36.16           C  
ANISOU 1798  CA  LEU B  96     3558   5980   4200   -131    512   -233       C  
ATOM   1799  C   LEU B  96     -22.931   3.843  30.163  1.00 35.28           C  
ANISOU 1799  C   LEU B  96     3461   5716   4228   -189    457   -203       C  
ATOM   1800  O   LEU B  96     -23.411   4.543  29.269  1.00 34.57           O  
ANISOU 1800  O   LEU B  96     3355   5572   4207   -153    403   -291       O  
ATOM   1801  CB  LEU B  96     -21.251   5.224  31.437  1.00 35.10           C  
ANISOU 1801  CB  LEU B  96     3529   5780   4026    -71    454   -301       C  
ATOM   1802  CG  LEU B  96     -20.901   5.932  32.736  1.00 36.67           C  
ANISOU 1802  CG  LEU B  96     3714   6134   4085    -17    494   -363       C  
ATOM   1803  CD1 LEU B  96     -19.512   6.511  32.634  1.00 36.61           C  
ANISOU 1803  CD1 LEU B  96     3807   6055   4050     17    430   -414       C  
ATOM   1804  CD2 LEU B  96     -21.946   6.995  33.094  1.00 34.22           C  
ANISOU 1804  CD2 LEU B  96     3315   5923   3763     51    530   -499       C  
ATOM   1805  N   HIS B  97     -22.718   2.542  29.998  1.00 35.14           N  
ANISOU 1805  N   HIS B  97     3471   5630   4252   -277    469    -82       N  
ATOM   1806  CA  HIS B  97     -23.022   1.884  28.719  1.00 34.78           C  
ANISOU 1806  CA  HIS B  97     3444   5442   4331   -342    416    -73       C  
ATOM   1807  C   HIS B  97     -22.294   2.573  27.529  1.00 31.41           C  
ANISOU 1807  C   HIS B  97     3112   4888   3937   -290    323   -162       C  
ATOM   1808  O   HIS B  97     -22.896   2.892  26.512  1.00 30.37           O  
ANISOU 1808  O   HIS B  97     2959   4711   3868   -289    267   -223       O  
ATOM   1809  CB  HIS B  97     -24.540   1.859  28.449  1.00 36.15           C  
ANISOU 1809  CB  HIS B  97     3490   5677   4569   -382    427    -96       C  
ATOM   1810  CG  HIS B  97     -25.401   1.546  29.644  1.00 41.39           C  
ANISOU 1810  CG  HIS B  97     4035   6504   5189   -415    527    -30       C  
ATOM   1811  ND1 HIS B  97     -25.701   0.257  30.043  1.00 45.77           N  
ANISOU 1811  ND1 HIS B  97     4554   7058   5778   -525    586    104       N  
ATOM   1812  CD2 HIS B  97     -26.104   2.363  30.470  1.00 45.66           C  
ANISOU 1812  CD2 HIS B  97     4474   7213   5660   -354    582    -82       C  
ATOM   1813  CE1 HIS B  97     -26.513   0.296  31.088  1.00 47.32           C  
ANISOU 1813  CE1 HIS B  97     4633   7430   5916   -534    676    146       C  
ATOM   1814  NE2 HIS B  97     -26.765   1.563  31.374  1.00 47.99           N  
ANISOU 1814  NE2 HIS B  97     4676   7627   5931   -427    678     27       N  
ATOM   1815  N   VAL B  98     -20.994   2.812  27.668  1.00 29.62           N  
ANISOU 1815  N   VAL B  98     2979   4614   3659   -247    307   -160       N  
ATOM   1816  CA  VAL B  98     -20.195   3.360  26.559  1.00 26.65           C  
ANISOU 1816  CA  VAL B  98     2693   4120   3312   -209    231   -222       C  
ATOM   1817  C   VAL B  98     -19.924   2.176  25.650  1.00 25.76           C  
ANISOU 1817  C   VAL B  98     2635   3881   3271   -279    212   -170       C  
ATOM   1818  O   VAL B  98     -19.441   1.154  26.147  1.00 25.07           O  
ANISOU 1818  O   VAL B  98     2572   3767   3187   -320    254    -78       O  
ATOM   1819  CB  VAL B  98     -18.901   3.950  27.093  1.00 26.62           C  
ANISOU 1819  CB  VAL B  98     2757   4122   3237   -152    227   -233       C  
ATOM   1820  CG1 VAL B  98     -18.034   4.516  25.969  1.00 23.51           C  
ANISOU 1820  CG1 VAL B  98     2447   3612   2874   -120    160   -282       C  
ATOM   1821  CG2 VAL B  98     -19.215   5.056  28.185  1.00 27.02           C  
ANISOU 1821  CG2 VAL B  98     2749   4309   3209    -89    256   -303       C  
ATOM   1822  N   ASP B  99     -20.264   2.248  24.355  1.00 24.60           N  
ANISOU 1822  N   ASP B  99     2504   3659   3182   -294    152   -225       N  
ATOM   1823  CA  ASP B  99     -19.910   1.115  23.474  1.00 25.05           C  
ANISOU 1823  CA  ASP B  99     2624   3594   3301   -359    136   -201       C  
ATOM   1824  C   ASP B  99     -18.372   1.010  23.365  1.00 24.97           C  
ANISOU 1824  C   ASP B  99     2718   3505   3265   -320    137   -179       C  
ATOM   1825  O   ASP B  99     -17.693   2.032  23.195  1.00 25.26           O  
ANISOU 1825  O   ASP B  99     2790   3552   3256   -253    107   -220       O  
ATOM   1826  CB  ASP B  99     -20.565   1.176  22.085  1.00 24.62           C  
ANISOU 1826  CB  ASP B  99     2565   3498   3291   -388     67   -273       C  
ATOM   1827  CG  ASP B  99     -20.378  -0.139  21.292  1.00 24.56           C  
ANISOU 1827  CG  ASP B  99     2610   3373   3348   -469     61   -270       C  
ATOM   1828  OD1 ASP B  99     -19.246  -0.387  20.825  1.00 20.73           O  
ANISOU 1828  OD1 ASP B  99     2222   2801   2855   -447     58   -273       O  
ATOM   1829  OD2 ASP B  99     -21.348  -0.943  21.140  1.00 28.15           O  
ANISOU 1829  OD2 ASP B  99     3008   3820   3868   -558     62   -270       O  
ATOM   1830  N   PRO B 100     -17.814  -0.201  23.501  1.00 25.88           N  
ANISOU 1830  N   PRO B 100     2873   3540   3420   -361    172   -109       N  
ATOM   1831  CA  PRO B 100     -16.339  -0.402  23.484  1.00 26.59           C  
ANISOU 1831  CA  PRO B 100     3045   3564   3494   -317    180    -76       C  
ATOM   1832  C   PRO B 100     -15.616   0.096  22.239  1.00 26.90           C  
ANISOU 1832  C   PRO B 100     3153   3538   3528   -281    131   -152       C  
ATOM   1833  O   PRO B 100     -14.410   0.351  22.270  1.00 27.23           O  
ANISOU 1833  O   PRO B 100     3242   3562   3541   -231    133   -137       O  
ATOM   1834  CB  PRO B 100     -16.166  -1.922  23.571  1.00 27.61           C  
ANISOU 1834  CB  PRO B 100     3197   3590   3704   -371    222      2       C  
ATOM   1835  CG  PRO B 100     -17.438  -2.430  24.134  1.00 28.63           C  
ANISOU 1835  CG  PRO B 100     3247   3760   3869   -445    253     44       C  
ATOM   1836  CD  PRO B 100     -18.544  -1.424  23.871  1.00 27.17           C  
ANISOU 1836  CD  PRO B 100     2995   3676   3652   -446    216    -42       C  
ATOM   1837  N   GLU B 101     -16.332   0.229  21.137  1.00 27.90           N  
ANISOU 1837  N   GLU B 101     3280   3643   3677   -309     87   -226       N  
ATOM   1838  CA  GLU B 101     -15.754   0.892  19.970  1.00 27.75           C  
ANISOU 1838  CA  GLU B 101     3318   3596   3629   -272     40   -288       C  
ATOM   1839  C   GLU B 101     -15.266   2.281  20.338  1.00 25.45           C  
ANISOU 1839  C   GLU B 101     3023   3367   3280   -203     23   -292       C  
ATOM   1840  O   GLU B 101     -14.232   2.725  19.866  1.00 25.83           O  
ANISOU 1840  O   GLU B 101     3124   3386   3304   -165     13   -298       O  
ATOM   1841  CB  GLU B 101     -16.762   0.935  18.804  1.00 28.58           C  
ANISOU 1841  CB  GLU B 101     3409   3704   3746   -312    -15   -359       C  
ATOM   1842  CG  GLU B 101     -16.191   1.398  17.455  1.00 31.55           C  
ANISOU 1842  CG  GLU B 101     3850   4056   4080   -285    -60   -411       C  
ATOM   1843  CD  GLU B 101     -14.865   0.727  17.028  1.00 34.29           C  
ANISOU 1843  CD  GLU B 101     4280   4321   4427   -271    -23   -409       C  
ATOM   1844  OE1 GLU B 101     -14.669  -0.505  17.102  1.00 38.92           O  
ANISOU 1844  OE1 GLU B 101     4890   4829   5069   -307     16   -406       O  
ATOM   1845  OE2 GLU B 101     -13.983   1.471  16.601  1.00 40.66           O  
ANISOU 1845  OE2 GLU B 101     5125   5137   5186   -220    -31   -407       O  
ATOM   1846  N   ASN B 102     -15.960   2.964  21.220  1.00 24.27           N  
ANISOU 1846  N   ASN B 102     2809   3301   3113   -186     26   -292       N  
ATOM   1847  CA  ASN B 102     -15.474   4.303  21.628  1.00 23.48           C  
ANISOU 1847  CA  ASN B 102     2708   3242   2971   -123     11   -314       C  
ATOM   1848  C   ASN B 102     -14.131   4.319  22.371  1.00 22.67           C  
ANISOU 1848  C   ASN B 102     2638   3140   2836    -98     39   -276       C  
ATOM   1849  O   ASN B 102     -13.413   5.294  22.271  1.00 20.86           O  
ANISOU 1849  O   ASN B 102     2431   2907   2588    -61     16   -301       O  
ATOM   1850  CB  ASN B 102     -16.554   5.034  22.417  1.00 23.66           C  
ANISOU 1850  CB  ASN B 102     2651   3353   2986   -103     15   -343       C  
ATOM   1851  CG  ASN B 102     -17.814   5.204  21.590  1.00 23.15           C  
ANISOU 1851  CG  ASN B 102     2541   3298   2958   -115    -25   -378       C  
ATOM   1852  OD1 ASN B 102     -17.781   5.827  20.542  1.00 21.40           O  
ANISOU 1852  OD1 ASN B 102     2348   3040   2744    -92    -78   -405       O  
ATOM   1853  ND2 ASN B 102     -18.887   4.576  22.008  1.00 21.95           N  
ANISOU 1853  ND2 ASN B 102     2315   3197   2827   -157     -1   -367       N  
ATOM   1854  N   PHE B 103     -13.800   3.234  23.077  1.00 23.24           N  
ANISOU 1854  N   PHE B 103     2708   3214   2909   -121     83   -209       N  
ATOM   1855  CA  PHE B 103     -12.541   3.130  23.783  1.00 23.43           C  
ANISOU 1855  CA  PHE B 103     2751   3252   2900    -95    101   -160       C  
ATOM   1856  C   PHE B 103     -11.411   3.093  22.746  1.00 24.47           C  
ANISOU 1856  C   PHE B 103     2943   3300   3053    -78     86   -166       C  
ATOM   1857  O   PHE B 103     -10.398   3.783  22.904  1.00 24.56           O  
ANISOU 1857  O   PHE B 103     2965   3330   3038    -48     73   -169       O  
ATOM   1858  CB  PHE B 103     -12.431   1.878  24.650  1.00 23.83           C  
ANISOU 1858  CB  PHE B 103     2785   3313   2956   -117    149    -63       C  
ATOM   1859  CG  PHE B 103     -13.505   1.708  25.657  1.00 23.43           C  
ANISOU 1859  CG  PHE B 103     2670   3353   2880   -142    179    -34       C  
ATOM   1860  CD1 PHE B 103     -14.147   2.789  26.235  1.00 22.68           C  
ANISOU 1860  CD1 PHE B 103     2527   3362   2729   -123    171    -97       C  
ATOM   1861  CD2 PHE B 103     -13.843   0.434  26.077  1.00 26.56           C  
ANISOU 1861  CD2 PHE B 103     3050   3728   3312   -185    224     61       C  
ATOM   1862  CE1 PHE B 103     -15.150   2.604  27.173  1.00 22.65           C  
ANISOU 1862  CE1 PHE B 103     2454   3459   2694   -144    212    -72       C  
ATOM   1863  CE2 PHE B 103     -14.829   0.235  27.035  1.00 25.39           C  
ANISOU 1863  CE2 PHE B 103     2834   3676   3135   -216    263    104       C  
ATOM   1864  CZ  PHE B 103     -15.491   1.340  27.587  1.00 23.58           C  
ANISOU 1864  CZ  PHE B 103     2551   3572   2836   -193    259     34       C  
ATOM   1865  N   ARG B 104     -11.584   2.336  21.666  1.00 24.76           N  
ANISOU 1865  N   ARG B 104     3018   3255   3136   -102     88   -176       N  
ATOM   1866  CA  ARG B 104     -10.533   2.308  20.632  1.00 25.02           C  
ANISOU 1866  CA  ARG B 104     3104   3225   3175    -81     84   -189       C  
ATOM   1867  C   ARG B 104     -10.448   3.617  19.818  1.00 23.03           C  
ANISOU 1867  C   ARG B 104     2868   2988   2895    -64     42   -241       C  
ATOM   1868  O   ARG B 104      -9.343   4.005  19.380  1.00 22.77           O  
ANISOU 1868  O   ARG B 104     2861   2941   2851    -41     44   -234       O  
ATOM   1869  CB  ARG B 104     -10.640   1.035  19.758  1.00 26.11           C  
ANISOU 1869  CB  ARG B 104     3282   3274   3364   -108    107   -199       C  
ATOM   1870  CG  ARG B 104     -11.086   1.270  18.365  1.00 31.17           C  
ANISOU 1870  CG  ARG B 104     3956   3892   3995   -126     75   -274       C  
ATOM   1871  CD  ARG B 104      -9.941   1.456  17.389  1.00 34.71           C  
ANISOU 1871  CD  ARG B 104     4453   4315   4418    -93     83   -291       C  
ATOM   1872  NE  ARG B 104     -10.366   2.204  16.197  1.00 36.66           N  
ANISOU 1872  NE  ARG B 104     4721   4589   4619   -100     40   -344       N  
ATOM   1873  CZ  ARG B 104     -11.150   1.715  15.237  1.00 42.05           C  
ANISOU 1873  CZ  ARG B 104     5424   5259   5294   -137     18   -404       C  
ATOM   1874  NH1 ARG B 104     -11.634   0.481  15.316  1.00 43.36           N  
ANISOU 1874  NH1 ARG B 104     5593   5369   5511   -177     38   -431       N  
ATOM   1875  NH2 ARG B 104     -11.481   2.475  14.192  1.00 46.22           N  
ANISOU 1875  NH2 ARG B 104     5966   5833   5764   -137    -28   -434       N  
ATOM   1876  N   LEU B 105     -11.560   4.353  19.696  1.00 21.71           N  
ANISOU 1876  N   LEU B 105     2676   2852   2722    -71      7   -281       N  
ATOM   1877  CA  LEU B 105     -11.515   5.690  19.008  1.00 20.76           C  
ANISOU 1877  CA  LEU B 105     2567   2735   2588    -47    -36   -310       C  
ATOM   1878  C   LEU B 105     -10.749   6.713  19.832  1.00 19.56           C  
ANISOU 1878  C   LEU B 105     2401   2605   2428    -20    -38   -306       C  
ATOM   1879  O   LEU B 105     -10.012   7.503  19.279  1.00 19.60           O  
ANISOU 1879  O   LEU B 105     2430   2584   2433     -8    -54   -303       O  
ATOM   1880  CB  LEU B 105     -12.895   6.237  18.644  1.00 20.81           C  
ANISOU 1880  CB  LEU B 105     2541   2763   2602    -48    -78   -344       C  
ATOM   1881  CG  LEU B 105     -13.669   5.520  17.520  1.00 22.67           C  
ANISOU 1881  CG  LEU B 105     2789   2988   2838    -82   -100   -363       C  
ATOM   1882  CD1 LEU B 105     -15.078   6.100  17.369  1.00 20.09           C  
ANISOU 1882  CD1 LEU B 105     2406   2706   2524    -77   -148   -388       C  
ATOM   1883  CD2 LEU B 105     -12.933   5.461  16.157  1.00 15.00           C  
ANISOU 1883  CD2 LEU B 105     1880   1985   1833    -82   -111   -365       C  
ATOM   1884  N   LEU B 106     -10.873   6.646  21.156  1.00 19.51           N  
ANISOU 1884  N   LEU B 106     2353   2650   2408    -17    -21   -305       N  
ATOM   1885  CA  LEU B 106     -10.171   7.556  22.052  1.00 18.92           C  
ANISOU 1885  CA  LEU B 106     2261   2610   2316      0    -28   -322       C  
ATOM   1886  C   LEU B 106      -8.694   7.167  22.085  1.00 19.24           C  
ANISOU 1886  C   LEU B 106     2319   2644   2349     -2    -13   -277       C  
ATOM   1887  O   LEU B 106      -7.823   8.044  22.126  1.00 19.58           O  
ANISOU 1887  O   LEU B 106     2363   2683   2395      1    -31   -290       O  
ATOM   1888  CB  LEU B 106     -10.783   7.562  23.473  1.00 18.71           C  
ANISOU 1888  CB  LEU B 106     2183   2671   2256      5    -12   -342       C  
ATOM   1889  CG  LEU B 106      -9.924   8.428  24.433  1.00 20.64           C  
ANISOU 1889  CG  LEU B 106     2411   2964   2468     16    -24   -378       C  
ATOM   1890  CD1 LEU B 106      -9.768   9.884  23.896  1.00 21.19           C  
ANISOU 1890  CD1 LEU B 106     2497   2970   2583     29    -62   -442       C  
ATOM   1891  CD2 LEU B 106     -10.419   8.446  25.828  1.00 20.15           C  
ANISOU 1891  CD2 LEU B 106     2301   3011   2346     22     -6   -406       C  
ATOM   1892  N   GLY B 107      -8.414   5.868  22.034  1.00 18.67           N  
ANISOU 1892  N   GLY B 107     2256   2561   2277     -8     20   -223       N  
ATOM   1893  CA  GLY B 107      -7.053   5.379  21.866  1.00 19.34           C  
ANISOU 1893  CA  GLY B 107     2351   2630   2367      3     39   -175       C  
ATOM   1894  C   GLY B 107      -6.323   5.907  20.633  1.00 19.92           C  
ANISOU 1894  C   GLY B 107     2457   2655   2458      6     34   -186       C  
ATOM   1895  O   GLY B 107      -5.144   6.308  20.712  1.00 19.66           O  
ANISOU 1895  O   GLY B 107     2408   2636   2425     11     34   -167       O  
ATOM   1896  N   ASP B 108      -7.024   5.882  19.489  1.00 20.13           N  
ANISOU 1896  N   ASP B 108     2521   2637   2492     -2     29   -211       N  
ATOM   1897  CA  ASP B 108      -6.519   6.388  18.216  1.00 19.30           C  
ANISOU 1897  CA  ASP B 108     2449   2502   2383     -2     26   -213       C  
ATOM   1898  C   ASP B 108      -6.210   7.868  18.289  1.00 19.16           C  
ANISOU 1898  C   ASP B 108     2418   2488   2373     -6     -6   -217       C  
ATOM   1899  O   ASP B 108      -5.229   8.295  17.745  1.00 19.25           O  
ANISOU 1899  O   ASP B 108     2435   2491   2388    -11      4   -191       O  
ATOM   1900  CB  ASP B 108      -7.546   6.168  17.097  1.00 19.95           C  
ANISOU 1900  CB  ASP B 108     2566   2562   2451    -12     12   -241       C  
ATOM   1901  CG  ASP B 108      -7.568   4.732  16.561  1.00 22.26           C  
ANISOU 1901  CG  ASP B 108     2887   2827   2744    -17     48   -253       C  
ATOM   1902  OD1 ASP B 108      -6.727   3.914  16.972  1.00 26.96           O  
ANISOU 1902  OD1 ASP B 108     3478   3406   3361     -1     91   -227       O  
ATOM   1903  OD2 ASP B 108      -8.439   4.428  15.709  1.00 29.30           O  
ANISOU 1903  OD2 ASP B 108     3802   3710   3620    -35     31   -291       O  
ATOM   1904  N   ILE B 109      -7.093   8.644  18.927  1.00 19.15           N  
ANISOU 1904  N   ILE B 109     2398   2495   2383     -6    -41   -253       N  
ATOM   1905  CA  ILE B 109      -6.946  10.055  19.067  1.00 19.05           C  
ANISOU 1905  CA  ILE B 109     2377   2461   2399     -8    -72   -272       C  
ATOM   1906  C   ILE B 109      -5.799  10.373  20.011  1.00 19.25           C  
ANISOU 1906  C   ILE B 109     2371   2514   2431    -23    -69   -275       C  
ATOM   1907  O   ILE B 109      -5.046  11.304  19.764  1.00 20.59           O  
ANISOU 1907  O   ILE B 109     2539   2652   2634    -42    -82   -270       O  
ATOM   1908  CB  ILE B 109      -8.276  10.677  19.581  1.00 21.29           C  
ANISOU 1908  CB  ILE B 109     2644   2746   2701      9   -102   -324       C  
ATOM   1909  CG1 ILE B 109      -9.280  10.820  18.403  1.00 23.22           C  
ANISOU 1909  CG1 ILE B 109     2910   2960   2951     22   -126   -312       C  
ATOM   1910  CG2 ILE B 109      -8.023  12.043  20.279  1.00 20.22           C  
ANISOU 1910  CG2 ILE B 109     2489   2585   2607     11   -128   -371       C  
ATOM   1911  CD1 ILE B 109     -10.678  10.918  18.805  1.00 26.51           C  
ANISOU 1911  CD1 ILE B 109     3295   3398   3379     44   -144   -352       C  
ATOM   1912  N   LEU B 110      -5.601   9.597  21.069  1.00 18.46           N  
ANISOU 1912  N   LEU B 110     2239   2474   2299    -18    -55   -276       N  
ATOM   1913  CA  LEU B 110      -4.497   9.901  21.966  1.00 18.31           C  
ANISOU 1913  CA  LEU B 110     2180   2503   2273    -33    -65   -279       C  
ATOM   1914  C   LEU B 110      -3.179   9.724  21.222  1.00 18.03           C  
ANISOU 1914  C   LEU B 110     2141   2453   2256    -44    -45   -223       C  
ATOM   1915  O   LEU B 110      -2.273  10.544  21.343  1.00 17.74           O  
ANISOU 1915  O   LEU B 110     2077   2418   2245    -73    -63   -229       O  
ATOM   1916  CB  LEU B 110      -4.536   9.034  23.212  1.00 18.42           C  
ANISOU 1916  CB  LEU B 110     2159   2604   2235    -21    -56   -268       C  
ATOM   1917  CG  LEU B 110      -3.280   9.084  24.099  1.00 17.50           C  
ANISOU 1917  CG  LEU B 110     1991   2564   2094    -33    -72   -253       C  
ATOM   1918  CD1 LEU B 110      -3.106  10.459  24.645  1.00 15.58           C  
ANISOU 1918  CD1 LEU B 110     1728   2332   1859    -64   -115   -339       C  
ATOM   1919  CD2 LEU B 110      -3.380   8.042  25.184  1.00 17.01           C  
ANISOU 1919  CD2 LEU B 110     1899   2594   1971    -12    -60   -209       C  
ATOM   1920  N   ILE B 111      -3.089   8.665  20.406  1.00 18.33           N  
ANISOU 1920  N   ILE B 111     2204   2475   2287    -23     -5   -175       N  
ATOM   1921  CA  ILE B 111      -1.906   8.462  19.580  1.00 17.21           C  
ANISOU 1921  CA  ILE B 111     2055   2326   2158    -22     27   -128       C  
ATOM   1922  C   ILE B 111      -1.637   9.613  18.639  1.00 18.08           C  
ANISOU 1922  C   ILE B 111     2181   2396   2293    -52     19   -124       C  
ATOM   1923  O   ILE B 111      -0.510  10.055  18.503  1.00 17.84           O  
ANISOU 1923  O   ILE B 111     2115   2379   2286    -75     28    -95       O  
ATOM   1924  CB  ILE B 111      -2.025   7.189  18.829  1.00 18.14           C  
ANISOU 1924  CB  ILE B 111     2205   2424   2265     10     74   -104       C  
ATOM   1925  CG1 ILE B 111      -1.981   6.067  19.875  1.00 17.02           C  
ANISOU 1925  CG1 ILE B 111     2036   2312   2120     37     86    -81       C  
ATOM   1926  CG2 ILE B 111      -0.928   7.115  17.731  1.00 16.66           C  
ANISOU 1926  CG2 ILE B 111     2015   2232   2082     16    119    -71       C  
ATOM   1927  CD1 ILE B 111      -1.407   4.809  19.440  1.00 19.51           C  
ANISOU 1927  CD1 ILE B 111     2355   2606   2453     77    138    -44       C  
ATOM   1928  N   ILE B 112      -2.682  10.136  18.001  1.00 18.67           N  
ANISOU 1928  N   ILE B 112     2301   2424   2368    -54      1   -142       N  
ATOM   1929  CA  ILE B 112      -2.515  11.325  17.138  1.00 19.18           C  
ANISOU 1929  CA  ILE B 112     2382   2442   2462    -81    -11   -117       C  
ATOM   1930  C   ILE B 112      -2.024  12.560  17.922  1.00 18.82           C  
ANISOU 1930  C   ILE B 112     2301   2371   2478   -119    -46   -139       C  
ATOM   1931  O   ILE B 112      -1.161  13.308  17.456  1.00 18.03           O  
ANISOU 1931  O   ILE B 112     2186   2246   2417   -158    -40    -99       O  
ATOM   1932  CB  ILE B 112      -3.780  11.604  16.368  1.00 19.35           C  
ANISOU 1932  CB  ILE B 112     2452   2427   2472    -65    -33   -121       C  
ATOM   1933  CG1 ILE B 112      -3.845  10.631  15.179  1.00 21.43           C  
ANISOU 1933  CG1 ILE B 112     2751   2717   2674    -48      3    -94       C  
ATOM   1934  CG2 ILE B 112      -3.765  12.992  15.845  1.00 18.82           C  
ANISOU 1934  CG2 ILE B 112     2397   2301   2455    -86    -59    -88       C  
ATOM   1935  CD1 ILE B 112      -5.251  10.316  14.670  1.00 20.57           C  
ANISOU 1935  CD1 ILE B 112     2677   2606   2533    -30    -24   -119       C  
ATOM   1936  N   VAL B 113      -2.544  12.728  19.129  1.00 19.26           N  
ANISOU 1936  N   VAL B 113     2338   2440   2539   -114    -80   -208       N  
ATOM   1937  CA  VAL B 113      -2.099  13.787  20.040  1.00 18.95           C  
ANISOU 1937  CA  VAL B 113     2264   2386   2549   -152   -116   -263       C  
ATOM   1938  C   VAL B 113      -0.668  13.505  20.494  1.00 19.30           C  
ANISOU 1938  C   VAL B 113     2249   2496   2588   -185   -108   -242       C  
ATOM   1939  O   VAL B 113       0.166  14.393  20.462  1.00 18.73           O  
ANISOU 1939  O   VAL B 113     2148   2395   2573   -239   -123   -241       O  
ATOM   1940  CB  VAL B 113      -3.021  13.896  21.271  1.00 19.32           C  
ANISOU 1940  CB  VAL B 113     2303   2460   2576   -131   -145   -355       C  
ATOM   1941  CG1 VAL B 113      -2.425  14.845  22.335  1.00 17.23           C  
ANISOU 1941  CG1 VAL B 113     1999   2204   2345   -174   -183   -437       C  
ATOM   1942  CG2 VAL B 113      -4.445  14.295  20.827  1.00 16.53           C  
ANISOU 1942  CG2 VAL B 113     1992   2045   2245    -94   -154   -377       C  
ATOM   1943  N   LEU B 114      -0.336  12.279  20.876  1.00 19.66           N  
ANISOU 1943  N   LEU B 114     2269   2624   2575   -155    -86   -215       N  
ATOM   1944  CA  LEU B 114       1.086  12.029  21.219  1.00 19.83           C  
ANISOU 1944  CA  LEU B 114     2221   2715   2600   -178    -81   -180       C  
ATOM   1945  C   LEU B 114       1.978  12.332  19.996  1.00 19.87           C  
ANISOU 1945  C   LEU B 114     2216   2685   2647   -205    -44   -113       C  
ATOM   1946  O   LEU B 114       3.122  12.840  20.115  1.00 21.81           O  
ANISOU 1946  O   LEU B 114     2397   2956   2933   -255    -51    -96       O  
ATOM   1947  CB  LEU B 114       1.281  10.615  21.740  1.00 19.58           C  
ANISOU 1947  CB  LEU B 114     2163   2764   2511   -126    -60   -142       C  
ATOM   1948  CG  LEU B 114       0.575  10.294  23.063  1.00 19.55           C  
ANISOU 1948  CG  LEU B 114     2152   2823   2453   -108    -92   -186       C  
ATOM   1949  CD1 LEU B 114       0.716   8.824  23.424  1.00 17.74           C  
ANISOU 1949  CD1 LEU B 114     1906   2651   2183    -54    -63   -117       C  
ATOM   1950  CD2 LEU B 114       1.123  11.129  24.187  1.00 21.49           C  
ANISOU 1950  CD2 LEU B 114     2341   3137   2689   -153   -149   -246       C  
ATOM   1951  N   ALA B 115       1.466  12.066  18.807  1.00 18.71           N  
ANISOU 1951  N   ALA B 115     2128   2491   2488   -178     -4    -74       N  
ATOM   1952  CA  ALA B 115       2.252  12.275  17.593  1.00 19.42           C  
ANISOU 1952  CA  ALA B 115     2213   2571   2595   -198     43     -4       C  
ATOM   1953  C   ALA B 115       2.544  13.767  17.393  1.00 20.34           C  
ANISOU 1953  C   ALA B 115     2319   2623   2785   -271     17      7       C  
ATOM   1954  O   ALA B 115       3.694  14.183  17.085  1.00 20.65           O  
ANISOU 1954  O   ALA B 115     2301   2679   2865   -322     39     58       O  
ATOM   1955  CB  ALA B 115       1.547  11.679  16.401  1.00 18.47           C  
ANISOU 1955  CB  ALA B 115     2161   2432   2424   -156     84     23       C  
ATOM   1956  N   ALA B 116       1.511  14.575  17.582  1.00 19.92           N  
ANISOU 1956  N   ALA B 116     2315   2492   2762   -277    -27    -37       N  
ATOM   1957  CA  ALA B 116       1.647  16.021  17.457  1.00 22.01           C  
ANISOU 1957  CA  ALA B 116     2579   2663   3119   -340    -56    -32       C  
ATOM   1958  C   ALA B 116       2.634  16.589  18.479  1.00 24.10           C  
ANISOU 1958  C   ALA B 116     2770   2942   3445   -408    -90    -83       C  
ATOM   1959  O   ALA B 116       3.373  17.541  18.165  1.00 25.27           O  
ANISOU 1959  O   ALA B 116     2889   3034   3679   -484    -91    -48       O  
ATOM   1960  CB  ALA B 116       0.280  16.722  17.580  1.00 21.17           C  
ANISOU 1960  CB  ALA B 116     2534   2464   3045   -313    -98    -82       C  
ATOM   1961  N   HIS B 117       2.673  15.999  19.678  1.00 24.55           N  
ANISOU 1961  N   HIS B 117     2791   3081   3456   -389   -118   -159       N  
ATOM   1962  CA  HIS B 117       3.455  16.560  20.759  1.00 27.09           C  
ANISOU 1962  CA  HIS B 117     3043   3434   3816   -454   -167   -229       C  
ATOM   1963  C   HIS B 117       4.915  16.110  20.711  1.00 28.38           C  
ANISOU 1963  C   HIS B 117     3111   3694   3977   -489   -147   -167       C  
ATOM   1964  O   HIS B 117       5.785  16.809  21.229  1.00 29.97           O  
ANISOU 1964  O   HIS B 117     3243   3909   4237   -570   -185   -201       O  
ATOM   1965  CB  HIS B 117       2.820  16.243  22.123  1.00 27.41           C  
ANISOU 1965  CB  HIS B 117     3082   3540   3793   -420   -212   -337       C  
ATOM   1966  CG  HIS B 117       1.793  17.247  22.563  1.00 30.29           C  
ANISOU 1966  CG  HIS B 117     3497   3810   4202   -424   -249   -443       C  
ATOM   1967  ND1 HIS B 117       0.494  17.259  22.083  1.00 31.66           N  
ANISOU 1967  ND1 HIS B 117     3745   3914   4373   -363   -232   -441       N  
ATOM   1968  CD2 HIS B 117       1.880  18.278  23.446  1.00 33.86           C  
ANISOU 1968  CD2 HIS B 117     3930   4227   4706   -478   -301   -564       C  
ATOM   1969  CE1 HIS B 117      -0.165  18.254  22.662  1.00 34.77           C  
ANISOU 1969  CE1 HIS B 117     4159   4232   4822   -369   -268   -549       C  
ATOM   1970  NE2 HIS B 117       0.652  18.889  23.488  1.00 32.31           N  
ANISOU 1970  NE2 HIS B 117     3798   3934   4545   -440   -308   -632       N  
ATOM   1971  N   PHE B 118       5.188  14.975  20.072  1.00 28.98           N  
ANISOU 1971  N   PHE B 118     3182   3835   3995   -429    -88    -84       N  
ATOM   1972  CA  PHE B 118       6.542  14.405  20.031  1.00 30.19           C  
ANISOU 1972  CA  PHE B 118     3235   4090   4146   -438    -61    -23       C  
ATOM   1973  C   PHE B 118       7.220  14.449  18.684  1.00 30.44           C  
ANISOU 1973  C   PHE B 118     3251   4108   4205   -453     14     77       C  
ATOM   1974  O   PHE B 118       8.423  14.196  18.588  1.00 31.69           O  
ANISOU 1974  O   PHE B 118     3311   4348   4382   -471     42    128       O  
ATOM   1975  CB  PHE B 118       6.541  12.977  20.564  1.00 30.09           C  
ANISOU 1975  CB  PHE B 118     3204   4176   4053   -349    -49    -11       C  
ATOM   1976  CG  PHE B 118       6.341  12.913  22.030  1.00 33.17           C  
ANISOU 1976  CG  PHE B 118     3566   4633   4405   -349   -121    -83       C  
ATOM   1977  CD1 PHE B 118       7.405  13.186  22.895  1.00 37.55           C  
ANISOU 1977  CD1 PHE B 118     4011   5284   4971   -400   -173   -100       C  
ATOM   1978  CD2 PHE B 118       5.105  12.646  22.561  1.00 35.15           C  
ANISOU 1978  CD2 PHE B 118     3891   4864   4602   -305   -140   -137       C  
ATOM   1979  CE1 PHE B 118       7.240  13.168  24.240  1.00 38.48           C  
ANISOU 1979  CE1 PHE B 118     4103   5486   5033   -404   -244   -170       C  
ATOM   1980  CE2 PHE B 118       4.917  12.645  23.905  1.00 37.43           C  
ANISOU 1980  CE2 PHE B 118     4152   5231   4838   -308   -199   -202       C  
ATOM   1981  CZ  PHE B 118       5.993  12.901  24.757  1.00 40.30           C  
ANISOU 1981  CZ  PHE B 118     4413   5700   5198   -356   -253   -220       C  
ATOM   1982  N   ALA B 119       6.490  14.801  17.645  1.00 30.20           N  
ANISOU 1982  N   ALA B 119     3307   3992   4176   -446     47    111       N  
ATOM   1983  CA  ALA B 119       7.108  15.017  16.354  1.00 30.98           C  
ANISOU 1983  CA  ALA B 119     3393   4089   4289   -471    119    211       C  
ATOM   1984  C   ALA B 119       7.972  13.806  15.985  1.00 32.15           C  
ANISOU 1984  C   ALA B 119     3479   4352   4384   -412    191    257       C  
ATOM   1985  O   ALA B 119       7.515  12.671  16.128  1.00 31.73           O  
ANISOU 1985  O   ALA B 119     3461   4330   4266   -323    205    229       O  
ATOM   1986  CB  ALA B 119       7.902  16.309  16.375  1.00 31.69           C  
ANISOU 1986  CB  ALA B 119     3420   4134   4485   -588    100    239       C  
ATOM   1987  N   LYS B 120       9.224  14.003  15.569  1.00 33.75           N  
ANISOU 1987  N   LYS B 120     3584   4615   4624   -457    239    324       N  
ATOM   1988  CA  LYS B 120       9.945  12.916  14.906  1.00 34.78           C  
ANISOU 1988  CA  LYS B 120     3667   4843   4705   -386    330    372       C  
ATOM   1989  C   LYS B 120      10.446  11.822  15.866  1.00 34.62           C  
ANISOU 1989  C   LYS B 120     3573   4905   4676   -315    314    341       C  
ATOM   1990  O   LYS B 120      10.910  10.766  15.420  1.00 35.05           O  
ANISOU 1990  O   LYS B 120     3598   5021   4699   -231    388    366       O  
ATOM   1991  CB  LYS B 120      11.108  13.475  14.094  1.00 37.20           C  
ANISOU 1991  CB  LYS B 120     3882   5201   5052   -452    400    464       C  
ATOM   1992  CG  LYS B 120      10.698  14.660  13.167  1.00 40.86           C  
ANISOU 1992  CG  LYS B 120     4410   5581   5535   -532    414    526       C  
ATOM   1993  CD  LYS B 120      11.770  14.943  12.093  1.00 45.75           C  
ANISOU 1993  CD  LYS B 120     4949   6274   6161   -580    515    640       C  
ATOM   1994  CE  LYS B 120      11.228  15.882  11.015  1.00 47.46           C  
ANISOU 1994  CE  LYS B 120     5249   6420   6365   -633    541    726       C  
ATOM   1995  NZ  LYS B 120      12.232  16.168   9.938  1.00 50.54           N  
ANISOU 1995  NZ  LYS B 120     5560   6895   6746   -683    649    852       N  
ATOM   1996  N   GLU B 121      10.356  12.085  17.175  1.00 33.03           N  
ANISOU 1996  N   GLU B 121     3342   4706   4501   -344    220    287       N  
ATOM   1997  CA  GLU B 121      10.659  11.108  18.181  1.00 31.38           C  
ANISOU 1997  CA  GLU B 121     3075   4577   4273   -276    190    271       C  
ATOM   1998  C   GLU B 121       9.554  10.060  18.331  1.00 28.58           C  
ANISOU 1998  C   GLU B 121     2823   4181   3854   -178    195    239       C  
ATOM   1999  O   GLU B 121       9.803   9.018  18.933  1.00 27.71           O  
ANISOU 1999  O   GLU B 121     2674   4126   3729   -102    194    253       O  
ATOM   2000  CB  GLU B 121      10.896  11.789  19.542  1.00 32.07           C  
ANISOU 2000  CB  GLU B 121     3096   4701   4387   -348     83    220       C  
ATOM   2001  CG  GLU B 121      12.137  12.720  19.581  1.00 36.45           C  
ANISOU 2001  CG  GLU B 121     3521   5308   5019   -456     66    244       C  
ATOM   2002  CD  GLU B 121      12.706  12.971  21.002  1.00 37.76           C  
ANISOU 2002  CD  GLU B 121     3583   5569   5196   -505    -39    194       C  
ATOM   2003  OE1 GLU B 121      13.889  12.579  21.275  1.00 36.79           O  
ANISOU 2003  OE1 GLU B 121     3315   5571   5091   -499    -42    244       O  
ATOM   2004  OE2 GLU B 121      11.969  13.577  21.820  1.00 38.29           O  
ANISOU 2004  OE2 GLU B 121     3707   5594   5247   -549   -118    102       O  
ATOM   2005  N   PHE B 122       8.337  10.348  17.851  1.00 25.33           N  
ANISOU 2005  N   PHE B 122     2535   3676   3414   -184    194    203       N  
ATOM   2006  CA  PHE B 122       7.242   9.349  17.838  1.00 23.13           C  
ANISOU 2006  CA  PHE B 122     2350   3356   3082   -104    205    174       C  
ATOM   2007  C   PHE B 122       7.504   8.455  16.620  1.00 21.80           C  
ANISOU 2007  C   PHE B 122     2202   3189   2892    -38    303    205       C  
ATOM   2008  O   PHE B 122       6.873   8.592  15.591  1.00 21.05           O  
ANISOU 2008  O   PHE B 122     2188   3049   2763    -41    337    196       O  
ATOM   2009  CB  PHE B 122       5.879  10.046  17.705  1.00 23.00           C  
ANISOU 2009  CB  PHE B 122     2440   3252   3048   -137    166    123       C  
ATOM   2010  CG  PHE B 122       4.689   9.209  18.112  1.00 23.19           C  
ANISOU 2010  CG  PHE B 122     2536   3245   3028    -80    150     83       C  
ATOM   2011  CD1 PHE B 122       4.514   8.826  19.408  1.00 26.17           C  
ANISOU 2011  CD1 PHE B 122     2888   3661   3396    -63    103     62       C  
ATOM   2012  CD2 PHE B 122       3.712   8.891  17.202  1.00 25.09           C  
ANISOU 2012  CD2 PHE B 122     2868   3429   3236    -55    179     68       C  
ATOM   2013  CE1 PHE B 122       3.388   8.094  19.798  1.00 27.14           C  
ANISOU 2013  CE1 PHE B 122     3071   3757   3484    -22     94     36       C  
ATOM   2014  CE2 PHE B 122       2.596   8.157  17.568  1.00 24.22           C  
ANISOU 2014  CE2 PHE B 122     2814   3289   3098    -18    164     31       C  
ATOM   2015  CZ  PHE B 122       2.434   7.753  18.853  1.00 26.07           C  
ANISOU 2015  CZ  PHE B 122     3020   3554   3332     -3    127     20       C  
ATOM   2016  N   THR B 123       8.523   7.625  16.735  1.00 21.56           N  
ANISOU 2016  N   THR B 123     2086   3223   2882     20    346    242       N  
ATOM   2017  CA  THR B 123       9.045   6.821  15.655  1.00 21.71           C  
ANISOU 2017  CA  THR B 123     2099   3259   2892     87    448    261       C  
ATOM   2018  C   THR B 123       8.021   5.709  15.356  1.00 20.95           C  
ANISOU 2018  C   THR B 123     2110   3090   2760    160    473    211       C  
ATOM   2019  O   THR B 123       7.141   5.439  16.186  1.00 19.92           O  
ANISOU 2019  O   THR B 123     2028   2916   2627    165    413    186       O  
ATOM   2020  CB  THR B 123      10.338   6.153  16.099  1.00 23.22           C  
ANISOU 2020  CB  THR B 123     2160   3532   3132    146    478    308       C  
ATOM   2021  OG1 THR B 123      10.050   5.343  17.256  1.00 19.61           O  
ANISOU 2021  OG1 THR B 123     1698   3064   2687    203    424    309       O  
ATOM   2022  CG2 THR B 123      11.481   7.220  16.433  1.00 23.03           C  
ANISOU 2022  CG2 THR B 123     2003   3596   3152     62    448    356       C  
ATOM   2023  N   PRO B 124       8.135   5.047  14.184  1.00 20.90           N  
ANISOU 2023  N   PRO B 124     2137   3077   2726    213    565    191       N  
ATOM   2024  CA  PRO B 124       7.153   3.999  13.936  1.00 20.34           C  
ANISOU 2024  CA  PRO B 124     2166   2928   2633    268    580    129       C  
ATOM   2025  C   PRO B 124       7.104   2.965  15.068  1.00 21.71           C  
ANISOU 2025  C   PRO B 124     2318   3064   2865    331    553    140       C  
ATOM   2026  O   PRO B 124       6.032   2.524  15.458  1.00 20.61           O  
ANISOU 2026  O   PRO B 124     2253   2856   2722    331    516    109       O  
ATOM   2027  CB  PRO B 124       7.607   3.406  12.614  1.00 20.82           C  
ANISOU 2027  CB  PRO B 124     2240   3008   2661    321    688     96       C  
ATOM   2028  CG  PRO B 124       8.267   4.551  11.907  1.00 21.42           C  
ANISOU 2028  CG  PRO B 124     2271   3167   2702    259    715    144       C  
ATOM   2029  CD  PRO B 124       9.013   5.262  13.019  1.00 21.27           C  
ANISOU 2029  CD  PRO B 124     2143   3188   2751    215    656    213       C  
ATOM   2030  N   GLU B 125       8.249   2.638  15.648  1.00 23.58           N  
ANISOU 2030  N   GLU B 125     2445   3356   3158    381    568    199       N  
ATOM   2031  CA  GLU B 125       8.270   1.674  16.695  1.00 25.48           C  
ANISOU 2031  CA  GLU B 125     2659   3570   3451    447    542    235       C  
ATOM   2032  C   GLU B 125       7.665   2.204  17.992  1.00 25.33           C  
ANISOU 2032  C   GLU B 125     2640   3570   3413    388    437    260       C  
ATOM   2033  O   GLU B 125       7.038   1.463  18.733  1.00 24.99           O  
ANISOU 2033  O   GLU B 125     2631   3483   3383    419    411    276       O  
ATOM   2034  CB  GLU B 125       9.690   1.212  16.901  1.00 27.88           C  
ANISOU 2034  CB  GLU B 125     2834   3941   3817    524    583    301       C  
ATOM   2035  CG  GLU B 125      10.255   0.466  15.649  1.00 33.01           C  
ANISOU 2035  CG  GLU B 125     3485   4568   4491    607    706    262       C  
ATOM   2036  CD  GLU B 125      10.935   1.410  14.615  1.00 39.53           C  
ANISOU 2036  CD  GLU B 125     4267   5482   5271    557    760    252       C  
ATOM   2037  OE1 GLU B 125      11.545   0.861  13.647  1.00 42.03           O  
ANISOU 2037  OE1 GLU B 125     4563   5812   5594    628    868    223       O  
ATOM   2038  OE2 GLU B 125      10.865   2.679  14.782  1.00 37.03           O  
ANISOU 2038  OE2 GLU B 125     3935   5218   4916    448    700    273       O  
ATOM   2039  N   CYS B 126       7.850   3.485  18.271  1.00 25.65           N  
ANISOU 2039  N   CYS B 126     2643   3677   3426    302    381    261       N  
ATOM   2040  CA  CYS B 126       7.173   4.105  19.379  1.00 26.02           C  
ANISOU 2040  CA  CYS B 126     2702   3741   3442    243    289    253       C  
ATOM   2041  C   CYS B 126       5.669   4.081  19.181  1.00 24.89           C  
ANISOU 2041  C   CYS B 126     2681   3513   3265    219    276    194       C  
ATOM   2042  O   CYS B 126       4.917   3.915  20.139  1.00 24.77           O  
ANISOU 2042  O   CYS B 126     2687   3494   3230    213    227    193       O  
ATOM   2043  CB  CYS B 126       7.589   5.548  19.529  1.00 26.52           C  
ANISOU 2043  CB  CYS B 126     2716   3863   3497    149    239    239       C  
ATOM   2044  SG  CYS B 126       7.162   6.155  21.167  1.00 33.38           S  
ANISOU 2044  SG  CYS B 126     3561   4788   4331     96    127    221       S  
ATOM   2045  N   GLN B 127       5.227   4.267  17.936  1.00 23.62           N  
ANISOU 2045  N   GLN B 127     2590   3296   3086    204    320    149       N  
ATOM   2046  CA  GLN B 127       3.794   4.263  17.638  1.00 21.68           C  
ANISOU 2046  CA  GLN B 127     2448   2981   2808    180    304     93       C  
ATOM   2047  C   GLN B 127       3.301   2.869  17.914  1.00 21.02           C  
ANISOU 2047  C   GLN B 127     2398   2840   2747    240    327     94       C  
ATOM   2048  O   GLN B 127       2.258   2.713  18.509  1.00 21.43           O  
ANISOU 2048  O   GLN B 127     2490   2863   2788    221    290     80       O  
ATOM   2049  CB  GLN B 127       3.491   4.711  16.186  1.00 20.67           C  
ANISOU 2049  CB  GLN B 127     2381   2826   2645    156    340     55       C  
ATOM   2050  CG  GLN B 127       2.099   4.487  15.785  1.00 20.26           C  
ANISOU 2050  CG  GLN B 127     2422   2715   2562    144    324      1       C  
ATOM   2051  CD  GLN B 127       1.787   4.872  14.368  1.00 18.57           C  
ANISOU 2051  CD  GLN B 127     2264   2497   2296    124    351    -29       C  
ATOM   2052  OE1 GLN B 127       2.659   5.251  13.576  1.00 15.71           O  
ANISOU 2052  OE1 GLN B 127     1877   2178   1916    122    397     -4       O  
ATOM   2053  NE2 GLN B 127       0.510   4.818  14.047  1.00 17.86           N  
ANISOU 2053  NE2 GLN B 127     2243   2370   2174    106    320    -75       N  
ATOM   2054  N   ALA B 128       4.067   1.859  17.565  1.00 21.84           N  
ANISOU 2054  N   ALA B 128     2479   2926   2894    311    391    116       N  
ATOM   2055  CA  ALA B 128       3.587   0.456  17.731  1.00 23.15           C  
ANISOU 2055  CA  ALA B 128     2685   3004   3106    368    421    115       C  
ATOM   2056  C   ALA B 128       3.354   0.060  19.186  1.00 23.91           C  
ANISOU 2056  C   ALA B 128     2750   3113   3224    378    372    188       C  
ATOM   2057  O   ALA B 128       2.321  -0.593  19.505  1.00 23.57           O  
ANISOU 2057  O   ALA B 128     2761   3001   3194    370    365    183       O  
ATOM   2058  CB  ALA B 128       4.495  -0.533  17.043  1.00 22.46           C  
ANISOU 2058  CB  ALA B 128     2578   2878   3075    454    506    115       C  
ATOM   2059  N   ALA B 129       4.284   0.490  20.051  1.00 24.77           N  
ANISOU 2059  N   ALA B 129     2765   3319   3327    388    337    256       N  
ATOM   2060  CA  ALA B 129       4.205   0.205  21.497  1.00 26.21           C  
ANISOU 2060  CA  ALA B 129     2904   3553   3503    399    284    336       C  
ATOM   2061  C   ALA B 129       2.975   0.883  22.103  1.00 25.78           C  
ANISOU 2061  C   ALA B 129     2894   3518   3382    323    228    297       C  
ATOM   2062  O   ALA B 129       2.207   0.234  22.790  1.00 26.01           O  
ANISOU 2062  O   ALA B 129     2948   3524   3409    328    220    333       O  
ATOM   2063  CB  ALA B 129       5.503   0.670  22.243  1.00 26.46           C  
ANISOU 2063  CB  ALA B 129     2815   3715   3525    414    245    403       C  
ATOM   2064  N   TRP B 130       2.813   2.183  21.846  1.00 25.55           N  
ANISOU 2064  N   TRP B 130     2872   3529   3307    256    193    229       N  
ATOM   2065  CA  TRP B 130       1.628   2.922  22.293  1.00 26.34           C  
ANISOU 2065  CA  TRP B 130     3014   3639   3355    194    147    175       C  
ATOM   2066  C   TRP B 130       0.328   2.388  21.691  1.00 25.78           C  
ANISOU 2066  C   TRP B 130     3029   3472   3295    186    174    135       C  
ATOM   2067  O   TRP B 130      -0.702   2.337  22.358  1.00 25.50           O  
ANISOU 2067  O   TRP B 130     3012   3443   3234    163    152    128       O  
ATOM   2068  CB  TRP B 130       1.823   4.420  22.070  1.00 26.19           C  
ANISOU 2068  CB  TRP B 130     2983   3657   3312    134    109    114       C  
ATOM   2069  CG  TRP B 130       2.732   4.874  23.100  1.00 30.46           C  
ANISOU 2069  CG  TRP B 130     3437   4304   3832    123     62    142       C  
ATOM   2070  CD1 TRP B 130       4.095   4.773  23.096  1.00 33.65           C  
ANISOU 2070  CD1 TRP B 130     3760   4764   4263    145     67    193       C  
ATOM   2071  CD2 TRP B 130       2.372   5.364  24.390  1.00 33.29           C  
ANISOU 2071  CD2 TRP B 130     3770   4748   4132     93      1    122       C  
ATOM   2072  NE1 TRP B 130       4.607   5.234  24.289  1.00 34.39           N  
ANISOU 2072  NE1 TRP B 130     3776   4973   4316    121      1    204       N  
ATOM   2073  CE2 TRP B 130       3.569   5.597  25.099  1.00 34.82           C  
ANISOU 2073  CE2 TRP B 130     3869   5050   4312     90    -39    156       C  
ATOM   2074  CE3 TRP B 130       1.158   5.666  25.000  1.00 33.54           C  
ANISOU 2074  CE3 TRP B 130     3842   4786   4116     69    -22     72       C  
ATOM   2075  CZ2 TRP B 130       3.581   6.124  26.378  1.00 37.14           C  
ANISOU 2075  CZ2 TRP B 130     4117   5459   4535     58   -106    130       C  
ATOM   2076  CZ3 TRP B 130       1.174   6.177  26.271  1.00 36.19           C  
ANISOU 2076  CZ3 TRP B 130     4133   5235   4383     45    -76     48       C  
ATOM   2077  CH2 TRP B 130       2.370   6.405  26.948  1.00 35.53           C  
ANISOU 2077  CH2 TRP B 130     3964   5260   4277     38   -120     72       C  
ATOM   2078  N   GLN B 131       0.378   1.916  20.455  1.00 26.60           N  
ANISOU 2078  N   GLN B 131     3177   3497   3433    205    224    105       N  
ATOM   2079  CA  GLN B 131      -0.807   1.274  19.906  1.00 26.36           C  
ANISOU 2079  CA  GLN B 131     3219   3381   3416    192    243     62       C  
ATOM   2080  C   GLN B 131      -1.110   0.083  20.795  1.00 26.79           C  
ANISOU 2080  C   GLN B 131     3266   3402   3510    219    256    127       C  
ATOM   2081  O   GLN B 131      -2.234  -0.089  21.220  1.00 26.49           O  
ANISOU 2081  O   GLN B 131     3251   3351   3464    184    241    121       O  
ATOM   2082  CB  GLN B 131      -0.622   0.790  18.479  1.00 26.17           C  
ANISOU 2082  CB  GLN B 131     3243   3288   3413    212    296     10       C  
ATOM   2083  CG  GLN B 131      -1.897   0.245  17.877  1.00 26.32           C  
ANISOU 2083  CG  GLN B 131     3331   3232   3436    182    300    -53       C  
ATOM   2084  CD  GLN B 131      -3.031   1.258  17.913  1.00 27.37           C  
ANISOU 2084  CD  GLN B 131     3480   3401   3518    122    243    -92       C  
ATOM   2085  OE1 GLN B 131      -2.807   2.509  17.796  1.00 26.70           O  
ANISOU 2085  OE1 GLN B 131     3380   3373   3392    103    212    -97       O  
ATOM   2086  NE2 GLN B 131      -4.270   0.741  18.022  1.00 26.01           N  
ANISOU 2086  NE2 GLN B 131     3336   3188   3358     91    231   -118       N  
ATOM   2087  N   LYS B 132      -0.101  -0.739  21.055  1.00 27.00           N  
ANISOU 2087  N   LYS B 132     3255   3416   3586    282    288    198       N  
ATOM   2088  CA  LYS B 132      -0.336  -1.945  21.822  1.00 27.99           C  
ANISOU 2088  CA  LYS B 132     3377   3490   3766    314    306    282       C  
ATOM   2089  C   LYS B 132      -0.939  -1.561  23.195  1.00 27.04           C  
ANISOU 2089  C   LYS B 132     3225   3467   3582    278    256    339       C  
ATOM   2090  O   LYS B 132      -1.963  -2.128  23.570  1.00 25.36           O  
ANISOU 2090  O   LYS B 132     3039   3214   3383    250    263    360       O  
ATOM   2091  CB  LYS B 132       0.942  -2.772  21.967  1.00 29.63           C  
ANISOU 2091  CB  LYS B 132     3536   3679   4042    403    341    366       C  
ATOM   2092  CG  LYS B 132       0.737  -4.142  22.673  1.00 32.42           C  
ANISOU 2092  CG  LYS B 132     3892   3949   4478    447    367    474       C  
ATOM   2093  CD  LYS B 132       1.747  -5.167  22.179  1.00 35.41           C  
ANISOU 2093  CD  LYS B 132     4256   4230   4967    545    427    508       C  
ATOM   2094  CE  LYS B 132       2.131  -6.173  23.247  1.00 36.89           C  
ANISOU 2094  CE  LYS B 132     4399   4394   5224    615    430    672       C  
ATOM   2095  NZ  LYS B 132       3.280  -6.960  22.752  1.00 38.48           N  
ANISOU 2095  NZ  LYS B 132     4569   4518   5536    727    486    700       N  
ATOM   2096  N   LEU B 133      -0.341  -0.550  23.865  1.00 25.85           N  
ANISOU 2096  N   LEU B 133     3016   3447   3359    269    207    348       N  
ATOM   2097  CA  LEU B 133      -0.844  -0.039  25.164  1.00 25.43           C  
ANISOU 2097  CA  LEU B 133     2930   3512   3222    236    159    375       C  
ATOM   2098  C   LEU B 133      -2.280   0.473  25.145  1.00 24.48           C  
ANISOU 2098  C   LEU B 133     2853   3384   3065    174    150    298       C  
ATOM   2099  O   LEU B 133      -3.044   0.109  26.017  1.00 25.10           O  
ANISOU 2099  O   LEU B 133     2923   3501   3113    160    151    344       O  
ATOM   2100  CB  LEU B 133       0.033   1.066  25.718  1.00 24.99           C  
ANISOU 2100  CB  LEU B 133     2810   3587   3100    226    105    358       C  
ATOM   2101  CG  LEU B 133      -0.376   1.626  27.080  1.00 27.36           C  
ANISOU 2101  CG  LEU B 133     3072   4025   3297    195     56    363       C  
ATOM   2102  CD1 LEU B 133      -0.219   0.567  28.149  1.00 30.63           C  
ANISOU 2102  CD1 LEU B 133     3447   4501   3688    236     59    504       C  
ATOM   2103  CD2 LEU B 133       0.484   2.794  27.422  1.00 28.08           C  
ANISOU 2103  CD2 LEU B 133     3109   4223   3337    171     -1    309       C  
ATOM   2104  N   VAL B 134      -2.641   1.325  24.183  1.00 22.90           N  
ANISOU 2104  N   VAL B 134     2689   3146   2865    142    142    192       N  
ATOM   2105  CA  VAL B 134      -3.984   1.869  24.175  1.00 21.65           C  
ANISOU 2105  CA  VAL B 134     2559   2990   2679     95    128    123       C  
ATOM   2106  C   VAL B 134      -4.985   0.758  23.894  1.00 22.39           C  
ANISOU 2106  C   VAL B 134     2688   2998   2822     83    164    143       C  
ATOM   2107  O   VAL B 134      -6.127   0.823  24.345  1.00 21.88           O  
ANISOU 2107  O   VAL B 134     2619   2959   2735     48    160    130       O  
ATOM   2108  CB  VAL B 134      -4.174   3.108  23.205  1.00 20.87           C  
ANISOU 2108  CB  VAL B 134     2487   2869   2574     69    103     21       C  
ATOM   2109  CG1 VAL B 134      -3.149   4.171  23.493  1.00 15.80           C  
ANISOU 2109  CG1 VAL B 134     1807   2292   1905     68     69      5       C  
ATOM   2110  CG2 VAL B 134      -4.189   2.678  21.698  1.00 20.18           C  
ANISOU 2110  CG2 VAL B 134     2453   2678   2535     73    133     -9       C  
ATOM   2111  N   ARG B 135      -4.546  -0.251  23.159  1.00 23.96           N  
ANISOU 2111  N   ARG B 135     2915   3094   3093    108    202    167       N  
ATOM   2112  CA  ARG B 135      -5.368  -1.412  22.873  1.00 26.91           C  
ANISOU 2112  CA  ARG B 135     3324   3365   3534     90    237    180       C  
ATOM   2113  C   ARG B 135      -5.632  -2.195  24.176  1.00 28.23           C  
ANISOU 2113  C   ARG B 135     3457   3561   3709     91    252    299       C  
ATOM   2114  O   ARG B 135      -6.760  -2.685  24.391  1.00 29.26           O  
ANISOU 2114  O   ARG B 135     3594   3662   3863     43    266    311       O  
ATOM   2115  CB  ARG B 135      -4.658  -2.347  21.872  1.00 28.34           C  
ANISOU 2115  CB  ARG B 135     3543   3425   3798    128    280    169       C  
ATOM   2116  CG  ARG B 135      -5.498  -2.871  20.712  1.00 33.64           C  
ANISOU 2116  CG  ARG B 135     4275   3988   4518     90    298     76       C  
ATOM   2117  CD  ARG B 135      -4.599  -3.491  19.591  1.00 40.03           C  
ANISOU 2117  CD  ARG B 135     5123   4706   5381    137    341     29       C  
ATOM   2118  NE  ARG B 135      -3.795  -4.619  20.112  1.00 44.36           N  
ANISOU 2118  NE  ARG B 135     5657   5178   6019    200    386    120       N  
ATOM   2119  CZ  ARG B 135      -2.475  -4.806  19.934  1.00 47.38           C  
ANISOU 2119  CZ  ARG B 135     6019   5556   6429    280    417    149       C  
ATOM   2120  NH1 ARG B 135      -1.732  -3.962  19.193  1.00 48.44           N  
ANISOU 2120  NH1 ARG B 135     6144   5757   6503    299    416     91       N  
ATOM   2121  NH2 ARG B 135      -1.881  -5.869  20.493  1.00 48.77           N  
ANISOU 2121  NH2 ARG B 135     6174   5657   6698    343    453    247       N  
ATOM   2122  N   VAL B 136      -4.608  -2.357  25.027  1.00 28.29           N  
ANISOU 2122  N   VAL B 136     3421   3631   3697    141    249    398       N  
ATOM   2123  CA  VAL B 136      -4.783  -3.205  26.204  1.00 29.43           C  
ANISOU 2123  CA  VAL B 136     3534   3804   3844    149    265    537       C  
ATOM   2124  C   VAL B 136      -5.591  -2.457  27.233  1.00 29.15           C  
ANISOU 2124  C   VAL B 136     3462   3917   3698    106    240    537       C  
ATOM   2125  O   VAL B 136      -6.387  -3.065  27.946  1.00 30.36           O  
ANISOU 2125  O   VAL B 136     3602   4086   3848     77    265    617       O  
ATOM   2126  CB  VAL B 136      -3.460  -3.773  26.815  1.00 30.47           C  
ANISOU 2126  CB  VAL B 136     3623   3962   3992    226    267    667       C  
ATOM   2127  CG1 VAL B 136      -2.641  -4.539  25.751  1.00 30.51           C  
ANISOU 2127  CG1 VAL B 136     3658   3814   4118    282    304    656       C  
ATOM   2128  CG2 VAL B 136      -2.633  -2.702  27.468  1.00 30.28           C  
ANISOU 2128  CG2 VAL B 136     3541   4109   3857    243    212    660       C  
ATOM   2129  N   VAL B 137      -5.445  -1.136  27.277  1.00 28.68           N  
ANISOU 2129  N   VAL B 137     3386   3959   3553     98    197    440       N  
ATOM   2130  CA  VAL B 137      -6.286  -0.331  28.174  1.00 28.88           C  
ANISOU 2130  CA  VAL B 137     3380   4118   3476     63    179    405       C  
ATOM   2131  C   VAL B 137      -7.749  -0.421  27.760  1.00 28.36           C  
ANISOU 2131  C   VAL B 137     3335   3999   3443     12    204    351       C  
ATOM   2132  O   VAL B 137      -8.598  -0.633  28.624  1.00 28.52           O  
ANISOU 2132  O   VAL B 137     3323   4094   3419    -15    225    397       O  
ATOM   2133  CB  VAL B 137      -5.834   1.142  28.277  1.00 28.89           C  
ANISOU 2133  CB  VAL B 137     3363   4213   3401     64    129    296       C  
ATOM   2134  CG1 VAL B 137      -6.865   1.982  29.096  1.00 29.33           C  
ANISOU 2134  CG1 VAL B 137     3393   4386   3366     35    120    228       C  
ATOM   2135  CG2 VAL B 137      -4.494   1.202  28.942  1.00 29.17           C  
ANISOU 2135  CG2 VAL B 137     3355   4338   3389    101     98    357       C  
ATOM   2136  N   ALA B 138      -8.035  -0.312  26.447  1.00 27.20           N  
ANISOU 2136  N   ALA B 138     3233   3734   3367     -3    201    261       N  
ATOM   2137  CA  ALA B 138      -9.425  -0.458  25.935  1.00 26.96           C  
ANISOU 2137  CA  ALA B 138     3214   3654   3376    -55    214    208       C  
ATOM   2138  C   ALA B 138     -10.040  -1.799  26.272  1.00 27.44           C  
ANISOU 2138  C   ALA B 138     3269   3658   3500    -89    259    306       C  
ATOM   2139  O   ALA B 138     -11.219  -1.858  26.588  1.00 27.66           O  
ANISOU 2139  O   ALA B 138     3265   3721   3522   -137    274    304       O  
ATOM   2140  CB  ALA B 138      -9.519  -0.257  24.402  1.00 26.04           C  
ANISOU 2140  CB  ALA B 138     3148   3430   3315    -63    197    108       C  
ATOM   2141  N   HIS B 139      -9.243  -2.859  26.143  1.00 27.81           N  
ANISOU 2141  N   HIS B 139     3341   3606   3618    -64    284    389       N  
ATOM   2142  CA  HIS B 139      -9.652  -4.247  26.466  1.00 29.45           C  
ANISOU 2142  CA  HIS B 139     3549   3724   3916    -94    331    502       C  
ATOM   2143  C   HIS B 139      -9.929  -4.374  27.983  1.00 29.75           C  
ANISOU 2143  C   HIS B 139     3528   3897   3878   -101    351    637       C  
ATOM   2144  O   HIS B 139     -10.925  -4.934  28.374  1.00 29.46           O  
ANISOU 2144  O   HIS B 139     3468   3856   3870   -159    386    695       O  
ATOM   2145  CB  HIS B 139      -8.537  -5.214  26.023  1.00 29.72           C  
ANISOU 2145  CB  HIS B 139     3623   3620   4049    -41    352    557       C  
ATOM   2146  CG  HIS B 139      -8.902  -6.660  26.099  1.00 34.58           C  
ANISOU 2146  CG  HIS B 139     4255   4089   4795    -69    401    654       C  
ATOM   2147  ND1 HIS B 139      -8.457  -7.492  27.110  1.00 39.24           N  
ANISOU 2147  ND1 HIS B 139     4821   4674   5415    -37    430    836       N  
ATOM   2148  CD2 HIS B 139      -9.659  -7.436  25.282  1.00 38.80           C  
ANISOU 2148  CD2 HIS B 139     4828   4469   5448   -131    423    596       C  
ATOM   2149  CE1 HIS B 139      -8.940  -8.712  26.918  1.00 42.36           C  
ANISOU 2149  CE1 HIS B 139     5241   4900   5954    -78    473    892       C  
ATOM   2150  NE2 HIS B 139      -9.677  -8.708  25.820  1.00 39.83           N  
ANISOU 2150  NE2 HIS B 139     4958   4484   5691   -140    469    739       N  
ATOM   2151  N   ALA B 140      -9.031  -3.818  28.814  1.00 30.11           N  
ANISOU 2151  N   ALA B 140     3545   4077   3820    -46    328    682       N  
ATOM   2152  CA  ALA B 140      -9.180  -3.826  30.285  1.00 30.66           C  
ANISOU 2152  CA  ALA B 140     3556   4314   3779    -45    340    802       C  
ATOM   2153  C   ALA B 140     -10.470  -3.105  30.677  1.00 30.38           C  
ANISOU 2153  C   ALA B 140     3483   4394   3664    -98    350    728       C  
ATOM   2154  O   ALA B 140     -11.152  -3.526  31.581  1.00 30.72           O  
ANISOU 2154  O   ALA B 140     3485   4523   3666   -130    391    828       O  
ATOM   2155  CB  ALA B 140      -7.989  -3.151  30.963  1.00 30.00           C  
ANISOU 2155  CB  ALA B 140     3445   4371   3583     16    295    817       C  
ATOM   2156  N   LEU B 141     -10.785  -2.031  29.968  1.00 29.37           N  
ANISOU 2156  N   LEU B 141     3368   4268   3523   -103    318    560       N  
ATOM   2157  CA  LEU B 141     -11.962  -1.249  30.252  1.00 30.13           C  
ANISOU 2157  CA  LEU B 141     3424   4467   3559   -135    325    475       C  
ATOM   2158  C   LEU B 141     -13.221  -1.977  29.799  1.00 31.35           C  
ANISOU 2158  C   LEU B 141     3567   4537   3808   -203    363    490       C  
ATOM   2159  O   LEU B 141     -14.268  -1.866  30.443  1.00 32.45           O  
ANISOU 2159  O   LEU B 141     3646   4781   3902   -238    398    501       O  
ATOM   2160  CB  LEU B 141     -11.863   0.091  29.562  1.00 29.05           C  
ANISOU 2160  CB  LEU B 141     3304   4330   3402   -111    275    308       C  
ATOM   2161  CG  LEU B 141     -12.318   1.376  30.235  1.00 30.08           C  
ANISOU 2161  CG  LEU B 141     3393   4610   3427    -95    263    206       C  
ATOM   2162  CD1 LEU B 141     -11.833   1.521  31.694  1.00 33.34           C  
ANISOU 2162  CD1 LEU B 141     3765   5201   3701    -74    271    262       C  
ATOM   2163  CD2 LEU B 141     -11.815   2.508  29.400  1.00 28.80           C  
ANISOU 2163  CD2 LEU B 141     3267   4392   3285    -66    208     75       C  
ATOM   2164  N   ALA B 142     -13.113  -2.753  28.723  1.00 31.96           N  
ANISOU 2164  N   ALA B 142     3694   4435   4015   -224    360    486       N  
ATOM   2165  CA  ALA B 142     -14.250  -3.498  28.187  1.00 32.85           C  
ANISOU 2165  CA  ALA B 142     3796   4454   4230   -301    386    484       C  
ATOM   2166  C   ALA B 142     -14.506  -4.783  28.941  1.00 35.17           C  
ANISOU 2166  C   ALA B 142     4068   4715   4580   -348    445    653       C  
ATOM   2167  O   ALA B 142     -15.446  -5.497  28.586  1.00 35.93           O  
ANISOU 2167  O   ALA B 142     4148   4727   4776   -427    470    663       O  
ATOM   2168  CB  ALA B 142     -14.037  -3.818  26.686  1.00 31.45           C  
ANISOU 2168  CB  ALA B 142     3686   4101   4163   -312    356    390       C  
ATOM   2169  N   ARG B 143     -13.698  -5.098  29.959  1.00 36.59           N  
ANISOU 2169  N   ARG B 143     4241   4960   4700   -304    465    793       N  
ATOM   2170  CA  ARG B 143     -13.761  -6.434  30.594  1.00 39.53           C  
ANISOU 2170  CA  ARG B 143     4604   5270   5147   -339    521    986       C  
ATOM   2171  C   ARG B 143     -15.107  -6.828  31.201  1.00 40.29           C  
ANISOU 2171  C   ARG B 143     4631   5429   5250   -429    578   1062       C  
ATOM   2172  O   ARG B 143     -15.398  -8.033  31.307  1.00 41.05           O  
ANISOU 2172  O   ARG B 143     4727   5404   5467   -488    624   1196       O  
ATOM   2173  CB  ARG B 143     -12.677  -6.618  31.662  1.00 41.16           C  
ANISOU 2173  CB  ARG B 143     4802   5571   5266   -268    524   1141       C  
ATOM   2174  CG  ARG B 143     -11.485  -7.463  31.201  1.00 43.81           C  
ANISOU 2174  CG  ARG B 143     5196   5734   5716   -211    513   1212       C  
ATOM   2175  CD  ARG B 143     -10.250  -7.277  32.101  1.00 48.16           C  
ANISOU 2175  CD  ARG B 143     5729   6415   6157   -122    488   1322       C  
ATOM   2176  NE  ARG B 143     -10.073  -8.324  33.123  1.00 53.89           N  
ANISOU 2176  NE  ARG B 143     6427   7155   6894   -113    527   1567       N  
ATOM   2177  CZ  ARG B 143     -10.714  -8.399  34.300  1.00 58.17           C  
ANISOU 2177  CZ  ARG B 143     6911   7866   7324   -150    563   1699       C  
ATOM   2178  NH1 ARG B 143     -11.632  -7.500  34.673  1.00 56.93           N  
ANISOU 2178  NH1 ARG B 143     6711   7884   7036   -196    571   1600       N  
ATOM   2179  NH2 ARG B 143     -10.437  -9.412  35.121  1.00 61.85           N  
ANISOU 2179  NH2 ARG B 143     7360   8329   7813   -135    596   1943       N  
ATOM   2180  N   LYS B 144     -15.904  -5.824  31.590  1.00 39.91           N  
ANISOU 2180  N   LYS B 144     4521   5560   5084   -439    579    978       N  
ATOM   2181  CA  LYS B 144     -17.233  -6.045  32.169  1.00 41.19           C  
ANISOU 2181  CA  LYS B 144     4599   5815   5238   -520    639   1034       C  
ATOM   2182  C   LYS B 144     -18.330  -6.257  31.137  1.00 41.13           C  
ANISOU 2182  C   LYS B 144     4573   5691   5365   -605    634    933       C  
ATOM   2183  O   LYS B 144     -19.443  -6.640  31.484  1.00 41.97           O  
ANISOU 2183  O   LYS B 144     4602   5843   5502   -689    686    990       O  
ATOM   2184  CB  LYS B 144     -17.597  -4.908  33.126  1.00 41.46           C  
ANISOU 2184  CB  LYS B 144     4564   6106   5083   -482    653    986       C  
ATOM   2185  CG  LYS B 144     -16.740  -4.927  34.419  1.00 42.96           C  
ANISOU 2185  CG  LYS B 144     4748   6454   5121   -426    671   1123       C  
ATOM   2186  CD  LYS B 144     -17.250  -5.963  35.422  1.00 44.75           C  
ANISOU 2186  CD  LYS B 144     4919   6747   5336   -488    754   1348       C  
ATOM   2187  CE  LYS B 144     -16.177  -6.395  36.389  1.00 47.53           C  
ANISOU 2187  CE  LYS B 144     5288   7179   5592   -434    755   1528       C  
ATOM   2188  NZ  LYS B 144     -16.756  -7.159  37.552  1.00 50.69           N  
ANISOU 2188  NZ  LYS B 144     5621   7710   5930   -487    841   1755       N  
ATOM   2189  N   TYR B 145     -18.016  -6.062  29.863  1.00 40.46           N  
ANISOU 2189  N   TYR B 145     4552   5463   5356   -589    572    790       N  
ATOM   2190  CA  TYR B 145     -18.943  -6.451  28.799  1.00 41.40           C  
ANISOU 2190  CA  TYR B 145     4662   5460   5608   -676    556    701       C  
ATOM   2191  C   TYR B 145     -18.889  -7.934  28.491  1.00 42.67           C  
ANISOU 2191  C   TYR B 145     4861   5414   5939   -752    584    794       C  
ATOM   2192  O   TYR B 145     -19.828  -8.468  27.900  1.00 43.42           O  
ANISOU 2192  O   TYR B 145     4926   5423   6149   -854    584    752       O  
ATOM   2193  CB  TYR B 145     -18.678  -5.677  27.510  1.00 40.16           C  
ANISOU 2193  CB  TYR B 145     4558   5246   5453   -634    477    514       C  
ATOM   2194  CG  TYR B 145     -19.159  -4.257  27.556  1.00 40.85           C  
ANISOU 2194  CG  TYR B 145     4596   5498   5428   -587    446    401       C  
ATOM   2195  CD1 TYR B 145     -20.468  -3.947  27.935  1.00 44.20           C  
ANISOU 2195  CD1 TYR B 145     4913   6044   5835   -633    471    389       C  
ATOM   2196  CD2 TYR B 145     -18.318  -3.219  27.223  1.00 41.48           C  
ANISOU 2196  CD2 TYR B 145     4726   5604   5430   -495    396    310       C  
ATOM   2197  CE1 TYR B 145     -20.905  -2.627  27.967  1.00 43.93           C  
ANISOU 2197  CE1 TYR B 145     4832   6146   5714   -574    445    281       C  
ATOM   2198  CE2 TYR B 145     -18.754  -1.898  27.245  1.00 42.30           C  
ANISOU 2198  CE2 TYR B 145     4789   5831   5453   -448    368    206       C  
ATOM   2199  CZ  TYR B 145     -20.037  -1.615  27.615  1.00 41.68           C  
ANISOU 2199  CZ  TYR B 145     4611   5862   5364   -481    392    190       C  
ATOM   2200  OH  TYR B 145     -20.442  -0.308  27.636  1.00 45.01           O  
ANISOU 2200  OH  TYR B 145     4992   6389   5722   -420    367     85       O  
ATOM   2201  N   HIS B 146     -17.798  -8.579  28.912  1.00 43.49           N  
ANISOU 2201  N   HIS B 146     5023   5439   6063   -702    605    919       N  
ATOM   2202  CA  HIS B 146     -17.458  -9.956  28.527  1.00 45.08           C  
ANISOU 2202  CA  HIS B 146     5281   5403   6443   -743    627    996       C  
ATOM   2203  C   HIS B 146     -17.357 -10.872  29.746  1.00 46.76           C  
ANISOU 2203  C   HIS B 146     5467   5616   6686   -762    698   1243       C  
ATOM   2204  O   HIS B 146     -16.933 -12.027  29.648  1.00 48.43           O  
ANISOU 2204  O   HIS B 146     5726   5627   7050   -777    725   1346       O  
ATOM   2205  CB  HIS B 146     -16.131  -9.949  27.757  1.00 43.85           C  
ANISOU 2205  CB  HIS B 146     5223   5126   6311   -646    587    922       C  
ATOM   2206  CG  HIS B 146     -16.146  -9.051  26.558  1.00 43.86           C  
ANISOU 2206  CG  HIS B 146     5256   5138   6272   -625    521    702       C  
ATOM   2207  ND1 HIS B 146     -16.767  -9.397  25.374  1.00 44.60           N  
ANISOU 2207  ND1 HIS B 146     5371   5104   6469   -699    495    564       N  
ATOM   2208  CD2 HIS B 146     -15.631  -7.809  26.363  1.00 43.22           C  
ANISOU 2208  CD2 HIS B 146     5184   5182   6056   -542    475    604       C  
ATOM   2209  CE1 HIS B 146     -16.616  -8.417  24.497  1.00 44.21           C  
ANISOU 2209  CE1 HIS B 146     5344   5112   6339   -656    436    404       C  
ATOM   2210  NE2 HIS B 146     -15.938  -7.439  25.075  1.00 43.49           N  
ANISOU 2210  NE2 HIS B 146     5247   5164   6113   -562    425    430       N  
ATOM   2211  OXT HIS B 146     -17.710 -10.492  30.862  1.00 47.48           O  
ANISOU 2211  OXT HIS B 146     5486   5907   6649   -761    734   1351       O  
TER    2212      HIS B 146                                                      
ATOM   2213  N   VAL C   1     -21.888   1.499  -3.765  1.00 45.04           N  
ANISOU 2213  N   VAL C   1     5789   5899   5425   -630    940     45       N  
ATOM   2214  CA  VAL C   1     -23.312   1.854  -4.058  1.00 44.15           C  
ANISOU 2214  CA  VAL C   1     5841   5684   5249   -598    816    163       C  
ATOM   2215  C   VAL C   1     -24.151   0.604  -4.211  1.00 41.90           C  
ANISOU 2215  C   VAL C   1     5578   5423   4919   -474    742    112       C  
ATOM   2216  O   VAL C   1     -23.615  -0.505  -4.336  1.00 42.61           O  
ANISOU 2216  O   VAL C   1     5587   5604   4998   -426    797     -3       O  
ATOM   2217  CB  VAL C   1     -23.457   2.712  -5.347  1.00 46.30           C  
ANISOU 2217  CB  VAL C   1     6278   5946   5368   -727    861    291       C  
ATOM   2218  CG1 VAL C   1     -22.620   4.011  -5.226  1.00 48.19           C  
ANISOU 2218  CG1 VAL C   1     6512   6145   5655   -874    936    355       C  
ATOM   2219  CG2 VAL C   1     -23.099   1.888  -6.633  1.00 47.40           C  
ANISOU 2219  CG2 VAL C   1     6456   6224   5330   -766    970    245       C  
ATOM   2220  N   LEU C   2     -25.467   0.800  -4.189  1.00 39.22           N  
ANISOU 2220  N   LEU C   2     5340   4996   4565   -422    611    191       N  
ATOM   2221  CA  LEU C   2     -26.416  -0.264  -4.435  1.00 36.77           C  
ANISOU 2221  CA  LEU C   2     5067   4698   4204   -327    530    160       C  
ATOM   2222  C   LEU C   2     -26.515  -0.523  -5.942  1.00 36.58           C  
ANISOU 2222  C   LEU C   2     5163   4743   3994   -381    574    186       C  
ATOM   2223  O   LEU C   2     -26.884   0.363  -6.717  1.00 37.77           O  
ANISOU 2223  O   LEU C   2     5443   4860   4048   -456    553    305       O  
ATOM   2224  CB  LEU C   2     -27.786   0.095  -3.880  1.00 35.66           C  
ANISOU 2224  CB  LEU C   2     4973   4452   4124   -262    380    225       C  
ATOM   2225  CG  LEU C   2     -27.858   0.407  -2.374  1.00 34.93           C  
ANISOU 2225  CG  LEU C   2     4780   4295   4195   -214    333    196       C  
ATOM   2226  CD1 LEU C   2     -29.296   0.863  -1.965  1.00 32.60           C  
ANISOU 2226  CD1 LEU C   2     4530   3905   3951   -155    199    251       C  
ATOM   2227  CD2 LEU C   2     -27.427  -0.771  -1.540  1.00 32.31           C  
ANISOU 2227  CD2 LEU C   2     4334   4015   3927   -147    346     82       C  
ATOM   2228  N   SER C   3     -26.187  -1.740  -6.350  1.00 34.56           N  
ANISOU 2228  N   SER C   3     4871   4578   3683   -343    626     74       N  
ATOM   2229  CA  SER C   3     -26.289  -2.152  -7.751  1.00 34.93           C  
ANISOU 2229  CA  SER C   3     5029   4704   3539   -389    671     69       C  
ATOM   2230  C   SER C   3     -27.742  -2.297  -8.169  1.00 33.74           C  
ANISOU 2230  C   SER C   3     5001   4500   3319   -345    518    139       C  
ATOM   2231  O   SER C   3     -28.643  -2.363  -7.312  1.00 33.08           O  
ANISOU 2231  O   SER C   3     4887   4332   3351   -263    392    156       O  
ATOM   2232  CB  SER C   3     -25.624  -3.519  -7.916  1.00 35.09           C  
ANISOU 2232  CB  SER C   3     4962   4818   3553   -333    752    -99       C  
ATOM   2233  OG  SER C   3     -26.404  -4.492  -7.202  1.00 34.21           O  
ANISOU 2233  OG  SER C   3     4816   4648   3535   -211    629   -152       O  
ATOM   2234  N   ALA C   4     -27.969  -2.400  -9.476  1.00 33.78           N  
ANISOU 2234  N   ALA C   4     5138   4566   3132   -404    531    166       N  
ATOM   2235  CA  ALA C   4     -29.303  -2.674 -10.013  1.00 32.93           C  
ANISOU 2235  CA  ALA C   4     5141   4426   2943   -364    380    214       C  
ATOM   2236  C   ALA C   4     -29.907  -3.920  -9.348  1.00 30.90           C  
ANISOU 2236  C   ALA C   4     4801   4151   2789   -246    302    104       C  
ATOM   2237  O   ALA C   4     -31.066  -3.878  -8.912  1.00 31.12           O  
ANISOU 2237  O   ALA C   4     4835   4103   2885   -188    156    150       O  
ATOM   2238  CB  ALA C   4     -29.268  -2.842 -11.546  1.00 34.66           C  
ANISOU 2238  CB  ALA C   4     5510   4741   2917   -449    421    226       C  
ATOM   2239  N   ALA C   5     -29.128  -5.002  -9.254  1.00 29.38           N  
ANISOU 2239  N   ALA C   5     4527   4020   2615   -213    396    -42       N  
ATOM   2240  CA  ALA C   5     -29.596  -6.247  -8.646  1.00 27.86           C  
ANISOU 2240  CA  ALA C   5     4271   3797   2518   -113    325   -144       C  
ATOM   2241  C   ALA C   5     -29.964  -6.030  -7.162  1.00 26.65           C  
ANISOU 2241  C   ALA C   5     4018   3551   2558    -53    248   -111       C  
ATOM   2242  O   ALA C   5     -30.932  -6.619  -6.671  1.00 25.94           O  
ANISOU 2242  O   ALA C   5     3918   3409   2529      3    137   -121       O  
ATOM   2243  CB  ALA C   5     -28.525  -7.361  -8.796  1.00 27.46           C  
ANISOU 2243  CB  ALA C   5     4149   3813   2471    -83    441   -308       C  
ATOM   2244  N   ASP C   6     -29.210  -5.163  -6.471  1.00 26.58           N  
ANISOU 2244  N   ASP C   6     3939   3526   2634    -77    311    -74       N  
ATOM   2245  CA  ASP C   6     -29.438  -4.893  -5.055  1.00 25.76           C  
ANISOU 2245  CA  ASP C   6     3746   3348   2695    -31    253    -54       C  
ATOM   2246  C   ASP C   6     -30.788  -4.202  -4.844  1.00 25.45           C  
ANISOU 2246  C   ASP C   6     3756   3236   2676    -21    127     45       C  
ATOM   2247  O   ASP C   6     -31.542  -4.549  -3.949  1.00 24.51           O  
ANISOU 2247  O   ASP C   6     3589   3072   2651     32     47     31       O  
ATOM   2248  CB  ASP C   6     -28.342  -3.976  -4.466  1.00 26.38           C  
ANISOU 2248  CB  ASP C   6     3750   3428   2847    -73    342    -37       C  
ATOM   2249  CG  ASP C   6     -27.043  -4.689  -4.159  1.00 26.87           C  
ANISOU 2249  CG  ASP C   6     3701   3546   2961    -53    440   -152       C  
ATOM   2250  OD1 ASP C   6     -27.056  -5.893  -3.873  1.00 27.59           O  
ANISOU 2250  OD1 ASP C   6     3753   3639   3091     21    411   -241       O  
ATOM   2251  OD2 ASP C   6     -26.002  -4.019  -4.180  1.00 28.10           O  
ANISOU 2251  OD2 ASP C   6     3806   3739   3131   -113    540   -154       O  
ATOM   2252  N   LYS C   7     -31.048  -3.194  -5.667  1.00 26.28           N  
ANISOU 2252  N   LYS C   7     3957   3331   2696    -76    112    144       N  
ATOM   2253  CA  LYS C   7     -32.277  -2.419  -5.624  1.00 25.67           C  
ANISOU 2253  CA  LYS C   7     3928   3181   2646    -59    -16    237       C  
ATOM   2254  C   LYS C   7     -33.449  -3.330  -5.967  1.00 25.42           C  
ANISOU 2254  C   LYS C   7     3921   3159   2578    -12   -126    208       C  
ATOM   2255  O   LYS C   7     -34.463  -3.286  -5.285  1.00 25.41           O  
ANISOU 2255  O   LYS C   7     3871   3109   2673     38   -223    214       O  
ATOM   2256  CB  LYS C   7     -32.217  -1.238  -6.613  1.00 26.96           C  
ANISOU 2256  CB  LYS C   7     4213   3325   2707   -131    -22    358       C  
ATOM   2257  CG  LYS C   7     -31.165  -0.153  -6.287  1.00 27.09           C  
ANISOU 2257  CG  LYS C   7     4213   3312   2768   -199     76    404       C  
ATOM   2258  CD  LYS C   7     -30.905   0.774  -7.499  1.00 29.29           C  
ANISOU 2258  CD  LYS C   7     4640   3587   2902   -302     96    524       C  
ATOM   2259  CE  LYS C   7     -29.888   1.893  -7.232  1.00 31.59           C  
ANISOU 2259  CE  LYS C   7     4924   3839   3239   -392    192    578       C  
ATOM   2260  NZ  LYS C   7     -29.993   3.045  -8.242  1.00 32.08           N  
ANISOU 2260  NZ  LYS C   7     5157   3845   3188   -491    160    737       N  
ATOM   2261  N   THR C   8     -33.322  -4.181  -6.990  1.00 25.40           N  
ANISOU 2261  N   THR C   8     3985   3225   2440    -31   -106    162       N  
ATOM   2262  CA  THR C   8     -34.386  -5.151  -7.278  1.00 24.74           C  
ANISOU 2262  CA  THR C   8     3919   3149   2330      5   -211    117       C  
ATOM   2263  C   THR C   8     -34.631  -6.108  -6.096  1.00 23.30           C  
ANISOU 2263  C   THR C   8     3627   2941   2286     60   -226     33       C  
ATOM   2264  O   THR C   8     -35.773  -6.374  -5.727  1.00 23.23           O  
ANISOU 2264  O   THR C   8     3589   2902   2336     87   -330     33       O  
ATOM   2265  CB  THR C   8     -34.057  -6.009  -8.502  1.00 26.30           C  
ANISOU 2265  CB  THR C   8     4205   3426   2363    -28   -173     53       C  
ATOM   2266  OG1 THR C   8     -33.880  -5.164  -9.643  1.00 28.24           O  
ANISOU 2266  OG1 THR C   8     4573   3707   2450    -96   -161    140       O  
ATOM   2267  CG2 THR C   8     -35.179  -7.032  -8.742  1.00 25.87           C  
ANISOU 2267  CG2 THR C   8     4165   3369   2294      3   -292     -2       C  
ATOM   2268  N   ASN C   9     -33.563  -6.648  -5.516  1.00 21.57           N  
ANISOU 2268  N   ASN C   9     3346   2734   2117     70   -125    -39       N  
ATOM   2269  CA  ASN C   9     -33.725  -7.555  -4.396  1.00 20.25           C  
ANISOU 2269  CA  ASN C   9     3097   2533   2066    113   -148   -102       C  
ATOM   2270  C   ASN C   9     -34.406  -6.887  -3.217  1.00 19.57           C  
ANISOU 2270  C   ASN C   9     2943   2397   2098    127   -199    -51       C  
ATOM   2271  O   ASN C   9     -35.317  -7.477  -2.606  1.00 16.88           O  
ANISOU 2271  O   ASN C   9     2567   2033   1814    141   -268    -70       O  
ATOM   2272  CB  ASN C   9     -32.379  -8.137  -3.940  1.00 19.98           C  
ANISOU 2272  CB  ASN C   9     3006   2511   2073    132    -49   -179       C  
ATOM   2273  CG  ASN C   9     -31.809  -9.126  -4.932  1.00 20.04           C  
ANISOU 2273  CG  ASN C   9     3058   2563   1993    137      0   -273       C  
ATOM   2274  OD1 ASN C   9     -32.529  -9.605  -5.802  1.00 17.21           O  
ANISOU 2274  OD1 ASN C   9     2776   2217   1544    127    -53   -291       O  
ATOM   2275  ND2 ASN C   9     -30.504  -9.405  -4.829  1.00 20.13           N  
ANISOU 2275  ND2 ASN C   9     3016   2602   2031    155    100   -344       N  
ATOM   2276  N   THR C  10     -33.972  -5.665  -2.886  1.00 19.56           N  
ANISOU 2276  N   THR C  10     2920   2380   2131    114   -160      7       N  
ATOM   2277  CA  THR C  10     -34.601  -4.988  -1.759  1.00 18.72           C  
ANISOU 2277  CA  THR C  10     2748   2228   2137    130   -202     36       C  
ATOM   2278  C   THR C  10     -36.035  -4.596  -2.071  1.00 20.43           C  
ANISOU 2278  C   THR C  10     2980   2423   2360    144   -310     77       C  
ATOM   2279  O   THR C  10     -36.902  -4.785  -1.248  1.00 18.93           O  
ANISOU 2279  O   THR C  10     2724   2220   2250    162   -357     54       O  
ATOM   2280  CB  THR C  10     -33.727  -3.909  -1.026  1.00 18.82           C  
ANISOU 2280  CB  THR C  10     2718   2217   2216    117   -135     60       C  
ATOM   2281  OG1 THR C  10     -34.485  -2.711  -0.730  1.00 21.98           O  
ANISOU 2281  OG1 THR C  10     3111   2565   2676    125   -188    115       O  
ATOM   2282  CG2 THR C  10     -32.424  -3.626  -1.664  1.00 13.05           C  
ANISOU 2282  CG2 THR C  10     2015   1516   1427     79    -41     66       C  
ATOM   2283  N   LYS C  11     -36.328  -4.140  -3.285  1.00 23.62           N  
ANISOU 2283  N   LYS C  11     3469   2831   2675    133   -356    132       N  
ATOM   2284  CA  LYS C  11     -37.717  -3.803  -3.618  1.00 24.90           C  
ANISOU 2284  CA  LYS C  11     3635   2972   2853    158   -484    167       C  
ATOM   2285  C   LYS C  11     -38.560  -5.083  -3.483  1.00 25.03           C  
ANISOU 2285  C   LYS C  11     3612   3020   2878    164   -537     97       C  
ATOM   2286  O   LYS C  11     -39.708  -5.047  -3.027  1.00 25.09           O  
ANISOU 2286  O   LYS C  11     3549   3018   2967    185   -614     84       O  
ATOM   2287  CB  LYS C  11     -37.829  -3.235  -5.022  1.00 26.81           C  
ANISOU 2287  CB  LYS C  11     3996   3216   2975    140   -542    246       C  
ATOM   2288  CG  LYS C  11     -37.525  -1.717  -5.068  1.00 30.06           C  
ANISOU 2288  CG  LYS C  11     4446   3561   3413    135   -542    342       C  
ATOM   2289  CD  LYS C  11     -37.839  -1.183  -6.459  1.00 33.76           C  
ANISOU 2289  CD  LYS C  11     5051   4023   3755    112   -631    439       C  
ATOM   2290  CE  LYS C  11     -37.393   0.263  -6.623  1.00 37.07           C  
ANISOU 2290  CE  LYS C  11     5538   4362   4184     88   -628    548       C  
ATOM   2291  NZ  LYS C  11     -38.050   1.223  -5.651  1.00 36.77           N  
ANISOU 2291  NZ  LYS C  11     5417   4224   4330    156   -695    560       N  
ATOM   2292  N   SER C  12     -37.969  -6.216  -3.849  1.00 24.48           N  
ANISOU 2292  N   SER C  12     3582   2986   2736    142   -490     41       N  
ATOM   2293  CA  SER C  12     -38.705  -7.459  -3.835  1.00 24.21           C  
ANISOU 2293  CA  SER C  12     3530   2964   2703    135   -544    -23       C  
ATOM   2294  C   SER C  12     -38.944  -7.969  -2.427  1.00 22.09           C  
ANISOU 2294  C   SER C  12     3166   2675   2550    134   -524    -63       C  
ATOM   2295  O   SER C  12     -40.025  -8.494  -2.161  1.00 22.60           O  
ANISOU 2295  O   SER C  12     3187   2744   2658    119   -590    -88       O  
ATOM   2296  CB  SER C  12     -38.086  -8.483  -4.769  1.00 25.16           C  
ANISOU 2296  CB  SER C  12     3735   3114   2711    117   -515    -79       C  
ATOM   2297  OG  SER C  12     -37.924  -9.718  -4.125  1.00 29.60           O  
ANISOU 2297  OG  SER C  12     4266   3658   3323    115   -493   -154       O  
ATOM   2298  N   VAL C  13     -38.023  -7.769  -1.489  1.00 20.48           N  
ANISOU 2298  N   VAL C  13     2928   2457   2397    140   -438    -65       N  
ATOM   2299  CA  VAL C  13     -38.383  -8.084  -0.113  1.00 19.16           C  
ANISOU 2299  CA  VAL C  13     2681   2276   2322    129   -430    -88       C  
ATOM   2300  C   VAL C  13     -39.467  -7.122   0.435  1.00 19.22           C  
ANISOU 2300  C   VAL C  13     2611   2286   2407    136   -470    -67       C  
ATOM   2301  O   VAL C  13     -40.438  -7.580   1.051  1.00 18.33           O  
ANISOU 2301  O   VAL C  13     2436   2186   2343    111   -500    -97       O  
ATOM   2302  CB  VAL C  13     -37.183  -8.397   0.853  1.00 19.82           C  
ANISOU 2302  CB  VAL C  13     2750   2346   2435    129   -352   -106       C  
ATOM   2303  CG1 VAL C  13     -35.892  -8.684   0.093  1.00 18.05           C  
ANISOU 2303  CG1 VAL C  13     2581   2126   2151    148   -299   -123       C  
ATOM   2304  CG2 VAL C  13     -37.025  -7.414   2.024  1.00 17.66           C  
ANISOU 2304  CG2 VAL C  13     2411   2068   2232    131   -314    -87       C  
ATOM   2305  N   PHE C  14     -39.359  -5.819   0.135  1.00 18.61           N  
ANISOU 2305  N   PHE C  14     2538   2193   2342    167   -473    -22       N  
ATOM   2306  CA  PHE C  14     -40.355  -4.874   0.626  1.00 18.61           C  
ANISOU 2306  CA  PHE C  14     2459   2181   2433    193   -516    -19       C  
ATOM   2307  C   PHE C  14     -41.723  -5.103   0.040  1.00 18.98           C  
ANISOU 2307  C   PHE C  14     2472   2246   2492    201   -621    -30       C  
ATOM   2308  O   PHE C  14     -42.674  -4.857   0.714  1.00 19.52           O  
ANISOU 2308  O   PHE C  14     2440   2327   2651    210   -644    -65       O  
ATOM   2309  CB  PHE C  14     -39.894  -3.414   0.540  1.00 18.89           C  
ANISOU 2309  CB  PHE C  14     2511   2169   2498    227   -504     31       C  
ATOM   2310  CG  PHE C  14     -38.989  -3.000   1.713  1.00 18.57           C  
ANISOU 2310  CG  PHE C  14     2436   2114   2505    215   -410     10       C  
ATOM   2311  CD1 PHE C  14     -39.526  -2.455   2.848  1.00 16.32           C  
ANISOU 2311  CD1 PHE C  14     2062   1822   2315    228   -398    -33       C  
ATOM   2312  CD2 PHE C  14     -37.610  -3.187   1.662  1.00 19.69           C  
ANISOU 2312  CD2 PHE C  14     2628   2258   2596    191   -335     23       C  
ATOM   2313  CE1 PHE C  14     -38.739  -2.101   3.922  1.00 16.80           C  
ANISOU 2313  CE1 PHE C  14     2098   1877   2406    211   -322    -58       C  
ATOM   2314  CE2 PHE C  14     -36.800  -2.837   2.728  1.00 19.79           C  
ANISOU 2314  CE2 PHE C  14     2604   2263   2652    179   -267      1       C  
ATOM   2315  CZ  PHE C  14     -37.375  -2.288   3.866  1.00 21.22           C  
ANISOU 2315  CZ  PHE C  14     2710   2435   2916    186   -265    -37       C  
ATOM   2316  N   ALA C  15     -41.831  -5.651  -1.168  1.00 19.82           N  
ANISOU 2316  N   ALA C  15     2656   2366   2508    193   -683    -13       N  
ATOM   2317  CA  ALA C  15     -43.117  -5.998  -1.727  1.00 20.39           C  
ANISOU 2317  CA  ALA C  15     2693   2464   2590    193   -796    -32       C  
ATOM   2318  C   ALA C  15     -43.775  -7.083  -0.881  1.00 20.99           C  
ANISOU 2318  C   ALA C  15     2685   2573   2719    140   -779   -103       C  
ATOM   2319  O   ALA C  15     -44.982  -7.068  -0.676  1.00 22.42           O  
ANISOU 2319  O   ALA C  15     2764   2781   2973    136   -840   -137       O  
ATOM   2320  CB  ALA C  15     -42.988  -6.484  -3.185  1.00 21.01           C  
ANISOU 2320  CB  ALA C  15     2888   2556   2537    180   -861    -10       C  
ATOM   2321  N   LYS C  16     -42.983  -8.022  -0.392  1.00 19.74           N  
ANISOU 2321  N   LYS C  16     2567   2409   2526     97   -699   -124       N  
ATOM   2322  CA  LYS C  16     -43.525  -9.130   0.323  1.00 20.18           C  
ANISOU 2322  CA  LYS C  16     2575   2480   2613     31   -689   -172       C  
ATOM   2323  C   LYS C  16     -43.814  -8.797   1.758  1.00 19.85           C  
ANISOU 2323  C   LYS C  16     2433   2454   2654      9   -625   -190       C  
ATOM   2324  O   LYS C  16     -44.783  -9.309   2.296  1.00 20.38           O  
ANISOU 2324  O   LYS C  16     2422   2555   2766    -51   -633   -229       O  
ATOM   2325  CB  LYS C  16     -42.605 -10.369   0.200  1.00 20.44           C  
ANISOU 2325  CB  LYS C  16     2706   2482   2578     -2   -654   -186       C  
ATOM   2326  CG  LYS C  16     -42.759 -11.061  -1.199  1.00 22.87           C  
ANISOU 2326  CG  LYS C  16     3097   2789   2805     -7   -729   -206       C  
ATOM   2327  CD  LYS C  16     -41.897 -12.267  -1.358  1.00 23.75           C  
ANISOU 2327  CD  LYS C  16     3298   2860   2868    -25   -698   -241       C  
ATOM   2328  CE  LYS C  16     -42.258 -13.055  -2.599  1.00 27.41           C  
ANISOU 2328  CE  LYS C  16     3833   3324   3258    -44   -774   -287       C  
ATOM   2329  NZ  LYS C  16     -41.165 -14.134  -2.901  1.00 31.61           N  
ANISOU 2329  NZ  LYS C  16     4462   3806   3742    -36   -732   -339       N  
ATOM   2330  N   ILE C  17     -43.002  -7.942   2.388  1.00 18.39           N  
ANISOU 2330  N   ILE C  17     2249   2253   2485     45   -556   -169       N  
ATOM   2331  CA  ILE C  17     -43.256  -7.603   3.810  1.00 17.51           C  
ANISOU 2331  CA  ILE C  17     2049   2167   2437     18   -489   -199       C  
ATOM   2332  C   ILE C  17     -44.080  -6.375   4.009  1.00 18.20           C  
ANISOU 2332  C   ILE C  17     2032   2272   2612     66   -504   -225       C  
ATOM   2333  O   ILE C  17     -44.473  -6.081   5.124  1.00 18.51           O  
ANISOU 2333  O   ILE C  17     1985   2345   2704     43   -447   -272       O  
ATOM   2334  CB  ILE C  17     -41.959  -7.439   4.643  1.00 15.77           C  
ANISOU 2334  CB  ILE C  17     1876   1924   2193     18   -407   -180       C  
ATOM   2335  CG1 ILE C  17     -41.235  -6.148   4.293  1.00 15.55           C  
ANISOU 2335  CG1 ILE C  17     1867   1864   2179     89   -396   -152       C  
ATOM   2336  CG2 ILE C  17     -41.021  -8.613   4.397  1.00 14.15           C  
ANISOU 2336  CG2 ILE C  17     1770   1688   1920     -5   -403   -160       C  
ATOM   2337  CD1 ILE C  17     -39.802  -6.174   4.694  1.00 13.72           C  
ANISOU 2337  CD1 ILE C  17     1692   1609   1912     88   -335   -132       C  
ATOM   2338  N   GLY C  18     -44.361  -5.657   2.935  1.00 19.59           N  
ANISOU 2338  N   GLY C  18     2218   2423   2802    134   -586   -199       N  
ATOM   2339  CA  GLY C  18     -44.999  -4.351   3.030  1.00 19.88           C  
ANISOU 2339  CA  GLY C  18     2170   2447   2938    205   -620   -218       C  
ATOM   2340  C   GLY C  18     -46.320  -4.349   3.748  1.00 20.36           C  
ANISOU 2340  C   GLY C  18     2071   2566   3097    192   -621   -303       C  
ATOM   2341  O   GLY C  18     -46.561  -3.488   4.572  1.00 21.10           O  
ANISOU 2341  O   GLY C  18     2079   2663   3275    224   -577   -355       O  
ATOM   2342  N   PRO C  19     -47.180  -5.344   3.472  1.00 20.87           N  
ANISOU 2342  N   PRO C  19     2090   2684   3155    135   -663   -331       N  
ATOM   2343  CA  PRO C  19     -48.431  -5.379   4.195  1.00 21.56           C  
ANISOU 2343  CA  PRO C  19     2008   2845   3339    104   -646   -423       C  
ATOM   2344  C   PRO C  19     -48.286  -5.600   5.739  1.00 22.06           C  
ANISOU 2344  C   PRO C  19     2023   2959   3399     23   -501   -475       C  
ATOM   2345  O   PRO C  19     -49.215  -5.289   6.488  1.00 23.14           O  
ANISOU 2345  O   PRO C  19     2010   3164   3620      8   -457   -566       O  
ATOM   2346  CB  PRO C  19     -49.207  -6.506   3.483  1.00 23.03           C  
ANISOU 2346  CB  PRO C  19     2178   3070   3502     39   -723   -430       C  
ATOM   2347  CG  PRO C  19     -48.531  -6.634   2.105  1.00 21.90           C  
ANISOU 2347  CG  PRO C  19     2189   2864   3268     83   -819   -347       C  
ATOM   2348  CD  PRO C  19     -47.101  -6.374   2.415  1.00 20.64           C  
ANISOU 2348  CD  PRO C  19     2153   2649   3038     98   -733   -292       C  
ATOM   2349  N   HIS C  20     -47.120  -6.060   6.212  1.00 20.98           N  
ANISOU 2349  N   HIS C  20     2010   2795   3167    -24   -431   -425       N  
ATOM   2350  CA  HIS C  20     -46.875  -6.306   7.631  1.00 20.67           C  
ANISOU 2350  CA  HIS C  20     1956   2799   3097   -106   -313   -456       C  
ATOM   2351  C   HIS C  20     -45.841  -5.337   8.235  1.00 20.93           C  
ANISOU 2351  C   HIS C  20     2036   2795   3123    -52   -258   -448       C  
ATOM   2352  O   HIS C  20     -45.324  -5.585   9.337  1.00 19.68           O  
ANISOU 2352  O   HIS C  20     1907   2662   2909   -119   -175   -455       O  
ATOM   2353  CB  HIS C  20     -46.334  -7.732   7.800  1.00 20.71           C  
ANISOU 2353  CB  HIS C  20     2073   2795   3000   -210   -297   -401       C  
ATOM   2354  CG  HIS C  20     -47.096  -8.752   7.027  1.00 18.56           C  
ANISOU 2354  CG  HIS C  20     1795   2532   2726   -264   -365   -397       C  
ATOM   2355  ND1 HIS C  20     -48.407  -9.047   7.306  1.00 18.22           N  
ANISOU 2355  ND1 HIS C  20     1621   2566   2737   -338   -356   -462       N  
ATOM   2356  CD2 HIS C  20     -46.753  -9.504   5.955  1.00 17.66           C  
ANISOU 2356  CD2 HIS C  20     1781   2362   2566   -256   -444   -350       C  
ATOM   2357  CE1 HIS C  20     -48.845  -9.942   6.439  1.00 20.94           C  
ANISOU 2357  CE1 HIS C  20     1987   2897   3071   -378   -436   -450       C  
ATOM   2358  NE2 HIS C  20     -47.856 -10.242   5.612  1.00 20.84           N  
ANISOU 2358  NE2 HIS C  20     2121   2802   2995   -327   -491   -384       N  
ATOM   2359  N   ALA C  21     -45.540  -4.260   7.516  1.00 20.78           N  
ANISOU 2359  N   ALA C  21     2030   2711   3154     57   -311   -429       N  
ATOM   2360  CA  ALA C  21     -44.453  -3.360   7.901  1.00 21.74           C  
ANISOU 2360  CA  ALA C  21     2210   2779   3270    100   -271   -412       C  
ATOM   2361  C   ALA C  21     -44.610  -2.914   9.342  1.00 22.16           C  
ANISOU 2361  C   ALA C  21     2189   2884   3347     65   -174   -498       C  
ATOM   2362  O   ALA C  21     -43.680  -2.868  10.132  1.00 21.19           O  
ANISOU 2362  O   ALA C  21     2125   2759   3168     32   -115   -491       O  
ATOM   2363  CB  ALA C  21     -44.466  -2.109   6.996  1.00 22.83           C  
ANISOU 2363  CB  ALA C  21     2351   2839   3486    211   -347   -391       C  
ATOM   2364  N   GLU C  22     -45.826  -2.584   9.650  1.00 23.57           N  
ANISOU 2364  N   GLU C  22     2231   3117   3609     75   -162   -590       N  
ATOM   2365  CA  GLU C  22     -46.151  -2.021  10.899  1.00 26.22           C  
ANISOU 2365  CA  GLU C  22     2478   3510   3975     54    -67   -697       C  
ATOM   2366  C   GLU C  22     -45.916  -3.031  11.990  1.00 25.59           C  
ANISOU 2366  C   GLU C  22     2435   3513   3775    -84     25   -697       C  
ATOM   2367  O   GLU C  22     -45.265  -2.739  12.963  1.00 26.54           O  
ANISOU 2367  O   GLU C  22     2593   3647   3843   -117     93   -720       O  
ATOM   2368  CB  GLU C  22     -47.612  -1.547  10.855  1.00 28.06           C  
ANISOU 2368  CB  GLU C  22     2533   3791   4336    100    -77   -809       C  
ATOM   2369  CG  GLU C  22     -48.154  -0.999  12.125  1.00 32.46           C  
ANISOU 2369  CG  GLU C  22     2969   4429   4934     77     37   -954       C  
ATOM   2370  CD  GLU C  22     -49.607  -0.623  11.963  1.00 37.83           C  
ANISOU 2370  CD  GLU C  22     3453   5163   5759    131     21  -1074       C  
ATOM   2371  OE1 GLU C  22     -49.906   0.239  11.082  1.00 39.15           O  
ANISOU 2371  OE1 GLU C  22     3579   5240   6056    272    -92  -1077       O  
ATOM   2372  OE2 GLU C  22     -50.429  -1.249  12.677  1.00 42.11           O  
ANISOU 2372  OE2 GLU C  22     3884   5835   6279     27    113  -1157       O  
ATOM   2373  N   GLU C  23     -46.423  -4.229  11.844  1.00 25.59           N  
ANISOU 2373  N   GLU C  23     2436   3562   3726   -174     20   -666       N  
ATOM   2374  CA  GLU C  23     -46.101  -5.242  12.854  1.00 26.05           C  
ANISOU 2374  CA  GLU C  23     2563   3676   3660   -313     91   -639       C  
ATOM   2375  C   GLU C  23     -44.599  -5.651  12.872  1.00 22.41           C  
ANISOU 2375  C   GLU C  23     2268   3141   3106   -314     60   -534       C  
ATOM   2376  O   GLU C  23     -44.067  -5.967  13.918  1.00 22.61           O  
ANISOU 2376  O   GLU C  23     2354   3197   3040   -392    112   -522       O  
ATOM   2377  CB  GLU C  23     -47.013  -6.479  12.782  1.00 27.00           C  
ANISOU 2377  CB  GLU C  23     2652   3855   3751   -430     94   -627       C  
ATOM   2378  CG  GLU C  23     -47.898  -6.649  11.497  1.00 32.50           C  
ANISOU 2378  CG  GLU C  23     3274   4535   4541   -379      3   -631       C  
ATOM   2379  CD  GLU C  23     -48.989  -5.574  11.259  1.00 36.90           C  
ANISOU 2379  CD  GLU C  23     3648   5132   5239   -289     -5   -744       C  
ATOM   2380  OE1 GLU C  23     -49.760  -5.210  12.208  1.00 39.28           O  
ANISOU 2380  OE1 GLU C  23     3816   5533   5576   -334     94   -858       O  
ATOM   2381  OE2 GLU C  23     -49.060  -5.102  10.084  1.00 39.33           O  
ANISOU 2381  OE2 GLU C  23     3951   5372   5622   -172   -117   -719       O  
ATOM   2382  N   TYR C  24     -43.915  -5.643  11.752  1.00 20.05           N  
ANISOU 2382  N   TYR C  24     2039   2753   2825   -232    -22   -463       N  
ATOM   2383  CA  TYR C  24     -42.475  -5.961  11.812  1.00 19.03           C  
ANISOU 2383  CA  TYR C  24     2038   2565   2626   -226    -41   -387       C  
ATOM   2384  C   TYR C  24     -41.656  -4.804  12.409  1.00 19.18           C  
ANISOU 2384  C   TYR C  24     2059   2569   2658   -179     -6   -418       C  
ATOM   2385  O   TYR C  24     -40.648  -5.050  13.020  1.00 19.12           O  
ANISOU 2385  O   TYR C  24     2125   2554   2587   -208      1   -386       O  
ATOM   2386  CB  TYR C  24     -41.916  -6.343  10.450  1.00 17.70           C  
ANISOU 2386  CB  TYR C  24     1940   2320   2463   -163   -120   -317       C  
ATOM   2387  CG  TYR C  24     -42.574  -7.523   9.791  1.00 14.76           C  
ANISOU 2387  CG  TYR C  24     1585   1949   2075   -208   -166   -292       C  
ATOM   2388  CD1 TYR C  24     -43.471  -8.323  10.459  1.00 16.28           C  
ANISOU 2388  CD1 TYR C  24     1744   2198   2245   -316   -138   -312       C  
ATOM   2389  CD2 TYR C  24     -42.259  -7.865   8.500  1.00 13.92           C  
ANISOU 2389  CD2 TYR C  24     1536   1787   1968   -156   -234   -250       C  
ATOM   2390  CE1 TYR C  24     -44.045  -9.421   9.866  1.00 15.32           C  
ANISOU 2390  CE1 TYR C  24     1642   2066   2114   -369   -184   -292       C  
ATOM   2391  CE2 TYR C  24     -42.834  -8.974   7.912  1.00 14.37           C  
ANISOU 2391  CE2 TYR C  24     1615   1838   2007   -202   -281   -239       C  
ATOM   2392  CZ  TYR C  24     -43.729  -9.741   8.583  1.00 12.96           C  
ANISOU 2392  CZ  TYR C  24     1399   1704   1820   -307   -261   -259       C  
ATOM   2393  OH  TYR C  24     -44.295 -10.882   7.981  1.00 13.46           O  
ANISOU 2393  OH  TYR C  24     1489   1750   1874   -366   -314   -250       O  
ATOM   2394  N   GLY C  25     -42.108  -3.554  12.252  1.00 19.93           N  
ANISOU 2394  N   GLY C  25     2073   2655   2845   -107      4   -484       N  
ATOM   2395  CA  GLY C  25     -41.426  -2.418  12.857  1.00 19.96           C  
ANISOU 2395  CA  GLY C  25     2078   2636   2872    -72     36   -527       C  
ATOM   2396  C   GLY C  25     -41.392  -2.552  14.356  1.00 20.52           C  
ANISOU 2396  C   GLY C  25     2142   2787   2868   -161    113   -586       C  
ATOM   2397  O   GLY C  25     -40.345  -2.445  14.961  1.00 21.74           O  
ANISOU 2397  O   GLY C  25     2362   2932   2967   -182    119   -570       O  
ATOM   2398  N   ALA C  26     -42.545  -2.829  14.941  1.00 21.08           N  
ANISOU 2398  N   ALA C  26     2134   2947   2929   -223    171   -655       N  
ATOM   2399  CA  ALA C  26     -42.687  -3.080  16.343  1.00 21.77           C  
ANISOU 2399  CA  ALA C  26     2221   3132   2919   -332    255   -709       C  
ATOM   2400  C   ALA C  26     -41.767  -4.189  16.846  1.00 21.40           C  
ANISOU 2400  C   ALA C  26     2307   3088   2737   -422    231   -607       C  
ATOM   2401  O   ALA C  26     -41.047  -3.996  17.820  1.00 22.11           O  
ANISOU 2401  O   ALA C  26     2451   3203   2748   -463    251   -618       O  
ATOM   2402  CB  ALA C  26     -44.130  -3.462  16.641  1.00 23.49           C  
ANISOU 2402  CB  ALA C  26     2331   3451   3144   -403    322   -782       C  
ATOM   2403  N   GLU C  27     -41.820  -5.349  16.187  1.00 20.58           N  
ANISOU 2403  N   GLU C  27     2254   2953   2611   -448    176   -513       N  
ATOM   2404  CA  GLU C  27     -41.053  -6.498  16.622  1.00 20.51           C  
ANISOU 2404  CA  GLU C  27     2371   2929   2493   -524    137   -415       C  
ATOM   2405  C   GLU C  27     -39.572  -6.222  16.589  1.00 19.38           C  
ANISOU 2405  C   GLU C  27     2302   2719   2342   -458     79   -371       C  
ATOM   2406  O   GLU C  27     -38.889  -6.654  17.502  1.00 18.93           O  
ANISOU 2406  O   GLU C  27     2324   2677   2190   -518     62   -334       O  
ATOM   2407  CB  GLU C  27     -41.325  -7.765  15.759  1.00 21.04           C  
ANISOU 2407  CB  GLU C  27     2484   2947   2563   -545     76   -333       C  
ATOM   2408  CG  GLU C  27     -40.896  -9.075  16.504  1.00 21.90           C  
ANISOU 2408  CG  GLU C  27     2720   3046   2556   -655     44   -243       C  
ATOM   2409  CD  GLU C  27     -41.188 -10.328  15.711  1.00 24.41           C  
ANISOU 2409  CD  GLU C  27     3089   3299   2887   -682    -18   -174       C  
ATOM   2410  OE1 GLU C  27     -42.188 -10.332  14.935  1.00 24.23           O  
ANISOU 2410  OE1 GLU C  27     2986   3292   2931   -677     -5   -211       O  
ATOM   2411  OE2 GLU C  27     -40.414 -11.309  15.863  1.00 23.78           O  
ANISOU 2411  OE2 GLU C  27     3129   3149   2758   -704    -89    -89       O  
ATOM   2412  N   THR C  28     -39.109  -5.570  15.503  1.00 17.91           N  
ANISOU 2412  N   THR C  28     2091   2461   2252   -343     42   -368       N  
ATOM   2413  CA  THR C  28     -37.748  -5.087  15.350  1.00 17.79           C  
ANISOU 2413  CA  THR C  28     2115   2391   2254   -280      4   -345       C  
ATOM   2414  C   THR C  28     -37.253  -4.268  16.583  1.00 19.19           C  
ANISOU 2414  C   THR C  28     2289   2611   2393   -311     39   -405       C  
ATOM   2415  O   THR C  28     -36.195  -4.571  17.116  1.00 19.38           O  
ANISOU 2415  O   THR C  28     2373   2628   2361   -329     -3   -369       O  
ATOM   2416  CB  THR C  28     -37.612  -4.224  14.086  1.00 16.88           C  
ANISOU 2416  CB  THR C  28     1960   2211   2243   -177    -11   -350       C  
ATOM   2417  OG1 THR C  28     -37.937  -5.008  12.931  1.00 15.66           O  
ANISOU 2417  OG1 THR C  28     1823   2023   2104   -152    -52   -297       O  
ATOM   2418  CG2 THR C  28     -36.224  -3.674  13.951  1.00 13.92           C  
ANISOU 2418  CG2 THR C  28     1613   1789   1887   -134    -33   -333       C  
ATOM   2419  N   LEU C  29     -38.034  -3.291  17.057  1.00 20.69           N  
ANISOU 2419  N   LEU C  29     2405   2846   2611   -317    108   -506       N  
ATOM   2420  CA  LEU C  29     -37.665  -2.531  18.261  1.00 22.34           C  
ANISOU 2420  CA  LEU C  29     2615   3102   2773   -355    146   -584       C  
ATOM   2421  C   LEU C  29     -37.726  -3.404  19.515  1.00 23.97           C  
ANISOU 2421  C   LEU C  29     2885   3397   2826   -478    162   -568       C  
ATOM   2422  O   LEU C  29     -36.863  -3.317  20.382  1.00 25.30           O  
ANISOU 2422  O   LEU C  29     3111   3587   2916   -516    137   -568       O  
ATOM   2423  CB  LEU C  29     -38.557  -1.306  18.465  1.00 23.32           C  
ANISOU 2423  CB  LEU C  29     2641   3247   2973   -325    220   -715       C  
ATOM   2424  CG  LEU C  29     -38.445  -0.211  17.436  1.00 22.96           C  
ANISOU 2424  CG  LEU C  29     2550   3100   3074   -211    195   -734       C  
ATOM   2425  CD1 LEU C  29     -39.598   0.721  17.624  1.00 24.10           C  
ANISOU 2425  CD1 LEU C  29     2593   3262   3303   -176    254   -862       C  
ATOM   2426  CD2 LEU C  29     -37.121   0.499  17.597  1.00 24.88           C  
ANISOU 2426  CD2 LEU C  29     2836   3286   3330   -192    163   -731       C  
ATOM   2427  N   GLU C  30     -38.743  -4.236  19.618  1.00 24.99           N  
ANISOU 2427  N   GLU C  30     3009   3579   2907   -550    198   -551       N  
ATOM   2428  CA  GLU C  30     -38.843  -5.114  20.761  1.00 27.10           C  
ANISOU 2428  CA  GLU C  30     3357   3924   3015   -686    212   -516       C  
ATOM   2429  C   GLU C  30     -37.546  -5.912  20.818  1.00 25.83           C  
ANISOU 2429  C   GLU C  30     3314   3699   2801   -681     96   -397       C  
ATOM   2430  O   GLU C  30     -36.910  -6.019  21.870  1.00 25.45           O  
ANISOU 2430  O   GLU C  30     3342   3689   2640   -745     67   -382       O  
ATOM   2431  CB  GLU C  30     -40.099  -6.027  20.649  1.00 29.00           C  
ANISOU 2431  CB  GLU C  30     3578   4212   3228   -774    260   -495       C  
ATOM   2432  CG  GLU C  30     -41.410  -5.381  21.271  1.00 34.18           C  
ANISOU 2432  CG  GLU C  30     4119   4992   3877   -837    399   -636       C  
ATOM   2433  CD  GLU C  30     -42.772  -5.687  20.561  1.00 39.33           C  
ANISOU 2433  CD  GLU C  30     4661   5671   4614   -846    446   -667       C  
ATOM   2434  OE1 GLU C  30     -42.920  -6.727  19.844  1.00 42.24           O  
ANISOU 2434  OE1 GLU C  30     5068   5987   4994   -865    387   -566       O  
ATOM   2435  OE2 GLU C  30     -43.725  -4.877  20.787  1.00 40.31           O  
ANISOU 2435  OE2 GLU C  30     4650   5873   4794   -839    544   -807       O  
ATOM   2436  N   ARG C  31     -37.139  -6.467  19.672  1.00 24.41           N  
ANISOU 2436  N   ARG C  31     3147   3423   2706   -601     23   -319       N  
ATOM   2437  CA  ARG C  31     -35.907  -7.282  19.626  1.00 23.45           C  
ANISOU 2437  CA  ARG C  31     3117   3231   2560   -576    -91   -221       C  
ATOM   2438  C   ARG C  31     -34.654  -6.451  19.883  1.00 22.52           C  
ANISOU 2438  C   ARG C  31     2989   3100   2466   -516   -131   -251       C  
ATOM   2439  O   ARG C  31     -33.786  -6.905  20.583  1.00 21.86           O  
ANISOU 2439  O   ARG C  31     2977   3015   2315   -541   -210   -203       O  
ATOM   2440  CB  ARG C  31     -35.800  -8.077  18.343  1.00 22.87           C  
ANISOU 2440  CB  ARG C  31     3053   3067   2570   -506   -145   -156       C  
ATOM   2441  CG  ARG C  31     -36.741  -9.294  18.344  1.00 22.67           C  
ANISOU 2441  CG  ARG C  31     3081   3038   2494   -593   -147    -99       C  
ATOM   2442  CD  ARG C  31     -36.810  -9.936  16.970  1.00 22.12           C  
ANISOU 2442  CD  ARG C  31     3008   2884   2514   -522   -189    -65       C  
ATOM   2443  NE  ARG C  31     -37.810 -10.993  16.976  1.00 22.26           N  
ANISOU 2443  NE  ARG C  31     3065   2897   2493   -618   -186    -24       N  
ATOM   2444  CZ  ARG C  31     -37.627 -12.192  17.502  1.00 19.74           C  
ANISOU 2444  CZ  ARG C  31     2862   2533   2105   -694   -251     62       C  
ATOM   2445  NH1 ARG C  31     -36.456 -12.517  18.040  1.00 19.54           N  
ANISOU 2445  NH1 ARG C  31     2920   2460   2045   -668   -339    117       N  
ATOM   2446  NH2 ARG C  31     -38.625 -13.072  17.479  1.00 21.35           N  
ANISOU 2446  NH2 ARG C  31     3098   2732   2280   -799   -238     94       N  
ATOM   2447  N   LEU C  32     -34.604  -5.232  19.353  1.00 21.70           N  
ANISOU 2447  N   LEU C  32     2799   2986   2461   -445    -83   -329       N  
ATOM   2448  CA  LEU C  32     -33.515  -4.328  19.634  1.00 21.87           C  
ANISOU 2448  CA  LEU C  32     2801   2997   2512   -409   -108   -371       C  
ATOM   2449  C   LEU C  32     -33.318  -4.092  21.120  1.00 23.29           C  
ANISOU 2449  C   LEU C  32     3023   3256   2572   -497   -109   -413       C  
ATOM   2450  O   LEU C  32     -32.192  -4.220  21.639  1.00 23.63           O  
ANISOU 2450  O   LEU C  32     3104   3295   2577   -500   -194   -388       O  
ATOM   2451  CB  LEU C  32     -33.761  -2.964  18.969  1.00 22.15           C  
ANISOU 2451  CB  LEU C  32     2750   3004   2664   -345    -44   -452       C  
ATOM   2452  CG  LEU C  32     -32.651  -1.931  19.142  1.00 20.17           C  
ANISOU 2452  CG  LEU C  32     2475   2727   2462   -318    -64   -499       C  
ATOM   2453  CD1 LEU C  32     -31.430  -2.426  18.379  1.00 19.90           C  
ANISOU 2453  CD1 LEU C  32     2448   2637   2475   -265   -137   -424       C  
ATOM   2454  CD2 LEU C  32     -33.094  -0.558  18.672  1.00 19.76           C  
ANISOU 2454  CD2 LEU C  32     2358   2635   2516   -274     -1   -581       C  
ATOM   2455  N   PHE C  33     -34.401  -3.753  21.802  1.00 24.05           N  
ANISOU 2455  N   PHE C  33     3105   3430   2603   -568    -19   -486       N  
ATOM   2456  CA  PHE C  33     -34.312  -3.394  23.222  1.00 26.01           C  
ANISOU 2456  CA  PHE C  33     3394   3770   2721   -661      0   -551       C  
ATOM   2457  C   PHE C  33     -34.031  -4.577  24.132  1.00 27.11           C  
ANISOU 2457  C   PHE C  33     3655   3952   2694   -760    -73   -452       C  
ATOM   2458  O   PHE C  33     -33.449  -4.393  25.201  1.00 28.61           O  
ANISOU 2458  O   PHE C  33     3903   4197   2771   -821   -113   -472       O  
ATOM   2459  CB  PHE C  33     -35.628  -2.765  23.671  1.00 27.07           C  
ANISOU 2459  CB  PHE C  33     3469   3986   2829   -712    135   -671       C  
ATOM   2460  CG  PHE C  33     -35.935  -1.474  22.998  1.00 26.38           C  
ANISOU 2460  CG  PHE C  33     3272   3850   2900   -616    193   -780       C  
ATOM   2461  CD1 PHE C  33     -34.931  -0.535  22.774  1.00 25.85           C  
ANISOU 2461  CD1 PHE C  33     3187   3714   2920   -548    148   -814       C  
ATOM   2462  CD2 PHE C  33     -37.246  -1.186  22.584  1.00 25.59           C  
ANISOU 2462  CD2 PHE C  33     3083   3768   2871   -595    285   -849       C  
ATOM   2463  CE1 PHE C  33     -35.223   0.683  22.173  1.00 24.30           C  
ANISOU 2463  CE1 PHE C  33     2908   3453   2870   -467    192   -904       C  
ATOM   2464  CE2 PHE C  33     -37.553   0.011  21.988  1.00 22.88           C  
ANISOU 2464  CE2 PHE C  33     2649   3365   2681   -499    318   -944       C  
ATOM   2465  CZ  PHE C  33     -36.560   0.947  21.771  1.00 25.52           C  
ANISOU 2465  CZ  PHE C  33     2987   3615   3095   -436    271   -965       C  
ATOM   2466  N   THR C  34     -34.505  -5.765  23.720  1.00 27.08           N  
ANISOU 2466  N   THR C  34     3698   3919   2674   -784    -93   -349       N  
ATOM   2467  CA  THR C  34     -34.315  -7.033  24.426  1.00 27.07           C  
ANISOU 2467  CA  THR C  34     3830   3925   2531   -877   -178   -229       C  
ATOM   2468  C   THR C  34     -32.908  -7.614  24.187  1.00 26.87           C  
ANISOU 2468  C   THR C  34     3857   3805   2547   -797   -341   -135       C  
ATOM   2469  O   THR C  34     -32.223  -8.001  25.127  1.00 28.09           O  
ANISOU 2469  O   THR C  34     4106   3978   2590   -848   -443    -81       O  
ATOM   2470  CB  THR C  34     -35.391  -8.085  23.987  1.00 27.43           C  
ANISOU 2470  CB  THR C  34     3902   3953   2566   -935   -140   -159       C  
ATOM   2471  OG1 THR C  34     -36.709  -7.588  24.229  1.00 26.75           O  
ANISOU 2471  OG1 THR C  34     3746   3967   2451  -1010     12   -256       O  
ATOM   2472  CG2 THR C  34     -35.242  -9.427  24.767  1.00 27.56           C  
ANISOU 2472  CG2 THR C  34     4082   3959   2432  -1049   -232    -21       C  
ATOM   2473  N   THR C  35     -32.494  -7.716  22.931  1.00 25.66           N  
ANISOU 2473  N   THR C  35     3641   3558   2552   -674   -371   -118       N  
ATOM   2474  CA  THR C  35     -31.180  -8.298  22.584  1.00 25.22           C  
ANISOU 2474  CA  THR C  35     3606   3416   2561   -585   -513    -50       C  
ATOM   2475  C   THR C  35     -29.986  -7.379  22.926  1.00 25.97           C  
ANISOU 2475  C   THR C  35     3648   3531   2690   -537   -562   -111       C  
ATOM   2476  O   THR C  35     -28.900  -7.867  23.192  1.00 25.88           O  
ANISOU 2476  O   THR C  35     3665   3486   2682   -501   -696    -62       O  
ATOM   2477  CB  THR C  35     -31.091  -8.648  21.055  1.00 23.75           C  
ANISOU 2477  CB  THR C  35     3359   3136   2528   -471   -509    -34       C  
ATOM   2478  OG1 THR C  35     -32.026  -9.673  20.759  1.00 23.19           O  
ANISOU 2478  OG1 THR C  35     3350   3033   2430   -516   -497     29       O  
ATOM   2479  CG2 THR C  35     -29.640  -9.149  20.621  1.00 21.28           C  
ANISOU 2479  CG2 THR C  35     3036   2744   2304   -363   -638      3       C  
ATOM   2480  N   TYR C  36     -30.208  -6.065  22.862  1.00 26.01           N  
ANISOU 2480  N   TYR C  36     3567   3579   2735   -533   -461   -221       N  
ATOM   2481  CA  TYR C  36     -29.195  -5.062  23.082  1.00 25.99           C  
ANISOU 2481  CA  TYR C  36     3504   3589   2782   -501   -489   -292       C  
ATOM   2482  C   TYR C  36     -29.774  -3.999  24.014  1.00 26.85           C  
ANISOU 2482  C   TYR C  36     3610   3784   2809   -583   -403   -400       C  
ATOM   2483  O   TYR C  36     -30.097  -2.871  23.584  1.00 26.50           O  
ANISOU 2483  O   TYR C  36     3485   3731   2854   -554   -308   -495       O  
ATOM   2484  CB  TYR C  36     -28.828  -4.420  21.745  1.00 25.37           C  
ANISOU 2484  CB  TYR C  36     3318   3445   2877   -400   -443   -327       C  
ATOM   2485  CG  TYR C  36     -28.348  -5.392  20.679  1.00 24.39           C  
ANISOU 2485  CG  TYR C  36     3184   3245   2838   -316   -498   -249       C  
ATOM   2486  CD1 TYR C  36     -27.032  -5.869  20.655  1.00 24.63           C  
ANISOU 2486  CD1 TYR C  36     3196   3247   2914   -261   -614   -219       C  
ATOM   2487  CD2 TYR C  36     -29.211  -5.856  19.728  1.00 21.54           C  
ANISOU 2487  CD2 TYR C  36     2826   2846   2511   -290   -440   -217       C  
ATOM   2488  CE1 TYR C  36     -26.620  -6.752  19.654  1.00 22.06           C  
ANISOU 2488  CE1 TYR C  36     2854   2854   2674   -176   -652   -172       C  
ATOM   2489  CE2 TYR C  36     -28.826  -6.712  18.771  1.00 21.57           C  
ANISOU 2489  CE2 TYR C  36     2827   2784   2583   -217   -482   -165       C  
ATOM   2490  CZ  TYR C  36     -27.526  -7.168  18.717  1.00 23.90           C  
ANISOU 2490  CZ  TYR C  36     3103   3050   2929   -157   -582   -147       C  
ATOM   2491  OH  TYR C  36     -27.196  -8.022  17.659  1.00 25.14           O  
ANISOU 2491  OH  TYR C  36     3247   3140   3163    -76   -607   -118       O  
ATOM   2492  N   PRO C  37     -29.927  -4.344  25.298  1.00 28.41           N  
ANISOU 2492  N   PRO C  37     3902   4061   2832   -688   -437   -389       N  
ATOM   2493  CA  PRO C  37     -30.630  -3.478  26.271  1.00 29.66           C  
ANISOU 2493  CA  PRO C  37     4068   4318   2882   -780   -338   -505       C  
ATOM   2494  C   PRO C  37     -30.045  -2.089  26.428  1.00 30.25           C  
ANISOU 2494  C   PRO C  37     4069   4397   3027   -754   -320   -635       C  
ATOM   2495  O   PRO C  37     -30.757  -1.142  26.758  1.00 30.70           O  
ANISOU 2495  O   PRO C  37     4092   4498   3074   -785   -208   -761       O  
ATOM   2496  CB  PRO C  37     -30.515  -4.238  27.610  1.00 31.67           C  
ANISOU 2496  CB  PRO C  37     4460   4655   2919   -901   -417   -445       C  
ATOM   2497  CG  PRO C  37     -29.782  -5.512  27.332  1.00 31.15           C  
ANISOU 2497  CG  PRO C  37     4461   4513   2863   -861   -572   -288       C  
ATOM   2498  CD  PRO C  37     -29.281  -5.510  25.920  1.00 29.05           C  
ANISOU 2498  CD  PRO C  37     4091   4137   2811   -719   -587   -272       C  
ATOM   2499  N   GLN C  38     -28.748  -1.951  26.202  1.00 31.47           N  
ANISOU 2499  N   GLN C  38     4194   4503   3261   -697   -430   -615       N  
ATOM   2500  CA  GLN C  38     -28.109  -0.643  26.277  1.00 31.62           C  
ANISOU 2500  CA  GLN C  38     4140   4511   3362   -682   -420   -733       C  
ATOM   2501  C   GLN C  38     -28.783   0.402  25.334  1.00 30.85           C  
ANISOU 2501  C   GLN C  38     3954   4350   3418   -625   -289   -814       C  
ATOM   2502  O   GLN C  38     -28.713   1.623  25.608  1.00 30.91           O  
ANISOU 2502  O   GLN C  38     3924   4351   3471   -638   -245   -939       O  
ATOM   2503  CB  GLN C  38     -26.602  -0.782  26.030  1.00 32.18           C  
ANISOU 2503  CB  GLN C  38     4171   4540   3515   -632   -557   -690       C  
ATOM   2504  CG  GLN C  38     -26.151  -1.013  24.577  1.00 31.82           C  
ANISOU 2504  CG  GLN C  38     4043   4401   3648   -527   -555   -627       C  
ATOM   2505  CD  GLN C  38     -26.104  -2.482  24.116  1.00 33.70           C  
ANISOU 2505  CD  GLN C  38     4320   4609   3875   -480   -624   -495       C  
ATOM   2506  OE1 GLN C  38     -26.665  -3.408  24.760  1.00 34.16           O  
ANISOU 2506  OE1 GLN C  38     4480   4700   3798   -529   -658   -428       O  
ATOM   2507  NE2 GLN C  38     -25.435  -2.696  22.959  1.00 32.97           N  
ANISOU 2507  NE2 GLN C  38     4152   4449   3928   -390   -638   -460       N  
ATOM   2508  N   THR C  39     -29.442  -0.064  24.263  1.00 28.08           N  
ANISOU 2508  N   THR C  39     3580   3947   3144   -566   -237   -746       N  
ATOM   2509  CA  THR C  39     -30.157   0.854  23.365  1.00 28.01           C  
ANISOU 2509  CA  THR C  39     3500   3874   3270   -509   -135   -807       C  
ATOM   2510  C   THR C  39     -31.415   1.532  23.961  1.00 29.10           C  
ANISOU 2510  C   THR C  39     3628   4061   3369   -546    -24   -928       C  
ATOM   2511  O   THR C  39     -31.909   2.528  23.415  1.00 28.13           O  
ANISOU 2511  O   THR C  39     3444   3876   3368   -495     42  -1004       O  
ATOM   2512  CB  THR C  39     -30.561   0.153  22.035  1.00 27.01           C  
ANISOU 2512  CB  THR C  39     3353   3685   3225   -437   -121   -705       C  
ATOM   2513  OG1 THR C  39     -31.644  -0.756  22.284  1.00 25.95           O  
ANISOU 2513  OG1 THR C  39     3260   3604   2996   -475    -87   -668       O  
ATOM   2514  CG2 THR C  39     -29.352  -0.591  21.451  1.00 25.10           C  
ANISOU 2514  CG2 THR C  39     3112   3404   3021   -395   -218   -605       C  
ATOM   2515  N   LYS C  40     -31.929   0.992  25.069  1.00 30.96           N  
ANISOU 2515  N   LYS C  40     3923   4405   3435   -637     -4   -947       N  
ATOM   2516  CA  LYS C  40     -33.067   1.591  25.781  1.00 33.26           C  
ANISOU 2516  CA  LYS C  40     4197   4770   3672   -685    114  -1085       C  
ATOM   2517  C   LYS C  40     -32.824   3.045  26.191  1.00 33.79           C  
ANISOU 2517  C   LYS C  40     4224   4814   3802   -674    145  -1249       C  
ATOM   2518  O   LYS C  40     -33.733   3.881  26.070  1.00 32.66           O  
ANISOU 2518  O   LYS C  40     4016   4652   3741   -638    242  -1371       O  
ATOM   2519  CB  LYS C  40     -33.431   0.806  27.062  1.00 35.17           C  
ANISOU 2519  CB  LYS C  40     4527   5152   3686   -815    129  -1082       C  
ATOM   2520  CG  LYS C  40     -34.691  -0.053  26.963  1.00 38.74           C  
ANISOU 2520  CG  LYS C  40     4980   5662   4079   -859    213  -1039       C  
ATOM   2521  CD  LYS C  40     -34.405  -1.548  26.951  1.00 41.36           C  
ANISOU 2521  CD  LYS C  40     5409   5998   4309   -908    123   -859       C  
ATOM   2522  CE  LYS C  40     -34.154  -2.147  28.336  1.00 44.94           C  
ANISOU 2522  CE  LYS C  40     5990   6560   4524  -1049     84   -827       C  
ATOM   2523  NZ  LYS C  40     -34.104  -3.665  28.229  1.00 45.61           N  
ANISOU 2523  NZ  LYS C  40     6176   6625   4529  -1095      0   -642       N  
ATOM   2524  N   THR C  41     -31.597   3.341  26.651  1.00 34.33           N  
ANISOU 2524  N   THR C  41     4325   4874   3845   -700     55  -1256       N  
ATOM   2525  CA  THR C  41     -31.265   4.672  27.151  1.00 35.61           C  
ANISOU 2525  CA  THR C  41     4464   5012   4055   -709     71  -1415       C  
ATOM   2526  C   THR C  41     -31.557   5.780  26.136  1.00 34.46           C  
ANISOU 2526  C   THR C  41     4238   4727   4129   -612    120  -1473       C  
ATOM   2527  O   THR C  41     -31.596   6.956  26.514  1.00 36.30           O  
ANISOU 2527  O   THR C  41     4450   4921   4422   -612    153  -1625       O  
ATOM   2528  CB  THR C  41     -29.795   4.769  27.663  1.00 36.81           C  
ANISOU 2528  CB  THR C  41     4651   5168   4167   -753    -55  -1401       C  
ATOM   2529  OG1 THR C  41     -28.892   4.801  26.551  1.00 37.83           O  
ANISOU 2529  OG1 THR C  41     4732   5188   4455   -683   -121  -1304       O  
ATOM   2530  CG2 THR C  41     -29.446   3.548  28.615  1.00 38.09           C  
ANISOU 2530  CG2 THR C  41     4909   5454   4110   -840   -140  -1311       C  
ATOM   2531  N   TYR C  42     -31.806   5.451  24.873  1.00 31.69           N  
ANISOU 2531  N   TYR C  42     3851   4296   3894   -532    120  -1360       N  
ATOM   2532  CA  TYR C  42     -32.243   6.494  23.951  1.00 31.53           C  
ANISOU 2532  CA  TYR C  42     3772   4146   4063   -446    160  -1407       C  
ATOM   2533  C   TYR C  42     -33.729   6.844  24.046  1.00 32.27           C  
ANISOU 2533  C   TYR C  42     3817   4254   4189   -408    260  -1516       C  
ATOM   2534  O   TYR C  42     -34.148   7.876  23.522  1.00 32.33           O  
ANISOU 2534  O   TYR C  42     3780   4150   4355   -334    282  -1588       O  
ATOM   2535  CB  TYR C  42     -31.925   6.142  22.522  1.00 29.06           C  
ANISOU 2535  CB  TYR C  42     3445   3741   3857   -379    119  -1254       C  
ATOM   2536  CG  TYR C  42     -30.474   6.190  22.236  1.00 27.95           C  
ANISOU 2536  CG  TYR C  42     3315   3557   3746   -398     41  -1186       C  
ATOM   2537  CD1 TYR C  42     -29.832   7.397  22.020  1.00 25.70           C  
ANISOU 2537  CD1 TYR C  42     3014   3168   3581   -398     29  -1243       C  
ATOM   2538  CD2 TYR C  42     -29.724   5.025  22.199  1.00 24.10           C  
ANISOU 2538  CD2 TYR C  42     2850   3130   3176   -419    -24  -1070       C  
ATOM   2539  CE1 TYR C  42     -28.475   7.436  21.751  1.00 28.39           C  
ANISOU 2539  CE1 TYR C  42     3348   3483   3956   -429    -34  -1187       C  
ATOM   2540  CE2 TYR C  42     -28.366   5.055  21.920  1.00 25.04           C  
ANISOU 2540  CE2 TYR C  42     2954   3220   3338   -431    -93  -1022       C  
ATOM   2541  CZ  TYR C  42     -27.742   6.242  21.694  1.00 25.48           C  
ANISOU 2541  CZ  TYR C  42     2982   3192   3509   -441    -93  -1081       C  
ATOM   2542  OH  TYR C  42     -26.402   6.263  21.426  1.00 23.03           O  
ANISOU 2542  OH  TYR C  42     2638   2866   3244   -466   -152  -1042       O  
ATOM   2543  N   PHE C  43     -34.496   5.973  24.677  1.00 33.16           N  
ANISOU 2543  N   PHE C  43     3938   4501   4160   -461    312  -1522       N  
ATOM   2544  CA  PHE C  43     -35.945   6.061  24.727  1.00 35.49           C  
ANISOU 2544  CA  PHE C  43     4166   4840   4480   -434    413  -1615       C  
ATOM   2545  C   PHE C  43     -36.374   6.079  26.201  1.00 39.50           C  
ANISOU 2545  C   PHE C  43     4687   5498   4822   -535    498  -1765       C  
ATOM   2546  O   PHE C  43     -37.220   5.289  26.608  1.00 39.67           O  
ANISOU 2546  O   PHE C  43     4700   5644   4729   -595    569  -1765       O  
ATOM   2547  CB  PHE C  43     -36.576   4.834  24.019  1.00 34.55           C  
ANISOU 2547  CB  PHE C  43     4035   4757   4334   -427    415  -1473       C  
ATOM   2548  CG  PHE C  43     -36.267   4.739  22.541  1.00 30.18           C  
ANISOU 2548  CG  PHE C  43     3473   4075   3920   -334    342  -1334       C  
ATOM   2549  CD1 PHE C  43     -37.178   5.182  21.599  1.00 27.97           C  
ANISOU 2549  CD1 PHE C  43     3119   3718   3788   -238    360  -1350       C  
ATOM   2550  CD2 PHE C  43     -35.076   4.192  22.097  1.00 29.19           C  
ANISOU 2550  CD2 PHE C  43     3409   3911   3771   -344    254  -1194       C  
ATOM   2551  CE1 PHE C  43     -36.912   5.091  20.227  1.00 27.34           C  
ANISOU 2551  CE1 PHE C  43     3045   3530   3811   -165    293  -1219       C  
ATOM   2552  CE2 PHE C  43     -34.795   4.089  20.710  1.00 27.52           C  
ANISOU 2552  CE2 PHE C  43     3191   3596   3670   -269    204  -1076       C  
ATOM   2553  CZ  PHE C  43     -35.705   4.539  19.783  1.00 25.52           C  
ANISOU 2553  CZ  PHE C  43     2884   3272   3542   -186    223  -1084       C  
ATOM   2554  N   PRO C  44     -35.773   6.978  27.013  1.00 43.04           N  
ANISOU 2554  N   PRO C  44     5163   5942   5248   -566    493  -1897       N  
ATOM   2555  CA  PRO C  44     -36.032   6.918  28.437  1.00 45.87           C  
ANISOU 2555  CA  PRO C  44     5557   6459   5412   -679    565  -2032       C  
ATOM   2556  C   PRO C  44     -37.406   7.509  28.756  1.00 47.73           C  
ANISOU 2556  C   PRO C  44     5695   6744   5694   -651    709  -2231       C  
ATOM   2557  O   PRO C  44     -37.997   7.176  29.799  1.00 50.09           O  
ANISOU 2557  O   PRO C  44     6005   7212   5816   -754    810  -2330       O  
ATOM   2558  CB  PRO C  44     -34.911   7.768  29.004  1.00 46.79           C  
ANISOU 2558  CB  PRO C  44     5725   6531   5523   -706    498  -2112       C  
ATOM   2559  CG  PRO C  44     -34.863   8.934  28.005  1.00 46.49           C  
ANISOU 2559  CG  PRO C  44     5619   6297   5749   -579    478  -2157       C  
ATOM   2560  CD  PRO C  44     -35.085   8.238  26.652  1.00 43.48           C  
ANISOU 2560  CD  PRO C  44     5206   5843   5470   -501    442  -1963       C  
ATOM   2561  N   HIS C  45     -37.898   8.346  27.837  1.00 47.74           N  
ANISOU 2561  N   HIS C  45     5604   6603   5933   -515    715  -2284       N  
ATOM   2562  CA  HIS C  45     -39.239   8.921  27.854  1.00 49.26           C  
ANISOU 2562  CA  HIS C  45     5672   6809   6235   -445    828  -2462       C  
ATOM   2563  C   HIS C  45     -40.311   7.974  27.268  1.00 49.04           C  
ANISOU 2563  C   HIS C  45     5569   6850   6215   -432    876  -2374       C  
ATOM   2564  O   HIS C  45     -41.462   8.359  27.145  1.00 50.20           O  
ANISOU 2564  O   HIS C  45     5590   7010   6473   -364    958  -2509       O  
ATOM   2565  CB  HIS C  45     -39.246  10.242  27.054  1.00 49.56           C  
ANISOU 2565  CB  HIS C  45     5654   6635   6542   -294    778  -2538       C  
ATOM   2566  CG  HIS C  45     -38.934  10.090  25.583  1.00 49.36           C  
ANISOU 2566  CG  HIS C  45     5635   6452   6666   -202    667  -2331       C  
ATOM   2567  ND1 HIS C  45     -37.717   9.644  25.112  1.00 48.73           N  
ANISOU 2567  ND1 HIS C  45     5651   6322   6542   -240    564  -2140       N  
ATOM   2568  CD2 HIS C  45     -39.681  10.352  24.481  1.00 50.19           C  
ANISOU 2568  CD2 HIS C  45     5664   6447   6961    -76    641  -2296       C  
ATOM   2569  CE1 HIS C  45     -37.729   9.627  23.792  1.00 46.28           C  
ANISOU 2569  CE1 HIS C  45     5327   5885   6373   -151    496  -1999       C  
ATOM   2570  NE2 HIS C  45     -38.909  10.051  23.384  1.00 47.52           N  
ANISOU 2570  NE2 HIS C  45     5389   6001   6667    -53    533  -2082       N  
ATOM   2571  N   PHE C  46     -39.933   6.761  26.869  1.00 47.34           N  
ANISOU 2571  N   PHE C  46     5422   6668   5898   -489    816  -2157       N  
ATOM   2572  CA  PHE C  46     -40.917   5.741  26.479  1.00 46.86           C  
ANISOU 2572  CA  PHE C  46     5305   6691   5811   -512    863  -2079       C  
ATOM   2573  C   PHE C  46     -41.169   4.795  27.647  1.00 48.48           C  
ANISOU 2573  C   PHE C  46     5564   7096   5759   -686    952  -2086       C  
ATOM   2574  O   PHE C  46     -40.250   4.475  28.419  1.00 48.21           O  
ANISOU 2574  O   PHE C  46     5657   7113   5549   -787    911  -2034       O  
ATOM   2575  CB  PHE C  46     -40.415   4.894  25.282  1.00 44.34           C  
ANISOU 2575  CB  PHE C  46     5035   6278   5535   -475    744  -1838       C  
ATOM   2576  CG  PHE C  46     -40.633   5.514  23.932  1.00 41.95           C  
ANISOU 2576  CG  PHE C  46     4663   5811   5464   -320    680  -1805       C  
ATOM   2577  CD1 PHE C  46     -40.854   6.874  23.772  1.00 43.97           C  
ANISOU 2577  CD1 PHE C  46     4852   5959   5895   -211    684  -1949       C  
ATOM   2578  CD2 PHE C  46     -40.601   4.713  22.798  1.00 40.88           C  
ANISOU 2578  CD2 PHE C  46     4543   5622   5369   -286    606  -1624       C  
ATOM   2579  CE1 PHE C  46     -41.043   7.437  22.499  1.00 44.07           C  
ANISOU 2579  CE1 PHE C  46     4823   5810   6112    -75    606  -1896       C  
ATOM   2580  CE2 PHE C  46     -40.765   5.254  21.531  1.00 40.76           C  
ANISOU 2580  CE2 PHE C  46     4484   5463   5541   -156    537  -1579       C  
ATOM   2581  CZ  PHE C  46     -40.990   6.630  21.376  1.00 42.61           C  
ANISOU 2581  CZ  PHE C  46     4660   5587   5943    -52    533  -1707       C  
ATOM   2582  N   ASP C  47     -42.408   4.322  27.766  1.00 50.29           N  
ANISOU 2582  N   ASP C  47     5700   7442   5966   -730   1065  -2142       N  
ATOM   2583  CA  ASP C  47     -42.618   3.066  28.459  1.00 51.65           C  
ANISOU 2583  CA  ASP C  47     5947   7773   5905   -905   1118  -2052       C  
ATOM   2584  C   ASP C  47     -42.180   2.011  27.468  1.00 50.92           C  
ANISOU 2584  C   ASP C  47     5922   7590   5836   -889    992  -1803       C  
ATOM   2585  O   ASP C  47     -42.692   1.949  26.334  1.00 50.21           O  
ANISOU 2585  O   ASP C  47     5743   7415   5919   -786    961  -1757       O  
ATOM   2586  CB  ASP C  47     -44.065   2.841  28.881  1.00 53.49           C  
ANISOU 2586  CB  ASP C  47     6053   8166   6105   -979   1288  -2186       C  
ATOM   2587  CG  ASP C  47     -44.262   1.488  29.542  1.00 53.73           C  
ANISOU 2587  CG  ASP C  47     6180   8347   5888  -1183   1338  -2066       C  
ATOM   2588  OD1 ASP C  47     -44.134   0.468  28.848  1.00 53.75           O  
ANISOU 2588  OD1 ASP C  47     6235   8293   5892  -1199   1251  -1863       O  
ATOM   2589  OD2 ASP C  47     -44.515   1.426  30.758  1.00 57.06           O  
ANISOU 2589  OD2 ASP C  47     6638   8937   6106  -1334   1460  -2169       O  
ATOM   2590  N   LEU C  48     -41.224   1.193  27.887  1.00 51.58           N  
ANISOU 2590  N   LEU C  48     6163   7688   5748   -984    910  -1651       N  
ATOM   2591  CA  LEU C  48     -40.582   0.258  26.985  1.00 50.57           C  
ANISOU 2591  CA  LEU C  48     6109   7456   5649   -953    776  -1430       C  
ATOM   2592  C   LEU C  48     -40.915  -1.188  27.324  1.00 51.98           C  
ANISOU 2592  C   LEU C  48     6371   7720   5659  -1100    786  -1296       C  
ATOM   2593  O   LEU C  48     -40.077  -2.075  27.137  1.00 51.34           O  
ANISOU 2593  O   LEU C  48     6410   7580   5518  -1120    665  -1119       O  
ATOM   2594  CB  LEU C  48     -39.077   0.497  27.016  1.00 49.77           C  
ANISOU 2594  CB  LEU C  48     6110   7264   5536   -914    644  -1357       C  
ATOM   2595  CG  LEU C  48     -38.657   1.897  26.534  1.00 48.56           C  
ANISOU 2595  CG  LEU C  48     5887   6997   5568   -778    621  -1464       C  
ATOM   2596  CD1 LEU C  48     -37.313   2.301  27.128  1.00 48.39           C  
ANISOU 2596  CD1 LEU C  48     5955   6950   5481   -798    535  -1463       C  
ATOM   2597  CD2 LEU C  48     -38.622   1.947  25.009  1.00 45.33           C  
ANISOU 2597  CD2 LEU C  48     5423   6441   5360   -643    552  -1369       C  
ATOM   2598  N   HIS C  49     -42.155  -1.420  27.770  1.00 54.40           N  
ANISOU 2598  N   HIS C  49     6606   8159   5905  -1199    928  -1382       N  
ATOM   2599  CA  HIS C  49     -42.638  -2.767  28.122  1.00 55.81           C  
ANISOU 2599  CA  HIS C  49     6860   8423   5924  -1365    957  -1262       C  
ATOM   2600  C   HIS C  49     -43.334  -3.436  26.950  1.00 54.71           C  
ANISOU 2600  C   HIS C  49     6644   8218   5926  -1319    936  -1178       C  
ATOM   2601  O   HIS C  49     -43.884  -2.766  26.082  1.00 54.18           O  
ANISOU 2601  O   HIS C  49     6427   8099   6058  -1186    953  -1265       O  
ATOM   2602  CB  HIS C  49     -43.563  -2.724  29.358  1.00 58.74           C  
ANISOU 2602  CB  HIS C  49     7204   8996   6117  -1538   1137  -1400       C  
ATOM   2603  CG  HIS C  49     -45.017  -2.446  29.062  1.00 61.92           C  
ANISOU 2603  CG  HIS C  49     7406   9481   6638  -1531   1290  -1550       C  
ATOM   2604  ND1 HIS C  49     -45.822  -3.315  28.351  1.00 64.87           N  
ANISOU 2604  ND1 HIS C  49     7720   9850   7078  -1565   1299  -1467       N  
ATOM   2605  CD2 HIS C  49     -45.832  -1.437  29.466  1.00 65.37           C  
ANISOU 2605  CD2 HIS C  49     7684  10019   7134  -1505   1440  -1792       C  
ATOM   2606  CE1 HIS C  49     -47.054  -2.833  28.292  1.00 66.11           C  
ANISOU 2606  CE1 HIS C  49     7679  10103   7338  -1555   1441  -1646       C  
ATOM   2607  NE2 HIS C  49     -47.083  -1.690  28.955  1.00 66.66           N  
ANISOU 2607  NE2 HIS C  49     7681  10235   7410  -1511   1529  -1847       N  
ATOM   2608  N   HIS C  50     -43.328  -4.765  26.945  1.00 54.61           N  
ANISOU 2608  N   HIS C  50     6740   8202   5808  -1433    890  -1010       N  
ATOM   2609  CA  HIS C  50     -43.897  -5.538  25.843  1.00 53.62           C  
ANISOU 2609  CA  HIS C  50     6566   8007   5802  -1405    852   -920       C  
ATOM   2610  C   HIS C  50     -45.329  -5.088  25.544  1.00 52.90           C  
ANISOU 2610  C   HIS C  50     6270   8001   5828  -1397    986  -1075       C  
ATOM   2611  O   HIS C  50     -46.211  -5.190  26.397  1.00 55.24           O  
ANISOU 2611  O   HIS C  50     6515   8454   6018  -1544   1133  -1168       O  
ATOM   2612  CB  HIS C  50     -43.831  -7.050  26.157  1.00 54.82           C  
ANISOU 2612  CB  HIS C  50     6874   8159   5797  -1570    807   -741       C  
ATOM   2613  CG  HIS C  50     -44.170  -7.936  24.991  1.00 57.42           C  
ANISOU 2613  CG  HIS C  50     7186   8387   6245  -1537    736   -634       C  
ATOM   2614  ND1 HIS C  50     -44.238  -7.471  23.688  1.00 59.33           N  
ANISOU 2614  ND1 HIS C  50     7316   8531   6698  -1359    682   -665       N  
ATOM   2615  CD2 HIS C  50     -44.437  -9.266  24.929  1.00 60.60           C  
ANISOU 2615  CD2 HIS C  50     7683   8763   6578  -1665    702   -497       C  
ATOM   2616  CE1 HIS C  50     -44.558  -8.471  22.882  1.00 59.63           C  
ANISOU 2616  CE1 HIS C  50     7373   8501   6785  -1378    624   -564       C  
ATOM   2617  NE2 HIS C  50     -44.680  -9.571  23.609  1.00 61.08           N  
ANISOU 2617  NE2 HIS C  50     7678   8719   6809  -1560    634   -464       N  
ATOM   2618  N   GLY C  51     -45.545  -4.565  24.340  1.00 50.08           N  
ANISOU 2618  N   GLY C  51     5794   7545   5688  -1225    933  -1107       N  
ATOM   2619  CA  GLY C  51     -46.874  -4.164  23.895  1.00 49.53           C  
ANISOU 2619  CA  GLY C  51     5521   7536   5763  -1188   1021  -1244       C  
ATOM   2620  C   GLY C  51     -47.215  -2.710  24.144  1.00 49.23           C  
ANISOU 2620  C   GLY C  51     5338   7533   5835  -1077   1098  -1454       C  
ATOM   2621  O   GLY C  51     -48.367  -2.306  23.964  1.00 50.73           O  
ANISOU 2621  O   GLY C  51     5340   7790   6145  -1046   1181  -1597       O  
ATOM   2622  N   SER C  52     -46.227  -1.913  24.542  1.00 47.34           N  
ANISOU 2622  N   SER C  52     5177   7241   5571  -1012   1064  -1481       N  
ATOM   2623  CA  SER C  52     -46.451  -0.492  24.767  1.00 46.80           C  
ANISOU 2623  CA  SER C  52     4989   7174   5617   -899   1122  -1683       C  
ATOM   2624  C   SER C  52     -46.947   0.193  23.502  1.00 45.44           C  
ANISOU 2624  C   SER C  52     4679   6886   5702   -709   1053  -1721       C  
ATOM   2625  O   SER C  52     -46.648  -0.214  22.388  1.00 44.57           O  
ANISOU 2625  O   SER C  52     4608   6658   5667   -639    930  -1574       O  
ATOM   2626  CB  SER C  52     -45.198   0.208  25.321  1.00 46.35           C  
ANISOU 2626  CB  SER C  52     5056   7060   5497   -867   1073  -1690       C  
ATOM   2627  OG  SER C  52     -44.420   0.793  24.308  1.00 43.60           O  
ANISOU 2627  OG  SER C  52     4730   6533   5304   -705    939  -1623       O  
ATOM   2628  N   ALA C  53     -47.746   1.223  23.682  1.00 46.04           N  
ANISOU 2628  N   ALA C  53     4591   6995   5908   -627   1132  -1927       N  
ATOM   2629  CA  ALA C  53     -48.347   1.900  22.575  1.00 45.17           C  
ANISOU 2629  CA  ALA C  53     4342   6779   6041   -450   1061  -1973       C  
ATOM   2630  C   ALA C  53     -47.297   2.779  21.911  1.00 43.49           C  
ANISOU 2630  C   ALA C  53     4221   6373   5930   -301    926  -1910       C  
ATOM   2631  O   ALA C  53     -47.357   3.054  20.704  1.00 42.13           O  
ANISOU 2631  O   ALA C  53     4023   6068   5915   -169    809  -1840       O  
ATOM   2632  CB  ALA C  53     -49.503   2.726  23.074  1.00 47.93           C  
ANISOU 2632  CB  ALA C  53     4484   7221   6505   -404   1183  -2226       C  
ATOM   2633  N   GLN C  54     -46.330   3.231  22.711  1.00 43.13           N  
ANISOU 2633  N   GLN C  54     4286   6316   5786   -334    943  -1936       N  
ATOM   2634  CA  GLN C  54     -45.244   4.045  22.180  1.00 41.99           C  
ANISOU 2634  CA  GLN C  54     4234   5997   5725   -224    828  -1876       C  
ATOM   2635  C   GLN C  54     -44.288   3.223  21.314  1.00 38.96           C  
ANISOU 2635  C   GLN C  54     3986   5526   5290   -235    706  -1640       C  
ATOM   2636  O   GLN C  54     -43.932   3.623  20.204  1.00 37.51           O  
ANISOU 2636  O   GLN C  54     3821   5198   5233   -121    598  -1556       O  
ATOM   2637  CB  GLN C  54     -44.480   4.702  23.309  1.00 43.10           C  
ANISOU 2637  CB  GLN C  54     4446   6159   5772   -271    877  -1979       C  
ATOM   2638  CG  GLN C  54     -45.193   5.852  23.897  1.00 45.89           C  
ANISOU 2638  CG  GLN C  54     4674   6532   6231   -207    967  -2225       C  
ATOM   2639  CD  GLN C  54     -44.425   6.405  25.028  1.00 49.01           C  
ANISOU 2639  CD  GLN C  54     5152   6957   6510   -271   1014  -2328       C  
ATOM   2640  OE1 GLN C  54     -44.215   5.717  26.035  1.00 51.83           O  
ANISOU 2640  OE1 GLN C  54     5582   7467   6646   -428   1087  -2325       O  
ATOM   2641  NE2 GLN C  54     -43.950   7.642  24.877  1.00 50.94           N  
ANISOU 2641  NE2 GLN C  54     5404   7053   6897   -160    960  -2411       N  
ATOM   2642  N   VAL C  55     -43.893   2.068  21.814  1.00 37.74           N  
ANISOU 2642  N   VAL C  55     3929   5461   4949   -373    722  -1535       N  
ATOM   2643  CA  VAL C  55     -43.053   1.170  21.021  1.00 36.21           C  
ANISOU 2643  CA  VAL C  55     3852   5192   4713   -380    612  -1329       C  
ATOM   2644  C   VAL C  55     -43.758   0.750  19.731  1.00 34.89           C  
ANISOU 2644  C   VAL C  55     3622   4974   4660   -312    555  -1256       C  
ATOM   2645  O   VAL C  55     -43.216   0.907  18.646  1.00 34.37           O  
ANISOU 2645  O   VAL C  55     3598   4785   4676   -220    454  -1158       O  
ATOM   2646  CB  VAL C  55     -42.593  -0.050  21.845  1.00 36.16           C  
ANISOU 2646  CB  VAL C  55     3963   5281   4497   -536    628  -1235       C  
ATOM   2647  CG1 VAL C  55     -41.813  -1.019  20.965  1.00 33.98           C  
ANISOU 2647  CG1 VAL C  55     3789   4918   4204   -525    513  -1042       C  
ATOM   2648  CG2 VAL C  55     -41.736   0.451  23.028  1.00 35.93           C  
ANISOU 2648  CG2 VAL C  55     4010   5289   4352   -592    652  -1296       C  
ATOM   2649  N   LYS C  56     -44.986   0.275  19.834  1.00 35.14           N  
ANISOU 2649  N   LYS C  56     3549   5105   4698   -360    621  -1313       N  
ATOM   2650  CA  LYS C  56     -45.726  -0.093  18.632  1.00 34.17           C  
ANISOU 2650  CA  LYS C  56     3356   4942   4686   -298    557  -1259       C  
ATOM   2651  C   LYS C  56     -45.908   1.118  17.692  1.00 32.35           C  
ANISOU 2651  C   LYS C  56     3052   4587   4652   -123    481  -1305       C  
ATOM   2652  O   LYS C  56     -45.675   1.021  16.489  1.00 31.06           O  
ANISOU 2652  O   LYS C  56     2928   4322   4551    -47    371  -1193       O  
ATOM   2653  CB  LYS C  56     -47.067  -0.755  19.011  1.00 36.42           C  
ANISOU 2653  CB  LYS C  56     3517   5369   4953   -395    649  -1335       C  
ATOM   2654  CG  LYS C  56     -46.899  -2.102  19.805  1.00 38.81           C  
ANISOU 2654  CG  LYS C  56     3921   5772   5051   -589    706  -1249       C  
ATOM   2655  CD  LYS C  56     -47.227  -3.381  18.939  1.00 40.07           C  
ANISOU 2655  CD  LYS C  56     4110   5912   5204   -641    638  -1114       C  
ATOM   2656  CE  LYS C  56     -47.440  -4.695  19.789  1.00 40.78           C  
ANISOU 2656  CE  LYS C  56     4273   6106   5117   -850    708  -1053       C  
ATOM   2657  NZ  LYS C  56     -46.205  -5.525  20.177  1.00 39.21           N  
ANISOU 2657  NZ  LYS C  56     4285   5853   4760   -924    648   -898       N  
ATOM   2658  N   ALA C  57     -46.282   2.266  18.240  1.00 32.31           N  
ANISOU 2658  N   ALA C  57     2955   4584   4738    -60    535  -1469       N  
ATOM   2659  CA  ALA C  57     -46.417   3.499  17.448  1.00 31.97           C  
ANISOU 2659  CA  ALA C  57     2859   4400   4888    109    452  -1512       C  
ATOM   2660  C   ALA C  57     -45.119   3.937  16.739  1.00 29.84           C  
ANISOU 2660  C   ALA C  57     2738   3973   4627    165    348  -1378       C  
ATOM   2661  O   ALA C  57     -45.140   4.471  15.611  1.00 29.05           O  
ANISOU 2661  O   ALA C  57     2645   3745   4648    276    241  -1316       O  
ATOM   2662  CB  ALA C  57     -46.924   4.638  18.359  1.00 34.31           C  
ANISOU 2662  CB  ALA C  57     3044   4719   5275    158    538  -1731       C  
ATOM   2663  N   HIS C  58     -43.996   3.712  17.410  1.00 28.50           N  
ANISOU 2663  N   HIS C  58     2685   3819   4324     80    378  -1334       N  
ATOM   2664  CA  HIS C  58     -42.692   4.125  16.899  1.00 27.14           C  
ANISOU 2664  CA  HIS C  58     2637   3521   4154    111    301  -1227       C  
ATOM   2665  C   HIS C  58     -42.219   3.128  15.817  1.00 26.69           C  
ANISOU 2665  C   HIS C  58     2662   3435   4043     98    224  -1044       C  
ATOM   2666  O   HIS C  58     -41.680   3.537  14.772  1.00 25.21           O  
ANISOU 2666  O   HIS C  58     2530   3131   3918    165    142   -953       O  
ATOM   2667  CB  HIS C  58     -41.705   4.248  18.053  1.00 26.79           C  
ANISOU 2667  CB  HIS C  58     2665   3515   3997     27    353  -1266       C  
ATOM   2668  CG  HIS C  58     -40.323   4.584  17.626  1.00 23.82           C  
ANISOU 2668  CG  HIS C  58     2398   3033   3621     40    285  -1166       C  
ATOM   2669  ND1 HIS C  58     -40.027   5.724  16.922  1.00 22.70           N  
ANISOU 2669  ND1 HIS C  58     2266   2744   3617    130    228  -1164       N  
ATOM   2670  CD2 HIS C  58     -39.159   3.914  17.776  1.00 24.99           C  
ANISOU 2670  CD2 HIS C  58     2643   3199   3654    -30    261  -1065       C  
ATOM   2671  CE1 HIS C  58     -38.737   5.734  16.645  1.00 25.84           C  
ANISOU 2671  CE1 HIS C  58     2756   3084   3976    101    186  -1066       C  
ATOM   2672  NE2 HIS C  58     -38.186   4.644  17.150  1.00 24.79           N  
ANISOU 2672  NE2 HIS C  58     2667   3053   3698     13    204  -1012       N  
ATOM   2673  N   GLY C  59     -42.477   1.833  16.046  1.00 26.77           N  
ANISOU 2673  N   GLY C  59     2681   3550   3939      7    252   -996       N  
ATOM   2674  CA  GLY C  59     -42.106   0.759  15.082  1.00 25.24           C  
ANISOU 2674  CA  GLY C  59     2562   3334   3693     -9    184   -844       C  
ATOM   2675  C   GLY C  59     -42.711   0.985  13.714  1.00 25.08           C  
ANISOU 2675  C   GLY C  59     2506   3241   3782     86    104   -802       C  
ATOM   2676  O   GLY C  59     -42.082   0.777  12.677  1.00 24.55           O  
ANISOU 2676  O   GLY C  59     2518   3103   3707    116     33   -689       O  
ATOM   2677  N   LYS C  60     -43.951   1.426  13.733  1.00 25.72           N  
ANISOU 2677  N   LYS C  60     2462   3348   3961    132    115   -901       N  
ATOM   2678  CA  LYS C  60     -44.696   1.748  12.564  1.00 25.71           C  
ANISOU 2678  CA  LYS C  60     2409   3285   4074    228     25   -880       C  
ATOM   2679  C   LYS C  60     -43.992   2.855  11.784  1.00 25.01           C  
ANISOU 2679  C   LYS C  60     2392   3048   4061    325    -54   -824       C  
ATOM   2680  O   LYS C  60     -43.914   2.813  10.541  1.00 24.63           O  
ANISOU 2680  O   LYS C  60     2398   2930   4030    372   -149   -720       O  
ATOM   2681  CB  LYS C  60     -46.088   2.204  13.048  1.00 28.03           C  
ANISOU 2681  CB  LYS C  60     2530   3641   4479    266     63  -1035       C  
ATOM   2682  CG  LYS C  60     -47.044   2.699  11.994  1.00 31.94           C  
ANISOU 2682  CG  LYS C  60     2937   4076   5123    385    -45  -1044       C  
ATOM   2683  CD  LYS C  60     -48.347   3.151  12.644  1.00 37.25           C  
ANISOU 2683  CD  LYS C  60     3412   4822   5918    424      8  -1226       C  
ATOM   2684  CE  LYS C  60     -49.262   3.843  11.642  1.00 40.25           C  
ANISOU 2684  CE  LYS C  60     3695   5122   6477    571   -125  -1246       C  
ATOM   2685  NZ  LYS C  60     -50.608   4.195  12.237  1.00 41.39           N  
ANISOU 2685  NZ  LYS C  60     3614   5352   6762    618    -75  -1441       N  
ATOM   2686  N   LYS C  61     -43.501   3.865  12.501  1.00 24.17           N  
ANISOU 2686  N   LYS C  61     2293   2893   3997    344    -15   -896       N  
ATOM   2687  CA  LYS C  61     -42.789   4.950  11.860  1.00 23.58           C  
ANISOU 2687  CA  LYS C  61     2296   2669   3996    413    -82   -843       C  
ATOM   2688  C   LYS C  61     -41.413   4.530  11.319  1.00 21.17           C  
ANISOU 2688  C   LYS C  61     2129   2331   3585    357    -98   -701       C  
ATOM   2689  O   LYS C  61     -41.002   4.977  10.254  1.00 20.94           O  
ANISOU 2689  O   LYS C  61     2173   2200   3585    397   -169   -604       O  
ATOM   2690  CB  LYS C  61     -42.613   6.095  12.827  1.00 25.87           C  
ANISOU 2690  CB  LYS C  61     2558   2912   4361    435    -34   -970       C  
ATOM   2691  CG  LYS C  61     -43.903   6.831  13.133  1.00 29.28           C  
ANISOU 2691  CG  LYS C  61     2849   3334   4941    528    -34  -1122       C  
ATOM   2692  CD  LYS C  61     -43.647   8.326  13.342  1.00 35.95           C  
ANISOU 2692  CD  LYS C  61     3707   4030   5922    606    -60  -1200       C  
ATOM   2693  CE  LYS C  61     -43.508   8.691  14.796  1.00 40.47           C  
ANISOU 2693  CE  LYS C  61     4237   4666   6476    561     54  -1370       C  
ATOM   2694  NZ  LYS C  61     -43.124  10.178  15.026  1.00 43.50           N  
ANISOU 2694  NZ  LYS C  61     4651   4884   6995    628     26  -1454       N  
ATOM   2695  N   VAL C  62     -40.717   3.677  12.041  1.00 18.81           N  
ANISOU 2695  N   VAL C  62     1863   2120   3165    264    -33   -692       N  
ATOM   2696  CA  VAL C  62     -39.405   3.234  11.613  1.00 18.67           C  
ANISOU 2696  CA  VAL C  62     1950   2082   3062    220    -44   -582       C  
ATOM   2697  C   VAL C  62     -39.592   2.379  10.337  1.00 18.37           C  
ANISOU 2697  C   VAL C  62     1950   2045   2985    233   -102   -474       C  
ATOM   2698  O   VAL C  62     -38.885   2.575   9.369  1.00 18.06           O  
ANISOU 2698  O   VAL C  62     1985   1940   2936    246   -140   -385       O  
ATOM   2699  CB  VAL C  62     -38.716   2.448  12.717  1.00 17.75           C  
ANISOU 2699  CB  VAL C  62     1852   2056   2835    131     16   -602       C  
ATOM   2700  CG1 VAL C  62     -37.528   1.712  12.189  1.00 16.95           C  
ANISOU 2700  CG1 VAL C  62     1833   1950   2658     99     -5   -495       C  
ATOM   2701  CG2 VAL C  62     -38.340   3.390  13.876  1.00 19.76           C  
ANISOU 2701  CG2 VAL C  62     2090   2305   3114    113     62   -705       C  
ATOM   2702  N   ALA C  63     -40.585   1.489  10.324  1.00 18.40           N  
ANISOU 2702  N   ALA C  63     1902   2124   2967    221   -106   -490       N  
ATOM   2703  CA  ALA C  63     -40.810   0.598   9.174  1.00 19.32           C  
ANISOU 2703  CA  ALA C  63     2055   2247   3040    224   -164   -405       C  
ATOM   2704  C   ALA C  63     -41.214   1.424   7.952  1.00 20.16           C  
ANISOU 2704  C   ALA C  63     2174   2265   3219    306   -251   -360       C  
ATOM   2705  O   ALA C  63     -40.776   1.137   6.831  1.00 19.44           O  
ANISOU 2705  O   ALA C  63     2166   2144   3076    310   -298   -266       O  
ATOM   2706  CB  ALA C  63     -41.873  -0.472   9.498  1.00 19.57           C  
ANISOU 2706  CB  ALA C  63     2019   2373   3044    180   -152   -443       C  
ATOM   2707  N   ALA C  64     -41.977   2.495   8.205  1.00 21.43           N  
ANISOU 2707  N   ALA C  64     2261   2381   3499    373   -273   -430       N  
ATOM   2708  CA  ALA C  64     -42.401   3.446   7.178  1.00 22.08           C  
ANISOU 2708  CA  ALA C  64     2361   2358   3670    461   -375   -386       C  
ATOM   2709  C   ALA C  64     -41.216   4.212   6.560  1.00 21.78           C  
ANISOU 2709  C   ALA C  64     2449   2213   3613    458   -392   -290       C  
ATOM   2710  O   ALA C  64     -41.180   4.487   5.324  1.00 21.74           O  
ANISOU 2710  O   ALA C  64     2525   2140   3596    486   -477   -188       O  
ATOM   2711  CB  ALA C  64     -43.495   4.449   7.785  1.00 23.48           C  
ANISOU 2711  CB  ALA C  64     2413   2501   4006    546   -394   -510       C  
ATOM   2712  N   ALA C  65     -40.234   4.537   7.402  1.00 20.84           N  
ANISOU 2712  N   ALA C  65     2351   2086   3482    411   -313   -321       N  
ATOM   2713  CA  ALA C  65     -39.018   5.188   6.905  1.00 20.48           C  
ANISOU 2713  CA  ALA C  65     2412   1954   3417    383   -310   -238       C  
ATOM   2714  C   ALA C  65     -38.291   4.215   5.973  1.00 19.41           C  
ANISOU 2714  C   ALA C  65     2355   1868   3151    331   -304   -136       C  
ATOM   2715  O   ALA C  65     -37.841   4.576   4.869  1.00 20.18           O  
ANISOU 2715  O   ALA C  65     2544   1905   3217    324   -340    -36       O  
ATOM   2716  CB  ALA C  65     -38.124   5.631   8.049  1.00 19.36           C  
ANISOU 2716  CB  ALA C  65     2259   1808   3288    336   -231   -305       C  
ATOM   2717  N   LEU C  66     -38.231   2.962   6.377  1.00 19.40           N  
ANISOU 2717  N   LEU C  66     2323   1975   3072    292   -260   -162       N  
ATOM   2718  CA  LEU C  66     -37.567   1.928   5.545  1.00 18.52           C  
ANISOU 2718  CA  LEU C  66     2278   1911   2848    253   -252    -90       C  
ATOM   2719  C   LEU C  66     -38.297   1.691   4.209  1.00 18.90           C  
ANISOU 2719  C   LEU C  66     2370   1948   2864    285   -333    -25       C  
ATOM   2720  O   LEU C  66     -37.669   1.636   3.145  1.00 19.01           O  
ANISOU 2720  O   LEU C  66     2472   1948   2805    265   -341     53       O  
ATOM   2721  CB  LEU C  66     -37.418   0.645   6.341  1.00 17.01           C  
ANISOU 2721  CB  LEU C  66     2051   1814   2599    212   -205   -135       C  
ATOM   2722  CG  LEU C  66     -36.446   0.657   7.517  1.00 17.74           C  
ANISOU 2722  CG  LEU C  66     2126   1929   2685    169   -139   -178       C  
ATOM   2723  CD1 LEU C  66     -36.524  -0.697   8.336  1.00 13.59           C  
ANISOU 2723  CD1 LEU C  66     1578   1488   2098    130   -119   -209       C  
ATOM   2724  CD2 LEU C  66     -34.966   0.912   7.103  1.00 12.74           C  
ANISOU 2724  CD2 LEU C  66     1545   1270   2025    141   -108   -132       C  
ATOM   2725  N   VAL C  67     -39.618   1.598   4.267  1.00 20.41           N  
ANISOU 2725  N   VAL C  67     2494   2153   3108    330   -393    -64       N  
ATOM   2726  CA  VAL C  67     -40.475   1.516   3.073  1.00 21.32           C  
ANISOU 2726  CA  VAL C  67     2636   2254   3210    369   -497    -12       C  
ATOM   2727  C   VAL C  67     -40.229   2.694   2.144  1.00 23.90           C  
ANISOU 2727  C   VAL C  67     3053   2475   3552    400   -562     76       C  
ATOM   2728  O   VAL C  67     -40.021   2.505   0.947  1.00 25.95           O  
ANISOU 2728  O   VAL C  67     3411   2730   3719    384   -608    163       O  
ATOM   2729  CB  VAL C  67     -41.952   1.409   3.448  1.00 21.55           C  
ANISOU 2729  CB  VAL C  67     2547   2314   3328    417   -552    -87       C  
ATOM   2730  CG1 VAL C  67     -42.893   1.580   2.209  1.00 20.55           C  
ANISOU 2730  CG1 VAL C  67     2437   2158   3213    473   -692    -35       C  
ATOM   2731  CG2 VAL C  67     -42.207   0.078   4.131  1.00 20.92           C  
ANISOU 2731  CG2 VAL C  67     2406   2341   3202    359   -493   -148       C  
ATOM   2732  N   GLU C  68     -40.189   3.904   2.681  1.00 25.43           N  
ANISOU 2732  N   GLU C  68     3229   2580   3855    433   -565     58       N  
ATOM   2733  CA  GLU C  68     -39.860   5.087   1.858  1.00 26.03           C  
ANISOU 2733  CA  GLU C  68     3411   2531   3950    448   -628    156       C  
ATOM   2734  C   GLU C  68     -38.441   5.035   1.246  1.00 24.74           C  
ANISOU 2734  C   GLU C  68     3367   2368   3665    357   -557    244       C  
ATOM   2735  O   GLU C  68     -38.238   5.428   0.095  1.00 24.91           O  
ANISOU 2735  O   GLU C  68     3505   2339   3621    337   -609    355       O  
ATOM   2736  CB  GLU C  68     -39.999   6.355   2.711  1.00 27.25           C  
ANISOU 2736  CB  GLU C  68     3521   2576   4257    495   -634     99       C  
ATOM   2737  CG  GLU C  68     -39.870   7.692   1.948  1.00 32.69           C  
ANISOU 2737  CG  GLU C  68     4320   3100   5000    520   -725    200       C  
ATOM   2738  CD  GLU C  68     -40.978   7.940   0.917  1.00 40.77           C  
ANISOU 2738  CD  GLU C  68     5374   4065   6050    602   -891    268       C  
ATOM   2739  OE1 GLU C  68     -41.962   7.159   0.825  1.00 43.31           O  
ANISOU 2739  OE1 GLU C  68     5609   4476   6371    649   -940    220       O  
ATOM   2740  OE2 GLU C  68     -40.851   8.947   0.176  1.00 49.56           O  
ANISOU 2740  OE2 GLU C  68     6606   5038   7186    614   -982    377       O  
ATOM   2741  N   ALA C  69     -37.440   4.630   2.026  1.00 22.61           N  
ANISOU 2741  N   ALA C  69     3066   2155   3370    298   -438    194       N  
ATOM   2742  CA  ALA C  69     -36.107   4.466   1.457  1.00 21.51           C  
ANISOU 2742  CA  ALA C  69     3008   2039   3127    214   -362    255       C  
ATOM   2743  C   ALA C  69     -36.161   3.433   0.323  1.00 21.57           C  
ANISOU 2743  C   ALA C  69     3074   2125   2998    196   -376    302       C  
ATOM   2744  O   ALA C  69     -35.573   3.657  -0.741  1.00 21.03           O  
ANISOU 2744  O   ALA C  69     3110   2046   2835    145   -367    388       O  
ATOM   2745  CB  ALA C  69     -35.092   4.068   2.517  1.00 20.62           C  
ANISOU 2745  CB  ALA C  69     2830   1985   3021    168   -253    181       C  
ATOM   2746  N   ALA C  70     -36.862   2.314   0.542  1.00 20.87           N  
ANISOU 2746  N   ALA C  70     2922   2114   2891    227   -395    243       N  
ATOM   2747  CA  ALA C  70     -36.978   1.287  -0.489  1.00 21.51           C  
ANISOU 2747  CA  ALA C  70     3058   2265   2851    212   -415    268       C  
ATOM   2748  C   ALA C  70     -37.702   1.811  -1.735  1.00 23.77           C  
ANISOU 2748  C   ALA C  70     3436   2507   3091    232   -530    357       C  
ATOM   2749  O   ALA C  70     -37.298   1.488  -2.881  1.00 22.92           O  
ANISOU 2749  O   ALA C  70     3429   2432   2845    188   -527    414       O  
ATOM   2750  CB  ALA C  70     -37.675   0.024   0.046  1.00 20.39           C  
ANISOU 2750  CB  ALA C  70     2836   2197   2716    233   -424    186       C  
ATOM   2751  N   ASN C  71     -38.749   2.610  -1.512  1.00 25.80           N  
ANISOU 2751  N   ASN C  71     3656   2690   3458    299   -633    363       N  
ATOM   2752  CA  ASN C  71     -39.531   3.239  -2.610  1.00 29.54           C  
ANISOU 2752  CA  ASN C  71     4212   3101   3912    336   -777    455       C  
ATOM   2753  C   ASN C  71     -38.736   4.290  -3.408  1.00 31.02           C  
ANISOU 2753  C   ASN C  71     4546   3201   4038    285   -780    579       C  
ATOM   2754  O   ASN C  71     -38.859   4.379  -4.633  1.00 31.69           O  
ANISOU 2754  O   ASN C  71     4756   3280   4005    261   -857    678       O  
ATOM   2755  CB  ASN C  71     -40.865   3.852  -2.103  1.00 31.08           C  
ANISOU 2755  CB  ASN C  71     4307   3231   4270    438   -896    413       C  
ATOM   2756  CG  ASN C  71     -41.937   2.781  -1.767  1.00 34.84           C  
ANISOU 2756  CG  ASN C  71     4658   3804   4776    473   -929    317       C  
ATOM   2757  OD1 ASN C  71     -41.834   1.638  -2.217  1.00 37.78           O  
ANISOU 2757  OD1 ASN C  71     5054   4268   5034    426   -907    307       O  
ATOM   2758  ND2 ASN C  71     -42.974   3.160  -0.978  1.00 37.38           N  
ANISOU 2758  ND2 ASN C  71     4843   4104   5256    549   -978    236       N  
ATOM   2759  N   HIS C  72     -37.886   5.051  -2.726  1.00 31.35           N  
ANISOU 2759  N   HIS C  72     4582   3182   4147    252   -694    576       N  
ATOM   2760  CA  HIS C  72     -36.990   5.997  -3.416  1.00 32.44           C  
ANISOU 2760  CA  HIS C  72     4858   3243   4226    174   -671    693       C  
ATOM   2761  C   HIS C  72     -35.505   5.636  -3.299  1.00 30.77           C  
ANISOU 2761  C   HIS C  72     4652   3106   3932     67   -499    675       C  
ATOM   2762  O   HIS C  72     -34.657   6.490  -3.043  1.00 29.83           O  
ANISOU 2762  O   HIS C  72     4560   2921   3851      5   -436    705       O  
ATOM   2763  CB  HIS C  72     -37.245   7.404  -2.918  1.00 34.03           C  
ANISOU 2763  CB  HIS C  72     5065   3280   4583    215   -738    720       C  
ATOM   2764  CG  HIS C  72     -38.666   7.835  -3.039  1.00 38.50           C  
ANISOU 2764  CG  HIS C  72     5609   3765   5254    334   -914    728       C  
ATOM   2765  ND1 HIS C  72     -39.183   8.390  -4.190  1.00 44.55           N  
ANISOU 2765  ND1 HIS C  72     6508   4448   5972    351  -1065    860       N  
ATOM   2766  CD2 HIS C  72     -39.681   7.799  -2.147  1.00 40.85           C  
ANISOU 2766  CD2 HIS C  72     5760   4055   5705    442   -965    614       C  
ATOM   2767  CE1 HIS C  72     -40.456   8.684  -3.997  1.00 45.75           C  
ANISOU 2767  CE1 HIS C  72     6585   4538   6260    478  -1214    824       C  
ATOM   2768  NE2 HIS C  72     -40.781   8.336  -2.763  1.00 44.48           N  
ANISOU 2768  NE2 HIS C  72     6247   4427   6225    533  -1146    668       N  
ATOM   2769  N   ILE C  73     -35.215   4.371  -3.582  1.00 29.23           N  
ANISOU 2769  N   ILE C  73     4435   3044   3626     45   -433    624       N  
ATOM   2770  CA  ILE C  73     -33.915   3.757  -3.373  1.00 28.35           C  
ANISOU 2770  CA  ILE C  73     4288   3023   3459    -27   -279    571       C  
ATOM   2771  C   ILE C  73     -32.799   4.313  -4.272  1.00 30.02           C  
ANISOU 2771  C   ILE C  73     4608   3237   3561   -143   -194    656       C  
ATOM   2772  O   ILE C  73     -31.625   4.081  -3.987  1.00 28.86           O  
ANISOU 2772  O   ILE C  73     4411   3151   3404   -205    -62    607       O  
ATOM   2773  CB  ILE C  73     -34.022   2.221  -3.595  1.00 27.82           C  
ANISOU 2773  CB  ILE C  73     4184   3081   3308     -6   -253    493       C  
ATOM   2774  CG1 ILE C  73     -32.922   1.458  -2.851  1.00 27.47           C  
ANISOU 2774  CG1 ILE C  73     4045   3111   3281    -29   -124    397       C  
ATOM   2775  CG2 ILE C  73     -33.987   1.894  -5.102  1.00 28.37           C  
ANISOU 2775  CG2 ILE C  73     4381   3203   3196    -55   -265    557       C  
ATOM   2776  CD1 ILE C  73     -33.144  -0.085  -2.831  1.00 25.02           C  
ANISOU 2776  CD1 ILE C  73     3690   2889   2928      9   -120    310       C  
ATOM   2777  N   ASP C  74     -33.142   5.037  -5.345  1.00 31.61           N  
ANISOU 2777  N   ASP C  74     4955   3378   3678   -179   -269    784       N  
ATOM   2778  CA  ASP C  74     -32.110   5.682  -6.186  1.00 33.87           C  
ANISOU 2778  CA  ASP C  74     5359   3661   3851   -315   -182    880       C  
ATOM   2779  C   ASP C  74     -31.407   6.825  -5.456  1.00 34.27           C  
ANISOU 2779  C   ASP C  74     5387   3607   4026   -370   -133    901       C  
ATOM   2780  O   ASP C  74     -30.239   7.154  -5.749  1.00 34.63           O  
ANISOU 2780  O   ASP C  74     5463   3682   4015   -497     -6    930       O  
ATOM   2781  CB  ASP C  74     -32.688   6.218  -7.505  1.00 35.60           C  
ANISOU 2781  CB  ASP C  74     5763   3829   3932   -352   -292   1031       C  
ATOM   2782  CG  ASP C  74     -33.079   5.100  -8.490  1.00 38.86           C  
ANISOU 2782  CG  ASP C  74     6228   4370   4169   -344   -313   1013       C  
ATOM   2783  OD1 ASP C  74     -32.445   3.997  -8.473  1.00 39.30           O  
ANISOU 2783  OD1 ASP C  74     6209   4562   4161   -362   -187    901       O  
ATOM   2784  OD2 ASP C  74     -34.006   5.337  -9.310  1.00 43.81           O  
ANISOU 2784  OD2 ASP C  74     6971   4954   4719   -321   -464   1109       O  
ATOM   2785  N   ASP C  75     -32.128   7.415  -4.501  1.00 33.94           N  
ANISOU 2785  N   ASP C  75     5287   3450   4159   -278   -228    875       N  
ATOM   2786  CA  ASP C  75     -31.684   8.607  -3.805  1.00 34.95           C  
ANISOU 2786  CA  ASP C  75     5409   3449   4420   -315   -215    891       C  
ATOM   2787  C   ASP C  75     -32.176   8.622  -2.341  1.00 33.13           C  
ANISOU 2787  C   ASP C  75     5033   3182   4373   -207   -247    764       C  
ATOM   2788  O   ASP C  75     -33.037   9.412  -1.946  1.00 34.17           O  
ANISOU 2788  O   ASP C  75     5169   3182   4629   -129   -359    770       O  
ATOM   2789  CB  ASP C  75     -32.154   9.849  -4.595  1.00 37.19           C  
ANISOU 2789  CB  ASP C  75     5864   3566   4701   -342   -336   1051       C  
ATOM   2790  CG  ASP C  75     -31.518  11.111  -4.109  1.00 39.11           C  
ANISOU 2790  CG  ASP C  75     6137   3664   5060   -416   -311   1085       C  
ATOM   2791  OD1 ASP C  75     -30.769  11.021  -3.127  1.00 40.00           O  
ANISOU 2791  OD1 ASP C  75     6126   3816   5255   -440   -206    976       O  
ATOM   2792  OD2 ASP C  75     -31.784  12.191  -4.693  1.00 44.24           O  
ANISOU 2792  OD2 ASP C  75     6936   4151   5720   -449   -409   1222       O  
ATOM   2793  N   ILE C  76     -31.569   7.763  -1.536  1.00 31.48           N  
ANISOU 2793  N   ILE C  76     4695   3091   4175   -207   -145    645       N  
ATOM   2794  CA  ILE C  76     -31.964   7.568  -0.152  1.00 30.15           C  
ANISOU 2794  CA  ILE C  76     4394   2924   4137   -123   -158    521       C  
ATOM   2795  C   ILE C  76     -31.645   8.771   0.734  1.00 30.33           C  
ANISOU 2795  C   ILE C  76     4398   2825   4300   -144   -156    495       C  
ATOM   2796  O   ILE C  76     -32.357   9.004   1.688  1.00 27.74           O  
ANISOU 2796  O   ILE C  76     4002   2453   4086    -62   -207    414       O  
ATOM   2797  CB  ILE C  76     -31.280   6.303   0.485  1.00 28.90           C  
ANISOU 2797  CB  ILE C  76     4121   2918   3943   -128    -60    414       C  
ATOM   2798  CG1 ILE C  76     -31.621   5.020  -0.254  1.00 27.95           C  
ANISOU 2798  CG1 ILE C  76     4010   2907   3702    -98    -63    413       C  
ATOM   2799  CG2 ILE C  76     -31.727   6.123   1.940  1.00 27.58           C  
ANISOU 2799  CG2 ILE C  76     3838   2755   3886    -57    -78    299       C  
ATOM   2800  CD1 ILE C  76     -30.650   3.859   0.104  1.00 26.92           C  
ANISOU 2800  CD1 ILE C  76     3794   2903   3530   -119     38    328       C  
ATOM   2801  N   SER C  77     -30.558   9.495   0.443  1.00 32.42           N  
ANISOU 2801  N   SER C  77     4718   3047   4555   -263    -89    550       N  
ATOM   2802  CA  SER C  77     -30.247  10.741   1.178  1.00 34.75           C  
ANISOU 2802  CA  SER C  77     5014   3202   4986   -298    -98    532       C  
ATOM   2803  C   SER C  77     -31.376  11.717   1.047  1.00 35.45           C  
ANISOU 2803  C   SER C  77     5181   3117   5173   -218   -235    581       C  
ATOM   2804  O   SER C  77     -31.798  12.277   2.045  1.00 35.28           O  
ANISOU 2804  O   SER C  77     5102   3013   5291   -153   -275    490       O  
ATOM   2805  CB  SER C  77     -28.995  11.454   0.672  1.00 36.40           C  
ANISOU 2805  CB  SER C  77     5291   3373   5166   -458    -16    608       C  
ATOM   2806  OG  SER C  77     -28.159  10.530   0.016  1.00 40.84           O  
ANISOU 2806  OG  SER C  77     5833   4097   5589   -531     93    620       O  
ATOM   2807  N   THR C  78     -31.888  11.935  -0.161  1.00 36.50           N  
ANISOU 2807  N   THR C  78     5443   3191   5233   -216   -315    716       N  
ATOM   2808  CA  THR C  78     -32.952  12.919  -0.224  1.00 38.80           C  
ANISOU 2808  CA  THR C  78     5799   3299   5644   -124   -466    757       C  
ATOM   2809  C   THR C  78     -34.214  12.416   0.478  1.00 37.73           C  
ANISOU 2809  C   THR C  78     5542   3200   5594     39   -540    638       C  
ATOM   2810  O   THR C  78     -34.774  13.154   1.281  1.00 38.11           O  
ANISOU 2810  O   THR C  78     5542   3134   5804    120   -598    559       O  
ATOM   2811  CB  THR C  78     -33.225  13.519  -1.642  1.00 40.77           C  
ANISOU 2811  CB  THR C  78     6239   3436   5814   -161   -569    949       C  
ATOM   2812  OG1 THR C  78     -33.971  12.584  -2.429  1.00 44.80           O  
ANISOU 2812  OG1 THR C  78     6762   4057   6203   -100   -626    984       O  
ATOM   2813  CG2 THR C  78     -31.918  13.910  -2.317  1.00 39.72           C  
ANISOU 2813  CG2 THR C  78     6219   3299   5574   -351   -465   1060       C  
ATOM   2814  N   ALA C  79     -34.613  11.162   0.247  1.00 36.93           N  
ANISOU 2814  N   ALA C  79     5381   3260   5389     78   -525    611       N  
ATOM   2815  CA  ALA C  79     -35.901  10.620   0.780  1.00 36.44           C  
ANISOU 2815  CA  ALA C  79     5205   3245   5397    215   -595    510       C  
ATOM   2816  C   ALA C  79     -35.981  10.640   2.303  1.00 36.21           C  
ANISOU 2816  C   ALA C  79     5034   3237   5486    256   -537    344       C  
ATOM   2817  O   ALA C  79     -37.041  10.880   2.857  1.00 36.52           O  
ANISOU 2817  O   ALA C  79     4995   3238   5642    364   -603    259       O  
ATOM   2818  CB  ALA C  79     -36.126   9.212   0.304  1.00 35.06           C  
ANISOU 2818  CB  ALA C  79     4999   3240   5083    218   -571    507       C  
ATOM   2819  N   LEU C  80     -34.849  10.380   2.950  1.00 35.68           N  
ANISOU 2819  N   LEU C  80     4932   3241   5384    168   -413    295       N  
ATOM   2820  CA  LEU C  80     -34.708  10.381   4.400  1.00 35.84           C  
ANISOU 2820  CA  LEU C  80     4839   3297   5483    180   -352    146       C  
ATOM   2821  C   LEU C  80     -34.076  11.692   4.903  1.00 37.50           C  
ANISOU 2821  C   LEU C  80     5082   3362   5802    134   -343    124       C  
ATOM   2822  O   LEU C  80     -33.371  11.736   5.904  1.00 36.38           O  
ANISOU 2822  O   LEU C  80     4881   3258   5683     85   -269     31       O  
ATOM   2823  CB  LEU C  80     -33.856   9.182   4.821  1.00 34.39           C  
ANISOU 2823  CB  LEU C  80     4593   3283   5189    116   -245    105       C  
ATOM   2824  CG  LEU C  80     -34.497   7.806   4.635  1.00 33.00           C  
ANISOU 2824  CG  LEU C  80     4369   3243   4925    160   -249     92       C  
ATOM   2825  CD1 LEU C  80     -33.819   6.823   5.534  1.00 33.08           C  
ANISOU 2825  CD1 LEU C  80     4304   3383   4882    121   -164     15       C  
ATOM   2826  CD2 LEU C  80     -35.973   7.816   4.970  1.00 34.14           C  
ANISOU 2826  CD2 LEU C  80     4451   3374   5145    264   -323     30       C  
ATOM   2827  N   SER C  81     -34.382  12.764   4.192  1.00 40.38           N  
ANISOU 2827  N   SER C  81     5551   3554   6239    151   -434    213       N  
ATOM   2828  CA  SER C  81     -33.956  14.123   4.537  1.00 42.41           C  
ANISOU 2828  CA  SER C  81     5862   3629   6621    115   -452    204       C  
ATOM   2829  C   SER C  81     -33.929  14.415   6.036  1.00 42.37           C  
ANISOU 2829  C   SER C  81     5749   3628   6722    140   -407     21       C  
ATOM   2830  O   SER C  81     -32.836  14.543   6.633  1.00 41.95           O  
ANISOU 2830  O   SER C  81     5680   3602   6657     37   -324    -23       O  
ATOM   2831  CB  SER C  81     -34.877  15.125   3.803  1.00 44.51           C  
ANISOU 2831  CB  SER C  81     6227   3693   6991    199   -602    288       C  
ATOM   2832  OG  SER C  81     -36.058  14.454   3.319  1.00 43.71           O  
ANISOU 2832  OG  SER C  81     6089   3657   6862    314   -683    302       O  
ATOM   2833  N   LYS C  82     -35.127  14.456   6.631  1.00 42.79           N  
ANISOU 2833  N   LYS C  82     5720   3671   6868    271   -458    -93       N  
ATOM   2834  CA  LYS C  82     -35.334  15.070   7.949  1.00 43.62           C  
ANISOU 2834  CA  LYS C  82     5745   3731   7096    310   -437   -274       C  
ATOM   2835  C   LYS C  82     -34.959  14.157   9.113  1.00 41.16           C  
ANISOU 2835  C   LYS C  82     5324   3616   6698    267   -326   -401       C  
ATOM   2836  O   LYS C  82     -35.124  14.547  10.257  1.00 43.44           O  
ANISOU 2836  O   LYS C  82     5548   3901   7057    288   -298   -559       O  
ATOM   2837  CB  LYS C  82     -36.798  15.556   8.181  1.00 45.12           C  
ANISOU 2837  CB  LYS C  82     5875   3836   7434    471   -526   -372       C  
ATOM   2838  CG  LYS C  82     -37.609  16.179   6.979  1.00 48.29           C  
ANISOU 2838  CG  LYS C  82     6360   4068   7920    565   -679   -248       C  
ATOM   2839  CD  LYS C  82     -37.609  17.746   6.898  1.00 50.96           C  
ANISOU 2839  CD  LYS C  82     6792   4129   8442    600   -777   -243       C  
ATOM   2840  CE  LYS C  82     -38.500  18.438   7.980  1.00 53.70           C  
ANISOU 2840  CE  LYS C  82     7026   4396   8982    734   -800   -463       C  
ATOM   2841  NZ  LYS C  82     -39.952  18.800   7.593  1.00 55.23           N  
ANISOU 2841  NZ  LYS C  82     7167   4488   9329    922   -944   -495       N  
ATOM   2842  N   LEU C  83     -34.487  12.948   8.858  1.00 38.70           N  
ANISOU 2842  N   LEU C  83     4996   3473   6236    211   -269   -339       N  
ATOM   2843  CA  LEU C  83     -34.181  12.026   9.960  1.00 36.58           C  
ANISOU 2843  CA  LEU C  83     4636   3380   5884    176   -186   -443       C  
ATOM   2844  C   LEU C  83     -32.717  12.075  10.348  1.00 35.13           C  
ANISOU 2844  C   LEU C  83     4467   3226   5655     56   -126   -442       C  
ATOM   2845  O   LEU C  83     -32.342  11.598  11.412  1.00 34.08           O  
ANISOU 2845  O   LEU C  83     4272   3204   5474     23    -78   -538       O  
ATOM   2846  CB  LEU C  83     -34.611  10.585   9.628  1.00 34.69           C  
ANISOU 2846  CB  LEU C  83     4357   3301   5523    197   -170   -399       C  
ATOM   2847  CG  LEU C  83     -36.119  10.424   9.442  1.00 34.85           C  
ANISOU 2847  CG  LEU C  83     4328   3322   5590    307   -225   -430       C  
ATOM   2848  CD1 LEU C  83     -36.394   8.997   8.932  1.00 34.37           C  
ANISOU 2848  CD1 LEU C  83     4249   3405   5406    303   -215   -366       C  
ATOM   2849  CD2 LEU C  83     -36.931  10.737  10.711  1.00 32.95           C  
ANISOU 2849  CD2 LEU C  83     3989   3103   5427    360   -200   -608       C  
ATOM   2850  N   SER C  84     -31.925  12.688   9.475  1.00 35.54           N  
ANISOU 2850  N   SER C  84     4603   3177   5724    -12   -137   -332       N  
ATOM   2851  CA  SER C  84     -30.473  12.772   9.587  1.00 35.66           C  
ANISOU 2851  CA  SER C  84     4625   3218   5706   -138    -81   -313       C  
ATOM   2852  C   SER C  84     -30.067  13.814  10.629  1.00 35.44           C  
ANISOU 2852  C   SER C  84     4584   3101   5781   -179    -80   -433       C  
ATOM   2853  O   SER C  84     -29.239  13.534  11.480  1.00 35.85           O  
ANISOU 2853  O   SER C  84     4579   3247   5797   -245    -38   -509       O  
ATOM   2854  CB  SER C  84     -29.866  13.107   8.199  1.00 37.20           C  
ANISOU 2854  CB  SER C  84     4917   3340   5878   -211    -81   -151       C  
ATOM   2855  OG  SER C  84     -28.658  12.404   7.915  1.00 36.11           O  
ANISOU 2855  OG  SER C  84     4751   3325   5645   -309     -6   -109       O  
ATOM   2856  N   ASP C  85     -30.671  14.991  10.603  1.00 35.51           N  
ANISOU 2856  N   ASP C  85     4646   2927   5920   -136   -136   -460       N  
ATOM   2857  CA  ASP C  85     -30.432  15.994  11.674  1.00 36.48           C  
ANISOU 2857  CA  ASP C  85     4757   2955   6150   -163   -140   -604       C  
ATOM   2858  C   ASP C  85     -30.762  15.392  13.018  1.00 33.73           C  
ANISOU 2858  C   ASP C  85     4308   2755   5752   -125   -104   -770       C  
ATOM   2859  O   ASP C  85     -29.985  15.523  13.972  1.00 34.53           O  
ANISOU 2859  O   ASP C  85     4376   2903   5839   -200    -74   -869       O  
ATOM   2860  CB  ASP C  85     -31.271  17.299  11.473  1.00 38.69           C  
ANISOU 2860  CB  ASP C  85     5104   2999   6597    -85   -220   -629       C  
ATOM   2861  CG  ASP C  85     -31.283  18.208  12.709  1.00 42.98           C  
ANISOU 2861  CG  ASP C  85     5621   3457   7253    -82   -221   -822       C  
ATOM   2862  OD1 ASP C  85     -30.201  18.498  13.275  1.00 48.06           O  
ANISOU 2862  OD1 ASP C  85     6263   4110   7890   -201   -187   -872       O  
ATOM   2863  OD2 ASP C  85     -32.375  18.669  13.123  1.00 48.68           O  
ANISOU 2863  OD2 ASP C  85     6318   4102   8076     40   -259   -939       O  
ATOM   2864  N   LEU C  86     -31.912  14.735  13.073  1.00 30.28           N  
ANISOU 2864  N   LEU C  86     3826   2396   5284    -18   -108   -795       N  
ATOM   2865  CA  LEU C  86     -32.458  14.206  14.312  1.00 29.28           C  
ANISOU 2865  CA  LEU C  86     3614   2406   5106     17    -69   -949       C  
ATOM   2866  C   LEU C  86     -31.576  13.136  14.976  1.00 27.14           C  
ANISOU 2866  C   LEU C  86     3303   2324   4685    -68    -20   -954       C  
ATOM   2867  O   LEU C  86     -31.324  13.186  16.191  1.00 27.85           O  
ANISOU 2867  O   LEU C  86     3359   2481   4741   -107      4  -1086       O  
ATOM   2868  CB  LEU C  86     -33.866  13.627  14.058  1.00 27.82           C  
ANISOU 2868  CB  LEU C  86     3382   2274   4915    132    -80   -953       C  
ATOM   2869  CG  LEU C  86     -34.567  12.932  15.221  1.00 27.58           C  
ANISOU 2869  CG  LEU C  86     3263   2405   4811    154    -24  -1095       C  
ATOM   2870  CD1 LEU C  86     -35.131  13.945  16.270  1.00 28.72           C  
ANISOU 2870  CD1 LEU C  86     3369   2487   5058    196     -8  -1300       C  
ATOM   2871  CD2 LEU C  86     -35.692  11.998  14.724  1.00 23.34           C  
ANISOU 2871  CD2 LEU C  86     2677   1957   4233    228    -27  -1047       C  
ATOM   2872  N   HIS C  87     -31.147  12.156  14.191  1.00 24.43           N  
ANISOU 2872  N   HIS C  87     2967   2064   4252    -91    -14   -817       N  
ATOM   2873  CA  HIS C  87     -30.321  11.055  14.729  1.00 22.68           C  
ANISOU 2873  CA  HIS C  87     2707   2008   3902   -153     14   -812       C  
ATOM   2874  C   HIS C  87     -28.887  11.453  14.993  1.00 23.62           C  
ANISOU 2874  C   HIS C  87     2825   2117   4032   -257     16   -820       C  
ATOM   2875  O   HIS C  87     -28.335  11.104  16.023  1.00 24.46           O  
ANISOU 2875  O   HIS C  87     2894   2323   4078   -302     17   -896       O  
ATOM   2876  CB  HIS C  87     -30.375   9.827  13.815  1.00 20.23           C  
ANISOU 2876  CB  HIS C  87     2398   1785   3505   -131     18   -683       C  
ATOM   2877  CG  HIS C  87     -31.702   9.145  13.805  1.00 14.14           C  
ANISOU 2877  CG  HIS C  87     1606   1068   2698    -50     16   -692       C  
ATOM   2878  ND1 HIS C  87     -32.734   9.547  12.993  1.00 14.92           N  
ANISOU 2878  ND1 HIS C  87     1723   1080   2866     26    -12   -657       N  
ATOM   2879  CD2 HIS C  87     -32.179   8.103  14.521  1.00 14.96           C  
ANISOU 2879  CD2 HIS C  87     1672   1305   2708    -42     34   -731       C  
ATOM   2880  CE1 HIS C  87     -33.800   8.794  13.217  1.00 14.13           C  
ANISOU 2880  CE1 HIS C  87     1580   1064   2725     79     -6   -687       C  
ATOM   2881  NE2 HIS C  87     -33.488   7.895  14.131  1.00 16.10           N  
ANISOU 2881  NE2 HIS C  87     1799   1446   2870     32     28   -728       N  
ATOM   2882  N   ALA C  88     -28.294  12.192  14.069  1.00 25.39           N  
ANISOU 2882  N   ALA C  88     3092   2225   4332   -301     12   -739       N  
ATOM   2883  CA  ALA C  88     -26.905  12.564  14.145  1.00 27.35           C  
ANISOU 2883  CA  ALA C  88     3326   2466   4600   -414     21   -736       C  
ATOM   2884  C   ALA C  88     -26.714  13.747  15.130  1.00 29.18           C  
ANISOU 2884  C   ALA C  88     3564   2603   4921   -460      2   -873       C  
ATOM   2885  O   ALA C  88     -25.941  13.659  16.067  1.00 29.95           O  
ANISOU 2885  O   ALA C  88     3614   2778   4989   -524     -3   -959       O  
ATOM   2886  CB  ALA C  88     -26.404  12.947  12.731  1.00 28.12           C  
ANISOU 2886  CB  ALA C  88     3475   2474   4736   -464     38   -595       C  
ATOM   2887  N   GLN C  89     -27.425  14.840  14.907  1.00 30.53           N  
ANISOU 2887  N   GLN C  89     3795   2601   5204   -424    -18   -897       N  
ATOM   2888  CA  GLN C  89     -27.164  16.099  15.647  1.00 32.85           C  
ANISOU 2888  CA  GLN C  89     4110   2766   5608   -475    -39  -1023       C  
ATOM   2889  C   GLN C  89     -27.925  16.216  16.947  1.00 31.97           C  
ANISOU 2889  C   GLN C  89     3968   2693   5487   -416    -41  -1207       C  
ATOM   2890  O   GLN C  89     -27.368  16.676  17.926  1.00 32.56           O  
ANISOU 2890  O   GLN C  89     4026   2773   5570   -483    -48  -1336       O  
ATOM   2891  CB  GLN C  89     -27.476  17.294  14.767  1.00 34.58           C  
ANISOU 2891  CB  GLN C  89     4420   2751   5968   -469    -70   -960       C  
ATOM   2892  CG  GLN C  89     -26.588  17.290  13.531  1.00 40.52           C  
ANISOU 2892  CG  GLN C  89     5214   3470   6711   -565    -54   -782       C  
ATOM   2893  CD  GLN C  89     -27.361  17.343  12.208  1.00 46.43           C  
ANISOU 2893  CD  GLN C  89     6045   4123   7473   -498    -77   -627       C  
ATOM   2894  OE1 GLN C  89     -27.927  18.399  11.827  1.00 50.18           O  
ANISOU 2894  OE1 GLN C  89     6609   4390   8068   -465   -133   -605       O  
ATOM   2895  NE2 GLN C  89     -27.359  16.200  11.474  1.00 46.27           N  
ANISOU 2895  NE2 GLN C  89     6003   4247   7331   -477    -46   -516       N  
ATOM   2896  N   LYS C  90     -29.181  15.782  16.976  1.00 30.50           N  
ANISOU 2896  N   LYS C  90     3768   2546   5276   -299    -33  -1228       N  
ATOM   2897  CA  LYS C  90     -29.948  15.903  18.196  1.00 31.41           C  
ANISOU 2897  CA  LYS C  90     3847   2713   5376   -252    -15  -1415       C  
ATOM   2898  C   LYS C  90     -29.810  14.699  19.111  1.00 29.83           C  
ANISOU 2898  C   LYS C  90     3595   2741   4999   -282     16  -1453       C  
ATOM   2899  O   LYS C  90     -29.365  14.843  20.249  1.00 31.12           O  
ANISOU 2899  O   LYS C  90     3745   2970   5107   -345     20  -1581       O  
ATOM   2900  CB  LYS C  90     -31.423  16.194  17.885  1.00 32.59           C  
ANISOU 2900  CB  LYS C  90     3990   2783   5609   -117    -18  -1451       C  
ATOM   2901  CG  LYS C  90     -31.724  17.656  17.586  1.00 36.53           C  
ANISOU 2901  CG  LYS C  90     4540   3035   6303    -73    -65  -1505       C  
ATOM   2902  CD  LYS C  90     -30.886  18.223  16.439  1.00 39.86           C  
ANISOU 2902  CD  LYS C  90     5048   3298   6801   -138   -112  -1335       C  
ATOM   2903  CE  LYS C  90     -31.317  19.647  16.051  1.00 43.19           C  
ANISOU 2903  CE  LYS C  90     5542   3446   7423    -86   -177  -1363       C  
ATOM   2904  NZ  LYS C  90     -30.274  20.274  15.180  1.00 45.16           N  
ANISOU 2904  NZ  LYS C  90     5887   3547   7725   -201   -210  -1214       N  
ATOM   2905  N   LEU C  91     -30.194  13.511  18.636  1.00 27.84           N  
ANISOU 2905  N   LEU C  91     3321   2605   4651   -242     31  -1341       N  
ATOM   2906  CA  LEU C  91     -30.201  12.318  19.484  1.00 25.86           C  
ANISOU 2906  CA  LEU C  91     3038   2554   4235   -267     52  -1363       C  
ATOM   2907  C   LEU C  91     -28.795  11.791  19.808  1.00 25.29           C  
ANISOU 2907  C   LEU C  91     2961   2570   4079   -363     21  -1318       C  
ATOM   2908  O   LEU C  91     -28.595  11.102  20.796  1.00 24.36           O  
ANISOU 2908  O   LEU C  91     2832   2591   3833   -402     14  -1365       O  
ATOM   2909  CB  LEU C  91     -31.065  11.234  18.844  1.00 25.18           C  
ANISOU 2909  CB  LEU C  91     2936   2542   4089   -199     69  -1260       C  
ATOM   2910  CG  LEU C  91     -32.567  11.547  18.704  1.00 25.04           C  
ANISOU 2910  CG  LEU C  91     2894   2482   4140   -101     95  -1323       C  
ATOM   2911  CD1 LEU C  91     -33.265  10.360  18.133  1.00 24.68           C  
ANISOU 2911  CD1 LEU C  91     2827   2527   4021    -60    104  -1221       C  
ATOM   2912  CD2 LEU C  91     -33.177  11.889  20.034  1.00 24.19           C  
ANISOU 2912  CD2 LEU C  91     2754   2435   4002   -106    141  -1518       C  
ATOM   2913  N   ARG C  92     -27.830  12.161  18.976  1.00 25.69           N  
ANISOU 2913  N   ARG C  92     3018   2536   4206   -404     -1  -1229       N  
ATOM   2914  CA  ARG C  92     -26.439  11.724  19.080  1.00 26.10           C  
ANISOU 2914  CA  ARG C  92     3039   2662   4214   -487    -32  -1185       C  
ATOM   2915  C   ARG C  92     -26.357  10.213  19.263  1.00 24.99           C  
ANISOU 2915  C   ARG C  92     2875   2684   3936   -467    -45  -1118       C  
ATOM   2916  O   ARG C  92     -25.707   9.728  20.180  1.00 25.86           O  
ANISOU 2916  O   ARG C  92     2964   2900   3962   -514    -86  -1159       O  
ATOM   2917  CB  ARG C  92     -25.714  12.524  20.177  1.00 27.81           C  
ANISOU 2917  CB  ARG C  92     3248   2872   4448   -572    -62  -1325       C  
ATOM   2918  CG  ARG C  92     -25.689  14.041  19.862  1.00 30.08           C  
ANISOU 2918  CG  ARG C  92     3570   2966   4895   -600    -57  -1381       C  
ATOM   2919  CD  ARG C  92     -24.616  14.768  20.586  1.00 36.59           C  
ANISOU 2919  CD  ARG C  92     4378   3771   5755   -710    -94  -1481       C  
ATOM   2920  NE  ARG C  92     -24.557  16.217  20.311  1.00 41.79           N  
ANISOU 2920  NE  ARG C  92     5079   4225   6572   -749    -94  -1535       N  
ATOM   2921  CZ  ARG C  92     -24.113  16.790  19.182  1.00 45.00           C  
ANISOU 2921  CZ  ARG C  92     5510   4496   7093   -791    -86  -1423       C  
ATOM   2922  NH1 ARG C  92     -23.717  16.071  18.126  1.00 44.56           N  
ANISOU 2922  NH1 ARG C  92     5433   4491   7008   -794    -64  -1257       N  
ATOM   2923  NH2 ARG C  92     -24.105  18.117  19.097  1.00 49.26           N  
ANISOU 2923  NH2 ARG C  92     6105   4839   7774   -833    -99  -1480       N  
ATOM   2924  N   VAL C  93     -27.056   9.487  18.383  1.00 23.71           N  
ANISOU 2924  N   VAL C  93     2723   2531   3756   -397    -21  -1014       N  
ATOM   2925  CA  VAL C  93     -27.067   8.021  18.383  1.00 21.51           C  
ANISOU 2925  CA  VAL C  93     2433   2376   3363   -372    -35   -938       C  
ATOM   2926  C   VAL C  93     -25.689   7.516  17.957  1.00 21.30           C  
ANISOU 2926  C   VAL C  93     2366   2387   3341   -409    -67   -868       C  
ATOM   2927  O   VAL C  93     -25.182   7.896  16.918  1.00 21.14           O  
ANISOU 2927  O   VAL C  93     2333   2299   3399   -420    -44   -807       O  
ATOM   2928  CB  VAL C  93     -28.133   7.450  17.446  1.00 19.93           C  
ANISOU 2928  CB  VAL C  93     2252   2162   3158   -295     -5   -854       C  
ATOM   2929  CG1 VAL C  93     -28.066   5.957  17.417  1.00 16.40           C  
ANISOU 2929  CG1 VAL C  93     1802   1822   2608   -279    -25   -779       C  
ATOM   2930  CG2 VAL C  93     -29.563   7.871  17.895  1.00 20.35           C  
ANISOU 2930  CG2 VAL C  93     2318   2196   3219   -251     27   -937       C  
ATOM   2931  N   ASP C  94     -25.079   6.696  18.803  1.00 21.55           N  
ANISOU 2931  N   ASP C  94     2375   2525   3287   -431   -122   -882       N  
ATOM   2932  CA  ASP C  94     -23.806   6.049  18.500  1.00 21.99           C  
ANISOU 2932  CA  ASP C  94     2372   2632   3353   -445   -165   -831       C  
ATOM   2933  C   ASP C  94     -24.041   5.237  17.208  1.00 21.61           C  
ANISOU 2933  C   ASP C  94     2325   2574   3311   -382   -128   -720       C  
ATOM   2934  O   ASP C  94     -24.922   4.374  17.168  1.00 19.29           O  
ANISOU 2934  O   ASP C  94     2072   2309   2947   -329   -128   -679       O  
ATOM   2935  CB  ASP C  94     -23.423   5.116  19.659  1.00 22.56           C  
ANISOU 2935  CB  ASP C  94     2439   2813   3318   -453   -253   -851       C  
ATOM   2936  CG  ASP C  94     -21.973   4.708  19.635  1.00 25.03           C  
ANISOU 2936  CG  ASP C  94     2670   3173   3667   -470   -322   -839       C  
ATOM   2937  OD1 ASP C  94     -21.456   4.452  18.539  1.00 26.84           O  
ANISOU 2937  OD1 ASP C  94     2846   3384   3967   -444   -290   -781       O  
ATOM   2938  OD2 ASP C  94     -21.343   4.646  20.719  1.00 27.36           O  
ANISOU 2938  OD2 ASP C  94     2948   3530   3918   -509   -412   -894       O  
ATOM   2939  N   PRO C  95     -23.247   5.501  16.164  1.00 22.54           N  
ANISOU 2939  N   PRO C  95     2399   2658   3507   -399    -94   -677       N  
ATOM   2940  CA  PRO C  95     -23.339   4.760  14.880  1.00 22.75           C  
ANISOU 2940  CA  PRO C  95     2428   2686   3530   -349    -54   -585       C  
ATOM   2941  C   PRO C  95     -23.385   3.244  14.993  1.00 22.79           C  
ANISOU 2941  C   PRO C  95     2429   2769   3463   -285    -98   -550       C  
ATOM   2942  O   PRO C  95     -24.062   2.607  14.181  1.00 23.68           O  
ANISOU 2942  O   PRO C  95     2580   2871   3546   -233    -71   -489       O  
ATOM   2943  CB  PRO C  95     -22.053   5.164  14.146  1.00 23.39           C  
ANISOU 2943  CB  PRO C  95     2435   2764   3688   -406    -18   -577       C  
ATOM   2944  CG  PRO C  95     -21.683   6.454  14.770  1.00 23.77           C  
ANISOU 2944  CG  PRO C  95     2472   2760   3800   -489    -23   -646       C  
ATOM   2945  CD  PRO C  95     -22.082   6.383  16.203  1.00 21.94           C  
ANISOU 2945  CD  PRO C  95     2260   2561   3514   -480    -93   -721       C  
ATOM   2946  N   VAL C  96     -22.714   2.654  15.995  1.00 22.96           N  
ANISOU 2946  N   VAL C  96     2413   2857   3453   -289   -179   -585       N  
ATOM   2947  CA  VAL C  96     -22.793   1.194  16.175  1.00 21.70           C  
ANISOU 2947  CA  VAL C  96     2267   2748   3229   -227   -240   -543       C  
ATOM   2948  C   VAL C  96     -24.223   0.674  16.379  1.00 20.81           C  
ANISOU 2948  C   VAL C  96     2249   2627   3030   -200   -232   -509       C  
ATOM   2949  O   VAL C  96     -24.516  -0.499  16.077  1.00 19.90           O  
ANISOU 2949  O   VAL C  96     2162   2523   2876   -150   -256   -455       O  
ATOM   2950  CB  VAL C  96     -21.865   0.664  17.301  1.00 22.87           C  
ANISOU 2950  CB  VAL C  96     2376   2959   3356   -233   -355   -575       C  
ATOM   2951  CG1 VAL C  96     -20.413   1.327  17.215  1.00 24.01           C  
ANISOU 2951  CG1 VAL C  96     2399   3121   3601   -274   -367   -632       C  
ATOM   2952  CG2 VAL C  96     -22.486   0.892  18.653  1.00 23.73           C  
ANISOU 2952  CG2 VAL C  96     2555   3093   3371   -277   -402   -610       C  
ATOM   2953  N   ASN C  97     -25.151   1.494  16.855  1.00 20.80           N  
ANISOU 2953  N   ASN C  97     2291   2605   3008   -231   -197   -546       N  
ATOM   2954  CA  ASN C  97     -26.497   0.949  17.091  1.00 20.95           C  
ANISOU 2954  CA  ASN C  97     2376   2634   2949   -213   -183   -525       C  
ATOM   2955  C   ASN C  97     -27.345   0.748  15.817  1.00 20.86           C  
ANISOU 2955  C   ASN C  97     2383   2577   2964   -165   -128   -469       C  
ATOM   2956  O   ASN C  97     -28.396   0.093  15.877  1.00 20.81           O  
ANISOU 2956  O   ASN C  97     2417   2587   2904   -150   -123   -446       O  
ATOM   2957  CB  ASN C  97     -27.272   1.775  18.095  1.00 21.26           C  
ANISOU 2957  CB  ASN C  97     2441   2684   2953   -257   -160   -604       C  
ATOM   2958  CG  ASN C  97     -26.589   1.830  19.454  1.00 22.88           C  
ANISOU 2958  CG  ASN C  97     2648   2950   3094   -314   -224   -662       C  
ATOM   2959  OD1 ASN C  97     -26.070   0.839  19.970  1.00 25.45           O  
ANISOU 2959  OD1 ASN C  97     2990   3328   3351   -318   -302   -623       O  
ATOM   2960  ND2 ASN C  97     -26.605   2.999  20.043  1.00 22.75           N  
ANISOU 2960  ND2 ASN C  97     2624   2921   3100   -356   -200   -757       N  
ATOM   2961  N   PHE C  98     -26.917   1.333  14.703  1.00 20.77           N  
ANISOU 2961  N   PHE C  98     2346   2515   3029   -153    -88   -448       N  
ATOM   2962  CA  PHE C  98     -27.644   1.232  13.451  1.00 20.87           C  
ANISOU 2962  CA  PHE C  98     2387   2488   3056   -114    -47   -393       C  
ATOM   2963  C   PHE C  98     -27.570  -0.203  12.900  1.00 21.13           C  
ANISOU 2963  C   PHE C  98     2431   2553   3045    -72    -70   -340       C  
ATOM   2964  O   PHE C  98     -28.580  -0.742  12.440  1.00 21.07           O  
ANISOU 2964  O   PHE C  98     2462   2538   3005    -44    -66   -307       O  
ATOM   2965  CB  PHE C  98     -27.179   2.304  12.452  1.00 20.52           C  
ANISOU 2965  CB  PHE C  98     2332   2380   3085   -131     -1   -376       C  
ATOM   2966  CG  PHE C  98     -27.673   3.687  12.811  1.00 21.89           C  
ANISOU 2966  CG  PHE C  98     2520   2485   3314   -156     15   -419       C  
ATOM   2967  CD1 PHE C  98     -28.850   4.157  12.307  1.00 21.76           C  
ANISOU 2967  CD1 PHE C  98     2542   2408   3318   -121     26   -402       C  
ATOM   2968  CD2 PHE C  98     -26.982   4.475  13.718  1.00 25.14           C  
ANISOU 2968  CD2 PHE C  98     2901   2889   3760   -208      6   -489       C  
ATOM   2969  CE1 PHE C  98     -29.334   5.369  12.693  1.00 25.89           C  
ANISOU 2969  CE1 PHE C  98     3073   2857   3906   -126     30   -456       C  
ATOM   2970  CE2 PHE C  98     -27.434   5.727  14.102  1.00 24.69           C  
ANISOU 2970  CE2 PHE C  98     2861   2757   3762   -227     16   -546       C  
ATOM   2971  CZ  PHE C  98     -28.628   6.175  13.610  1.00 26.68           C  
ANISOU 2971  CZ  PHE C  98     3152   2941   4045   -180     29   -533       C  
ATOM   2972  N   LYS C  99     -26.410  -0.825  13.018  1.00 21.70           N  
ANISOU 2972  N   LYS C  99     2464   2657   3122    -66   -103   -342       N  
ATOM   2973  CA  LYS C  99     -26.243  -2.220  12.644  1.00 22.27           C  
ANISOU 2973  CA  LYS C  99     2548   2747   3168    -18   -139   -309       C  
ATOM   2974  C   LYS C  99     -27.098  -3.110  13.516  1.00 21.07           C  
ANISOU 2974  C   LYS C  99     2453   2609   2945    -18   -193   -292       C  
ATOM   2975  O   LYS C  99     -27.522  -4.203  13.076  1.00 22.47           O  
ANISOU 2975  O   LYS C  99     2669   2774   3094     14   -214   -255       O  
ATOM   2976  CB  LYS C  99     -24.801  -2.735  12.889  1.00 23.42           C  
ANISOU 2976  CB  LYS C  99     2626   2923   3350      1   -187   -332       C  
ATOM   2977  CG  LYS C  99     -23.623  -1.992  12.286  1.00 28.60           C  
ANISOU 2977  CG  LYS C  99     3195   3589   4081    -17   -138   -365       C  
ATOM   2978  CD  LYS C  99     -22.248  -2.526  12.909  1.00 32.82           C  
ANISOU 2978  CD  LYS C  99     3640   4168   4663      4   -213   -407       C  
ATOM   2979  CE  LYS C  99     -21.169  -1.438  13.226  1.00 36.78           C  
ANISOU 2979  CE  LYS C  99     4046   4696   5234    -58   -199   -462       C  
ATOM   2980  NZ  LYS C  99     -20.306  -1.758  14.459  1.00 38.19           N  
ANISOU 2980  NZ  LYS C  99     4167   4915   5430    -52   -318   -502       N  
ATOM   2981  N   LEU C 100     -27.243  -2.731  14.785  1.00 19.31           N  
ANISOU 2981  N   LEU C 100     2240   2412   2685    -64   -220   -321       N  
ATOM   2982  CA  LEU C 100     -27.992  -3.546  15.713  1.00 18.09           C  
ANISOU 2982  CA  LEU C 100     2147   2282   2443    -89   -263   -301       C  
ATOM   2983  C   LEU C 100     -29.445  -3.558  15.291  1.00 16.43           C  
ANISOU 2983  C   LEU C 100     1969   2063   2212    -96   -207   -289       C  
ATOM   2984  O   LEU C 100     -30.061  -4.620  15.174  1.00 16.29           O  
ANISOU 2984  O   LEU C 100     1996   2042   2151    -95   -228   -246       O  
ATOM   2985  CB  LEU C 100     -27.839  -3.082  17.164  1.00 17.78           C  
ANISOU 2985  CB  LEU C 100     2118   2290   2348   -150   -295   -343       C  
ATOM   2986  CG  LEU C 100     -26.395  -2.916  17.630  1.00 18.21           C  
ANISOU 2986  CG  LEU C 100     2126   2359   2432   -149   -364   -366       C  
ATOM   2987  CD1 LEU C 100     -26.252  -2.588  19.157  1.00 14.98           C  
ANISOU 2987  CD1 LEU C 100     1746   2006   1940   -217   -417   -407       C  
ATOM   2988  CD2 LEU C 100     -25.622  -4.125  17.282  1.00 16.61           C  
ANISOU 2988  CD2 LEU C 100     1919   2141   2250    -91   -442   -317       C  
ATOM   2989  N   LEU C 101     -29.979  -2.393  14.986  1.00 15.61           N  
ANISOU 2989  N   LEU C 101     1838   1945   2150    -99   -144   -327       N  
ATOM   2990  CA  LEU C 101     -31.365  -2.286  14.613  1.00 15.35           C  
ANISOU 2990  CA  LEU C 101     1813   1905   2114    -95   -102   -329       C  
ATOM   2991  C   LEU C 101     -31.548  -3.048  13.286  1.00 15.86           C  
ANISOU 2991  C   LEU C 101     1894   1937   2194    -50   -109   -271       C  
ATOM   2992  O   LEU C 101     -32.566  -3.696  13.054  1.00 16.29           O  
ANISOU 2992  O   LEU C 101     1969   1999   2223    -53   -110   -252       O  
ATOM   2993  CB  LEU C 101     -31.765  -0.822  14.504  1.00 13.64           C  
ANISOU 2993  CB  LEU C 101     1562   1659   1963    -89    -53   -384       C  
ATOM   2994  CG  LEU C 101     -33.248  -0.602  14.238  1.00 13.84           C  
ANISOU 2994  CG  LEU C 101     1574   1679   2003    -74    -22   -404       C  
ATOM   2995  CD1 LEU C 101     -33.674   0.788  14.697  1.00 11.15           C  
ANISOU 2995  CD1 LEU C 101     1198   1316   1724    -72     14   -488       C  
ATOM   2996  CD2 LEU C 101     -33.646  -0.852  12.783  1.00  9.94           C  
ANISOU 2996  CD2 LEU C 101     1089   1143   1544    -24    -31   -344       C  
ATOM   2997  N   GLY C 102     -30.546  -2.977  12.416  1.00 16.30           N  
ANISOU 2997  N   GLY C 102     1937   1965   2290    -15   -110   -251       N  
ATOM   2998  CA  GLY C 102     -30.676  -3.572  11.072  1.00 16.55           C  
ANISOU 2998  CA  GLY C 102     1989   1974   2326     25   -106   -212       C  
ATOM   2999  C   GLY C 102     -30.644  -5.084  11.208  1.00 16.73           C  
ANISOU 2999  C   GLY C 102     2047   2003   2308     34   -156   -188       C  
ATOM   3000  O   GLY C 102     -31.399  -5.816  10.541  1.00 16.22           O  
ANISOU 3000  O   GLY C 102     2015   1924   2223     46   -165   -166       O  
ATOM   3001  N   GLN C 103     -29.747  -5.534  12.080  1.00 16.13           N  
ANISOU 3001  N   GLN C 103     1966   1939   2224     29   -201   -193       N  
ATOM   3002  CA  GLN C 103     -29.636  -6.940  12.414  1.00 17.11           C  
ANISOU 3002  CA  GLN C 103     2136   2048   2316     38   -270   -165       C  
ATOM   3003  C   GLN C 103     -30.978  -7.440  12.969  1.00 16.51           C  
ANISOU 3003  C   GLN C 103     2114   1980   2179    -18   -277   -140       C  
ATOM   3004  O   GLN C 103     -31.425  -8.539  12.623  1.00 15.84           O  
ANISOU 3004  O   GLN C 103     2078   1864   2077    -17   -309   -110       O  
ATOM   3005  CB  GLN C 103     -28.430  -7.147  13.370  1.00 17.37           C  
ANISOU 3005  CB  GLN C 103     2152   2092   2357     43   -337   -172       C  
ATOM   3006  CG  GLN C 103     -28.357  -8.447  14.112  1.00 21.82           C  
ANISOU 3006  CG  GLN C 103     2780   2629   2880     40   -434   -130       C  
ATOM   3007  CD  GLN C 103     -27.939  -9.682  13.252  1.00 25.79           C  
ANISOU 3007  CD  GLN C 103     3303   3070   3428    113   -482   -118       C  
ATOM   3008  OE1 GLN C 103     -28.016 -10.822  13.728  1.00 28.98           O  
ANISOU 3008  OE1 GLN C 103     3777   3426   3809    113   -569    -76       O  
ATOM   3009  NE2 GLN C 103     -27.475  -9.450  12.020  1.00 24.03           N  
ANISOU 3009  NE2 GLN C 103     3023   2844   3263    170   -426   -159       N  
ATOM   3010  N   CYS C 104     -31.665  -6.623  13.776  1.00 16.68           N  
ANISOU 3010  N   CYS C 104     2122   2044   2172    -72   -239   -164       N  
ATOM   3011  CA  CYS C 104     -32.914  -7.090  14.377  1.00 16.10           C  
ANISOU 3011  CA  CYS C 104     2083   1998   2037   -140   -229   -153       C  
ATOM   3012  C   CYS C 104     -34.023  -7.154  13.349  1.00 15.88           C  
ANISOU 3012  C   CYS C 104     2039   1958   2036   -128   -196   -155       C  
ATOM   3013  O   CYS C 104     -34.879  -8.049  13.412  1.00 16.43           O  
ANISOU 3013  O   CYS C 104     2142   2030   2072   -173   -207   -131       O  
ATOM   3014  CB  CYS C 104     -33.343  -6.219  15.550  1.00 17.24           C  
ANISOU 3014  CB  CYS C 104     2206   2204   2140   -202   -186   -201       C  
ATOM   3015  SG  CYS C 104     -32.344  -6.473  17.049  1.00 16.67           S  
ANISOU 3015  SG  CYS C 104     2183   2163   1986   -252   -249   -189       S  
ATOM   3016  N   PHE C 105     -34.019  -6.196  12.416  1.00 14.65           N  
ANISOU 3016  N   PHE C 105     1837   1788   1941    -75   -161   -178       N  
ATOM   3017  CA  PHE C 105     -34.929  -6.186  11.275  1.00 13.30           C  
ANISOU 3017  CA  PHE C 105     1655   1602   1797    -49   -152   -174       C  
ATOM   3018  C   PHE C 105     -34.851  -7.460  10.387  1.00 12.99           C  
ANISOU 3018  C   PHE C 105     1666   1528   1742    -32   -195   -138       C  
ATOM   3019  O   PHE C 105     -35.871  -8.074  10.029  1.00 13.99           O  
ANISOU 3019  O   PHE C 105     1804   1655   1858    -56   -209   -132       O  
ATOM   3020  CB  PHE C 105     -34.622  -4.984  10.404  1.00 12.90           C  
ANISOU 3020  CB  PHE C 105     1574   1527   1802      4   -127   -184       C  
ATOM   3021  CG  PHE C 105     -35.595  -4.787   9.309  1.00 12.91           C  
ANISOU 3021  CG  PHE C 105     1568   1514   1824     30   -134   -176       C  
ATOM   3022  CD1 PHE C 105     -36.909  -4.484   9.592  1.00 16.89           C  
ANISOU 3022  CD1 PHE C 105     2028   2042   2349     15   -129   -206       C  
ATOM   3023  CD2 PHE C 105     -35.225  -4.936   8.000  1.00 14.93           C  
ANISOU 3023  CD2 PHE C 105     1856   1741   2074     68   -149   -144       C  
ATOM   3024  CE1 PHE C 105     -37.823  -4.321   8.576  1.00 16.19           C  
ANISOU 3024  CE1 PHE C 105     1923   1940   2287     46   -157   -199       C  
ATOM   3025  CE2 PHE C 105     -36.164  -4.792   6.969  1.00 14.53           C  
ANISOU 3025  CE2 PHE C 105     1810   1681   2028     89   -174   -131       C  
ATOM   3026  CZ  PHE C 105     -37.433  -4.488   7.276  1.00 14.17           C  
ANISOU 3026  CZ  PHE C 105     1717   1651   2015     82   -187   -155       C  
ATOM   3027  N   LEU C 106     -33.643  -7.843  10.019  1.00 12.70           N  
ANISOU 3027  N   LEU C 106     1651   1461   1712     10   -216   -127       N  
ATOM   3028  CA  LEU C 106     -33.428  -9.068   9.245  1.00 12.15           C  
ANISOU 3028  CA  LEU C 106     1630   1351   1636     37   -256   -115       C  
ATOM   3029  C   LEU C 106     -33.845 -10.345  10.001  1.00 12.96           C  
ANISOU 3029  C   LEU C 106     1789   1427   1707    -13   -310    -88       C  
ATOM   3030  O   LEU C 106     -34.375 -11.270   9.384  1.00 13.24           O  
ANISOU 3030  O   LEU C 106     1866   1429   1737    -20   -339    -83       O  
ATOM   3031  CB  LEU C 106     -31.980  -9.137   8.833  1.00 12.05           C  
ANISOU 3031  CB  LEU C 106     1607   1321   1650     96   -257   -129       C  
ATOM   3032  CG  LEU C 106     -31.573  -8.029   7.870  1.00 12.30           C  
ANISOU 3032  CG  LEU C 106     1601   1372   1700    125   -197   -145       C  
ATOM   3033  CD1 LEU C 106     -30.131  -8.224   7.406  1.00 14.21           C  
ANISOU 3033  CD1 LEU C 106     1817   1612   1968    172   -183   -172       C  
ATOM   3034  CD2 LEU C 106     -32.461  -7.949   6.670  1.00  9.58           C  
ANISOU 3034  CD2 LEU C 106     1282   1027   1333    129   -185   -138       C  
ATOM   3035  N   VAL C 107     -33.647 -10.395  11.329  1.00 13.03           N  
ANISOU 3035  N   VAL C 107     1811   1452   1689    -59   -327    -70       N  
ATOM   3036  CA  VAL C 107     -34.162 -11.535  12.130  1.00 13.29           C  
ANISOU 3036  CA  VAL C 107     1915   1461   1674   -132   -376    -27       C  
ATOM   3037  C   VAL C 107     -35.679 -11.575  11.988  1.00 13.63           C  
ANISOU 3037  C   VAL C 107     1946   1537   1698   -205   -338    -32       C  
ATOM   3038  O   VAL C 107     -36.226 -12.630  11.707  1.00 13.19           O  
ANISOU 3038  O   VAL C 107     1941   1437   1633   -243   -373    -10       O  
ATOM   3039  CB  VAL C 107     -33.789 -11.422  13.628  1.00 14.29           C  
ANISOU 3039  CB  VAL C 107     2066   1617   1747   -188   -397     -1       C  
ATOM   3040  CG1 VAL C 107     -34.711 -12.267  14.472  1.00 13.06           C  
ANISOU 3040  CG1 VAL C 107     1982   1463   1518   -302   -413     47       C  
ATOM   3041  CG2 VAL C 107     -32.316 -11.795  13.824  1.00 12.56           C  
ANISOU 3041  CG2 VAL C 107     1868   1350   1555   -119   -474     13       C  
ATOM   3042  N   VAL C 108     -36.370 -10.417  12.102  1.00 14.19           N  
ANISOU 3042  N   VAL C 108     1940   1677   1775   -219   -269    -72       N  
ATOM   3043  CA  VAL C 108     -37.873 -10.415  11.916  1.00 14.01           C  
ANISOU 3043  CA  VAL C 108     1876   1695   1754   -278   -236    -93       C  
ATOM   3044  C   VAL C 108     -38.303 -10.917  10.549  1.00 14.33           C  
ANISOU 3044  C   VAL C 108     1920   1695   1828   -243   -269    -95       C  
ATOM   3045  O   VAL C 108     -39.232 -11.704  10.415  1.00 16.11           O  
ANISOU 3045  O   VAL C 108     2157   1919   2046   -308   -285    -90       O  
ATOM   3046  CB  VAL C 108     -38.494  -9.046  12.184  1.00 14.12           C  
ANISOU 3046  CB  VAL C 108     1794   1777   1794   -272   -169   -151       C  
ATOM   3047  CG1 VAL C 108     -40.026  -9.048  11.851  1.00 11.71           C  
ANISOU 3047  CG1 VAL C 108     1418   1515   1515   -313   -146   -187       C  
ATOM   3048  CG2 VAL C 108     -38.214  -8.690  13.674  1.00 11.83           C  
ANISOU 3048  CG2 VAL C 108     1508   1538   1449   -331   -131   -164       C  
ATOM   3049  N   VAL C 109     -37.630 -10.478   9.511  1.00 14.88           N  
ANISOU 3049  N   VAL C 109     1986   1737   1929   -151   -279   -104       N  
ATOM   3050  CA  VAL C 109     -38.034 -10.934   8.172  1.00 14.63           C  
ANISOU 3050  CA  VAL C 109     1971   1678   1909   -123   -312   -112       C  
ATOM   3051  C   VAL C 109     -37.805 -12.417   8.006  1.00 15.43           C  
ANISOU 3051  C   VAL C 109     2155   1714   1994   -145   -366    -96       C  
ATOM   3052  O   VAL C 109     -38.639 -13.115   7.430  1.00 17.22           O  
ANISOU 3052  O   VAL C 109     2399   1925   2219   -181   -398   -105       O  
ATOM   3053  CB  VAL C 109     -37.261 -10.181   7.139  1.00 14.72           C  
ANISOU 3053  CB  VAL C 109     1978   1681   1934    -36   -302   -121       C  
ATOM   3054  CG1 VAL C 109     -37.505 -10.736   5.788  1.00 12.29           C  
ANISOU 3054  CG1 VAL C 109     1707   1351   1611    -12   -338   -131       C  
ATOM   3055  CG2 VAL C 109     -37.672  -8.647   7.220  1.00 11.55           C  
ANISOU 3055  CG2 VAL C 109     1504   1322   1563    -17   -263   -132       C  
ATOM   3056  N   ALA C 110     -36.672 -12.893   8.523  1.00 14.12           N  
ANISOU 3056  N   ALA C 110     2038   1503   1824   -121   -387    -76       N  
ATOM   3057  CA  ALA C 110     -36.273 -14.270   8.404  1.00 13.71           C  
ANISOU 3057  CA  ALA C 110     2070   1365   1775   -119   -452    -64       C  
ATOM   3058  C   ALA C 110     -37.263 -15.138   9.094  1.00 13.76           C  
ANISOU 3058  C   ALA C 110     2121   1349   1758   -232   -480    -29       C  
ATOM   3059  O   ALA C 110     -37.675 -16.129   8.533  1.00 15.57           O  
ANISOU 3059  O   ALA C 110     2402   1517   1997   -257   -525    -35       O  
ATOM   3060  CB  ALA C 110     -34.836 -14.509   8.967  1.00 12.91           C  
ANISOU 3060  CB  ALA C 110     1996   1219   1690    -60   -483    -51       C  
ATOM   3061  N   ILE C 111     -37.635 -14.779  10.310  1.00 14.08           N  
ANISOU 3061  N   ILE C 111     2144   1442   1764   -311   -449      2       N  
ATOM   3062  CA  ILE C 111     -38.640 -15.524  11.065  1.00 14.48           C  
ANISOU 3062  CA  ILE C 111     2233   1493   1777   -448   -454     39       C  
ATOM   3063  C   ILE C 111     -39.930 -15.722  10.269  1.00 15.10           C  
ANISOU 3063  C   ILE C 111     2266   1593   1876   -500   -442      3       C  
ATOM   3064  O   ILE C 111     -40.474 -16.778  10.252  1.00 15.42           O  
ANISOU 3064  O   ILE C 111     2364   1581   1912   -584   -481     24       O  
ATOM   3065  CB  ILE C 111     -38.997 -14.827  12.374  1.00 14.63           C  
ANISOU 3065  CB  ILE C 111     2213   1604   1740   -529   -391     52       C  
ATOM   3066  CG1 ILE C 111     -37.872 -15.042  13.388  1.00 14.98           C  
ANISOU 3066  CG1 ILE C 111     2336   1614   1742   -523   -434    106       C  
ATOM   3067  CG2 ILE C 111     -40.311 -15.377  12.945  1.00 12.59           C  
ANISOU 3067  CG2 ILE C 111     1957   1385   1442   -688   -359     68       C  
ATOM   3068  CD1 ILE C 111     -37.902 -14.147  14.599  1.00 12.70           C  
ANISOU 3068  CD1 ILE C 111     2013   1423   1389   -575   -373    102       C  
ATOM   3069  N   HIS C 112     -40.390 -14.700   9.577  1.00 15.35           N  
ANISOU 3069  N   HIS C 112     2199   1697   1936   -448   -402    -49       N  
ATOM   3070  CA  HIS C 112     -41.730 -14.728   9.006  1.00 15.60           C  
ANISOU 3070  CA  HIS C 112     2164   1773   1992   -502   -397    -86       C  
ATOM   3071  C   HIS C 112     -41.688 -15.144   7.564  1.00 15.63           C  
ANISOU 3071  C   HIS C 112     2196   1724   2018   -439   -459   -113       C  
ATOM   3072  O   HIS C 112     -42.693 -15.535   7.027  1.00 16.69           O  
ANISOU 3072  O   HIS C 112     2304   1870   2169   -493   -486   -139       O  
ATOM   3073  CB  HIS C 112     -42.338 -13.315   9.099  1.00 15.73           C  
ANISOU 3073  CB  HIS C 112     2051   1892   2034   -472   -336   -131       C  
ATOM   3074  CG  HIS C 112     -42.787 -12.942  10.484  1.00 16.65           C  
ANISOU 3074  CG  HIS C 112     2117   2085   2125   -560   -262   -136       C  
ATOM   3075  ND1 HIS C 112     -42.008 -12.206  11.347  1.00 18.13           N  
ANISOU 3075  ND1 HIS C 112     2309   2294   2285   -530   -219   -129       N  
ATOM   3076  CD2 HIS C 112     -43.929 -13.216  11.150  1.00 18.37           C  
ANISOU 3076  CD2 HIS C 112     2278   2371   2333   -686   -216   -155       C  
ATOM   3077  CE1 HIS C 112     -42.651 -12.034  12.483  1.00 15.73           C  
ANISOU 3077  CE1 HIS C 112     1961   2069   1945   -630   -151   -148       C  
ATOM   3078  NE2 HIS C 112     -43.820 -12.644  12.389  1.00 22.84           N  
ANISOU 3078  NE2 HIS C 112     2821   3003   2855   -729   -140   -164       N  
ATOM   3079  N   HIS C 113     -40.550 -14.992   6.911  1.00 14.31           N  
ANISOU 3079  N   HIS C 113     2074   1514   1850   -329   -475   -116       N  
ATOM   3080  CA  HIS C 113     -40.501 -15.224   5.500  1.00 15.07           C  
ANISOU 3080  CA  HIS C 113     2196   1583   1948   -270   -517   -154       C  
ATOM   3081  C   HIS C 113     -39.338 -16.171   5.176  1.00 14.96           C  
ANISOU 3081  C   HIS C 113     2282   1472   1931   -216   -552   -160       C  
ATOM   3082  O   HIS C 113     -38.359 -15.753   4.569  1.00 14.62           O  
ANISOU 3082  O   HIS C 113     2243   1429   1881   -121   -534   -182       O  
ATOM   3083  CB  HIS C 113     -40.395 -13.884   4.767  1.00 13.96           C  
ANISOU 3083  CB  HIS C 113     1993   1506   1806   -187   -489   -170       C  
ATOM   3084  CG  HIS C 113     -41.606 -13.007   4.949  1.00 16.38           C  
ANISOU 3084  CG  HIS C 113     2195   1889   2138   -218   -476   -178       C  
ATOM   3085  ND1 HIS C 113     -42.656 -13.005   4.058  1.00 13.71           N  
ANISOU 3085  ND1 HIS C 113     1819   1578   1810   -230   -527   -206       N  
ATOM   3086  CD2 HIS C 113     -41.936 -12.112   5.925  1.00 15.98           C  
ANISOU 3086  CD2 HIS C 113     2063   1894   2113   -234   -423   -176       C  
ATOM   3087  CE1 HIS C 113     -43.589 -12.174   4.488  1.00 17.43           C  
ANISOU 3087  CE1 HIS C 113     2181   2117   2327   -246   -510   -220       C  
ATOM   3088  NE2 HIS C 113     -43.176 -11.617   5.615  1.00 17.74           N  
ANISOU 3088  NE2 HIS C 113     2193   2174   2375   -248   -440   -207       N  
ATOM   3089  N   PRO C 114     -39.443 -17.448   5.580  1.00 15.63           N  
ANISOU 3089  N   PRO C 114     2444   1470   2027   -280   -602   -146       N  
ATOM   3090  CA  PRO C 114     -38.294 -18.319   5.315  1.00 16.64           C  
ANISOU 3090  CA  PRO C 114     2658   1493   2173   -207   -645   -164       C  
ATOM   3091  C   PRO C 114     -38.103 -18.444   3.796  1.00 17.03           C  
ANISOU 3091  C   PRO C 114     2721   1536   2212   -135   -655   -244       C  
ATOM   3092  O   PRO C 114     -39.085 -18.475   3.045  1.00 19.03           O  
ANISOU 3092  O   PRO C 114     2964   1820   2445   -179   -673   -272       O  
ATOM   3093  CB  PRO C 114     -38.682 -19.664   5.982  1.00 17.15           C  
ANISOU 3093  CB  PRO C 114     2813   1447   2256   -304   -712   -128       C  
ATOM   3094  CG  PRO C 114     -40.168 -19.597   6.117  1.00 17.88           C  
ANISOU 3094  CG  PRO C 114     2861   1600   2332   -434   -698   -116       C  
ATOM   3095  CD  PRO C 114     -40.447 -18.118   6.411  1.00 16.60           C  
ANISOU 3095  CD  PRO C 114     2581   1578   2150   -417   -619   -110       C  
ATOM   3096  N   SER C 115     -36.852 -18.423   3.373  1.00 17.23           N  
ANISOU 3096  N   SER C 115     2761   1539   2246    -29   -639   -282       N  
ATOM   3097  CA  SER C 115     -36.440 -18.622   2.021  1.00 18.09           C  
ANISOU 3097  CA  SER C 115     2894   1646   2332     40   -633   -367       C  
ATOM   3098  C   SER C 115     -36.542 -17.334   1.232  1.00 17.73           C  
ANISOU 3098  C   SER C 115     2791   1720   2228     64   -571   -371       C  
ATOM   3099  O   SER C 115     -36.250 -17.325   0.052  1.00 20.64           O  
ANISOU 3099  O   SER C 115     3183   2111   2548    105   -555   -433       O  
ATOM   3100  CB  SER C 115     -37.271 -19.689   1.312  1.00 18.92           C  
ANISOU 3100  CB  SER C 115     3069   1689   2432    -12   -699   -418       C  
ATOM   3101  OG  SER C 115     -38.345 -19.099   0.542  1.00 21.37           O  
ANISOU 3101  OG  SER C 115     3346   2087   2686    -60   -698   -425       O  
ATOM   3102  N   LEU C 116     -36.955 -16.243   1.848  1.00 17.46           N  
ANISOU 3102  N   LEU C 116     2688   1755   2190     35   -539   -307       N  
ATOM   3103  CA  LEU C 116     -36.944 -14.931   1.171  1.00 16.24           C  
ANISOU 3103  CA  LEU C 116     2488   1690   1992     64   -491   -296       C  
ATOM   3104  C   LEU C 116     -35.529 -14.385   1.204  1.00 15.47           C  
ANISOU 3104  C   LEU C 116     2371   1607   1898    134   -424   -303       C  
ATOM   3105  O   LEU C 116     -35.039 -13.854   0.162  1.00 14.51           O  
ANISOU 3105  O   LEU C 116     2258   1531   1723    168   -380   -329       O  
ATOM   3106  CB  LEU C 116     -37.833 -13.907   1.899  1.00 16.04           C  
ANISOU 3106  CB  LEU C 116     2390   1719   1986     21   -482   -238       C  
ATOM   3107  CG  LEU C 116     -37.866 -12.531   1.225  1.00 16.27           C  
ANISOU 3107  CG  LEU C 116     2385   1813   1984     55   -453   -218       C  
ATOM   3108  CD1 LEU C 116     -38.304 -12.619  -0.279  1.00 11.38           C  
ANISOU 3108  CD1 LEU C 116     1815   1215   1295     62   -494   -244       C  
ATOM   3109  CD2 LEU C 116     -38.806 -11.649   2.052  1.00 15.29           C  
ANISOU 3109  CD2 LEU C 116     2182   1724   1904     23   -453   -181       C  
ATOM   3110  N   LEU C 117     -34.888 -14.433   2.390  1.00 13.54           N  
ANISOU 3110  N   LEU C 117     2101   1336   1708    143   -415   -277       N  
ATOM   3111  CA  LEU C 117     -33.512 -13.919   2.474  1.00 12.67           C  
ANISOU 3111  CA  LEU C 117     1954   1246   1616    205   -358   -292       C  
ATOM   3112  C   LEU C 117     -32.540 -14.976   2.090  1.00 13.21           C  
ANISOU 3112  C   LEU C 117     2050   1260   1710    268   -369   -364       C  
ATOM   3113  O   LEU C 117     -31.875 -15.564   2.940  1.00 14.43           O  
ANISOU 3113  O   LEU C 117     2199   1357   1926    298   -404   -365       O  
ATOM   3114  CB  LEU C 117     -33.152 -13.351   3.827  1.00 11.59           C  
ANISOU 3114  CB  LEU C 117     1766   1116   1520    194   -350   -243       C  
ATOM   3115  CG  LEU C 117     -34.037 -12.224   4.362  1.00 14.15           C  
ANISOU 3115  CG  LEU C 117     2050   1491   1834    141   -331   -191       C  
ATOM   3116  CD1 LEU C 117     -33.600 -11.903   5.772  1.00 12.70           C  
ANISOU 3116  CD1 LEU C 117     1832   1310   1682    126   -329   -161       C  
ATOM   3117  CD2 LEU C 117     -34.066 -10.934   3.439  1.00 10.46           C  
ANISOU 3117  CD2 LEU C 117     1557   1081   1338    155   -279   -185       C  
ATOM   3118  N   THR C 118     -32.423 -15.211   0.781  1.00 12.95           N  
ANISOU 3118  N   THR C 118     2047   1245   1627    292   -342   -432       N  
ATOM   3119  CA  THR C 118     -31.396 -16.092   0.264  1.00 13.85           C  
ANISOU 3119  CA  THR C 118     2171   1322   1767    365   -330   -530       C  
ATOM   3120  C   THR C 118     -30.046 -15.439   0.597  1.00 14.54           C  
ANISOU 3120  C   THR C 118     2172   1454   1897    417   -262   -544       C  
ATOM   3121  O   THR C 118     -30.040 -14.281   1.011  1.00 16.46           O  
ANISOU 3121  O   THR C 118     2369   1757   2128    382   -223   -476       O  
ATOM   3122  CB  THR C 118     -31.523 -16.226  -1.305  1.00 14.96           C  
ANISOU 3122  CB  THR C 118     2359   1509   1817    368   -288   -610       C  
ATOM   3123  OG1 THR C 118     -31.455 -14.913  -1.870  1.00 14.56           O  
ANISOU 3123  OG1 THR C 118     2282   1562   1688    339   -211   -570       O  
ATOM   3124  CG2 THR C 118     -32.831 -16.890  -1.741  1.00 12.21           C  
ANISOU 3124  CG2 THR C 118     2090   1121   1427    315   -365   -612       C  
ATOM   3125  N   PRO C 119     -28.894 -16.125   0.383  1.00 14.83           N  
ANISOU 3125  N   PRO C 119     2177   1466   1991    499   -246   -641       N  
ATOM   3126  CA  PRO C 119     -27.646 -15.384   0.625  1.00 15.41           C  
ANISOU 3126  CA  PRO C 119     2147   1604   2106    535   -174   -659       C  
ATOM   3127  C   PRO C 119     -27.495 -14.071  -0.181  1.00 17.21           C  
ANISOU 3127  C   PRO C 119     2344   1950   2246    483    -57   -642       C  
ATOM   3128  O   PRO C 119     -27.122 -13.026   0.381  1.00 16.20           O  
ANISOU 3128  O   PRO C 119     2154   1865   2135    454    -22   -585       O  
ATOM   3129  CB  PRO C 119     -26.545 -16.402   0.268  1.00 16.75           C  
ANISOU 3129  CB  PRO C 119     2277   1736   2351    638   -170   -792       C  
ATOM   3130  CG  PRO C 119     -27.208 -17.761   0.481  1.00 16.75           C  
ANISOU 3130  CG  PRO C 119     2371   1602   2390    663   -288   -806       C  
ATOM   3131  CD  PRO C 119     -28.672 -17.577   0.214  1.00 14.58           C  
ANISOU 3131  CD  PRO C 119     2189   1331   2019    565   -310   -730       C  
ATOM   3132  N   GLU C 120     -27.773 -14.128  -1.473  1.00 18.87           N  
ANISOU 3132  N   GLU C 120     2608   2204   2358    463     -4   -689       N  
ATOM   3133  CA  GLU C 120     -27.682 -12.956  -2.329  1.00 20.53           C  
ANISOU 3133  CA  GLU C 120     2820   2516   2466    402     96   -659       C  
ATOM   3134  C   GLU C 120     -28.587 -11.807  -1.838  1.00 19.81           C  
ANISOU 3134  C   GLU C 120     2749   2427   2351    334     63   -524       C  
ATOM   3135  O   GLU C 120     -28.128 -10.673  -1.724  1.00 20.98           O  
ANISOU 3135  O   GLU C 120     2854   2622   2496    298    124   -476       O  
ATOM   3136  CB  GLU C 120     -28.082 -13.300  -3.772  1.00 21.27           C  
ANISOU 3136  CB  GLU C 120     3000   2651   2432    381    129   -717       C  
ATOM   3137  CG  GLU C 120     -27.268 -14.416  -4.447  1.00 27.10           C  
ANISOU 3137  CG  GLU C 120     3726   3393   3180    448    176   -879       C  
ATOM   3138  CD  GLU C 120     -27.940 -15.848  -4.407  1.00 31.65           C  
ANISOU 3138  CD  GLU C 120     4371   3860   3794    495     66   -942       C  
ATOM   3139  OE1 GLU C 120     -27.998 -16.423  -5.520  1.00 37.07           O  
ANISOU 3139  OE1 GLU C 120     5117   4572   4397    499     97  -1046       O  
ATOM   3140  OE2 GLU C 120     -28.367 -16.389  -3.314  1.00 25.00           O  
ANISOU 3140  OE2 GLU C 120     3532   2912   3056    518    -45   -892       O  
ATOM   3141  N   VAL C 121     -29.873 -12.103  -1.603  1.00 19.41           N  
ANISOU 3141  N   VAL C 121     2759   2326   2288    314    -30   -473       N  
ATOM   3142  CA  VAL C 121     -30.875 -11.129  -1.159  1.00 17.81           C  
ANISOU 3142  CA  VAL C 121     2566   2124   2078    263    -69   -368       C  
ATOM   3143  C   VAL C 121     -30.498 -10.593   0.194  1.00 17.63           C  
ANISOU 3143  C   VAL C 121     2470   2083   2144    265    -71   -326       C  
ATOM   3144  O   VAL C 121     -30.631  -9.420   0.431  1.00 17.98           O  
ANISOU 3144  O   VAL C 121     2494   2148   2190    232    -50   -266       O  
ATOM   3145  CB  VAL C 121     -32.300 -11.747  -1.085  1.00 17.93           C  
ANISOU 3145  CB  VAL C 121     2633   2095   2082    242   -167   -347       C  
ATOM   3146  CG1 VAL C 121     -33.328 -10.762  -0.472  1.00 14.76           C  
ANISOU 3146  CG1 VAL C 121     2211   1697   1700    203   -204   -259       C  
ATOM   3147  CG2 VAL C 121     -32.767 -12.166  -2.483  1.00 18.88           C  
ANISOU 3147  CG2 VAL C 121     2833   2241   2102    231   -178   -388       C  
ATOM   3148  N   HIS C 122     -30.001 -11.446   1.069  1.00 17.37           N  
ANISOU 3148  N   HIS C 122     2407   2006   2187    304   -106   -360       N  
ATOM   3149  CA  HIS C 122     -29.404 -11.016   2.354  1.00 17.43           C  
ANISOU 3149  CA  HIS C 122     2347   2006   2269    308   -113   -333       C  
ATOM   3150  C   HIS C 122     -28.275  -9.992   2.113  1.00 18.08           C  
ANISOU 3150  C   HIS C 122     2361   2148   2361    304    -23   -345       C  
ATOM   3151  O   HIS C 122     -28.237  -8.947   2.756  1.00 19.07           O  
ANISOU 3151  O   HIS C 122     2451   2287   2507    269    -10   -297       O  
ATOM   3152  CB  HIS C 122     -28.888 -12.297   3.067  1.00 17.62           C  
ANISOU 3152  CB  HIS C 122     2366   1967   2362    361   -180   -374       C  
ATOM   3153  CG  HIS C 122     -28.312 -12.097   4.442  1.00 17.26           C  
ANISOU 3153  CG  HIS C 122     2269   1909   2381    367   -217   -345       C  
ATOM   3154  ND1 HIS C 122     -28.076 -13.158   5.296  1.00 14.32           N  
ANISOU 3154  ND1 HIS C 122     1914   1465   2061    401   -309   -347       N  
ATOM   3155  CD2 HIS C 122     -27.939 -10.986   5.118  1.00 15.19           C  
ANISOU 3155  CD2 HIS C 122     1948   1689   2134    338   -188   -313       C  
ATOM   3156  CE1 HIS C 122     -27.545 -12.710   6.419  1.00 15.24           C  
ANISOU 3156  CE1 HIS C 122     1985   1594   2212    395   -336   -317       C  
ATOM   3157  NE2 HIS C 122     -27.444 -11.397   6.332  1.00 14.90           N  
ANISOU 3157  NE2 HIS C 122     1890   1621   2149    356   -260   -304       N  
ATOM   3158  N   ALA C 123     -27.369 -10.293   1.187  1.00 17.55           N  
ANISOU 3158  N   ALA C 123     2272   2118   2279    332     43   -419       N  
ATOM   3159  CA  ALA C 123     -26.292  -9.405   0.848  1.00 18.55           C  
ANISOU 3159  CA  ALA C 123     2328   2310   2408    310    142   -438       C  
ATOM   3160  C   ALA C 123     -26.848  -8.030   0.392  1.00 19.43           C  
ANISOU 3160  C   ALA C 123     2484   2448   2451    231    185   -352       C  
ATOM   3161  O   ALA C 123     -26.383  -6.999   0.849  1.00 18.70           O  
ANISOU 3161  O   ALA C 123     2342   2368   2393    192    219   -318       O  
ATOM   3162  CB  ALA C 123     -25.385 -10.038  -0.257  1.00 16.95           C  
ANISOU 3162  CB  ALA C 123     2100   2158   2180    344    225   -546       C  
ATOM   3163  N   SER C 124     -27.833  -8.041  -0.512  1.00 19.44           N  
ANISOU 3163  N   SER C 124     2578   2448   2359    209    170   -319       N  
ATOM   3164  CA  SER C 124     -28.423  -6.787  -1.020  1.00 19.46           C  
ANISOU 3164  CA  SER C 124     2636   2458   2301    146    184   -231       C  
ATOM   3165  C   SER C 124     -29.085  -5.973   0.095  1.00 19.31           C  
ANISOU 3165  C   SER C 124     2597   2388   2351    135    125   -163       C  
ATOM   3166  O   SER C 124     -28.922  -4.744   0.154  1.00 19.55           O  
ANISOU 3166  O   SER C 124     2623   2412   2392     92    154   -111       O  
ATOM   3167  CB  SER C 124     -29.435  -7.080  -2.102  1.00 18.45           C  
ANISOU 3167  CB  SER C 124     2609   2333   2066    137    146   -211       C  
ATOM   3168  OG  SER C 124     -28.760  -7.542  -3.250  1.00 17.42           O  
ANISOU 3168  OG  SER C 124     2507   2264   1847    128    223   -274       O  
ATOM   3169  N   LEU C 125     -29.827  -6.661   0.952  1.00 19.07           N  
ANISOU 3169  N   LEU C 125     2560   2321   2365    168     46   -171       N  
ATOM   3170  CA  LEU C 125     -30.540  -6.012   2.035  1.00 19.18           C  
ANISOU 3170  CA  LEU C 125     2551   2301   2435    156     -1   -129       C  
ATOM   3171  C   LEU C 125     -29.564  -5.514   3.065  1.00 18.22           C  
ANISOU 3171  C   LEU C 125     2358   2182   2383    149     29   -143       C  
ATOM   3172  O   LEU C 125     -29.821  -4.535   3.717  1.00 18.67           O  
ANISOU 3172  O   LEU C 125     2397   2220   2476    126     23   -115       O  
ATOM   3173  CB  LEU C 125     -31.564  -6.926   2.718  1.00 18.69           C  
ANISOU 3173  CB  LEU C 125     2498   2213   2389    172    -77   -136       C  
ATOM   3174  CG  LEU C 125     -33.021  -6.720   2.321  1.00 22.05           C  
ANISOU 3174  CG  LEU C 125     2960   2629   2789    160   -129   -103       C  
ATOM   3175  CD1 LEU C 125     -33.589  -5.300   2.679  1.00 20.73           C  
ANISOU 3175  CD1 LEU C 125     2769   2447   2659    146   -133    -60       C  
ATOM   3176  CD2 LEU C 125     -33.188  -6.963   0.827  1.00 22.52           C  
ANISOU 3176  CD2 LEU C 125     3085   2705   2765    162   -132   -101       C  
ATOM   3177  N   ASP C 126     -28.439  -6.173   3.209  1.00 19.24           N  
ANISOU 3177  N   ASP C 126     2441   2333   2537    173     53   -196       N  
ATOM   3178  CA  ASP C 126     -27.396  -5.658   4.087  1.00 19.44           C  
ANISOU 3178  CA  ASP C 126     2387   2370   2629    162     74   -215       C  
ATOM   3179  C   ASP C 126     -26.856  -4.346   3.533  1.00 20.64           C  
ANISOU 3179  C   ASP C 126     2525   2541   2778    106    152   -192       C  
ATOM   3180  O   ASP C 126     -26.576  -3.427   4.289  1.00 20.27           O  
ANISOU 3180  O   ASP C 126     2440   2481   2780     73    155   -181       O  
ATOM   3181  CB  ASP C 126     -26.246  -6.639   4.223  1.00 19.57           C  
ANISOU 3181  CB  ASP C 126     2342   2407   2685    210     74   -285       C  
ATOM   3182  CG  ASP C 126     -25.011  -6.024   4.926  1.00 20.69           C  
ANISOU 3182  CG  ASP C 126     2384   2578   2900    195     97   -314       C  
ATOM   3183  OD1 ASP C 126     -25.098  -5.765   6.127  1.00 22.29           O  
ANISOU 3183  OD1 ASP C 126     2569   2762   3137    186     40   -298       O  
ATOM   3184  OD2 ASP C 126     -23.944  -5.839   4.293  1.00 24.61           O  
ANISOU 3184  OD2 ASP C 126     2815   3122   3414    187    174   -360       O  
ATOM   3185  N   LYS C 127     -26.606  -4.283   2.224  1.00 21.25           N  
ANISOU 3185  N   LYS C 127     2635   2649   2791     86    218   -189       N  
ATOM   3186  CA  LYS C 127     -26.076  -3.044   1.678  1.00 22.02           C  
ANISOU 3186  CA  LYS C 127     2735   2758   2875     12    294   -153       C  
ATOM   3187  C   LYS C 127     -27.111  -1.920   1.791  1.00 20.97           C  
ANISOU 3187  C   LYS C 127     2669   2558   2740    -18    251    -70       C  
ATOM   3188  O   LYS C 127     -26.733  -0.783   1.947  1.00 22.08           O  
ANISOU 3188  O   LYS C 127     2801   2673   2914    -74    281    -39       O  
ATOM   3189  CB  LYS C 127     -25.571  -3.207   0.250  1.00 22.87           C  
ANISOU 3189  CB  LYS C 127     2873   2923   2892    -21    384   -164       C  
ATOM   3190  CG  LYS C 127     -24.273  -4.003   0.200  1.00 25.43           C  
ANISOU 3190  CG  LYS C 127     3094   3317   3250      4    451   -268       C  
ATOM   3191  CD  LYS C 127     -23.980  -4.607  -1.188  1.00 27.62           C  
ANISOU 3191  CD  LYS C 127     3405   3663   3426     -4    535   -315       C  
ATOM   3192  CE  LYS C 127     -22.795  -5.577  -1.117  1.00 30.68           C  
ANISOU 3192  CE  LYS C 127     3671   4111   3876     53    585   -446       C  
ATOM   3193  NZ  LYS C 127     -23.080  -6.918  -0.372  1.00 29.18           N  
ANISOU 3193  NZ  LYS C 127     3460   3870   3757    170    475   -504       N  
ATOM   3194  N   PHE C 128     -28.392  -2.247   1.730  1.00 20.00           N  
ANISOU 3194  N   PHE C 128     2604   2404   2589     21    177    -43       N  
ATOM   3195  CA  PHE C 128     -29.471  -1.252   1.832  1.00 19.28           C  
ANISOU 3195  CA  PHE C 128     2562   2249   2516     14    123     20       C  
ATOM   3196  C   PHE C 128     -29.552  -0.681   3.237  1.00 19.50           C  
ANISOU 3196  C   PHE C 128     2530   2241   2638     18     97     -3       C  
ATOM   3197  O   PHE C 128     -29.599   0.528   3.405  1.00 20.25           O  
ANISOU 3197  O   PHE C 128     2635   2282   2778    -12     99     26       O  
ATOM   3198  CB  PHE C 128     -30.808  -1.905   1.452  1.00 18.74           C  
ANISOU 3198  CB  PHE C 128     2542   2173   2405     58     47     34       C  
ATOM   3199  CG  PHE C 128     -32.026  -1.068   1.774  1.00 17.10           C  
ANISOU 3199  CG  PHE C 128     2347   1905   2244     75    -24     71       C  
ATOM   3200  CD1 PHE C 128     -32.320   0.070   1.034  1.00 17.72           C  
ANISOU 3200  CD1 PHE C 128     2489   1930   2314     56    -44    143       C  
ATOM   3201  CD2 PHE C 128     -32.897  -1.448   2.770  1.00 15.05           C  
ANISOU 3201  CD2 PHE C 128     2039   1641   2036    108    -72     33       C  
ATOM   3202  CE1 PHE C 128     -33.497   0.845   1.287  1.00 17.29           C  
ANISOU 3202  CE1 PHE C 128     2438   1808   2323     92   -124    166       C  
ATOM   3203  CE2 PHE C 128     -34.077  -0.693   3.039  1.00 16.90           C  
ANISOU 3203  CE2 PHE C 128     2264   1830   2325    133   -130     45       C  
ATOM   3204  CZ  PHE C 128     -34.368   0.452   2.292  1.00 15.50           C  
ANISOU 3204  CZ  PHE C 128     2139   1591   2160    135   -162    107       C  
ATOM   3205  N   LEU C 129     -29.538  -1.555   4.247  1.00 19.53           N  
ANISOU 3205  N   LEU C 129     2481   2270   2668     49     72    -57       N  
ATOM   3206  CA  LEU C 129     -29.576  -1.112   5.642  1.00 18.88           C  
ANISOU 3206  CA  LEU C 129     2349   2172   2651     44     51    -89       C  
ATOM   3207  C   LEU C 129     -28.373  -0.234   5.956  1.00 20.17           C  
ANISOU 3207  C   LEU C 129     2470   2332   2862     -3     97   -104       C  
ATOM   3208  O   LEU C 129     -28.498   0.772   6.661  1.00 19.43           O  
ANISOU 3208  O   LEU C 129     2365   2197   2822    -26     90   -113       O  
ATOM   3209  CB  LEU C 129     -29.703  -2.302   6.610  1.00 17.33           C  
ANISOU 3209  CB  LEU C 129     2126   2009   2449     70     11   -129       C  
ATOM   3210  CG  LEU C 129     -31.070  -2.967   6.409  1.00 17.13           C  
ANISOU 3210  CG  LEU C 129     2140   1980   2390     94    -34   -114       C  
ATOM   3211  CD1 LEU C 129     -31.135  -4.387   6.997  1.00 14.10           C  
ANISOU 3211  CD1 LEU C 129     1757   1618   1984    107    -71   -135       C  
ATOM   3212  CD2 LEU C 129     -32.248  -2.085   6.912  1.00 14.41           C  
ANISOU 3212  CD2 LEU C 129     1788   1608   2079     90    -53   -114       C  
ATOM   3213  N   CYS C 130     -27.227  -0.570   5.370  1.00 22.18           N  
ANISOU 3213  N   CYS C 130     2697   2629   3103    -21    149   -115       N  
ATOM   3214  CA  CYS C 130     -26.007   0.189   5.583  1.00 24.85           C  
ANISOU 3214  CA  CYS C 130     2975   2975   3490    -78    199   -136       C  
ATOM   3215  C   CYS C 130     -26.152   1.563   4.957  1.00 24.49           C  
ANISOU 3215  C   CYS C 130     2984   2868   3452   -141    233    -78       C  
ATOM   3216  O   CYS C 130     -25.888   2.546   5.622  1.00 26.07           O  
ANISOU 3216  O   CYS C 130     3163   3024   3717   -183    231    -89       O  
ATOM   3217  CB  CYS C 130     -24.764  -0.556   5.021  1.00 26.13           C  
ANISOU 3217  CB  CYS C 130     3074   3210   3643    -80    256   -176       C  
ATOM   3218  SG  CYS C 130     -23.146   0.355   5.170  1.00 39.73           S  
ANISOU 3218  SG  CYS C 130     4693   4966   5437   -168    332   -214       S  
ATOM   3219  N   ALA C 131     -26.587   1.655   3.700  1.00 23.94           N  
ANISOU 3219  N   ALA C 131     2995   2785   3315   -150    253    -14       N  
ATOM   3220  CA  ALA C 131     -26.744   2.960   3.057  1.00 24.47           C  
ANISOU 3220  CA  ALA C 131     3136   2776   3384   -213    268     61       C  
ATOM   3221  C   ALA C 131     -27.746   3.834   3.844  1.00 23.05           C  
ANISOU 3221  C   ALA C 131     2981   2499   3278   -184    192     69       C  
ATOM   3222  O   ALA C 131     -27.562   5.043   3.935  1.00 24.07           O  
ANISOU 3222  O   ALA C 131     3135   2545   3464   -236    196     96       O  
ATOM   3223  CB  ALA C 131     -27.195   2.816   1.607  1.00 25.06           C  
ANISOU 3223  CB  ALA C 131     3312   2857   3354   -223    278    137       C  
ATOM   3224  N   VAL C 132     -28.781   3.217   4.414  1.00 20.96           N  
ANISOU 3224  N   VAL C 132     2705   2242   3018   -105    129     38       N  
ATOM   3225  CA  VAL C 132     -29.718   3.953   5.261  1.00 20.69           C  
ANISOU 3225  CA  VAL C 132     2667   2135   3058    -71     72     14       C  
ATOM   3226  C   VAL C 132     -29.010   4.433   6.547  1.00 20.60           C  
ANISOU 3226  C   VAL C 132     2590   2121   3118   -104     90    -60       C  
ATOM   3227  O   VAL C 132     -29.172   5.565   6.909  1.00 20.23           O  
ANISOU 3227  O   VAL C 132     2555   1988   3142   -121     76    -71       O  
ATOM   3228  CB  VAL C 132     -31.006   3.137   5.625  1.00 19.60           C  
ANISOU 3228  CB  VAL C 132     2515   2027   2906      4     16    -14       C  
ATOM   3229  CG1 VAL C 132     -31.811   3.861   6.682  1.00 17.31           C  
ANISOU 3229  CG1 VAL C 132     2192   1687   2697     33    -18    -72       C  
ATOM   3230  CG2 VAL C 132     -31.881   2.873   4.387  1.00 20.10           C  
ANISOU 3230  CG2 VAL C 132     2643   2078   2914     37    -26     53       C  
ATOM   3231  N   ALA C 133     -28.263   3.557   7.215  1.00 20.10           N  
ANISOU 3231  N   ALA C 133     2460   2143   3034   -109    107   -113       N  
ATOM   3232  CA  ALA C 133     -27.486   3.947   8.354  1.00 21.70           C  
ANISOU 3232  CA  ALA C 133     2602   2355   3287   -147    112   -180       C  
ATOM   3233  C   ALA C 133     -26.643   5.125   7.985  1.00 22.74           C  
ANISOU 3233  C   ALA C 133     2740   2427   3473   -225    151   -161       C  
ATOM   3234  O   ALA C 133     -26.637   6.115   8.696  1.00 24.05           O  
ANISOU 3234  O   ALA C 133     2903   2529   3707   -254    137   -201       O  
ATOM   3235  CB  ALA C 133     -26.579   2.777   8.877  1.00 21.34           C  
ANISOU 3235  CB  ALA C 133     2488   2409   3212   -141    111   -221       C  
ATOM   3236  N   ASN C 134     -25.951   5.045   6.860  1.00 23.94           N  
ANISOU 3236  N   ASN C 134     2906   2598   3593   -268    205   -106       N  
ATOM   3237  CA  ASN C 134     -25.048   6.124   6.456  1.00 25.65           C  
ANISOU 3237  CA  ASN C 134     3129   2765   3852   -370    257    -80       C  
ATOM   3238  C   ASN C 134     -25.739   7.444   6.277  1.00 26.46           C  
ANISOU 3238  C   ASN C 134     3321   2726   4006   -392    227    -31       C  
ATOM   3239  O   ASN C 134     -25.152   8.495   6.587  1.00 26.62           O  
ANISOU 3239  O   ASN C 134     3339   2676   4100   -471    240    -44       O  
ATOM   3240  CB  ASN C 134     -24.273   5.795   5.172  1.00 27.57           C  
ANISOU 3240  CB  ASN C 134     3379   3066   4030   -426    338    -26       C  
ATOM   3241  CG  ASN C 134     -23.198   4.733   5.393  1.00 28.36           C  
ANISOU 3241  CG  ASN C 134     3361   3293   4121   -419    378    -98       C  
ATOM   3242  OD1 ASN C 134     -22.962   4.293   6.519  1.00 31.47           O  
ANISOU 3242  OD1 ASN C 134     3677   3723   4556   -380    332   -173       O  
ATOM   3243  ND2 ASN C 134     -22.562   4.314   4.320  1.00 31.60           N  
ANISOU 3243  ND2 ASN C 134     3761   3772   4474   -455    459    -79       N  
ATOM   3244  N   VAL C 135     -26.978   7.402   5.800  1.00 25.87           N  
ANISOU 3244  N   VAL C 135     3320   2602   3905   -320    176     18       N  
ATOM   3245  CA  VAL C 135     -27.764   8.615   5.686  1.00 27.01           C  
ANISOU 3245  CA  VAL C 135     3546   2599   4119   -312    123     56       C  
ATOM   3246  C   VAL C 135     -28.125   9.195   7.089  1.00 27.70           C  
ANISOU 3246  C   VAL C 135     3584   2633   4306   -279     84    -51       C  
ATOM   3247  O   VAL C 135     -27.976  10.387   7.324  1.00 28.68           O  
ANISOU 3247  O   VAL C 135     3741   2638   4519   -321     70    -61       O  
ATOM   3248  CB  VAL C 135     -29.016   8.407   4.795  1.00 26.96           C  
ANISOU 3248  CB  VAL C 135     3616   2558   4067   -234     62    131       C  
ATOM   3249  CG1 VAL C 135     -29.949   9.613   4.866  1.00 26.21           C  
ANISOU 3249  CG1 VAL C 135     3583   2302   4072   -192    -19    149       C  
ATOM   3250  CG2 VAL C 135     -28.581   8.185   3.373  1.00 25.98           C  
ANISOU 3250  CG2 VAL C 135     3568   2463   3840   -292    100    239       C  
ATOM   3251  N   LEU C 136     -28.505   8.350   8.032  1.00 27.23           N  
ANISOU 3251  N   LEU C 136     3454   2665   4225   -218     72   -136       N  
ATOM   3252  CA  LEU C 136     -28.927   8.832   9.333  1.00 27.69           C  
ANISOU 3252  CA  LEU C 136     3474   2695   4351   -192     45   -246       C  
ATOM   3253  C   LEU C 136     -27.785   9.369  10.206  1.00 28.09           C  
ANISOU 3253  C   LEU C 136     3481   2746   4445   -275     69   -318       C  
ATOM   3254  O   LEU C 136     -28.043  10.167  11.102  1.00 27.44           O  
ANISOU 3254  O   LEU C 136     3392   2601   4431   -274     48   -406       O  
ATOM   3255  CB  LEU C 136     -29.743   7.735  10.064  1.00 27.24           C  
ANISOU 3255  CB  LEU C 136     3368   2746   4238   -120     31   -305       C  
ATOM   3256  CG  LEU C 136     -31.275   7.762   9.868  1.00 28.45           C  
ANISOU 3256  CG  LEU C 136     3536   2863   4411    -31    -10   -307       C  
ATOM   3257  CD1 LEU C 136     -31.678   8.208   8.462  1.00 28.84           C  
ANISOU 3257  CD1 LEU C 136     3660   2819   4478     -8    -44   -197       C  
ATOM   3258  CD2 LEU C 136     -31.891   6.438  10.189  1.00 25.90           C  
ANISOU 3258  CD2 LEU C 136     3172   2660   4007      7     -9   -326       C  
ATOM   3259  N   THR C 137     -26.541   8.946   9.946  1.00 28.60           N  
ANISOU 3259  N   THR C 137     3507   2884   4475   -346    110   -293       N  
ATOM   3260  CA  THR C 137     -25.381   9.298  10.782  1.00 29.57           C  
ANISOU 3260  CA  THR C 137     3566   3032   4637   -427    122   -367       C  
ATOM   3261  C   THR C 137     -24.455  10.393  10.194  1.00 32.84           C  
ANISOU 3261  C   THR C 137     4001   3356   5120   -542    158   -329       C  
ATOM   3262  O   THR C 137     -23.367  10.666  10.764  1.00 33.72           O  
ANISOU 3262  O   THR C 137     4045   3497   5270   -626    170   -389       O  
ATOM   3263  CB  THR C 137     -24.488   8.075  11.015  1.00 29.21           C  
ANISOU 3263  CB  THR C 137     3435   3136   4528   -431    134   -384       C  
ATOM   3264  OG1 THR C 137     -23.738   7.791   9.821  1.00 26.08           O  
ANISOU 3264  OG1 THR C 137     3030   2771   4110   -473    192   -309       O  
ATOM   3265  CG2 THR C 137     -25.309   6.840  11.422  1.00 27.64           C  
ANISOU 3265  CG2 THR C 137     3232   3021   4250   -336    101   -395       C  
ATOM   3266  N   ALA C 138     -24.885  11.029   9.087  1.00 34.50           N  
ANISOU 3266  N   ALA C 138     4307   3457   5345   -555    167   -228       N  
ATOM   3267  CA  ALA C 138     -24.028  11.933   8.265  1.00 36.30           C  
ANISOU 3267  CA  ALA C 138     4578   3604   5610   -683    213   -154       C  
ATOM   3268  C   ALA C 138     -23.956  13.373   8.790  1.00 37.86           C  
ANISOU 3268  C   ALA C 138     4820   3638   5929   -748    182   -193       C  
ATOM   3269  O   ALA C 138     -24.934  13.895   9.327  1.00 38.40           O  
ANISOU 3269  O   ALA C 138     4930   3603   6056   -670    118   -241       O  
ATOM   3270  CB  ALA C 138     -24.518  11.936   6.786  1.00 36.33           C  
ANISOU 3270  CB  ALA C 138     4690   3562   5551   -680    227    -10       C  
TER    3271      ALA C 138                                                      
ATOM   3272  N   VAL D   1     -17.727 -13.751  31.796  1.00 40.69           N  
ANISOU 3272  N   VAL D   1     4831   7011   3618    229   -322    264       N  
ATOM   3273  CA  VAL D   1     -19.197 -13.761  31.558  1.00 39.11           C  
ANISOU 3273  CA  VAL D   1     4681   6718   3462    255   -246    262       C  
ATOM   3274  C   VAL D   1     -19.880 -14.679  32.577  1.00 40.31           C  
ANISOU 3274  C   VAL D   1     4800   6993   3522    321   -196    394       C  
ATOM   3275  O   VAL D   1     -19.281 -15.631  33.079  1.00 40.42           O  
ANISOU 3275  O   VAL D   1     4758   7104   3497    356   -205    532       O  
ATOM   3276  CB  VAL D   1     -19.514 -14.187  30.102  1.00 38.19           C  
ANISOU 3276  CB  VAL D   1     4588   6395   3527    242   -209    300       C  
ATOM   3277  CG1 VAL D   1     -18.900 -15.545  29.803  1.00 36.44           C  
ANISOU 3277  CG1 VAL D   1     4316   6155   3373    267   -200    462       C  
ATOM   3278  CG2 VAL D   1     -21.002 -14.143  29.832  1.00 35.78           C  
ANISOU 3278  CG2 VAL D   1     4320   6009   3265    261   -141    290       C  
ATOM   3279  N   GLN D   2     -21.125 -14.337  32.896  1.00 40.15           N  
ANISOU 3279  N   GLN D   2     4813   6973   3468    342   -141    354       N  
ATOM   3280  CA  GLN D   2     -21.974 -15.085  33.823  1.00 40.94           C  
ANISOU 3280  CA  GLN D   2     4887   7181   3487    401    -78    471       C  
ATOM   3281  C   GLN D   2     -23.229 -15.468  33.057  1.00 38.56           C  
ANISOU 3281  C   GLN D   2     4604   6732   3316    406     -1    511       C  
ATOM   3282  O   GLN D   2     -23.846 -14.617  32.418  1.00 39.23           O  
ANISOU 3282  O   GLN D   2     4732   6715   3458    384      8    391       O  
ATOM   3283  CB  GLN D   2     -22.356 -14.217  35.039  1.00 42.25           C  
ANISOU 3283  CB  GLN D   2     5068   7513   3472    422    -79    370       C  
ATOM   3284  CG  GLN D   2     -21.612 -14.542  36.319  1.00 47.20           C  
ANISOU 3284  CG  GLN D   2     5648   8368   3921    455   -117    432       C  
ATOM   3285  CD  GLN D   2     -22.514 -15.208  37.361  1.00 52.85           C  
ANISOU 3285  CD  GLN D   2     6338   9217   4526    524    -42    555       C  
ATOM   3286  OE1 GLN D   2     -23.711 -14.870  37.495  1.00 54.47           O  
ANISOU 3286  OE1 GLN D   2     6572   9401   4723    542     26    512       O  
ATOM   3287  NE2 GLN D   2     -21.945 -16.160  38.108  1.00 54.84           N  
ANISOU 3287  NE2 GLN D   2     6533   9613   4693    569    -49    717       N  
ATOM   3288  N   TRP D   3     -23.605 -16.733  33.123  1.00 36.82           N  
ANISOU 3288  N   TRP D   3     4345   6501   3143    435     55    679       N  
ATOM   3289  CA  TRP D   3     -24.750 -17.219  32.411  1.00 34.79           C  
ANISOU 3289  CA  TRP D   3     4092   6113   3013    429    124    722       C  
ATOM   3290  C   TRP D   3     -25.902 -17.428  33.394  1.00 36.00           C  
ANISOU 3290  C   TRP D   3     4224   6373   3081    471    200    781       C  
ATOM   3291  O   TRP D   3     -25.735 -18.140  34.387  1.00 37.58           O  
ANISOU 3291  O   TRP D   3     4386   6702   3189    511    225    908       O  
ATOM   3292  CB  TRP D   3     -24.402 -18.531  31.762  1.00 33.31           C  
ANISOU 3292  CB  TRP D   3     3878   5820   2956    422    145    864       C  
ATOM   3293  CG  TRP D   3     -23.486 -18.415  30.591  1.00 31.10           C  
ANISOU 3293  CG  TRP D   3     3620   5411   2786    383     90    810       C  
ATOM   3294  CD1 TRP D   3     -22.196 -18.826  30.529  1.00 28.66           C  
ANISOU 3294  CD1 TRP D   3     3291   5116   2483    387     47    862       C  
ATOM   3295  CD2 TRP D   3     -23.809 -17.894  29.290  1.00 27.47           C  
ANISOU 3295  CD2 TRP D   3     3199   4794   2444    339     80    704       C  
ATOM   3296  NE1 TRP D   3     -21.691 -18.601  29.281  1.00 29.76           N  
ANISOU 3296  NE1 TRP D   3     3456   5115   2737    347     15    794       N  
ATOM   3297  CE2 TRP D   3     -22.657 -18.028  28.495  1.00 28.57           C  
ANISOU 3297  CE2 TRP D   3     3344   4858   2653    317     34    697       C  
ATOM   3298  CE3 TRP D   3     -24.971 -17.350  28.716  1.00 28.03           C  
ANISOU 3298  CE3 TRP D   3     3295   4790   2565    323    108    624       C  
ATOM   3299  CZ2 TRP D   3     -22.614 -17.618  27.142  1.00 26.31           C  
ANISOU 3299  CZ2 TRP D   3     3094   4425   2478    277     16    611       C  
ATOM   3300  CZ3 TRP D   3     -24.941 -16.946  27.363  1.00 24.55           C  
ANISOU 3300  CZ3 TRP D   3     2888   4205   2235    287     84    541       C  
ATOM   3301  CH2 TRP D   3     -23.771 -17.080  26.602  1.00 25.63           C  
ANISOU 3301  CH2 TRP D   3     3036   4271   2431    263     40    536       C  
ATOM   3302  N   SER D   4     -27.064 -16.826  33.139  1.00 34.62           N  
ANISOU 3302  N   SER D   4     4065   6154   2933    468    240    700       N  
ATOM   3303  CA  SER D   4     -28.243 -17.147  33.960  1.00 35.15           C  
ANISOU 3303  CA  SER D   4     4101   6313   2942    506    325    772       C  
ATOM   3304  C   SER D   4     -28.776 -18.530  33.601  1.00 34.40           C  
ANISOU 3304  C   SER D   4     3961   6136   2973    494    390    937       C  
ATOM   3305  O   SER D   4     -28.439 -19.094  32.550  1.00 33.42           O  
ANISOU 3305  O   SER D   4     3841   5863   2995    454    372    963       O  
ATOM   3306  CB  SER D   4     -29.358 -16.158  33.691  1.00 34.72           C  
ANISOU 3306  CB  SER D   4     4067   6227   2899    511    353    645       C  
ATOM   3307  OG  SER D   4     -29.874 -16.393  32.375  1.00 34.06           O  
ANISOU 3307  OG  SER D   4     3981   5970   2990    471    359    640       O  
ATOM   3308  N   ALA D   5     -29.680 -19.025  34.438  1.00 35.04           N  
ANISOU 3308  N   ALA D   5     4001   6309   3003    525    473   1038       N  
ATOM   3309  CA  ALA D   5     -30.345 -20.314  34.216  1.00 34.58           C  
ANISOU 3309  CA  ALA D   5     3896   6175   3067    506    551   1195       C  
ATOM   3310  C   ALA D   5     -31.230 -20.257  32.978  1.00 33.15           C  
ANISOU 3310  C   ALA D   5     3711   5834   3051    452    563   1129       C  
ATOM   3311  O   ALA D   5     -31.310 -21.210  32.199  1.00 31.86           O  
ANISOU 3311  O   ALA D   5     3530   5536   3037    407    582   1200       O  
ATOM   3312  CB  ALA D   5     -31.169 -20.700  35.441  1.00 35.95           C  
ANISOU 3312  CB  ALA D   5     4024   6496   3138    551    643   1310       C  
ATOM   3313  N   GLU D   6     -31.893 -19.115  32.829  1.00 33.06           N  
ANISOU 3313  N   GLU D   6     3714   5843   3004    462    552    990       N  
ATOM   3314  CA  GLU D   6     -32.769 -18.823  31.708  1.00 32.54           C  
ANISOU 3314  CA  GLU D   6     3641   5657   3065    425    554    912       C  
ATOM   3315  C   GLU D   6     -31.977 -18.928  30.383  1.00 30.10           C  
ANISOU 3315  C   GLU D   6     3370   5189   2879    376    482    862       C  
ATOM   3316  O   GLU D   6     -32.351 -19.660  29.447  1.00 30.04           O  
ANISOU 3316  O   GLU D   6     3340   5061   3014    326    494    895       O  
ATOM   3317  CB  GLU D   6     -33.329 -17.394  31.864  1.00 33.27           C  
ANISOU 3317  CB  GLU D   6     3756   5809   3076    465    544    765       C  
ATOM   3318  CG  GLU D   6     -34.321 -17.126  33.040  1.00 37.75           C  
ANISOU 3318  CG  GLU D   6     4286   6531   3527    521    624    787       C  
ATOM   3319  CD  GLU D   6     -33.680 -16.828  34.447  1.00 42.31           C  
ANISOU 3319  CD  GLU D   6     4887   7280   3910    575    627    793       C  
ATOM   3320  OE1 GLU D   6     -32.527 -16.320  34.556  1.00 42.58           O  
ANISOU 3320  OE1 GLU D   6     4976   7329   3875    577    552    721       O  
ATOM   3321  OE2 GLU D   6     -34.384 -17.079  35.458  1.00 43.89           O  
ANISOU 3321  OE2 GLU D   6     5045   7611   4019    616    706    868       O  
ATOM   3322  N   GLU D   7     -30.871 -18.207  30.319  1.00 27.95           N  
ANISOU 3322  N   GLU D   7     3151   4921   2547    386    410    778       N  
ATOM   3323  CA  GLU D   7     -30.004 -18.225  29.165  1.00 26.09           C  
ANISOU 3323  CA  GLU D   7     2952   4555   2408    347    346    733       C  
ATOM   3324  C   GLU D   7     -29.540 -19.614  28.806  1.00 25.39           C  
ANISOU 3324  C   GLU D   7     2842   4385   2419    317    362    857       C  
ATOM   3325  O   GLU D   7     -29.590 -20.007  27.643  1.00 24.10           O  
ANISOU 3325  O   GLU D   7     2684   4086   2385    274    351    841       O  
ATOM   3326  CB  GLU D   7     -28.809 -17.316  29.389  1.00 26.10           C  
ANISOU 3326  CB  GLU D   7     3001   4598   2319    361    275    644       C  
ATOM   3327  CG  GLU D   7     -29.192 -15.843  29.451  1.00 26.61           C  
ANISOU 3327  CG  GLU D   7     3103   4691   2318    381    256    494       C  
ATOM   3328  CD  GLU D   7     -28.077 -14.951  29.937  1.00 28.27           C  
ANISOU 3328  CD  GLU D   7     3355   4962   2424    387    196    404       C  
ATOM   3329  OE1 GLU D   7     -27.325 -15.338  30.837  1.00 34.29           O  
ANISOU 3329  OE1 GLU D   7     4102   5833   3094    399    183    462       O  
ATOM   3330  OE2 GLU D   7     -27.956 -13.838  29.426  1.00 30.71           O  
ANISOU 3330  OE2 GLU D   7     3710   5215   2744    378    162    275       O  
ATOM   3331  N   LYS D   8     -29.109 -20.387  29.785  1.00 26.52           N  
ANISOU 3331  N   LYS D   8     2962   4609   2505    344    393    984       N  
ATOM   3332  CA  LYS D   8     -28.585 -21.726  29.479  1.00 26.86           C  
ANISOU 3332  CA  LYS D   8     2991   4563   2651    326    416   1111       C  
ATOM   3333  C   LYS D   8     -29.715 -22.573  28.908  1.00 27.17           C  
ANISOU 3333  C   LYS D   8     2999   4497   2829    280    482   1160       C  
ATOM   3334  O   LYS D   8     -29.529 -23.378  28.002  1.00 27.12           O  
ANISOU 3334  O   LYS D   8     2997   4350   2958    238    488   1183       O  
ATOM   3335  CB  LYS D   8     -28.015 -22.353  30.732  1.00 28.56           C  
ANISOU 3335  CB  LYS D   8     3183   4898   2769    377    444   1253       C  
ATOM   3336  CG  LYS D   8     -27.453 -23.762  30.579  1.00 32.08           C  
ANISOU 3336  CG  LYS D   8     3615   5257   3318    376    480   1405       C  
ATOM   3337  CD  LYS D   8     -26.738 -24.225  31.848  1.00 34.47           C  
ANISOU 3337  CD  LYS D   8     3894   5700   3501    444    495   1549       C  
ATOM   3338  CE  LYS D   8     -26.074 -25.606  31.614  1.00 37.20           C  
ANISOU 3338  CE  LYS D   8     4231   5941   3964    455    533   1704       C  
ATOM   3339  NZ  LYS D   8     -25.402 -26.196  32.867  1.00 39.57           N  
ANISOU 3339  NZ  LYS D   8     4500   6382   4153    534    556   1878       N  
ATOM   3340  N   GLN D   9     -30.912 -22.363  29.429  1.00 27.81           N  
ANISOU 3340  N   GLN D   9     3042   4649   2875    284    534   1166       N  
ATOM   3341  CA  GLN D   9     -32.055 -23.139  28.996  1.00 28.79           C  
ANISOU 3341  CA  GLN D   9     3120   4695   3125    232    599   1213       C  
ATOM   3342  C   GLN D   9     -32.414 -22.793  27.527  1.00 27.28           C  
ANISOU 3342  C   GLN D   9     2942   4379   3044    178    552   1085       C  
ATOM   3343  O   GLN D   9     -32.604 -23.666  26.686  1.00 27.42           O  
ANISOU 3343  O   GLN D   9     2948   4270   3199    119    567   1105       O  
ATOM   3344  CB  GLN D   9     -33.212 -22.953  29.998  1.00 29.45           C  
ANISOU 3344  CB  GLN D   9     3150   4908   3132    257    669   1257       C  
ATOM   3345  CG  GLN D   9     -34.556 -23.484  29.569  1.00 33.14           C  
ANISOU 3345  CG  GLN D   9     3554   5320   3718    199    731   1280       C  
ATOM   3346  CD  GLN D   9     -34.543 -24.936  29.108  1.00 36.11           C  
ANISOU 3346  CD  GLN D   9     3911   5558   4253    132    777   1386       C  
ATOM   3347  OE1 GLN D   9     -35.458 -25.368  28.379  1.00 38.04           O  
ANISOU 3347  OE1 GLN D   9     4111   5718   4624     61    802   1367       O  
ATOM   3348  NE2 GLN D   9     -33.518 -25.699  29.523  1.00 33.02           N  
ANISOU 3348  NE2 GLN D   9     3548   5140   3859    155    790   1496       N  
ATOM   3349  N   LEU D  10     -32.424 -21.516  27.203  1.00 26.23           N  
ANISOU 3349  N   LEU D  10     2838   4280   2849    200    493    952       N  
ATOM   3350  CA  LEU D  10     -32.731 -21.097  25.859  1.00 24.52           C  
ANISOU 3350  CA  LEU D  10     2634   3966   2716    163    447    841       C  
ATOM   3351  C   LEU D  10     -31.694 -21.602  24.878  1.00 23.94           C  
ANISOU 3351  C   LEU D  10     2604   3766   2725    130    404    828       C  
ATOM   3352  O   LEU D  10     -32.044 -22.030  23.764  1.00 24.28           O  
ANISOU 3352  O   LEU D  10     2641   3705   2879     78    395    794       O  
ATOM   3353  CB  LEU D  10     -32.875 -19.550  25.783  1.00 23.51           C  
ANISOU 3353  CB  LEU D  10     2536   3897   2501    207    400    712       C  
ATOM   3354  CG  LEU D  10     -34.081 -19.051  26.588  1.00 22.53           C  
ANISOU 3354  CG  LEU D  10     2365   3886   2311    242    451    712       C  
ATOM   3355  CD1 LEU D  10     -34.082 -17.542  26.828  1.00 18.45           C  
ANISOU 3355  CD1 LEU D  10     1887   3432   1692    301    421    597       C  
ATOM   3356  CD2 LEU D  10     -35.393 -19.514  25.925  1.00 23.08           C  
ANISOU 3356  CD2 LEU D  10     2364   3918   2487    198    484    723       C  
ATOM   3357  N   ILE D  11     -30.426 -21.513  25.252  1.00 23.53           N  
ANISOU 3357  N   ILE D  11     2593   3733   2616    162    374    847       N  
ATOM   3358  CA  ILE D  11     -29.348 -21.931  24.369  1.00 22.41           C  
ANISOU 3358  CA  ILE D  11     2488   3481   2543    143    337    837       C  
ATOM   3359  C   ILE D  11     -29.348 -23.470  24.161  1.00 23.43           C  
ANISOU 3359  C   ILE D  11     2598   3511   2794    107    393    944       C  
ATOM   3360  O   ILE D  11     -29.323 -23.962  23.020  1.00 22.60           O  
ANISOU 3360  O   ILE D  11     2507   3281   2798     61    385    905       O  
ATOM   3361  CB  ILE D  11     -27.950 -21.433  24.926  1.00 22.83           C  
ANISOU 3361  CB  ILE D  11     2575   3598   2500    188    292    837       C  
ATOM   3362  CG1 ILE D  11     -27.836 -19.894  24.827  1.00 22.42           C  
ANISOU 3362  CG1 ILE D  11     2557   3599   2363    205    234    706       C  
ATOM   3363  CG2 ILE D  11     -26.796 -22.104  24.215  1.00 19.32           C  
ANISOU 3363  CG2 ILE D  11     2155   3056   2132    177    273    863       C  
ATOM   3364  CD1 ILE D  11     -26.733 -19.286  25.661  1.00 18.46           C  
ANISOU 3364  CD1 ILE D  11     2072   3194   1746    240    194    696       C  
ATOM   3365  N   SER D  12     -29.373 -24.242  25.246  1.00 24.32           N  
ANISOU 3365  N   SER D  12     2681   3674   2887    129    453   1078       N  
ATOM   3366  CA  SER D  12     -29.217 -25.685  25.088  1.00 25.32           C  
ANISOU 3366  CA  SER D  12     2798   3688   3134    102    512   1187       C  
ATOM   3367  C   SER D  12     -30.431 -26.278  24.388  1.00 25.27           C  
ANISOU 3367  C   SER D  12     2760   3587   3253     25    554   1164       C  
ATOM   3368  O   SER D  12     -30.324 -27.117  23.492  1.00 25.47           O  
ANISOU 3368  O   SER D  12     2800   3471   3407    -24    568   1155       O  
ATOM   3369  CB  SER D  12     -28.967 -26.360  26.436  1.00 26.25           C  
ANISOU 3369  CB  SER D  12     2891   3884   3200    151    573   1353       C  
ATOM   3370  OG  SER D  12     -30.180 -26.381  27.107  1.00 28.74           O  
ANISOU 3370  OG  SER D  12     3158   4269   3492    138    629   1394       O  
ATOM   3371  N   SER D  13     -31.588 -25.808  24.785  1.00 25.87           N  
ANISOU 3371  N   SER D  13     2792   3748   3290     15    573   1147       N  
ATOM   3372  CA  SER D  13     -32.836 -26.256  24.219  1.00 26.72           C  
ANISOU 3372  CA  SER D  13     2852   3798   3504    -60    607   1123       C  
ATOM   3373  C   SER D  13     -32.875 -26.159  22.674  1.00 26.24           C  
ANISOU 3373  C   SER D  13     2814   3627   3528   -116    549    990       C  
ATOM   3374  O   SER D  13     -33.198 -27.141  21.988  1.00 26.08           O  
ANISOU 3374  O   SER D  13     2782   3489   3640   -188    578    991       O  
ATOM   3375  CB  SER D  13     -33.943 -25.384  24.790  1.00 26.91           C  
ANISOU 3375  CB  SER D  13     2825   3957   3443    -43    615   1095       C  
ATOM   3376  OG  SER D  13     -35.176 -25.723  24.197  1.00 28.82           O  
ANISOU 3376  OG  SER D  13     3006   4161   3784   -117    639   1064       O  
ATOM   3377  N   LEU D  14     -32.561 -24.970  22.162  1.00 25.38           N  
ANISOU 3377  N   LEU D  14     2739   3561   3342    -82    472    878       N  
ATOM   3378  CA  LEU D  14     -32.469 -24.691  20.696  1.00 25.19           C  
ANISOU 3378  CA  LEU D  14     2745   3457   3370   -117    410    755       C  
ATOM   3379  C   LEU D  14     -31.309 -25.416  20.016  1.00 24.76           C  
ANISOU 3379  C   LEU D  14     2746   3280   3382   -128    402    756       C  
ATOM   3380  O   LEU D  14     -31.470 -25.954  18.946  1.00 23.51           O  
ANISOU 3380  O   LEU D  14     2595   3023   3314   -185    395    698       O  
ATOM   3381  CB  LEU D  14     -32.341 -23.180  20.422  1.00 23.81           C  
ANISOU 3381  CB  LEU D  14     2597   3357   3091    -66    340    655       C  
ATOM   3382  CG  LEU D  14     -32.801 -22.710  19.028  1.00 24.89           C  
ANISOU 3382  CG  LEU D  14     2739   3457   3262    -97    285    538       C  
ATOM   3383  CD1 LEU D  14     -34.349 -22.602  19.016  1.00 20.54           C  
ANISOU 3383  CD1 LEU D  14     2108   2965   2730   -126    301    521       C  
ATOM   3384  CD2 LEU D  14     -32.171 -21.315  18.619  1.00 20.42           C  
ANISOU 3384  CD2 LEU D  14     2227   2922   2608    -40    219    455       C  
ATOM   3385  N   TRP D  15     -30.139 -25.438  20.654  1.00 26.06           N  
ANISOU 3385  N   TRP D  15     2946   3460   3497    -72    404    821       N  
ATOM   3386  CA  TRP D  15     -29.023 -26.203  20.116  1.00 26.24           C  
ANISOU 3386  CA  TRP D  15     3012   3372   3587    -71    409    840       C  
ATOM   3387  C   TRP D  15     -29.494 -27.613  19.836  1.00 27.84           C  
ANISOU 3387  C   TRP D  15     3198   3450   3930   -133    477    888       C  
ATOM   3388  O   TRP D  15     -29.339 -28.110  18.732  1.00 27.75           O  
ANISOU 3388  O   TRP D  15     3213   3324   4006   -175    471    820       O  
ATOM   3389  CB  TRP D  15     -27.817 -26.247  21.056  1.00 26.62           C  
ANISOU 3389  CB  TRP D  15     3076   3468   3571      0    415    937       C  
ATOM   3390  CG  TRP D  15     -26.742 -27.088  20.453  1.00 27.29           C  
ANISOU 3390  CG  TRP D  15     3197   3435   3738      7    428    961       C  
ATOM   3391  CD1 TRP D  15     -26.344 -28.302  20.879  1.00 32.65           C  
ANISOU 3391  CD1 TRP D  15     3872   4043   4492     22    495   1082       C  
ATOM   3392  CD2 TRP D  15     -26.021 -26.831  19.246  1.00 29.38           C  
ANISOU 3392  CD2 TRP D  15     3505   3631   4028      2    383    862       C  
ATOM   3393  NE1 TRP D  15     -25.401 -28.822  20.029  1.00 35.07           N  
ANISOU 3393  NE1 TRP D  15     4217   4237   4871     30    496   1061       N  
ATOM   3394  CE2 TRP D  15     -25.169 -27.923  19.030  1.00 33.31           C  
ANISOU 3394  CE2 TRP D  15     4023   4021   4614     17    427    925       C  
ATOM   3395  CE3 TRP D  15     -25.991 -25.768  18.343  1.00 29.05           C  
ANISOU 3395  CE3 TRP D  15     3488   3610   3941     -8    316    735       C  
ATOM   3396  CZ2 TRP D  15     -24.303 -27.989  17.951  1.00 35.98           C  
ANISOU 3396  CZ2 TRP D  15     4401   4278   4991     22    407    858       C  
ATOM   3397  CZ3 TRP D  15     -25.124 -25.820  17.297  1.00 30.71           C  
ANISOU 3397  CZ3 TRP D  15     3738   3745   4185     -6    296    677       C  
ATOM   3398  CH2 TRP D  15     -24.301 -26.927  17.087  1.00 32.69           C  
ANISOU 3398  CH2 TRP D  15     4006   3894   4520      8    341    733       C  
ATOM   3399  N   GLY D  16     -30.117 -28.240  20.824  1.00 29.21           N  
ANISOU 3399  N   GLY D  16     3328   3646   4126   -141    545   1000       N  
ATOM   3400  CA  GLY D  16     -30.648 -29.594  20.638  1.00 31.28           C  
ANISOU 3400  CA  GLY D  16     3570   3779   4536   -211    622   1051       C  
ATOM   3401  C   GLY D  16     -31.487 -29.797  19.387  1.00 31.64           C  
ANISOU 3401  C   GLY D  16     3605   3743   4674   -305    602    923       C  
ATOM   3402  O   GLY D  16     -31.618 -30.900  18.922  1.00 32.42           O  
ANISOU 3402  O   GLY D  16     3709   3705   4904   -368    651    927       O  
ATOM   3403  N   LYS D  17     -32.053 -28.722  18.850  1.00 30.94           N  
ANISOU 3403  N   LYS D  17     3501   3742   4515   -312    531    810       N  
ATOM   3404  CA  LYS D  17     -32.920 -28.804  17.687  1.00 30.94           C  
ANISOU 3404  CA  LYS D  17     3477   3699   4578   -395    501    689       C  
ATOM   3405  C   LYS D  17     -32.265 -28.345  16.393  1.00 29.34           C  
ANISOU 3405  C   LYS D  17     3333   3460   4356   -387    428    564       C  
ATOM   3406  O   LYS D  17     -32.811 -28.525  15.317  1.00 29.57           O  
ANISOU 3406  O   LYS D  17     3352   3450   4435   -453    400    459       O  
ATOM   3407  CB  LYS D  17     -34.154 -27.960  17.943  1.00 31.19           C  
ANISOU 3407  CB  LYS D  17     3437   3863   4549   -404    476    660       C  
ATOM   3408  CG  LYS D  17     -34.940 -28.385  19.180  1.00 33.14           C  
ANISOU 3408  CG  LYS D  17     3617   4162   4813   -416    555    780       C  
ATOM   3409  CD  LYS D  17     -36.203 -27.578  19.370  1.00 32.70           C  
ANISOU 3409  CD  LYS D  17     3483   4238   4704   -422    537    746       C  
ATOM   3410  CE  LYS D  17     -37.062 -28.167  20.471  1.00 34.41           C  
ANISOU 3410  CE  LYS D  17     3624   4495   4956   -449    627    865       C  
ATOM   3411  NZ  LYS D  17     -38.379 -27.455  20.560  1.00 35.08           N  
ANISOU 3411  NZ  LYS D  17     3618   4706   5003   -459    615    827       N  
ATOM   3412  N   VAL D  18     -31.095 -27.748  16.496  1.00 27.79           N  
ANISOU 3412  N   VAL D  18     3192   3285   4083   -309    399    574       N  
ATOM   3413  CA  VAL D  18     -30.362 -27.330  15.303  1.00 27.15           C  
ANISOU 3413  CA  VAL D  18     3166   3168   3981   -296    341    471       C  
ATOM   3414  C   VAL D  18     -29.943 -28.513  14.363  1.00 27.90           C  
ANISOU 3414  C   VAL D  18     3299   3109   4191   -346    371    430       C  
ATOM   3415  O   VAL D  18     -29.417 -29.525  14.810  1.00 28.29           O  
ANISOU 3415  O   VAL D  18     3365   3066   4319   -342    437    513       O  
ATOM   3416  CB  VAL D  18     -29.133 -26.561  15.711  1.00 25.67           C  
ANISOU 3416  CB  VAL D  18     3022   3028   3703   -210    315    504       C  
ATOM   3417  CG1 VAL D  18     -28.311 -26.219  14.523  1.00 26.07           C  
ANISOU 3417  CG1 VAL D  18     3127   3036   3742   -197    271    415       C  
ATOM   3418  CG2 VAL D  18     -29.526 -25.349  16.465  1.00 24.10           C  
ANISOU 3418  CG2 VAL D  18     2797   2965   3393   -167    283    512       C  
ATOM   3419  N   ASN D  19     -30.246 -28.384  13.075  1.00 28.19           N  
ANISOU 3419  N   ASN D  19     3349   3125   4237   -389    326    304       N  
ATOM   3420  CA  ASN D  19     -29.616 -29.208  12.051  1.00 28.65           C  
ANISOU 3420  CA  ASN D  19     3460   3057   4368   -416    342    238       C  
ATOM   3421  C   ASN D  19     -28.287 -28.554  11.714  1.00 27.67           C  
ANISOU 3421  C   ASN D  19     3396   2947   4172   -335    312    231       C  
ATOM   3422  O   ASN D  19     -28.246 -27.545  10.986  1.00 28.06           O  
ANISOU 3422  O   ASN D  19     3459   3068   4136   -315    247    155       O  
ATOM   3423  CB  ASN D  19     -30.481 -29.282  10.792  1.00 28.79           C  
ANISOU 3423  CB  ASN D  19     3465   3070   4404   -495    299     98       C  
ATOM   3424  CG  ASN D  19     -29.931 -30.277   9.800  1.00 31.83           C  
ANISOU 3424  CG  ASN D  19     3905   3317   4871   -532    327     21       C  
ATOM   3425  OD1 ASN D  19     -28.833 -30.095   9.256  1.00 32.46           O  
ANISOU 3425  OD1 ASN D  19     4047   3369   4917   -476    320     -3       O  
ATOM   3426  ND2 ASN D  19     -30.650 -31.391   9.616  1.00 34.68           N  
ANISOU 3426  ND2 ASN D  19     4245   3583   5348   -628    370    -16       N  
ATOM   3427  N   VAL D  20     -27.212 -29.093  12.255  1.00 27.52           N  
ANISOU 3427  N   VAL D  20     3406   2866   4186   -285    362    318       N  
ATOM   3428  CA  VAL D  20     -25.877 -28.483  12.162  1.00 27.55           C  
ANISOU 3428  CA  VAL D  20     3448   2895   4124   -206    340    334       C  
ATOM   3429  C   VAL D  20     -25.393 -28.350  10.711  1.00 28.10           C  
ANISOU 3429  C   VAL D  20     3567   2924   4186   -210    312    218       C  
ATOM   3430  O   VAL D  20     -24.817 -27.336  10.302  1.00 28.15           O  
ANISOU 3430  O   VAL D  20     3593   2997   4107   -169    264    186       O  
ATOM   3431  CB  VAL D  20     -24.862 -29.319  12.926  1.00 27.58           C  
ANISOU 3431  CB  VAL D  20     3463   2833   4183   -154    404    452       C  
ATOM   3432  CG1 VAL D  20     -23.486 -28.755  12.811  1.00 27.44           C  
ANISOU 3432  CG1 VAL D  20     3472   2849   4106    -80    381    467       C  
ATOM   3433  CG2 VAL D  20     -25.253 -29.407  14.341  1.00 28.74           C  
ANISOU 3433  CG2 VAL D  20     3565   3038   4318   -140    430    574       C  
ATOM   3434  N   ALA D  21     -25.630 -29.385   9.921  1.00 29.07           N  
ANISOU 3434  N   ALA D  21     3712   2935   4400   -264    348    152       N  
ATOM   3435  CA  ALA D  21     -25.101 -29.422   8.574  1.00 28.58           C  
ANISOU 3435  CA  ALA D  21     3700   2830   4329   -263    335     45       C  
ATOM   3436  C   ALA D  21     -25.777 -28.341   7.731  1.00 27.18           C  
ANISOU 3436  C   ALA D  21     3514   2759   4052   -284    254    -54       C  
ATOM   3437  O   ALA D  21     -25.135 -27.559   7.029  1.00 27.30           O  
ANISOU 3437  O   ALA D  21     3561   2820   3991   -242    220    -92       O  
ATOM   3438  CB  ALA D  21     -25.264 -30.842   7.990  1.00 29.43           C  
ANISOU 3438  CB  ALA D  21     3835   2787   4559   -321    397    -14       C  
ATOM   3439  N   GLU D  22     -27.076 -28.231   7.892  1.00 26.89           N  
ANISOU 3439  N   GLU D  22     3429   2772   4015   -342    227    -78       N  
ATOM   3440  CA  GLU D  22     -27.863 -27.207   7.210  1.00 25.80           C  
ANISOU 3440  CA  GLU D  22     3270   2746   3786   -354    151   -154       C  
ATOM   3441  C   GLU D  22     -27.541 -25.772   7.644  1.00 22.89           C  
ANISOU 3441  C   GLU D  22     2899   2486   3312   -280    109   -103       C  
ATOM   3442  O   GLU D  22     -27.390 -24.891   6.792  1.00 22.13           O  
ANISOU 3442  O   GLU D  22     2825   2445   3137   -253     62   -156       O  
ATOM   3443  CB  GLU D  22     -29.344 -27.517   7.418  1.00 27.02           C  
ANISOU 3443  CB  GLU D  22     3357   2932   3978   -431    139   -178       C  
ATOM   3444  CG  GLU D  22     -30.290 -26.772   6.516  1.00 30.96           C  
ANISOU 3444  CG  GLU D  22     3824   3536   4402   -454     64   -269       C  
ATOM   3445  CD  GLU D  22     -31.746 -27.128   6.809  1.00 36.31           C  
ANISOU 3445  CD  GLU D  22     4418   4253   5125   -533     56   -285       C  
ATOM   3446  OE1 GLU D  22     -32.585 -26.186   6.788  1.00 37.60           O  
ANISOU 3446  OE1 GLU D  22     4530   4540   5218   -517      1   -290       O  
ATOM   3447  OE2 GLU D  22     -32.028 -28.340   7.047  1.00 38.00           O  
ANISOU 3447  OE2 GLU D  22     4618   4370   5452   -609    108   -288       O  
ATOM   3448  N   CYS D  23     -27.439 -25.529   8.947  1.00 21.02           N  
ANISOU 3448  N   CYS D  23     2638   2277   3073   -249    128     -2       N  
ATOM   3449  CA  CYS D  23     -27.286 -24.170   9.439  1.00 19.83           C  
ANISOU 3449  CA  CYS D  23     2481   2224   2828   -192     89     31       C  
ATOM   3450  C   CYS D  23     -25.833 -23.802   9.320  1.00 18.48           C  
ANISOU 3450  C   CYS D  23     2360   2035   2628   -137     94     53       C  
ATOM   3451  O   CYS D  23     -25.518 -22.659   9.059  1.00 15.11           O  
ANISOU 3451  O   CYS D  23     1951   1664   2128   -100     56     37       O  
ATOM   3452  CB  CYS D  23     -27.784 -23.972  10.878  1.00 19.73           C  
ANISOU 3452  CB  CYS D  23     2423   2267   2807   -181    105    115       C  
ATOM   3453  SG  CYS D  23     -29.536 -24.139  11.038  1.00 23.38           S  
ANISOU 3453  SG  CYS D  23     2813   2778   3291   -239     99     94       S  
ATOM   3454  N   GLY D  24     -24.954 -24.795   9.423  1.00 19.11           N  
ANISOU 3454  N   GLY D  24     2459   2029   2772   -131    143     88       N  
ATOM   3455  CA  GLY D  24     -23.527 -24.570   9.140  1.00 19.30           C  
ANISOU 3455  CA  GLY D  24     2520   2034   2778    -81    151    104       C  
ATOM   3456  C   GLY D  24     -23.218 -24.157   7.718  1.00 19.13           C  
ANISOU 3456  C   GLY D  24     2540   2009   2720    -78    128     16       C  
ATOM   3457  O   GLY D  24     -22.494 -23.217   7.488  1.00 19.26           O  
ANISOU 3457  O   GLY D  24     2574   2067   2678    -41    106     19       O  
ATOM   3458  N   ALA D  25     -23.792 -24.861   6.764  1.00 20.64           N  
ANISOU 3458  N   ALA D  25     2745   2153   2945   -121    134    -63       N  
ATOM   3459  CA  ALA D  25     -23.644 -24.515   5.353  1.00 22.01           C  
ANISOU 3459  CA  ALA D  25     2956   2339   3069   -119    110   -152       C  
ATOM   3460  C   ALA D  25     -24.246 -23.170   5.040  1.00 21.87           C  
ANISOU 3460  C   ALA D  25     2929   2424   2957   -107     48   -173       C  
ATOM   3461  O   ALA D  25     -23.660 -22.368   4.273  1.00 22.57           O  
ANISOU 3461  O   ALA D  25     3050   2544   2982    -72     31   -191       O  
ATOM   3462  CB  ALA D  25     -24.280 -25.614   4.427  1.00 21.99           C  
ANISOU 3462  CB  ALA D  25     2966   2275   3114   -179    124   -250       C  
ATOM   3463  N   GLU D  26     -25.433 -22.916   5.574  1.00 22.38           N  
ANISOU 3463  N   GLU D  26     2949   2539   3015   -132     19   -168       N  
ATOM   3464  CA  GLU D  26     -26.028 -21.592   5.374  1.00 21.69           C  
ANISOU 3464  CA  GLU D  26     2851   2545   2845   -106    -34   -176       C  
ATOM   3465  C   GLU D  26     -25.083 -20.512   5.915  1.00 19.80           C  
ANISOU 3465  C   GLU D  26     2632   2326   2564    -51    -33   -116       C  
ATOM   3466  O   GLU D  26     -24.881 -19.467   5.276  1.00 20.07           O  
ANISOU 3466  O   GLU D  26     2692   2398   2537    -18    -58   -129       O  
ATOM   3467  CB  GLU D  26     -27.416 -21.465   6.026  1.00 21.71           C  
ANISOU 3467  CB  GLU D  26     2792   2604   2851   -132    -57   -168       C  
ATOM   3468  CG  GLU D  26     -28.580 -22.015   5.156  1.00 25.68           C  
ANISOU 3468  CG  GLU D  26     3263   3131   3363   -187    -85   -248       C  
ATOM   3469  CD  GLU D  26     -29.033 -21.022   4.054  1.00 28.94           C  
ANISOU 3469  CD  GLU D  26     3680   3632   3685   -157   -143   -296       C  
ATOM   3470  OE1 GLU D  26     -28.375 -19.970   3.924  1.00 26.69           O  
ANISOU 3470  OE1 GLU D  26     3433   3366   3343    -96   -150   -264       O  
ATOM   3471  OE2 GLU D  26     -30.040 -21.279   3.317  1.00 33.34           O  
ANISOU 3471  OE2 GLU D  26     4199   4241   4226   -195   -182   -361       O  
ATOM   3472  N   ALA D  27     -24.556 -20.721   7.109  1.00 17.68           N  
ANISOU 3472  N   ALA D  27     2351   2038   2329    -42     -6    -50       N  
ATOM   3473  CA  ALA D  27     -23.856 -19.641   7.790  1.00 16.91           C  
ANISOU 3473  CA  ALA D  27     2261   1975   2189     -3    -14     -4       C  
ATOM   3474  C   ALA D  27     -22.574 -19.234   7.016  1.00 16.79           C  
ANISOU 3474  C   ALA D  27     2287   1937   2155     22     -7    -10       C  
ATOM   3475  O   ALA D  27     -22.301 -18.044   6.802  1.00 17.05           O  
ANISOU 3475  O   ALA D  27     2339   2000   2140     45    -26    -12       O  
ATOM   3476  CB  ALA D  27     -23.557 -20.052   9.212  1.00 16.23           C  
ANISOU 3476  CB  ALA D  27     2145   1889   2131      0      9     65       C  
ATOM   3477  N   LEU D  28     -21.849 -20.243   6.526  1.00 16.92           N  
ANISOU 3477  N   LEU D  28     2317   1895   2216     17     28    -16       N  
ATOM   3478  CA  LEU D  28     -20.589 -20.032   5.820  1.00 17.14           C  
ANISOU 3478  CA  LEU D  28     2375   1904   2234     42     47    -15       C  
ATOM   3479  C   LEU D  28     -20.748 -19.539   4.400  1.00 16.23           C  
ANISOU 3479  C   LEU D  28     2296   1803   2068     48     34    -73       C  
ATOM   3480  O   LEU D  28     -19.976 -18.662   3.964  1.00 14.70           O  
ANISOU 3480  O   LEU D  28     2124   1625   1838     72     36    -61       O  
ATOM   3481  CB  LEU D  28     -19.711 -21.289   5.809  1.00 17.87           C  
ANISOU 3481  CB  LEU D  28     2468   1930   2391     48     98      4       C  
ATOM   3482  CG  LEU D  28     -18.300 -20.946   5.313  1.00 21.96           C  
ANISOU 3482  CG  LEU D  28     3001   2444   2899     81    121     21       C  
ATOM   3483  CD1 LEU D  28     -17.494 -20.045   6.347  1.00 20.94           C  
ANISOU 3483  CD1 LEU D  28     2841   2363   2753     95    106     87       C  
ATOM   3484  CD2 LEU D  28     -17.552 -22.275   4.882  1.00 24.03           C  
ANISOU 3484  CD2 LEU D  28     3273   2632   3225     97    181     18       C  
ATOM   3485  N   ALA D  29     -21.725 -20.090   3.686  1.00 15.62           N  
ANISOU 3485  N   ALA D  29     2224   1726   1986     24     21   -134       N  
ATOM   3486  CA  ALA D  29     -22.114 -19.541   2.413  1.00 15.41           C  
ANISOU 3486  CA  ALA D  29     2224   1741   1892     33     -4   -186       C  
ATOM   3487  C   ALA D  29     -22.448 -18.033   2.506  1.00 15.13           C  
ANISOU 3487  C   ALA D  29     2188   1764   1796     62    -40   -156       C  
ATOM   3488  O   ALA D  29     -21.967 -17.236   1.677  1.00 13.57           O  
ANISOU 3488  O   ALA D  29     2023   1586   1548     92    -38   -151       O  
ATOM   3489  CB  ALA D  29     -23.286 -20.374   1.766  1.00 16.25           C  
ANISOU 3489  CB  ALA D  29     2318   1856   1998     -7    -26   -264       C  
ATOM   3490  N   ARG D  30     -23.203 -17.641   3.530  1.00 14.72           N  
ANISOU 3490  N   ARG D  30     2104   1736   1754     58    -62   -131       N  
ATOM   3491  CA  ARG D  30     -23.561 -16.245   3.737  1.00 14.66           C  
ANISOU 3491  CA  ARG D  30     2099   1770   1702     89    -87   -106       C  
ATOM   3492  C   ARG D  30     -22.388 -15.404   4.139  1.00 15.04           C  
ANISOU 3492  C   ARG D  30     2170   1794   1752    108    -66    -63       C  
ATOM   3493  O   ARG D  30     -22.262 -14.271   3.707  1.00 16.91           O  
ANISOU 3493  O   ARG D  30     2433   2040   1952    135    -71    -50       O  
ATOM   3494  CB  ARG D  30     -24.679 -16.098   4.778  1.00 15.51           C  
ANISOU 3494  CB  ARG D  30     2164   1909   1820     83   -108    -96       C  
ATOM   3495  CG  ARG D  30     -26.007 -16.587   4.313  1.00 16.54           C  
ANISOU 3495  CG  ARG D  30     2260   2082   1942     66   -136   -137       C  
ATOM   3496  CD  ARG D  30     -27.079 -16.677   5.462  1.00 15.85           C  
ANISOU 3496  CD  ARG D  30     2117   2026   1878     53   -144   -121       C  
ATOM   3497  NE  ARG D  30     -28.168 -17.418   4.879  1.00 13.70           N  
ANISOU 3497  NE  ARG D  30     1804   1788   1612     19   -167   -167       N  
ATOM   3498  CZ  ARG D  30     -29.203 -16.911   4.228  1.00 16.36           C  
ANISOU 3498  CZ  ARG D  30     2114   2197   1905     36   -208   -190       C  
ATOM   3499  NH1 ARG D  30     -29.427 -15.598   4.226  1.00 15.32           N  
ANISOU 3499  NH1 ARG D  30     1991   2105   1725     99   -223   -161       N  
ATOM   3500  NH2 ARG D  30     -30.086 -17.747   3.641  1.00 14.24           N  
ANISOU 3500  NH2 ARG D  30     1801   1963   1645    -11   -233   -244       N  
ATOM   3501  N   LEU D  31     -21.479 -15.925   4.945  1.00 16.01           N  
ANISOU 3501  N   LEU D  31     2280   1886   1918     92    -42    -36       N  
ATOM   3502  CA  LEU D  31     -20.310 -15.137   5.258  1.00 14.90           C  
ANISOU 3502  CA  LEU D  31     2151   1734   1779    100    -27     -3       C  
ATOM   3503  C   LEU D  31     -19.613 -14.755   3.977  1.00 15.23           C  
ANISOU 3503  C   LEU D  31     2228   1763   1796    115     -8     -7       C  
ATOM   3504  O   LEU D  31     -19.180 -13.587   3.790  1.00 16.49           O  
ANISOU 3504  O   LEU D  31     2409   1920   1938    126     -4     12       O  
ATOM   3505  CB  LEU D  31     -19.369 -15.923   6.148  1.00 15.60           C  
ANISOU 3505  CB  LEU D  31     2210   1805   1911     86     -6     29       C  
ATOM   3506  CG  LEU D  31     -18.088 -15.223   6.607  1.00 16.57           C  
ANISOU 3506  CG  LEU D  31     2326   1931   2039     84      3     60       C  
ATOM   3507  CD1 LEU D  31     -18.423 -14.044   7.544  1.00 18.58           C  
ANISOU 3507  CD1 LEU D  31     2578   2211   2270     78    -24     59       C  
ATOM   3508  CD2 LEU D  31     -17.129 -16.210   7.289  1.00 15.58           C  
ANISOU 3508  CD2 LEU D  31     2162   1803   1955     82     23     99       C  
ATOM   3509  N   LEU D  32     -19.439 -15.726   3.087  1.00 14.06           N  
ANISOU 3509  N   LEU D  32     2089   1602   1650    115     11    -32       N  
ATOM   3510  CA  LEU D  32     -18.634 -15.493   1.913  1.00 13.39           C  
ANISOU 3510  CA  LEU D  32     2037   1513   1539    133     40    -31       C  
ATOM   3511  C   LEU D  32     -19.332 -14.626   0.889  1.00 13.72           C  
ANISOU 3511  C   LEU D  32     2110   1590   1513    158     21    -42       C  
ATOM   3512  O   LEU D  32     -18.679 -14.030   0.031  1.00 15.22           O  
ANISOU 3512  O   LEU D  32     2329   1783   1672    178     47    -21       O  
ATOM   3513  CB  LEU D  32     -18.255 -16.846   1.262  1.00 15.34           C  
ANISOU 3513  CB  LEU D  32     2288   1736   1804    131     72    -65       C  
ATOM   3514  CG  LEU D  32     -17.270 -17.753   2.021  1.00 15.34           C  
ANISOU 3514  CG  LEU D  32     2259   1695   1873    126    107    -38       C  
ATOM   3515  CD1 LEU D  32     -17.037 -19.094   1.317  1.00 17.76           C  
ANISOU 3515  CD1 LEU D  32     2579   1963   2204    131    146    -80       C  
ATOM   3516  CD2 LEU D  32     -15.993 -17.059   2.068  1.00 19.80           C  
ANISOU 3516  CD2 LEU D  32     2817   2264   2443    137    132      9       C  
ATOM   3517  N   ILE D  33     -20.653 -14.631   0.897  1.00 13.68           N  
ANISOU 3517  N   ILE D  33     2096   1617   1483    160    -19    -69       N  
ATOM   3518  CA  ILE D  33     -21.407 -13.940  -0.105  1.00 15.57           C  
ANISOU 3518  CA  ILE D  33     2357   1906   1654    192    -42    -75       C  
ATOM   3519  C   ILE D  33     -21.819 -12.527   0.413  1.00 16.30           C  
ANISOU 3519  C   ILE D  33     2454   2001   1739    219    -56    -30       C  
ATOM   3520  O   ILE D  33     -21.677 -11.580  -0.278  1.00 16.77           O  
ANISOU 3520  O   ILE D  33     2545   2067   1762    254    -46      3       O  
ATOM   3521  CB  ILE D  33     -22.655 -14.773  -0.560  1.00 16.36           C  
ANISOU 3521  CB  ILE D  33     2435   2055   1725    181    -81   -135       C  
ATOM   3522  CG1 ILE D  33     -22.237 -16.036  -1.316  1.00 14.36           C  
ANISOU 3522  CG1 ILE D  33     2194   1791   1473    157    -61   -192       C  
ATOM   3523  CG2 ILE D  33     -23.519 -13.954  -1.517  1.00 16.78           C  
ANISOU 3523  CG2 ILE D  33     2498   2181   1697    223   -115   -130       C  
ATOM   3524  CD1 ILE D  33     -23.397 -17.011  -1.525  1.00 14.54           C  
ANISOU 3524  CD1 ILE D  33     2188   1845   1493    122    -97   -266       C  
ATOM   3525  N   VAL D  34     -22.299 -12.401   1.651  1.00 17.55           N  
ANISOU 3525  N   VAL D  34     2583   2148   1935    206    -72    -28       N  
ATOM   3526  CA  VAL D  34     -22.644 -11.089   2.222  1.00 17.39           C  
ANISOU 3526  CA  VAL D  34     2572   2119   1915    233    -77      2       C  
ATOM   3527  C   VAL D  34     -21.369 -10.248   2.474  1.00 17.53           C  
ANISOU 3527  C   VAL D  34     2619   2081   1961    223    -41     35       C  
ATOM   3528  O   VAL D  34     -21.392  -9.047   2.269  1.00 17.73           O  
ANISOU 3528  O   VAL D  34     2675   2083   1979    251    -29     64       O  
ATOM   3529  CB  VAL D  34     -23.408 -11.269   3.518  1.00 18.42           C  
ANISOU 3529  CB  VAL D  34     2664   2260   2074    220    -97    -13       C  
ATOM   3530  CG1 VAL D  34     -23.765  -9.860   4.181  1.00 18.98           C  
ANISOU 3530  CG1 VAL D  34     2750   2314   2146    253    -95      7       C  
ATOM   3531  CG2 VAL D  34     -24.658 -12.157   3.283  1.00 15.27           C  
ANISOU 3531  CG2 VAL D  34     2224   1917   1659    216   -129    -44       C  
ATOM   3532  N   TYR D  35     -20.230 -10.899   2.791  1.00 16.55           N  
ANISOU 3532  N   TYR D  35     2483   1934   1872    185    -19     34       N  
ATOM   3533  CA  TYR D  35     -19.011 -10.197   3.107  1.00 15.84           C  
ANISOU 3533  CA  TYR D  35     2403   1803   1813    164     10     60       C  
ATOM   3534  C   TYR D  35     -17.873 -10.733   2.285  1.00 15.84           C  
ANISOU 3534  C   TYR D  35     2405   1797   1817    155     45     75       C  
ATOM   3535  O   TYR D  35     -16.995 -11.447   2.811  1.00 16.50           O  
ANISOU 3535  O   TYR D  35     2457   1877   1937    128     56     76       O  
ATOM   3536  CB  TYR D  35     -18.728 -10.280   4.615  1.00 15.33           C  
ANISOU 3536  CB  TYR D  35     2304   1734   1785    130     -3     49       C  
ATOM   3537  CG  TYR D  35     -19.847  -9.732   5.455  1.00 17.22           C  
ANISOU 3537  CG  TYR D  35     2543   1985   2016    144    -29     31       C  
ATOM   3538  CD1 TYR D  35     -20.254  -8.395   5.348  1.00 22.27           C  
ANISOU 3538  CD1 TYR D  35     3218   2595   2648    169    -23     35       C  
ATOM   3539  CD2 TYR D  35     -20.532 -10.532   6.331  1.00 18.80           C  
ANISOU 3539  CD2 TYR D  35     2707   2220   2217    138    -51     14       C  
ATOM   3540  CE1 TYR D  35     -21.287  -7.895   6.144  1.00 21.52           C  
ANISOU 3540  CE1 TYR D  35     3121   2509   2546    192    -39     15       C  
ATOM   3541  CE2 TYR D  35     -21.553 -10.051   7.104  1.00 17.71           C  
ANISOU 3541  CE2 TYR D  35     2562   2099   2066    156    -67     -1       C  
ATOM   3542  CZ  TYR D  35     -21.930  -8.751   7.014  1.00 20.10           C  
ANISOU 3542  CZ  TYR D  35     2900   2377   2361    185    -62     -4       C  
ATOM   3543  OH  TYR D  35     -22.975  -8.313   7.796  1.00 22.70           O  
ANISOU 3543  OH  TYR D  35     3220   2726   2679    211    -71    -22       O  
ATOM   3544  N   PRO D  36     -17.849 -10.373   0.985  1.00 15.62           N  
ANISOU 3544  N   PRO D  36     2412   1775   1748    184     66     93       N  
ATOM   3545  CA  PRO D  36     -17.046 -11.150   0.062  1.00 16.42           C  
ANISOU 3545  CA  PRO D  36     2515   1887   1835    187    100     94       C  
ATOM   3546  C   PRO D  36     -15.550 -11.029   0.266  1.00 16.88           C  
ANISOU 3546  C   PRO D  36     2556   1919   1940    159    142    125       C  
ATOM   3547  O   PRO D  36     -14.803 -11.814  -0.306  1.00 17.28           O  
ANISOU 3547  O   PRO D  36     2597   1979   1990    164    176    124       O  
ATOM   3548  CB  PRO D  36     -17.433 -10.600  -1.333  1.00 17.14           C  
ANISOU 3548  CB  PRO D  36     2649   2005   1856    230    112    114       C  
ATOM   3549  CG  PRO D  36     -18.374  -9.545  -1.136  1.00 14.58           C  
ANISOU 3549  CG  PRO D  36     2343   1678   1518    254     86    133       C  
ATOM   3550  CD  PRO D  36     -18.553  -9.278   0.299  1.00 16.29           C  
ANISOU 3550  CD  PRO D  36     2535   1862   1791    225     64    119       C  
ATOM   3551  N   TRP D  37     -15.090 -10.065   1.051  1.00 15.86           N  
ANISOU 3551  N   TRP D  37     2416   1759   1850    130    144    147       N  
ATOM   3552  CA  TRP D  37     -13.647 -10.015   1.275  1.00 16.51           C  
ANISOU 3552  CA  TRP D  37     2464   1829   1978     95    179    173       C  
ATOM   3553  C   TRP D  37     -13.195 -11.277   2.071  1.00 16.24           C  
ANISOU 3553  C   TRP D  37     2376   1818   1975     83    167    156       C  
ATOM   3554  O   TRP D  37     -12.026 -11.673   2.013  1.00 15.72           O  
ANISOU 3554  O   TRP D  37     2272   1760   1939     73    199    178       O  
ATOM   3555  CB  TRP D  37     -13.239  -8.741   2.009  1.00 16.18           C  
ANISOU 3555  CB  TRP D  37     2419   1752   1977     52    178    186       C  
ATOM   3556  CG  TRP D  37     -13.891  -8.584   3.346  1.00 15.13           C  
ANISOU 3556  CG  TRP D  37     2273   1619   1857     34    129    149       C  
ATOM   3557  CD1 TRP D  37     -13.426  -9.033   4.498  1.00 17.69           C  
ANISOU 3557  CD1 TRP D  37     2546   1969   2207      2    105    133       C  
ATOM   3558  CD2 TRP D  37     -15.126  -7.889   3.641  1.00 15.45           C  
ANISOU 3558  CD2 TRP D  37     2351   1642   1877     56    103    129       C  
ATOM   3559  NE1 TRP D  37     -14.283  -8.688   5.542  1.00 19.91           N  
ANISOU 3559  NE1 TRP D  37     2833   2253   2480     -3     65     98       N  
ATOM   3560  CE2 TRP D  37     -15.326  -7.967   5.030  1.00 17.49           C  
ANISOU 3560  CE2 TRP D  37     2580   1915   2150     30     66     94       C  
ATOM   3561  CE3 TRP D  37     -16.051  -7.180   2.871  1.00 17.67           C  
ANISOU 3561  CE3 TRP D  37     2683   1902   2128    100    109    142       C  
ATOM   3562  CZ2 TRP D  37     -16.422  -7.381   5.670  1.00 18.33           C  
ANISOU 3562  CZ2 TRP D  37     2709   2012   2242     47     42     65       C  
ATOM   3563  CZ3 TRP D  37     -17.173  -6.588   3.526  1.00 16.57           C  
ANISOU 3563  CZ3 TRP D  37     2562   1751   1981    121     81    119       C  
ATOM   3564  CH2 TRP D  37     -17.326  -6.689   4.896  1.00 17.23           C  
ANISOU 3564  CH2 TRP D  37     2618   1846   2083     93     51     77       C  
ATOM   3565  N   THR D  38     -14.101 -11.888   2.832  1.00 14.69           N  
ANISOU 3565  N   THR D  38     2172   1632   1776     87    126    126       N  
ATOM   3566  CA  THR D  38     -13.686 -13.039   3.591  1.00 14.42           C  
ANISOU 3566  CA  THR D  38     2091   1613   1774     82    122    127       C  
ATOM   3567  C   THR D  38     -13.287 -14.215   2.685  1.00 14.65           C  
ANISOU 3567  C   THR D  38     2121   1638   1806    111    161    124       C  
ATOM   3568  O   THR D  38     -12.691 -15.162   3.187  1.00 14.78           O  
ANISOU 3568  O   THR D  38     2099   1657   1861    116    173    138       O  
ATOM   3569  CB  THR D  38     -14.788 -13.542   4.476  1.00 13.79           C  
ANISOU 3569  CB  THR D  38     2005   1544   1691     83     81    104       C  
ATOM   3570  OG1 THR D  38     -15.883 -13.902   3.627  1.00 16.97           O  
ANISOU 3570  OG1 THR D  38     2444   1942   2061    106     76     73       O  
ATOM   3571  CG2 THR D  38     -15.203 -12.499   5.499  1.00 13.86           C  
ANISOU 3571  CG2 THR D  38     2011   1561   1693     62     47     97       C  
ATOM   3572  N   GLN D  39     -13.630 -14.181   1.388  1.00 14.58           N  
ANISOU 3572  N   GLN D  39     2157   1626   1754    135    182    106       N  
ATOM   3573  CA  GLN D  39     -13.204 -15.226   0.434  1.00 15.09           C  
ANISOU 3573  CA  GLN D  39     2232   1688   1814    162    226     89       C  
ATOM   3574  C   GLN D  39     -11.705 -15.354   0.353  1.00 15.93           C  
ANISOU 3574  C   GLN D  39     2301   1795   1957    168    278    130       C  
ATOM   3575  O   GLN D  39     -11.187 -16.394  -0.023  1.00 17.17           O  
ANISOU 3575  O   GLN D  39     2449   1942   2131    194    318    121       O  
ATOM   3576  CB  GLN D  39     -13.781 -14.981  -0.973  1.00 15.63           C  
ANISOU 3576  CB  GLN D  39     2355   1774   1810    187    236     62       C  
ATOM   3577  CG  GLN D  39     -15.324 -15.117  -1.042  1.00 16.45           C  
ANISOU 3577  CG  GLN D  39     2483   1891   1874    187    183     14       C  
ATOM   3578  CD  GLN D  39     -15.930 -14.634  -2.338  1.00 17.57           C  
ANISOU 3578  CD  GLN D  39     2671   2074   1933    214    180     -2       C  
ATOM   3579  OE1 GLN D  39     -17.064 -14.117  -2.352  1.00 18.56           O  
ANISOU 3579  OE1 GLN D  39     2808   2224   2021    219    134    -11       O  
ATOM   3580  NE2 GLN D  39     -15.200 -14.805  -3.431  1.00 18.67           N  
ANISOU 3580  NE2 GLN D  39     2832   2229   2034    238    230     -1       N  
ATOM   3581  N   ARG D  40     -10.987 -14.298   0.696  1.00 16.90           N  
ANISOU 3581  N   ARG D  40     2398   1927   2096    141    280    172       N  
ATOM   3582  CA  ARG D  40      -9.544 -14.340   0.623  1.00 18.33           C  
ANISOU 3582  CA  ARG D  40     2529   2121   2314    140    328    214       C  
ATOM   3583  C   ARG D  40      -8.958 -15.495   1.428  1.00 18.55           C  
ANISOU 3583  C   ARG D  40     2499   2156   2394    155    332    226       C  
ATOM   3584  O   ARG D  40      -7.927 -16.054   1.070  1.00 18.60           O  
ANISOU 3584  O   ARG D  40     2470   2171   2427    181    384    251       O  
ATOM   3585  CB  ARG D  40      -8.978 -13.049   1.173  1.00 18.65           C  
ANISOU 3585  CB  ARG D  40     2541   2169   2378     90    316    247       C  
ATOM   3586  CG  ARG D  40      -7.474 -12.975   1.117  1.00 21.06           C  
ANISOU 3586  CG  ARG D  40     2778   2498   2725     76    362    292       C  
ATOM   3587  CD  ARG D  40      -6.972 -11.568   1.591  1.00 25.31           C  
ANISOU 3587  CD  ARG D  40     3290   3035   3290      8    349    313       C  
ATOM   3588  NE  ARG D  40      -5.546 -11.551   1.948  1.00 29.16           N  
ANISOU 3588  NE  ARG D  40     3686   3563   3831    -22    372    351       N  
ATOM   3589  CZ  ARG D  40      -5.067 -11.453   3.198  1.00 32.48           C  
ANISOU 3589  CZ  ARG D  40     4035   4021   4286    -65    325    350       C  
ATOM   3590  NH1 ARG D  40      -5.893 -11.356   4.256  1.00 33.21           N  
ANISOU 3590  NH1 ARG D  40     4143   4113   4363    -81    258    314       N  
ATOM   3591  NH2 ARG D  40      -3.737 -11.437   3.400  1.00 31.62           N  
ANISOU 3591  NH2 ARG D  40     3832   3962   4221    -91    346    387       N  
ATOM   3592  N   PHE D  41      -9.602 -15.793   2.556  1.00 18.42           N  
ANISOU 3592  N   PHE D  41     2469   2138   2391    142    280    218       N  
ATOM   3593  CA  PHE D  41      -9.161 -16.865   3.465  1.00 18.13           C  
ANISOU 3593  CA  PHE D  41     2378   2109   2401    162    280    245       C  
ATOM   3594  C   PHE D  41      -9.439 -18.288   3.005  1.00 18.08           C  
ANISOU 3594  C   PHE D  41     2396   2060   2414    209    317    225       C  
ATOM   3595  O   PHE D  41      -8.843 -19.207   3.566  1.00 18.05           O  
ANISOU 3595  O   PHE D  41     2347   2053   2459    239    337    263       O  
ATOM   3596  CB  PHE D  41      -9.800 -16.641   4.826  1.00 17.18           C  
ANISOU 3596  CB  PHE D  41     2240   2009   2279    134    217    248       C  
ATOM   3597  CG  PHE D  41      -9.371 -15.351   5.467  1.00 16.92           C  
ANISOU 3597  CG  PHE D  41     2177   2016   2237     85    183    258       C  
ATOM   3598  CD1 PHE D  41      -8.084 -15.201   5.949  1.00 17.85           C  
ANISOU 3598  CD1 PHE D  41     2218   2180   2383     71    187    299       C  
ATOM   3599  CD2 PHE D  41     -10.235 -14.286   5.561  1.00 15.64           C  
ANISOU 3599  CD2 PHE D  41     2058   1841   2042     53    149    223       C  
ATOM   3600  CE1 PHE D  41      -7.697 -13.992   6.538  1.00 20.15           C  
ANISOU 3600  CE1 PHE D  41     2481   2504   2670     12    154    292       C  
ATOM   3601  CE2 PHE D  41      -9.855 -13.105   6.122  1.00 15.15           C  
ANISOU 3601  CE2 PHE D  41     1978   1799   1980      4    125    220       C  
ATOM   3602  CZ  PHE D  41      -8.599 -12.957   6.632  1.00 14.62           C  
ANISOU 3602  CZ  PHE D  41     1837   1776   1941    -23    125    249       C  
ATOM   3603  N   PHE D  42     -10.281 -18.444   1.961  1.00 17.40           N  
ANISOU 3603  N   PHE D  42     2378   1943   2291    215    328    168       N  
ATOM   3604  CA  PHE D  42     -10.880 -19.722   1.572  1.00 17.32           C  
ANISOU 3604  CA  PHE D  42     2403   1884   2296    240    350    122       C  
ATOM   3605  C   PHE D  42     -10.673 -20.061   0.138  1.00 17.79           C  
ANISOU 3605  C   PHE D  42     2506   1928   2326    269    404     75       C  
ATOM   3606  O   PHE D  42     -11.402 -20.899  -0.392  1.00 19.45           O  
ANISOU 3606  O   PHE D  42     2761   2100   2531    274    413     11       O  
ATOM   3607  CB  PHE D  42     -12.401 -19.707   1.802  1.00 16.55           C  
ANISOU 3607  CB  PHE D  42     2341   1775   2174    210    297     76       C  
ATOM   3608  CG  PHE D  42     -12.779 -19.615   3.236  1.00 16.94           C  
ANISOU 3608  CG  PHE D  42     2352   1836   2248    188    252    114       C  
ATOM   3609  CD1 PHE D  42     -12.784 -20.747   4.025  1.00 20.37           C  
ANISOU 3609  CD1 PHE D  42     2762   2239   2741    201    265    140       C  
ATOM   3610  CD2 PHE D  42     -13.109 -18.401   3.805  1.00 14.70           C  
ANISOU 3610  CD2 PHE D  42     2060   1594   1930    158    203    126       C  
ATOM   3611  CE1 PHE D  42     -13.083 -20.662   5.358  1.00 20.07           C  
ANISOU 3611  CE1 PHE D  42     2687   2226   2714    187    228    184       C  
ATOM   3612  CE2 PHE D  42     -13.418 -18.315   5.111  1.00 17.78           C  
ANISOU 3612  CE2 PHE D  42     2418   2006   2332    142    166    154       C  
ATOM   3613  CZ  PHE D  42     -13.414 -19.452   5.910  1.00 18.49           C  
ANISOU 3613  CZ  PHE D  42     2478   2078   2467    157    177    186       C  
ATOM   3614  N   THR D  43      -9.700 -19.439  -0.515  1.00 18.08           N  
ANISOU 3614  N   THR D  43     2532   1997   2342    283    443    102       N  
ATOM   3615  CA  THR D  43      -9.381 -19.752  -1.889  1.00 17.28           C  
ANISOU 3615  CA  THR D  43     2470   1895   2202    318    504     63       C  
ATOM   3616  C   THR D  43      -9.031 -21.213  -2.136  1.00 16.61           C  
ANISOU 3616  C   THR D  43     2391   1757   2164    364    564     30       C  
ATOM   3617  O   THR D  43      -9.258 -21.718  -3.214  1.00 17.13           O  
ANISOU 3617  O   THR D  43     2510   1808   2190    385    600    -40       O  
ATOM   3618  CB  THR D  43      -8.228 -18.879  -2.425  1.00 18.70           C  
ANISOU 3618  CB  THR D  43     2622   2120   2363    328    549    116       C  
ATOM   3619  OG1 THR D  43      -7.140 -18.869  -1.494  1.00 20.67           O  
ANISOU 3619  OG1 THR D  43     2790   2382   2683    328    559    187       O  
ATOM   3620  CG2 THR D  43      -8.699 -17.438  -2.731  1.00 19.01           C  
ANISOU 3620  CG2 THR D  43     2688   2195   2342    291    512    131       C  
ATOM   3621  N   SER D  44      -8.506 -21.887  -1.129  1.00 15.71           N  
ANISOU 3621  N   SER D  44     2224   1613   2131    381    574     79       N  
ATOM   3622  CA  SER D  44      -8.152 -23.316  -1.200  1.00 15.33           C  
ANISOU 3622  CA  SER D  44     2180   1497   2149    433    637     61       C  
ATOM   3623  C   SER D  44      -9.370 -24.235  -1.357  1.00 16.17           C  
ANISOU 3623  C   SER D  44     2349   1531   2265    414    626    -24       C  
ATOM   3624  O   SER D  44      -9.225 -25.393  -1.715  1.00 16.43           O  
ANISOU 3624  O   SER D  44     2408   1490   2344    450    687    -66       O  
ATOM   3625  CB  SER D  44      -7.360 -23.721   0.025  1.00 13.19           C  
ANISOU 3625  CB  SER D  44     1830   1221   1959    460    643    154       C  
ATOM   3626  OG  SER D  44      -8.214 -23.812   1.128  1.00 13.95           O  
ANISOU 3626  OG  SER D  44     1921   1304   2077    424    581    172       O  
ATOM   3627  N   PHE D  45     -10.571 -23.691  -1.144  1.00 16.95           N  
ANISOU 3627  N   PHE D  45     2470   1649   2320    357    551    -54       N  
ATOM   3628  CA  PHE D  45     -11.806 -24.473  -1.183  1.00 17.49           C  
ANISOU 3628  CA  PHE D  45     2582   1661   2402    324    530   -130       C  
ATOM   3629  C   PHE D  45     -12.303 -24.757  -2.578  1.00 17.58           C  
ANISOU 3629  C   PHE D  45     2660   1668   2351    318    548   -245       C  
ATOM   3630  O   PHE D  45     -13.226 -25.520  -2.738  1.00 18.24           O  
ANISOU 3630  O   PHE D  45     2777   1703   2452    287    537   -323       O  
ATOM   3631  CB  PHE D  45     -12.899 -23.703  -0.431  1.00 18.19           C  
ANISOU 3631  CB  PHE D  45     2658   1789   2463    268    444   -115       C  
ATOM   3632  CG  PHE D  45     -12.853 -23.863   1.047  1.00 17.65           C  
ANISOU 3632  CG  PHE D  45     2538   1708   2460    263    423    -34       C  
ATOM   3633  CD1 PHE D  45     -11.689 -24.156   1.705  1.00 20.40           C  
ANISOU 3633  CD1 PHE D  45     2837   2050   2863    306    461     48       C  
ATOM   3634  CD2 PHE D  45     -14.001 -23.674   1.785  1.00 20.03           C  
ANISOU 3634  CD2 PHE D  45     2833   2019   2757    218    365    -35       C  
ATOM   3635  CE1 PHE D  45     -11.667 -24.327   3.093  1.00 18.93           C  
ANISOU 3635  CE1 PHE D  45     2601   1868   2723    306    438    128       C  
ATOM   3636  CE2 PHE D  45     -13.998 -23.823   3.144  1.00 18.45           C  
ANISOU 3636  CE2 PHE D  45     2588   1818   2603    216    349     40       C  
ATOM   3637  CZ  PHE D  45     -12.812 -24.151   3.800  1.00 20.20           C  
ANISOU 3637  CZ  PHE D  45     2764   2037   2873    260    384    123       C  
ATOM   3638  N   GLY D  46     -11.716 -24.122  -3.585  1.00 18.40           N  
ANISOU 3638  N   GLY D  46     2781   1832   2379    345    573   -254       N  
ATOM   3639  CA  GLY D  46     -12.107 -24.324  -4.987  1.00 19.25           C  
ANISOU 3639  CA  GLY D  46     2952   1960   2404    348    590   -361       C  
ATOM   3640  C   GLY D  46     -13.019 -23.260  -5.573  1.00 19.42           C  
ANISOU 3640  C   GLY D  46     2994   2071   2313    316    521   -384       C  
ATOM   3641  O   GLY D  46     -12.708 -22.050  -5.511  1.00 17.00           O  
ANISOU 3641  O   GLY D  46     2667   1828   1964    322    501   -307       O  
ATOM   3642  N   ASN D  47     -14.125 -23.694  -6.174  1.00 20.09           N  
ANISOU 3642  N   ASN D  47     3119   2164   2352    284    486   -489       N  
ATOM   3643  CA  ASN D  47     -14.948 -22.750  -6.939  1.00 21.30           C  
ANISOU 3643  CA  ASN D  47     3292   2419   2383    270    425   -512       C  
ATOM   3644  C   ASN D  47     -15.777 -21.816  -6.061  1.00 20.13           C  
ANISOU 3644  C   ASN D  47     3108   2302   2240    236    346   -447       C  
ATOM   3645  O   ASN D  47     -16.780 -22.220  -5.530  1.00 21.42           O  
ANISOU 3645  O   ASN D  47     3258   2444   2437    193    298   -483       O  
ATOM   3646  CB  ASN D  47     -15.884 -23.467  -7.926  1.00 22.33           C  
ANISOU 3646  CB  ASN D  47     3466   2572   2447    244    404   -651       C  
ATOM   3647  CG  ASN D  47     -16.494 -22.493  -8.961  1.00 25.20           C  
ANISOU 3647  CG  ASN D  47     3849   3065   2661    253    354   -665       C  
ATOM   3648  OD1 ASN D  47     -16.450 -21.255  -8.800  1.00 26.18           O  
ANISOU 3648  OD1 ASN D  47     3955   3246   2747    272    328   -566       O  
ATOM   3649  ND2 ASN D  47     -17.046 -23.046 -10.019  1.00 26.29           N  
ANISOU 3649  ND2 ASN D  47     4025   3251   2715    243    343   -787       N  
ATOM   3650  N   LEU D  48     -15.358 -20.563  -5.969  1.00 19.72           N  
ANISOU 3650  N   LEU D  48     3042   2299   2153    257    338   -357       N  
ATOM   3651  CA  LEU D  48     -16.036 -19.549  -5.229  1.00 19.06           C  
ANISOU 3651  CA  LEU D  48     2932   2241   2067    237    274   -298       C  
ATOM   3652  C   LEU D  48     -16.531 -18.441  -6.199  1.00 20.09           C  
ANISOU 3652  C   LEU D  48     3090   2462   2082    258    245   -286       C  
ATOM   3653  O   LEU D  48     -16.695 -17.293  -5.799  1.00 17.81           O  
ANISOU 3653  O   LEU D  48     2789   2194   1786    261    218   -214       O  
ATOM   3654  CB  LEU D  48     -15.037 -18.955  -4.223  1.00 17.81           C  
ANISOU 3654  CB  LEU D  48     2737   2052   1980    242    297   -198       C  
ATOM   3655  CG  LEU D  48     -14.446 -19.873  -3.134  1.00 17.35           C  
ANISOU 3655  CG  LEU D  48     2641   1922   2029    234    323   -179       C  
ATOM   3656  CD1 LEU D  48     -13.554 -19.056  -2.175  1.00 14.21           C  
ANISOU 3656  CD1 LEU D  48     2197   1526   1675    234    326    -83       C  
ATOM   3657  CD2 LEU D  48     -15.525 -20.652  -2.381  1.00 13.42           C  
ANISOU 3657  CD2 LEU D  48     2133   1388   1579    198    282   -218       C  
ATOM   3658  N   SER D  49     -16.716 -18.769  -7.490  1.00 21.41           N  
ANISOU 3658  N   SER D  49     3295   2685   2156    277    256   -354       N  
ATOM   3659  CA  SER D  49     -16.805 -17.709  -8.515  1.00 21.78           C  
ANISOU 3659  CA  SER D  49     3368   2822   2084    316    251   -316       C  
ATOM   3660  C   SER D  49     -18.182 -17.042  -8.723  1.00 22.26           C  
ANISOU 3660  C   SER D  49     3426   2960   2072    315    169   -319       C  
ATOM   3661  O   SER D  49     -18.325 -16.200  -9.597  1.00 23.90           O  
ANISOU 3661  O   SER D  49     3655   3247   2178    356    164   -279       O  
ATOM   3662  CB  SER D  49     -16.303 -18.251  -9.841  1.00 22.26           C  
ANISOU 3662  CB  SER D  49     3470   2930   2057    348    303   -377       C  
ATOM   3663  OG  SER D  49     -17.150 -19.278 -10.282  1.00 23.20           O  
ANISOU 3663  OG  SER D  49     3604   3069   2143    323    268   -503       O  
ATOM   3664  N   SER D  50     -19.183 -17.437  -7.957  1.00 21.86           N  
ANISOU 3664  N   SER D  50     3344   2891   2071    274    110   -359       N  
ATOM   3665  CA  SER D  50     -20.525 -16.865  -8.036  1.00 22.45           C  
ANISOU 3665  CA  SER D  50     3400   3041   2090    275     32   -360       C  
ATOM   3666  C   SER D  50     -21.230 -17.309  -6.767  1.00 21.53           C  
ANISOU 3666  C   SER D  50     3238   2868   2074    224     -5   -377       C  
ATOM   3667  O   SER D  50     -20.745 -18.176  -6.062  1.00 21.75           O  
ANISOU 3667  O   SER D  50     3258   2812   2195    191     26   -399       O  
ATOM   3668  CB  SER D  50     -21.312 -17.396  -9.259  1.00 23.75           C  
ANISOU 3668  CB  SER D  50     3577   3308   2139    275     -7   -457       C  
ATOM   3669  OG  SER D  50     -21.648 -18.806  -9.203  1.00 24.33           O  
ANISOU 3669  OG  SER D  50     3642   3346   2254    216    -15   -580       O  
ATOM   3670  N   ALA D  51     -22.378 -16.748  -6.476  1.00 21.22           N  
ANISOU 3670  N   ALA D  51     3167   2879   2016    224    -68   -361       N  
ATOM   3671  CA  ALA D  51     -23.171 -17.237  -5.335  1.00 20.12           C  
ANISOU 3671  CA  ALA D  51     2980   2702   1962    175   -101   -382       C  
ATOM   3672  C   ALA D  51     -23.567 -18.724  -5.481  1.00 19.86           C  
ANISOU 3672  C   ALA D  51     2936   2649   1962    114   -107   -494       C  
ATOM   3673  O   ALA D  51     -23.503 -19.477  -4.504  1.00 18.14           O  
ANISOU 3673  O   ALA D  51     2697   2348   1847     72    -89   -501       O  
ATOM   3674  CB  ALA D  51     -24.427 -16.373  -5.106  1.00 19.29           C  
ANISOU 3674  CB  ALA D  51     2837   2670   1824    193   -165   -350       C  
ATOM   3675  N   SER D  52     -24.005 -19.150  -6.659  1.00 20.98           N  
ANISOU 3675  N   SER D  52     3089   2863   2017    107   -133   -580       N  
ATOM   3676  CA  SER D  52     -24.471 -20.526  -6.760  1.00 23.00           C  
ANISOU 3676  CA  SER D  52     3334   3090   2315     37   -140   -698       C  
ATOM   3677  C   SER D  52     -23.328 -21.518  -6.478  1.00 22.46           C  
ANISOU 3677  C   SER D  52     3302   2895   2337     23    -59   -720       C  
ATOM   3678  O   SER D  52     -23.510 -22.535  -5.770  1.00 21.85           O  
ANISOU 3678  O   SER D  52     3207   2729   2365    -32    -42   -757       O  
ATOM   3679  CB  SER D  52     -25.143 -20.797  -8.116  1.00 24.49           C  
ANISOU 3679  CB  SER D  52     3528   3392   2384     26   -187   -804       C  
ATOM   3680  OG  SER D  52     -24.300 -20.429  -9.178  1.00 30.14           O  
ANISOU 3680  OG  SER D  52     4300   4154   3000     85   -153   -798       O  
ATOM   3681  N   ALA D  53     -22.152 -21.191  -7.014  1.00 22.48           N  
ANISOU 3681  N   ALA D  53     3351   2891   2301     77     -5   -685       N  
ATOM   3682  CA  ALA D  53     -20.924 -21.968  -6.815  1.00 22.29           C  
ANISOU 3682  CA  ALA D  53     3355   2761   2353     85     78   -687       C  
ATOM   3683  C   ALA D  53     -20.499 -22.015  -5.364  1.00 21.50           C  
ANISOU 3683  C   ALA D  53     3225   2569   2377     78    102   -600       C  
ATOM   3684  O   ALA D  53     -20.043 -23.077  -4.901  1.00 21.92           O  
ANISOU 3684  O   ALA D  53     3280   2522   2524     60    151   -621       O  
ATOM   3685  CB  ALA D  53     -19.803 -21.381  -7.640  1.00 22.86           C  
ANISOU 3685  CB  ALA D  53     3468   2866   2353    149    129   -648       C  
ATOM   3686  N   ILE D  54     -20.631 -20.893  -4.644  1.00 19.48           N  
ANISOU 3686  N   ILE D  54     2941   2343   2118     95     72   -504       N  
ATOM   3687  CA  ILE D  54     -20.228 -20.842  -3.238  1.00 18.63           C  
ANISOU 3687  CA  ILE D  54     2802   2169   2108     90     88   -423       C  
ATOM   3688  C   ILE D  54     -21.193 -21.762  -2.483  1.00 19.49           C  
ANISOU 3688  C   ILE D  54     2879   2237   2291     34     66   -461       C  
ATOM   3689  O   ILE D  54     -20.793 -22.570  -1.642  1.00 19.35           O  
ANISOU 3689  O   ILE D  54     2849   2136   2368     20    105   -440       O  
ATOM   3690  CB  ILE D  54     -20.237 -19.396  -2.629  1.00 18.26           C  
ANISOU 3690  CB  ILE D  54     2737   2163   2038    115     60   -329       C  
ATOM   3691  CG1 ILE D  54     -19.019 -18.593  -3.081  1.00 16.23           C  
ANISOU 3691  CG1 ILE D  54     2505   1914   1749    159    101   -272       C  
ATOM   3692  CG2 ILE D  54     -20.281 -19.429  -1.052  1.00 16.39           C  
ANISOU 3692  CG2 ILE D  54     2459   1881   1889     95     55   -271       C  
ATOM   3693  CD1 ILE D  54     -19.146 -17.114  -2.926  1.00 13.28           C  
ANISOU 3693  CD1 ILE D  54     2130   1582   1336    181     76   -203       C  
ATOM   3694  N   ILE D  55     -22.471 -21.642  -2.808  1.00 19.95           N  
ANISOU 3694  N   ILE D  55     2918   2359   2305      4      7   -512       N  
ATOM   3695  CA  ILE D  55     -23.512 -22.376  -2.112  1.00 20.19           C  
ANISOU 3695  CA  ILE D  55     2906   2364   2402    -56    -16   -543       C  
ATOM   3696  C   ILE D  55     -23.435 -23.865  -2.431  1.00 20.94           C  
ANISOU 3696  C   ILE D  55     3020   2375   2563   -103     24   -632       C  
ATOM   3697  O   ILE D  55     -23.767 -24.670  -1.624  1.00 22.31           O  
ANISOU 3697  O   ILE D  55     3169   2478   2831   -146     41   -629       O  
ATOM   3698  CB  ILE D  55     -24.929 -21.825  -2.462  1.00 20.30           C  
ANISOU 3698  CB  ILE D  55     2882   2484   2348    -75    -93   -576       C  
ATOM   3699  CG1 ILE D  55     -25.115 -20.448  -1.869  1.00 18.35           C  
ANISOU 3699  CG1 ILE D  55     2614   2292   2066    -29   -121   -481       C  
ATOM   3700  CG2 ILE D  55     -26.094 -22.811  -1.970  1.00 21.05           C  
ANISOU 3700  CG2 ILE D  55     2926   2558   2516   -156   -113   -632       C  
ATOM   3701  CD1 ILE D  55     -26.317 -19.755  -2.377  1.00 15.59           C  
ANISOU 3701  CD1 ILE D  55     2231   2053   1638    -21   -189   -499       C  
ATOM   3702  N   GLY D  56     -23.017 -24.228  -3.619  1.00 22.13           N  
ANISOU 3702  N   GLY D  56     3216   2531   2663    -94     43   -713       N  
ATOM   3703  CA  GLY D  56     -22.891 -25.632  -3.964  1.00 22.75           C  
ANISOU 3703  CA  GLY D  56     3322   2515   2807   -136     90   -810       C  
ATOM   3704  C   GLY D  56     -21.481 -26.199  -3.746  1.00 22.25           C  
ANISOU 3704  C   GLY D  56     3295   2345   2813    -90    180   -772       C  
ATOM   3705  O   GLY D  56     -21.223 -27.297  -4.175  1.00 23.09           O  
ANISOU 3705  O   GLY D  56     3437   2368   2970   -107    231   -854       O  
ATOM   3706  N   ASN D  57     -20.562 -25.466  -3.100  1.00 20.86           N  
ANISOU 3706  N   ASN D  57     3109   2172   2643    -31    200   -653       N  
ATOM   3707  CA  ASN D  57     -19.149 -25.912  -3.026  1.00 19.72           C  
ANISOU 3707  CA  ASN D  57     2989   1952   2550     22    282   -613       C  
ATOM   3708  C   ASN D  57     -18.972 -26.869  -1.840  1.00 19.76           C  
ANISOU 3708  C   ASN D  57     2972   1843   2691     11    325   -560       C  
ATOM   3709  O   ASN D  57     -19.306 -26.500  -0.685  1.00 17.37           O  
ANISOU 3709  O   ASN D  57     2625   1554   2421      0    296   -474       O  
ATOM   3710  CB  ASN D  57     -18.185 -24.723  -2.970  1.00 19.08           C  
ANISOU 3710  CB  ASN D  57     2900   1934   2414     82    285   -517       C  
ATOM   3711  CG  ASN D  57     -16.748 -25.142  -2.725  1.00 20.04           C  
ANISOU 3711  CG  ASN D  57     3024   1992   2597    136    363   -461       C  
ATOM   3712  OD1 ASN D  57     -16.497 -25.974  -1.877  1.00 21.19           O  
ANISOU 3712  OD1 ASN D  57     3153   2054   2845    137    398   -425       O  
ATOM   3713  ND2 ASN D  57     -15.797 -24.545  -3.455  1.00 17.44           N  
ANISOU 3713  ND2 ASN D  57     2711   1709   2207    184    393   -442       N  
ATOM   3714  N   PRO D  58     -18.487 -28.098  -2.113  1.00 19.84           N  
ANISOU 3714  N   PRO D  58     3016   1744   2779     17    398   -611       N  
ATOM   3715  CA  PRO D  58     -18.492 -29.157  -1.115  1.00 21.20           C  
ANISOU 3715  CA  PRO D  58     3173   1796   3085      4    445   -567       C  
ATOM   3716  C   PRO D  58     -17.642 -28.873   0.124  1.00 21.62           C  
ANISOU 3716  C   PRO D  58     3184   1846   3185     59    465   -414       C  
ATOM   3717  O   PRO D  58     -17.920 -29.380   1.220  1.00 21.37           O  
ANISOU 3717  O   PRO D  58     3123   1760   3237     45    476   -345       O  
ATOM   3718  CB  PRO D  58     -17.975 -30.377  -1.863  1.00 22.49           C  
ANISOU 3718  CB  PRO D  58     3391   1844   3311     17    529   -656       C  
ATOM   3719  CG  PRO D  58     -17.656 -29.955  -3.258  1.00 21.23           C  
ANISOU 3719  CG  PRO D  58     3274   1756   3037     39    526   -751       C  
ATOM   3720  CD  PRO D  58     -18.123 -28.587  -3.459  1.00 22.14           C  
ANISOU 3720  CD  PRO D  58     3364   2019   3028     31    439   -727       C  
ATOM   3721  N   MET D  59     -16.659 -28.007  -0.062  1.00 21.51           N  
ANISOU 3721  N   MET D  59     3162   1902   3109    117    464   -362       N  
ATOM   3722  CA  MET D  59     -15.788 -27.549   1.010  1.00 21.81           C  
ANISOU 3722  CA  MET D  59     3152   1966   3169    164    469   -229       C  
ATOM   3723  C   MET D  59     -16.409 -26.514   1.904  1.00 20.32           C  
ANISOU 3723  C   MET D  59     2922   1863   2936    135    394   -168       C  
ATOM   3724  O   MET D  59     -16.167 -26.498   3.083  1.00 19.78           O  
ANISOU 3724  O   MET D  59     2812   1799   2906    149    392    -73       O  
ATOM   3725  CB  MET D  59     -14.589 -26.887   0.393  1.00 22.62           C  
ANISOU 3725  CB  MET D  59     3255   2122   3216    220    491   -208       C  
ATOM   3726  CG  MET D  59     -13.392 -27.466   0.800  1.00 26.48           C  
ANISOU 3726  CG  MET D  59     3722   2564   3775    282    556   -136       C  
ATOM   3727  SD  MET D  59     -13.492 -28.989   0.039  1.00 32.68           S  
ANISOU 3727  SD  MET D  59     4565   3216   4636    291    637   -232       S  
ATOM   3728  CE  MET D  59     -12.887 -28.468  -1.585  1.00 18.12           C  
ANISOU 3728  CE  MET D  59     2764   1432   2690    320    661   -321       C  
ATOM   3729  N   VAL D  60     -17.157 -25.602   1.315  1.00 20.50           N  
ANISOU 3729  N   VAL D  60     2956   1962   2870    104    335   -222       N  
ATOM   3730  CA  VAL D  60     -17.948 -24.642   2.073  1.00 19.39           C  
ANISOU 3730  CA  VAL D  60     2783   1894   2689     77    268   -183       C  
ATOM   3731  C   VAL D  60     -18.921 -25.407   2.987  1.00 21.31           C  
ANISOU 3731  C   VAL D  60     3001   2094   3000     35    263   -171       C  
ATOM   3732  O   VAL D  60     -18.918 -25.189   4.202  1.00 21.50           O  
ANISOU 3732  O   VAL D  60     2987   2138   3044     40    252    -86       O  
ATOM   3733  CB  VAL D  60     -18.655 -23.616   1.131  1.00 18.66           C  
ANISOU 3733  CB  VAL D  60     2710   1884   2495     61    213   -244       C  
ATOM   3734  CG1 VAL D  60     -19.703 -22.742   1.862  1.00 17.22           C  
ANISOU 3734  CG1 VAL D  60     2496   1766   2281     36    149   -217       C  
ATOM   3735  CG2 VAL D  60     -17.619 -22.698   0.515  1.00 14.70           C  
ANISOU 3735  CG2 VAL D  60     2224   1428   1934    105    224   -219       C  
ATOM   3736  N   ARG D  61     -19.668 -26.358   2.423  1.00 22.72           N  
ANISOU 3736  N   ARG D  61     3201   2213   3217     -9    277   -255       N  
ATOM   3737  CA  ARG D  61     -20.601 -27.176   3.177  1.00 24.14           C  
ANISOU 3737  CA  ARG D  61     3358   2340   3475    -59    284   -247       C  
ATOM   3738  C   ARG D  61     -19.913 -27.894   4.330  1.00 24.74           C  
ANISOU 3738  C   ARG D  61     3414   2346   3640    -26    340   -139       C  
ATOM   3739  O   ARG D  61     -20.392 -27.815   5.464  1.00 25.42           O  
ANISOU 3739  O   ARG D  61     3459   2454   3744    -38    326    -63       O  
ATOM   3740  CB  ARG D  61     -21.357 -28.164   2.259  1.00 25.51           C  
ANISOU 3740  CB  ARG D  61     3560   2447   3686   -120    299   -369       C  
ATOM   3741  CG  ARG D  61     -22.150 -27.369   1.168  1.00 29.92           C  
ANISOU 3741  CG  ARG D  61     4125   3107   4136   -149    228   -467       C  
ATOM   3742  CD  ARG D  61     -23.418 -28.022   0.542  1.00 36.34           C  
ANISOU 3742  CD  ARG D  61     4933   3911   4963   -235    203   -587       C  
ATOM   3743  NE  ARG D  61     -23.128 -28.584  -0.768  1.00 39.90           N  
ANISOU 3743  NE  ARG D  61     5438   4331   5392   -243    224   -709       N  
ATOM   3744  CZ  ARG D  61     -22.466 -29.723  -0.950  1.00 43.63           C  
ANISOU 3744  CZ  ARG D  61     5952   4675   5951   -240    302   -745       C  
ATOM   3745  NH1 ARG D  61     -22.072 -30.421   0.099  1.00 46.65           N  
ANISOU 3745  NH1 ARG D  61     6324   4950   6450   -228    363   -656       N  
ATOM   3746  NH2 ARG D  61     -22.187 -30.179  -2.177  1.00 45.89           N  
ANISOU 3746  NH2 ARG D  61     6291   4939   6204   -243    324   -868       N  
ATOM   3747  N   ALA D  62     -18.796 -28.573   4.059  1.00 24.44           N  
ANISOU 3747  N   ALA D  62     3400   2234   3651     23    404   -124       N  
ATOM   3748  CA  ALA D  62     -18.131 -29.341   5.090  1.00 24.65           C  
ANISOU 3748  CA  ALA D  62     3406   2195   3765     65    461    -14       C  
ATOM   3749  C   ALA D  62     -17.604 -28.397   6.134  1.00 23.35           C  
ANISOU 3749  C   ALA D  62     3192   2133   3547    105    423     97       C  
ATOM   3750  O   ALA D  62     -17.741 -28.642   7.340  1.00 23.45           O  
ANISOU 3750  O   ALA D  62     3168   2151   3592    112    429    193       O  
ATOM   3751  CB  ALA D  62     -16.969 -30.189   4.513  1.00 25.56           C  
ANISOU 3751  CB  ALA D  62     3552   2217   3941    125    540    -19       C  
ATOM   3752  N   HIS D  63     -16.977 -27.325   5.675  1.00 22.42           N  
ANISOU 3752  N   HIS D  63     3074   2099   3346    129    388     83       N  
ATOM   3753  CA  HIS D  63     -16.363 -26.393   6.597  1.00 21.08           C  
ANISOU 3753  CA  HIS D  63     2859   2024   3128    159    353    171       C  
ATOM   3754  C   HIS D  63     -17.434 -25.786   7.476  1.00 20.59           C  
ANISOU 3754  C   HIS D  63     2772   2025   3027    118    298    189       C  
ATOM   3755  O   HIS D  63     -17.259 -25.724   8.664  1.00 20.39           O  
ANISOU 3755  O   HIS D  63     2707   2039   3001    136    292    276       O  
ATOM   3756  CB  HIS D  63     -15.523 -25.326   5.878  1.00 20.50           C  
ANISOU 3756  CB  HIS D  63     2791   2016   2983    180    332    148       C  
ATOM   3757  CG  HIS D  63     -14.841 -24.400   6.828  1.00 20.72           C  
ANISOU 3757  CG  HIS D  63     2770   2132   2971    198    297    226       C  
ATOM   3758  ND1 HIS D  63     -13.823 -24.816   7.653  1.00 20.50           N  
ANISOU 3758  ND1 HIS D  63     2695   2114   2979    245    322    319       N  
ATOM   3759  CD2 HIS D  63     -15.096 -23.118   7.162  1.00 23.39           C  
ANISOU 3759  CD2 HIS D  63     3095   2553   3238    175    238    222       C  
ATOM   3760  CE1 HIS D  63     -13.454 -23.820   8.428  1.00 22.94           C  
ANISOU 3760  CE1 HIS D  63     2963   2518   3234    241    274    360       C  
ATOM   3761  NE2 HIS D  63     -14.204 -22.773   8.145  1.00 24.87           N  
ANISOU 3761  NE2 HIS D  63     3232   2800   3417    198    226    299       N  
ATOM   3762  N   GLY D  64     -18.558 -25.379   6.885  1.00 21.30           N  
ANISOU 3762  N   GLY D  64     2882   2131   3079     69    261    107       N  
ATOM   3763  CA  GLY D  64     -19.724 -24.844   7.634  1.00 21.95           C  
ANISOU 3763  CA  GLY D  64     2938   2273   3129     34    216    116       C  
ATOM   3764  C   GLY D  64     -20.184 -25.716   8.808  1.00 22.68           C  
ANISOU 3764  C   GLY D  64     2998   2335   3283     24    245    190       C  
ATOM   3765  O   GLY D  64     -20.402 -25.227   9.919  1.00 21.39           O  
ANISOU 3765  O   GLY D  64     2800   2240   3085     31    223    253       O  
ATOM   3766  N   LYS D  65     -20.310 -27.016   8.539  1.00 23.78           N  
ANISOU 3766  N   LYS D  65     3153   2368   3514      8    300    181       N  
ATOM   3767  CA  LYS D  65     -20.690 -28.014   9.560  1.00 24.84           C  
ANISOU 3767  CA  LYS D  65     3263   2450   3727     -1    346    263       C  
ATOM   3768  C   LYS D  65     -19.720 -27.998  10.724  1.00 24.26           C  
ANISOU 3768  C   LYS D  65     3157   2415   3645     64    362    391       C  
ATOM   3769  O   LYS D  65     -20.115 -28.036  11.871  1.00 24.25           O  
ANISOU 3769  O   LYS D  65     3121   2457   3636     66    362    473       O  
ATOM   3770  CB  LYS D  65     -20.723 -29.412   8.956  1.00 26.21           C  
ANISOU 3770  CB  LYS D  65     3468   2478   4012    -21    415    229       C  
ATOM   3771  CG  LYS D  65     -21.473 -30.454   9.779  1.00 29.12           C  
ANISOU 3771  CG  LYS D  65     3816   2772   4475    -56    466    293       C  
ATOM   3772  CD  LYS D  65     -21.144 -31.866   9.306  1.00 33.12           C  
ANISOU 3772  CD  LYS D  65     4361   3113   5109    -58    550    279       C  
ATOM   3773  CE  LYS D  65     -21.552 -32.957  10.314  1.00 36.06           C  
ANISOU 3773  CE  LYS D  65     4715   3396   5590    -70    621    386       C  
ATOM   3774  NZ  LYS D  65     -22.685 -33.825   9.807  1.00 37.34           N  
ANISOU 3774  NZ  LYS D  65     4891   3445   5850   -170    654    298       N  
ATOM   3775  N   LYS D  66     -18.440 -27.927  10.429  1.00 23.91           N  
ANISOU 3775  N   LYS D  66     3120   2369   3595    120    373    410       N  
ATOM   3776  CA  LYS D  66     -17.453 -27.916  11.468  1.00 24.35           C  
ANISOU 3776  CA  LYS D  66     3135   2477   3638    182    381    528       C  
ATOM   3777  C   LYS D  66     -17.455 -26.623  12.271  1.00 22.80           C  
ANISOU 3777  C   LYS D  66     2904   2424   3334    182    311    549       C  
ATOM   3778  O   LYS D  66     -17.142 -26.645  13.464  1.00 24.60           O  
ANISOU 3778  O   LYS D  66     3090   2718   3539    214    308    647       O  
ATOM   3779  CB  LYS D  66     -16.082 -28.122  10.860  1.00 25.39           C  
ANISOU 3779  CB  LYS D  66     3273   2581   3794    239    409    536       C  
ATOM   3780  CG  LYS D  66     -15.867 -29.520  10.242  1.00 30.02           C  
ANISOU 3780  CG  LYS D  66     3894   3018   4495    260    494    531       C  
ATOM   3781  CD  LYS D  66     -14.407 -29.635   9.796  1.00 33.88           C  
ANISOU 3781  CD  LYS D  66     4375   3500   4998    333    525    556       C  
ATOM   3782  CE  LYS D  66     -14.011 -30.998   9.240  1.00 37.30           C  
ANISOU 3782  CE  LYS D  66     4842   3782   5546    374    619    557       C  
ATOM   3783  NZ  LYS D  66     -12.512 -31.171   9.414  1.00 42.50           N  
ANISOU 3783  NZ  LYS D  66     5461   4465   6222    471    653    646       N  
ATOM   3784  N   VAL D  67     -17.754 -25.497  11.638  1.00 20.39           N  
ANISOU 3784  N   VAL D  67     2617   2168   2963    150    259    458       N  
ATOM   3785  CA  VAL D  67     -17.850 -24.238  12.372  1.00 19.38           C  
ANISOU 3785  CA  VAL D  67     2465   2156   2742    145    200    462       C  
ATOM   3786  C   VAL D  67     -18.994 -24.327  13.384  1.00 19.70           C  
ANISOU 3786  C   VAL D  67     2485   2233   2767    124    195    495       C  
ATOM   3787  O   VAL D  67     -18.811 -24.095  14.572  1.00 19.02           O  
ANISOU 3787  O   VAL D  67     2364   2229   2636    145    182    565       O  
ATOM   3788  CB  VAL D  67     -18.060 -23.038  11.417  1.00 18.57           C  
ANISOU 3788  CB  VAL D  67     2393   2078   2584    118    156    362       C  
ATOM   3789  CG1 VAL D  67     -18.446 -21.812  12.192  1.00 17.16           C  
ANISOU 3789  CG1 VAL D  67     2199   1994   2326    107    105    355       C  
ATOM   3790  CG2 VAL D  67     -16.769 -22.802  10.543  1.00 17.07           C  
ANISOU 3790  CG2 VAL D  67     2215   1873   2398    142    165    345       C  
ATOM   3791  N   LEU D  68     -20.169 -24.695  12.915  1.00 20.23           N  
ANISOU 3791  N   LEU D  68     2569   2248   2869     81    206    446       N  
ATOM   3792  CA  LEU D  68     -21.303 -24.717  13.796  1.00 21.38           C  
ANISOU 3792  CA  LEU D  68     2688   2433   3000     58    206    475       C  
ATOM   3793  C   LEU D  68     -21.166 -25.859  14.832  1.00 22.82           C  
ANISOU 3793  C   LEU D  68     2843   2592   3236     80    261    594       C  
ATOM   3794  O   LEU D  68     -21.641 -25.694  15.914  1.00 22.44           O  
ANISOU 3794  O   LEU D  68     2764   2617   3146     85    259    652       O  
ATOM   3795  CB  LEU D  68     -22.612 -24.754  12.997  1.00 21.98           C  
ANISOU 3795  CB  LEU D  68     2776   2475   3101      2    199    389       C  
ATOM   3796  CG  LEU D  68     -23.932 -24.582  13.759  1.00 22.69           C  
ANISOU 3796  CG  LEU D  68     2830   2621   3171    -26    195    404       C  
ATOM   3797  CD1 LEU D  68     -24.006 -23.299  14.540  1.00 23.74           C  
ANISOU 3797  CD1 LEU D  68     2948   2870   3202      1    152    408       C  
ATOM   3798  CD2 LEU D  68     -25.124 -24.673  12.809  1.00 24.01           C  
ANISOU 3798  CD2 LEU D  68     2997   2758   3367    -83    183    315       C  
ATOM   3799  N   THR D  69     -20.453 -26.958  14.535  1.00 23.80           N  
ANISOU 3799  N   THR D  69     2979   2620   3445    103    313    638       N  
ATOM   3800  CA  THR D  69     -20.101 -27.973  15.554  1.00 25.17           C  
ANISOU 3800  CA  THR D  69     3126   2773   3665    144    369    774       C  
ATOM   3801  C   THR D  69     -19.279 -27.266  16.665  1.00 25.25           C  
ANISOU 3801  C   THR D  69     3097   2923   3575    200    331    852       C  
ATOM   3802  O   THR D  69     -19.533 -27.451  17.884  1.00 25.11           O  
ANISOU 3802  O   THR D  69     3045   2975   3523    221    343    950       O  
ATOM   3803  CB  THR D  69     -19.305 -29.206  14.939  1.00 26.43           C  
ANISOU 3803  CB  THR D  69     3309   2794   3938    175    437    804       C  
ATOM   3804  OG1 THR D  69     -20.137 -29.908  14.010  1.00 28.77           O  
ANISOU 3804  OG1 THR D  69     3642   2963   4325    114    473    722       O  
ATOM   3805  CG2 THR D  69     -18.823 -30.239  16.003  1.00 26.11           C  
ANISOU 3805  CG2 THR D  69     3241   2730   3949    236    499    966       C  
ATOM   3806  N   SER D  70     -18.333 -26.437  16.225  1.00 23.70           N  
ANISOU 3806  N   SER D  70     2904   2774   3328    218    285    802       N  
ATOM   3807  CA  SER D  70     -17.510 -25.619  17.117  1.00 23.26           C  
ANISOU 3807  CA  SER D  70     2809   2855   3175    253    236    844       C  
ATOM   3808  C   SER D  70     -18.377 -24.811  18.095  1.00 22.37           C  
ANISOU 3808  C   SER D  70     2680   2853   2968    232    200    836       C  
ATOM   3809  O   SER D  70     -18.135 -24.834  19.314  1.00 21.82           O  
ANISOU 3809  O   SER D  70     2571   2884   2836    266    193    923       O  
ATOM   3810  CB  SER D  70     -16.613 -24.664  16.284  1.00 22.66           C  
ANISOU 3810  CB  SER D  70     2743   2799   3067    248    192    760       C  
ATOM   3811  OG  SER D  70     -15.462 -24.299  17.012  1.00 24.60           O  
ANISOU 3811  OG  SER D  70     2940   3149   3257    287    161    817       O  
ATOM   3812  N   PHE D  71     -19.405 -24.126  17.575  1.00 20.26           N  
ANISOU 3812  N   PHE D  71     2441   2572   2686    182    179    736       N  
ATOM   3813  CA  PHE D  71     -20.358 -23.415  18.475  1.00 20.29           C  
ANISOU 3813  CA  PHE D  71     2429   2670   2608    168    157    726       C  
ATOM   3814  C   PHE D  71     -21.066 -24.363  19.458  1.00 20.16           C  
ANISOU 3814  C   PHE D  71     2385   2666   2609    178    208    832       C  
ATOM   3815  O   PHE D  71     -21.345 -24.009  20.607  1.00 19.80           O  
ANISOU 3815  O   PHE D  71     2312   2731   2479    196    200    874       O  
ATOM   3816  CB  PHE D  71     -21.429 -22.637  17.705  1.00 19.17           C  
ANISOU 3816  CB  PHE D  71     2317   2507   2462    123    135    614       C  
ATOM   3817  CG  PHE D  71     -20.951 -21.379  17.115  1.00 16.64           C  
ANISOU 3817  CG  PHE D  71     2021   2210   2093    118     83    524       C  
ATOM   3818  CD1 PHE D  71     -20.926 -20.228  17.860  1.00 16.81           C  
ANISOU 3818  CD1 PHE D  71     2037   2328   2022    125     44    495       C  
ATOM   3819  CD2 PHE D  71     -20.580 -21.318  15.788  1.00 19.89           C  
ANISOU 3819  CD2 PHE D  71     2465   2543   2550    104     78    463       C  
ATOM   3820  CE1 PHE D  71     -20.487 -19.002  17.304  1.00 17.05           C  
ANISOU 3820  CE1 PHE D  71     2094   2365   2019    114      3    411       C  
ATOM   3821  CE2 PHE D  71     -20.137 -20.094  15.205  1.00 20.84           C  
ANISOU 3821  CE2 PHE D  71     2610   2680   2628     99     37    389       C  
ATOM   3822  CZ  PHE D  71     -20.098 -18.938  15.967  1.00 17.36           C  
ANISOU 3822  CZ  PHE D  71     2164   2323   2109    101      2    365       C  
ATOM   3823  N   GLY D  72     -21.318 -25.571  19.018  1.00 20.95           N  
ANISOU 3823  N   GLY D  72     2492   2650   2817    168    266    874       N  
ATOM   3824  CA  GLY D  72     -21.955 -26.547  19.882  1.00 23.44           C  
ANISOU 3824  CA  GLY D  72     2782   2956   3169    173    327    985       C  
ATOM   3825  C   GLY D  72     -21.030 -26.876  21.019  1.00 24.23           C  
ANISOU 3825  C   GLY D  72     2849   3138   3219    242    338   1117       C  
ATOM   3826  O   GLY D  72     -21.465 -27.040  22.162  1.00 26.52           O  
ANISOU 3826  O   GLY D  72     3109   3511   3456    261    360   1207       O  
ATOM   3827  N   ASP D  73     -19.740 -26.963  20.724  1.00 24.19           N  
ANISOU 3827  N   ASP D  73     2845   3124   3223    283    322   1133       N  
ATOM   3828  CA  ASP D  73     -18.800 -27.151  21.780  1.00 25.01           C  
ANISOU 3828  CA  ASP D  73     2907   3331   3265    352    317   1254       C  
ATOM   3829  C   ASP D  73     -18.807 -25.949  22.790  1.00 24.00           C  
ANISOU 3829  C   ASP D  73     2751   3390   2978    357    250   1228       C  
ATOM   3830  O   ASP D  73     -18.575 -26.148  23.953  1.00 26.36           O  
ANISOU 3830  O   ASP D  73     3012   3802   3203    404    253   1334       O  
ATOM   3831  CB  ASP D  73     -17.425 -27.659  21.253  1.00 26.14           C  
ANISOU 3831  CB  ASP D  73     3044   3422   3467    402    324   1292       C  
ATOM   3832  CG  ASP D  73     -17.285 -29.250  21.360  1.00 32.26           C  
ANISOU 3832  CG  ASP D  73     3817   4077   4362    451    418   1432       C  
ATOM   3833  OD1 ASP D  73     -18.103 -30.041  20.803  1.00 34.72           O  
ANISOU 3833  OD1 ASP D  73     4165   4239   4786    411    481   1419       O  
ATOM   3834  OD2 ASP D  73     -16.354 -29.722  22.053  1.00 39.29           O  
ANISOU 3834  OD2 ASP D  73     4667   5026   5236    530    429   1562       O  
ATOM   3835  N   ALA D  74     -19.162 -24.733  22.410  1.00 22.66           N  
ANISOU 3835  N   ALA D  74     2603   3253   2754    311    196   1092       N  
ATOM   3836  CA  ALA D  74     -19.465 -23.704  23.434  1.00 22.91           C  
ANISOU 3836  CA  ALA D  74     2618   3439   2647    311    151   1061       C  
ATOM   3837  C   ALA D  74     -20.759 -24.042  24.236  1.00 23.83           C  
ANISOU 3837  C   ALA D  74     2726   3589   2741    308    199   1115       C  
ATOM   3838  O   ALA D  74     -20.799 -23.944  25.476  1.00 24.04           O  
ANISOU 3838  O   ALA D  74     2722   3752   2662    343    198   1183       O  
ATOM   3839  CB  ALA D  74     -19.591 -22.342  22.812  1.00 20.65           C  
ANISOU 3839  CB  ALA D  74     2364   3159   2324    267     95    906       C  
ATOM   3840  N   VAL D  75     -21.801 -24.442  23.504  1.00 24.31           N  
ANISOU 3840  N   VAL D  75     2808   3532   2897    266    241   1084       N  
ATOM   3841  CA  VAL D  75     -23.109 -24.765  24.073  1.00 25.51           C  
ANISOU 3841  CA  VAL D  75     2944   3700   3048    250    292   1126       C  
ATOM   3842  C   VAL D  75     -22.974 -25.864  25.090  1.00 27.71           C  
ANISOU 3842  C   VAL D  75     3189   4009   3328    295    353   1297       C  
ATOM   3843  O   VAL D  75     -23.687 -25.877  26.057  1.00 29.07           O  
ANISOU 3843  O   VAL D  75     3337   4272   3437    306    383   1357       O  
ATOM   3844  CB  VAL D  75     -24.129 -25.257  22.992  1.00 25.66           C  
ANISOU 3844  CB  VAL D  75     2980   3574   3195    189    329   1074       C  
ATOM   3845  CG1 VAL D  75     -25.426 -25.827  23.649  1.00 24.22           C  
ANISOU 3845  CG1 VAL D  75     2765   3404   3033    169    395   1145       C  
ATOM   3846  CG2 VAL D  75     -24.432 -24.154  21.956  1.00 23.34           C  
ANISOU 3846  CG2 VAL D  75     2717   3259   2894    151    272    915       C  
ATOM   3847  N   LYS D  76     -22.065 -26.806  24.862  1.00 29.75           N  
ANISOU 3847  N   LYS D  76     3447   4193   3663    326    378   1384       N  
ATOM   3848  CA  LYS D  76     -21.906 -27.947  25.781  1.00 31.38           C  
ANISOU 3848  CA  LYS D  76     3625   4412   3887    379    446   1568       C  
ATOM   3849  C   LYS D  76     -21.189 -27.618  27.073  1.00 31.43           C  
ANISOU 3849  C   LYS D  76     3592   4609   3740    450    414   1657       C  
ATOM   3850  O   LYS D  76     -21.177 -28.457  28.007  1.00 32.66           O  
ANISOU 3850  O   LYS D  76     3718   4809   3881    503    470   1824       O  
ATOM   3851  CB  LYS D  76     -21.165 -29.108  25.092  1.00 32.86           C  
ANISOU 3851  CB  LYS D  76     3826   4442   4216    400    493   1637       C  
ATOM   3852  CG  LYS D  76     -22.095 -30.058  24.325  1.00 35.42           C  
ANISOU 3852  CG  LYS D  76     4176   4578   4703    340    570   1630       C  
ATOM   3853  CD  LYS D  76     -21.811 -30.148  22.829  1.00 37.52           C  
ANISOU 3853  CD  LYS D  76     4486   4692   5078    298    556   1505       C  
ATOM   3854  CE  LYS D  76     -21.152 -31.480  22.457  1.00 40.29           C  
ANISOU 3854  CE  LYS D  76     4854   4888   5569    332    629   1595       C  
ATOM   3855  NZ  LYS D  76     -19.872 -31.708  23.197  1.00 42.51           N  
ANISOU 3855  NZ  LYS D  76     5106   5248   5799    434    626   1728       N  
ATOM   3856  N   ASN D  77     -20.576 -26.441  27.142  1.00 29.37           N  
ANISOU 3856  N   ASN D  77     3329   4462   3367    451    326   1552       N  
ATOM   3857  CA  ASN D  77     -19.629 -26.166  28.215  1.00 30.16           C  
ANISOU 3857  CA  ASN D  77     3388   4744   3329    514    281   1620       C  
ATOM   3858  C   ASN D  77     -19.466 -24.644  28.377  1.00 29.13           C  
ANISOU 3858  C   ASN D  77     3263   4737   3068    485    191   1463       C  
ATOM   3859  O   ASN D  77     -18.382 -24.073  28.304  1.00 27.59           O  
ANISOU 3859  O   ASN D  77     3053   4606   2825    491    123   1413       O  
ATOM   3860  CB  ASN D  77     -18.305 -26.929  27.931  1.00 30.75           C  
ANISOU 3860  CB  ASN D  77     3440   4776   3466    568    280   1713       C  
ATOM   3861  CG  ASN D  77     -17.332 -26.945  29.120  1.00 31.69           C  
ANISOU 3861  CG  ASN D  77     3499   5091   3449    646    242   1827       C  
ATOM   3862  OD1 ASN D  77     -17.690 -26.587  30.259  1.00 35.20           O  
ANISOU 3862  OD1 ASN D  77     3921   5703   3751    665    229   1860       O  
ATOM   3863  ND2 ASN D  77     -16.075 -27.351  28.846  1.00 27.62           N  
ANISOU 3863  ND2 ASN D  77     2952   4568   2973    695    223   1885       N  
ATOM   3864  N   LEU D  78     -20.610 -24.029  28.658  1.00 29.05           N  
ANISOU 3864  N   LEU D  78     3271   4761   3007    452    202   1392       N  
ATOM   3865  CA  LEU D  78     -20.815 -22.602  28.594  1.00 27.89           C  
ANISOU 3865  CA  LEU D  78     3147   4673   2776    415    140   1225       C  
ATOM   3866  C   LEU D  78     -19.926 -21.799  29.531  1.00 29.06           C  
ANISOU 3866  C   LEU D  78     3271   5006   2766    439     69   1193       C  
ATOM   3867  O   LEU D  78     -19.615 -20.647  29.199  1.00 28.88           O  
ANISOU 3867  O   LEU D  78     3270   4995   2709    401      8   1046       O  
ATOM   3868  CB  LEU D  78     -22.299 -22.280  28.835  1.00 28.23           C  
ANISOU 3868  CB  LEU D  78     3205   4722   2800    393    183   1184       C  
ATOM   3869  CG  LEU D  78     -23.203 -22.539  27.617  1.00 26.24           C  
ANISOU 3869  CG  LEU D  78     2981   4293   2697    342    220   1133       C  
ATOM   3870  CD1 LEU D  78     -24.619 -22.547  28.068  1.00 21.46           C  
ANISOU 3870  CD1 LEU D  78     2365   3715   2075    334    276   1145       C  
ATOM   3871  CD2 LEU D  78     -22.938 -21.455  26.506  1.00 19.72           C  
ANISOU 3871  CD2 LEU D  78     2196   3396   1900    301    158    967       C  
ATOM   3872  N   ASP D  79     -19.474 -22.388  30.647  1.00 30.06           N  
ANISOU 3872  N   ASP D  79     3350   5272   2799    499     75   1329       N  
ATOM   3873  CA  ASP D  79     -18.546 -21.691  31.568  1.00 31.05           C  
ANISOU 3873  CA  ASP D  79     3441   5595   2761    519     -3   1299       C  
ATOM   3874  C   ASP D  79     -17.070 -21.892  31.251  1.00 30.96           C  
ANISOU 3874  C   ASP D  79     3390   5596   2775    534    -58   1329       C  
ATOM   3875  O   ASP D  79     -16.230 -21.319  31.938  1.00 31.95           O  
ANISOU 3875  O   ASP D  79     3477   5888   2775    541   -131   1297       O  
ATOM   3876  CB  ASP D  79     -18.781 -22.057  33.048  1.00 32.75           C  
ANISOU 3876  CB  ASP D  79     3618   6003   2823    582     19   1419       C  
ATOM   3877  CG  ASP D  79     -20.185 -21.667  33.549  1.00 34.86           C  
ANISOU 3877  CG  ASP D  79     3915   6301   3031    571     69   1375       C  
ATOM   3878  OD1 ASP D  79     -20.677 -20.555  33.237  1.00 31.34           O  
ANISOU 3878  OD1 ASP D  79     3509   5830   2569    522     45   1204       O  
ATOM   3879  OD2 ASP D  79     -20.784 -22.480  34.299  1.00 38.16           O  
ANISOU 3879  OD2 ASP D  79     4311   6773   3414    618    140   1522       O  
ATOM   3880  N   ASN D  80     -16.717 -22.653  30.214  1.00 29.81           N  
ANISOU 3880  N   ASN D  80     3251   5287   2789    536    -27   1380       N  
ATOM   3881  CA  ASN D  80     -15.290 -22.763  29.846  1.00 29.13           C  
ANISOU 3881  CA  ASN D  80     3122   5215   2731    552    -76   1400       C  
ATOM   3882  C   ASN D  80     -15.025 -22.514  28.373  1.00 28.07           C  
ANISOU 3882  C   ASN D  80     3025   4901   2738    500    -79   1298       C  
ATOM   3883  O   ASN D  80     -14.207 -23.171  27.700  1.00 28.31           O  
ANISOU 3883  O   ASN D  80     3036   4853   2868    525    -66   1357       O  
ATOM   3884  CB  ASN D  80     -14.761 -24.102  30.269  1.00 29.53           C  
ANISOU 3884  CB  ASN D  80     3123   5288   2809    638    -34   1605       C  
ATOM   3885  CG  ASN D  80     -14.729 -24.246  31.771  1.00 31.80           C  
ANISOU 3885  CG  ASN D  80     3361   5794   2929    699    -48   1714       C  
ATOM   3886  OD1 ASN D  80     -13.920 -23.574  32.475  1.00 29.79           O  
ANISOU 3886  OD1 ASN D  80     3056   5732   2532    705   -133   1677       O  
ATOM   3887  ND2 ASN D  80     -15.613 -25.110  32.287  1.00 25.18           N  
ANISOU 3887  ND2 ASN D  80     2533   4935   2100    740     36   1848       N  
ATOM   3888  N   ILE D  81     -15.700 -21.505  27.889  1.00 27.30           N  
ANISOU 3888  N   ILE D  81     2980   4750   2642    433    -95   1143       N  
ATOM   3889  CA  ILE D  81     -15.600 -21.145  26.521  1.00 26.71           C  
ANISOU 3889  CA  ILE D  81     2946   4519   2682    384    -96   1042       C  
ATOM   3890  C   ILE D  81     -14.179 -20.706  26.178  1.00 26.65           C  
ANISOU 3890  C   ILE D  81     2902   4550   2675    373   -156   1006       C  
ATOM   3891  O   ILE D  81     -13.698 -21.046  25.097  1.00 26.78           O  
ANISOU 3891  O   ILE D  81     2926   4445   2804    369   -137   1006       O  
ATOM   3892  CB  ILE D  81     -16.634 -20.070  26.195  1.00 25.70           C  
ANISOU 3892  CB  ILE D  81     2879   4347   2541    326   -102    895       C  
ATOM   3893  CG1 ILE D  81     -18.027 -20.720  26.155  1.00 26.35           C  
ANISOU 3893  CG1 ILE D  81     2990   4352   2671    334    -31    941       C  
ATOM   3894  CG2 ILE D  81     -16.271 -19.398  24.901  1.00 26.56           C  
ANISOU 3894  CG2 ILE D  81     3023   4338   2732    277   -123    783       C  
ATOM   3895  CD1 ILE D  81     -19.219 -19.768  26.124  1.00 25.54           C  
ANISOU 3895  CD1 ILE D  81     2930   4238   2534    298    -29    825       C  
ATOM   3896  N   LYS D  82     -13.505 -19.988  27.080  1.00 26.77           N  
ANISOU 3896  N   LYS D  82     2870   4736   2564    366   -225    973       N  
ATOM   3897  CA  LYS D  82     -12.175 -19.411  26.767  1.00 27.28           C  
ANISOU 3897  CA  LYS D  82     2890   4848   2629    337   -288    919       C  
ATOM   3898  C   LYS D  82     -11.197 -20.475  26.328  1.00 26.57           C  
ANISOU 3898  C   LYS D  82     2746   4725   2623    393   -266   1046       C  
ATOM   3899  O   LYS D  82     -10.434 -20.276  25.365  1.00 25.84           O  
ANISOU 3899  O   LYS D  82     2646   4560   2613    369   -273   1004       O  
ATOM   3900  CB  LYS D  82     -11.551 -18.663  27.955  1.00 29.04           C  
ANISOU 3900  CB  LYS D  82     3056   5284   2696    323   -369    878       C  
ATOM   3901  CG  LYS D  82     -12.249 -17.330  28.426  1.00 33.77           C  
ANISOU 3901  CG  LYS D  82     3704   5928   3199    258   -403    715       C  
ATOM   3902  CD  LYS D  82     -11.585 -16.869  29.808  1.00 40.88           C  
ANISOU 3902  CD  LYS D  82     4536   7070   3925    256   -482    695       C  
ATOM   3903  CE  LYS D  82     -12.000 -15.473  30.347  1.00 43.61           C  
ANISOU 3903  CE  LYS D  82     4925   7477   4169    188   -523    513       C  
ATOM   3904  NZ  LYS D  82     -11.022 -15.010  31.437  1.00 43.01           N  
ANISOU 3904  NZ  LYS D  82     4772   7629   3943    167   -614    472       N  
ATOM   3905  N   ASN D  83     -11.230 -21.602  27.042  1.00 26.95           N  
ANISOU 3905  N   ASN D  83     2758   4827   2653    474   -232   1206       N  
ATOM   3906  CA  ASN D  83     -10.329 -22.706  26.798  1.00 27.42           C  
ANISOU 3906  CA  ASN D  83     2765   4865   2790    547   -202   1347       C  
ATOM   3907  C   ASN D  83     -10.762 -23.581  25.624  1.00 26.50           C  
ANISOU 3907  C   ASN D  83     2708   4524   2838    561   -114   1376       C  
ATOM   3908  O   ASN D  83      -9.937 -24.071  24.850  1.00 26.39           O  
ANISOU 3908  O   ASN D  83     2672   4436   2920    589    -92   1411       O  
ATOM   3909  CB  ASN D  83     -10.148 -23.512  28.081  1.00 28.65           C  
ANISOU 3909  CB  ASN D  83     2858   5174   2854    635   -200   1515       C  
ATOM   3910  CG  ASN D  83      -9.258 -22.807  29.039  1.00 31.83           C  
ANISOU 3910  CG  ASN D  83     3176   5811   3105    632   -297   1496       C  
ATOM   3911  OD1 ASN D  83      -9.259 -23.086  30.224  1.00 40.24           O  
ANISOU 3911  OD1 ASN D  83     4197   7045   4049    685   -316   1592       O  
ATOM   3912  ND2 ASN D  83      -8.452 -21.890  28.529  1.00 34.83           N  
ANISOU 3912  ND2 ASN D  83     3531   6212   3491    567   -360   1372       N  
ATOM   3913  N   THR D  84     -12.060 -23.748  25.474  1.00 25.84           N  
ANISOU 3913  N   THR D  84     2695   4338   2786    537    -64   1352       N  
ATOM   3914  CA  THR D  84     -12.589 -24.561  24.399  1.00 25.71           C  
ANISOU 3914  CA  THR D  84     2735   4116   2918    537     14   1362       C  
ATOM   3915  C   THR D  84     -12.087 -24.025  23.064  1.00 24.52           C  
ANISOU 3915  C   THR D  84     2610   3865   2843    491      1   1245       C  
ATOM   3916  O   THR D  84     -11.784 -24.805  22.165  1.00 26.30           O  
ANISOU 3916  O   THR D  84     2850   3959   3183    516     54   1275       O  
ATOM   3917  CB  THR D  84     -14.135 -24.589  24.468  1.00 25.52           C  
ANISOU 3917  CB  THR D  84     2773   4023   2902    499     54   1328       C  
ATOM   3918  OG1 THR D  84     -14.514 -25.303  25.624  1.00 23.82           O  
ANISOU 3918  OG1 THR D  84     2530   3885   2635    552     87   1465       O  
ATOM   3919  CG2 THR D  84     -14.761 -25.232  23.224  1.00 26.14           C  
ANISOU 3919  CG2 THR D  84     2912   3892   3127    474    121   1297       C  
ATOM   3920  N   PHE D  85     -11.932 -22.708  22.980  1.00 23.97           N  
ANISOU 3920  N   PHE D  85     2544   3860   2705    429    -66   1117       N  
ATOM   3921  CA  PHE D  85     -11.465 -22.025  21.782  1.00 22.74           C  
ANISOU 3921  CA  PHE D  85     2411   3624   2605    381    -80   1008       C  
ATOM   3922  C   PHE D  85      -9.982 -21.583  21.774  1.00 23.30           C  
ANISOU 3922  C   PHE D  85     2409   3790   2654    382   -129   1006       C  
ATOM   3923  O   PHE D  85      -9.595 -20.829  20.880  1.00 21.79           O  
ANISOU 3923  O   PHE D  85     2233   3550   2496    332   -144    911       O  
ATOM   3924  CB  PHE D  85     -12.390 -20.820  21.524  1.00 22.09           C  
ANISOU 3924  CB  PHE D  85     2391   3518   2485    306   -107    865       C  
ATOM   3925  CG  PHE D  85     -13.743 -21.240  21.084  1.00 20.21           C  
ANISOU 3925  CG  PHE D  85     2218   3161   2299    297    -54    851       C  
ATOM   3926  CD1 PHE D  85     -13.991 -21.470  19.732  1.00 14.36           C  
ANISOU 3926  CD1 PHE D  85     1527   2272   1658    279    -17    803       C  
ATOM   3927  CD2 PHE D  85     -14.726 -21.507  22.016  1.00 17.76           C  
ANISOU 3927  CD2 PHE D  85     1912   2897   1939    309    -40    893       C  
ATOM   3928  CE1 PHE D  85     -15.207 -21.938  19.327  1.00 19.81           C  
ANISOU 3928  CE1 PHE D  85     2265   2864   2397    267     26    790       C  
ATOM   3929  CE2 PHE D  85     -15.977 -21.978  21.616  1.00 19.92           C  
ANISOU 3929  CE2 PHE D  85     2233   3066   2271    297     11    887       C  
ATOM   3930  CZ  PHE D  85     -16.215 -22.204  20.270  1.00 17.72           C  
ANISOU 3930  CZ  PHE D  85     1998   2641   2093    272     40    833       C  
ATOM   3931  N   ALA D  86      -9.129 -22.101  22.671  1.00 24.22           N  
ANISOU 3931  N   ALA D  86     2440   4036   2725    442   -150   1119       N  
ATOM   3932  CA  ALA D  86      -7.739 -21.572  22.710  1.00 24.73           C  
ANISOU 3932  CA  ALA D  86     2421   4214   2763    432   -207   1107       C  
ATOM   3933  C   ALA D  86      -6.900 -21.915  21.467  1.00 24.31           C  
ANISOU 3933  C   ALA D  86     2356   4054   2826    449   -166   1114       C  
ATOM   3934  O   ALA D  86      -6.193 -21.065  20.977  1.00 24.98           O  
ANISOU 3934  O   ALA D  86     2415   4162   2915    395   -200   1035       O  
ATOM   3935  CB  ALA D  86      -7.001 -21.955  23.999  1.00 25.28           C  
ANISOU 3935  CB  ALA D  86     2388   4478   2739    493   -252   1223       C  
ATOM   3936  N   GLN D  87      -6.972 -23.142  20.965  1.00 24.20           N  
ANISOU 3936  N   GLN D  87     2362   3925   2909    520    -88   1205       N  
ATOM   3937  CA  GLN D  87      -6.235 -23.499  19.753  1.00 23.76           C  
ANISOU 3937  CA  GLN D  87     2303   3765   2960    542    -39   1203       C  
ATOM   3938  C   GLN D  87      -6.837 -22.764  18.570  1.00 21.16           C  
ANISOU 3938  C   GLN D  87     2062   3308   2669    464    -25   1062       C  
ATOM   3939  O   GLN D  87      -6.125 -22.204  17.792  1.00 18.80           O  
ANISOU 3939  O   GLN D  87     1748   3000   2396    434    -30   1006       O  
ATOM   3940  CB  GLN D  87      -6.279 -25.001  19.500  1.00 25.27           C  
ANISOU 3940  CB  GLN D  87     2509   3844   3249    637     49   1320       C  
ATOM   3941  CG  GLN D  87      -5.150 -25.533  18.570  1.00 28.00           C  
ANISOU 3941  CG  GLN D  87     2816   4133   3689    694    100   1354       C  
ATOM   3942  CD  GLN D  87      -5.014 -27.065  18.690  1.00 35.69           C  
ANISOU 3942  CD  GLN D  87     3785   5027   4750    808    183   1497       C  
ATOM   3943  OE1 GLN D  87      -4.039 -27.616  19.314  1.00 41.85           O  
ANISOU 3943  OE1 GLN D  87     4469   5905   5527    899    184   1630       O  
ATOM   3944  NE2 GLN D  87      -5.996 -27.770  18.127  1.00 35.47           N  
ANISOU 3944  NE2 GLN D  87     3854   4822   4800    805    255   1475       N  
ATOM   3945  N   LEU D  88      -8.162 -22.708  18.488  1.00 20.83           N  
ANISOU 3945  N   LEU D  88     2107   3185   2624    430    -10   1009       N  
ATOM   3946  CA  LEU D  88      -8.841 -21.893  17.432  1.00 19.94           C  
ANISOU 3946  CA  LEU D  88     2075   2972   2530    358     -6    877       C  
ATOM   3947  C   LEU D  88      -8.444 -20.414  17.457  1.00 20.07           C  
ANISOU 3947  C   LEU D  88     2075   3067   2485    285    -71    782       C  
ATOM   3948  O   LEU D  88      -8.344 -19.789  16.420  1.00 19.31           O  
ANISOU 3948  O   LEU D  88     2014   2902   2421    245    -61    704       O  
ATOM   3949  CB  LEU D  88     -10.356 -22.057  17.518  1.00 19.41           C  
ANISOU 3949  CB  LEU D  88     2083   2833   2458    338     12    846       C  
ATOM   3950  CG  LEU D  88     -10.807 -23.499  17.283  1.00 19.50           C  
ANISOU 3950  CG  LEU D  88     2120   2734   2554    391     86    922       C  
ATOM   3951  CD1 LEU D  88     -12.322 -23.556  17.521  1.00 18.76           C  
ANISOU 3951  CD1 LEU D  88     2084   2596   2449    358     95    891       C  
ATOM   3952  CD2 LEU D  88     -10.388 -23.914  15.835  1.00 17.98           C  
ANISOU 3952  CD2 LEU D  88     1961   2416   2455    401    139    884       C  
ATOM   3953  N   SER D  89      -8.158 -19.854  18.621  1.00 21.44           N  
ANISOU 3953  N   SER D  89     2193   3383   2571    268   -134    787       N  
ATOM   3954  CA  SER D  89      -7.735 -18.457  18.652  1.00 22.23           C  
ANISOU 3954  CA  SER D  89     2279   3544   2624    190   -191    687       C  
ATOM   3955  C   SER D  89      -6.390 -18.318  17.983  1.00 22.56           C  
ANISOU 3955  C   SER D  89     2258   3599   2716    183   -188    697       C  
ATOM   3956  O   SER D  89      -6.181 -17.441  17.178  1.00 22.09           O  
ANISOU 3956  O   SER D  89     2222   3488   2681    125   -186    617       O  
ATOM   3957  CB  SER D  89      -7.628 -17.954  20.083  1.00 23.27           C  
ANISOU 3957  CB  SER D  89     2359   3837   2646    170   -261    682       C  
ATOM   3958  OG  SER D  89      -7.320 -16.576  20.078  1.00 24.40           O  
ANISOU 3958  OG  SER D  89     2501   4015   2756     84   -310    568       O  
ATOM   3959  N   GLU D  90      -5.454 -19.178  18.364  1.00 24.25           N  
ANISOU 3959  N   GLU D  90     2383   3890   2941    248   -184    804       N  
ATOM   3960  CA  GLU D  90      -4.123 -19.230  17.753  1.00 24.29           C  
ANISOU 3960  CA  GLU D  90     2311   3918   2999    259   -172    833       C  
ATOM   3961  C   GLU D  90      -4.188 -19.432  16.256  1.00 24.05           C  
ANISOU 3961  C   GLU D  90     2345   3733   3062    266    -97    805       C  
ATOM   3962  O   GLU D  90      -3.509 -18.737  15.480  1.00 23.92           O  
ANISOU 3962  O   GLU D  90     2311   3704   3074    221    -91    757       O  
ATOM   3963  CB  GLU D  90      -3.357 -20.375  18.379  1.00 26.06           C  
ANISOU 3963  CB  GLU D  90     2443   4229   3229    356   -164    973       C  
ATOM   3964  CG  GLU D  90      -2.074 -20.746  17.657  1.00 28.02           C  
ANISOU 3964  CG  GLU D  90     2613   4484   3551    398   -128   1026       C  
ATOM   3965  CD  GLU D  90      -1.355 -21.895  18.335  1.00 31.12           C  
ANISOU 3965  CD  GLU D  90     2910   4964   3951    509   -118   1176       C  
ATOM   3966  OE1 GLU D  90      -2.000 -22.887  18.760  1.00 33.84           O  
ANISOU 3966  OE1 GLU D  90     3292   5264   4302    583    -83   1258       O  
ATOM   3967  OE2 GLU D  90      -0.144 -21.812  18.425  1.00 33.42           O  
ANISOU 3967  OE2 GLU D  90     3085   5366   4245    525   -140   1220       O  
ATOM   3968  N   LEU D  91      -5.023 -20.371  15.824  1.00 23.37           N  
ANISOU 3968  N   LEU D  91     2333   3528   3019    318    -38    831       N  
ATOM   3969  CA  LEU D  91      -5.197 -20.578  14.398  1.00 23.65           C  
ANISOU 3969  CA  LEU D  91     2437   3423   3126    322     30    790       C  
ATOM   3970  C   LEU D  91      -5.684 -19.293  13.694  1.00 23.55           C  
ANISOU 3970  C   LEU D  91     2489   3364   3093    235     12    673       C  
ATOM   3971  O   LEU D  91      -5.091 -18.839  12.735  1.00 23.93           O  
ANISOU 3971  O   LEU D  91     2537   3383   3173    214     37    641       O  
ATOM   3972  CB  LEU D  91      -6.156 -21.753  14.126  1.00 23.30           C  
ANISOU 3972  CB  LEU D  91     2465   3259   3128    376     88    818       C  
ATOM   3973  CG  LEU D  91      -6.428 -22.088  12.645  1.00 22.48           C  
ANISOU 3973  CG  LEU D  91     2438   3015   3089    382    157    764       C  
ATOM   3974  CD1 LEU D  91      -5.171 -22.650  12.049  1.00 24.54           C  
ANISOU 3974  CD1 LEU D  91     2643   3272   3408    442    209    815       C  
ATOM   3975  CD2 LEU D  91      -7.541 -23.124  12.495  1.00 19.40           C  
ANISOU 3975  CD2 LEU D  91     2121   2512   2739    409    202    768       C  
ATOM   3976  N   HIS D  92      -6.764 -18.708  14.170  1.00 23.89           N  
ANISOU 3976  N   HIS D  92     2588   3403   3085    191    -25    617       N  
ATOM   3977  CA  HIS D  92      -7.368 -17.619  13.444  1.00 24.39           C  
ANISOU 3977  CA  HIS D  92     2724   3405   3139    128    -30    519       C  
ATOM   3978  C   HIS D  92      -6.464 -16.399  13.469  1.00 27.17           C  
ANISOU 3978  C   HIS D  92     3030   3817   3476     62    -65    478       C  
ATOM   3979  O   HIS D  92      -6.232 -15.810  12.431  1.00 26.20           O  
ANISOU 3979  O   HIS D  92     2936   3635   3384     33    -36    439       O  
ATOM   3980  CB  HIS D  92      -8.760 -17.343  13.979  1.00 23.08           C  
ANISOU 3980  CB  HIS D  92     2622   3221   2927    109    -55    476       C  
ATOM   3981  CG  HIS D  92      -9.750 -18.365  13.536  1.00 20.54           C  
ANISOU 3981  CG  HIS D  92     2357   2809   2638    151    -10    493       C  
ATOM   3982  ND1 HIS D  92      -9.811 -19.620  14.091  1.00 20.23           N  
ANISOU 3982  ND1 HIS D  92     2293   2774   2621    207     13    574       N  
ATOM   3983  CD2 HIS D  92     -10.645 -18.357  12.530  1.00 18.98           C  
ANISOU 3983  CD2 HIS D  92     2235   2514   2462    143     18    441       C  
ATOM   3984  CE1 HIS D  92     -10.750 -20.320  13.490  1.00 21.20           C  
ANISOU 3984  CE1 HIS D  92     2476   2797   2782    221     53    562       C  
ATOM   3985  NE2 HIS D  92     -11.262 -19.580  12.524  1.00 21.12           N  
ANISOU 3985  NE2 HIS D  92     2525   2733   2768    183     53    478       N  
ATOM   3986  N   CYS D  93      -5.904 -16.096  14.641  1.00 30.49           N  
ANISOU 3986  N   CYS D  93     3375   4360   3851     40   -122    491       N  
ATOM   3987  CA  CYS D  93      -5.082 -14.924  14.856  1.00 33.53           C  
ANISOU 3987  CA  CYS D  93     3709   4811   4221    -38   -163    440       C  
ATOM   3988  C   CYS D  93      -3.609 -15.119  14.455  1.00 36.50           C  
ANISOU 3988  C   CYS D  93     3986   5239   4645    -33   -148    491       C  
ATOM   3989  O   CYS D  93      -3.202 -14.610  13.380  1.00 37.60           O  
ANISOU 3989  O   CYS D  93     4140   5313   4833    -64   -107    466       O  
ATOM   3990  CB  CYS D  93      -5.154 -14.490  16.335  1.00 35.21           C  
ANISOU 3990  CB  CYS D  93     3880   5147   4351    -71   -239    415       C  
ATOM   3991  SG  CYS D  93      -6.848 -14.259  17.101  1.00 35.51           S  
ANISOU 3991  SG  CYS D  93     4015   5158   4318    -69   -258    361       S  
ATOM   3992  N   ASP D  94      -2.838 -15.873  15.270  1.00 38.30           N  
ANISOU 3992  N   ASP D  94     4111   5585   4856     14   -173    571       N  
ATOM   3993  CA  ASP D  94      -1.384 -16.081  15.073  1.00 40.32           C  
ANISOU 3993  CA  ASP D  94     4248   5921   5152     26   -166    629       C  
ATOM   3994  C   ASP D  94      -0.992 -16.581  13.660  1.00 39.67           C  
ANISOU 3994  C   ASP D  94     4184   5737   5153     71    -77    662       C  
ATOM   3995  O   ASP D  94       0.149 -16.397  13.258  1.00 41.32           O  
ANISOU 3995  O   ASP D  94     4308   5993   5401     58    -61    685       O  
ATOM   3996  CB  ASP D  94      -0.782 -17.094  16.095  1.00 42.02           C  
ANISOU 3996  CB  ASP D  94     4357   6270   5338    104   -195    737       C  
ATOM   3997  CG  ASP D  94      -0.631 -16.539  17.549  1.00 45.80           C  
ANISOU 3997  CG  ASP D  94     4766   6913   5721     56   -294    715       C  
ATOM   3998  OD1 ASP D  94      -1.193 -15.473  17.890  1.00 49.13           O  
ANISOU 3998  OD1 ASP D  94     5240   7332   6096    -33   -337    609       O  
ATOM   3999  OD2 ASP D  94       0.037 -17.220  18.384  1.00 48.53           O  
ANISOU 3999  OD2 ASP D  94     5007   7399   6033    115   -327    807       O  
ATOM   4000  N   LYS D  95      -1.905 -17.220  12.920  1.00 38.18           N  
ANISOU 4000  N   LYS D  95     4100   5419   4988    123    -18    661       N  
ATOM   4001  CA  LYS D  95      -1.548 -17.899  11.673  1.00 36.84           C  
ANISOU 4001  CA  LYS D  95     3947   5164   4884    181     68    691       C  
ATOM   4002  C   LYS D  95      -2.273 -17.394  10.438  1.00 34.79           C  
ANISOU 4002  C   LYS D  95     3801   4781   4637    149    112    617       C  
ATOM   4003  O   LYS D  95      -1.681 -17.311   9.361  1.00 34.09           O  
ANISOU 4003  O   LYS D  95     3710   4657   4586    156    170    617       O  
ATOM   4004  CB  LYS D  95      -1.862 -19.367  11.821  1.00 37.32           C  
ANISOU 4004  CB  LYS D  95     4024   5186   4970    285    107    762       C  
ATOM   4005  CG  LYS D  95      -2.042 -20.104  10.477  1.00 39.88           C  
ANISOU 4005  CG  LYS D  95     4420   5381   5353    340    199    755       C  
ATOM   4006  CD  LYS D  95      -3.072 -21.211  10.560  1.00 42.33           C  
ANISOU 4006  CD  LYS D  95     4808   5599   5678    397    229    768       C  
ATOM   4007  CE  LYS D  95      -2.575 -22.496   9.845  1.00 44.89           C  
ANISOU 4007  CE  LYS D  95     5130   5850   6075    495    319    819       C  
ATOM   4008  NZ  LYS D  95      -2.236 -22.205   8.404  1.00 45.50           N  
ANISOU 4008  NZ  LYS D  95     5244   5870   6174    487    379    761       N  
ATOM   4009  N   LEU D  96      -3.577 -17.182  10.590  1.00 33.25           N  
ANISOU 4009  N   LEU D  96     3701   4525   4406    129     90    564       N  
ATOM   4010  CA  LEU D  96      -4.471 -16.727   9.515  1.00 32.83           C  
ANISOU 4010  CA  LEU D  96     3757   4365   4351    107    121    498       C  
ATOM   4011  C   LEU D  96      -4.555 -15.186   9.427  1.00 32.82           C  
ANISOU 4011  C   LEU D  96     3777   4365   4327     17     90    434       C  
ATOM   4012  O   LEU D  96      -4.677 -14.648   8.335  1.00 34.10           O  
ANISOU 4012  O   LEU D  96     3994   4463   4499      0    129    405       O  
ATOM   4013  CB  LEU D  96      -5.911 -17.324   9.643  1.00 31.33           C  
ANISOU 4013  CB  LEU D  96     3654   4108   4142    134    117    475       C  
ATOM   4014  CG  LEU D  96      -5.997 -18.843   9.573  1.00 32.19           C  
ANISOU 4014  CG  LEU D  96     3764   4179   4288    214    161    527       C  
ATOM   4015  CD1 LEU D  96      -7.330 -19.427  10.134  1.00 27.07           C  
ANISOU 4015  CD1 LEU D  96     3171   3490   3623    226    145    519       C  
ATOM   4016  CD2 LEU D  96      -5.626 -19.393   8.122  1.00 32.20           C  
ANISOU 4016  CD2 LEU D  96     3798   4105   4333    256    241    519       C  
ATOM   4017  N   HIS D  97      -4.489 -14.492  10.565  1.00 32.42           N  
ANISOU 4017  N   HIS D  97     3688   4386   4245    -37     24    413       N  
ATOM   4018  CA  HIS D  97      -4.572 -13.061  10.579  1.00 31.64           C  
ANISOU 4018  CA  HIS D  97     3613   4275   4135   -122     -1    347       C  
ATOM   4019  C   HIS D  97      -5.936 -12.663  10.015  1.00 29.17           C  
ANISOU 4019  C   HIS D  97     3418   3861   3802   -119     12    297       C  
ATOM   4020  O   HIS D  97      -6.047 -11.770   9.154  1.00 29.97           O  
ANISOU 4020  O   HIS D  97     3571   3898   3918   -152     40    267       O  
ATOM   4021  CB  HIS D  97      -3.391 -12.453   9.797  1.00 33.10           C  
ANISOU 4021  CB  HIS D  97     3747   4462   4367   -165     36    358       C  
ATOM   4022  CG  HIS D  97      -2.055 -13.084  10.111  1.00 37.04           C  
ANISOU 4022  CG  HIS D  97     4120   5062   4893   -146     36    422       C  
ATOM   4023  ND1 HIS D  97      -1.216 -12.609  11.102  1.00 42.07           N  
ANISOU 4023  ND1 HIS D  97     4654   5809   5521   -206    -22    417       N  
ATOM   4024  CD2 HIS D  97      -1.405 -14.139   9.547  1.00 39.89           C  
ANISOU 4024  CD2 HIS D  97     4437   5433   5288    -71     89    491       C  
ATOM   4025  CE1 HIS D  97      -0.113 -13.341  11.135  1.00 43.92           C  
ANISOU 4025  CE1 HIS D  97     4778   6125   5783   -165     -8    489       C  
ATOM   4026  NE2 HIS D  97      -0.204 -14.278  10.206  1.00 42.61           N  
ANISOU 4026  NE2 HIS D  97     4649   5895   5646    -79     63    537       N  
ATOM   4027  N   VAL D  98      -6.972 -13.366  10.500  1.00 25.94           N  
ANISOU 4027  N   VAL D  98     3048   3445   3363    -76     -5    297       N  
ATOM   4028  CA  VAL D  98      -8.359 -12.958  10.343  1.00 21.86           C  
ANISOU 4028  CA  VAL D  98     2623   2864   2819    -76    -11    248       C  
ATOM   4029  C   VAL D  98      -8.625 -11.876  11.377  1.00 21.14           C  
ANISOU 4029  C   VAL D  98     2532   2807   2692   -132    -62    194       C  
ATOM   4030  O   VAL D  98      -8.536 -12.173  12.573  1.00 20.02           O  
ANISOU 4030  O   VAL D  98     2343   2747   2518   -133   -104    201       O  
ATOM   4031  CB  VAL D  98      -9.322 -14.102  10.702  1.00 21.97           C  
ANISOU 4031  CB  VAL D  98     2659   2873   2817    -20    -13    269       C  
ATOM   4032  CG1 VAL D  98     -10.793 -13.614  10.632  1.00 18.13           C  
ANISOU 4032  CG1 VAL D  98     2251   2338   2300    -24    -25    217       C  
ATOM   4033  CG2 VAL D  98      -9.046 -15.342   9.866  1.00 18.91           C  
ANISOU 4033  CG2 VAL D  98     2268   2449   2468     36     38    314       C  
ATOM   4034  N   ASP D  99      -8.972 -10.647  10.950  1.00 19.38           N  
ANISOU 4034  N   ASP D  99     2366   2523   2474   -174    -56    140       N  
ATOM   4035  CA  ASP D  99      -9.383  -9.595  11.883  1.00 18.70           C  
ANISOU 4035  CA  ASP D  99     2299   2448   2359   -222    -95     74       C  
ATOM   4036  C   ASP D  99     -10.634 -10.025  12.676  1.00 18.59           C  
ANISOU 4036  C   ASP D  99     2315   2454   2293   -181   -120     60       C  
ATOM   4037  O   ASP D  99     -11.561 -10.590  12.080  1.00 16.11           O  
ANISOU 4037  O   ASP D  99     2047   2096   1980   -131    -97     79       O  
ATOM   4038  CB  ASP D  99      -9.721  -8.319  11.152  1.00 19.16           C  
ANISOU 4038  CB  ASP D  99     2426   2411   2441   -254    -69     31       C  
ATOM   4039  CG  ASP D  99      -9.784  -7.137  12.074  1.00 19.29           C  
ANISOU 4039  CG  ASP D  99     2454   2427   2446   -315   -100    -45       C  
ATOM   4040  OD1 ASP D  99      -8.736  -6.532  12.310  1.00 20.85           O  
ANISOU 4040  OD1 ASP D  99     2606   2644   2671   -386   -109    -67       O  
ATOM   4041  OD2 ASP D  99     -10.868  -6.846  12.611  1.00 20.31           O  
ANISOU 4041  OD2 ASP D  99     2634   2544   2540   -294   -114    -87       O  
ATOM   4042  N   PRO D 100     -10.655  -9.773  14.014  1.00 19.62           N  
ANISOU 4042  N   PRO D 100     2417   2663   2377   -205   -166     26       N  
ATOM   4043  CA  PRO D 100     -11.770 -10.123  14.914  1.00 19.83           C  
ANISOU 4043  CA  PRO D 100     2462   2725   2347   -169   -185     16       C  
ATOM   4044  C   PRO D 100     -13.111  -9.607  14.497  1.00 19.41           C  
ANISOU 4044  C   PRO D 100     2491   2593   2291   -146   -165    -22       C  
ATOM   4045  O   PRO D 100     -14.094 -10.240  14.766  1.00 19.63           O  
ANISOU 4045  O   PRO D 100     2531   2633   2293   -103   -162     -4       O  
ATOM   4046  CB  PRO D 100     -11.395  -9.455  16.219  1.00 19.68           C  
ANISOU 4046  CB  PRO D 100     2410   2793   2275   -216   -233    -40       C  
ATOM   4047  CG  PRO D 100      -9.923  -9.538  16.234  1.00 21.96           C  
ANISOU 4047  CG  PRO D 100     2619   3139   2585   -256   -250    -17       C  
ATOM   4048  CD  PRO D 100      -9.544  -9.191  14.792  1.00 21.69           C  
ANISOU 4048  CD  PRO D 100     2614   2998   2629   -270   -203     -6       C  
ATOM   4049  N   GLU D 101     -13.160  -8.473  13.817  1.00 20.53           N  
ANISOU 4049  N   GLU D 101     2683   2654   2463   -173   -147    -66       N  
ATOM   4050  CA  GLU D 101     -14.438  -7.945  13.348  1.00 21.49           C  
ANISOU 4050  CA  GLU D 101     2878   2705   2584   -140   -126    -91       C  
ATOM   4051  C   GLU D 101     -15.169  -8.994  12.503  1.00 19.84           C  
ANISOU 4051  C   GLU D 101     2679   2478   2382    -83   -106    -37       C  
ATOM   4052  O   GLU D 101     -16.372  -9.098  12.571  1.00 21.54           O  
ANISOU 4052  O   GLU D 101     2921   2687   2576    -46   -104    -45       O  
ATOM   4053  CB  GLU D 101     -14.250  -6.634  12.580  1.00 22.83           C  
ANISOU 4053  CB  GLU D 101     3098   2780   2795   -168    -99   -124       C  
ATOM   4054  CG  GLU D 101     -15.551  -6.035  12.004  1.00 27.89           C  
ANISOU 4054  CG  GLU D 101     3812   3350   3437   -120    -75   -137       C  
ATOM   4055  CD  GLU D 101     -16.479  -5.465  13.094  1.00 32.62           C  
ANISOU 4055  CD  GLU D 101     4434   3963   3998   -106    -89   -198       C  
ATOM   4056  OE1 GLU D 101     -16.026  -5.274  14.248  1.00 36.27           O  
ANISOU 4056  OE1 GLU D 101     4869   4480   4433   -147   -115   -247       O  
ATOM   4057  OE2 GLU D 101     -17.654  -5.217  12.784  1.00 35.05           O  
ANISOU 4057  OE2 GLU D 101     4782   4237   4298    -52    -73   -199       O  
ATOM   4058  N   ASN D 102     -14.453  -9.832  11.775  1.00 18.60           N  
ANISOU 4058  N   ASN D 102     2495   2319   2253    -77    -90     14       N  
ATOM   4059  CA  ASN D 102     -15.099 -10.932  11.055  1.00 16.60           C  
ANISOU 4059  CA  ASN D 102     2250   2050   2006    -31    -73     50       C  
ATOM   4060  C   ASN D 102     -15.794 -11.986  11.918  1.00 15.86           C  
ANISOU 4060  C   ASN D 102     2129   2005   1890     -6    -86     71       C  
ATOM   4061  O   ASN D 102     -16.795 -12.566  11.511  1.00 14.20           O  
ANISOU 4061  O   ASN D 102     1938   1775   1682     21    -76     77       O  
ATOM   4062  CB  ASN D 102     -14.083 -11.515  10.096  1.00 16.78           C  
ANISOU 4062  CB  ASN D 102     2255   2055   2065    -30    -45     89       C  
ATOM   4063  CG  ASN D 102     -13.651 -10.485   9.080  1.00 16.82           C  
ANISOU 4063  CG  ASN D 102     2295   2007   2088    -48    -21     78       C  
ATOM   4064  OD1 ASN D 102     -14.504  -9.845   8.468  1.00 14.96           O  
ANISOU 4064  OD1 ASN D 102     2114   1727   1842    -32    -13     59       O  
ATOM   4065  ND2 ASN D 102     -12.356 -10.239   8.973  1.00 14.88           N  
ANISOU 4065  ND2 ASN D 102     2014   1770   1870    -82     -9     94       N  
ATOM   4066  N   PHE D 103     -15.295 -12.218  13.110  1.00 15.95           N  
ANISOU 4066  N   PHE D 103     2094   2086   1879    -18   -107     85       N  
ATOM   4067  CA  PHE D 103     -15.954 -13.152  14.033  1.00 17.23           C  
ANISOU 4067  CA  PHE D 103     2230   2299   2017      8   -113    118       C  
ATOM   4068  C   PHE D 103     -17.331 -12.621  14.448  1.00 17.35           C  
ANISOU 4068  C   PHE D 103     2279   2317   1997     18   -119     78       C  
ATOM   4069  O   PHE D 103     -18.333 -13.356  14.534  1.00 17.57           O  
ANISOU 4069  O   PHE D 103     2305   2346   2025     43   -107     99       O  
ATOM   4070  CB  PHE D 103     -15.172 -13.342  15.347  1.00 17.22           C  
ANISOU 4070  CB  PHE D 103     2171   2393   1978     -2   -140    143       C  
ATOM   4071  CG  PHE D 103     -13.721 -13.684  15.199  1.00 16.30           C  
ANISOU 4071  CG  PHE D 103     2004   2301   1887    -11   -143    183       C  
ATOM   4072  CD1 PHE D 103     -13.240 -14.368  14.101  1.00 17.19           C  
ANISOU 4072  CD1 PHE D 103     2117   2355   2058      6   -109    219       C  
ATOM   4073  CD2 PHE D 103     -12.868 -13.389  16.214  1.00 15.37           C  
ANISOU 4073  CD2 PHE D 103     1833   2278   1730    -33   -179    184       C  
ATOM   4074  CE1 PHE D 103     -11.950 -14.698  14.016  1.00 13.77           C  
ANISOU 4074  CE1 PHE D 103     1630   1952   1649      6   -106    260       C  
ATOM   4075  CE2 PHE D 103     -11.590 -13.704  16.141  1.00 16.91           C  
ANISOU 4075  CE2 PHE D 103     1969   2511   1947    -39   -185    224       C  
ATOM   4076  CZ  PHE D 103     -11.112 -14.367  15.023  1.00 14.32           C  
ANISOU 4076  CZ  PHE D 103     1638   2117   1684    -16   -145    267       C  
ATOM   4077  N   ARG D 104     -17.367 -11.353  14.780  1.00 17.98           N  
ANISOU 4077  N   ARG D 104     2383   2399   2051     -1   -133     18       N  
ATOM   4078  CA  ARG D 104     -18.676 -10.677  14.956  1.00 18.64           C  
ANISOU 4078  CA  ARG D 104     2503   2468   2110     20   -128    -25       C  
ATOM   4079  C   ARG D 104     -19.596 -10.883  13.718  1.00 17.92           C  
ANISOU 4079  C   ARG D 104     2442   2315   2052     49   -108    -15       C  
ATOM   4080  O   ARG D 104     -20.758 -11.320  13.866  1.00 18.05           O  
ANISOU 4080  O   ARG D 104     2452   2349   2058     75   -103     -7       O  
ATOM   4081  CB  ARG D 104     -18.456  -9.181  15.271  1.00 19.02           C  
ANISOU 4081  CB  ARG D 104     2586   2497   2143     -3   -136    -97       C  
ATOM   4082  CG  ARG D 104     -19.724  -8.345  15.615  1.00 21.03           C  
ANISOU 4082  CG  ARG D 104     2879   2739   2371     28   -125   -147       C  
ATOM   4083  CD  ARG D 104     -20.221  -7.632  14.357  1.00 25.01           C  
ANISOU 4083  CD  ARG D 104     3434   3151   2917     51   -104   -154       C  
ATOM   4084  NE  ARG D 104     -21.434  -6.847  14.596  1.00 31.45           N  
ANISOU 4084  NE  ARG D 104     4281   3953   3716     95    -89   -191       N  
ATOM   4085  CZ  ARG D 104     -21.455  -5.582  15.016  1.00 33.37           C  
ANISOU 4085  CZ  ARG D 104     4566   4157   3956     93    -78   -255       C  
ATOM   4086  NH1 ARG D 104     -20.326  -4.926  15.268  1.00 36.37           N  
ANISOU 4086  NH1 ARG D 104     4960   4510   4350     38    -84   -296       N  
ATOM   4087  NH2 ARG D 104     -22.619  -4.973  15.201  1.00 35.13           N  
ANISOU 4087  NH2 ARG D 104     4814   4367   4167    147    -57   -281       N  
ATOM   4088  N   LEU D 105     -19.090 -10.565  12.518  1.00 16.13           N  
ANISOU 4088  N   LEU D 105     2242   2027   1858     42    -98    -15       N  
ATOM   4089  CA  LEU D 105     -19.885 -10.750  11.311  1.00 16.39           C  
ANISOU 4089  CA  LEU D 105     2300   2019   1907     70    -86     -8       C  
ATOM   4090  C   LEU D 105     -20.423 -12.193  11.138  1.00 16.44           C  
ANISOU 4090  C   LEU D 105     2277   2044   1925     79    -82     23       C  
ATOM   4091  O   LEU D 105     -21.606 -12.390  10.775  1.00 17.52           O  
ANISOU 4091  O   LEU D 105     2416   2183   2058     99    -84     16       O  
ATOM   4092  CB  LEU D 105     -19.091 -10.312  10.070  1.00 16.80           C  
ANISOU 4092  CB  LEU D 105     2382   2018   1984     62    -71     -2       C  
ATOM   4093  CG  LEU D 105     -18.709  -8.803  10.015  1.00 17.48           C  
ANISOU 4093  CG  LEU D 105     2506   2060   2074     50    -64    -29       C  
ATOM   4094  CD1 LEU D 105     -17.949  -8.411   8.778  1.00 13.21           C  
ANISOU 4094  CD1 LEU D 105     1992   1469   1559     43    -39     -9       C  
ATOM   4095  CD2 LEU D 105     -19.927  -7.888  10.175  1.00 15.76           C  
ANISOU 4095  CD2 LEU D 105     2323   1826   1840     86    -63    -58       C  
ATOM   4096  N   LEU D 106     -19.603 -13.204  11.398  1.00 15.25           N  
ANISOU 4096  N   LEU D 106     2095   1905   1795     65    -76     59       N  
ATOM   4097  CA  LEU D 106     -20.089 -14.579  11.319  1.00 15.50           C  
ANISOU 4097  CA  LEU D 106     2103   1935   1850     70    -63     88       C  
ATOM   4098  C   LEU D 106     -21.203 -14.832  12.326  1.00 15.77           C  
ANISOU 4098  C   LEU D 106     2113   2013   1866     77    -67     95       C  
ATOM   4099  O   LEU D 106     -22.164 -15.517  12.022  1.00 15.34           O  
ANISOU 4099  O   LEU D 106     2048   1950   1829     77    -59     96       O  
ATOM   4100  CB  LEU D 106     -18.976 -15.604  11.583  1.00 15.42           C  
ANISOU 4100  CB  LEU D 106     2063   1925   1871     66    -47    136       C  
ATOM   4101  CG  LEU D 106     -19.366 -17.073  11.418  1.00 16.05           C  
ANISOU 4101  CG  LEU D 106     2127   1977   1994     70    -22    166       C  
ATOM   4102  CD1 LEU D 106     -20.227 -17.254  10.144  1.00 18.70           C  
ANISOU 4102  CD1 LEU D 106     2494   2269   2344     66    -18    121       C  
ATOM   4103  CD2 LEU D 106     -18.143 -17.945  11.333  1.00 14.46           C  
ANISOU 4103  CD2 LEU D 106     1908   1755   1832     80      3    211       C  
ATOM   4104  N   GLY D 107     -21.061 -14.310  13.540  1.00 16.41           N  
ANISOU 4104  N   GLY D 107     2180   2147   1908     78    -77     97       N  
ATOM   4105  CA  GLY D 107     -22.083 -14.536  14.571  1.00 17.11           C  
ANISOU 4105  CA  GLY D 107     2243   2289   1970     89    -73    110       C  
ATOM   4106  C   GLY D 107     -23.444 -13.934  14.240  1.00 17.56           C  
ANISOU 4106  C   GLY D 107     2313   2344   2017    105    -73     72       C  
ATOM   4107  O   GLY D 107     -24.453 -14.563  14.429  1.00 18.30           O  
ANISOU 4107  O   GLY D 107     2378   2458   2119    109    -61     89       O  
ATOM   4108  N   ASP D 108     -23.445 -12.686  13.800  1.00 18.04           N  
ANISOU 4108  N   ASP D 108     2411   2383   2061    118    -84     25       N  
ATOM   4109  CA  ASP D 108     -24.612 -12.027  13.296  1.00 18.24           C  
ANISOU 4109  CA  ASP D 108     2449   2402   2081    147    -85     -4       C  
ATOM   4110  C   ASP D 108     -25.281 -12.849  12.224  1.00 18.06           C  
ANISOU 4110  C   ASP D 108     2410   2363   2089    143    -87      8       C  
ATOM   4111  O   ASP D 108     -26.499 -12.968  12.226  1.00 19.00           O  
ANISOU 4111  O   ASP D 108     2501   2512   2205    158    -86      4       O  
ATOM   4112  CB  ASP D 108     -24.229 -10.647  12.694  1.00 18.50           C  
ANISOU 4112  CB  ASP D 108     2534   2387   2108    162    -89    -41       C  
ATOM   4113  CG  ASP D 108     -23.948  -9.583  13.761  1.00 21.86           C  
ANISOU 4113  CG  ASP D 108     2979   2824   2503    166    -86    -78       C  
ATOM   4114  OD1 ASP D 108     -24.151  -9.866  14.984  1.00 22.19           O  
ANISOU 4114  OD1 ASP D 108     2993   2927   2512    164    -84    -78       O  
ATOM   4115  OD2 ASP D 108     -23.510  -8.462  13.369  1.00 26.57           O  
ANISOU 4115  OD2 ASP D 108     3621   3366   3108    168    -83   -108       O  
ATOM   4116  N   ILE D 109     -24.514 -13.350  11.251  1.00 18.06           N  
ANISOU 4116  N   ILE D 109     2427   2320   2116    125    -88     13       N  
ATOM   4117  CA  ILE D 109     -25.071 -14.248  10.210  1.00 16.78           C  
ANISOU 4117  CA  ILE D 109     2253   2145   1980    113    -91      9       C  
ATOM   4118  C   ILE D 109     -25.749 -15.517  10.802  1.00 17.68           C  
ANISOU 4118  C   ILE D 109     2317   2277   2124     87    -78     31       C  
ATOM   4119  O   ILE D 109     -26.888 -15.856  10.435  1.00 17.16           O  
ANISOU 4119  O   ILE D 109     2222   2232   2067     80    -85     16       O  
ATOM   4120  CB  ILE D 109     -24.022 -14.596   9.203  1.00 16.66           C  
ANISOU 4120  CB  ILE D 109     2266   2082   1982    100    -86      8       C  
ATOM   4121  CG1 ILE D 109     -23.904 -13.445   8.219  1.00 14.38           C  
ANISOU 4121  CG1 ILE D 109     2019   1779   1665    127    -96    -12       C  
ATOM   4122  CG2 ILE D 109     -24.387 -15.931   8.448  1.00 16.72           C  
ANISOU 4122  CG2 ILE D 109     2258   2072   2023     75    -80     -3       C  
ATOM   4123  CD1 ILE D 109     -22.593 -13.464   7.468  1.00 18.01           C  
ANISOU 4123  CD1 ILE D 109     2510   2199   2134    118    -82     -5       C  
ATOM   4124  N   LEU D 110     -25.073 -16.173  11.740  1.00 17.20           N  
ANISOU 4124  N   LEU D 110     2242   2215   2078     74    -59     72       N  
ATOM   4125  CA  LEU D 110     -25.673 -17.300  12.484  1.00 18.67           C  
ANISOU 4125  CA  LEU D 110     2384   2415   2296     53    -35    110       C  
ATOM   4126  C   LEU D 110     -26.996 -16.952  13.199  1.00 18.85           C  
ANISOU 4126  C   LEU D 110     2369   2499   2294     63    -33    111       C  
ATOM   4127  O   LEU D 110     -27.956 -17.731  13.171  1.00 20.09           O  
ANISOU 4127  O   LEU D 110     2485   2663   2485     38    -20    120       O  
ATOM   4128  CB  LEU D 110     -24.672 -17.904  13.499  1.00 18.85           C  
ANISOU 4128  CB  LEU D 110     2397   2440   2325     53    -13    171       C  
ATOM   4129  CG  LEU D 110     -25.234 -19.130  14.211  1.00 19.46           C  
ANISOU 4129  CG  LEU D 110     2432   2518   2442     35     21    228       C  
ATOM   4130  CD1 LEU D 110     -25.540 -20.185  13.146  1.00 18.27           C  
ANISOU 4130  CD1 LEU D 110     2284   2293   2366      0     37    209       C  
ATOM   4131  CD2 LEU D 110     -24.262 -19.646  15.283  1.00 19.06           C  
ANISOU 4131  CD2 LEU D 110     2370   2487   2386     51     42    305       C  
ATOM   4132  N   ILE D 111     -27.094 -15.776  13.795  1.00 19.06           N  
ANISOU 4132  N   ILE D 111     2407   2570   2266     97    -43     95       N  
ATOM   4133  CA  ILE D 111     -28.388 -15.380  14.368  1.00 19.11           C  
ANISOU 4133  CA  ILE D 111     2376   2635   2248    118    -35     91       C  
ATOM   4134  C   ILE D 111     -29.452 -15.404  13.273  1.00 17.81           C  
ANISOU 4134  C   ILE D 111     2190   2470   2106    115    -51     61       C  
ATOM   4135  O   ILE D 111     -30.511 -15.987  13.438  1.00 17.44           O  
ANISOU 4135  O   ILE D 111     2088   2458   2082     98    -40     73       O  
ATOM   4136  CB  ILE D 111     -28.284 -13.996  15.003  1.00 19.65           C  
ANISOU 4136  CB  ILE D 111     2473   2735   2257    161    -40     61       C  
ATOM   4137  CG1 ILE D 111     -27.346 -14.080  16.207  1.00 22.57           C  
ANISOU 4137  CG1 ILE D 111     2850   3133   2593    157    -30     86       C  
ATOM   4138  CG2 ILE D 111     -29.621 -13.491  15.420  1.00 17.89           C  
ANISOU 4138  CG2 ILE D 111     2217   2569   2011    196    -27     50       C  
ATOM   4139  CD1 ILE D 111     -27.756 -15.157  17.168  1.00 22.14           C  
ANISOU 4139  CD1 ILE D 111     2745   3127   2540    144      0    148       C  
ATOM   4140  N   ILE D 112     -29.162 -14.788  12.126  1.00 16.97           N  
ANISOU 4140  N   ILE D 112     2123   2331   1993    129    -78     25       N  
ATOM   4141  CA  ILE D 112     -30.150 -14.740  11.035  1.00 16.40           C  
ANISOU 4141  CA  ILE D 112     2027   2278   1927    134   -103     -3       C  
ATOM   4142  C   ILE D 112     -30.471 -16.137  10.475  1.00 16.11           C  
ANISOU 4142  C   ILE D 112     1954   2228   1940     73   -104     -8       C  
ATOM   4143  O   ILE D 112     -31.607 -16.439  10.219  1.00 17.81           O  
ANISOU 4143  O   ILE D 112     2113   2486   2168     57   -115    -21       O  
ATOM   4144  CB  ILE D 112     -29.722 -13.843   9.925  1.00 16.45           C  
ANISOU 4144  CB  ILE D 112     2083   2258   1907    166   -127    -28       C  
ATOM   4145  CG1 ILE D 112     -29.616 -12.423  10.472  1.00 16.32           C  
ANISOU 4145  CG1 ILE D 112     2101   2244   1856    222   -119    -28       C  
ATOM   4146  CG2 ILE D 112     -30.743 -13.936   8.742  1.00 15.68           C  
ANISOU 4146  CG2 ILE D 112     1953   2200   1803    171   -159    -51       C  
ATOM   4147  CD1 ILE D 112     -28.833 -11.505   9.588  1.00 15.49           C  
ANISOU 4147  CD1 ILE D 112     2059   2091   1736    248   -128    -38       C  
ATOM   4148  N   VAL D 113     -29.490 -17.000  10.355  1.00 15.97           N  
ANISOU 4148  N   VAL D 113     1963   2149   1956     38    -89      1       N  
ATOM   4149  CA  VAL D 113     -29.732 -18.386   9.940  1.00 16.45           C  
ANISOU 4149  CA  VAL D 113     1998   2176   2077    -23    -79     -9       C  
ATOM   4150  C   VAL D 113     -30.694 -19.096  10.913  1.00 16.93           C  
ANISOU 4150  C   VAL D 113     1992   2264   2175    -55    -51     26       C  
ATOM   4151  O   VAL D 113     -31.644 -19.729  10.498  1.00 18.34           O  
ANISOU 4151  O   VAL D 113     2122   2455   2390   -100    -56      1       O  
ATOM   4152  CB  VAL D 113     -28.384 -19.157   9.798  1.00 17.30           C  
ANISOU 4152  CB  VAL D 113     2151   2203   2219    -40    -55      5       C  
ATOM   4153  CG1 VAL D 113     -28.631 -20.664   9.523  1.00 16.25           C  
ANISOU 4153  CG1 VAL D 113     1997   2014   2163   -102    -29     -5       C  
ATOM   4154  CG2 VAL D 113     -27.516 -18.546   8.676  1.00 15.44           C  
ANISOU 4154  CG2 VAL D 113     1972   1945   1949    -15    -76    -31       C  
ATOM   4155  N   LEU D 114     -30.477 -18.936  12.204  1.00 16.72           N  
ANISOU 4155  N   LEU D 114     1959   2258   2134    -33    -21     82       N  
ATOM   4156  CA  LEU D 114     -31.328 -19.545  13.226  1.00 16.93           C  
ANISOU 4156  CA  LEU D 114     1925   2321   2189    -55     16    130       C  
ATOM   4157  C   LEU D 114     -32.744 -18.982  13.171  1.00 18.75           C  
ANISOU 4157  C   LEU D 114     2094   2630   2399    -45      1    107       C  
ATOM   4158  O   LEU D 114     -33.752 -19.740  13.303  1.00 21.06           O  
ANISOU 4158  O   LEU D 114     2317   2943   2740    -93     20    119       O  
ATOM   4159  CB  LEU D 114     -30.701 -19.358  14.619  1.00 17.10           C  
ANISOU 4159  CB  LEU D 114     1958   2366   2173    -21     47    194       C  
ATOM   4160  CG  LEU D 114     -29.409 -20.157  14.968  1.00 16.49           C  
ANISOU 4160  CG  LEU D 114     1914   2229   2122    -29     70    245       C  
ATOM   4161  CD1 LEU D 114     -28.783 -19.688  16.215  1.00 17.59           C  
ANISOU 4161  CD1 LEU D 114     2062   2422   2199     13     81    294       C  
ATOM   4162  CD2 LEU D 114     -29.676 -21.679  15.107  1.00 19.60           C  
ANISOU 4162  CD2 LEU D 114     2277   2567   2605    -82    117    296       C  
ATOM   4163  N   ALA D 115     -32.852 -17.668  12.932  1.00 18.18           N  
ANISOU 4163  N   ALA D 115     2043   2601   2264     16    -29     77       N  
ATOM   4164  CA  ALA D 115     -34.140 -17.029  12.823  1.00 17.55           C  
ANISOU 4164  CA  ALA D 115     1906   2599   2164     44    -42     60       C  
ATOM   4165  C   ALA D 115     -34.926 -17.698  11.765  1.00 17.56           C  
ANISOU 4165  C   ALA D 115     1855   2610   2206     -9    -71     24       C  
ATOM   4166  O   ALA D 115     -36.058 -18.021  11.991  1.00 17.97           O  
ANISOU 4166  O   ALA D 115     1825   2720   2283    -33    -62     32       O  
ATOM   4167  CB  ALA D 115     -34.009 -15.508  12.472  1.00 17.92           C  
ANISOU 4167  CB  ALA D 115     1997   2664   2148    124    -70     31       C  
ATOM   4168  N   ALA D 116     -34.345 -17.854  10.580  1.00 18.39           N  
ANISOU 4168  N   ALA D 116     2005   2669   2315    -26   -106    -20       N  
ATOM   4169  CA  ALA D 116     -35.033 -18.511   9.465  1.00 19.82           C  
ANISOU 4169  CA  ALA D 116     2141   2865   2523    -82   -141    -71       C  
ATOM   4170  C   ALA D 116     -35.414 -19.957   9.820  1.00 21.36           C  
ANISOU 4170  C   ALA D 116     2286   3027   2804   -176   -108    -65       C  
ATOM   4171  O   ALA D 116     -36.495 -20.430   9.442  1.00 21.01           O  
ANISOU 4171  O   ALA D 116     2163   3030   2792   -230   -125    -96       O  
ATOM   4172  CB  ALA D 116     -34.179 -18.487   8.176  1.00 18.63           C  
ANISOU 4172  CB  ALA D 116     2060   2669   2350    -83   -176   -121       C  
ATOM   4173  N   HIS D 117     -34.520 -20.625  10.549  1.00 22.77           N  
ANISOU 4173  N   HIS D 117     2506   3124   3020   -194    -59    -21       N  
ATOM   4174  CA  HIS D 117     -34.663 -22.065  10.853  1.00 25.70           C  
ANISOU 4174  CA  HIS D 117     2849   3430   3485   -279    -15     -4       C  
ATOM   4175  C   HIS D 117     -35.777 -22.319  11.829  1.00 25.18           C  
ANISOU 4175  C   HIS D 117     2694   3421   3451   -304     22     47       C  
ATOM   4176  O   HIS D 117     -36.542 -23.239  11.648  1.00 25.71           O  
ANISOU 4176  O   HIS D 117     2701   3476   3592   -386     35     31       O  
ATOM   4177  CB  HIS D 117     -33.357 -22.610  11.458  1.00 26.49           C  
ANISOU 4177  CB  HIS D 117     3016   3437   3611   -268     32     51       C  
ATOM   4178  CG  HIS D 117     -33.185 -24.099  11.360  1.00 31.05           C  
ANISOU 4178  CG  HIS D 117     3595   3911   4293   -345     76     56       C  
ATOM   4179  ND1 HIS D 117     -33.556 -24.835  10.250  1.00 36.23           N  
ANISOU 4179  ND1 HIS D 117     4241   4521   5002   -418     58    -28       N  
ATOM   4180  CD2 HIS D 117     -32.594 -24.979  12.210  1.00 35.36           C  
ANISOU 4180  CD2 HIS D 117     4157   4382   4897   -354    140    134       C  
ATOM   4181  CE1 HIS D 117     -33.252 -26.111  10.447  1.00 37.75           C  
ANISOU 4181  CE1 HIS D 117     4447   4603   5294   -474    116     -7       C  
ATOM   4182  NE2 HIS D 117     -32.642 -26.220  11.615  1.00 36.54           N  
ANISOU 4182  NE2 HIS D 117     4309   4427   5146   -431    167    100       N  
ATOM   4183  N   PHE D 118     -35.893 -21.460  12.838  1.00 24.04           N  
ANISOU 4183  N   PHE D 118     2542   3344   3248   -234     39    101       N  
ATOM   4184  CA  PHE D 118     -36.838 -21.699  13.926  1.00 24.43           C  
ANISOU 4184  CA  PHE D 118     2511   3453   3318   -247     88    163       C  
ATOM   4185  C   PHE D 118     -38.123 -20.888  13.974  1.00 23.57           C  
ANISOU 4185  C   PHE D 118     2319   3463   3173   -216     71    150       C  
ATOM   4186  O   PHE D 118     -39.029 -21.209  14.742  1.00 23.07           O  
ANISOU 4186  O   PHE D 118     2174   3453   3136   -239    115    197       O  
ATOM   4187  CB  PHE D 118     -36.092 -21.553  15.247  1.00 24.30           C  
ANISOU 4187  CB  PHE D 118     2535   3433   3264   -196    138    244       C  
ATOM   4188  CG  PHE D 118     -35.123 -22.640  15.458  1.00 25.94           C  
ANISOU 4188  CG  PHE D 118     2789   3538   3529   -233    174    289       C  
ATOM   4189  CD1 PHE D 118     -35.580 -23.944  15.620  1.00 29.87           C  
ANISOU 4189  CD1 PHE D 118     3241   3981   4126   -314    225    328       C  
ATOM   4190  CD2 PHE D 118     -33.777 -22.397  15.448  1.00 25.34           C  
ANISOU 4190  CD2 PHE D 118     2795   3415   3417   -190    162    293       C  
ATOM   4191  CE1 PHE D 118     -34.701 -24.997  15.800  1.00 31.57           C  
ANISOU 4191  CE1 PHE D 118     3501   4089   4407   -340    267    377       C  
ATOM   4192  CE2 PHE D 118     -32.883 -23.451  15.638  1.00 30.68           C  
ANISOU 4192  CE2 PHE D 118     3506   3998   4151   -215    200    343       C  
ATOM   4193  CZ  PHE D 118     -33.350 -24.752  15.813  1.00 30.30           C  
ANISOU 4193  CZ  PHE D 118     3419   3889   4204   -285    254    387       C  
ATOM   4194  N   ALA D 119     -38.204 -19.848  13.167  1.00 22.16           N  
ANISOU 4194  N   ALA D 119     2158   3328   2935   -160     12     95       N  
ATOM   4195  CA  ALA D 119     -39.403 -19.030  13.130  1.00 22.22           C  
ANISOU 4195  CA  ALA D 119     2085   3448   2909   -114     -5     86       C  
ATOM   4196  C   ALA D 119     -39.667 -18.480  14.539  1.00 22.21           C  
ANISOU 4196  C   ALA D 119     2067   3503   2870    -51     53    148       C  
ATOM   4197  O   ALA D 119     -38.709 -18.042  15.205  1.00 21.11           O  
ANISOU 4197  O   ALA D 119     2009   3327   2684     -2     74    169       O  
ATOM   4198  CB  ALA D 119     -40.579 -19.849  12.544  1.00 22.38           C  
ANISOU 4198  CB  ALA D 119     1994   3515   2996   -202    -22     59       C  
ATOM   4199  N   LYS D 120     -40.923 -18.554  14.999  1.00 23.99           N  
ANISOU 4199  N   LYS D 120     2183   3820   3113    -57     82    174       N  
ATOM   4200  CA  LYS D 120     -41.406 -17.968  16.247  1.00 25.56           C  
ANISOU 4200  CA  LYS D 120     2350   4095   3267     11    140    224       C  
ATOM   4201  C   LYS D 120     -40.804 -18.548  17.562  1.00 25.32           C  
ANISOU 4201  C   LYS D 120     2353   4036   3232     -3    211    295       C  
ATOM   4202  O   LYS D 120     -40.837 -17.891  18.635  1.00 25.48           O  
ANISOU 4202  O   LYS D 120     2383   4112   3184     70    255    325       O  
ATOM   4203  CB  LYS D 120     -42.941 -18.125  16.293  1.00 28.51           C  
ANISOU 4203  CB  LYS D 120     2580   4576   3675     -8    157    239       C  
ATOM   4204  CG  LYS D 120     -43.742 -16.838  16.079  1.00 33.61           C  
ANISOU 4204  CG  LYS D 120     3184   5322   4267     98    136    216       C  
ATOM   4205  CD  LYS D 120     -44.318 -16.688  14.669  1.00 39.37           C  
ANISOU 4205  CD  LYS D 120     3858   6087   5013     86     56    163       C  
ATOM   4206  CE  LYS D 120     -44.973 -15.296  14.522  1.00 41.43           C  
ANISOU 4206  CE  LYS D 120     4092   6436   5215    217     42    157       C  
ATOM   4207  NZ  LYS D 120     -46.035 -15.301  13.491  1.00 44.05           N  
ANISOU 4207  NZ  LYS D 120     4307   6864   5566    206    -17    135       N  
ATOM   4208  N   GLU D 121     -40.279 -19.776  17.481  1.00 23.98           N  
ANISOU 4208  N   GLU D 121     2200   3782   3130    -91    225    322       N  
ATOM   4209  CA  GLU D 121     -39.498 -20.361  18.567  1.00 22.57           C  
ANISOU 4209  CA  GLU D 121     2066   3565   2944    -96    283    397       C  
ATOM   4210  C   GLU D 121     -38.266 -19.524  18.844  1.00 21.57           C  
ANISOU 4210  C   GLU D 121     2047   3416   2733    -21    260    379       C  
ATOM   4211  O   GLU D 121     -37.764 -19.532  19.962  1.00 20.90           O  
ANISOU 4211  O   GLU D 121     1990   3354   2598     10    302    435       O  
ATOM   4212  CB  GLU D 121     -39.064 -21.793  18.237  1.00 22.24           C  
ANISOU 4212  CB  GLU D 121     2032   3415   3002   -194    299    424       C  
ATOM   4213  CG  GLU D 121     -38.397 -22.549  19.417  1.00 23.97           C  
ANISOU 4213  CG  GLU D 121     2280   3603   3225   -197    369    529       C  
ATOM   4214  CD  GLU D 121     -38.392 -24.078  19.228  1.00 28.36           C  
ANISOU 4214  CD  GLU D 121     2816   4055   3906   -298    411    575       C  
ATOM   4215  OE1 GLU D 121     -38.805 -24.541  18.129  1.00 29.65           O  
ANISOU 4215  OE1 GLU D 121     2952   4164   4150   -374    379    507       O  
ATOM   4216  OE2 GLU D 121     -37.960 -24.808  20.160  1.00 30.15           O  
ANISOU 4216  OE2 GLU D 121     3056   4253   4149   -300    477    678       O  
ATOM   4217  N   PHE D 122     -37.764 -18.811  17.829  1.00 20.45           N  
ANISOU 4217  N   PHE D 122     1962   3235   2571      4    195    304       N  
ATOM   4218  CA  PHE D 122     -36.620 -17.921  18.033  1.00 18.97           C  
ANISOU 4218  CA  PHE D 122     1871   3025   2311     67    173    281       C  
ATOM   4219  C   PHE D 122     -37.125 -16.613  18.652  1.00 17.90           C  
ANISOU 4219  C   PHE D 122     1732   2973   2095    154    184    259       C  
ATOM   4220  O   PHE D 122     -37.120 -15.607  18.011  1.00 16.90           O  
ANISOU 4220  O   PHE D 122     1637   2841   1944    202    146    202       O  
ATOM   4221  CB  PHE D 122     -35.892 -17.662  16.724  1.00 17.66           C  
ANISOU 4221  CB  PHE D 122     1767   2783   2159     59    110    218       C  
ATOM   4222  CG  PHE D 122     -34.479 -17.209  16.903  1.00 18.93           C  
ANISOU 4222  CG  PHE D 122     2021   2895   2277     89     96    210       C  
ATOM   4223  CD1 PHE D 122     -33.540 -18.058  17.473  1.00 17.59           C  
ANISOU 4223  CD1 PHE D 122     1877   2685   2121     60    120    262       C  
ATOM   4224  CD2 PHE D 122     -34.065 -15.946  16.470  1.00 18.19           C  
ANISOU 4224  CD2 PHE D 122     1984   2794   2134    145     60    155       C  
ATOM   4225  CE1 PHE D 122     -32.246 -17.651  17.635  1.00 17.50           C  
ANISOU 4225  CE1 PHE D 122     1935   2643   2070     84    102    254       C  
ATOM   4226  CE2 PHE D 122     -32.770 -15.542  16.624  1.00 18.35           C  
ANISOU 4226  CE2 PHE D 122     2079   2772   2122    159     47    144       C  
ATOM   4227  CZ  PHE D 122     -31.843 -16.392  17.180  1.00 16.60           C  
ANISOU 4227  CZ  PHE D 122     1874   2524   1911    127     64    191       C  
ATOM   4228  N   THR D 123     -37.535 -16.664  19.913  1.00 17.84           N  
ANISOU 4228  N   THR D 123     1690   3040   2050    178    242    308       N  
ATOM   4229  CA  THR D 123     -38.126 -15.530  20.579  1.00 18.11           C  
ANISOU 4229  CA  THR D 123     1714   3155   2010    261    266    284       C  
ATOM   4230  C   THR D 123     -37.114 -14.412  20.825  1.00 18.64           C  
ANISOU 4230  C   THR D 123     1882   3198   2004    320    243    228       C  
ATOM   4231  O   THR D 123     -35.912 -14.575  20.556  1.00 18.82           O  
ANISOU 4231  O   THR D 123     1972   3150   2028    292    210    219       O  
ATOM   4232  CB  THR D 123     -38.740 -15.978  21.921  1.00 19.05           C  
ANISOU 4232  CB  THR D 123     1774   3367   2098    268    342    354       C  
ATOM   4233  OG1 THR D 123     -37.693 -16.535  22.741  1.00 18.70           O  
ANISOU 4233  OG1 THR D 123     1778   3308   2018    250    360    402       O  
ATOM   4234  CG2 THR D 123     -39.864 -17.004  21.700  1.00 15.91           C  
ANISOU 4234  CG2 THR D 123     1264   2995   1784    204    373    408       C  
ATOM   4235  N   PRO D 124     -37.586 -13.257  21.325  1.00 19.24           N  
ANISOU 4235  N   PRO D 124     1966   3327   2018    401    265    186       N  
ATOM   4236  CA  PRO D 124     -36.640 -12.214  21.613  1.00 19.55           C  
ANISOU 4236  CA  PRO D 124     2100   3334   1995    444    249    125       C  
ATOM   4237  C   PRO D 124     -35.625 -12.618  22.701  1.00 20.12           C  
ANISOU 4237  C   PRO D 124     2210   3429   2006    421    262    149       C  
ATOM   4238  O   PRO D 124     -34.412 -12.432  22.555  1.00 18.87           O  
ANISOU 4238  O   PRO D 124     2120   3214   1834    401    223    122       O  
ATOM   4239  CB  PRO D 124     -37.543 -11.073  22.083  1.00 19.79           C  
ANISOU 4239  CB  PRO D 124     2119   3422   1979    534    287     81       C  
ATOM   4240  CG  PRO D 124     -38.781 -11.247  21.273  1.00 20.77           C  
ANISOU 4240  CG  PRO D 124     2156   3570   2166    543    287    103       C  
ATOM   4241  CD  PRO D 124     -38.969 -12.744  21.317  1.00 20.19           C  
ANISOU 4241  CD  PRO D 124     2013   3518   2142    456    295    179       C  
ATOM   4242  N   GLU D 125     -36.127 -13.195  23.774  1.00 21.78           N  
ANISOU 4242  N   GLU D 125     2368   3729   2178    424    317    208       N  
ATOM   4243  CA  GLU D 125     -35.263 -13.691  24.825  1.00 23.04           C  
ANISOU 4243  CA  GLU D 125     2550   3932   2272    408    330    251       C  
ATOM   4244  C   GLU D 125     -34.243 -14.686  24.236  1.00 22.29           C  
ANISOU 4244  C   GLU D 125     2473   3756   2238    340    291    299       C  
ATOM   4245  O   GLU D 125     -33.064 -14.657  24.583  1.00 23.69           O  
ANISOU 4245  O   GLU D 125     2701   3927   2373    333    265    295       O  
ATOM   4246  CB  GLU D 125     -36.104 -14.324  25.930  1.00 24.63           C  
ANISOU 4246  CB  GLU D 125     2681   4245   2434    420    404    331       C  
ATOM   4247  CG  GLU D 125     -37.024 -13.340  26.732  1.00 28.56           C  
ANISOU 4247  CG  GLU D 125     3162   4840   2849    500    455    283       C  
ATOM   4248  CD  GLU D 125     -38.340 -12.911  26.022  1.00 32.63           C  
ANISOU 4248  CD  GLU D 125     3618   5352   3427    531    472    259       C  
ATOM   4249  OE1 GLU D 125     -38.688 -13.411  24.907  1.00 31.24           O  
ANISOU 4249  OE1 GLU D 125     3402   5112   3354    485    442    279       O  
ATOM   4250  OE2 GLU D 125     -39.045 -12.056  26.616  1.00 36.19           O  
ANISOU 4250  OE2 GLU D 125     4059   5874   3818    607    518    217       O  
ATOM   4251  N   CYS D 126     -34.684 -15.547  23.335  1.00 21.67           N  
ANISOU 4251  N   CYS D 126     2353   3621   2262    290    287    337       N  
ATOM   4252  CA  CYS D 126     -33.803 -16.539  22.724  1.00 21.27           C  
ANISOU 4252  CA  CYS D 126     2320   3484   2278    230    261    377       C  
ATOM   4253  C   CYS D 126     -32.721 -15.895  21.868  1.00 20.90           C  
ANISOU 4253  C   CYS D 126     2346   3358   2236    230    198    306       C  
ATOM   4254  O   CYS D 126     -31.565 -16.294  21.924  1.00 20.56           O  
ANISOU 4254  O   CYS D 126     2339   3282   2192    211    179    329       O  
ATOM   4255  CB  CYS D 126     -34.601 -17.517  21.888  1.00 21.32           C  
ANISOU 4255  CB  CYS D 126     2267   3441   2392    173    271    410       C  
ATOM   4256  SG  CYS D 126     -33.660 -18.852  21.178  1.00 24.62           S  
ANISOU 4256  SG  CYS D 126     2706   3745   2903    102    257    455       S  
ATOM   4257  N   GLN D 127     -33.099 -14.882  21.092  1.00 21.15           N  
ANISOU 4257  N   GLN D 127     2398   3365   2273    257    170    229       N  
ATOM   4258  CA  GLN D 127     -32.170 -14.121  20.291  1.00 19.41           C  
ANISOU 4258  CA  GLN D 127     2247   3073   2055    261    121    165       C  
ATOM   4259  C   GLN D 127     -31.189 -13.474  21.221  1.00 19.19           C  
ANISOU 4259  C   GLN D 127     2269   3074   1948    282    115    140       C  
ATOM   4260  O   GLN D 127     -29.999 -13.534  20.974  1.00 18.21           O  
ANISOU 4260  O   GLN D 127     2185   2905   1829    257     84    134       O  
ATOM   4261  CB  GLN D 127     -32.903 -13.018  19.503  1.00 19.72           C  
ANISOU 4261  CB  GLN D 127     2296   3094   2102    303    105    101       C  
ATOM   4262  CG  GLN D 127     -31.974 -12.171  18.655  1.00 20.08           C  
ANISOU 4262  CG  GLN D 127     2416   3061   2154    309     64     45       C  
ATOM   4263  CD  GLN D 127     -32.662 -11.039  17.935  1.00 20.96           C  
ANISOU 4263  CD  GLN D 127     2542   3152   2271    363     56     -3       C  
ATOM   4264  OE1 GLN D 127     -33.912 -10.925  17.927  1.00 19.94           O  
ANISOU 4264  OE1 GLN D 127     2357   3072   2146    399     75      4       O  
ATOM   4265  NE2 GLN D 127     -31.845 -10.172  17.326  1.00 15.25           N  
ANISOU 4265  NE2 GLN D 127     1887   2357   1549    373     31    -45       N  
ATOM   4266  N   ALA D 128     -31.671 -12.871  22.306  1.00 19.45           N  
ANISOU 4266  N   ALA D 128     2295   3190   1905    325    147    121       N  
ATOM   4267  CA  ALA D 128     -30.743 -12.227  23.297  1.00 19.79           C  
ANISOU 4267  CA  ALA D 128     2385   3278   1859    340    138     81       C  
ATOM   4268  C   ALA D 128     -29.671 -13.186  23.779  1.00 20.38           C  
ANISOU 4268  C   ALA D 128     2452   3376   1916    303    124    148       C  
ATOM   4269  O   ALA D 128     -28.478 -12.850  23.796  1.00 19.35           O  
ANISOU 4269  O   ALA D 128     2361   3229   1764    286     85    116       O  
ATOM   4270  CB  ALA D 128     -31.489 -11.683  24.485  1.00 19.52           C  
ANISOU 4270  CB  ALA D 128     2336   3344   1735    391    182     57       C  
ATOM   4271  N   ALA D 129     -30.110 -14.395  24.139  1.00 21.41           N  
ANISOU 4271  N   ALA D 129     2527   3543   2066    291    160    247       N  
ATOM   4272  CA  ALA D 129     -29.215 -15.422  24.686  1.00 21.19           C  
ANISOU 4272  CA  ALA D 129     2485   3542   2025    270    160    336       C  
ATOM   4273  C   ALA D 129     -28.220 -15.865  23.641  1.00 20.77           C  
ANISOU 4273  C   ALA D 129     2454   3385   2052    232    121    343       C  
ATOM   4274  O   ALA D 129     -27.050 -16.011  23.958  1.00 19.53           O  
ANISOU 4274  O   ALA D 129     2311   3245   1865    228     95    362       O  
ATOM   4275  CB  ALA D 129     -30.024 -16.651  25.231  1.00 21.21           C  
ANISOU 4275  CB  ALA D 129     2425   3586   2050    266    221    452       C  
ATOM   4276  N   TRP D 130     -28.688 -16.096  22.400  1.00 21.28           N  
ANISOU 4276  N   TRP D 130     2519   3354   2213    208    116    327       N  
ATOM   4277  CA  TRP D 130     -27.810 -16.533  21.313  1.00 21.69           C  
ANISOU 4277  CA  TRP D 130     2595   3308   2340    175     87    327       C  
ATOM   4278  C   TRP D 130     -26.835 -15.479  20.793  1.00 21.07           C  
ANISOU 4278  C   TRP D 130     2570   3195   2242    177     39    248       C  
ATOM   4279  O   TRP D 130     -25.699 -15.806  20.437  1.00 21.98           O  
ANISOU 4279  O   TRP D 130     2700   3271   2382    160     18    264       O  
ATOM   4280  CB  TRP D 130     -28.608 -17.144  20.165  1.00 22.04           C  
ANISOU 4280  CB  TRP D 130     2621   3273   2478    145     96    327       C  
ATOM   4281  CG  TRP D 130     -28.892 -18.609  20.456  1.00 23.45           C  
ANISOU 4281  CG  TRP D 130     2755   3439   2714    117    140    422       C  
ATOM   4282  CD1 TRP D 130     -29.928 -19.091  21.147  1.00 24.22           C  
ANISOU 4282  CD1 TRP D 130     2802   3587   2813    115    187    475       C  
ATOM   4283  CD2 TRP D 130     -28.089 -19.730  20.094  1.00 24.07           C  
ANISOU 4283  CD2 TRP D 130     2840   3445   2861     91    149    477       C  
ATOM   4284  NE1 TRP D 130     -29.843 -20.445  21.259  1.00 26.76           N  
ANISOU 4284  NE1 TRP D 130     3099   3865   3204     83    226    563       N  
ATOM   4285  CE2 TRP D 130     -28.728 -20.874  20.603  1.00 26.64           C  
ANISOU 4285  CE2 TRP D 130     3121   3768   3234     72    205    564       C  
ATOM   4286  CE3 TRP D 130     -26.894 -19.882  19.386  1.00 26.66           C  
ANISOU 4286  CE3 TRP D 130     3206   3705   3220     86    122    464       C  
ATOM   4287  CZ2 TRP D 130     -28.238 -22.170  20.414  1.00 27.58           C  
ANISOU 4287  CZ2 TRP D 130     3238   3806   3436     48    236    636       C  
ATOM   4288  CZ3 TRP D 130     -26.393 -21.180  19.198  1.00 27.32           C  
ANISOU 4288  CZ3 TRP D 130     3283   3718   3380     68    153    533       C  
ATOM   4289  CH2 TRP D 130     -27.071 -22.302  19.710  1.00 27.72           C  
ANISOU 4289  CH2 TRP D 130     3295   3755   3482     51    209    617       C  
ATOM   4290  N   GLN D 131     -27.252 -14.230  20.777  1.00 21.04           N  
ANISOU 4290  N   GLN D 131     2593   3202   2200    200     29    168       N  
ATOM   4291  CA  GLN D 131     -26.313 -13.135  20.533  1.00 21.69           C  
ANISOU 4291  CA  GLN D 131     2726   3256   2260    198     -7     95       C  
ATOM   4292  C   GLN D 131     -25.201 -13.023  21.614  1.00 21.10           C  
ANISOU 4292  C   GLN D 131     2653   3252   2114    191    -25     98       C  
ATOM   4293  O   GLN D 131     -24.038 -12.709  21.311  1.00 20.46           O  
ANISOU 4293  O   GLN D 131     2592   3142   2039    167    -58     73       O  
ATOM   4294  CB  GLN D 131     -27.063 -11.800  20.437  1.00 21.92           C  
ANISOU 4294  CB  GLN D 131     2787   3276   2267    231     -3     13       C  
ATOM   4295  CG  GLN D 131     -26.134 -10.608  20.030  1.00 25.51           C  
ANISOU 4295  CG  GLN D 131     3300   3671   2720    221    -31    -63       C  
ATOM   4296  CD  GLN D 131     -25.394 -10.837  18.712  1.00 29.71           C  
ANISOU 4296  CD  GLN D 131     3851   4115   3323    191    -54    -49       C  
ATOM   4297  OE1 GLN D 131     -26.004 -11.107  17.661  1.00 32.45           O  
ANISOU 4297  OE1 GLN D 131     4194   4413   3722    198    -50    -33       O  
ATOM   4298  NE2 GLN D 131     -24.087 -10.718  18.758  1.00 30.29           N  
ANISOU 4298  NE2 GLN D 131     3938   4178   3394    158    -77    -58       N  
ATOM   4299  N   LYS D 132     -25.560 -13.237  22.870  1.00 19.83           N  
ANISOU 4299  N   LYS D 132     2464   3195   1877    212     -4    126       N  
ATOM   4300  CA  LYS D 132     -24.567 -13.207  23.920  1.00 20.79           C  
ANISOU 4300  CA  LYS D 132     2577   3407   1916    209    -27    133       C  
ATOM   4301  C   LYS D 132     -23.570 -14.341  23.653  1.00 19.50           C  
ANISOU 4301  C   LYS D 132     2385   3227   1797    190    -40    225       C  
ATOM   4302  O   LYS D 132     -22.367 -14.130  23.731  1.00 18.83           O  
ANISOU 4302  O   LYS D 132     2302   3160   1694    173    -78    211       O  
ATOM   4303  CB  LYS D 132     -25.251 -13.331  25.278  1.00 22.02           C  
ANISOU 4303  CB  LYS D 132     2706   3688   1974    243      5    159       C  
ATOM   4304  CG  LYS D 132     -24.340 -13.387  26.530  1.00 25.80           C  
ANISOU 4304  CG  LYS D 132     3166   4297   2338    248    -19    175       C  
ATOM   4305  CD  LYS D 132     -25.252 -13.283  27.797  1.00 25.41           C  
ANISOU 4305  CD  LYS D 132     3100   4375   2179    290     21    181       C  
ATOM   4306  CE  LYS D 132     -24.487 -13.427  29.079  1.00 30.12           C  
ANISOU 4306  CE  LYS D 132     3674   5125   2646    301     -1    207       C  
ATOM   4307  NZ  LYS D 132     -25.317 -13.097  30.307  1.00 30.24           N  
ANISOU 4307  NZ  LYS D 132     3684   5273   2533    344     38    187       N  
ATOM   4308  N   LEU D 133     -24.071 -15.522  23.293  1.00 19.39           N  
ANISOU 4308  N   LEU D 133     2344   3172   1850    193     -5    313       N  
ATOM   4309  CA  LEU D 133     -23.192 -16.668  22.987  1.00 20.46           C  
ANISOU 4309  CA  LEU D 133     2457   3273   2042    184     -5    402       C  
ATOM   4310  C   LEU D 133     -22.201 -16.409  21.857  1.00 20.23           C  
ANISOU 4310  C   LEU D 133     2455   3157   2075    159    -37    360       C  
ATOM   4311  O   LEU D 133     -21.006 -16.642  22.010  1.00 19.95           O  
ANISOU 4311  O   LEU D 133     2403   3144   2031    158    -60    391       O  
ATOM   4312  CB  LEU D 133     -23.972 -17.932  22.676  1.00 19.85           C  
ANISOU 4312  CB  LEU D 133     2357   3141   2046    182     46    487       C  
ATOM   4313  CG  LEU D 133     -23.053 -19.146  22.433  1.00 22.55           C  
ANISOU 4313  CG  LEU D 133     2681   3435   2451    183     57    581       C  
ATOM   4314  CD1 LEU D 133     -22.058 -19.362  23.607  1.00 18.29           C  
ANISOU 4314  CD1 LEU D 133     2111   3008   1830    215     44    655       C  
ATOM   4315  CD2 LEU D 133     -23.883 -20.421  22.204  1.00 24.17           C  
ANISOU 4315  CD2 LEU D 133     2867   3572   2745    173    116    659       C  
ATOM   4316  N   VAL D 134     -22.695 -15.938  20.712  1.00 21.27           N  
ANISOU 4316  N   VAL D 134     2620   3197   2265    144    -38    295       N  
ATOM   4317  CA  VAL D 134     -21.810 -15.675  19.594  1.00 20.73           C  
ANISOU 4317  CA  VAL D 134     2577   3049   2249    123    -61    260       C  
ATOM   4318  C   VAL D 134     -20.853 -14.559  19.981  1.00 21.42           C  
ANISOU 4318  C   VAL D 134     2678   3179   2280    111   -100    200       C  
ATOM   4319  O   VAL D 134     -19.689 -14.608  19.628  1.00 20.49           O  
ANISOU 4319  O   VAL D 134     2555   3047   2185     95   -119    208       O  
ATOM   4320  CB  VAL D 134     -22.553 -15.337  18.280  1.00 20.17           C  
ANISOU 4320  CB  VAL D 134     2542   2887   2237    114    -56    208       C  
ATOM   4321  CG1 VAL D 134     -23.417 -16.506  17.838  1.00 19.03           C  
ANISOU 4321  CG1 VAL D 134     2377   2702   2153    111    -23    255       C  
ATOM   4322  CG2 VAL D 134     -23.315 -14.058  18.413  1.00 20.35           C  
ANISOU 4322  CG2 VAL D 134     2590   2924   2217    125    -63    132       C  
ATOM   4323  N   ARG D 135     -21.300 -13.604  20.786  1.00 23.55           N  
ANISOU 4323  N   ARG D 135     2961   3508   2478    117   -108    140       N  
ATOM   4324  CA  ARG D 135     -20.375 -12.530  21.247  1.00 25.53           C  
ANISOU 4324  CA  ARG D 135     3224   3799   2677     93   -146     68       C  
ATOM   4325  C   ARG D 135     -19.280 -13.086  22.184  1.00 25.55           C  
ANISOU 4325  C   ARG D 135     3175   3907   2626     89   -172    121       C  
ATOM   4326  O   ARG D 135     -18.112 -12.690  22.087  1.00 26.67           O  
ANISOU 4326  O   ARG D 135     3306   4059   2767     57   -207     94       O  
ATOM   4327  CB  ARG D 135     -21.145 -11.360  21.867  1.00 26.73           C  
ANISOU 4327  CB  ARG D 135     3410   3979   2769    102   -142    -23       C  
ATOM   4328  CG  ARG D 135     -20.288 -10.350  22.617  1.00 33.42           C  
ANISOU 4328  CG  ARG D 135     4267   4882   3551     71   -178   -107       C  
ATOM   4329  CD  ARG D 135     -21.122  -9.149  23.199  1.00 41.26           C  
ANISOU 4329  CD  ARG D 135     5304   5882   4490     85   -163   -212       C  
ATOM   4330  NE  ARG D 135     -22.116  -9.524  24.229  1.00 46.90           N  
ANISOU 4330  NE  ARG D 135     5999   6693   5126    131   -136   -188       N  
ATOM   4331  CZ  ARG D 135     -23.428  -9.738  24.012  1.00 51.70           C  
ANISOU 4331  CZ  ARG D 135     6611   7276   5756    174    -92   -161       C  
ATOM   4332  NH1 ARG D 135     -23.964  -9.631  22.792  1.00 51.60           N  
ANISOU 4332  NH1 ARG D 135     6619   7151   5835    181    -77   -157       N  
ATOM   4333  NH2 ARG D 135     -24.227 -10.052  25.038  1.00 52.71           N  
ANISOU 4333  NH2 ARG D 135     6714   7505   5809    211    -63   -137       N  
ATOM   4334  N   VAL D 136     -19.632 -14.035  23.045  1.00 24.64           N  
ANISOU 4334  N   VAL D 136     3022   3871   2468    121   -155    206       N  
ATOM   4335  CA  VAL D 136     -18.657 -14.655  23.971  1.00 24.13           C  
ANISOU 4335  CA  VAL D 136     2903   3921   2345    133   -178    278       C  
ATOM   4336  C   VAL D 136     -17.695 -15.583  23.200  1.00 22.45           C  
ANISOU 4336  C   VAL D 136     2662   3652   2217    134   -177    358       C  
ATOM   4337  O   VAL D 136     -16.482 -15.607  23.451  1.00 22.38           O  
ANISOU 4337  O   VAL D 136     2613   3705   2187    128   -213    377       O  
ATOM   4338  CB  VAL D 136     -19.391 -15.366  25.159  1.00 25.21           C  
ANISOU 4338  CB  VAL D 136     3010   4163   2405    176   -150    358       C  
ATOM   4339  CG1 VAL D 136     -18.453 -16.153  26.036  1.00 25.33           C  
ANISOU 4339  CG1 VAL D 136     2965   4295   2362    202   -169    460       C  
ATOM   4340  CG2 VAL D 136     -20.129 -14.304  26.012  1.00 24.40           C  
ANISOU 4340  CG2 VAL D 136     2933   4137   2202    177   -154    263       C  
ATOM   4341  N   VAL D 137     -18.203 -16.281  22.210  1.00 20.04           N  
ANISOU 4341  N   VAL D 137     2375   3231   2007    142   -137    394       N  
ATOM   4342  CA  VAL D 137     -17.295 -17.078  21.376  1.00 18.81           C  
ANISOU 4342  CA  VAL D 137     2203   3009   1935    146   -128    452       C  
ATOM   4343  C   VAL D 137     -16.364 -16.203  20.540  1.00 18.09           C  
ANISOU 4343  C   VAL D 137     2125   2876   1871    109   -159    376       C  
ATOM   4344  O   VAL D 137     -15.156 -16.493  20.435  1.00 16.61           O  
ANISOU 4344  O   VAL D 137     1898   2711   1701    112   -174    415       O  
ATOM   4345  CB  VAL D 137     -18.032 -18.031  20.479  1.00 17.89           C  
ANISOU 4345  CB  VAL D 137     2108   2776   1913    155    -77    491       C  
ATOM   4346  CG1 VAL D 137     -17.114 -18.498  19.357  1.00 15.29           C  
ANISOU 4346  CG1 VAL D 137     1780   2360   1668    154    -68    505       C  
ATOM   4347  CG2 VAL D 137     -18.545 -19.236  21.349  1.00 17.77           C  
ANISOU 4347  CG2 VAL D 137     2061   2798   1894    191    -37    605       C  
ATOM   4348  N   ALA D 138     -16.906 -15.122  19.979  1.00 17.44           N  
ANISOU 4348  N   ALA D 138     2094   2737   1794     80   -164    278       N  
ATOM   4349  CA  ALA D 138     -16.063 -14.178  19.253  1.00 18.14           C  
ANISOU 4349  CA  ALA D 138     2199   2786   1909     41   -187    210       C  
ATOM   4350  C   ALA D 138     -14.939 -13.662  20.161  1.00 18.51           C  
ANISOU 4350  C   ALA D 138     2200   2941   1894     16   -233    192       C  
ATOM   4351  O   ALA D 138     -13.793 -13.584  19.739  1.00 20.24           O  
ANISOU 4351  O   ALA D 138     2388   3157   2145     -7   -248    198       O  
ATOM   4352  CB  ALA D 138     -16.883 -13.030  18.646  1.00 15.75           C  
ANISOU 4352  CB  ALA D 138     1960   2409   1615     22   -181    118       C  
ATOM   4353  N   HIS D 139     -15.256 -13.330  21.408  1.00 19.24           N  
ANISOU 4353  N   HIS D 139     2280   3137   1893     17   -257    168       N  
ATOM   4354  CA  HIS D 139     -14.275 -12.814  22.362  1.00 19.68           C  
ANISOU 4354  CA  HIS D 139     2288   3315   1873    -12   -309    135       C  
ATOM   4355  C   HIS D 139     -13.196 -13.863  22.702  1.00 20.27           C  
ANISOU 4355  C   HIS D 139     2282   3479   1943     14   -327    244       C  
ATOM   4356  O   HIS D 139     -11.988 -13.575  22.705  1.00 21.93           O  
ANISOU 4356  O   HIS D 139     2441   3739   2152    -18   -365    232       O  
ATOM   4357  CB  HIS D 139     -15.007 -12.345  23.622  1.00 20.32           C  
ANISOU 4357  CB  HIS D 139     2381   3496   1844     -6   -323     86       C  
ATOM   4358  CG  HIS D 139     -14.135 -11.613  24.593  1.00 23.82           C  
ANISOU 4358  CG  HIS D 139     2786   4067   2197    -48   -383     17       C  
ATOM   4359  ND1 HIS D 139     -13.730 -12.162  25.800  1.00 29.80           N  
ANISOU 4359  ND1 HIS D 139     3479   4994   2849    -23   -417     72       N  
ATOM   4360  CD2 HIS D 139     -13.561 -10.387  24.532  1.00 27.06           C  
ANISOU 4360  CD2 HIS D 139     3211   4464   2605   -118   -416   -104       C  
ATOM   4361  CE1 HIS D 139     -12.947 -11.305  26.437  1.00 27.15           C  
ANISOU 4361  CE1 HIS D 139     3116   4756   2444    -78   -475    -21       C  
ATOM   4362  NE2 HIS D 139     -12.824 -10.222  25.689  1.00 28.13           N  
ANISOU 4362  NE2 HIS D 139     3288   4766   2636   -141   -474   -132       N  
ATOM   4363  N   ALA D 140     -13.614 -15.095  22.953  1.00 19.91           N  
ANISOU 4363  N   ALA D 140     2218   3446   1901     75   -294    357       N  
ATOM   4364  CA  ALA D 140     -12.670 -16.185  23.204  1.00 20.12           C  
ANISOU 4364  CA  ALA D 140     2173   3536   1937    118   -297    478       C  
ATOM   4365  C   ALA D 140     -11.719 -16.391  22.012  1.00 19.99           C  
ANISOU 4365  C   ALA D 140     2140   3432   2023    108   -285    493       C  
ATOM   4366  O   ALA D 140     -10.560 -16.740  22.176  1.00 21.89           O  
ANISOU 4366  O   ALA D 140     2310   3744   2265    123   -307    550       O  
ATOM   4367  CB  ALA D 140     -13.460 -17.477  23.541  1.00 18.12           C  
ANISOU 4367  CB  ALA D 140     1919   3270   1693    183   -245    598       C  
ATOM   4368  N   LEU D 141     -12.206 -16.144  20.811  1.00 20.52           N  
ANISOU 4368  N   LEU D 141     2271   3354   2170     88   -250    442       N  
ATOM   4369  CA  LEU D 141     -11.451 -16.428  19.613  1.00 22.29           C  
ANISOU 4369  CA  LEU D 141     2490   3492   2487     88   -225    458       C  
ATOM   4370  C   LEU D 141     -10.416 -15.308  19.377  1.00 24.23           C  
ANISOU 4370  C   LEU D 141     2711   3768   2729     27   -264    385       C  
ATOM   4371  O   LEU D 141      -9.374 -15.554  18.768  1.00 24.22           O  
ANISOU 4371  O   LEU D 141     2666   3756   2780     29   -256    418       O  
ATOM   4372  CB  LEU D 141     -12.395 -16.604  18.420  1.00 21.18           C  
ANISOU 4372  CB  LEU D 141     2427   3202   2419     90   -174    432       C  
ATOM   4373  CG  LEU D 141     -12.224 -17.686  17.338  1.00 23.78           C  
ANISOU 4373  CG  LEU D 141     2766   3430   2841    126   -120    487       C  
ATOM   4374  CD1 LEU D 141     -11.850 -19.088  17.919  1.00 22.44           C  
ANISOU 4374  CD1 LEU D 141     2545   3293   2689    190    -95    609       C  
ATOM   4375  CD2 LEU D 141     -13.495 -17.796  16.463  1.00 21.67           C  
ANISOU 4375  CD2 LEU D 141     2574   3049   2612    121    -85    445       C  
ATOM   4376  N   ALA D 142     -10.681 -14.104  19.889  1.00 27.04           N  
ANISOU 4376  N   ALA D 142     3088   4158   3026    -28   -302    286       N  
ATOM   4377  CA  ALA D 142      -9.776 -12.935  19.731  1.00 29.82           C  
ANISOU 4377  CA  ALA D 142     3421   4527   3383   -102   -336    203       C  
ATOM   4378  C   ALA D 142      -8.743 -12.877  20.839  1.00 33.96           C  
ANISOU 4378  C   ALA D 142     3851   5216   3837   -122   -398    213       C  
ATOM   4379  O   ALA D 142      -7.946 -11.953  20.907  1.00 34.73           O  
ANISOU 4379  O   ALA D 142     3917   5349   3931   -194   -434    141       O  
ATOM   4380  CB  ALA D 142     -10.569 -11.651  19.725  1.00 28.41           C  
ANISOU 4380  CB  ALA D 142     3319   4290   3186   -151   -340     86       C  
ATOM   4381  N   ARG D 143      -8.763 -13.877  21.716  1.00 39.03           N  
ANISOU 4381  N   ARG D 143     4444   5962   4422    -59   -409    306       N  
ATOM   4382  CA  ARG D 143      -8.005 -13.842  22.980  1.00 43.04           C  
ANISOU 4382  CA  ARG D 143     4863   6660   4832    -66   -476    319       C  
ATOM   4383  C   ARG D 143      -6.506 -13.873  22.671  1.00 46.33           C  
ANISOU 4383  C   ARG D 143     5181   7134   5287    -89   -503    348       C  
ATOM   4384  O   ARG D 143      -5.736 -13.037  23.197  1.00 47.40           O  
ANISOU 4384  O   ARG D 143     5259   7375   5375   -160   -566    274       O  
ATOM   4385  CB  ARG D 143      -8.449 -14.986  23.911  1.00 43.11           C  
ANISOU 4385  CB  ARG D 143     4847   6759   4773     21   -469    435       C  
ATOM   4386  CG  ARG D 143      -8.051 -14.794  25.336  1.00 47.60           C  
ANISOU 4386  CG  ARG D 143     5347   7533   5206     17   -539    432       C  
ATOM   4387  CD  ARG D 143      -8.825 -15.655  26.325  1.00 50.11           C  
ANISOU 4387  CD  ARG D 143     5668   7933   5440     96   -523    529       C  
ATOM   4388  NE  ARG D 143      -8.291 -15.447  27.677  1.00 55.93           N  
ANISOU 4388  NE  ARG D 143     6328   8892   6029     95   -597    527       N  
ATOM   4389  CZ  ARG D 143      -8.756 -14.568  28.587  1.00 59.06           C  
ANISOU 4389  CZ  ARG D 143     6750   9384   6305     53   -637    416       C  
ATOM   4390  NH1 ARG D 143      -9.814 -13.778  28.337  1.00 58.27           N  
ANISOU 4390  NH1 ARG D 143     6750   9171   6219     14   -606    300       N  
ATOM   4391  NH2 ARG D 143      -8.155 -14.478  29.781  1.00 59.91           N  
ANISOU 4391  NH2 ARG D 143     6779   9712   6270     55   -709    419       N  
ATOM   4392  N   LYS D 144      -6.104 -14.784  21.770  1.00 48.55           N  
ANISOU 4392  N   LYS D 144     5445   7341   5660    -35   -453    445       N  
ATOM   4393  CA  LYS D 144      -4.689 -14.911  21.392  1.00 51.32           C  
ANISOU 4393  CA  LYS D 144     5697   7745   6059    -43   -466    486       C  
ATOM   4394  C   LYS D 144      -4.273 -13.899  20.311  1.00 52.91           C  
ANISOU 4394  C   LYS D 144     5921   7844   6337   -127   -449    394       C  
ATOM   4395  O   LYS D 144      -3.087 -13.809  19.971  1.00 53.84           O  
ANISOU 4395  O   LYS D 144     5953   8007   6497   -151   -459    413       O  
ATOM   4396  CB  LYS D 144      -4.338 -16.346  20.970  1.00 51.08           C  
ANISOU 4396  CB  LYS D 144     5629   7688   6091     61   -413    632       C  
ATOM   4397  CG  LYS D 144      -4.695 -17.407  22.015  1.00 52.43           C  
ANISOU 4397  CG  LYS D 144     5776   7949   6198    150   -417    745       C  
ATOM   4398  CD  LYS D 144      -4.033 -17.172  23.396  1.00 53.78           C  
ANISOU 4398  CD  LYS D 144     5843   8345   6247    143   -504    761       C  
ATOM   4399  CE  LYS D 144      -4.417 -18.285  24.392  1.00 54.32           C  
ANISOU 4399  CE  LYS D 144     5891   8501   6249    245   -497    897       C  
ATOM   4400  NZ  LYS D 144      -4.191 -17.899  25.825  1.00 55.61           N  
ANISOU 4400  NZ  LYS D 144     5985   8885   6259    232   -584    887       N  
ATOM   4401  N   TYR D 145      -5.228 -13.138  19.771  1.00 54.32           N  
ANISOU 4401  N   TYR D 145     6211   7892   6538   -168   -422    304       N  
ATOM   4402  CA  TYR D 145      -4.850 -11.952  19.001  1.00 55.91           C  
ANISOU 4402  CA  TYR D 145     6434   8016   6795   -259   -415    212       C  
ATOM   4403  C   TYR D 145      -4.186 -11.017  20.032  1.00 58.11           C  
ANISOU 4403  C   TYR D 145     6645   8425   7008   -347   -492    128       C  
ATOM   4404  O   TYR D 145      -3.007 -10.666  19.875  1.00 59.72           O  
ANISOU 4404  O   TYR D 145     6762   8685   7245   -404   -514    120       O  
ATOM   4405  CB  TYR D 145      -6.042 -11.276  18.272  1.00 55.15           C  
ANISOU 4405  CB  TYR D 145     6469   7759   6728   -275   -371    140       C  
ATOM   4406  CG  TYR D 145      -5.811 -11.017  16.775  1.00 55.72           C  
ANISOU 4406  CG  TYR D 145     6578   7697   6897   -288   -310    143       C  
ATOM   4407  CD1 TYR D 145      -4.675 -10.332  16.329  1.00 58.67           C  
ANISOU 4407  CD1 TYR D 145     6897   8076   7320   -359   -311    121       C  
ATOM   4408  CD2 TYR D 145      -6.725 -11.454  15.819  1.00 53.91           C  
ANISOU 4408  CD2 TYR D 145     6434   7345   6703   -234   -253    168       C  
ATOM   4409  CE1 TYR D 145      -4.446 -10.098  14.948  1.00 59.57           C  
ANISOU 4409  CE1 TYR D 145     7044   8075   7513   -366   -247    135       C  
ATOM   4410  CE2 TYR D 145      -6.513 -11.242  14.456  1.00 55.29           C  
ANISOU 4410  CE2 TYR D 145     6643   7416   6947   -239   -198    174       C  
ATOM   4411  CZ  TYR D 145      -5.375 -10.554  14.007  1.00 57.39           C  
ANISOU 4411  CZ  TYR D 145     6859   7687   7260   -302   -191    162       C  
ATOM   4412  OH  TYR D 145      -5.167 -10.318  12.652  1.00 52.16           O  
ANISOU 4412  OH  TYR D 145     6231   6928   6658   -304   -130    175       O  
ATOM   4413  N   HIS D 146      -4.917 -10.687  21.106  1.00 59.09           N  
ANISOU 4413  N   HIS D 146     6802   8612   7038   -355   -533     67       N  
ATOM   4414  CA  HIS D 146      -4.408  -9.817  22.198  1.00 60.76           C  
ANISOU 4414  CA  HIS D 146     6959   8958   7169   -439   -611    -32       C  
ATOM   4415  C   HIS D 146      -3.123 -10.329  22.867  1.00 62.39           C  
ANISOU 4415  C   HIS D 146     7016   9360   7331   -439   -675     30       C  
ATOM   4416  O   HIS D 146      -2.618  -9.731  23.832  1.00 63.99           O  
ANISOU 4416  O   HIS D 146     7154   9705   7453   -507   -750    -49       O  
ATOM   4417  CB  HIS D 146      -5.496  -9.582  23.260  1.00 60.81           C  
ANISOU 4417  CB  HIS D 146     7029   9010   7066   -424   -634    -94       C  
ATOM   4418  CG  HIS D 146      -6.418  -8.450  22.922  1.00 61.87           C  
ANISOU 4418  CG  HIS D 146     7282   8998   7228   -474   -602   -217       C  
ATOM   4419  ND1 HIS D 146      -6.278  -7.189  23.465  1.00 61.81           N  
ANISOU 4419  ND1 HIS D 146     7289   9006   7189   -571   -639   -365       N  
ATOM   4420  CD2 HIS D 146      -7.472  -8.378  22.069  1.00 61.54           C  
ANISOU 4420  CD2 HIS D 146     7346   8789   7247   -437   -535   -213       C  
ATOM   4421  CE1 HIS D 146      -7.207  -6.392  22.967  1.00 61.38           C  
ANISOU 4421  CE1 HIS D 146     7350   8793   7180   -584   -590   -440       C  
ATOM   4422  NE2 HIS D 146      -7.944  -7.088  22.120  1.00 61.78           N  
ANISOU 4422  NE2 HIS D 146     7452   8739   7282   -501   -529   -346       N  
TER    4423      HIS D 146                                                      
HETATM 4424  CHA HEM A 201      -2.083  -1.185  -4.539  1.00 27.10           C  
ANISOU 4424  CHA HEM A 201     4169   3248   2881   -365    -85   -166       C  
HETATM 4425  CHB HEM A 201      -3.707   3.117  -3.132  1.00 24.63           C  
ANISOU 4425  CHB HEM A 201     3774   2958   2627   -351   -291     76       C  
HETATM 4426  CHC HEM A 201      -5.362   1.178   0.916  1.00 22.48           C  
ANISOU 4426  CHC HEM A 201     3241   2656   2642   -195   -326     75       C  
HETATM 4427  CHD HEM A 201      -3.223  -3.044  -0.166  1.00 22.87           C  
ANISOU 4427  CHD HEM A 201     3394   2622   2675   -183   -157    -98       C  
HETATM 4428  C1A HEM A 201      -2.321   0.156  -4.485  1.00 27.61           C  
ANISOU 4428  C1A HEM A 201     4227   3337   2926   -383   -130    -98       C  
HETATM 4429  C2A HEM A 201      -1.888   1.123  -5.453  1.00 31.41           C  
ANISOU 4429  C2A HEM A 201     4782   3842   3309   -440   -105    -80       C  
HETATM 4430  C3A HEM A 201      -2.330   2.329  -5.095  1.00 28.88           C  
ANISOU 4430  C3A HEM A 201     4446   3522   3004   -439   -168     -6       C  
HETATM 4431  C4A HEM A 201      -3.062   2.147  -3.860  1.00 27.49           C  
ANISOU 4431  C4A HEM A 201     4178   3330   2937   -378   -227     16       C  
HETATM 4432  CMA HEM A 201      -2.082   3.659  -5.846  1.00 25.16           C  
ANISOU 4432  CMA HEM A 201     4055   3056   2448   -493   -166     48       C  
HETATM 4433  CAA HEM A 201      -1.031   0.768  -6.668  1.00 35.58           C  
ANISOU 4433  CAA HEM A 201     5398   4388   3732   -492     -6   -140       C  
HETATM 4434  CBA HEM A 201      -1.895   0.437  -7.875  1.00 40.84           C  
ANISOU 4434  CBA HEM A 201     6192   5048   4277   -554    -70   -150       C  
HETATM 4435  CGA HEM A 201      -0.977   0.364  -9.075  1.00 45.54           C  
ANISOU 4435  CGA HEM A 201     6890   5666   4746   -614     43   -204       C  
HETATM 4436  O1A HEM A 201      -1.493   0.170 -10.210  1.00 48.69           O  
ANISOU 4436  O1A HEM A 201     7420   6069   5012   -679      4   -218       O  
HETATM 4437  O2A HEM A 201       0.275   0.493  -8.889  1.00 47.98           O  
ANISOU 4437  O2A HEM A 201     7147   5998   5087   -601    172   -236       O  
HETATM 4438  C1B HEM A 201      -4.318   2.954  -1.936  1.00 20.97           C  
ANISOU 4438  C1B HEM A 201     3225   2485   2258   -298   -323     89       C  
HETATM 4439  C2B HEM A 201      -5.021   4.000  -1.210  1.00 21.02           C  
ANISOU 4439  C2B HEM A 201     3192   2479   2315   -265   -376    141       C  
HETATM 4440  C3B HEM A 201      -5.492   3.468  -0.087  1.00 20.55           C  
ANISOU 4440  C3B HEM A 201     3056   2419   2334   -222   -380    134       C  
HETATM 4441  C4B HEM A 201      -5.093   2.076  -0.074  1.00 20.39           C  
ANISOU 4441  C4B HEM A 201     3030   2401   2315   -226   -337     86       C  
HETATM 4442  CMB HEM A 201      -5.179   5.427  -1.688  1.00 15.94           C  
ANISOU 4442  CMB HEM A 201     2602   1817   1639   -277   -414    195       C  
HETATM 4443  CAB HEM A 201      -6.323   4.131   1.027  1.00 21.54           C  
ANISOU 4443  CAB HEM A 201     3116   2535   2533   -174   -411    165       C  
HETATM 4444  CBB HEM A 201      -6.251   5.426   1.296  1.00 23.13           C  
ANISOU 4444  CBB HEM A 201     3325   2720   2744   -156   -418    193       C  
HETATM 4445  C1C HEM A 201      -4.851  -0.109   1.030  1.00 23.68           C  
ANISOU 4445  C1C HEM A 201     3399   2793   2804   -188   -281     36       C  
HETATM 4446  C2C HEM A 201      -4.927  -0.971   2.207  1.00 22.81           C  
ANISOU 4446  C2C HEM A 201     3248   2664   2755   -151   -262     38       C  
HETATM 4447  C3C HEM A 201      -4.311  -2.118   1.858  1.00 25.12           C  
ANISOU 4447  C3C HEM A 201     3574   2928   3043   -147   -223     -3       C  
HETATM 4448  C4C HEM A 201      -3.872  -2.019   0.496  1.00 24.66           C  
ANISOU 4448  C4C HEM A 201     3573   2878   2920   -183   -208    -40       C  
HETATM 4449  CMC HEM A 201      -5.563  -0.549   3.569  1.00 19.77           C  
ANISOU 4449  CMC HEM A 201     2805   2287   2421   -121   -276     78       C  
HETATM 4450  CAC HEM A 201      -4.056  -3.426   2.618  1.00 22.89           C  
ANISOU 4450  CAC HEM A 201     3291   2600   2808   -109   -193    -13       C  
HETATM 4451  CBC HEM A 201      -4.192  -3.468   3.931  1.00 27.61           C  
ANISOU 4451  CBC HEM A 201     3849   3196   3446    -73   -196     26       C  
HETATM 4452  C1D HEM A 201      -2.689  -2.917  -1.419  1.00 24.62           C  
ANISOU 4452  C1D HEM A 201     3675   2857   2823   -219   -122   -141       C  
HETATM 4453  C2D HEM A 201      -1.916  -3.934  -2.070  1.00 22.23           C  
ANISOU 4453  C2D HEM A 201     3419   2525   2503   -209    -48   -213       C  
HETATM 4454  C3D HEM A 201      -1.573  -3.334  -3.425  1.00 25.50           C  
ANISOU 4454  C3D HEM A 201     3902   2975   2811   -269    -17   -242       C  
HETATM 4455  C4D HEM A 201      -2.181  -2.030  -3.453  1.00 26.47           C  
ANISOU 4455  C4D HEM A 201     4019   3137   2903   -305    -86   -174       C  
HETATM 4456  CMD HEM A 201      -1.493  -5.290  -1.539  1.00 24.24           C  
ANISOU 4456  CMD HEM A 201     3668   2717   2826   -148     -5   -250       C  
HETATM 4457  CAD HEM A 201      -0.743  -3.981  -4.525  1.00 26.44           C  
ANISOU 4457  CAD HEM A 201     4093   3086   2869   -283     78   -327       C  
HETATM 4458  CBD HEM A 201       0.713  -4.005  -4.061  1.00 26.67           C  
ANISOU 4458  CBD HEM A 201     4038   3135   2960   -214    178   -354       C  
HETATM 4459  CGD HEM A 201       1.483  -4.702  -5.140  1.00 29.30           C  
ANISOU 4459  CGD HEM A 201     4434   3458   3241   -220    288   -448       C  
HETATM 4460  O1D HEM A 201       2.090  -4.043  -6.018  1.00 30.35           O  
ANISOU 4460  O1D HEM A 201     4596   3642   3293   -269    358   -470       O  
HETATM 4461  O2D HEM A 201       1.484  -5.937  -5.110  1.00 32.41           O  
ANISOU 4461  O2D HEM A 201     4855   3785   3673   -177    313   -504       O  
HETATM 4462  NA  HEM A 201      -3.037   0.813  -3.527  1.00 26.15           N  
ANISOU 4462  NA  HEM A 201     3977   3148   2810   -352   -202    -37       N  
HETATM 4463  NB  HEM A 201      -4.398   1.790  -1.221  1.00 21.42           N  
ANISOU 4463  NB  HEM A 201     3229   2537   2371   -268   -304     55       N  
HETATM 4464  NC  HEM A 201      -4.219  -0.773   0.027  1.00 22.97           N  
ANISOU 4464  NC  HEM A 201     3365   2695   2666   -213   -246    -10       N  
HETATM 4465  ND  HEM A 201      -2.848  -1.814  -2.263  1.00 21.78           N  
ANISOU 4465  ND  HEM A 201     3351   2536   2388   -270   -146   -121       N  
HETATM 4466 FE   HEM A 201      -3.682   0.022  -1.708  1.00 25.26          FE  
ANISOU 4466 FE   HEM A 201     3748   3010   2841   -275   -233    -26      FE  
HETATM 4467  O1  OXY A 202      -2.220   0.542  -1.242  1.00 23.91           O  
ANISOU 4467  O1  OXY A 202     3534   2863   2688   -248   -152    -36       O  
HETATM 4468  O2  OXY A 202      -1.486   0.372  -0.315  1.00 26.77           O  
ANISOU 4468  O2  OXY A 202     3832   3233   3108   -202   -116    -45       O  
HETATM 4469  CHA HEM B 201     -15.190   8.774  33.571  1.00 33.94           C  
ANISOU 4469  CHA HEM B 201     3675   5685   3535     94    262   -629       C  
HETATM 4470  CHB HEM B 201     -11.058   6.660  32.093  1.00 29.02           C  
ANISOU 4470  CHB HEM B 201     3215   4811   3000     16    128   -292       C  
HETATM 4471  CHC HEM B 201     -12.906   6.240  27.629  1.00 27.29           C  
ANISOU 4471  CHC HEM B 201     3094   4113   3161     -9    106   -301       C  
HETATM 4472  CHD HEM B 201     -16.969   8.450  29.049  1.00 29.67           C  
ANISOU 4472  CHD HEM B 201     3188   4649   3435     79    177   -559       C  
HETATM 4473  C1A HEM B 201     -13.860   8.365  33.538  1.00 33.97           C  
ANISOU 4473  C1A HEM B 201     3728   5662   3517     68    218   -555       C  
HETATM 4474  C2A HEM B 201     -12.837   8.578  34.540  1.00 35.94           C  
ANISOU 4474  C2A HEM B 201     3978   6036   3641     66    194   -577       C  
HETATM 4475  C3A HEM B 201     -11.714   8.006  34.134  1.00 33.54           C  
ANISOU 4475  C3A HEM B 201     3712   5666   3366     44    152   -476       C  
HETATM 4476  C4A HEM B 201     -11.956   7.380  32.854  1.00 30.78           C  
ANISOU 4476  C4A HEM B 201     3397   5144   3156     32    154   -395       C  
HETATM 4477  CMA HEM B 201     -10.402   8.025  34.950  1.00 31.31           C  
ANISOU 4477  CMA HEM B 201     3426   5495   2975     36    108   -460       C  
HETATM 4478  CAA HEM B 201     -12.925   9.365  35.864  1.00 41.56           C  
ANISOU 4478  CAA HEM B 201     4650   6938   4204     88    209   -709       C  
HETATM 4479  CBA HEM B 201     -14.034   8.890  36.779  1.00 44.42           C  
ANISOU 4479  CBA HEM B 201     4945   7476   4455     94    294   -675       C  
HETATM 4480  CGA HEM B 201     -14.546  10.127  37.528  1.00 47.43           C  
ANISOU 4480  CGA HEM B 201     5293   7963   4763    138    316   -888       C  
HETATM 4481  O1A HEM B 201     -13.759  10.567  38.418  1.00 45.37           O  
ANISOU 4481  O1A HEM B 201     5035   7830   4373    136    286   -969       O  
HETATM 4482  O2A HEM B 201     -15.692  10.650  37.232  1.00 44.81           O  
ANISOU 4482  O2A HEM B 201     4931   7591   4506    177    359   -979       O  
HETATM 4483  C1B HEM B 201     -11.196   6.352  30.749  1.00 29.48           C  
ANISOU 4483  C1B HEM B 201     3314   4702   3185      8    120   -265       C  
HETATM 4484  C2B HEM B 201     -10.211   5.716  29.887  1.00 28.99           C  
ANISOU 4484  C2B HEM B 201     3296   4527   3192      1     99   -186       C  
HETATM 4485  C3B HEM B 201     -10.748   5.612  28.683  1.00 29.28           C  
ANISOU 4485  C3B HEM B 201     3364   4435   3325     -7    100   -199       C  
HETATM 4486  C4B HEM B 201     -12.076   6.153  28.706  1.00 27.72           C  
ANISOU 4486  C4B HEM B 201     3137   4260   3134     -4    113   -273       C  
HETATM 4487  CMB HEM B 201      -8.787   5.212  30.209  1.00 28.42           C  
ANISOU 4487  CMB HEM B 201     3228   4480   3090      7     79   -101       C  
HETATM 4488  CAB HEM B 201     -10.048   5.011  27.463  1.00 30.14           C  
ANISOU 4488  CAB HEM B 201     3525   4410   3518    -12     88   -149       C  
HETATM 4489  CBB HEM B 201     -10.526   3.879  26.961  1.00 31.70           C  
ANISOU 4489  CBB HEM B 201     3736   4542   3768    -33    118    -82       C  
HETATM 4490  C1C HEM B 201     -14.149   6.839  27.621  1.00 27.83           C  
ANISOU 4490  C1C HEM B 201     3121   4208   3245      5    113   -371       C  
HETATM 4491  C2C HEM B 201     -14.972   7.023  26.449  1.00 26.77           C  
ANISOU 4491  C2C HEM B 201     2990   3990   3191      5     89   -398       C  
HETATM 4492  C3C HEM B 201     -16.096   7.622  26.854  1.00 25.40           C  
ANISOU 4492  C3C HEM B 201     2754   3880   3015     30    104   -459       C  
HETATM 4493  C4C HEM B 201     -16.010   7.830  28.278  1.00 29.71           C  
ANISOU 4493  C4C HEM B 201     3262   4554   3472     44    144   -484       C  
HETATM 4494  CMC HEM B 201     -14.555   6.600  24.997  1.00 22.91           C  
ANISOU 4494  CMC HEM B 201     2563   3376   2767    -16     55   -364       C  
HETATM 4495  CAC HEM B 201     -17.309   8.058  26.030  1.00 23.91           C  
ANISOU 4495  CAC HEM B 201     2528   3660   2896     48     82   -501       C  
HETATM 4496  CBC HEM B 201     -17.128   8.397  24.754  1.00 24.25           C  
ANISOU 4496  CBC HEM B 201     2616   3598   2998     55     27   -505       C  
HETATM 4497  C1D HEM B 201     -16.863   8.744  30.373  1.00 30.54           C  
ANISOU 4497  C1D HEM B 201     3264   4895   3442     97    215   -604       C  
HETATM 4498  C2D HEM B 201     -17.914   9.372  31.115  1.00 32.13           C  
ANISOU 4498  C2D HEM B 201     3389   5207   3610    139    261   -695       C  
HETATM 4499  C3D HEM B 201     -17.384   9.459  32.523  1.00 33.76           C  
ANISOU 4499  C3D HEM B 201     3584   5569   3673    143    296   -726       C  
HETATM 4500  C4D HEM B 201     -16.052   8.879  32.493  1.00 32.75           C  
ANISOU 4500  C4D HEM B 201     3521   5409   3513    103    259   -639       C  
HETATM 4501  CMD HEM B 201     -19.275   9.877  30.603  1.00 31.40           C  
ANISOU 4501  CMD HEM B 201     3233   5095   3604    180    271   -753       C  
HETATM 4502  CAD HEM B 201     -18.171  10.102  33.667  1.00 36.04           C  
ANISOU 4502  CAD HEM B 201     3799   6023   3872    189    358   -839       C  
HETATM 4503  CBD HEM B 201     -17.770  11.561  33.759  1.00 37.67           C  
ANISOU 4503  CBD HEM B 201     4036   6178   4100    248    320  -1019       C  
HETATM 4504  CGD HEM B 201     -18.475  12.091  34.971  1.00 40.96           C  
ANISOU 4504  CGD HEM B 201     4382   6771   4411    295    390  -1144       C  
HETATM 4505  O1D HEM B 201     -19.651  12.484  34.808  1.00 41.47           O  
ANISOU 4505  O1D HEM B 201     4381   6838   4539    347    430  -1203       O  
HETATM 4506  O2D HEM B 201     -17.869  12.075  36.078  1.00 43.80           O  
ANISOU 4506  O2D HEM B 201     4743   7280   4619    282    405  -1179       O  
HETATM 4507  NA  HEM B 201     -13.276   7.618  32.538  1.00 32.08           N  
ANISOU 4507  NA  HEM B 201     3536   5284   3369     42    189   -446       N  
HETATM 4508  NB  HEM B 201     -12.330   6.600  29.981  1.00 27.92           N  
ANISOU 4508  NB  HEM B 201     3116   4430   3064      9    132   -314       N  
HETATM 4509  NC  HEM B 201     -14.817   7.339  28.722  1.00 28.66           N  
ANISOU 4509  NC  HEM B 201     3168   4437   3287     25    143   -426       N  
HETATM 4510  ND  HEM B 201     -15.800   8.445  31.206  1.00 29.99           N  
ANISOU 4510  ND  HEM B 201     3221   4898   3278     79    218   -568       N  
HETATM 4511 FE   HEM B 201     -14.097   7.490  30.593  1.00 29.57          FE  
ANISOU 4511 FE   HEM B 201     3252   4739   3244     36    172   -436      FE  
HETATM 4512  O1  OXY B 202     -13.168   9.122  30.287  1.00 34.93           O  
ANISOU 4512  O1  OXY B 202     3976   5344   3953     70    105   -580       O  
HETATM 4513  O2  OXY B 202     -13.875   9.741  29.513  1.00 33.26           O  
ANISOU 4513  O2  OXY B 202     3766   5047   3825     93     93   -637       O  
HETATM 4514  CHA HEM C 201     -36.926   8.730  15.673  1.00 23.50           C  
ANISOU 4514  CHA HEM C 201     2571   2417   3940    181     82  -1051       C  
HETATM 4515  CHB HEM C 201     -36.155   6.131  11.712  1.00 20.77           C  
ANISOU 4515  CHB HEM C 201     2369   2086   3435    186    -42   -551       C  
HETATM 4516  CHC HEM C 201     -32.390   4.046  13.869  1.00 20.63           C  
ANISOU 4516  CHC HEM C 201     2387   2306   3145    -39     25   -538       C  
HETATM 4517  CHD HEM C 201     -33.419   6.279  18.017  1.00 26.51           C  
ANISOU 4517  CHD HEM C 201     3059   3120   3893   -120    113   -971       C  
HETATM 4518  C1A HEM C 201     -37.102   8.175  14.440  1.00 24.54           C  
ANISOU 4518  C1A HEM C 201     2726   2530   4069    213     35   -912       C  
HETATM 4519  C2A HEM C 201     -38.223   8.362  13.535  1.00 27.51           C  
ANISOU 4519  C2A HEM C 201     3070   2848   4537    307    -16   -887       C  
HETATM 4520  C3A HEM C 201     -37.999   7.633  12.447  1.00 22.86           C  
ANISOU 4520  C3A HEM C 201     2529   2267   3891    300    -55   -741       C  
HETATM 4521  C4A HEM C 201     -36.752   6.954  12.634  1.00 24.03           C  
ANISOU 4521  C4A HEM C 201     2730   2476   3925    211    -24   -680       C  
HETATM 4522  CMA HEM C 201     -38.875   7.542  11.187  1.00 23.41           C  
ANISOU 4522  CMA HEM C 201     2599   2288   4010    376   -132   -659       C  
HETATM 4523  CAA HEM C 201     -39.450   9.285  13.805  1.00 29.54           C  
ANISOU 4523  CAA HEM C 201     3242   3042   4939    405    -28  -1022       C  
HETATM 4524  CBA HEM C 201     -39.036  10.732  13.636  1.00 32.33           C  
ANISOU 4524  CBA HEM C 201     3646   3211   5427    446    -75  -1045       C  
HETATM 4525  CGA HEM C 201     -39.989  11.631  14.422  1.00 39.70           C  
ANISOU 4525  CGA HEM C 201     4487   4101   6496    528    -59  -1238       C  
HETATM 4526  O1A HEM C 201     -41.224  11.520  14.171  1.00 42.15           O  
ANISOU 4526  O1A HEM C 201     4704   4432   6879    617    -83  -1285       O  
HETATM 4527  O2A HEM C 201     -39.538  12.442  15.308  1.00 42.02           O  
ANISOU 4527  O2A HEM C 201     4790   4346   6828    505    -23  -1360       O  
HETATM 4528  C1B HEM C 201     -35.088   5.342  11.956  1.00 21.24           C  
ANISOU 4528  C1B HEM C 201     2454   2215   3399    118    -16   -513       C  
HETATM 4529  C2B HEM C 201     -34.600   4.362  11.035  1.00 18.78           C  
ANISOU 4529  C2B HEM C 201     2182   1938   3014    104    -28   -407       C  
HETATM 4530  C3B HEM C 201     -33.564   3.774  11.589  1.00 18.31           C  
ANISOU 4530  C3B HEM C 201     2127   1939   2891     50     -6   -407       C  
HETATM 4531  C4B HEM C 201     -33.360   4.341  12.928  1.00 19.44           C  
ANISOU 4531  C4B HEM C 201     2241   2097   3047     18     17   -507       C  
HETATM 4532  CMB HEM C 201     -35.138   4.047   9.644  1.00 16.49           C  
ANISOU 4532  CMB HEM C 201     1925   1621   2718    146    -70   -316       C  
HETATM 4533  CAB HEM C 201     -32.869   2.636  10.812  1.00 17.13           C  
ANISOU 4533  CAB HEM C 201     2007   1834   2669     38    -11   -322       C  
HETATM 4534  CBB HEM C 201     -31.631   2.343  11.028  1.00 21.52           C  
ANISOU 4534  CBB HEM C 201     2562   2417   3197      0      0   -314       C  
HETATM 4535  C1C HEM C 201     -32.363   4.443  15.189  1.00 22.41           C  
ANISOU 4535  C1C HEM C 201     2593   2566   3355    -75     40   -640       C  
HETATM 4536  C2C HEM C 201     -31.435   3.969  16.200  1.00 21.19           C  
ANISOU 4536  C2C HEM C 201     2443   2487   3123   -136     27   -663       C  
HETATM 4537  C3C HEM C 201     -31.751   4.568  17.341  1.00 20.38           C  
ANISOU 4537  C3C HEM C 201     2329   2408   3007   -165     47   -774       C  
HETATM 4538  C4C HEM C 201     -32.838   5.470  17.078  1.00 24.69           C  
ANISOU 4538  C4C HEM C 201     2852   2887   3641   -115     79   -834       C  
HETATM 4539  CMC HEM C 201     -30.334   2.900  15.962  1.00 21.00           C  
ANISOU 4539  CMC HEM C 201     2429   2507   3043   -153    -11   -582       C  
HETATM 4540  CAC HEM C 201     -31.131   4.431  18.741  1.00 19.59           C  
ANISOU 4540  CAC HEM C 201     2238   2390   2815   -235     33   -842       C  
HETATM 4541  CBC HEM C 201     -30.670   3.258  19.186  1.00 18.32           C  
ANISOU 4541  CBC HEM C 201     2102   2312   2546   -269     -7   -786       C  
HETATM 4542  C1D HEM C 201     -34.464   7.136  17.787  1.00 26.06           C  
ANISOU 4542  C1D HEM C 201     2968   2994   3942    -55    135  -1044       C  
HETATM 4543  C2D HEM C 201     -35.092   7.932  18.810  1.00 25.29           C  
ANISOU 4543  C2D HEM C 201     2833   2905   3870    -53    181  -1213       C  
HETATM 4544  C3D HEM C 201     -36.147   8.683  18.043  1.00 28.23           C  
ANISOU 4544  C3D HEM C 201     3163   3172   4392     49    174  -1242       C  
HETATM 4545  C4D HEM C 201     -36.088   8.260  16.667  1.00 24.58           C  
ANISOU 4545  C4D HEM C 201     2726   2653   3958     88    122  -1081       C  
HETATM 4546  CMD HEM C 201     -34.797   8.075  20.311  1.00 25.42           C  
ANISOU 4546  CMD HEM C 201     2854   3014   3790   -131    219  -1347       C  
HETATM 4547  CAD HEM C 201     -37.117   9.671  18.681  1.00 30.25           C  
ANISOU 4547  CAD HEM C 201     3355   3393   4745    104    214  -1426       C  
HETATM 4548  CBD HEM C 201     -38.231   8.808  19.253  1.00 32.07           C  
ANISOU 4548  CBD HEM C 201     3512   3781   4891     94    283  -1490       C  
HETATM 4549  CGD HEM C 201     -39.278   9.714  19.821  1.00 35.03           C  
ANISOU 4549  CGD HEM C 201     3799   4140   5372    158    334  -1688       C  
HETATM 4550  O1D HEM C 201     -40.353   9.858  19.171  1.00 34.67           O  
ANISOU 4550  O1D HEM C 201     3675   4056   5443    254    320  -1703       O  
HETATM 4551  O2D HEM C 201     -38.957  10.300  20.894  1.00 37.82           O  
ANISOU 4551  O2D HEM C 201     4161   4515   5695    114    381  -1832       O  
HETATM 4552  NA  HEM C 201     -36.226   7.303  13.860  1.00 24.93           N  
ANISOU 4552  NA  HEM C 201     2831   2619   4023    162     23   -781       N  
HETATM 4553  NB  HEM C 201     -34.310   5.308  13.107  1.00 21.98           N  
ANISOU 4553  NB  HEM C 201     2539   2361   3452     59     18   -576       N  
HETATM 4554  NC  HEM C 201     -33.193   5.386  15.756  1.00 23.49           N  
ANISOU 4554  NC  HEM C 201     2706   2671   3547    -58     64   -744       N  
HETATM 4555  ND  HEM C 201     -35.064   7.359  16.559  1.00 22.85           N  
ANISOU 4555  ND  HEM C 201     2554   2497   3631     22    110   -975       N  
HETATM 4556 FE   HEM C 201     -34.670   6.352  14.843  1.00 23.27          FE  
ANISOU 4556 FE   HEM C 201     2652   2531   3657     41     59   -765      FE  
HETATM 4557  O1  OXY C 202     -35.679   5.164  15.478  1.00 27.94           O  
ANISOU 4557  O1  OXY C 202     3203   3261   4152     29     91   -797       O  
HETATM 4558  O2  OXY C 202     -35.618   4.283  16.285  1.00 28.01           O  
ANISOU 4558  O2  OXY C 202     3213   3376   4053    -28    114   -810       O  
HETATM 4559  CHA HEM D 201     -10.841 -22.881  10.600  1.00 19.71           C  
ANISOU 4559  CHA HEM D 201     2390   2322   2778    301    223    543       C  
HETATM 4560  CHB HEM D 201     -14.368 -22.036  13.800  1.00 19.67           C  
ANISOU 4560  CHB HEM D 201     2395   2448   2630    213    107    552       C  
HETATM 4561  CHC HEM D 201     -14.683 -17.401  12.388  1.00 16.60           C  
ANISOU 4561  CHC HEM D 201     2092   2123   2092     91    -12    296       C  
HETATM 4562  CHD HEM D 201     -11.641 -18.459   8.776  1.00 13.99           C  
ANISOU 4562  CHD HEM D 201     1766   1659   1891    144    114    313       C  
HETATM 4563  C1A HEM D 201     -11.787 -23.078  11.587  1.00 22.51           C  
ANISOU 4563  C1A HEM D 201     2745   2692   3115    288    200    567       C  
HETATM 4564  C2A HEM D 201     -12.034 -24.287  12.290  1.00 23.02           C  
ANISOU 4564  C2A HEM D 201     2796   2723   3227    326    236    646       C  
HETATM 4565  C3A HEM D 201     -13.010 -24.063  13.166  1.00 22.81           C  
ANISOU 4565  C3A HEM D 201     2772   2735   3161    298    204    654       C  
HETATM 4566  C4A HEM D 201     -13.403 -22.686  13.049  1.00 19.40           C  
ANISOU 4566  C4A HEM D 201     2356   2360   2655    246    147    573       C  
HETATM 4567  CMA HEM D 201     -13.636 -25.094  14.141  1.00 22.70           C  
ANISOU 4567  CMA HEM D 201     2746   2703   3176    321    233    740       C  
HETATM 4568  CAA HEM D 201     -11.309 -25.610  12.031  1.00 30.79           C  
ANISOU 4568  CAA HEM D 201     3770   3630   4300    393    308    713       C  
HETATM 4569  CBA HEM D 201     -12.253 -26.543  11.248  1.00 35.70           C  
ANISOU 4569  CBA HEM D 201     4461   4113   4992    378    362    661       C  
HETATM 4570  CGA HEM D 201     -11.529 -27.842  10.916  1.00 40.09           C  
ANISOU 4570  CGA HEM D 201     5016   4570   5645    447    445    713       C  
HETATM 4571  O1A HEM D 201     -11.851 -28.449   9.860  1.00 43.94           O  
ANISOU 4571  O1A HEM D 201     5563   4942   6189    437    494    637       O  
HETATM 4572  O2A HEM D 201     -10.624 -28.260  11.683  1.00 42.94           O  
ANISOU 4572  O2A HEM D 201     5319   4971   6025    514    461    826       O  
HETATM 4573  C1B HEM D 201     -14.690 -20.720  13.720  1.00 17.48           C  
ANISOU 4573  C1B HEM D 201     2135   2214   2292    174     61    479       C  
HETATM 4574  C2B HEM D 201     -15.590 -20.059  14.643  1.00 19.43           C  
ANISOU 4574  C2B HEM D 201     2382   2525   2476    153     26    463       C  
HETATM 4575  C3B HEM D 201     -15.703 -18.800  14.279  1.00 16.79           C  
ANISOU 4575  C3B HEM D 201     2072   2204   2102    122     -7    387       C  
HETATM 4576  C4B HEM D 201     -14.859 -18.585  13.094  1.00 19.20           C  
ANISOU 4576  C4B HEM D 201     2392   2461   2441    118      6    359       C  
HETATM 4577  CMB HEM D 201     -16.314 -20.687  15.850  1.00 17.26           C  
ANISOU 4577  CMB HEM D 201     2084   2292   2183    167     34    527       C  
HETATM 4578  CAB HEM D 201     -16.590 -17.837  15.092  1.00 20.87           C  
ANISOU 4578  CAB HEM D 201     2598   2779   2551    102    -41    347       C  
HETATM 4579  CBB HEM D 201     -16.440 -16.541  14.952  1.00 21.48           C  
ANISOU 4579  CBB HEM D 201     2695   2874   2594     77    -70    282       C  
HETATM 4580  C1C HEM D 201     -13.972 -17.309  11.211  1.00 14.90           C  
ANISOU 4580  C1C HEM D 201     1891   1862   1907     92     11    280       C  
HETATM 4581  C2C HEM D 201     -13.991 -16.178  10.299  1.00 12.39           C  
ANISOU 4581  C2C HEM D 201     1613   1519   1574     68      6    225       C  
HETATM 4582  C3C HEM D 201     -13.139 -16.495   9.328  1.00 13.56           C  
ANISOU 4582  C3C HEM D 201     1761   1637   1755     81     40    236       C  
HETATM 4583  C4C HEM D 201     -12.545 -17.812   9.572  1.00 15.54           C  
ANISOU 4583  C4C HEM D 201     1973   1885   2046    115     69    291       C  
HETATM 4584  CMC HEM D 201     -14.861 -14.870  10.475  1.00  7.69           C  
ANISOU 4584  CMC HEM D 201     1055    930    937     43    -25    171       C  
HETATM 4585  CAC HEM D 201     -12.771 -15.664   8.105  1.00 13.76           C  
ANISOU 4585  CAC HEM D 201     1821   1632   1777     69     58    205       C  
HETATM 4586  CBC HEM D 201     -13.578 -14.676   7.706  1.00 14.79           C  
ANISOU 4586  CBC HEM D 201     1999   1744   1877     53     43    164       C  
HETATM 4587  C1D HEM D 201     -11.107 -19.723   8.905  1.00 16.91           C  
ANISOU 4587  C1D HEM D 201     2106   2010   2309    188    152    365       C  
HETATM 4588  C2D HEM D 201     -10.153 -20.350   7.996  1.00 17.70           C  
ANISOU 4588  C2D HEM D 201     2198   2074   2452    226    209    380       C  
HETATM 4589  C3D HEM D 201      -9.922 -21.718   8.602  1.00 19.82           C  
ANISOU 4589  C3D HEM D 201     2436   2320   2775    278    242    446       C  
HETATM 4590  C4D HEM D 201     -10.764 -21.779   9.776  1.00 18.85           C  
ANISOU 4590  C4D HEM D 201     2305   2225   2631    262    202    470       C  
HETATM 4591  CMD HEM D 201      -9.404 -19.887   6.682  1.00 14.34           C  
ANISOU 4591  CMD HEM D 201     1789   1635   2026    228    246    350       C  
HETATM 4592  CAD HEM D 201      -8.995 -22.825   8.037  1.00 20.41           C  
ANISOU 4592  CAD HEM D 201     2494   2345   2915    342    314    483       C  
HETATM 4593  CBD HEM D 201      -9.867 -23.577   7.022  1.00 26.45           C  
ANISOU 4593  CBD HEM D 201     3339   3003   3707    343    357    413       C  
HETATM 4594  CGD HEM D 201      -9.126 -24.537   6.088  1.00 28.23           C  
ANISOU 4594  CGD HEM D 201     3578   3159   3991    400    438    408       C  
HETATM 4595  O1D HEM D 201      -8.516 -24.141   5.105  1.00 30.56           O  
ANISOU 4595  O1D HEM D 201     3881   3463   4266    407    464    374       O  
HETATM 4596  O2D HEM D 201      -9.195 -25.753   6.263  1.00 35.21           O  
ANISOU 4596  O2D HEM D 201     4470   3968   4942    440    486    435       O  
HETATM 4597  NA  HEM D 201     -12.631 -22.112  12.092  1.00 18.92           N  
ANISOU 4597  NA  HEM D 201     2302   2290   2595    240    146    526       N  
HETATM 4598  NB  HEM D 201     -14.238 -19.804  12.781  1.00 16.17           N  
ANISOU 4598  NB  HEM D 201     1991   2036   2116    152     47    415       N  
HETATM 4599  NC  HEM D 201     -13.060 -18.269  10.752  1.00 17.64           N  
ANISOU 4599  NC  HEM D 201     2216   2185   2303    121     49    323       N  
HETATM 4600  ND  HEM D 201     -11.432 -20.594   9.932  1.00 15.93           N  
ANISOU 4600  ND  HEM D 201     1957   1894   2201    210    150    417       N  
HETATM 4601 FE   HEM D 201     -12.807 -20.193  11.390  1.00 17.42          FE  
ANISOU 4601 FE   HEM D 201     2147   2136   2334    178     93    418      FE  
HETATM 4602  O1  OXY D 202     -14.032 -20.766  10.613  1.00 25.94           O  
ANISOU 4602  O1  OXY D 202     3285   3130   3440    169    117    371       O  
HETATM 4603  O2  OXY D 202     -14.619 -20.893   9.573  1.00 29.68           O  
ANISOU 4603  O2  OXY D 202     3805   3544   3926    158    133    313       O  
HETATM 4604  O   HOH A 301      -7.954   7.539  12.922  1.00 10.01           O  
HETATM 4605  O   HOH A 302      -1.310  18.264  -3.141  1.00 36.52           O  
HETATM 4606  O   HOH A 303       8.703  -0.663   5.948  1.00 27.40           O  
HETATM 4607  O   HOH A 304      -8.810  -9.728   8.081  1.00 11.69           O  
HETATM 4608  O   HOH A 305       1.996 -10.357  10.097  1.00 22.19           O  
HETATM 4609  O   HOH A 306      -0.900  -7.703  -6.903  1.00 24.29           O  
HETATM 4610  O   HOH A 307     -10.520   5.589   6.407  1.00 33.31           O  
HETATM 4611  O   HOH A 308      -0.938   6.358  -7.556  1.00 23.25           O  
HETATM 4612  O   HOH A 309       9.254  17.574   9.369  1.00 27.87           O  
HETATM 4613  O   HOH A 310     -17.078   7.739  -1.116  1.00 28.82           O  
HETATM 4614  O   HOH A 311       3.117  -0.965  -5.733  1.00 30.89           O  
HETATM 4615  O   HOH A 312      -6.025   1.938  15.488  1.00 19.19           O  
HETATM 4616  O   HOH A 313     -13.262   0.869   5.629  1.00 20.88           O  
HETATM 4617  O   HOH A 314     -14.490   4.096  -8.679  1.00 34.24           O  
HETATM 4618  O   HOH A 315     -12.819   3.411   6.485  1.00 21.13           O  
HETATM 4619  O   HOH A 316     -16.398  -4.147   0.779  1.00 34.51           O  
HETATM 4620  O   HOH A 317       2.545  23.536   8.551  1.00 28.32           O  
HETATM 4621  O   HOH A 318      -5.244  20.982  -2.475  1.00 23.89           O  
HETATM 4622  O   HOH A 319       8.631  18.141   6.491  1.00 30.01           O  
HETATM 4623  O   HOH A 320     -10.985 -17.943  -5.428  1.00  8.62           O  
HETATM 4624  O   HOH A 321      -3.600  25.357  14.842  1.00 21.95           O  
HETATM 4625  O   HOH A 322      -8.755  24.615   6.853  1.00 23.46           O  
HETATM 4626  O   HOH A 323       9.853   7.691  -9.128  1.00 33.83           O  
HETATM 4627  O   HOH A 324      -5.348  24.276   9.863  1.00 32.02           O  
HETATM 4628  O   HOH A 325      -1.635  12.627  -8.104  1.00 17.67           O  
HETATM 4629  O   HOH A 326       9.478   4.936  -7.467  1.00 24.55           O  
HETATM 4630  O   HOH A 327     -12.791  12.528 -10.750  1.00 16.62           O  
HETATM 4631  O   HOH A 328       7.830   7.592  -1.410  1.00 30.34           O  
HETATM 4632  O   HOH A 329     -14.968  12.662  11.693  1.00 36.54           O  
HETATM 4633  O   HOH A 330     -14.074  23.558   9.858  1.00 23.19           O  
HETATM 4634  O   HOH A 331     -15.672   3.926   5.385  1.00 44.15           O  
HETATM 4635  O   HOH A 332       9.701  -0.729  12.132  1.00 51.75           O  
HETATM 4636  O   HOH A 333      10.829   8.998  -6.696  1.00 23.05           O  
HETATM 4637  O   HOH A 334      10.036   6.118   8.660  1.00 42.72           O  
HETATM 4638  O   HOH A 335      10.335   6.092  -4.876  1.00 24.83           O  
HETATM 4639  O   HOH A 336     -15.197   3.352  14.007  1.00 36.97           O  
HETATM 4640  O   HOH A 337     -16.569  12.013  -4.682  1.00 21.43           O  
HETATM 4641  O   HOH A 338       1.139  -2.378  17.464  1.00 21.51           O  
HETATM 4642  O   HOH A 339      -6.812  -8.044   8.420  1.00 22.98           O  
HETATM 4643  O   HOH A 340     -14.266  -6.912   8.600  1.00 18.35           O  
HETATM 4644  O   HOH A 341      10.906   2.545   2.728  1.00 25.77           O  
HETATM 4645  O   HOH A 342     -13.761  -6.825  -1.089  1.00 37.17           O  
HETATM 4646  O   HOH A 343     -10.697  22.652  15.533  1.00 18.08           O  
HETATM 4647  O   HOH A 344      -5.836  17.998 -10.564  1.00 36.25           O  
HETATM 4648  O   HOH A 345      -3.261   3.603 -10.484  1.00 26.08           O  
HETATM 4649  O   HOH A 346     -16.021  -5.056   8.702  1.00 13.47           O  
HETATM 4650  O   HOH A 347     -12.427   7.505  12.106  1.00 30.72           O  
HETATM 4651  O   HOH A 348      -3.554  14.649  -7.988  1.00 46.85           O  
HETATM 4652  O   HOH A 349      -2.504  -9.610  -1.377  1.00 26.06           O  
HETATM 4653  O   HOH A 350       4.722  -9.958   3.944  1.00 32.53           O  
HETATM 4654  O   HOH A 351      -1.232   4.117  -8.802  1.00 45.52           O  
HETATM 4655  O   HOH A 352     -16.502  23.077  -0.702  1.00 44.40           O  
HETATM 4656  O   HOH A 353      -9.420 -15.928  -6.019  1.00 24.78           O  
HETATM 4657  O   HOH A 354      -1.194 -10.128  -3.711  1.00 34.53           O  
HETATM 4658  O   HOH A 355     -13.894  17.965  -7.362  1.00 34.08           O  
HETATM 4659  O   HOH A 356      10.223   8.494   0.077  1.00 30.41           O  
HETATM 4660  O   HOH A 357     -11.730   5.307  10.812  1.00 34.36           O  
HETATM 4661  O   HOH A 358       1.081  -7.398  -2.715  1.00 41.10           O  
HETATM 4662  O   HOH A 359     -15.126  -1.883   9.459  1.00 56.30           O  
HETATM 4663  O   HOH A 360     -16.064  17.470   9.886  1.00 34.57           O  
HETATM 4664  O   HOH A 361      13.472  -2.557  -1.658  1.00 31.70           O  
HETATM 4665  O   HOH A 362      16.635   5.796   2.654  1.00 23.26           O  
HETATM 4666  O   HOH A 363      -9.098  24.649  12.003  1.00 23.98           O  
HETATM 4667  O   HOH A 364     -19.485  19.406  -6.416  1.00 25.89           O  
HETATM 4668  O   HOH A 365     -12.526   1.894  -9.287  1.00 28.96           O  
HETATM 4669  O   HOH A 366     -14.300 -11.812  -3.301  1.00 26.98           O  
HETATM 4670  O   HOH A 367       8.517  14.234  -0.430  1.00 47.22           O  
HETATM 4671  O   HOH A 368       3.650  -8.995  -2.699  1.00 29.81           O  
HETATM 4672  O   HOH A 369     -12.024  -0.413  -9.951  1.00 56.39           O  
HETATM 4673  O   HOH A 370      10.133   1.027  10.443  1.00 47.85           O  
HETATM 4674  O   HOH A 371     -18.880  16.978   9.913  1.00 22.40           O  
HETATM 4675  O   HOH A 372     -18.677   5.362   6.007  1.00 44.34           O  
HETATM 4676  O   HOH A 373      -9.353   9.868  13.941  1.00 23.72           O  
HETATM 4677  O   HOH A 374       5.541  -4.312  15.504  1.00 23.46           O  
HETATM 4678  O   HOH A 375      -9.658  -1.172  12.206  1.00 35.98           O  
HETATM 4679  O   HOH A 376       8.998  -6.117  -6.177  1.00 33.18           O  
HETATM 4680  O   HOH A 377       8.416  -8.580   8.153  1.00 34.53           O  
HETATM 4681  O   HOH A 378     -13.084  17.255 -11.245  1.00 26.14           O  
HETATM 4682  O   HOH A 379       6.806  -9.876   2.568  1.00 27.82           O  
HETATM 4683  O   HOH B 301     -23.737   8.745  21.729  1.00 12.06           O  
HETATM 4684  O   HOH B 302     -15.623  26.464  16.915  1.00 15.62           O  
HETATM 4685  O   HOH B 303       9.751   9.164  13.264  1.00 23.46           O  
HETATM 4686  O   HOH B 304      -1.955   4.121  15.562  1.00 16.37           O  
HETATM 4687  O   HOH B 305      -0.281   8.519  36.480  1.00 19.71           O  
HETATM 4688  O   HOH B 306      -6.288  19.365  31.574  1.00 12.07           O  
HETATM 4689  O   HOH B 307     -23.167  -0.838  26.125  1.00 35.64           O  
HETATM 4690  O   HOH B 308       7.196  -1.403  19.057  1.00 12.09           O  
HETATM 4691  O   HOH B 309      -7.740   2.899  13.261  1.00 23.06           O  
HETATM 4692  O   HOH B 310       5.731  -9.650  30.023  1.00 38.95           O  
HETATM 4693  O   HOH B 311       5.186  -1.794  38.810  1.00 26.10           O  
HETATM 4694  O   HOH B 312     -17.677  20.773  17.464  1.00 30.09           O  
HETATM 4695  O   HOH B 313       3.585  16.726  26.093  1.00 29.09           O  
HETATM 4696  O   HOH B 314       4.914  -1.608  34.627  1.00 21.33           O  
HETATM 4697  O   HOH B 315      -8.511  17.070  36.710  1.00 18.50           O  
HETATM 4698  O   HOH B 316     -17.701  24.130  15.990  1.00 16.90           O  
HETATM 4699  O   HOH B 317     -17.913  18.491  16.064  1.00 27.30           O  
HETATM 4700  O   HOH B 318     -24.716  20.025  28.171  1.00 11.80           O  
HETATM 4701  O   HOH B 319     -11.456  27.088  22.509  1.00 27.39           O  
HETATM 4702  O   HOH B 320     -10.752  -4.883  34.097  1.00 25.94           O  
HETATM 4703  O   HOH B 321     -14.350  14.486  35.558  1.00 27.05           O  
HETATM 4704  O   HOH B 322      -7.562   1.685  40.561  1.00 17.39           O  
HETATM 4705  O   HOH B 323      12.151   4.188  18.145  1.00 19.44           O  
HETATM 4706  O   HOH B 324      12.473  -2.683  29.479  1.00 32.46           O  
HETATM 4707  O   HOH B 325     -10.178  22.967  34.023  1.00 19.15           O  
HETATM 4708  O   HOH B 326      13.629   4.502  23.396  1.00 34.25           O  
HETATM 4709  O   HOH B 327      13.370   4.440  14.505  1.00 29.34           O  
HETATM 4710  O   HOH B 328      -7.384   6.679  37.044  1.00 30.43           O  
HETATM 4711  O   HOH B 329     -18.331  -2.283  19.423  1.00 23.93           O  
HETATM 4712  O   HOH B 330     -24.952  12.229  29.662  1.00 23.73           O  
HETATM 4713  O   HOH B 331       5.088  -3.123  19.772  1.00 18.95           O  
HETATM 4714  O   HOH B 332     -20.502  28.684  19.527  1.00 23.97           O  
HETATM 4715  O   HOH B 333      12.545   1.429  18.460  1.00 20.11           O  
HETATM 4716  O   HOH B 334       7.886  -2.650  16.730  1.00 23.32           O  
HETATM 4717  O   HOH B 335      10.255  -3.611  16.470  1.00 23.22           O  
HETATM 4718  O   HOH B 336      -4.122  -6.464  41.764  1.00 30.91           O  
HETATM 4719  O   HOH B 337     -22.050  -3.395  19.488  1.00 23.41           O  
HETATM 4720  O   HOH B 338     -10.274   6.514  38.529  1.00 27.36           O  
HETATM 4721  O   HOH B 339      -3.982  21.514  25.066  1.00 27.88           O  
HETATM 4722  O   HOH B 340      -9.774   6.272  14.089  1.00 36.78           O  
HETATM 4723  O   HOH B 341     -24.537   6.999  29.583  1.00 31.31           O  
HETATM 4724  O   HOH B 342       7.823   6.684  32.985  1.00 30.32           O  
HETATM 4725  O   HOH B 343      -9.509  -2.073  14.705  1.00 20.94           O  
HETATM 4726  O   HOH B 344     -15.284   8.077  38.932  1.00 20.07           O  
HETATM 4727  O   HOH B 345       9.107  -5.126  20.416  1.00 17.68           O  
HETATM 4728  O   HOH B 346      11.784  -5.727  30.229  1.00 29.49           O  
HETATM 4729  O   HOH B 347       5.746  15.801  24.698  1.00 48.55           O  
HETATM 4730  O   HOH B 348     -24.666  -1.814  31.143  1.00 37.71           O  
HETATM 4731  O   HOH B 349       4.443  17.905  15.678  1.00 26.56           O  
HETATM 4732  O   HOH B 350      -3.051 -12.416  29.097  1.00 40.48           O  
HETATM 4733  O   HOH B 351     -23.999  18.214  21.984  1.00 30.61           O  
HETATM 4734  O   HOH B 352     -23.464   0.930  24.235  1.00 43.68           O  
HETATM 4735  O   HOH B 353     -10.608   0.830  38.031  1.00 22.04           O  
HETATM 4736  O   HOH B 354      12.675  13.876  24.244  1.00 26.80           O  
HETATM 4737  O   HOH B 355      -1.760  13.108  36.756  1.00 18.11           O  
HETATM 4738  O   HOH B 356     -20.051  20.102  18.726  1.00 37.32           O  
HETATM 4739  O   HOH B 357     -10.213  16.766  38.821  1.00 28.33           O  
HETATM 4740  O   HOH B 358      11.377  16.434  16.138  1.00 24.54           O  
HETATM 4741  O   HOH B 359      15.198  -0.550  24.567  1.00 38.47           O  
HETATM 4742  O   HOH B 360       2.323  -6.431  37.652  1.00 43.48           O  
HETATM 4743  O   HOH B 361      -5.972  20.869  33.712  1.00 27.92           O  
HETATM 4744  O   HOH B 362     -27.195  -1.781  28.940  1.00 37.02           O  
HETATM 4745  O   HOH B 363      -0.491   0.666  38.197  1.00 34.52           O  
HETATM 4746  O   HOH B 364       9.943  14.362  21.165  1.00 31.27           O  
HETATM 4747  O   HOH B 365      -9.050  25.871  25.629  1.00 40.86           O  
HETATM 4748  O   HOH B 366       9.667  -2.951  19.934  1.00 23.25           O  
HETATM 4749  O   HOH B 367      10.107   6.454  20.481  1.00 30.31           O  
HETATM 4750  O   HOH B 368      13.152  -6.629  23.091  1.00 32.18           O  
HETATM 4751  O   HOH B 369     -14.488  17.731  34.561  1.00 25.96           O  
HETATM 4752  O   HOH C 301     -47.753 -12.249   3.965  1.00  5.48           O  
HETATM 4753  O   HOH C 302     -43.387   4.935   3.936  1.00 18.66           O  
HETATM 4754  O   HOH C 303     -41.122  -2.938  -3.281  1.00 19.46           O  
HETATM 4755  O   HOH C 304     -35.860 -15.123   4.931  1.00  8.38           O  
HETATM 4756  O   HOH C 305     -41.888   7.355   9.095  1.00 10.52           O  
HETATM 4757  O   HOH C 306     -45.442   1.524  -0.071  1.00 26.42           O  
HETATM 4758  O   HOH C 307     -38.265 -18.251  -2.313  1.00 19.31           O  
HETATM 4759  O   HOH C 308     -45.635  -6.942  16.239  1.00 21.41           O  
HETATM 4760  O   HOH C 309     -26.946  17.129  21.349  1.00 36.15           O  
HETATM 4761  O   HOH C 310     -26.319  -9.871  -3.741  1.00  7.61           O  
HETATM 4762  O   HOH C 311     -22.600  12.358  15.008  1.00 33.52           O  
HETATM 4763  O   HOH C 312     -31.491  -9.394  27.334  1.00 18.59           O  
HETATM 4764  O   HOH C 313     -24.725  -6.708  -6.716  1.00 13.18           O  
HETATM 4765  O   HOH C 314     -46.319 -10.590  13.078  1.00 19.12           O  
HETATM 4766  O   HOH C 315     -26.278   5.943   1.588  1.00 24.88           O  
HETATM 4767  O   HOH C 316     -38.381 -15.493  -2.729  1.00 25.07           O  
HETATM 4768  O   HOH C 317     -34.818  -6.272  27.728  1.00 34.24           O  
HETATM 4769  O   HOH C 318     -33.896 -17.362   4.702  1.00 29.80           O  
HETATM 4770  O   HOH C 319     -35.580  10.245  -3.148  1.00 22.86           O  
HETATM 4771  O   HOH C 320     -36.263 -22.056   3.620  1.00 41.79           O  
HETATM 4772  O   HOH C 321     -27.199  -4.234   9.770  1.00 33.88           O  
HETATM 4773  O   HOH C 322     -26.030   3.335  23.089  1.00 26.81           O  
HETATM 4774  O   HOH C 323     -26.781  -4.732 -10.854  1.00 17.38           O  
HETATM 4775  O   HOH C 324     -41.575 -13.675  16.219  1.00 12.23           O  
HETATM 4776  O   HOH C 325     -28.161 -19.595  -5.664  1.00 14.69           O  
HETATM 4777  O   HOH C 326     -18.667   4.256  18.121  1.00 22.55           O  
HETATM 4778  O   HOH C 327     -31.897 -15.276  -4.648  1.00 18.36           O  
HETATM 4779  O   HOH C 328     -25.917  -9.487   8.115  1.00 22.44           O  
HETATM 4780  O   HOH C 329     -22.218   4.037  23.073  1.00 19.00           O  
HETATM 4781  O   HOH C 330     -31.365  10.132  26.441  1.00 19.62           O  
HETATM 4782  O   HOH C 331     -22.064  -8.961  -1.765  1.00 25.87           O  
HETATM 4783  O   HOH C 332     -29.612 -18.928  -3.412  1.00 13.00           O  
HETATM 4784  O   HOH C 333     -46.012  -0.481   4.270  1.00 17.36           O  
HETATM 4785  O   HOH C 334     -30.333  11.498  22.920  1.00 20.16           O  
HETATM 4786  O   HOH C 335     -35.784 -18.547  -1.848  1.00 15.34           O  
HETATM 4787  O   HOH C 336     -29.380 -11.533  -6.858  1.00 15.58           O  
HETATM 4788  O   HOH C 337     -20.200   2.768   4.860  1.00 42.63           O  
HETATM 4789  O   HOH C 338     -26.726  -8.217  10.281  1.00 21.18           O  
HETATM 4790  O   HOH C 339     -45.998   5.854   9.912  1.00 24.44           O  
HETATM 4791  O   HOH C 340     -32.926  -2.558 -10.096  1.00 39.20           O  
HETATM 4792  O   HOH C 341     -47.337   6.210  12.900  1.00 33.79           O  
HETATM 4793  O   HOH C 342     -44.036  -2.273  -1.885  1.00 27.24           O  
HETATM 4794  O   HOH C 343     -36.587 -11.978  -3.703  1.00 16.52           O  
HETATM 4795  O   HOH C 344     -46.449  -1.203  15.174  1.00 20.78           O  
HETATM 4796  O   HOH C 345     -35.015   1.728  -8.762  1.00 48.36           O  
HETATM 4797  O   HOH C 346     -44.282   6.313  19.710  1.00 22.56           O  
HETATM 4798  O   HOH C 347     -48.013   0.301  27.671  1.00 32.78           O  
HETATM 4799  O   HOH C 348     -26.785   3.206  -5.989  1.00 32.83           O  
HETATM 4800  O   HOH C 349     -45.040   1.218   5.912  1.00 20.39           O  
HETATM 4801  O   HOH C 350     -45.583  -0.885   1.577  1.00 13.01           O  
HETATM 4802  O   HOH C 351     -18.028   3.961  15.671  1.00 18.48           O  
HETATM 4803  O   HOH C 352     -32.039 -18.226  -5.128  1.00 22.01           O  
HETATM 4804  O   HOH C 353     -49.664   2.910  16.478  1.00 25.46           O  
HETATM 4805  O   HOH C 354     -45.399 -15.545   9.224  1.00 32.37           O  
HETATM 4806  O   HOH C 355     -29.718   6.029  -2.639  1.00 25.44           O  
HETATM 4807  O   HOH C 356     -23.031  -5.483   7.585  1.00 46.00           O  
HETATM 4808  O   HOH C 357     -32.048  20.497  10.407  1.00 22.63           O  
HETATM 4809  O   HOH C 358     -24.511  -0.381  21.836  1.00 36.99           O  
HETATM 4810  O   HOH C 359     -41.770  -0.292  -0.473  1.00 35.05           O  
HETATM 4811  O   HOH C 360     -40.790  -5.578  -6.560  1.00 21.52           O  
HETATM 4812  O   HOH C 361     -51.815   2.069  11.941  1.00 18.81           O  
HETATM 4813  O   HOH C 362     -35.637   5.476  -7.008  1.00 27.80           O  
HETATM 4814  O   HOH C 363     -49.055  -8.192   9.707  1.00 27.27           O  
HETATM 4815  O   HOH C 364     -46.632 -12.613   8.635  1.00 15.30           O  
HETATM 4816  O   HOH C 365     -35.863 -14.080  -2.338  1.00 19.52           O  
HETATM 4817  O   HOH C 366     -34.496 -19.937   4.987  1.00 54.27           O  
HETATM 4818  O   HOH C 367     -41.432  -8.398  21.455  1.00 39.10           O  
HETATM 4819  O   HOH C 368     -34.442 -15.044  -5.034  1.00 20.08           O  
HETATM 4820  O   HOH C 369     -32.986   9.915  23.322  1.00 25.20           O  
HETATM 4821  O   HOH C 370     -44.554   7.588   9.346  1.00 15.08           O  
HETATM 4822  O   HOH C 371     -45.674   3.348   4.425  1.00 21.37           O  
HETATM 4823  O   HOH C 372     -42.260  -2.433  23.742  1.00 33.55           O  
HETATM 4824  O   HOH C 373     -48.340  -3.261   8.087  1.00 31.65           O  
HETATM 4825  O   HOH C 374     -32.713  16.290   9.197  1.00 58.12           O  
HETATM 4826  O   HOH C 375     -37.234   3.286  -6.906  1.00 21.04           O  
HETATM 4827  O   HOH C 376     -28.396  20.696  16.883  1.00 17.15           O  
HETATM 4828  O   HOH C 377     -24.570   9.503  14.795  1.00 19.81           O  
HETATM 4829  O   HOH C 378     -37.733   9.097  -6.085  1.00 32.79           O  
HETATM 4830  O   HOH C 379     -45.502   1.241   8.682  1.00 20.03           O  
HETATM 4831  O   HOH C 380     -44.556  -3.150  22.587  1.00 28.63           O  
HETATM 4832  O   HOH C 381     -22.804   9.902  12.864  1.00 27.14           O  
HETATM 4833  O   HOH C 382     -23.434  -7.194   2.123  1.00 23.40           O  
HETATM 4834  O   HOH C 383     -34.571 -21.768   1.652  1.00 31.80           O  
HETATM 4835  O   HOH C 384     -40.369   0.418  -5.553  1.00 28.49           O  
HETATM 4836  O   HOH C 385     -37.225  12.453   6.027  1.00 30.72           O  
HETATM 4837  O   HOH C 386     -46.925  -5.595  -0.831  1.00 28.16           O  
HETATM 4838  O   HOH C 387     -41.539   9.687  10.875  1.00 29.36           O  
HETATM 4839  O   HOH C 388     -51.235   2.123  14.569  1.00 28.18           O  
HETATM 4840  O   HOH C 389     -42.236  -3.420  -5.952  1.00 26.23           O  
HETATM 4841  O   HOH C 390     -47.532  -8.258  -0.725  1.00 27.84           O  
HETATM 4842  O   HOH C 391     -41.751   2.607  -4.796  1.00 49.82           O  
HETATM 4843  O   HOH C 392     -43.371  -1.918   0.835  1.00 21.17           O  
HETATM 4844  O   HOH C 393     -47.721   1.878   8.326  1.00 17.43           O  
HETATM 4845  O   HOH C 394     -32.066  14.772   2.730  1.00 37.68           O  
HETATM 4846  O   HOH C 395     -39.448  10.839  -6.213  1.00 29.15           O  
HETATM 4847  O   HOH C 396     -28.530   8.867  -1.523  1.00 16.96           O  
HETATM 4848  O   HOH C 397     -24.748  15.859  11.423  1.00 31.70           O  
HETATM 4849  O   HOH C 398     -43.999   7.802  17.371  1.00 28.12           O  
HETATM 4850  O   HOH D 301     -32.116 -13.943  27.110  1.00 15.89           O  
HETATM 4851  O   HOH D 302     -33.214 -23.455   7.977  1.00 37.85           O  
HETATM 4852  O   HOH D 303     -32.030 -27.927  28.247  1.00 27.54           O  
HETATM 4853  O   HOH D 304     -10.230 -10.173   3.483  1.00  4.69           O  
HETATM 4854  O   HOH D 305     -25.560 -24.179  -5.570  1.00 14.37           O  
HETATM 4855  O   HOH D 306      -9.567 -24.585  20.710  1.00 15.20           O  
HETATM 4856  O   HOH D 307      -4.619  -9.842   7.591  1.00 26.48           O  
HETATM 4857  O   HOH D 308       1.028 -19.858  16.543  1.00 15.20           O  
HETATM 4858  O   HOH D 309     -31.487 -21.035   8.153  1.00 29.92           O  
HETATM 4859  O   HOH D 310     -15.676 -28.457  17.176  1.00 19.06           O  
HETATM 4860  O   HOH D 311     -20.912 -11.597  -2.890  1.00 19.91           O  
HETATM 4861  O   HOH D 312     -12.954 -28.499  14.380  1.00 24.87           O  
HETATM 4862  O   HOH D 313     -38.832 -19.195   9.391  1.00 19.76           O  
HETATM 4863  O   HOH D 314      -6.070 -15.456  -0.848  1.00 20.14           O  
HETATM 4864  O   HOH D 315     -37.466 -10.435  28.029  1.00 24.03           O  
HETATM 4865  O   HOH D 316     -12.606 -27.408   7.183  1.00 32.56           O  
HETATM 4866  O   HOH D 317      -6.559  -6.214  10.674  1.00 19.28           O  
HETATM 4867  O   HOH D 318     -13.798 -10.416  19.343  1.00 26.68           O  
HETATM 4868  O   HOH D 319     -29.024 -10.124  17.132  1.00 11.46           O  
HETATM 4869  O   HOH D 320     -25.006 -17.241  -8.805  1.00 21.98           O  
HETATM 4870  O   HOH D 321     -17.645 -19.183  29.564  1.00 19.38           O  
HETATM 4871  O   HOH D 322     -17.023 -11.998  -5.134  1.00 36.28           O  
HETATM 4872  O   HOH D 323     -34.862 -22.379  23.195  1.00 15.12           O  
HETATM 4873  O   HOH D 324     -22.958 -28.668   6.071  1.00 20.27           O  
HETATM 4874  O   HOH D 325     -10.574 -20.401  -7.659  1.00 15.90           O  
HETATM 4875  O   HOH D 326     -17.230 -24.574  25.755  1.00 11.22           O  
HETATM 4876  O   HOH D 327     -35.848 -24.234  22.010  1.00 29.95           O  
HETATM 4877  O   HOH D 328     -23.910 -14.842  -8.085  1.00 27.45           O  
HETATM 4878  O   HOH D 329      -7.941  -4.177  13.372  1.00 26.47           O  
HETATM 4879  O   HOH D 330      -6.675 -18.354   0.832  1.00 20.82           O  
HETATM 4880  O   HOH D 331     -28.051 -30.158  17.241  1.00 25.41           O  
HETATM 4881  O   HOH D 332     -13.232 -19.584  -8.085  1.00 18.67           O  
HETATM 4882  O   HOH D 333     -24.688  -7.842  16.482  1.00 16.69           O  
HETATM 4883  O   HOH D 334      -9.472 -18.565  23.865  1.00 19.04           O  
HETATM 4884  O   HOH D 335     -10.623 -20.629  -5.155  1.00 15.06           O  
HETATM 4885  O   HOH D 336     -28.167 -10.438  24.420  1.00 13.94           O  
HETATM 4886  O   HOH D 337      -3.592 -14.243   5.864  1.00 35.49           O  
HETATM 4887  O   HOH D 338     -31.881 -14.080  31.536  1.00 31.35           O  
HETATM 4888  O   HOH D 339     -39.787 -21.867   8.595  1.00 28.33           O  
HETATM 4889  O   HOH D 340     -24.126  -7.378  11.312  1.00 29.89           O  
HETATM 4890  O   HOH D 341      -6.552 -18.774   5.021  1.00 20.46           O  
HETATM 4891  O   HOH D 342     -35.552 -27.181   8.749  1.00 47.32           O  
HETATM 4892  O   HOH D 343     -26.020 -32.461  10.728  1.00 25.51           O  
HETATM 4893  O   HOH D 344     -10.267 -11.329  23.340  1.00 14.75           O  
HETATM 4894  O   HOH D 345     -17.068 -25.526  34.954  1.00 10.70           O  
HETATM 4895  O   HOH D 346     -19.880 -25.268  -6.471  1.00 21.82           O  
HETATM 4896  O   HOH D 347       2.324 -16.380  10.583  1.00 27.90           O  
HETATM 4897  O   HOH D 348     -13.128 -27.885   4.134  1.00 34.10           O  
HETATM 4898  O   HOH D 349      -3.311 -13.406  25.421  1.00 28.77           O  
HETATM 4899  O   HOH D 350     -19.707 -25.315  31.244  1.00 14.84           O  
HETATM 4900  O   HOH D 351     -18.856 -32.748   6.146  1.00 22.69           O  
HETATM 4901  O   HOH D 352     -14.557 -26.473  -6.325  1.00 10.94           O  
HETATM 4902  O   HOH D 353     -38.750 -19.801  24.157  1.00 11.48           O  
HETATM 4903  O   HOH D 354     -31.029 -25.486  31.381  1.00 19.53           O  
HETATM 4904  O   HOH D 355     -12.822 -26.936  20.919  1.00 23.16           O  
HETATM 4905  O   HOH D 356     -29.746 -13.190  27.507  1.00 26.30           O  
HETATM 4906  O   HOH D 357     -15.771 -28.517  14.781  1.00 24.16           O  
HETATM 4907  O   HOH D 358     -18.796 -15.971 -11.979  1.00 31.99           O  
HETATM 4908  O   HOH D 359      -7.611 -21.108   1.715  1.00 24.19           O  
HETATM 4909  O   HOH D 360     -17.946 -31.655  12.974  1.00 31.41           O  
HETATM 4910  O   HOH D 361      -2.536 -14.820   3.078  1.00 22.70           O  
HETATM 4911  O   HOH D 362     -20.233 -29.462  19.334  1.00 24.95           O  
HETATM 4912  O   HOH D 363     -36.946 -20.555  22.472  1.00 22.15           O  
HETATM 4913  O   HOH D 364     -17.252 -10.044  21.626  1.00 18.65           O  
HETATM 4914  O   HOH D 365     -17.444 -31.538   7.903  1.00 17.75           O  
HETATM 4915  O   HOH D 366     -40.762 -15.081  18.120  1.00 24.85           O  
HETATM 4916  O   HOH D 367       0.353 -23.468  16.343  1.00 41.80           O  
HETATM 4917  O   HOH D 368      -9.193 -26.081   8.897  1.00 29.86           O  
HETATM 4918  O   HOH D 369      -4.851 -10.787  -0.609  1.00 28.69           O  
HETATM 4919  O   HOH D 370     -40.084 -10.774  24.823  1.00 29.06           O  
HETATM 4920  O   HOH D 371      -2.121 -15.985   7.116  1.00 26.72           O  
HETATM 4921  O   HOH D 372      -8.001 -14.005  14.641  1.00 28.30           O  
HETATM 4922  O   HOH D 373     -18.965 -31.630   1.754  1.00 17.74           O  
HETATM 4923  O   HOH D 374     -33.067 -15.762  29.470  1.00 24.60           O  
HETATM 4924  O   HOH D 375     -33.259 -11.514  27.449  1.00 26.58           O  
HETATM 4925  O   HOH D 376     -20.319 -19.745 -11.030  1.00 21.66           O  
HETATM 4926  O   HOH D 377      -2.078 -25.183  17.477  1.00 36.22           O  
HETATM 4927  O   HOH D 378     -21.905  -5.174  11.545  1.00 58.69           O  
HETATM 4928  O   HOH D 379       2.424 -18.700  11.730  1.00 33.06           O  
HETATM 4929  O   HOH D 380     -28.973 -26.988  31.477  1.00 28.66           O  
HETATM 4930  O   HOH D 381     -14.551 -19.530  29.504  1.00 41.94           O  
HETATM 4931  O   HOH D 382     -28.731 -33.107   8.993  1.00 33.74           O  
HETATM 4932  O   HOH D 383     -20.654 -34.514  22.756  1.00 30.92           O  
HETATM 4933  O   HOH D 384      -5.785 -17.196  -3.086  1.00 24.28           O  
HETATM 4934  O   HOH D 385     -31.230 -19.911   6.046  1.00 37.34           O  
HETATM 4935  O   HOH D 386     -17.554 -26.853  -6.821  1.00 12.31           O  
HETATM 4936  O   HOH D 387     -34.049 -29.639  22.454  1.00 21.37           O  
HETATM 4937  O   HOH D 388     -25.553 -25.550  28.027  1.00 66.35           O  
HETATM 4938  O   HOH D 389     -26.193 -26.041  -3.905  1.00 30.00           O  
HETATM 4939  O   HOH D 390     -13.029 -17.093  -7.131  1.00 18.41           O  
HETATM 4940  O   HOH D 391     -13.604 -20.349 -10.719  1.00 24.21           O  
HETATM 4941  O   HOH D 392     -11.819 -27.619  16.605  1.00 26.39           O  
HETATM 4942  O   HOH D 393     -35.710 -22.001   7.009  1.00 27.40           O  
HETATM 4943  O   HOH D 394       1.991 -15.634  18.866  1.00 36.51           O  
HETATM 4944  O   HOH D 395     -35.845 -25.653   6.117  1.00 44.88           O  
HETATM 4945  O   HOH D 396      -8.097 -13.357  31.815  1.00 33.24           O  
HETATM 4946  O   HOH D 397     -11.609 -12.607  33.472  1.00 28.32           O  
HETATM 4947  O   HOH D 398     -11.820  -9.632  28.654  1.00 26.69           O  
HETATM 4948  O   HOH D 399     -25.750 -13.290  -6.793  1.00 18.18           O  
HETATM 4949  O   HOH D 400      -4.574  -5.715  23.816  1.00 40.77           O  
HETATM 4950  O   HOH D 401      -9.568 -11.827  25.915  1.00 49.37           O  
HETATM 4951  O   HOH D 402     -11.561  -5.251  14.153  1.00 33.06           O  
HETATM 4952  O   HOH D 403     -39.422 -23.905  15.599  1.00 21.00           O  
HETATM 4953  O   HOH D 404     -19.515 -29.864  29.968  1.00 15.17           O  
HETATM 4954  O   HOH D 405     -30.591 -23.966  33.231  1.00 28.80           O  
HETATM 4955  O   HOH D 406     -36.533 -22.582  26.610  1.00 37.78           O  
HETATM 4956  O   HOH D 407     -34.488 -27.596  13.237  1.00 32.23           O  
HETATM 4957  O   HOH D 408     -17.594 -28.640  24.692  1.00 31.92           O  
HETATM 4958  O   HOH D 409      -7.490 -18.657  25.810  1.00 41.28           O  
HETATM 4959  O   HOH D 410      -4.146 -13.981  -0.923  1.00 34.49           O  
HETATM 4960  O   HOH D 411     -37.746 -16.947  28.024  1.00 20.03           O  
HETATM 4961  O   HOH D 412     -38.474 -17.511  25.309  1.00 14.46           O  
HETATM 4962  O   HOH D 413     -24.998  -6.231  14.508  1.00 35.39           O  
HETATM 4963  O   HOH D 414     -13.891  -5.428  15.761  1.00 35.79           O  
CONECT  669 4466                                                                
CONECT 1773 4511                                                                
CONECT 2881 4556                                                                
CONECT 3985 4601                                                                
CONECT 4424 4428 4455                                                           
CONECT 4425 4431 4438                                                           
CONECT 4426 4441 4445                                                           
CONECT 4427 4448 4452                                                           
CONECT 4428 4424 4429 4462                                                      
CONECT 4429 4428 4430 4433                                                      
CONECT 4430 4429 4431 4432                                                      
CONECT 4431 4425 4430 4462                                                      
CONECT 4432 4430                                                                
CONECT 4433 4429 4434                                                           
CONECT 4434 4433 4435                                                           
CONECT 4435 4434 4436 4437                                                      
CONECT 4436 4435                                                                
CONECT 4437 4435                                                                
CONECT 4438 4425 4439 4463                                                      
CONECT 4439 4438 4440 4442                                                      
CONECT 4440 4439 4441 4443                                                      
CONECT 4441 4426 4440 4463                                                      
CONECT 4442 4439                                                                
CONECT 4443 4440 4444                                                           
CONECT 4444 4443                                                                
CONECT 4445 4426 4446 4464                                                      
CONECT 4446 4445 4447 4449                                                      
CONECT 4447 4446 4448 4450                                                      
CONECT 4448 4427 4447 4464                                                      
CONECT 4449 4446                                                                
CONECT 4450 4447 4451                                                           
CONECT 4451 4450                                                                
CONECT 4452 4427 4453 4465                                                      
CONECT 4453 4452 4454 4456                                                      
CONECT 4454 4453 4455 4457                                                      
CONECT 4455 4424 4454 4465                                                      
CONECT 4456 4453                                                                
CONECT 4457 4454 4458                                                           
CONECT 4458 4457 4459                                                           
CONECT 4459 4458 4460 4461                                                      
CONECT 4460 4459                                                                
CONECT 4461 4459                                                                
CONECT 4462 4428 4431 4466                                                      
CONECT 4463 4438 4441 4466                                                      
CONECT 4464 4445 4448 4466                                                      
CONECT 4465 4452 4455 4466                                                      
CONECT 4466  669 4462 4463 4464                                                 
CONECT 4466 4465 4468                                                           
CONECT 4467 4468                                                                
CONECT 4468 4466 4467                                                           
CONECT 4469 4473 4500                                                           
CONECT 4470 4476 4483                                                           
CONECT 4471 4486 4490                                                           
CONECT 4472 4493 4497                                                           
CONECT 4473 4469 4474 4507                                                      
CONECT 4474 4473 4475 4478                                                      
CONECT 4475 4474 4476 4477                                                      
CONECT 4476 4470 4475 4507                                                      
CONECT 4477 4475                                                                
CONECT 4478 4474 4479                                                           
CONECT 4479 4478 4480                                                           
CONECT 4480 4479 4481 4482                                                      
CONECT 4481 4480                                                                
CONECT 4482 4480                                                                
CONECT 4483 4470 4484 4508                                                      
CONECT 4484 4483 4485 4487                                                      
CONECT 4485 4484 4486 4488                                                      
CONECT 4486 4471 4485 4508                                                      
CONECT 4487 4484                                                                
CONECT 4488 4485 4489                                                           
CONECT 4489 4488                                                                
CONECT 4490 4471 4491 4509                                                      
CONECT 4491 4490 4492 4494                                                      
CONECT 4492 4491 4493 4495                                                      
CONECT 4493 4472 4492 4509                                                      
CONECT 4494 4491                                                                
CONECT 4495 4492 4496                                                           
CONECT 4496 4495                                                                
CONECT 4497 4472 4498 4510                                                      
CONECT 4498 4497 4499 4501                                                      
CONECT 4499 4498 4500 4502                                                      
CONECT 4500 4469 4499 4510                                                      
CONECT 4501 4498                                                                
CONECT 4502 4499 4503                                                           
CONECT 4503 4502 4504                                                           
CONECT 4504 4503 4505 4506                                                      
CONECT 4505 4504                                                                
CONECT 4506 4504                                                                
CONECT 4507 4473 4476 4511                                                      
CONECT 4508 4483 4486 4511                                                      
CONECT 4509 4490 4493 4511                                                      
CONECT 4510 4497 4500 4511                                                      
CONECT 4511 1773 4507 4508 4509                                                 
CONECT 4511 4510 4512 4513                                                      
CONECT 4512 4511 4513                                                           
CONECT 4513 4511 4512                                                           
CONECT 4514 4518 4545                                                           
CONECT 4515 4521 4528                                                           
CONECT 4516 4531 4535                                                           
CONECT 4517 4538 4542                                                           
CONECT 4518 4514 4519 4552                                                      
CONECT 4519 4518 4520 4523                                                      
CONECT 4520 4519 4521 4522                                                      
CONECT 4521 4515 4520 4552                                                      
CONECT 4522 4520                                                                
CONECT 4523 4519 4524                                                           
CONECT 4524 4523 4525                                                           
CONECT 4525 4524 4526 4527                                                      
CONECT 4526 4525                                                                
CONECT 4527 4525                                                                
CONECT 4528 4515 4529 4553                                                      
CONECT 4529 4528 4530 4532                                                      
CONECT 4530 4529 4531 4533                                                      
CONECT 4531 4516 4530 4553                                                      
CONECT 4532 4529                                                                
CONECT 4533 4530 4534                                                           
CONECT 4534 4533                                                                
CONECT 4535 4516 4536 4554                                                      
CONECT 4536 4535 4537 4539                                                      
CONECT 4537 4536 4538 4540                                                      
CONECT 4538 4517 4537 4554                                                      
CONECT 4539 4536                                                                
CONECT 4540 4537 4541                                                           
CONECT 4541 4540                                                                
CONECT 4542 4517 4543 4555                                                      
CONECT 4543 4542 4544 4546                                                      
CONECT 4544 4543 4545 4547                                                      
CONECT 4545 4514 4544 4555                                                      
CONECT 4546 4543                                                                
CONECT 4547 4544 4548                                                           
CONECT 4548 4547 4549                                                           
CONECT 4549 4548 4550 4551                                                      
CONECT 4550 4549                                                                
CONECT 4551 4549                                                                
CONECT 4552 4518 4521 4556                                                      
CONECT 4553 4528 4531 4556                                                      
CONECT 4554 4535 4538 4556                                                      
CONECT 4555 4542 4545 4556                                                      
CONECT 4556 2881 4552 4553 4554                                                 
CONECT 4556 4555 4558                                                           
CONECT 4557 4558                                                                
CONECT 4558 4556 4557                                                           
CONECT 4559 4563 4590                                                           
CONECT 4560 4566 4573                                                           
CONECT 4561 4576 4580                                                           
CONECT 4562 4583 4587                                                           
CONECT 4563 4559 4564 4597                                                      
CONECT 4564 4563 4565 4568                                                      
CONECT 4565 4564 4566 4567                                                      
CONECT 4566 4560 4565 4597                                                      
CONECT 4567 4565                                                                
CONECT 4568 4564 4569                                                           
CONECT 4569 4568 4570                                                           
CONECT 4570 4569 4571 4572                                                      
CONECT 4571 4570                                                                
CONECT 4572 4570                                                                
CONECT 4573 4560 4574 4598                                                      
CONECT 4574 4573 4575 4577                                                      
CONECT 4575 4574 4576 4578                                                      
CONECT 4576 4561 4575 4598                                                      
CONECT 4577 4574                                                                
CONECT 4578 4575 4579                                                           
CONECT 4579 4578                                                                
CONECT 4580 4561 4581 4599                                                      
CONECT 4581 4580 4582 4584                                                      
CONECT 4582 4581 4583 4585                                                      
CONECT 4583 4562 4582 4599                                                      
CONECT 4584 4581                                                                
CONECT 4585 4582 4586                                                           
CONECT 4586 4585                                                                
CONECT 4587 4562 4588 4600                                                      
CONECT 4588 4587 4589 4591                                                      
CONECT 4589 4588 4590 4592                                                      
CONECT 4590 4559 4589 4600                                                      
CONECT 4591 4588                                                                
CONECT 4592 4589 4593                                                           
CONECT 4593 4592 4594                                                           
CONECT 4594 4593 4595 4596                                                      
CONECT 4595 4594                                                                
CONECT 4596 4594                                                                
CONECT 4597 4563 4566 4601                                                      
CONECT 4598 4573 4576 4601                                                      
CONECT 4599 4580 4583 4601                                                      
CONECT 4600 4587 4590 4601                                                      
CONECT 4601 3985 4597 4598 4599                                                 
CONECT 4601 4600 4603                                                           
CONECT 4602 4603                                                                
CONECT 4603 4601 4602                                                           
MASTER      461    0    8   39    0    0   20    6 4959    4  188   46          
END                                                                             



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